data_8VYF
# 
_entry.id   8VYF 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.388 
_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   8VYF         pdb_00008vyf 10.2210/pdb8vyf/pdb 
WWPDB D_1000281321 ?            ?                   
EMDB  EMD-43659    ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-03-27 
# 
_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             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8VYF 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-08 
_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_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB  .                                                                                     8VYE      unspecified            
PDB  .                                                                                     8VYG      unspecified            
EMDB 'SARS-CoV-2 S NTD (C.37 Lambda variant) plus S2L20 and S2X303 Fabs, local refinement' EMD-43659 'associated EM volume' 
# 
_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 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'McCallum, M.'                                                       1 ? 
'Veesler, D.'                                                        2 ? 
'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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                2175 
_citation.page_last                 2175 
_citation.title                     'Quantifying how single dose Ad26.COV2.S vaccine efficacy depends on Spike sequence features.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-024-46536-w 
_citation.pdbx_database_id_PubMed   38467646 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Magaret, C.A.'    1  0000-0002-5056-2664 
primary 'Li, L.'           2  0000-0002-7112-9309 
primary 'deCamp, A.C.'     3  0000-0003-1404-4322 
primary 'Rolland, M.'      4  0000-0003-3650-8490 
primary 'Juraska, M.'      5  0000-0002-0920-2915 
primary 'Williamson, B.D.' 6  0000-0002-7024-548X 
primary 'Ludwig, J.'       7  0000-0003-3500-3490 
primary 'Molitor, C.'      8  ?                   
primary 'Benkeser, D.'     9  0000-0002-1019-8343 
primary 'Luedtke, A.'      10 ?                   
primary 'Simpkins, B.'     11 0009-0002-1044-0053 
primary 'Heng, F.'         12 0000-0002-6701-7873 
primary 'Sun, Y.'          13 0000-0002-3140-4572 
primary 'Carpp, L.N.'      14 0000-0003-0333-5925 
primary 'Bai, H.'          15 0000-0002-3501-3974 
primary 'Dearlove, B.L.'   16 0000-0003-3653-4592 
primary 'Giorgi, E.E.'     17 ?                   
primary 'Jongeneelen, M.'  18 ?                   
primary 'Brandenburg, B.'  19 ?                   
primary 'McCallum, M.'     20 0000-0001-8398-8330 
primary 'Bowen, J.E.'      21 ?                   
primary 'Veesler, D.'      22 0000-0002-6019-8675 
primary 'Sadoff, J.'       23 0000-0002-4839-3013 
primary 'Gray, G.E.'       24 ?                   
primary 'Roels, S.'        25 ?                   
primary 'Vandebosch, A.'   26 ?                   
primary 'Stieh, D.J.'      27 0009-0003-8523-1528 
primary 'Le Gars, M.'      28 ?                   
primary 'Vingerhoets, J.'  29 0000-0001-5939-9501 
primary 'Grinsztejn, B.'   30 ?                   
primary 'Goepfert, P.A.'   31 0000-0001-8441-5737 
primary 'de Sousa, L.P.'   32 0000-0001-9004-5154 
primary 'Silva, M.S.T.'    33 ?                   
primary 'Casapia, M.'      34 0000-0002-5972-0948 
primary 'Losso, M.H.'      35 0000-0002-4273-4833 
primary 'Little, S.J.'     36 0000-0002-7645-9737 
primary 'Gaur, A.'         37 ?                   
primary 'Bekker, L.G.'     38 0000-0002-0755-4386 
primary 'Garrett, N.'      39 0000-0002-4530-234X 
primary 'Truyers, C.'      40 ?                   
primary 'Van Dromme, I.'   41 ?                   
primary 'Swann, E.'        42 ?                   
primary 'Marovich, M.A.'   43 ?                   
primary 'Follmann, D.'     44 0000-0003-4073-0393 
primary 'Neuzil, K.M.'     45 0000-0001-9480-2714 
primary 'Corey, L.'        46 0000-0002-2179-2436 
primary 'Greninger, A.L.'  47 0000-0002-7443-0527 
primary 'Roychoudhury, P.' 48 0000-0002-4567-8232 
primary 'Hyrien, O.'       49 ?                   
primary 'Gilbert, P.B.'    50 0000-0002-2662-9427 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Spike glycoprotein' 140929.156 1 ? ? ? 'Lambda spike glycoprotein, NTD' 
2 polymer     man 'S2L20 Heavy Chain' 13541.036  1 ? ? ? ?                                
3 polymer     man 'S2L20 Light Chain' 11829.141  1 ? ? ? ?                                
4 polymer     man 'S2X303 Heavy Chain' 13737.725  1 ? ? ? ?                                
5 polymer     man 'S2X303 Light Chain' 11270.294  1 ? ? ? ?                                
6 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 
? ? ? ?                                
7 branched    man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401    2 ? ? ? ? 
8 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208    5 ? ? ? ?                                
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'S glycoprotein,E2,Peplomer protein' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MFVFLVLLPLVSSQCVNLTTRTQLPPAYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFHAIHVSGTNVIKRFD
NPVLPFNDGVYFASTEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVVIKVCEFQFCNDPFLGVYYHKNNKSWMESEFRVY
SSANNCTFEYVSQPFLMDLEGKQGNFKNLREFVFKNIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGINITRFQT
LLALHNSSSGWTAGAAAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQTSNFRVQPTESIV
RFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVCPTKLNDLCFTNVYADSFVIRGDEV
RQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYQYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFN
CYSPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFNFNGLTGTGVLTESNKKFLPFQQFGR
DIADTTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNQVAVLYQGVNCTEVPVAIHADQLTPTWRVYSTGSNVFQTRA
GCLIGAEHVNNSYECDIPIGAGICASYQTQTNSPRRARSVASQSIIAYTMSLGAENSVAYSNNSIAIPTNFTISVTTEIL
PVSMTKTSVDCTMYICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKDFGGFNFSQILP
DPSKPSKRSPIEDLLFNKVTLADAGFIKQYGDCLGDIAARDLICAQKFNGLNVLPPLLTDEMIAQYTSALLAGTITSGWT
FGAGPALQIPFPMQMAYRFNGIGVTQNVLYENQKLIANQFNSAIGKIQDSLSSTPSALGKLQDVVNQNAQALNTLVKQLS
SNFGAISSVLNDILSRLCPPEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGY
HLMSFPQSAPHGVVFLHVTYVPAQEKNFTTAPAICHDGKAHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNTFVSGNCD
VVIGIVNNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE
QGSGYIPEAPRDGQAYVRKDGEWVLLSTFLGRSLEVLFQGPGSGGLNDIFEAQKIEWHEGSGHHHHHHHH
;
;MFVFLVLLPLVSSQCVNLTTRTQLPPAYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFHAIHVSGTNVIKRFD
NPVLPFNDGVYFASTEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVVIKVCEFQFCNDPFLGVYYHKNNKSWMESEFRVY
SSANNCTFEYVSQPFLMDLEGKQGNFKNLREFVFKNIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGINITRFQT
LLALHNSSSGWTAGAAAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQTSNFRVQPTESIV
RFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVCPTKLNDLCFTNVYADSFVIRGDEV
RQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYQYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFN
CYSPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFNFNGLTGTGVLTESNKKFLPFQQFGR
DIADTTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNQVAVLYQGVNCTEVPVAIHADQLTPTWRVYSTGSNVFQTRA
GCLIGAEHVNNSYECDIPIGAGICASYQTQTNSPRRARSVASQSIIAYTMSLGAENSVAYSNNSIAIPTNFTISVTTEIL
PVSMTKTSVDCTMYICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKDFGGFNFSQILP
DPSKPSKRSPIEDLLFNKVTLADAGFIKQYGDCLGDIAARDLICAQKFNGLNVLPPLLTDEMIAQYTSALLAGTITSGWT
FGAGPALQIPFPMQMAYRFNGIGVTQNVLYENQKLIANQFNSAIGKIQDSLSSTPSALGKLQDVVNQNAQALNTLVKQLS
SNFGAISSVLNDILSRLCPPEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGY
HLMSFPQSAPHGVVFLHVTYVPAQEKNFTTAPAICHDGKAHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNTFVSGNCD
VVIGIVNNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYE
QGSGYIPEAPRDGQAYVRKDGEWVLLSTFLGRSLEVLFQGPGSGGLNDIFEAQKIEWHEGSGHHHHHHHH
;
A ? 
2 'polypeptide(L)' no no 
;EVQLVESGGGVVQPGGSLRLSCAASGFTFNSYGMHWVRQAPGKGLEWVAFIRYDGGNKYYADSVKGRFTISRDNSKNTLY
LQMKSLRAEDTAVYYCANLKDSRYSGSYYDYWGQGTLVTVSS
;
;EVQLVESGGGVVQPGGSLRLSCAASGFTFNSYGMHWVRQAPGKGLEWVAFIRYDGGNKYYADSVKGRFTISRDNSKNTLY
LQMKSLRAEDTAVYYCANLKDSRYSGSYYDYWGQGTLVTVSS
;
B ? 
3 'polypeptide(L)' no no 
;VIWMTQSPSSLSASVGDRVTITCQASQDIRFYLNWYQQKPGKAPKLLISDASNMETGVPSRFSGSGSGTDFTFTISSLQP
EDIATYYCQQYDNLPFTFGPGTKVDFK
;
;VIWMTQSPSSLSASVGDRVTITCQASQDIRFYLNWYQQKPGKAPKLLISDASNMETGVPSRFSGSGSGTDFTFTISSLQP
EDIATYYCQQYDNLPFTFGPGTKVDFK
;
C ? 
4 'polypeptide(L)' no no 
;QITLKESGPTLVKPTQTLTLTCKLSGFSVNTGGVGVGWIRQPPGKALEWLALIYWNDDKLYSPSLKSRLTVTKDTSKNQV
VLTMTNMDPVDTATYYCAHVLVWFGEVLPDAFDVWGQGTMVTVSS
;
;QITLKESGPTLVKPTQTLTLTCKLSGFSVNTGGVGVGWIRQPPGKALEWLALIYWNDDKLYSPSLKSRLTVTKDTSKNQV
VLTMTNMDPVDTATYYCAHVLVWFGEVLPDAFDVWGQGTMVTVSS
;
H ? 
5 'polypeptide(L)' no no 
;SYELTQPPSVSVSPGQTASITCSGDKLGETYASWYQQKPGQSPILVIYQDNKRPSGIPERFSGSNSENTATLTISGTQTM
DEADYYCQAWDKTIAGFGGGTKLTV
;
;SYELTQPPSVSVSPGQTASITCSGDKLGETYASWYQQKPGQSPILVIYQDNKRPSGIPERFSGSNSENTATLTISGTQTM
DEADYYCQAWDKTIAGFGGGTKLTV
;
L ? 
# 
_pdbx_entity_nonpoly.entity_id   8 
_pdbx_entity_nonpoly.name        2-acetamido-2-deoxy-beta-D-glucopyranose 
_pdbx_entity_nonpoly.comp_id     NAG 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    MET n 
1 2    PHE n 
1 3    VAL n 
1 4    PHE n 
1 5    LEU n 
1 6    VAL n 
1 7    LEU n 
1 8    LEU n 
1 9    PRO n 
1 10   LEU n 
1 11   VAL n 
1 12   SER n 
1 13   SER n 
1 14   GLN n 
1 15   CYS n 
1 16   VAL n 
1 17   ASN n 
1 18   LEU n 
1 19   THR n 
1 20   THR n 
1 21   ARG n 
1 22   THR n 
1 23   GLN n 
1 24   LEU n 
1 25   PRO n 
1 26   PRO n 
1 27   ALA n 
1 28   TYR n 
1 29   THR n 
1 30   ASN n 
1 31   SER n 
1 32   PHE n 
1 33   THR n 
1 34   ARG n 
1 35   GLY n 
1 36   VAL n 
1 37   TYR n 
1 38   TYR n 
1 39   PRO n 
1 40   ASP n 
1 41   LYS n 
1 42   VAL n 
1 43   PHE n 
1 44   ARG n 
1 45   SER n 
1 46   SER n 
1 47   VAL n 
1 48   LEU n 
1 49   HIS n 
1 50   SER n 
1 51   THR n 
1 52   GLN n 
1 53   ASP n 
1 54   LEU n 
1 55   PHE n 
1 56   LEU n 
1 57   PRO n 
1 58   PHE n 
1 59   PHE n 
1 60   SER n 
1 61   ASN n 
1 62   VAL n 
1 63   THR n 
1 64   TRP n 
1 65   PHE n 
1 66   HIS n 
1 67   ALA n 
1 68   ILE n 
1 69   HIS n 
1 70   VAL n 
1 71   SER n 
1 72   GLY n 
1 73   THR n 
1 74   ASN n 
1 75   VAL n 
1 76   ILE n 
1 77   LYS n 
1 78   ARG n 
1 79   PHE n 
1 80   ASP n 
1 81   ASN n 
1 82   PRO n 
1 83   VAL n 
1 84   LEU n 
1 85   PRO n 
1 86   PHE n 
1 87   ASN n 
1 88   ASP n 
1 89   GLY n 
1 90   VAL n 
1 91   TYR n 
1 92   PHE n 
1 93   ALA n 
1 94   SER n 
1 95   THR n 
1 96   GLU n 
1 97   LYS n 
1 98   SER n 
1 99   ASN n 
1 100  ILE n 
1 101  ILE n 
1 102  ARG n 
1 103  GLY n 
1 104  TRP n 
1 105  ILE n 
1 106  PHE n 
1 107  GLY n 
1 108  THR n 
1 109  THR n 
1 110  LEU n 
1 111  ASP n 
1 112  SER n 
1 113  LYS n 
1 114  THR n 
1 115  GLN n 
1 116  SER n 
1 117  LEU n 
1 118  LEU n 
1 119  ILE n 
1 120  VAL n 
1 121  ASN n 
1 122  ASN n 
1 123  ALA n 
1 124  THR n 
1 125  ASN n 
1 126  VAL n 
1 127  VAL n 
1 128  ILE n 
1 129  LYS n 
1 130  VAL n 
1 131  CYS n 
1 132  GLU n 
1 133  PHE n 
1 134  GLN n 
1 135  PHE n 
1 136  CYS n 
1 137  ASN n 
1 138  ASP n 
1 139  PRO n 
1 140  PHE n 
1 141  LEU n 
1 142  GLY n 
1 143  VAL n 
1 144  TYR n 
1 145  TYR n 
1 146  HIS n 
1 147  LYS n 
1 148  ASN n 
1 149  ASN n 
1 150  LYS n 
1 151  SER n 
1 152  TRP n 
1 153  MET n 
1 154  GLU n 
1 155  SER n 
1 156  GLU n 
1 157  PHE n 
1 158  ARG n 
1 159  VAL n 
1 160  TYR n 
1 161  SER n 
1 162  SER n 
1 163  ALA n 
1 164  ASN n 
1 165  ASN n 
1 166  CYS n 
1 167  THR n 
1 168  PHE n 
1 169  GLU n 
1 170  TYR n 
1 171  VAL n 
1 172  SER n 
1 173  GLN n 
1 174  PRO n 
1 175  PHE n 
1 176  LEU n 
1 177  MET n 
1 178  ASP n 
1 179  LEU n 
1 180  GLU n 
1 181  GLY n 
1 182  LYS n 
1 183  GLN n 
1 184  GLY n 
1 185  ASN n 
1 186  PHE n 
1 187  LYS n 
1 188  ASN n 
1 189  LEU n 
1 190  ARG n 
1 191  GLU n 
1 192  PHE n 
1 193  VAL n 
1 194  PHE n 
1 195  LYS n 
1 196  ASN n 
1 197  ILE n 
1 198  ASP n 
1 199  GLY n 
1 200  TYR n 
1 201  PHE n 
1 202  LYS n 
1 203  ILE n 
1 204  TYR n 
1 205  SER n 
1 206  LYS n 
1 207  HIS n 
1 208  THR n 
1 209  PRO n 
1 210  ILE n 
1 211  ASN n 
1 212  LEU n 
1 213  VAL n 
1 214  ARG n 
1 215  ASP n 
1 216  LEU n 
1 217  PRO n 
1 218  GLN n 
1 219  GLY n 
1 220  PHE n 
1 221  SER n 
1 222  ALA n 
1 223  LEU n 
1 224  GLU n 
1 225  PRO n 
1 226  LEU n 
1 227  VAL n 
1 228  ASP n 
1 229  LEU n 
1 230  PRO n 
1 231  ILE n 
1 232  GLY n 
1 233  ILE n 
1 234  ASN n 
1 235  ILE n 
1 236  THR n 
1 237  ARG n 
1 238  PHE n 
1 239  GLN n 
1 240  THR n 
1 241  LEU n 
1 242  LEU n 
1 243  ALA n 
1 244  LEU n 
1 245  HIS n 
1 246  ASN n 
1 247  SER n 
1 248  SER n 
1 249  SER n 
1 250  GLY n 
1 251  TRP n 
1 252  THR n 
1 253  ALA n 
1 254  GLY n 
1 255  ALA n 
1 256  ALA n 
1 257  ALA n 
1 258  TYR n 
1 259  TYR n 
1 260  VAL n 
1 261  GLY n 
1 262  TYR n 
1 263  LEU n 
1 264  GLN n 
1 265  PRO n 
1 266  ARG n 
1 267  THR n 
1 268  PHE n 
1 269  LEU n 
1 270  LEU n 
1 271  LYS n 
1 272  TYR n 
1 273  ASN n 
1 274  GLU n 
1 275  ASN n 
1 276  GLY n 
1 277  THR n 
1 278  ILE n 
1 279  THR n 
1 280  ASP n 
1 281  ALA n 
1 282  VAL n 
1 283  ASP n 
1 284  CYS n 
1 285  ALA n 
1 286  LEU n 
1 287  ASP n 
1 288  PRO n 
1 289  LEU n 
1 290  SER n 
1 291  GLU n 
1 292  THR n 
1 293  LYS n 
1 294  CYS n 
1 295  THR n 
1 296  LEU n 
1 297  LYS n 
1 298  SER n 
1 299  PHE n 
1 300  THR n 
1 301  VAL n 
1 302  GLU n 
1 303  LYS n 
1 304  GLY n 
1 305  ILE n 
1 306  TYR n 
1 307  GLN n 
1 308  THR n 
1 309  SER n 
1 310  ASN n 
1 311  PHE n 
1 312  ARG n 
1 313  VAL n 
1 314  GLN n 
1 315  PRO n 
1 316  THR n 
1 317  GLU n 
1 318  SER n 
1 319  ILE n 
1 320  VAL n 
1 321  ARG n 
1 322  PHE n 
1 323  PRO n 
1 324  ASN n 
1 325  ILE n 
1 326  THR n 
1 327  ASN n 
1 328  LEU n 
1 329  CYS n 
1 330  PRO n 
1 331  PHE n 
1 332  GLY n 
1 333  GLU n 
1 334  VAL n 
1 335  PHE n 
1 336  ASN n 
1 337  ALA n 
1 338  THR n 
1 339  ARG n 
1 340  PHE n 
1 341  ALA n 
1 342  SER n 
1 343  VAL n 
1 344  TYR n 
1 345  ALA n 
1 346  TRP n 
1 347  ASN n 
1 348  ARG n 
1 349  LYS n 
1 350  ARG n 
1 351  ILE n 
1 352  SER n 
1 353  ASN n 
1 354  CYS n 
1 355  VAL n 
1 356  ALA n 
1 357  ASP n 
1 358  TYR n 
1 359  SER n 
1 360  VAL n 
1 361  LEU n 
1 362  TYR n 
1 363  ASN n 
1 364  SER n 
1 365  ALA n 
1 366  SER n 
1 367  PHE n 
1 368  SER n 
1 369  THR n 
1 370  PHE n 
1 371  LYS n 
1 372  CYS n 
1 373  TYR n 
1 374  GLY n 
1 375  VAL n 
1 376  CYS n 
1 377  PRO n 
1 378  THR n 
1 379  LYS n 
1 380  LEU n 
1 381  ASN n 
1 382  ASP n 
1 383  LEU n 
1 384  CYS n 
1 385  PHE n 
1 386  THR n 
1 387  ASN n 
1 388  VAL n 
1 389  TYR n 
1 390  ALA n 
1 391  ASP n 
1 392  SER n 
1 393  PHE n 
1 394  VAL n 
1 395  ILE n 
1 396  ARG n 
1 397  GLY n 
1 398  ASP n 
1 399  GLU n 
1 400  VAL n 
1 401  ARG n 
1 402  GLN n 
1 403  ILE n 
1 404  ALA n 
1 405  PRO n 
1 406  GLY n 
1 407  GLN n 
1 408  THR n 
1 409  GLY n 
1 410  LYS n 
1 411  ILE n 
1 412  ALA n 
1 413  ASP n 
1 414  TYR n 
1 415  ASN n 
1 416  TYR n 
1 417  LYS n 
1 418  LEU n 
1 419  PRO n 
1 420  ASP n 
1 421  ASP n 
1 422  PHE n 
1 423  THR n 
1 424  GLY n 
1 425  CYS n 
1 426  VAL n 
1 427  ILE n 
1 428  ALA n 
1 429  TRP n 
1 430  ASN n 
1 431  SER n 
1 432  ASN n 
1 433  ASN n 
1 434  LEU n 
1 435  ASP n 
1 436  SER n 
1 437  LYS n 
1 438  VAL n 
1 439  GLY n 
1 440  GLY n 
1 441  ASN n 
1 442  TYR n 
1 443  ASN n 
1 444  TYR n 
1 445  GLN n 
1 446  TYR n 
1 447  ARG n 
1 448  LEU n 
1 449  PHE n 
1 450  ARG n 
1 451  LYS n 
1 452  SER n 
1 453  ASN n 
1 454  LEU n 
1 455  LYS n 
1 456  PRO n 
1 457  PHE n 
1 458  GLU n 
1 459  ARG n 
1 460  ASP n 
1 461  ILE n 
1 462  SER n 
1 463  THR n 
1 464  GLU n 
1 465  ILE n 
1 466  TYR n 
1 467  GLN n 
1 468  ALA n 
1 469  GLY n 
1 470  SER n 
1 471  THR n 
1 472  PRO n 
1 473  CYS n 
1 474  ASN n 
1 475  GLY n 
1 476  VAL n 
1 477  GLU n 
1 478  GLY n 
1 479  PHE n 
1 480  ASN n 
1 481  CYS n 
1 482  TYR n 
1 483  SER n 
1 484  PRO n 
1 485  LEU n 
1 486  GLN n 
1 487  SER n 
1 488  TYR n 
1 489  GLY n 
1 490  PHE n 
1 491  GLN n 
1 492  PRO n 
1 493  THR n 
1 494  ASN n 
1 495  GLY n 
1 496  VAL n 
1 497  GLY n 
1 498  TYR n 
1 499  GLN n 
1 500  PRO n 
1 501  TYR n 
1 502  ARG n 
1 503  VAL n 
1 504  VAL n 
1 505  VAL n 
1 506  LEU n 
1 507  SER n 
1 508  PHE n 
1 509  GLU n 
1 510  LEU n 
1 511  LEU n 
1 512  HIS n 
1 513  ALA n 
1 514  PRO n 
1 515  ALA n 
1 516  THR n 
1 517  VAL n 
1 518  CYS n 
1 519  GLY n 
1 520  PRO n 
1 521  LYS n 
1 522  LYS n 
1 523  SER n 
1 524  THR n 
1 525  ASN n 
1 526  LEU n 
1 527  VAL n 
1 528  LYS n 
1 529  ASN n 
1 530  LYS n 
1 531  CYS n 
1 532  VAL n 
1 533  ASN n 
1 534  PHE n 
1 535  ASN n 
1 536  PHE n 
1 537  ASN n 
1 538  GLY n 
1 539  LEU n 
1 540  THR n 
1 541  GLY n 
1 542  THR n 
1 543  GLY n 
1 544  VAL n 
1 545  LEU n 
1 546  THR n 
1 547  GLU n 
1 548  SER n 
1 549  ASN n 
1 550  LYS n 
1 551  LYS n 
1 552  PHE n 
1 553  LEU n 
1 554  PRO n 
1 555  PHE n 
1 556  GLN n 
1 557  GLN n 
1 558  PHE n 
1 559  GLY n 
1 560  ARG n 
1 561  ASP n 
1 562  ILE n 
1 563  ALA n 
1 564  ASP n 
1 565  THR n 
1 566  THR n 
1 567  ASP n 
1 568  ALA n 
1 569  VAL n 
1 570  ARG n 
1 571  ASP n 
1 572  PRO n 
1 573  GLN n 
1 574  THR n 
1 575  LEU n 
1 576  GLU n 
1 577  ILE n 
1 578  LEU n 
1 579  ASP n 
1 580  ILE n 
1 581  THR n 
1 582  PRO n 
1 583  CYS n 
1 584  SER n 
1 585  PHE n 
1 586  GLY n 
1 587  GLY n 
1 588  VAL n 
1 589  SER n 
1 590  VAL n 
1 591  ILE n 
1 592  THR n 
1 593  PRO n 
1 594  GLY n 
1 595  THR n 
1 596  ASN n 
1 597  THR n 
1 598  SER n 
1 599  ASN n 
1 600  GLN n 
1 601  VAL n 
1 602  ALA n 
1 603  VAL n 
1 604  LEU n 
1 605  TYR n 
1 606  GLN n 
1 607  GLY n 
1 608  VAL n 
1 609  ASN n 
1 610  CYS n 
1 611  THR n 
1 612  GLU n 
1 613  VAL n 
1 614  PRO n 
1 615  VAL n 
1 616  ALA n 
1 617  ILE n 
1 618  HIS n 
1 619  ALA n 
1 620  ASP n 
1 621  GLN n 
1 622  LEU n 
1 623  THR n 
1 624  PRO n 
1 625  THR n 
1 626  TRP n 
1 627  ARG n 
1 628  VAL n 
1 629  TYR n 
1 630  SER n 
1 631  THR n 
1 632  GLY n 
1 633  SER n 
1 634  ASN n 
1 635  VAL n 
1 636  PHE n 
1 637  GLN n 
1 638  THR n 
1 639  ARG n 
1 640  ALA n 
1 641  GLY n 
1 642  CYS n 
1 643  LEU n 
1 644  ILE n 
1 645  GLY n 
1 646  ALA n 
1 647  GLU n 
1 648  HIS n 
1 649  VAL n 
1 650  ASN n 
1 651  ASN n 
1 652  SER n 
1 653  TYR n 
1 654  GLU n 
1 655  CYS n 
1 656  ASP n 
1 657  ILE n 
1 658  PRO n 
1 659  ILE n 
1 660  GLY n 
1 661  ALA n 
1 662  GLY n 
1 663  ILE n 
1 664  CYS n 
1 665  ALA n 
1 666  SER n 
1 667  TYR n 
1 668  GLN n 
1 669  THR n 
1 670  GLN n 
1 671  THR n 
1 672  ASN n 
1 673  SER n 
1 674  PRO n 
1 675  ARG n 
1 676  ARG n 
1 677  ALA n 
1 678  ARG n 
1 679  SER n 
1 680  VAL n 
1 681  ALA n 
1 682  SER n 
1 683  GLN n 
1 684  SER n 
1 685  ILE n 
1 686  ILE n 
1 687  ALA n 
1 688  TYR n 
1 689  THR n 
1 690  MET n 
1 691  SER n 
1 692  LEU n 
1 693  GLY n 
1 694  ALA n 
1 695  GLU n 
1 696  ASN n 
1 697  SER n 
1 698  VAL n 
1 699  ALA n 
1 700  TYR n 
1 701  SER n 
1 702  ASN n 
1 703  ASN n 
1 704  SER n 
1 705  ILE n 
1 706  ALA n 
1 707  ILE n 
1 708  PRO n 
1 709  THR n 
1 710  ASN n 
1 711  PHE n 
1 712  THR n 
1 713  ILE n 
1 714  SER n 
1 715  VAL n 
1 716  THR n 
1 717  THR n 
1 718  GLU n 
1 719  ILE n 
1 720  LEU n 
1 721  PRO n 
1 722  VAL n 
1 723  SER n 
1 724  MET n 
1 725  THR n 
1 726  LYS n 
1 727  THR n 
1 728  SER n 
1 729  VAL n 
1 730  ASP n 
1 731  CYS n 
1 732  THR n 
1 733  MET n 
1 734  TYR n 
1 735  ILE n 
1 736  CYS n 
1 737  GLY n 
1 738  ASP n 
1 739  SER n 
1 740  THR n 
1 741  GLU n 
1 742  CYS n 
1 743  SER n 
1 744  ASN n 
1 745  LEU n 
1 746  LEU n 
1 747  LEU n 
1 748  GLN n 
1 749  TYR n 
1 750  GLY n 
1 751  SER n 
1 752  PHE n 
1 753  CYS n 
1 754  THR n 
1 755  GLN n 
1 756  LEU n 
1 757  ASN n 
1 758  ARG n 
1 759  ALA n 
1 760  LEU n 
1 761  THR n 
1 762  GLY n 
1 763  ILE n 
1 764  ALA n 
1 765  VAL n 
1 766  GLU n 
1 767  GLN n 
1 768  ASP n 
1 769  LYS n 
1 770  ASN n 
1 771  THR n 
1 772  GLN n 
1 773  GLU n 
1 774  VAL n 
1 775  PHE n 
1 776  ALA n 
1 777  GLN n 
1 778  VAL n 
1 779  LYS n 
1 780  GLN n 
1 781  ILE n 
1 782  TYR n 
1 783  LYS n 
1 784  THR n 
1 785  PRO n 
1 786  PRO n 
1 787  ILE n 
1 788  LYS n 
1 789  ASP n 
1 790  PHE n 
1 791  GLY n 
1 792  GLY n 
1 793  PHE n 
1 794  ASN n 
1 795  PHE n 
1 796  SER n 
1 797  GLN n 
1 798  ILE n 
1 799  LEU n 
1 800  PRO n 
1 801  ASP n 
1 802  PRO n 
1 803  SER n 
1 804  LYS n 
1 805  PRO n 
1 806  SER n 
1 807  LYS n 
1 808  ARG n 
1 809  SER n 
1 810  PRO n 
1 811  ILE n 
1 812  GLU n 
1 813  ASP n 
1 814  LEU n 
1 815  LEU n 
1 816  PHE n 
1 817  ASN n 
1 818  LYS n 
1 819  VAL n 
1 820  THR n 
1 821  LEU n 
1 822  ALA n 
1 823  ASP n 
1 824  ALA n 
1 825  GLY n 
1 826  PHE n 
1 827  ILE n 
1 828  LYS n 
1 829  GLN n 
1 830  TYR n 
1 831  GLY n 
1 832  ASP n 
1 833  CYS n 
1 834  LEU n 
1 835  GLY n 
1 836  ASP n 
1 837  ILE n 
1 838  ALA n 
1 839  ALA n 
1 840  ARG n 
1 841  ASP n 
1 842  LEU n 
1 843  ILE n 
1 844  CYS n 
1 845  ALA n 
1 846  GLN n 
1 847  LYS n 
1 848  PHE n 
1 849  ASN n 
1 850  GLY n 
1 851  LEU n 
1 852  ASN n 
1 853  VAL n 
1 854  LEU n 
1 855  PRO n 
1 856  PRO n 
1 857  LEU n 
1 858  LEU n 
1 859  THR n 
1 860  ASP n 
1 861  GLU n 
1 862  MET n 
1 863  ILE n 
1 864  ALA n 
1 865  GLN n 
1 866  TYR n 
1 867  THR n 
1 868  SER n 
1 869  ALA n 
1 870  LEU n 
1 871  LEU n 
1 872  ALA n 
1 873  GLY n 
1 874  THR n 
1 875  ILE n 
1 876  THR n 
1 877  SER n 
1 878  GLY n 
1 879  TRP n 
1 880  THR n 
1 881  PHE n 
1 882  GLY n 
1 883  ALA n 
1 884  GLY n 
1 885  PRO n 
1 886  ALA n 
1 887  LEU n 
1 888  GLN n 
1 889  ILE n 
1 890  PRO n 
1 891  PHE n 
1 892  PRO n 
1 893  MET n 
1 894  GLN n 
1 895  MET n 
1 896  ALA n 
1 897  TYR n 
1 898  ARG n 
1 899  PHE n 
1 900  ASN n 
1 901  GLY n 
1 902  ILE n 
1 903  GLY n 
1 904  VAL n 
1 905  THR n 
1 906  GLN n 
1 907  ASN n 
1 908  VAL n 
1 909  LEU n 
1 910  TYR n 
1 911  GLU n 
1 912  ASN n 
1 913  GLN n 
1 914  LYS n 
1 915  LEU n 
1 916  ILE n 
1 917  ALA n 
1 918  ASN n 
1 919  GLN n 
1 920  PHE n 
1 921  ASN n 
1 922  SER n 
1 923  ALA n 
1 924  ILE n 
1 925  GLY n 
1 926  LYS n 
1 927  ILE n 
1 928  GLN n 
1 929  ASP n 
1 930  SER n 
1 931  LEU n 
1 932  SER n 
1 933  SER n 
1 934  THR n 
1 935  PRO n 
1 936  SER n 
1 937  ALA n 
1 938  LEU n 
1 939  GLY n 
1 940  LYS n 
1 941  LEU n 
1 942  GLN n 
1 943  ASP n 
1 944  VAL n 
1 945  VAL n 
1 946  ASN n 
1 947  GLN n 
1 948  ASN n 
1 949  ALA n 
1 950  GLN n 
1 951  ALA n 
1 952  LEU n 
1 953  ASN n 
1 954  THR n 
1 955  LEU n 
1 956  VAL n 
1 957  LYS n 
1 958  GLN n 
1 959  LEU n 
1 960  SER n 
1 961  SER n 
1 962  ASN n 
1 963  PHE n 
1 964  GLY n 
1 965  ALA n 
1 966  ILE n 
1 967  SER n 
1 968  SER n 
1 969  VAL n 
1 970  LEU n 
1 971  ASN n 
1 972  ASP n 
1 973  ILE n 
1 974  LEU n 
1 975  SER n 
1 976  ARG n 
1 977  LEU n 
1 978  CYS n 
1 979  PRO n 
1 980  PRO n 
1 981  GLU n 
1 982  ALA n 
1 983  GLU n 
1 984  VAL n 
1 985  GLN n 
1 986  ILE n 
1 987  ASP n 
1 988  ARG n 
1 989  LEU n 
1 990  ILE n 
1 991  THR n 
1 992  GLY n 
1 993  ARG n 
1 994  LEU n 
1 995  GLN n 
1 996  SER n 
1 997  LEU n 
1 998  GLN n 
1 999  THR n 
1 1000 TYR n 
1 1001 VAL n 
1 1002 THR n 
1 1003 GLN n 
1 1004 GLN n 
1 1005 LEU n 
1 1006 ILE n 
1 1007 ARG n 
1 1008 ALA n 
1 1009 ALA n 
1 1010 GLU n 
1 1011 ILE n 
1 1012 ARG n 
1 1013 ALA n 
1 1014 SER n 
1 1015 ALA n 
1 1016 ASN n 
1 1017 LEU n 
1 1018 ALA n 
1 1019 ALA n 
1 1020 THR n 
1 1021 LYS n 
1 1022 MET n 
1 1023 SER n 
1 1024 GLU n 
1 1025 CYS n 
1 1026 VAL n 
1 1027 LEU n 
1 1028 GLY n 
1 1029 GLN n 
1 1030 SER n 
1 1031 LYS n 
1 1032 ARG n 
1 1033 VAL n 
1 1034 ASP n 
1 1035 PHE n 
1 1036 CYS n 
1 1037 GLY n 
1 1038 LYS n 
1 1039 GLY n 
1 1040 TYR n 
1 1041 HIS n 
1 1042 LEU n 
1 1043 MET n 
1 1044 SER n 
1 1045 PHE n 
1 1046 PRO n 
1 1047 GLN n 
1 1048 SER n 
1 1049 ALA n 
1 1050 PRO n 
1 1051 HIS n 
1 1052 GLY n 
1 1053 VAL n 
1 1054 VAL n 
1 1055 PHE n 
1 1056 LEU n 
1 1057 HIS n 
1 1058 VAL n 
1 1059 THR n 
1 1060 TYR n 
1 1061 VAL n 
1 1062 PRO n 
1 1063 ALA n 
1 1064 GLN n 
1 1065 GLU n 
1 1066 LYS n 
1 1067 ASN n 
1 1068 PHE n 
1 1069 THR n 
1 1070 THR n 
1 1071 ALA n 
1 1072 PRO n 
1 1073 ALA n 
1 1074 ILE n 
1 1075 CYS n 
1 1076 HIS n 
1 1077 ASP n 
1 1078 GLY n 
1 1079 LYS n 
1 1080 ALA n 
1 1081 HIS n 
1 1082 PHE n 
1 1083 PRO n 
1 1084 ARG n 
1 1085 GLU n 
1 1086 GLY n 
1 1087 VAL n 
1 1088 PHE n 
1 1089 VAL n 
1 1090 SER n 
1 1091 ASN n 
1 1092 GLY n 
1 1093 THR n 
1 1094 HIS n 
1 1095 TRP n 
1 1096 PHE n 
1 1097 VAL n 
1 1098 THR n 
1 1099 GLN n 
1 1100 ARG n 
1 1101 ASN n 
1 1102 PHE n 
1 1103 TYR n 
1 1104 GLU n 
1 1105 PRO n 
1 1106 GLN n 
1 1107 ILE n 
1 1108 ILE n 
1 1109 THR n 
1 1110 THR n 
1 1111 ASP n 
1 1112 ASN n 
1 1113 THR n 
1 1114 PHE n 
1 1115 VAL n 
1 1116 SER n 
1 1117 GLY n 
1 1118 ASN n 
1 1119 CYS n 
1 1120 ASP n 
1 1121 VAL n 
1 1122 VAL n 
1 1123 ILE n 
1 1124 GLY n 
1 1125 ILE n 
1 1126 VAL n 
1 1127 ASN n 
1 1128 ASN n 
1 1129 THR n 
1 1130 VAL n 
1 1131 TYR n 
1 1132 ASP n 
1 1133 PRO n 
1 1134 LEU n 
1 1135 GLN n 
1 1136 PRO n 
1 1137 GLU n 
1 1138 LEU n 
1 1139 ASP n 
1 1140 SER n 
1 1141 PHE n 
1 1142 LYS n 
1 1143 GLU n 
1 1144 GLU n 
1 1145 LEU n 
1 1146 ASP n 
1 1147 LYS n 
1 1148 TYR n 
1 1149 PHE n 
1 1150 LYS n 
1 1151 ASN n 
1 1152 HIS n 
1 1153 THR n 
1 1154 SER n 
1 1155 PRO n 
1 1156 ASP n 
1 1157 VAL n 
1 1158 ASP n 
1 1159 LEU n 
1 1160 GLY n 
1 1161 ASP n 
1 1162 ILE n 
1 1163 SER n 
1 1164 GLY n 
1 1165 ILE n 
1 1166 ASN n 
1 1167 ALA n 
1 1168 SER n 
1 1169 VAL n 
1 1170 VAL n 
1 1171 ASN n 
1 1172 ILE n 
1 1173 GLN n 
1 1174 LYS n 
1 1175 GLU n 
1 1176 ILE n 
1 1177 ASP n 
1 1178 ARG n 
1 1179 LEU n 
1 1180 ASN n 
1 1181 GLU n 
1 1182 VAL n 
1 1183 ALA n 
1 1184 LYS n 
1 1185 ASN n 
1 1186 LEU n 
1 1187 ASN n 
1 1188 GLU n 
1 1189 SER n 
1 1190 LEU n 
1 1191 ILE n 
1 1192 ASP n 
1 1193 LEU n 
1 1194 GLN n 
1 1195 GLU n 
1 1196 LEU n 
1 1197 GLY n 
1 1198 LYS n 
1 1199 TYR n 
1 1200 GLU n 
1 1201 GLN n 
1 1202 GLY n 
1 1203 SER n 
1 1204 GLY n 
1 1205 TYR n 
1 1206 ILE n 
1 1207 PRO n 
1 1208 GLU n 
1 1209 ALA n 
1 1210 PRO n 
1 1211 ARG n 
1 1212 ASP n 
1 1213 GLY n 
1 1214 GLN n 
1 1215 ALA n 
1 1216 TYR n 
1 1217 VAL n 
1 1218 ARG n 
1 1219 LYS n 
1 1220 ASP n 
1 1221 GLY n 
1 1222 GLU n 
1 1223 TRP n 
1 1224 VAL n 
1 1225 LEU n 
1 1226 LEU n 
1 1227 SER n 
1 1228 THR n 
1 1229 PHE n 
1 1230 LEU n 
1 1231 GLY n 
1 1232 ARG n 
1 1233 SER n 
1 1234 LEU n 
1 1235 GLU n 
1 1236 VAL n 
1 1237 LEU n 
1 1238 PHE n 
1 1239 GLN n 
1 1240 GLY n 
1 1241 PRO n 
1 1242 GLY n 
1 1243 SER n 
1 1244 GLY n 
1 1245 GLY n 
1 1246 LEU n 
1 1247 ASN n 
1 1248 ASP n 
1 1249 ILE n 
1 1250 PHE n 
1 1251 GLU n 
1 1252 ALA n 
1 1253 GLN n 
1 1254 LYS n 
1 1255 ILE n 
1 1256 GLU n 
1 1257 TRP n 
1 1258 HIS n 
1 1259 GLU n 
1 1260 GLY n 
1 1261 SER n 
1 1262 GLY n 
1 1263 HIS n 
1 1264 HIS n 
1 1265 HIS n 
1 1266 HIS n 
1 1267 HIS n 
1 1268 HIS n 
1 1269 HIS n 
1 1270 HIS n 
2 1    GLU n 
2 2    VAL n 
2 3    GLN n 
2 4    LEU n 
2 5    VAL n 
2 6    GLU n 
2 7    SER n 
2 8    GLY n 
2 9    GLY n 
2 10   GLY n 
2 11   VAL n 
2 12   VAL n 
2 13   GLN n 
2 14   PRO n 
2 15   GLY n 
2 16   GLY n 
2 17   SER n 
2 18   LEU n 
2 19   ARG n 
2 20   LEU n 
2 21   SER n 
2 22   CYS n 
2 23   ALA n 
2 24   ALA n 
2 25   SER n 
2 26   GLY n 
2 27   PHE n 
2 28   THR n 
2 29   PHE n 
2 30   ASN n 
2 31   SER n 
2 32   TYR n 
2 33   GLY n 
2 34   MET n 
2 35   HIS n 
2 36   TRP n 
2 37   VAL n 
2 38   ARG n 
2 39   GLN n 
2 40   ALA n 
2 41   PRO n 
2 42   GLY n 
2 43   LYS n 
2 44   GLY n 
2 45   LEU n 
2 46   GLU n 
2 47   TRP n 
2 48   VAL n 
2 49   ALA n 
2 50   PHE n 
2 51   ILE n 
2 52   ARG n 
2 53   TYR n 
2 54   ASP n 
2 55   GLY n 
2 56   GLY n 
2 57   ASN n 
2 58   LYS n 
2 59   TYR n 
2 60   TYR n 
2 61   ALA n 
2 62   ASP n 
2 63   SER n 
2 64   VAL n 
2 65   LYS n 
2 66   GLY n 
2 67   ARG n 
2 68   PHE n 
2 69   THR n 
2 70   ILE n 
2 71   SER n 
2 72   ARG n 
2 73   ASP n 
2 74   ASN n 
2 75   SER n 
2 76   LYS n 
2 77   ASN n 
2 78   THR n 
2 79   LEU n 
2 80   TYR n 
2 81   LEU n 
2 82   GLN n 
2 83   MET n 
2 84   LYS n 
2 85   SER n 
2 86   LEU n 
2 87   ARG n 
2 88   ALA n 
2 89   GLU n 
2 90   ASP n 
2 91   THR n 
2 92   ALA n 
2 93   VAL n 
2 94   TYR n 
2 95   TYR n 
2 96   CYS n 
2 97   ALA n 
2 98   ASN n 
2 99   LEU n 
2 100  LYS n 
2 101  ASP n 
2 102  SER n 
2 103  ARG n 
2 104  TYR n 
2 105  SER n 
2 106  GLY n 
2 107  SER n 
2 108  TYR n 
2 109  TYR n 
2 110  ASP n 
2 111  TYR n 
2 112  TRP n 
2 113  GLY n 
2 114  GLN n 
2 115  GLY n 
2 116  THR n 
2 117  LEU n 
2 118  VAL n 
2 119  THR n 
2 120  VAL n 
2 121  SER n 
2 122  SER n 
3 1    VAL n 
3 2    ILE n 
3 3    TRP n 
3 4    MET n 
3 5    THR n 
3 6    GLN n 
3 7    SER n 
3 8    PRO n 
3 9    SER n 
3 10   SER n 
3 11   LEU n 
3 12   SER n 
3 13   ALA n 
3 14   SER n 
3 15   VAL n 
3 16   GLY n 
3 17   ASP n 
3 18   ARG n 
3 19   VAL n 
3 20   THR n 
3 21   ILE n 
3 22   THR n 
3 23   CYS n 
3 24   GLN n 
3 25   ALA n 
3 26   SER n 
3 27   GLN n 
3 28   ASP n 
3 29   ILE n 
3 30   ARG n 
3 31   PHE n 
3 32   TYR n 
3 33   LEU n 
3 34   ASN n 
3 35   TRP n 
3 36   TYR n 
3 37   GLN n 
3 38   GLN n 
3 39   LYS n 
3 40   PRO n 
3 41   GLY n 
3 42   LYS n 
3 43   ALA n 
3 44   PRO n 
3 45   LYS n 
3 46   LEU n 
3 47   LEU n 
3 48   ILE n 
3 49   SER n 
3 50   ASP n 
3 51   ALA n 
3 52   SER n 
3 53   ASN n 
3 54   MET n 
3 55   GLU n 
3 56   THR n 
3 57   GLY n 
3 58   VAL n 
3 59   PRO n 
3 60   SER n 
3 61   ARG n 
3 62   PHE n 
3 63   SER n 
3 64   GLY n 
3 65   SER n 
3 66   GLY n 
3 67   SER n 
3 68   GLY n 
3 69   THR n 
3 70   ASP n 
3 71   PHE n 
3 72   THR n 
3 73   PHE n 
3 74   THR n 
3 75   ILE n 
3 76   SER n 
3 77   SER n 
3 78   LEU n 
3 79   GLN n 
3 80   PRO n 
3 81   GLU n 
3 82   ASP n 
3 83   ILE n 
3 84   ALA n 
3 85   THR n 
3 86   TYR n 
3 87   TYR n 
3 88   CYS n 
3 89   GLN n 
3 90   GLN n 
3 91   TYR n 
3 92   ASP n 
3 93   ASN n 
3 94   LEU n 
3 95   PRO n 
3 96   PHE n 
3 97   THR n 
3 98   PHE n 
3 99   GLY n 
3 100  PRO n 
3 101  GLY n 
3 102  THR n 
3 103  LYS n 
3 104  VAL n 
3 105  ASP n 
3 106  PHE n 
3 107  LYS n 
4 1    GLN n 
4 2    ILE n 
4 3    THR n 
4 4    LEU n 
4 5    LYS n 
4 6    GLU n 
4 7    SER n 
4 8    GLY n 
4 9    PRO n 
4 10   THR n 
4 11   LEU n 
4 12   VAL n 
4 13   LYS n 
4 14   PRO n 
4 15   THR n 
4 16   GLN n 
4 17   THR n 
4 18   LEU n 
4 19   THR n 
4 20   LEU n 
4 21   THR n 
4 22   CYS n 
4 23   LYS n 
4 24   LEU n 
4 25   SER n 
4 26   GLY n 
4 27   PHE n 
4 28   SER n 
4 29   VAL n 
4 30   ASN n 
4 31   THR n 
4 32   GLY n 
4 33   GLY n 
4 34   VAL n 
4 35   GLY n 
4 36   VAL n 
4 37   GLY n 
4 38   TRP n 
4 39   ILE n 
4 40   ARG n 
4 41   GLN n 
4 42   PRO n 
4 43   PRO n 
4 44   GLY n 
4 45   LYS n 
4 46   ALA n 
4 47   LEU n 
4 48   GLU n 
4 49   TRP n 
4 50   LEU n 
4 51   ALA n 
4 52   LEU n 
4 53   ILE n 
4 54   TYR n 
4 55   TRP n 
4 56   ASN n 
4 57   ASP n 
4 58   ASP n 
4 59   LYS n 
4 60   LEU n 
4 61   TYR n 
4 62   SER n 
4 63   PRO n 
4 64   SER n 
4 65   LEU n 
4 66   LYS n 
4 67   SER n 
4 68   ARG n 
4 69   LEU n 
4 70   THR n 
4 71   VAL n 
4 72   THR n 
4 73   LYS n 
4 74   ASP n 
4 75   THR n 
4 76   SER n 
4 77   LYS n 
4 78   ASN n 
4 79   GLN n 
4 80   VAL n 
4 81   VAL n 
4 82   LEU n 
4 83   THR n 
4 84   MET n 
4 85   THR n 
4 86   ASN n 
4 87   MET n 
4 88   ASP n 
4 89   PRO n 
4 90   VAL n 
4 91   ASP n 
4 92   THR n 
4 93   ALA n 
4 94   THR n 
4 95   TYR n 
4 96   TYR n 
4 97   CYS n 
4 98   ALA n 
4 99   HIS n 
4 100  VAL n 
4 101  LEU n 
4 102  VAL n 
4 103  TRP n 
4 104  PHE n 
4 105  GLY n 
4 106  GLU n 
4 107  VAL n 
4 108  LEU n 
4 109  PRO n 
4 110  ASP n 
4 111  ALA n 
4 112  PHE n 
4 113  ASP n 
4 114  VAL n 
4 115  TRP n 
4 116  GLY n 
4 117  GLN n 
4 118  GLY n 
4 119  THR n 
4 120  MET n 
4 121  VAL n 
4 122  THR n 
4 123  VAL n 
4 124  SER n 
4 125  SER n 
5 1    SER n 
5 2    TYR n 
5 3    GLU n 
5 4    LEU n 
5 5    THR n 
5 6    GLN n 
5 7    PRO n 
5 8    PRO n 
5 9    SER n 
5 10   VAL n 
5 11   SER n 
5 12   VAL n 
5 13   SER n 
5 14   PRO n 
5 15   GLY n 
5 16   GLN n 
5 17   THR n 
5 18   ALA n 
5 19   SER n 
5 20   ILE n 
5 21   THR n 
5 22   CYS n 
5 23   SER n 
5 24   GLY n 
5 25   ASP n 
5 26   LYS n 
5 27   LEU n 
5 28   GLY n 
5 29   GLU n 
5 30   THR n 
5 31   TYR n 
5 32   ALA n 
5 33   SER n 
5 34   TRP n 
5 35   TYR n 
5 36   GLN n 
5 37   GLN n 
5 38   LYS n 
5 39   PRO n 
5 40   GLY n 
5 41   GLN n 
5 42   SER n 
5 43   PRO n 
5 44   ILE n 
5 45   LEU n 
5 46   VAL n 
5 47   ILE n 
5 48   TYR n 
5 49   GLN n 
5 50   ASP n 
5 51   ASN n 
5 52   LYS n 
5 53   ARG n 
5 54   PRO n 
5 55   SER n 
5 56   GLY n 
5 57   ILE n 
5 58   PRO n 
5 59   GLU n 
5 60   ARG n 
5 61   PHE n 
5 62   SER n 
5 63   GLY n 
5 64   SER n 
5 65   ASN n 
5 66   SER n 
5 67   GLU n 
5 68   ASN n 
5 69   THR n 
5 70   ALA n 
5 71   THR n 
5 72   LEU n 
5 73   THR n 
5 74   ILE n 
5 75   SER n 
5 76   GLY n 
5 77   THR n 
5 78   GLN n 
5 79   THR n 
5 80   MET n 
5 81   ASP n 
5 82   GLU n 
5 83   ALA n 
5 84   ASP n 
5 85   TYR n 
5 86   TYR n 
5 87   CYS n 
5 88   GLN n 
5 89   ALA n 
5 90   TRP n 
5 91   ASP n 
5 92   LYS n 
5 93   THR n 
5 94   ILE n 
5 95   ALA n 
5 96   GLY n 
5 97   PHE n 
5 98   GLY n 
5 99   GLY n 
5 100  GLY n 
5 101  THR n 
5 102  LYS n 
5 103  LEU n 
5 104  THR n 
5 105  VAL 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 1270 ? ? 'S, 2' ? ? ? ? ? ? 'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? ? ? ? 
? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 122  ? ? ?      ? ? ? ? ? ? 'Homo sapiens'                                    9606    ? ? ? ? ? 
? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 107  ? ? ?      ? ? ? ? ? ? 'Homo sapiens'                                    9606    ? ? ? ? ? 
? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 125  ? ? ?      ? ? ? ? ? ? 'Homo sapiens'                                    9606    ? ? ? ? ? 
? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
5 1 sample 'Biological sequence' 1 105  ? ? ?      ? ? ? ? ? ? 'Homo sapiens'                                    9606    ? ? ? ? ? 
? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
6 oligosaccharide 
7 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 6 DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH                                          'Glycam Condensed Sequence' GMML       1.0   
2 6 '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 6 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}'           LINUCS                      PDB-CARE   ?     
4 7 DGlcpNAcb1-4DGlcpNAcb1-ROH                                                   'Glycam Condensed Sequence' GMML       1.0   
5 7 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1'                        WURCS                       PDB2Glycan 1.1.0 
6 7 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}'                              LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 6 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 6 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
3 7 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
# 
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                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    1    ?   ?   ?   A . n 
A 1 2    PHE 2    2    ?   ?   ?   A . n 
A 1 3    VAL 3    3    ?   ?   ?   A . n 
A 1 4    PHE 4    4    ?   ?   ?   A . n 
A 1 5    LEU 5    5    ?   ?   ?   A . n 
A 1 6    VAL 6    6    ?   ?   ?   A . n 
A 1 7    LEU 7    7    ?   ?   ?   A . n 
A 1 8    LEU 8    8    ?   ?   ?   A . n 
A 1 9    PRO 9    9    ?   ?   ?   A . n 
A 1 10   LEU 10   10   ?   ?   ?   A . n 
A 1 11   VAL 11   11   ?   ?   ?   A . n 
A 1 12   SER 12   12   ?   ?   ?   A . n 
A 1 13   SER 13   13   ?   ?   ?   A . n 
A 1 14   GLN 14   14   14  GLN GLN A . n 
A 1 15   CYS 15   15   15  CYS CYS A . n 
A 1 16   VAL 16   16   16  VAL VAL A . n 
A 1 17   ASN 17   17   17  ASN ASN A . n 
A 1 18   LEU 18   18   18  LEU LEU A . n 
A 1 19   THR 19   19   ?   ?   ?   A . n 
A 1 20   THR 20   20   ?   ?   ?   A . n 
A 1 21   ARG 21   21   21  ARG ARG A . n 
A 1 22   THR 22   22   22  THR THR A . n 
A 1 23   GLN 23   23   23  GLN GLN A . n 
A 1 24   LEU 24   24   24  LEU LEU A . n 
A 1 25   PRO 25   25   25  PRO PRO A . n 
A 1 26   PRO 26   26   26  PRO PRO A . n 
A 1 27   ALA 27   27   27  ALA ALA A . n 
A 1 28   TYR 28   28   28  TYR TYR A . n 
A 1 29   THR 29   29   29  THR THR A . n 
A 1 30   ASN 30   30   30  ASN ASN A . n 
A 1 31   SER 31   31   31  SER SER A . n 
A 1 32   PHE 32   32   32  PHE PHE A . n 
A 1 33   THR 33   33   33  THR THR A . n 
A 1 34   ARG 34   34   34  ARG ARG A . n 
A 1 35   GLY 35   35   35  GLY GLY A . n 
A 1 36   VAL 36   36   36  VAL VAL A . n 
A 1 37   TYR 37   37   37  TYR TYR A . n 
A 1 38   TYR 38   38   38  TYR TYR A . n 
A 1 39   PRO 39   39   39  PRO PRO A . n 
A 1 40   ASP 40   40   40  ASP ASP A . n 
A 1 41   LYS 41   41   41  LYS LYS A . n 
A 1 42   VAL 42   42   42  VAL VAL A . n 
A 1 43   PHE 43   43   43  PHE PHE A . n 
A 1 44   ARG 44   44   44  ARG ARG A . n 
A 1 45   SER 45   45   45  SER SER A . n 
A 1 46   SER 46   46   46  SER SER A . n 
A 1 47   VAL 47   47   47  VAL VAL A . n 
A 1 48   LEU 48   48   48  LEU LEU A . n 
A 1 49   HIS 49   49   49  HIS HIS A . n 
A 1 50   SER 50   50   50  SER SER A . n 
A 1 51   THR 51   51   51  THR THR A . n 
A 1 52   GLN 52   52   52  GLN GLN A . n 
A 1 53   ASP 53   53   53  ASP ASP A . n 
A 1 54   LEU 54   54   54  LEU LEU A . n 
A 1 55   PHE 55   55   55  PHE PHE A . n 
A 1 56   LEU 56   56   56  LEU LEU A . n 
A 1 57   PRO 57   57   57  PRO PRO A . n 
A 1 58   PHE 58   58   58  PHE PHE A . n 
A 1 59   PHE 59   59   59  PHE PHE A . n 
A 1 60   SER 60   60   60  SER SER A . n 
A 1 61   ASN 61   61   61  ASN ASN A . n 
A 1 62   VAL 62   62   62  VAL VAL A . n 
A 1 63   THR 63   63   63  THR THR A . n 
A 1 64   TRP 64   64   64  TRP TRP A . n 
A 1 65   PHE 65   65   65  PHE PHE A . n 
A 1 66   HIS 66   66   66  HIS HIS A . n 
A 1 67   ALA 67   67   67  ALA ALA A . n 
A 1 68   ILE 68   68   68  ILE ILE A . n 
A 1 69   HIS 69   69   69  HIS HIS A . n 
A 1 70   VAL 70   70   ?   ?   ?   A . n 
A 1 71   SER 71   71   ?   ?   ?   A . n 
A 1 72   GLY 72   72   ?   ?   ?   A . n 
A 1 73   THR 73   73   ?   ?   ?   A . n 
A 1 74   ASN 74   74   ?   ?   ?   A . n 
A 1 75   VAL 75   75   ?   ?   ?   A . n 
A 1 76   ILE 76   76   ?   ?   ?   A . n 
A 1 77   LYS 77   77   ?   ?   ?   A . n 
A 1 78   ARG 78   78   ?   ?   ?   A . n 
A 1 79   PHE 79   79   79  PHE PHE A . n 
A 1 80   ASP 80   80   80  ASP ASP A . n 
A 1 81   ASN 81   81   81  ASN ASN A . n 
A 1 82   PRO 82   82   82  PRO PRO A . n 
A 1 83   VAL 83   83   83  VAL VAL A . n 
A 1 84   LEU 84   84   84  LEU LEU A . n 
A 1 85   PRO 85   85   85  PRO PRO A . n 
A 1 86   PHE 86   86   86  PHE PHE A . n 
A 1 87   ASN 87   87   87  ASN ASN A . n 
A 1 88   ASP 88   88   88  ASP ASP A . n 
A 1 89   GLY 89   89   89  GLY GLY A . n 
A 1 90   VAL 90   90   90  VAL VAL A . n 
A 1 91   TYR 91   91   91  TYR TYR A . n 
A 1 92   PHE 92   92   92  PHE PHE A . n 
A 1 93   ALA 93   93   93  ALA ALA A . n 
A 1 94   SER 94   94   94  SER SER A . n 
A 1 95   THR 95   95   95  THR THR A . n 
A 1 96   GLU 96   96   96  GLU GLU A . n 
A 1 97   LYS 97   97   97  LYS LYS A . n 
A 1 98   SER 98   98   98  SER SER A . n 
A 1 99   ASN 99   99   99  ASN ASN A . n 
A 1 100  ILE 100  100  100 ILE ILE A . n 
A 1 101  ILE 101  101  101 ILE ILE A . n 
A 1 102  ARG 102  102  102 ARG ARG A . n 
A 1 103  GLY 103  103  103 GLY GLY A . n 
A 1 104  TRP 104  104  104 TRP TRP A . n 
A 1 105  ILE 105  105  105 ILE ILE A . n 
A 1 106  PHE 106  106  106 PHE PHE A . n 
A 1 107  GLY 107  107  107 GLY GLY A . n 
A 1 108  THR 108  108  108 THR THR A . n 
A 1 109  THR 109  109  109 THR THR A . n 
A 1 110  LEU 110  110  110 LEU LEU A . n 
A 1 111  ASP 111  111  111 ASP ASP A . n 
A 1 112  SER 112  112  112 SER SER A . n 
A 1 113  LYS 113  113  113 LYS LYS A . n 
A 1 114  THR 114  114  114 THR THR A . n 
A 1 115  GLN 115  115  115 GLN GLN A . n 
A 1 116  SER 116  116  116 SER SER A . n 
A 1 117  LEU 117  117  117 LEU LEU A . n 
A 1 118  LEU 118  118  118 LEU LEU A . n 
A 1 119  ILE 119  119  119 ILE ILE A . n 
A 1 120  VAL 120  120  120 VAL VAL A . n 
A 1 121  ASN 121  121  121 ASN ASN A . n 
A 1 122  ASN 122  122  122 ASN ASN A . n 
A 1 123  ALA 123  123  123 ALA ALA A . n 
A 1 124  THR 124  124  124 THR THR A . n 
A 1 125  ASN 125  125  125 ASN ASN A . n 
A 1 126  VAL 126  126  126 VAL VAL A . n 
A 1 127  VAL 127  127  127 VAL VAL A . n 
A 1 128  ILE 128  128  128 ILE ILE A . n 
A 1 129  LYS 129  129  129 LYS LYS A . n 
A 1 130  VAL 130  130  130 VAL VAL A . n 
A 1 131  CYS 131  131  131 CYS CYS A . n 
A 1 132  GLU 132  132  132 GLU GLU A . n 
A 1 133  PHE 133  133  133 PHE PHE A . n 
A 1 134  GLN 134  134  134 GLN GLN A . n 
A 1 135  PHE 135  135  135 PHE PHE A . n 
A 1 136  CYS 136  136  136 CYS CYS A . n 
A 1 137  ASN 137  137  137 ASN ASN A . n 
A 1 138  ASP 138  138  138 ASP ASP A . n 
A 1 139  PRO 139  139  139 PRO PRO A . n 
A 1 140  PHE 140  140  140 PHE PHE A . n 
A 1 141  LEU 141  141  141 LEU LEU A . n 
A 1 142  GLY 142  142  142 GLY GLY A . n 
A 1 143  VAL 143  143  143 VAL VAL A . n 
A 1 144  TYR 144  144  144 TYR TYR A . n 
A 1 145  TYR 145  145  145 TYR TYR A . n 
A 1 146  HIS 146  146  146 HIS HIS A . n 
A 1 147  LYS 147  147  147 LYS LYS A . n 
A 1 148  ASN 148  148  148 ASN ASN A . n 
A 1 149  ASN 149  149  149 ASN ASN A . n 
A 1 150  LYS 150  150  150 LYS LYS A . n 
A 1 151  SER 151  151  151 SER SER A . n 
A 1 152  TRP 152  152  152 TRP TRP A . n 
A 1 153  MET 153  153  153 MET MET A . n 
A 1 154  GLU 154  154  154 GLU GLU A . n 
A 1 155  SER 155  155  155 SER SER A . n 
A 1 156  GLU 156  156  156 GLU GLU A . n 
A 1 157  PHE 157  157  157 PHE PHE A . n 
A 1 158  ARG 158  158  158 ARG ARG A . n 
A 1 159  VAL 159  159  159 VAL VAL A . n 
A 1 160  TYR 160  160  160 TYR TYR A . n 
A 1 161  SER 161  161  161 SER SER A . n 
A 1 162  SER 162  162  162 SER SER A . n 
A 1 163  ALA 163  163  163 ALA ALA A . n 
A 1 164  ASN 164  164  164 ASN ASN A . n 
A 1 165  ASN 165  165  165 ASN ASN A . n 
A 1 166  CYS 166  166  166 CYS CYS A . n 
A 1 167  THR 167  167  167 THR THR A . n 
A 1 168  PHE 168  168  168 PHE PHE A . n 
A 1 169  GLU 169  169  169 GLU GLU A . n 
A 1 170  TYR 170  170  170 TYR TYR A . n 
A 1 171  VAL 171  171  171 VAL VAL A . n 
A 1 172  SER 172  172  172 SER SER A . n 
A 1 173  GLN 173  173  173 GLN GLN A . n 
A 1 174  PRO 174  174  174 PRO PRO A . n 
A 1 175  PHE 175  175  175 PHE PHE A . n 
A 1 176  LEU 176  176  176 LEU LEU A . n 
A 1 177  MET 177  177  ?   ?   ?   A . n 
A 1 178  ASP 178  178  ?   ?   ?   A . n 
A 1 179  LEU 179  179  ?   ?   ?   A . n 
A 1 180  GLU 180  180  ?   ?   ?   A . n 
A 1 181  GLY 181  181  ?   ?   ?   A . n 
A 1 182  LYS 182  182  ?   ?   ?   A . n 
A 1 183  GLN 183  183  ?   ?   ?   A . n 
A 1 184  GLY 184  184  ?   ?   ?   A . n 
A 1 185  ASN 185  185  ?   ?   ?   A . n 
A 1 186  PHE 186  186  186 PHE PHE A . n 
A 1 187  LYS 187  187  187 LYS LYS A . n 
A 1 188  ASN 188  188  188 ASN ASN A . n 
A 1 189  LEU 189  189  189 LEU LEU A . n 
A 1 190  ARG 190  190  190 ARG ARG A . n 
A 1 191  GLU 191  191  191 GLU GLU A . n 
A 1 192  PHE 192  192  192 PHE PHE A . n 
A 1 193  VAL 193  193  193 VAL VAL A . n 
A 1 194  PHE 194  194  194 PHE PHE A . n 
A 1 195  LYS 195  195  195 LYS LYS A . n 
A 1 196  ASN 196  196  196 ASN ASN A . n 
A 1 197  ILE 197  197  197 ILE ILE A . n 
A 1 198  ASP 198  198  198 ASP ASP A . n 
A 1 199  GLY 199  199  199 GLY GLY A . n 
A 1 200  TYR 200  200  200 TYR TYR A . n 
A 1 201  PHE 201  201  201 PHE PHE A . n 
A 1 202  LYS 202  202  202 LYS LYS A . n 
A 1 203  ILE 203  203  203 ILE ILE A . n 
A 1 204  TYR 204  204  204 TYR TYR A . n 
A 1 205  SER 205  205  205 SER SER A . n 
A 1 206  LYS 206  206  206 LYS LYS A . n 
A 1 207  HIS 207  207  207 HIS HIS A . n 
A 1 208  THR 208  208  208 THR THR A . n 
A 1 209  PRO 209  209  209 PRO PRO A . n 
A 1 210  ILE 210  210  210 ILE ILE A . n 
A 1 211  ASN 211  211  211 ASN ASN A . n 
A 1 212  LEU 212  212  212 LEU LEU A . n 
A 1 213  VAL 213  213  213 VAL VAL A . n 
A 1 214  ARG 214  214  214 ARG ARG A . n 
A 1 215  ASP 215  215  215 ASP ASP A . n 
A 1 216  LEU 216  216  216 LEU LEU A . n 
A 1 217  PRO 217  217  217 PRO PRO A . n 
A 1 218  GLN 218  218  218 GLN GLN A . n 
A 1 219  GLY 219  219  219 GLY GLY A . n 
A 1 220  PHE 220  220  220 PHE PHE A . n 
A 1 221  SER 221  221  221 SER SER A . n 
A 1 222  ALA 222  222  222 ALA ALA A . n 
A 1 223  LEU 223  223  223 LEU LEU A . n 
A 1 224  GLU 224  224  224 GLU GLU A . n 
A 1 225  PRO 225  225  225 PRO PRO A . n 
A 1 226  LEU 226  226  226 LEU LEU A . n 
A 1 227  VAL 227  227  227 VAL VAL A . n 
A 1 228  ASP 228  228  228 ASP ASP A . n 
A 1 229  LEU 229  229  229 LEU LEU A . n 
A 1 230  PRO 230  230  230 PRO PRO A . n 
A 1 231  ILE 231  231  231 ILE ILE A . n 
A 1 232  GLY 232  232  232 GLY GLY A . n 
A 1 233  ILE 233  233  233 ILE ILE A . n 
A 1 234  ASN 234  234  234 ASN ASN A . n 
A 1 235  ILE 235  235  235 ILE ILE A . n 
A 1 236  THR 236  236  236 THR THR A . n 
A 1 237  ARG 237  237  237 ARG ARG A . n 
A 1 238  PHE 238  238  238 PHE PHE A . n 
A 1 239  GLN 239  239  239 GLN GLN A . n 
A 1 240  THR 240  240  240 THR THR A . n 
A 1 241  LEU 241  241  241 LEU LEU A . n 
A 1 242  LEU 242  242  242 LEU LEU A . n 
A 1 243  ALA 243  243  243 ALA ALA A . n 
A 1 244  LEU 244  244  244 LEU LEU A . n 
A 1 245  HIS 245  245  245 HIS HIS A . n 
A 1 246  ASN 246  246  246 ASN ASN A . n 
A 1 247  SER 247  247  247 SER SER A . n 
A 1 248  SER 248  248  248 SER SER A . n 
A 1 249  SER 249  249  249 SER SER A . n 
A 1 250  GLY 250  250  250 GLY GLY A . n 
A 1 251  TRP 251  251  251 TRP TRP A . n 
A 1 252  THR 252  252  252 THR THR A . n 
A 1 253  ALA 253  253  253 ALA ALA A . n 
A 1 254  GLY 254  254  254 GLY GLY A . n 
A 1 255  ALA 255  255  255 ALA ALA A . n 
A 1 256  ALA 256  256  256 ALA ALA A . n 
A 1 257  ALA 257  257  257 ALA ALA A . n 
A 1 258  TYR 258  258  258 TYR TYR A . n 
A 1 259  TYR 259  259  259 TYR TYR A . n 
A 1 260  VAL 260  260  260 VAL VAL A . n 
A 1 261  GLY 261  261  261 GLY GLY A . n 
A 1 262  TYR 262  262  262 TYR TYR A . n 
A 1 263  LEU 263  263  263 LEU LEU A . n 
A 1 264  GLN 264  264  264 GLN GLN A . n 
A 1 265  PRO 265  265  265 PRO PRO A . n 
A 1 266  ARG 266  266  266 ARG ARG A . n 
A 1 267  THR 267  267  267 THR THR A . n 
A 1 268  PHE 268  268  268 PHE PHE A . n 
A 1 269  LEU 269  269  269 LEU LEU A . n 
A 1 270  LEU 270  270  270 LEU LEU A . n 
A 1 271  LYS 271  271  271 LYS LYS A . n 
A 1 272  TYR 272  272  272 TYR TYR A . n 
A 1 273  ASN 273  273  273 ASN ASN A . n 
A 1 274  GLU 274  274  274 GLU GLU A . n 
A 1 275  ASN 275  275  275 ASN ASN A . n 
A 1 276  GLY 276  276  276 GLY GLY A . n 
A 1 277  THR 277  277  277 THR THR A . n 
A 1 278  ILE 278  278  278 ILE ILE A . n 
A 1 279  THR 279  279  279 THR THR A . n 
A 1 280  ASP 280  280  280 ASP ASP A . n 
A 1 281  ALA 281  281  281 ALA ALA A . n 
A 1 282  VAL 282  282  282 VAL VAL A . n 
A 1 283  ASP 283  283  283 ASP ASP A . n 
A 1 284  CYS 284  284  284 CYS CYS A . n 
A 1 285  ALA 285  285  285 ALA ALA A . n 
A 1 286  LEU 286  286  286 LEU LEU A . n 
A 1 287  ASP 287  287  287 ASP ASP A . n 
A 1 288  PRO 288  288  288 PRO PRO A . n 
A 1 289  LEU 289  289  289 LEU LEU A . n 
A 1 290  SER 290  290  290 SER SER A . n 
A 1 291  GLU 291  291  291 GLU GLU A . n 
A 1 292  THR 292  292  292 THR THR A . n 
A 1 293  LYS 293  293  293 LYS LYS A . n 
A 1 294  CYS 294  294  294 CYS CYS A . n 
A 1 295  THR 295  295  295 THR THR A . n 
A 1 296  LEU 296  296  296 LEU LEU A . n 
A 1 297  LYS 297  297  297 LYS LYS A . n 
A 1 298  SER 298  298  298 SER SER A . n 
A 1 299  PHE 299  299  ?   ?   ?   A . n 
A 1 300  THR 300  300  ?   ?   ?   A . n 
A 1 301  VAL 301  301  ?   ?   ?   A . n 
A 1 302  GLU 302  302  ?   ?   ?   A . n 
A 1 303  LYS 303  303  ?   ?   ?   A . n 
A 1 304  GLY 304  304  ?   ?   ?   A . n 
A 1 305  ILE 305  305  ?   ?   ?   A . n 
A 1 306  TYR 306  306  ?   ?   ?   A . n 
A 1 307  GLN 307  307  ?   ?   ?   A . n 
A 1 308  THR 308  308  ?   ?   ?   A . n 
A 1 309  SER 309  309  ?   ?   ?   A . n 
A 1 310  ASN 310  310  ?   ?   ?   A . n 
A 1 311  PHE 311  311  ?   ?   ?   A . n 
A 1 312  ARG 312  312  ?   ?   ?   A . n 
A 1 313  VAL 313  313  ?   ?   ?   A . n 
A 1 314  GLN 314  314  ?   ?   ?   A . n 
A 1 315  PRO 315  315  ?   ?   ?   A . n 
A 1 316  THR 316  316  ?   ?   ?   A . n 
A 1 317  GLU 317  317  ?   ?   ?   A . n 
A 1 318  SER 318  318  ?   ?   ?   A . n 
A 1 319  ILE 319  319  ?   ?   ?   A . n 
A 1 320  VAL 320  320  ?   ?   ?   A . n 
A 1 321  ARG 321  321  ?   ?   ?   A . n 
A 1 322  PHE 322  322  ?   ?   ?   A . n 
A 1 323  PRO 323  323  ?   ?   ?   A . n 
A 1 324  ASN 324  324  ?   ?   ?   A . n 
A 1 325  ILE 325  325  ?   ?   ?   A . n 
A 1 326  THR 326  326  ?   ?   ?   A . n 
A 1 327  ASN 327  327  ?   ?   ?   A . n 
A 1 328  LEU 328  328  ?   ?   ?   A . n 
A 1 329  CYS 329  329  ?   ?   ?   A . n 
A 1 330  PRO 330  330  ?   ?   ?   A . n 
A 1 331  PHE 331  331  ?   ?   ?   A . n 
A 1 332  GLY 332  332  ?   ?   ?   A . n 
A 1 333  GLU 333  333  ?   ?   ?   A . n 
A 1 334  VAL 334  334  ?   ?   ?   A . n 
A 1 335  PHE 335  335  ?   ?   ?   A . n 
A 1 336  ASN 336  336  ?   ?   ?   A . n 
A 1 337  ALA 337  337  ?   ?   ?   A . n 
A 1 338  THR 338  338  ?   ?   ?   A . n 
A 1 339  ARG 339  339  ?   ?   ?   A . n 
A 1 340  PHE 340  340  ?   ?   ?   A . n 
A 1 341  ALA 341  341  ?   ?   ?   A . n 
A 1 342  SER 342  342  ?   ?   ?   A . n 
A 1 343  VAL 343  343  ?   ?   ?   A . n 
A 1 344  TYR 344  344  ?   ?   ?   A . n 
A 1 345  ALA 345  345  ?   ?   ?   A . n 
A 1 346  TRP 346  346  ?   ?   ?   A . n 
A 1 347  ASN 347  347  ?   ?   ?   A . n 
A 1 348  ARG 348  348  ?   ?   ?   A . n 
A 1 349  LYS 349  349  ?   ?   ?   A . n 
A 1 350  ARG 350  350  ?   ?   ?   A . n 
A 1 351  ILE 351  351  ?   ?   ?   A . n 
A 1 352  SER 352  352  ?   ?   ?   A . n 
A 1 353  ASN 353  353  ?   ?   ?   A . n 
A 1 354  CYS 354  354  ?   ?   ?   A . n 
A 1 355  VAL 355  355  ?   ?   ?   A . n 
A 1 356  ALA 356  356  ?   ?   ?   A . n 
A 1 357  ASP 357  357  ?   ?   ?   A . n 
A 1 358  TYR 358  358  ?   ?   ?   A . n 
A 1 359  SER 359  359  ?   ?   ?   A . n 
A 1 360  VAL 360  360  ?   ?   ?   A . n 
A 1 361  LEU 361  361  ?   ?   ?   A . n 
A 1 362  TYR 362  362  ?   ?   ?   A . n 
A 1 363  ASN 363  363  ?   ?   ?   A . n 
A 1 364  SER 364  364  ?   ?   ?   A . n 
A 1 365  ALA 365  365  ?   ?   ?   A . n 
A 1 366  SER 366  366  ?   ?   ?   A . n 
A 1 367  PHE 367  367  ?   ?   ?   A . n 
A 1 368  SER 368  368  ?   ?   ?   A . n 
A 1 369  THR 369  369  ?   ?   ?   A . n 
A 1 370  PHE 370  370  ?   ?   ?   A . n 
A 1 371  LYS 371  371  ?   ?   ?   A . n 
A 1 372  CYS 372  372  ?   ?   ?   A . n 
A 1 373  TYR 373  373  ?   ?   ?   A . n 
A 1 374  GLY 374  374  ?   ?   ?   A . n 
A 1 375  VAL 375  375  ?   ?   ?   A . n 
A 1 376  CYS 376  376  ?   ?   ?   A . n 
A 1 377  PRO 377  377  ?   ?   ?   A . n 
A 1 378  THR 378  378  ?   ?   ?   A . n 
A 1 379  LYS 379  379  ?   ?   ?   A . n 
A 1 380  LEU 380  380  ?   ?   ?   A . n 
A 1 381  ASN 381  381  ?   ?   ?   A . n 
A 1 382  ASP 382  382  ?   ?   ?   A . n 
A 1 383  LEU 383  383  ?   ?   ?   A . n 
A 1 384  CYS 384  384  ?   ?   ?   A . n 
A 1 385  PHE 385  385  ?   ?   ?   A . n 
A 1 386  THR 386  386  ?   ?   ?   A . n 
A 1 387  ASN 387  387  ?   ?   ?   A . n 
A 1 388  VAL 388  388  ?   ?   ?   A . n 
A 1 389  TYR 389  389  ?   ?   ?   A . n 
A 1 390  ALA 390  390  ?   ?   ?   A . n 
A 1 391  ASP 391  391  ?   ?   ?   A . n 
A 1 392  SER 392  392  ?   ?   ?   A . n 
A 1 393  PHE 393  393  ?   ?   ?   A . n 
A 1 394  VAL 394  394  ?   ?   ?   A . n 
A 1 395  ILE 395  395  ?   ?   ?   A . n 
A 1 396  ARG 396  396  ?   ?   ?   A . n 
A 1 397  GLY 397  397  ?   ?   ?   A . n 
A 1 398  ASP 398  398  ?   ?   ?   A . n 
A 1 399  GLU 399  399  ?   ?   ?   A . n 
A 1 400  VAL 400  400  ?   ?   ?   A . n 
A 1 401  ARG 401  401  ?   ?   ?   A . n 
A 1 402  GLN 402  402  ?   ?   ?   A . n 
A 1 403  ILE 403  403  ?   ?   ?   A . n 
A 1 404  ALA 404  404  ?   ?   ?   A . n 
A 1 405  PRO 405  405  ?   ?   ?   A . n 
A 1 406  GLY 406  406  ?   ?   ?   A . n 
A 1 407  GLN 407  407  ?   ?   ?   A . n 
A 1 408  THR 408  408  ?   ?   ?   A . n 
A 1 409  GLY 409  409  ?   ?   ?   A . n 
A 1 410  LYS 410  410  ?   ?   ?   A . n 
A 1 411  ILE 411  411  ?   ?   ?   A . n 
A 1 412  ALA 412  412  ?   ?   ?   A . n 
A 1 413  ASP 413  413  ?   ?   ?   A . n 
A 1 414  TYR 414  414  ?   ?   ?   A . n 
A 1 415  ASN 415  415  ?   ?   ?   A . n 
A 1 416  TYR 416  416  ?   ?   ?   A . n 
A 1 417  LYS 417  417  ?   ?   ?   A . n 
A 1 418  LEU 418  418  ?   ?   ?   A . n 
A 1 419  PRO 419  419  ?   ?   ?   A . n 
A 1 420  ASP 420  420  ?   ?   ?   A . n 
A 1 421  ASP 421  421  ?   ?   ?   A . n 
A 1 422  PHE 422  422  ?   ?   ?   A . n 
A 1 423  THR 423  423  ?   ?   ?   A . n 
A 1 424  GLY 424  424  ?   ?   ?   A . n 
A 1 425  CYS 425  425  ?   ?   ?   A . n 
A 1 426  VAL 426  426  ?   ?   ?   A . n 
A 1 427  ILE 427  427  ?   ?   ?   A . n 
A 1 428  ALA 428  428  ?   ?   ?   A . n 
A 1 429  TRP 429  429  ?   ?   ?   A . n 
A 1 430  ASN 430  430  ?   ?   ?   A . n 
A 1 431  SER 431  431  ?   ?   ?   A . n 
A 1 432  ASN 432  432  ?   ?   ?   A . n 
A 1 433  ASN 433  433  ?   ?   ?   A . n 
A 1 434  LEU 434  434  ?   ?   ?   A . n 
A 1 435  ASP 435  435  ?   ?   ?   A . n 
A 1 436  SER 436  436  ?   ?   ?   A . n 
A 1 437  LYS 437  437  ?   ?   ?   A . n 
A 1 438  VAL 438  438  ?   ?   ?   A . n 
A 1 439  GLY 439  439  ?   ?   ?   A . n 
A 1 440  GLY 440  440  ?   ?   ?   A . n 
A 1 441  ASN 441  441  ?   ?   ?   A . n 
A 1 442  TYR 442  442  ?   ?   ?   A . n 
A 1 443  ASN 443  443  ?   ?   ?   A . n 
A 1 444  TYR 444  444  ?   ?   ?   A . n 
A 1 445  GLN 445  445  ?   ?   ?   A . n 
A 1 446  TYR 446  446  ?   ?   ?   A . n 
A 1 447  ARG 447  447  ?   ?   ?   A . n 
A 1 448  LEU 448  448  ?   ?   ?   A . n 
A 1 449  PHE 449  449  ?   ?   ?   A . n 
A 1 450  ARG 450  450  ?   ?   ?   A . n 
A 1 451  LYS 451  451  ?   ?   ?   A . n 
A 1 452  SER 452  452  ?   ?   ?   A . n 
A 1 453  ASN 453  453  ?   ?   ?   A . n 
A 1 454  LEU 454  454  ?   ?   ?   A . n 
A 1 455  LYS 455  455  ?   ?   ?   A . n 
A 1 456  PRO 456  456  ?   ?   ?   A . n 
A 1 457  PHE 457  457  ?   ?   ?   A . n 
A 1 458  GLU 458  458  ?   ?   ?   A . n 
A 1 459  ARG 459  459  ?   ?   ?   A . n 
A 1 460  ASP 460  460  ?   ?   ?   A . n 
A 1 461  ILE 461  461  ?   ?   ?   A . n 
A 1 462  SER 462  462  ?   ?   ?   A . n 
A 1 463  THR 463  463  ?   ?   ?   A . n 
A 1 464  GLU 464  464  ?   ?   ?   A . n 
A 1 465  ILE 465  465  ?   ?   ?   A . n 
A 1 466  TYR 466  466  ?   ?   ?   A . n 
A 1 467  GLN 467  467  ?   ?   ?   A . n 
A 1 468  ALA 468  468  ?   ?   ?   A . n 
A 1 469  GLY 469  469  ?   ?   ?   A . n 
A 1 470  SER 470  470  ?   ?   ?   A . n 
A 1 471  THR 471  471  ?   ?   ?   A . n 
A 1 472  PRO 472  472  ?   ?   ?   A . n 
A 1 473  CYS 473  473  ?   ?   ?   A . n 
A 1 474  ASN 474  474  ?   ?   ?   A . n 
A 1 475  GLY 475  475  ?   ?   ?   A . n 
A 1 476  VAL 476  476  ?   ?   ?   A . n 
A 1 477  GLU 477  477  ?   ?   ?   A . n 
A 1 478  GLY 478  478  ?   ?   ?   A . n 
A 1 479  PHE 479  479  ?   ?   ?   A . n 
A 1 480  ASN 480  480  ?   ?   ?   A . n 
A 1 481  CYS 481  481  ?   ?   ?   A . n 
A 1 482  TYR 482  482  ?   ?   ?   A . n 
A 1 483  SER 483  483  ?   ?   ?   A . n 
A 1 484  PRO 484  484  ?   ?   ?   A . n 
A 1 485  LEU 485  485  ?   ?   ?   A . n 
A 1 486  GLN 486  486  ?   ?   ?   A . n 
A 1 487  SER 487  487  ?   ?   ?   A . n 
A 1 488  TYR 488  488  ?   ?   ?   A . n 
A 1 489  GLY 489  489  ?   ?   ?   A . n 
A 1 490  PHE 490  490  ?   ?   ?   A . n 
A 1 491  GLN 491  491  ?   ?   ?   A . n 
A 1 492  PRO 492  492  ?   ?   ?   A . n 
A 1 493  THR 493  493  ?   ?   ?   A . n 
A 1 494  ASN 494  494  ?   ?   ?   A . n 
A 1 495  GLY 495  495  ?   ?   ?   A . n 
A 1 496  VAL 496  496  ?   ?   ?   A . n 
A 1 497  GLY 497  497  ?   ?   ?   A . n 
A 1 498  TYR 498  498  ?   ?   ?   A . n 
A 1 499  GLN 499  499  ?   ?   ?   A . n 
A 1 500  PRO 500  500  ?   ?   ?   A . n 
A 1 501  TYR 501  501  ?   ?   ?   A . n 
A 1 502  ARG 502  502  ?   ?   ?   A . n 
A 1 503  VAL 503  503  ?   ?   ?   A . n 
A 1 504  VAL 504  504  ?   ?   ?   A . n 
A 1 505  VAL 505  505  ?   ?   ?   A . n 
A 1 506  LEU 506  506  ?   ?   ?   A . n 
A 1 507  SER 507  507  ?   ?   ?   A . n 
A 1 508  PHE 508  508  ?   ?   ?   A . n 
A 1 509  GLU 509  509  ?   ?   ?   A . n 
A 1 510  LEU 510  510  ?   ?   ?   A . n 
A 1 511  LEU 511  511  ?   ?   ?   A . n 
A 1 512  HIS 512  512  ?   ?   ?   A . n 
A 1 513  ALA 513  513  ?   ?   ?   A . n 
A 1 514  PRO 514  514  ?   ?   ?   A . n 
A 1 515  ALA 515  515  ?   ?   ?   A . n 
A 1 516  THR 516  516  ?   ?   ?   A . n 
A 1 517  VAL 517  517  ?   ?   ?   A . n 
A 1 518  CYS 518  518  ?   ?   ?   A . n 
A 1 519  GLY 519  519  ?   ?   ?   A . n 
A 1 520  PRO 520  520  ?   ?   ?   A . n 
A 1 521  LYS 521  521  ?   ?   ?   A . n 
A 1 522  LYS 522  522  ?   ?   ?   A . n 
A 1 523  SER 523  523  ?   ?   ?   A . n 
A 1 524  THR 524  524  ?   ?   ?   A . n 
A 1 525  ASN 525  525  ?   ?   ?   A . n 
A 1 526  LEU 526  526  ?   ?   ?   A . n 
A 1 527  VAL 527  527  ?   ?   ?   A . n 
A 1 528  LYS 528  528  ?   ?   ?   A . n 
A 1 529  ASN 529  529  ?   ?   ?   A . n 
A 1 530  LYS 530  530  ?   ?   ?   A . n 
A 1 531  CYS 531  531  ?   ?   ?   A . n 
A 1 532  VAL 532  532  ?   ?   ?   A . n 
A 1 533  ASN 533  533  ?   ?   ?   A . n 
A 1 534  PHE 534  534  ?   ?   ?   A . n 
A 1 535  ASN 535  535  ?   ?   ?   A . n 
A 1 536  PHE 536  536  ?   ?   ?   A . n 
A 1 537  ASN 537  537  ?   ?   ?   A . n 
A 1 538  GLY 538  538  ?   ?   ?   A . n 
A 1 539  LEU 539  539  ?   ?   ?   A . n 
A 1 540  THR 540  540  ?   ?   ?   A . n 
A 1 541  GLY 541  541  ?   ?   ?   A . n 
A 1 542  THR 542  542  ?   ?   ?   A . n 
A 1 543  GLY 543  543  ?   ?   ?   A . n 
A 1 544  VAL 544  544  ?   ?   ?   A . n 
A 1 545  LEU 545  545  ?   ?   ?   A . n 
A 1 546  THR 546  546  ?   ?   ?   A . n 
A 1 547  GLU 547  547  ?   ?   ?   A . n 
A 1 548  SER 548  548  ?   ?   ?   A . n 
A 1 549  ASN 549  549  ?   ?   ?   A . n 
A 1 550  LYS 550  550  ?   ?   ?   A . n 
A 1 551  LYS 551  551  ?   ?   ?   A . n 
A 1 552  PHE 552  552  ?   ?   ?   A . n 
A 1 553  LEU 553  553  ?   ?   ?   A . n 
A 1 554  PRO 554  554  ?   ?   ?   A . n 
A 1 555  PHE 555  555  ?   ?   ?   A . n 
A 1 556  GLN 556  556  ?   ?   ?   A . n 
A 1 557  GLN 557  557  ?   ?   ?   A . n 
A 1 558  PHE 558  558  ?   ?   ?   A . n 
A 1 559  GLY 559  559  ?   ?   ?   A . n 
A 1 560  ARG 560  560  ?   ?   ?   A . n 
A 1 561  ASP 561  561  ?   ?   ?   A . n 
A 1 562  ILE 562  562  ?   ?   ?   A . n 
A 1 563  ALA 563  563  ?   ?   ?   A . n 
A 1 564  ASP 564  564  ?   ?   ?   A . n 
A 1 565  THR 565  565  ?   ?   ?   A . n 
A 1 566  THR 566  566  ?   ?   ?   A . n 
A 1 567  ASP 567  567  ?   ?   ?   A . n 
A 1 568  ALA 568  568  ?   ?   ?   A . n 
A 1 569  VAL 569  569  ?   ?   ?   A . n 
A 1 570  ARG 570  570  ?   ?   ?   A . n 
A 1 571  ASP 571  571  ?   ?   ?   A . n 
A 1 572  PRO 572  572  ?   ?   ?   A . n 
A 1 573  GLN 573  573  ?   ?   ?   A . n 
A 1 574  THR 574  574  ?   ?   ?   A . n 
A 1 575  LEU 575  575  ?   ?   ?   A . n 
A 1 576  GLU 576  576  ?   ?   ?   A . n 
A 1 577  ILE 577  577  ?   ?   ?   A . n 
A 1 578  LEU 578  578  ?   ?   ?   A . n 
A 1 579  ASP 579  579  ?   ?   ?   A . n 
A 1 580  ILE 580  580  ?   ?   ?   A . n 
A 1 581  THR 581  581  ?   ?   ?   A . n 
A 1 582  PRO 582  582  ?   ?   ?   A . n 
A 1 583  CYS 583  583  ?   ?   ?   A . n 
A 1 584  SER 584  584  ?   ?   ?   A . n 
A 1 585  PHE 585  585  ?   ?   ?   A . n 
A 1 586  GLY 586  586  ?   ?   ?   A . n 
A 1 587  GLY 587  587  ?   ?   ?   A . n 
A 1 588  VAL 588  588  ?   ?   ?   A . n 
A 1 589  SER 589  589  ?   ?   ?   A . n 
A 1 590  VAL 590  590  ?   ?   ?   A . n 
A 1 591  ILE 591  591  ?   ?   ?   A . n 
A 1 592  THR 592  592  ?   ?   ?   A . n 
A 1 593  PRO 593  593  ?   ?   ?   A . n 
A 1 594  GLY 594  594  ?   ?   ?   A . n 
A 1 595  THR 595  595  ?   ?   ?   A . n 
A 1 596  ASN 596  596  ?   ?   ?   A . n 
A 1 597  THR 597  597  ?   ?   ?   A . n 
A 1 598  SER 598  598  ?   ?   ?   A . n 
A 1 599  ASN 599  599  ?   ?   ?   A . n 
A 1 600  GLN 600  600  ?   ?   ?   A . n 
A 1 601  VAL 601  601  ?   ?   ?   A . n 
A 1 602  ALA 602  602  ?   ?   ?   A . n 
A 1 603  VAL 603  603  ?   ?   ?   A . n 
A 1 604  LEU 604  604  ?   ?   ?   A . n 
A 1 605  TYR 605  605  ?   ?   ?   A . n 
A 1 606  GLN 606  606  ?   ?   ?   A . n 
A 1 607  GLY 607  607  ?   ?   ?   A . n 
A 1 608  VAL 608  608  ?   ?   ?   A . n 
A 1 609  ASN 609  609  ?   ?   ?   A . n 
A 1 610  CYS 610  610  ?   ?   ?   A . n 
A 1 611  THR 611  611  ?   ?   ?   A . n 
A 1 612  GLU 612  612  ?   ?   ?   A . n 
A 1 613  VAL 613  613  ?   ?   ?   A . n 
A 1 614  PRO 614  614  ?   ?   ?   A . n 
A 1 615  VAL 615  615  ?   ?   ?   A . n 
A 1 616  ALA 616  616  ?   ?   ?   A . n 
A 1 617  ILE 617  617  ?   ?   ?   A . n 
A 1 618  HIS 618  618  ?   ?   ?   A . n 
A 1 619  ALA 619  619  ?   ?   ?   A . n 
A 1 620  ASP 620  620  ?   ?   ?   A . n 
A 1 621  GLN 621  621  ?   ?   ?   A . n 
A 1 622  LEU 622  622  ?   ?   ?   A . n 
A 1 623  THR 623  623  ?   ?   ?   A . n 
A 1 624  PRO 624  624  ?   ?   ?   A . n 
A 1 625  THR 625  625  ?   ?   ?   A . n 
A 1 626  TRP 626  626  ?   ?   ?   A . n 
A 1 627  ARG 627  627  ?   ?   ?   A . n 
A 1 628  VAL 628  628  ?   ?   ?   A . n 
A 1 629  TYR 629  629  ?   ?   ?   A . n 
A 1 630  SER 630  630  ?   ?   ?   A . n 
A 1 631  THR 631  631  ?   ?   ?   A . n 
A 1 632  GLY 632  632  ?   ?   ?   A . n 
A 1 633  SER 633  633  ?   ?   ?   A . n 
A 1 634  ASN 634  634  ?   ?   ?   A . n 
A 1 635  VAL 635  635  ?   ?   ?   A . n 
A 1 636  PHE 636  636  ?   ?   ?   A . n 
A 1 637  GLN 637  637  ?   ?   ?   A . n 
A 1 638  THR 638  638  ?   ?   ?   A . n 
A 1 639  ARG 639  639  ?   ?   ?   A . n 
A 1 640  ALA 640  640  ?   ?   ?   A . n 
A 1 641  GLY 641  641  ?   ?   ?   A . n 
A 1 642  CYS 642  642  ?   ?   ?   A . n 
A 1 643  LEU 643  643  ?   ?   ?   A . n 
A 1 644  ILE 644  644  ?   ?   ?   A . n 
A 1 645  GLY 645  645  ?   ?   ?   A . n 
A 1 646  ALA 646  646  ?   ?   ?   A . n 
A 1 647  GLU 647  647  ?   ?   ?   A . n 
A 1 648  HIS 648  648  ?   ?   ?   A . n 
A 1 649  VAL 649  649  ?   ?   ?   A . n 
A 1 650  ASN 650  650  ?   ?   ?   A . n 
A 1 651  ASN 651  651  ?   ?   ?   A . n 
A 1 652  SER 652  652  ?   ?   ?   A . n 
A 1 653  TYR 653  653  ?   ?   ?   A . n 
A 1 654  GLU 654  654  ?   ?   ?   A . n 
A 1 655  CYS 655  655  ?   ?   ?   A . n 
A 1 656  ASP 656  656  ?   ?   ?   A . n 
A 1 657  ILE 657  657  ?   ?   ?   A . n 
A 1 658  PRO 658  658  ?   ?   ?   A . n 
A 1 659  ILE 659  659  ?   ?   ?   A . n 
A 1 660  GLY 660  660  ?   ?   ?   A . n 
A 1 661  ALA 661  661  ?   ?   ?   A . n 
A 1 662  GLY 662  662  ?   ?   ?   A . n 
A 1 663  ILE 663  663  ?   ?   ?   A . n 
A 1 664  CYS 664  664  ?   ?   ?   A . n 
A 1 665  ALA 665  665  ?   ?   ?   A . n 
A 1 666  SER 666  666  ?   ?   ?   A . n 
A 1 667  TYR 667  667  ?   ?   ?   A . n 
A 1 668  GLN 668  668  ?   ?   ?   A . n 
A 1 669  THR 669  669  ?   ?   ?   A . n 
A 1 670  GLN 670  670  ?   ?   ?   A . n 
A 1 671  THR 671  671  ?   ?   ?   A . n 
A 1 672  ASN 672  672  ?   ?   ?   A . n 
A 1 673  SER 673  673  ?   ?   ?   A . n 
A 1 674  PRO 674  674  ?   ?   ?   A . n 
A 1 675  ARG 675  675  ?   ?   ?   A . n 
A 1 676  ARG 676  676  ?   ?   ?   A . n 
A 1 677  ALA 677  677  ?   ?   ?   A . n 
A 1 678  ARG 678  678  ?   ?   ?   A . n 
A 1 679  SER 679  679  ?   ?   ?   A . n 
A 1 680  VAL 680  680  ?   ?   ?   A . n 
A 1 681  ALA 681  681  ?   ?   ?   A . n 
A 1 682  SER 682  682  ?   ?   ?   A . n 
A 1 683  GLN 683  683  ?   ?   ?   A . n 
A 1 684  SER 684  684  ?   ?   ?   A . n 
A 1 685  ILE 685  685  ?   ?   ?   A . n 
A 1 686  ILE 686  686  ?   ?   ?   A . n 
A 1 687  ALA 687  687  ?   ?   ?   A . n 
A 1 688  TYR 688  688  ?   ?   ?   A . n 
A 1 689  THR 689  689  ?   ?   ?   A . n 
A 1 690  MET 690  690  ?   ?   ?   A . n 
A 1 691  SER 691  691  ?   ?   ?   A . n 
A 1 692  LEU 692  692  ?   ?   ?   A . n 
A 1 693  GLY 693  693  ?   ?   ?   A . n 
A 1 694  ALA 694  694  ?   ?   ?   A . n 
A 1 695  GLU 695  695  ?   ?   ?   A . n 
A 1 696  ASN 696  696  ?   ?   ?   A . n 
A 1 697  SER 697  697  ?   ?   ?   A . n 
A 1 698  VAL 698  698  ?   ?   ?   A . n 
A 1 699  ALA 699  699  ?   ?   ?   A . n 
A 1 700  TYR 700  700  ?   ?   ?   A . n 
A 1 701  SER 701  701  ?   ?   ?   A . n 
A 1 702  ASN 702  702  ?   ?   ?   A . n 
A 1 703  ASN 703  703  ?   ?   ?   A . n 
A 1 704  SER 704  704  ?   ?   ?   A . n 
A 1 705  ILE 705  705  ?   ?   ?   A . n 
A 1 706  ALA 706  706  ?   ?   ?   A . n 
A 1 707  ILE 707  707  ?   ?   ?   A . n 
A 1 708  PRO 708  708  ?   ?   ?   A . n 
A 1 709  THR 709  709  ?   ?   ?   A . n 
A 1 710  ASN 710  710  ?   ?   ?   A . n 
A 1 711  PHE 711  711  ?   ?   ?   A . n 
A 1 712  THR 712  712  ?   ?   ?   A . n 
A 1 713  ILE 713  713  ?   ?   ?   A . n 
A 1 714  SER 714  714  ?   ?   ?   A . n 
A 1 715  VAL 715  715  ?   ?   ?   A . n 
A 1 716  THR 716  716  ?   ?   ?   A . n 
A 1 717  THR 717  717  ?   ?   ?   A . n 
A 1 718  GLU 718  718  ?   ?   ?   A . n 
A 1 719  ILE 719  719  ?   ?   ?   A . n 
A 1 720  LEU 720  720  ?   ?   ?   A . n 
A 1 721  PRO 721  721  ?   ?   ?   A . n 
A 1 722  VAL 722  722  ?   ?   ?   A . n 
A 1 723  SER 723  723  ?   ?   ?   A . n 
A 1 724  MET 724  724  ?   ?   ?   A . n 
A 1 725  THR 725  725  ?   ?   ?   A . n 
A 1 726  LYS 726  726  ?   ?   ?   A . n 
A 1 727  THR 727  727  ?   ?   ?   A . n 
A 1 728  SER 728  728  ?   ?   ?   A . n 
A 1 729  VAL 729  729  ?   ?   ?   A . n 
A 1 730  ASP 730  730  ?   ?   ?   A . n 
A 1 731  CYS 731  731  ?   ?   ?   A . n 
A 1 732  THR 732  732  ?   ?   ?   A . n 
A 1 733  MET 733  733  ?   ?   ?   A . n 
A 1 734  TYR 734  734  ?   ?   ?   A . n 
A 1 735  ILE 735  735  ?   ?   ?   A . n 
A 1 736  CYS 736  736  ?   ?   ?   A . n 
A 1 737  GLY 737  737  ?   ?   ?   A . n 
A 1 738  ASP 738  738  ?   ?   ?   A . n 
A 1 739  SER 739  739  ?   ?   ?   A . n 
A 1 740  THR 740  740  ?   ?   ?   A . n 
A 1 741  GLU 741  741  ?   ?   ?   A . n 
A 1 742  CYS 742  742  ?   ?   ?   A . n 
A 1 743  SER 743  743  ?   ?   ?   A . n 
A 1 744  ASN 744  744  ?   ?   ?   A . n 
A 1 745  LEU 745  745  ?   ?   ?   A . n 
A 1 746  LEU 746  746  ?   ?   ?   A . n 
A 1 747  LEU 747  747  ?   ?   ?   A . n 
A 1 748  GLN 748  748  ?   ?   ?   A . n 
A 1 749  TYR 749  749  ?   ?   ?   A . n 
A 1 750  GLY 750  750  ?   ?   ?   A . n 
A 1 751  SER 751  751  ?   ?   ?   A . n 
A 1 752  PHE 752  752  ?   ?   ?   A . n 
A 1 753  CYS 753  753  ?   ?   ?   A . n 
A 1 754  THR 754  754  ?   ?   ?   A . n 
A 1 755  GLN 755  755  ?   ?   ?   A . n 
A 1 756  LEU 756  756  ?   ?   ?   A . n 
A 1 757  ASN 757  757  ?   ?   ?   A . n 
A 1 758  ARG 758  758  ?   ?   ?   A . n 
A 1 759  ALA 759  759  ?   ?   ?   A . n 
A 1 760  LEU 760  760  ?   ?   ?   A . n 
A 1 761  THR 761  761  ?   ?   ?   A . n 
A 1 762  GLY 762  762  ?   ?   ?   A . n 
A 1 763  ILE 763  763  ?   ?   ?   A . n 
A 1 764  ALA 764  764  ?   ?   ?   A . n 
A 1 765  VAL 765  765  ?   ?   ?   A . n 
A 1 766  GLU 766  766  ?   ?   ?   A . n 
A 1 767  GLN 767  767  ?   ?   ?   A . n 
A 1 768  ASP 768  768  ?   ?   ?   A . n 
A 1 769  LYS 769  769  ?   ?   ?   A . n 
A 1 770  ASN 770  770  ?   ?   ?   A . n 
A 1 771  THR 771  771  ?   ?   ?   A . n 
A 1 772  GLN 772  772  ?   ?   ?   A . n 
A 1 773  GLU 773  773  ?   ?   ?   A . n 
A 1 774  VAL 774  774  ?   ?   ?   A . n 
A 1 775  PHE 775  775  ?   ?   ?   A . n 
A 1 776  ALA 776  776  ?   ?   ?   A . n 
A 1 777  GLN 777  777  ?   ?   ?   A . n 
A 1 778  VAL 778  778  ?   ?   ?   A . n 
A 1 779  LYS 779  779  ?   ?   ?   A . n 
A 1 780  GLN 780  780  ?   ?   ?   A . n 
A 1 781  ILE 781  781  ?   ?   ?   A . n 
A 1 782  TYR 782  782  ?   ?   ?   A . n 
A 1 783  LYS 783  783  ?   ?   ?   A . n 
A 1 784  THR 784  784  ?   ?   ?   A . n 
A 1 785  PRO 785  785  ?   ?   ?   A . n 
A 1 786  PRO 786  786  ?   ?   ?   A . n 
A 1 787  ILE 787  787  ?   ?   ?   A . n 
A 1 788  LYS 788  788  ?   ?   ?   A . n 
A 1 789  ASP 789  789  ?   ?   ?   A . n 
A 1 790  PHE 790  790  ?   ?   ?   A . n 
A 1 791  GLY 791  791  ?   ?   ?   A . n 
A 1 792  GLY 792  792  ?   ?   ?   A . n 
A 1 793  PHE 793  793  ?   ?   ?   A . n 
A 1 794  ASN 794  794  ?   ?   ?   A . n 
A 1 795  PHE 795  795  ?   ?   ?   A . n 
A 1 796  SER 796  796  ?   ?   ?   A . n 
A 1 797  GLN 797  797  ?   ?   ?   A . n 
A 1 798  ILE 798  798  ?   ?   ?   A . n 
A 1 799  LEU 799  799  ?   ?   ?   A . n 
A 1 800  PRO 800  800  ?   ?   ?   A . n 
A 1 801  ASP 801  801  ?   ?   ?   A . n 
A 1 802  PRO 802  802  ?   ?   ?   A . n 
A 1 803  SER 803  803  ?   ?   ?   A . n 
A 1 804  LYS 804  804  ?   ?   ?   A . n 
A 1 805  PRO 805  805  ?   ?   ?   A . n 
A 1 806  SER 806  806  ?   ?   ?   A . n 
A 1 807  LYS 807  807  ?   ?   ?   A . n 
A 1 808  ARG 808  808  ?   ?   ?   A . n 
A 1 809  SER 809  809  ?   ?   ?   A . n 
A 1 810  PRO 810  810  ?   ?   ?   A . n 
A 1 811  ILE 811  811  ?   ?   ?   A . n 
A 1 812  GLU 812  812  ?   ?   ?   A . n 
A 1 813  ASP 813  813  ?   ?   ?   A . n 
A 1 814  LEU 814  814  ?   ?   ?   A . n 
A 1 815  LEU 815  815  ?   ?   ?   A . n 
A 1 816  PHE 816  816  ?   ?   ?   A . n 
A 1 817  ASN 817  817  ?   ?   ?   A . n 
A 1 818  LYS 818  818  ?   ?   ?   A . n 
A 1 819  VAL 819  819  ?   ?   ?   A . n 
A 1 820  THR 820  820  ?   ?   ?   A . n 
A 1 821  LEU 821  821  ?   ?   ?   A . n 
A 1 822  ALA 822  822  ?   ?   ?   A . n 
A 1 823  ASP 823  823  ?   ?   ?   A . n 
A 1 824  ALA 824  824  ?   ?   ?   A . n 
A 1 825  GLY 825  825  ?   ?   ?   A . n 
A 1 826  PHE 826  826  ?   ?   ?   A . n 
A 1 827  ILE 827  827  ?   ?   ?   A . n 
A 1 828  LYS 828  828  ?   ?   ?   A . n 
A 1 829  GLN 829  829  ?   ?   ?   A . n 
A 1 830  TYR 830  830  ?   ?   ?   A . n 
A 1 831  GLY 831  831  ?   ?   ?   A . n 
A 1 832  ASP 832  832  ?   ?   ?   A . n 
A 1 833  CYS 833  833  ?   ?   ?   A . n 
A 1 834  LEU 834  834  ?   ?   ?   A . n 
A 1 835  GLY 835  835  ?   ?   ?   A . n 
A 1 836  ASP 836  836  ?   ?   ?   A . n 
A 1 837  ILE 837  837  ?   ?   ?   A . n 
A 1 838  ALA 838  838  ?   ?   ?   A . n 
A 1 839  ALA 839  839  ?   ?   ?   A . n 
A 1 840  ARG 840  840  ?   ?   ?   A . n 
A 1 841  ASP 841  841  ?   ?   ?   A . n 
A 1 842  LEU 842  842  ?   ?   ?   A . n 
A 1 843  ILE 843  843  ?   ?   ?   A . n 
A 1 844  CYS 844  844  ?   ?   ?   A . n 
A 1 845  ALA 845  845  ?   ?   ?   A . n 
A 1 846  GLN 846  846  ?   ?   ?   A . n 
A 1 847  LYS 847  847  ?   ?   ?   A . n 
A 1 848  PHE 848  848  ?   ?   ?   A . n 
A 1 849  ASN 849  849  ?   ?   ?   A . n 
A 1 850  GLY 850  850  ?   ?   ?   A . n 
A 1 851  LEU 851  851  ?   ?   ?   A . n 
A 1 852  ASN 852  852  ?   ?   ?   A . n 
A 1 853  VAL 853  853  ?   ?   ?   A . n 
A 1 854  LEU 854  854  ?   ?   ?   A . n 
A 1 855  PRO 855  855  ?   ?   ?   A . n 
A 1 856  PRO 856  856  ?   ?   ?   A . n 
A 1 857  LEU 857  857  ?   ?   ?   A . n 
A 1 858  LEU 858  858  ?   ?   ?   A . n 
A 1 859  THR 859  859  ?   ?   ?   A . n 
A 1 860  ASP 860  860  ?   ?   ?   A . n 
A 1 861  GLU 861  861  ?   ?   ?   A . n 
A 1 862  MET 862  862  ?   ?   ?   A . n 
A 1 863  ILE 863  863  ?   ?   ?   A . n 
A 1 864  ALA 864  864  ?   ?   ?   A . n 
A 1 865  GLN 865  865  ?   ?   ?   A . n 
A 1 866  TYR 866  866  ?   ?   ?   A . n 
A 1 867  THR 867  867  ?   ?   ?   A . n 
A 1 868  SER 868  868  ?   ?   ?   A . n 
A 1 869  ALA 869  869  ?   ?   ?   A . n 
A 1 870  LEU 870  870  ?   ?   ?   A . n 
A 1 871  LEU 871  871  ?   ?   ?   A . n 
A 1 872  ALA 872  872  ?   ?   ?   A . n 
A 1 873  GLY 873  873  ?   ?   ?   A . n 
A 1 874  THR 874  874  ?   ?   ?   A . n 
A 1 875  ILE 875  875  ?   ?   ?   A . n 
A 1 876  THR 876  876  ?   ?   ?   A . n 
A 1 877  SER 877  877  ?   ?   ?   A . n 
A 1 878  GLY 878  878  ?   ?   ?   A . n 
A 1 879  TRP 879  879  ?   ?   ?   A . n 
A 1 880  THR 880  880  ?   ?   ?   A . n 
A 1 881  PHE 881  881  ?   ?   ?   A . n 
A 1 882  GLY 882  882  ?   ?   ?   A . n 
A 1 883  ALA 883  883  ?   ?   ?   A . n 
A 1 884  GLY 884  884  ?   ?   ?   A . n 
A 1 885  PRO 885  885  ?   ?   ?   A . n 
A 1 886  ALA 886  886  ?   ?   ?   A . n 
A 1 887  LEU 887  887  ?   ?   ?   A . n 
A 1 888  GLN 888  888  ?   ?   ?   A . n 
A 1 889  ILE 889  889  ?   ?   ?   A . n 
A 1 890  PRO 890  890  ?   ?   ?   A . n 
A 1 891  PHE 891  891  ?   ?   ?   A . n 
A 1 892  PRO 892  892  ?   ?   ?   A . n 
A 1 893  MET 893  893  ?   ?   ?   A . n 
A 1 894  GLN 894  894  ?   ?   ?   A . n 
A 1 895  MET 895  895  ?   ?   ?   A . n 
A 1 896  ALA 896  896  ?   ?   ?   A . n 
A 1 897  TYR 897  897  ?   ?   ?   A . n 
A 1 898  ARG 898  898  ?   ?   ?   A . n 
A 1 899  PHE 899  899  ?   ?   ?   A . n 
A 1 900  ASN 900  900  ?   ?   ?   A . n 
A 1 901  GLY 901  901  ?   ?   ?   A . n 
A 1 902  ILE 902  902  ?   ?   ?   A . n 
A 1 903  GLY 903  903  ?   ?   ?   A . n 
A 1 904  VAL 904  904  ?   ?   ?   A . n 
A 1 905  THR 905  905  ?   ?   ?   A . n 
A 1 906  GLN 906  906  ?   ?   ?   A . n 
A 1 907  ASN 907  907  ?   ?   ?   A . n 
A 1 908  VAL 908  908  ?   ?   ?   A . n 
A 1 909  LEU 909  909  ?   ?   ?   A . n 
A 1 910  TYR 910  910  ?   ?   ?   A . n 
A 1 911  GLU 911  911  ?   ?   ?   A . n 
A 1 912  ASN 912  912  ?   ?   ?   A . n 
A 1 913  GLN 913  913  ?   ?   ?   A . n 
A 1 914  LYS 914  914  ?   ?   ?   A . n 
A 1 915  LEU 915  915  ?   ?   ?   A . n 
A 1 916  ILE 916  916  ?   ?   ?   A . n 
A 1 917  ALA 917  917  ?   ?   ?   A . n 
A 1 918  ASN 918  918  ?   ?   ?   A . n 
A 1 919  GLN 919  919  ?   ?   ?   A . n 
A 1 920  PHE 920  920  ?   ?   ?   A . n 
A 1 921  ASN 921  921  ?   ?   ?   A . n 
A 1 922  SER 922  922  ?   ?   ?   A . n 
A 1 923  ALA 923  923  ?   ?   ?   A . n 
A 1 924  ILE 924  924  ?   ?   ?   A . n 
A 1 925  GLY 925  925  ?   ?   ?   A . n 
A 1 926  LYS 926  926  ?   ?   ?   A . n 
A 1 927  ILE 927  927  ?   ?   ?   A . n 
A 1 928  GLN 928  928  ?   ?   ?   A . n 
A 1 929  ASP 929  929  ?   ?   ?   A . n 
A 1 930  SER 930  930  ?   ?   ?   A . n 
A 1 931  LEU 931  931  ?   ?   ?   A . n 
A 1 932  SER 932  932  ?   ?   ?   A . n 
A 1 933  SER 933  933  ?   ?   ?   A . n 
A 1 934  THR 934  934  ?   ?   ?   A . n 
A 1 935  PRO 935  935  ?   ?   ?   A . n 
A 1 936  SER 936  936  ?   ?   ?   A . n 
A 1 937  ALA 937  937  ?   ?   ?   A . n 
A 1 938  LEU 938  938  ?   ?   ?   A . n 
A 1 939  GLY 939  939  ?   ?   ?   A . n 
A 1 940  LYS 940  940  ?   ?   ?   A . n 
A 1 941  LEU 941  941  ?   ?   ?   A . n 
A 1 942  GLN 942  942  ?   ?   ?   A . n 
A 1 943  ASP 943  943  ?   ?   ?   A . n 
A 1 944  VAL 944  944  ?   ?   ?   A . n 
A 1 945  VAL 945  945  ?   ?   ?   A . n 
A 1 946  ASN 946  946  ?   ?   ?   A . n 
A 1 947  GLN 947  947  ?   ?   ?   A . n 
A 1 948  ASN 948  948  ?   ?   ?   A . n 
A 1 949  ALA 949  949  ?   ?   ?   A . n 
A 1 950  GLN 950  950  ?   ?   ?   A . n 
A 1 951  ALA 951  951  ?   ?   ?   A . n 
A 1 952  LEU 952  952  ?   ?   ?   A . n 
A 1 953  ASN 953  953  ?   ?   ?   A . n 
A 1 954  THR 954  954  ?   ?   ?   A . n 
A 1 955  LEU 955  955  ?   ?   ?   A . n 
A 1 956  VAL 956  956  ?   ?   ?   A . n 
A 1 957  LYS 957  957  ?   ?   ?   A . n 
A 1 958  GLN 958  958  ?   ?   ?   A . n 
A 1 959  LEU 959  959  ?   ?   ?   A . n 
A 1 960  SER 960  960  ?   ?   ?   A . n 
A 1 961  SER 961  961  ?   ?   ?   A . n 
A 1 962  ASN 962  962  ?   ?   ?   A . n 
A 1 963  PHE 963  963  ?   ?   ?   A . n 
A 1 964  GLY 964  964  ?   ?   ?   A . n 
A 1 965  ALA 965  965  ?   ?   ?   A . n 
A 1 966  ILE 966  966  ?   ?   ?   A . n 
A 1 967  SER 967  967  ?   ?   ?   A . n 
A 1 968  SER 968  968  ?   ?   ?   A . n 
A 1 969  VAL 969  969  ?   ?   ?   A . n 
A 1 970  LEU 970  970  ?   ?   ?   A . n 
A 1 971  ASN 971  971  ?   ?   ?   A . n 
A 1 972  ASP 972  972  ?   ?   ?   A . n 
A 1 973  ILE 973  973  ?   ?   ?   A . n 
A 1 974  LEU 974  974  ?   ?   ?   A . n 
A 1 975  SER 975  975  ?   ?   ?   A . n 
A 1 976  ARG 976  976  ?   ?   ?   A . n 
A 1 977  LEU 977  977  ?   ?   ?   A . n 
A 1 978  CYS 978  978  ?   ?   ?   A . n 
A 1 979  PRO 979  979  ?   ?   ?   A . n 
A 1 980  PRO 980  980  ?   ?   ?   A . n 
A 1 981  GLU 981  981  ?   ?   ?   A . n 
A 1 982  ALA 982  982  ?   ?   ?   A . n 
A 1 983  GLU 983  983  ?   ?   ?   A . n 
A 1 984  VAL 984  984  ?   ?   ?   A . n 
A 1 985  GLN 985  985  ?   ?   ?   A . n 
A 1 986  ILE 986  986  ?   ?   ?   A . n 
A 1 987  ASP 987  987  ?   ?   ?   A . n 
A 1 988  ARG 988  988  ?   ?   ?   A . n 
A 1 989  LEU 989  989  ?   ?   ?   A . n 
A 1 990  ILE 990  990  ?   ?   ?   A . n 
A 1 991  THR 991  991  ?   ?   ?   A . n 
A 1 992  GLY 992  992  ?   ?   ?   A . n 
A 1 993  ARG 993  993  ?   ?   ?   A . n 
A 1 994  LEU 994  994  ?   ?   ?   A . n 
A 1 995  GLN 995  995  ?   ?   ?   A . n 
A 1 996  SER 996  996  ?   ?   ?   A . n 
A 1 997  LEU 997  997  ?   ?   ?   A . n 
A 1 998  GLN 998  998  ?   ?   ?   A . n 
A 1 999  THR 999  999  ?   ?   ?   A . n 
A 1 1000 TYR 1000 1000 ?   ?   ?   A . n 
A 1 1001 VAL 1001 1001 ?   ?   ?   A . n 
A 1 1002 THR 1002 1002 ?   ?   ?   A . n 
A 1 1003 GLN 1003 1003 ?   ?   ?   A . n 
A 1 1004 GLN 1004 1004 ?   ?   ?   A . n 
A 1 1005 LEU 1005 1005 ?   ?   ?   A . n 
A 1 1006 ILE 1006 1006 ?   ?   ?   A . n 
A 1 1007 ARG 1007 1007 ?   ?   ?   A . n 
A 1 1008 ALA 1008 1008 ?   ?   ?   A . n 
A 1 1009 ALA 1009 1009 ?   ?   ?   A . n 
A 1 1010 GLU 1010 1010 ?   ?   ?   A . n 
A 1 1011 ILE 1011 1011 ?   ?   ?   A . n 
A 1 1012 ARG 1012 1012 ?   ?   ?   A . n 
A 1 1013 ALA 1013 1013 ?   ?   ?   A . n 
A 1 1014 SER 1014 1014 ?   ?   ?   A . n 
A 1 1015 ALA 1015 1015 ?   ?   ?   A . n 
A 1 1016 ASN 1016 1016 ?   ?   ?   A . n 
A 1 1017 LEU 1017 1017 ?   ?   ?   A . n 
A 1 1018 ALA 1018 1018 ?   ?   ?   A . n 
A 1 1019 ALA 1019 1019 ?   ?   ?   A . n 
A 1 1020 THR 1020 1020 ?   ?   ?   A . n 
A 1 1021 LYS 1021 1021 ?   ?   ?   A . n 
A 1 1022 MET 1022 1022 ?   ?   ?   A . n 
A 1 1023 SER 1023 1023 ?   ?   ?   A . n 
A 1 1024 GLU 1024 1024 ?   ?   ?   A . n 
A 1 1025 CYS 1025 1025 ?   ?   ?   A . n 
A 1 1026 VAL 1026 1026 ?   ?   ?   A . n 
A 1 1027 LEU 1027 1027 ?   ?   ?   A . n 
A 1 1028 GLY 1028 1028 ?   ?   ?   A . n 
A 1 1029 GLN 1029 1029 ?   ?   ?   A . n 
A 1 1030 SER 1030 1030 ?   ?   ?   A . n 
A 1 1031 LYS 1031 1031 ?   ?   ?   A . n 
A 1 1032 ARG 1032 1032 ?   ?   ?   A . n 
A 1 1033 VAL 1033 1033 ?   ?   ?   A . n 
A 1 1034 ASP 1034 1034 ?   ?   ?   A . n 
A 1 1035 PHE 1035 1035 ?   ?   ?   A . n 
A 1 1036 CYS 1036 1036 ?   ?   ?   A . n 
A 1 1037 GLY 1037 1037 ?   ?   ?   A . n 
A 1 1038 LYS 1038 1038 ?   ?   ?   A . n 
A 1 1039 GLY 1039 1039 ?   ?   ?   A . n 
A 1 1040 TYR 1040 1040 ?   ?   ?   A . n 
A 1 1041 HIS 1041 1041 ?   ?   ?   A . n 
A 1 1042 LEU 1042 1042 ?   ?   ?   A . n 
A 1 1043 MET 1043 1043 ?   ?   ?   A . n 
A 1 1044 SER 1044 1044 ?   ?   ?   A . n 
A 1 1045 PHE 1045 1045 ?   ?   ?   A . n 
A 1 1046 PRO 1046 1046 ?   ?   ?   A . n 
A 1 1047 GLN 1047 1047 ?   ?   ?   A . n 
A 1 1048 SER 1048 1048 ?   ?   ?   A . n 
A 1 1049 ALA 1049 1049 ?   ?   ?   A . n 
A 1 1050 PRO 1050 1050 ?   ?   ?   A . n 
A 1 1051 HIS 1051 1051 ?   ?   ?   A . n 
A 1 1052 GLY 1052 1052 ?   ?   ?   A . n 
A 1 1053 VAL 1053 1053 ?   ?   ?   A . n 
A 1 1054 VAL 1054 1054 ?   ?   ?   A . n 
A 1 1055 PHE 1055 1055 ?   ?   ?   A . n 
A 1 1056 LEU 1056 1056 ?   ?   ?   A . n 
A 1 1057 HIS 1057 1057 ?   ?   ?   A . n 
A 1 1058 VAL 1058 1058 ?   ?   ?   A . n 
A 1 1059 THR 1059 1059 ?   ?   ?   A . n 
A 1 1060 TYR 1060 1060 ?   ?   ?   A . n 
A 1 1061 VAL 1061 1061 ?   ?   ?   A . n 
A 1 1062 PRO 1062 1062 ?   ?   ?   A . n 
A 1 1063 ALA 1063 1063 ?   ?   ?   A . n 
A 1 1064 GLN 1064 1064 ?   ?   ?   A . n 
A 1 1065 GLU 1065 1065 ?   ?   ?   A . n 
A 1 1066 LYS 1066 1066 ?   ?   ?   A . n 
A 1 1067 ASN 1067 1067 ?   ?   ?   A . n 
A 1 1068 PHE 1068 1068 ?   ?   ?   A . n 
A 1 1069 THR 1069 1069 ?   ?   ?   A . n 
A 1 1070 THR 1070 1070 ?   ?   ?   A . n 
A 1 1071 ALA 1071 1071 ?   ?   ?   A . n 
A 1 1072 PRO 1072 1072 ?   ?   ?   A . n 
A 1 1073 ALA 1073 1073 ?   ?   ?   A . n 
A 1 1074 ILE 1074 1074 ?   ?   ?   A . n 
A 1 1075 CYS 1075 1075 ?   ?   ?   A . n 
A 1 1076 HIS 1076 1076 ?   ?   ?   A . n 
A 1 1077 ASP 1077 1077 ?   ?   ?   A . n 
A 1 1078 GLY 1078 1078 ?   ?   ?   A . n 
A 1 1079 LYS 1079 1079 ?   ?   ?   A . n 
A 1 1080 ALA 1080 1080 ?   ?   ?   A . n 
A 1 1081 HIS 1081 1081 ?   ?   ?   A . n 
A 1 1082 PHE 1082 1082 ?   ?   ?   A . n 
A 1 1083 PRO 1083 1083 ?   ?   ?   A . n 
A 1 1084 ARG 1084 1084 ?   ?   ?   A . n 
A 1 1085 GLU 1085 1085 ?   ?   ?   A . n 
A 1 1086 GLY 1086 1086 ?   ?   ?   A . n 
A 1 1087 VAL 1087 1087 ?   ?   ?   A . n 
A 1 1088 PHE 1088 1088 ?   ?   ?   A . n 
A 1 1089 VAL 1089 1089 ?   ?   ?   A . n 
A 1 1090 SER 1090 1090 ?   ?   ?   A . n 
A 1 1091 ASN 1091 1091 ?   ?   ?   A . n 
A 1 1092 GLY 1092 1092 ?   ?   ?   A . n 
A 1 1093 THR 1093 1093 ?   ?   ?   A . n 
A 1 1094 HIS 1094 1094 ?   ?   ?   A . n 
A 1 1095 TRP 1095 1095 ?   ?   ?   A . n 
A 1 1096 PHE 1096 1096 ?   ?   ?   A . n 
A 1 1097 VAL 1097 1097 ?   ?   ?   A . n 
A 1 1098 THR 1098 1098 ?   ?   ?   A . n 
A 1 1099 GLN 1099 1099 ?   ?   ?   A . n 
A 1 1100 ARG 1100 1100 ?   ?   ?   A . n 
A 1 1101 ASN 1101 1101 ?   ?   ?   A . n 
A 1 1102 PHE 1102 1102 ?   ?   ?   A . n 
A 1 1103 TYR 1103 1103 ?   ?   ?   A . n 
A 1 1104 GLU 1104 1104 ?   ?   ?   A . n 
A 1 1105 PRO 1105 1105 ?   ?   ?   A . n 
A 1 1106 GLN 1106 1106 ?   ?   ?   A . n 
A 1 1107 ILE 1107 1107 ?   ?   ?   A . n 
A 1 1108 ILE 1108 1108 ?   ?   ?   A . n 
A 1 1109 THR 1109 1109 ?   ?   ?   A . n 
A 1 1110 THR 1110 1110 ?   ?   ?   A . n 
A 1 1111 ASP 1111 1111 ?   ?   ?   A . n 
A 1 1112 ASN 1112 1112 ?   ?   ?   A . n 
A 1 1113 THR 1113 1113 ?   ?   ?   A . n 
A 1 1114 PHE 1114 1114 ?   ?   ?   A . n 
A 1 1115 VAL 1115 1115 ?   ?   ?   A . n 
A 1 1116 SER 1116 1116 ?   ?   ?   A . n 
A 1 1117 GLY 1117 1117 ?   ?   ?   A . n 
A 1 1118 ASN 1118 1118 ?   ?   ?   A . n 
A 1 1119 CYS 1119 1119 ?   ?   ?   A . n 
A 1 1120 ASP 1120 1120 ?   ?   ?   A . n 
A 1 1121 VAL 1121 1121 ?   ?   ?   A . n 
A 1 1122 VAL 1122 1122 ?   ?   ?   A . n 
A 1 1123 ILE 1123 1123 ?   ?   ?   A . n 
A 1 1124 GLY 1124 1124 ?   ?   ?   A . n 
A 1 1125 ILE 1125 1125 ?   ?   ?   A . n 
A 1 1126 VAL 1126 1126 ?   ?   ?   A . n 
A 1 1127 ASN 1127 1127 ?   ?   ?   A . n 
A 1 1128 ASN 1128 1128 ?   ?   ?   A . n 
A 1 1129 THR 1129 1129 ?   ?   ?   A . n 
A 1 1130 VAL 1130 1130 ?   ?   ?   A . n 
A 1 1131 TYR 1131 1131 ?   ?   ?   A . n 
A 1 1132 ASP 1132 1132 ?   ?   ?   A . n 
A 1 1133 PRO 1133 1133 ?   ?   ?   A . n 
A 1 1134 LEU 1134 1134 ?   ?   ?   A . n 
A 1 1135 GLN 1135 1135 ?   ?   ?   A . n 
A 1 1136 PRO 1136 1136 ?   ?   ?   A . n 
A 1 1137 GLU 1137 1137 ?   ?   ?   A . n 
A 1 1138 LEU 1138 1138 ?   ?   ?   A . n 
A 1 1139 ASP 1139 1139 ?   ?   ?   A . n 
A 1 1140 SER 1140 1140 ?   ?   ?   A . n 
A 1 1141 PHE 1141 1141 ?   ?   ?   A . n 
A 1 1142 LYS 1142 1142 ?   ?   ?   A . n 
A 1 1143 GLU 1143 1143 ?   ?   ?   A . n 
A 1 1144 GLU 1144 1144 ?   ?   ?   A . n 
A 1 1145 LEU 1145 1145 ?   ?   ?   A . n 
A 1 1146 ASP 1146 1146 ?   ?   ?   A . n 
A 1 1147 LYS 1147 1147 ?   ?   ?   A . n 
A 1 1148 TYR 1148 1148 ?   ?   ?   A . n 
A 1 1149 PHE 1149 1149 ?   ?   ?   A . n 
A 1 1150 LYS 1150 1150 ?   ?   ?   A . n 
A 1 1151 ASN 1151 1151 ?   ?   ?   A . n 
A 1 1152 HIS 1152 1152 ?   ?   ?   A . n 
A 1 1153 THR 1153 1153 ?   ?   ?   A . n 
A 1 1154 SER 1154 1154 ?   ?   ?   A . n 
A 1 1155 PRO 1155 1155 ?   ?   ?   A . n 
A 1 1156 ASP 1156 1156 ?   ?   ?   A . n 
A 1 1157 VAL 1157 1157 ?   ?   ?   A . n 
A 1 1158 ASP 1158 1158 ?   ?   ?   A . n 
A 1 1159 LEU 1159 1159 ?   ?   ?   A . n 
A 1 1160 GLY 1160 1160 ?   ?   ?   A . n 
A 1 1161 ASP 1161 1161 ?   ?   ?   A . n 
A 1 1162 ILE 1162 1162 ?   ?   ?   A . n 
A 1 1163 SER 1163 1163 ?   ?   ?   A . n 
A 1 1164 GLY 1164 1164 ?   ?   ?   A . n 
A 1 1165 ILE 1165 1165 ?   ?   ?   A . n 
A 1 1166 ASN 1166 1166 ?   ?   ?   A . n 
A 1 1167 ALA 1167 1167 ?   ?   ?   A . n 
A 1 1168 SER 1168 1168 ?   ?   ?   A . n 
A 1 1169 VAL 1169 1169 ?   ?   ?   A . n 
A 1 1170 VAL 1170 1170 ?   ?   ?   A . n 
A 1 1171 ASN 1171 1171 ?   ?   ?   A . n 
A 1 1172 ILE 1172 1172 ?   ?   ?   A . n 
A 1 1173 GLN 1173 1173 ?   ?   ?   A . n 
A 1 1174 LYS 1174 1174 ?   ?   ?   A . n 
A 1 1175 GLU 1175 1175 ?   ?   ?   A . n 
A 1 1176 ILE 1176 1176 ?   ?   ?   A . n 
A 1 1177 ASP 1177 1177 ?   ?   ?   A . n 
A 1 1178 ARG 1178 1178 ?   ?   ?   A . n 
A 1 1179 LEU 1179 1179 ?   ?   ?   A . n 
A 1 1180 ASN 1180 1180 ?   ?   ?   A . n 
A 1 1181 GLU 1181 1181 ?   ?   ?   A . n 
A 1 1182 VAL 1182 1182 ?   ?   ?   A . n 
A 1 1183 ALA 1183 1183 ?   ?   ?   A . n 
A 1 1184 LYS 1184 1184 ?   ?   ?   A . n 
A 1 1185 ASN 1185 1185 ?   ?   ?   A . n 
A 1 1186 LEU 1186 1186 ?   ?   ?   A . n 
A 1 1187 ASN 1187 1187 ?   ?   ?   A . n 
A 1 1188 GLU 1188 1188 ?   ?   ?   A . n 
A 1 1189 SER 1189 1189 ?   ?   ?   A . n 
A 1 1190 LEU 1190 1190 ?   ?   ?   A . n 
A 1 1191 ILE 1191 1191 ?   ?   ?   A . n 
A 1 1192 ASP 1192 1192 ?   ?   ?   A . n 
A 1 1193 LEU 1193 1193 ?   ?   ?   A . n 
A 1 1194 GLN 1194 1194 ?   ?   ?   A . n 
A 1 1195 GLU 1195 1195 ?   ?   ?   A . n 
A 1 1196 LEU 1196 1196 ?   ?   ?   A . n 
A 1 1197 GLY 1197 1197 ?   ?   ?   A . n 
A 1 1198 LYS 1198 1198 ?   ?   ?   A . n 
A 1 1199 TYR 1199 1199 ?   ?   ?   A . n 
A 1 1200 GLU 1200 1200 ?   ?   ?   A . n 
A 1 1201 GLN 1201 1201 ?   ?   ?   A . n 
A 1 1202 GLY 1202 1202 ?   ?   ?   A . n 
A 1 1203 SER 1203 1203 ?   ?   ?   A . n 
A 1 1204 GLY 1204 1204 ?   ?   ?   A . n 
A 1 1205 TYR 1205 1205 ?   ?   ?   A . n 
A 1 1206 ILE 1206 1206 ?   ?   ?   A . n 
A 1 1207 PRO 1207 1207 ?   ?   ?   A . n 
A 1 1208 GLU 1208 1208 ?   ?   ?   A . n 
A 1 1209 ALA 1209 1209 ?   ?   ?   A . n 
A 1 1210 PRO 1210 1210 ?   ?   ?   A . n 
A 1 1211 ARG 1211 1211 ?   ?   ?   A . n 
A 1 1212 ASP 1212 1212 ?   ?   ?   A . n 
A 1 1213 GLY 1213 1213 ?   ?   ?   A . n 
A 1 1214 GLN 1214 1214 ?   ?   ?   A . n 
A 1 1215 ALA 1215 1215 ?   ?   ?   A . n 
A 1 1216 TYR 1216 1216 ?   ?   ?   A . n 
A 1 1217 VAL 1217 1217 ?   ?   ?   A . n 
A 1 1218 ARG 1218 1218 ?   ?   ?   A . n 
A 1 1219 LYS 1219 1219 ?   ?   ?   A . n 
A 1 1220 ASP 1220 1220 ?   ?   ?   A . n 
A 1 1221 GLY 1221 1221 ?   ?   ?   A . n 
A 1 1222 GLU 1222 1222 ?   ?   ?   A . n 
A 1 1223 TRP 1223 1223 ?   ?   ?   A . n 
A 1 1224 VAL 1224 1224 ?   ?   ?   A . n 
A 1 1225 LEU 1225 1225 ?   ?   ?   A . n 
A 1 1226 LEU 1226 1226 ?   ?   ?   A . n 
A 1 1227 SER 1227 1227 ?   ?   ?   A . n 
A 1 1228 THR 1228 1228 ?   ?   ?   A . n 
A 1 1229 PHE 1229 1229 ?   ?   ?   A . n 
A 1 1230 LEU 1230 1230 ?   ?   ?   A . n 
A 1 1231 GLY 1231 1231 ?   ?   ?   A . n 
A 1 1232 ARG 1232 1232 ?   ?   ?   A . n 
A 1 1233 SER 1233 1233 ?   ?   ?   A . n 
A 1 1234 LEU 1234 1234 ?   ?   ?   A . n 
A 1 1235 GLU 1235 1235 ?   ?   ?   A . n 
A 1 1236 VAL 1236 1236 ?   ?   ?   A . n 
A 1 1237 LEU 1237 1237 ?   ?   ?   A . n 
A 1 1238 PHE 1238 1238 ?   ?   ?   A . n 
A 1 1239 GLN 1239 1239 ?   ?   ?   A . n 
A 1 1240 GLY 1240 1240 ?   ?   ?   A . n 
A 1 1241 PRO 1241 1241 ?   ?   ?   A . n 
A 1 1242 GLY 1242 1242 ?   ?   ?   A . n 
A 1 1243 SER 1243 1243 ?   ?   ?   A . n 
A 1 1244 GLY 1244 1244 ?   ?   ?   A . n 
A 1 1245 GLY 1245 1245 ?   ?   ?   A . n 
A 1 1246 LEU 1246 1246 ?   ?   ?   A . n 
A 1 1247 ASN 1247 1247 ?   ?   ?   A . n 
A 1 1248 ASP 1248 1248 ?   ?   ?   A . n 
A 1 1249 ILE 1249 1249 ?   ?   ?   A . n 
A 1 1250 PHE 1250 1250 ?   ?   ?   A . n 
A 1 1251 GLU 1251 1251 ?   ?   ?   A . n 
A 1 1252 ALA 1252 1252 ?   ?   ?   A . n 
A 1 1253 GLN 1253 1253 ?   ?   ?   A . n 
A 1 1254 LYS 1254 1254 ?   ?   ?   A . n 
A 1 1255 ILE 1255 1255 ?   ?   ?   A . n 
A 1 1256 GLU 1256 1256 ?   ?   ?   A . n 
A 1 1257 TRP 1257 1257 ?   ?   ?   A . n 
A 1 1258 HIS 1258 1258 ?   ?   ?   A . n 
A 1 1259 GLU 1259 1259 ?   ?   ?   A . n 
A 1 1260 GLY 1260 1260 ?   ?   ?   A . n 
A 1 1261 SER 1261 1261 ?   ?   ?   A . n 
A 1 1262 GLY 1262 1262 ?   ?   ?   A . n 
A 1 1263 HIS 1263 1263 ?   ?   ?   A . n 
A 1 1264 HIS 1264 1264 ?   ?   ?   A . n 
A 1 1265 HIS 1265 1265 ?   ?   ?   A . n 
A 1 1266 HIS 1266 1266 ?   ?   ?   A . n 
A 1 1267 HIS 1267 1267 ?   ?   ?   A . n 
A 1 1268 HIS 1268 1268 ?   ?   ?   A . n 
A 1 1269 HIS 1269 1269 ?   ?   ?   A . n 
A 1 1270 HIS 1270 1270 ?   ?   ?   A . n 
B 2 1    GLU 1    1    1   GLU GLU B . n 
B 2 2    VAL 2    2    2   VAL VAL B . n 
B 2 3    GLN 3    3    3   GLN GLN B . n 
B 2 4    LEU 4    4    4   LEU LEU B . n 
B 2 5    VAL 5    5    5   VAL VAL B . n 
B 2 6    GLU 6    6    6   GLU GLU B . n 
B 2 7    SER 7    7    7   SER SER B . n 
B 2 8    GLY 8    8    8   GLY GLY B . n 
B 2 9    GLY 9    9    9   GLY GLY B . n 
B 2 10   GLY 10   10   10  GLY GLY B . n 
B 2 11   VAL 11   11   11  VAL VAL B . n 
B 2 12   VAL 12   12   12  VAL VAL B . n 
B 2 13   GLN 13   13   13  GLN GLN B . n 
B 2 14   PRO 14   14   14  PRO PRO B . n 
B 2 15   GLY 15   15   15  GLY GLY B . n 
B 2 16   GLY 16   16   16  GLY GLY B . n 
B 2 17   SER 17   17   17  SER SER B . n 
B 2 18   LEU 18   18   18  LEU LEU B . n 
B 2 19   ARG 19   19   19  ARG ARG B . n 
B 2 20   LEU 20   20   20  LEU LEU B . n 
B 2 21   SER 21   21   21  SER SER B . n 
B 2 22   CYS 22   22   22  CYS CYS B . n 
B 2 23   ALA 23   23   23  ALA ALA B . n 
B 2 24   ALA 24   24   24  ALA ALA B . n 
B 2 25   SER 25   25   25  SER SER B . n 
B 2 26   GLY 26   26   26  GLY GLY B . n 
B 2 27   PHE 27   27   27  PHE PHE B . n 
B 2 28   THR 28   28   28  THR THR B . n 
B 2 29   PHE 29   29   29  PHE PHE B . n 
B 2 30   ASN 30   30   30  ASN ASN B . n 
B 2 31   SER 31   31   31  SER SER B . n 
B 2 32   TYR 32   32   32  TYR TYR B . n 
B 2 33   GLY 33   33   33  GLY GLY B . n 
B 2 34   MET 34   34   34  MET MET B . n 
B 2 35   HIS 35   35   35  HIS HIS B . n 
B 2 36   TRP 36   36   36  TRP TRP B . n 
B 2 37   VAL 37   37   37  VAL VAL B . n 
B 2 38   ARG 38   38   38  ARG ARG B . n 
B 2 39   GLN 39   39   39  GLN GLN B . n 
B 2 40   ALA 40   40   40  ALA ALA B . n 
B 2 41   PRO 41   41   41  PRO PRO B . n 
B 2 42   GLY 42   42   42  GLY GLY B . n 
B 2 43   LYS 43   43   43  LYS LYS B . n 
B 2 44   GLY 44   44   44  GLY GLY B . n 
B 2 45   LEU 45   45   45  LEU LEU B . n 
B 2 46   GLU 46   46   46  GLU GLU B . n 
B 2 47   TRP 47   47   47  TRP TRP B . n 
B 2 48   VAL 48   48   48  VAL VAL B . n 
B 2 49   ALA 49   49   49  ALA ALA B . n 
B 2 50   PHE 50   50   50  PHE PHE B . n 
B 2 51   ILE 51   51   51  ILE ILE B . n 
B 2 52   ARG 52   52   52  ARG ARG B . n 
B 2 53   TYR 53   53   53  TYR TYR B . n 
B 2 54   ASP 54   54   54  ASP ASP B . n 
B 2 55   GLY 55   55   55  GLY GLY B . n 
B 2 56   GLY 56   56   56  GLY GLY B . n 
B 2 57   ASN 57   57   57  ASN ASN B . n 
B 2 58   LYS 58   58   58  LYS LYS B . n 
B 2 59   TYR 59   59   59  TYR TYR B . n 
B 2 60   TYR 60   60   60  TYR TYR B . n 
B 2 61   ALA 61   61   61  ALA ALA B . n 
B 2 62   ASP 62   62   62  ASP ASP B . n 
B 2 63   SER 63   63   63  SER SER B . n 
B 2 64   VAL 64   64   64  VAL VAL B . n 
B 2 65   LYS 65   65   65  LYS LYS B . n 
B 2 66   GLY 66   66   66  GLY GLY B . n 
B 2 67   ARG 67   67   67  ARG ARG B . n 
B 2 68   PHE 68   68   68  PHE PHE B . n 
B 2 69   THR 69   69   69  THR THR B . n 
B 2 70   ILE 70   70   70  ILE ILE B . n 
B 2 71   SER 71   71   71  SER SER B . n 
B 2 72   ARG 72   72   72  ARG ARG B . n 
B 2 73   ASP 73   73   73  ASP ASP B . n 
B 2 74   ASN 74   74   74  ASN ASN B . n 
B 2 75   SER 75   75   75  SER SER B . n 
B 2 76   LYS 76   76   76  LYS LYS B . n 
B 2 77   ASN 77   77   77  ASN ASN B . n 
B 2 78   THR 78   78   78  THR THR B . n 
B 2 79   LEU 79   79   79  LEU LEU B . n 
B 2 80   TYR 80   80   80  TYR TYR B . n 
B 2 81   LEU 81   81   81  LEU LEU B . n 
B 2 82   GLN 82   82   82  GLN GLN B . n 
B 2 83   MET 83   83   83  MET MET B . n 
B 2 84   LYS 84   84   84  LYS LYS B . n 
B 2 85   SER 85   85   85  SER SER B . n 
B 2 86   LEU 86   86   86  LEU LEU B . n 
B 2 87   ARG 87   87   87  ARG ARG B . n 
B 2 88   ALA 88   88   88  ALA ALA B . n 
B 2 89   GLU 89   89   89  GLU GLU B . n 
B 2 90   ASP 90   90   90  ASP ASP B . n 
B 2 91   THR 91   91   91  THR THR B . n 
B 2 92   ALA 92   92   92  ALA ALA B . n 
B 2 93   VAL 93   93   93  VAL VAL B . n 
B 2 94   TYR 94   94   94  TYR TYR B . n 
B 2 95   TYR 95   95   95  TYR TYR B . n 
B 2 96   CYS 96   96   96  CYS CYS B . n 
B 2 97   ALA 97   97   97  ALA ALA B . n 
B 2 98   ASN 98   98   98  ASN ASN B . n 
B 2 99   LEU 99   99   99  LEU LEU B . n 
B 2 100  LYS 100  100  100 LYS LYS B . n 
B 2 101  ASP 101  101  101 ASP ASP B . n 
B 2 102  SER 102  102  102 SER SER B . n 
B 2 103  ARG 103  103  103 ARG ARG B . n 
B 2 104  TYR 104  104  104 TYR TYR B . n 
B 2 105  SER 105  105  105 SER SER B . n 
B 2 106  GLY 106  106  106 GLY GLY B . n 
B 2 107  SER 107  107  107 SER SER B . n 
B 2 108  TYR 108  108  108 TYR TYR B . n 
B 2 109  TYR 109  109  109 TYR TYR B . n 
B 2 110  ASP 110  110  110 ASP ASP B . n 
B 2 111  TYR 111  111  111 TYR TYR B . n 
B 2 112  TRP 112  112  112 TRP TRP B . n 
B 2 113  GLY 113  113  113 GLY GLY B . n 
B 2 114  GLN 114  114  114 GLN GLN B . n 
B 2 115  GLY 115  115  115 GLY GLY B . n 
B 2 116  THR 116  116  116 THR THR B . n 
B 2 117  LEU 117  117  117 LEU LEU B . n 
B 2 118  VAL 118  118  118 VAL VAL B . n 
B 2 119  THR 119  119  119 THR THR B . n 
B 2 120  VAL 120  120  120 VAL VAL B . n 
B 2 121  SER 121  121  121 SER SER B . n 
B 2 122  SER 122  122  ?   ?   ?   B . n 
C 3 1    VAL 1    1    ?   ?   ?   C . n 
C 3 2    ILE 2    2    2   ILE ILE C . n 
C 3 3    TRP 3    3    3   TRP TRP C . n 
C 3 4    MET 4    4    4   MET MET C . n 
C 3 5    THR 5    5    5   THR THR C . n 
C 3 6    GLN 6    6    6   GLN GLN C . n 
C 3 7    SER 7    7    7   SER SER C . n 
C 3 8    PRO 8    8    8   PRO PRO C . n 
C 3 9    SER 9    9    9   SER SER C . n 
C 3 10   SER 10   10   10  SER SER C . n 
C 3 11   LEU 11   11   11  LEU LEU C . n 
C 3 12   SER 12   12   12  SER SER C . n 
C 3 13   ALA 13   13   13  ALA ALA C . n 
C 3 14   SER 14   14   14  SER SER C . n 
C 3 15   VAL 15   15   15  VAL VAL C . n 
C 3 16   GLY 16   16   16  GLY GLY C . n 
C 3 17   ASP 17   17   17  ASP ASP C . n 
C 3 18   ARG 18   18   18  ARG ARG C . n 
C 3 19   VAL 19   19   19  VAL VAL C . n 
C 3 20   THR 20   20   20  THR THR C . n 
C 3 21   ILE 21   21   21  ILE ILE C . n 
C 3 22   THR 22   22   22  THR THR C . n 
C 3 23   CYS 23   23   23  CYS CYS C . n 
C 3 24   GLN 24   24   24  GLN GLN C . n 
C 3 25   ALA 25   25   25  ALA ALA C . n 
C 3 26   SER 26   26   26  SER SER C . n 
C 3 27   GLN 27   27   27  GLN GLN C . n 
C 3 28   ASP 28   28   28  ASP ASP C . n 
C 3 29   ILE 29   29   29  ILE ILE C . n 
C 3 30   ARG 30   30   30  ARG ARG C . n 
C 3 31   PHE 31   31   31  PHE PHE C . n 
C 3 32   TYR 32   32   32  TYR TYR C . n 
C 3 33   LEU 33   33   33  LEU LEU C . n 
C 3 34   ASN 34   34   34  ASN ASN C . n 
C 3 35   TRP 35   35   35  TRP TRP C . n 
C 3 36   TYR 36   36   36  TYR TYR C . n 
C 3 37   GLN 37   37   37  GLN GLN C . n 
C 3 38   GLN 38   38   38  GLN GLN C . n 
C 3 39   LYS 39   39   39  LYS LYS C . n 
C 3 40   PRO 40   40   40  PRO PRO C . n 
C 3 41   GLY 41   41   41  GLY GLY C . n 
C 3 42   LYS 42   42   42  LYS LYS C . n 
C 3 43   ALA 43   43   43  ALA ALA C . n 
C 3 44   PRO 44   44   44  PRO PRO C . n 
C 3 45   LYS 45   45   45  LYS LYS C . n 
C 3 46   LEU 46   46   46  LEU LEU C . n 
C 3 47   LEU 47   47   47  LEU LEU C . n 
C 3 48   ILE 48   48   48  ILE ILE C . n 
C 3 49   SER 49   49   49  SER SER C . n 
C 3 50   ASP 50   50   50  ASP ASP C . n 
C 3 51   ALA 51   51   51  ALA ALA C . n 
C 3 52   SER 52   52   52  SER SER C . n 
C 3 53   ASN 53   53   53  ASN ASN C . n 
C 3 54   MET 54   54   54  MET MET C . n 
C 3 55   GLU 55   55   55  GLU GLU C . n 
C 3 56   THR 56   56   56  THR THR C . n 
C 3 57   GLY 57   57   57  GLY GLY C . n 
C 3 58   VAL 58   58   58  VAL VAL C . n 
C 3 59   PRO 59   59   59  PRO PRO C . n 
C 3 60   SER 60   60   60  SER SER C . n 
C 3 61   ARG 61   61   61  ARG ARG C . n 
C 3 62   PHE 62   62   62  PHE PHE C . n 
C 3 63   SER 63   63   63  SER SER C . n 
C 3 64   GLY 64   64   64  GLY GLY C . n 
C 3 65   SER 65   65   65  SER SER C . n 
C 3 66   GLY 66   66   66  GLY GLY C . n 
C 3 67   SER 67   67   67  SER SER C . n 
C 3 68   GLY 68   68   68  GLY GLY C . n 
C 3 69   THR 69   69   69  THR THR C . n 
C 3 70   ASP 70   70   70  ASP ASP C . n 
C 3 71   PHE 71   71   71  PHE PHE C . n 
C 3 72   THR 72   72   72  THR THR C . n 
C 3 73   PHE 73   73   73  PHE PHE C . n 
C 3 74   THR 74   74   74  THR THR C . n 
C 3 75   ILE 75   75   75  ILE ILE C . n 
C 3 76   SER 76   76   76  SER SER C . n 
C 3 77   SER 77   77   77  SER SER C . n 
C 3 78   LEU 78   78   78  LEU LEU C . n 
C 3 79   GLN 79   79   79  GLN GLN C . n 
C 3 80   PRO 80   80   80  PRO PRO C . n 
C 3 81   GLU 81   81   81  GLU GLU C . n 
C 3 82   ASP 82   82   82  ASP ASP C . n 
C 3 83   ILE 83   83   83  ILE ILE C . n 
C 3 84   ALA 84   84   84  ALA ALA C . n 
C 3 85   THR 85   85   85  THR THR C . n 
C 3 86   TYR 86   86   86  TYR TYR C . n 
C 3 87   TYR 87   87   87  TYR TYR C . n 
C 3 88   CYS 88   88   88  CYS CYS C . n 
C 3 89   GLN 89   89   89  GLN GLN C . n 
C 3 90   GLN 90   90   90  GLN GLN C . n 
C 3 91   TYR 91   91   91  TYR TYR C . n 
C 3 92   ASP 92   92   92  ASP ASP C . n 
C 3 93   ASN 93   93   93  ASN ASN C . n 
C 3 94   LEU 94   94   94  LEU LEU C . n 
C 3 95   PRO 95   95   95  PRO PRO C . n 
C 3 96   PHE 96   96   96  PHE PHE C . n 
C 3 97   THR 97   97   97  THR THR C . n 
C 3 98   PHE 98   98   98  PHE PHE C . n 
C 3 99   GLY 99   99   99  GLY GLY C . n 
C 3 100  PRO 100  100  100 PRO PRO C . n 
C 3 101  GLY 101  101  101 GLY GLY C . n 
C 3 102  THR 102  102  102 THR THR C . n 
C 3 103  LYS 103  103  103 LYS LYS C . n 
C 3 104  VAL 104  104  104 VAL VAL C . n 
C 3 105  ASP 105  105  105 ASP ASP C . n 
C 3 106  PHE 106  106  106 PHE PHE C . n 
C 3 107  LYS 107  107  ?   ?   ?   C . n 
D 4 1    GLN 1    1    ?   ?   ?   H . n 
D 4 2    ILE 2    2    ?   ?   ?   H . n 
D 4 3    THR 3    3    ?   ?   ?   H . n 
D 4 4    LEU 4    4    ?   ?   ?   H . n 
D 4 5    LYS 5    5    5   LYS LYS H . n 
D 4 6    GLU 6    6    6   GLU GLU H . n 
D 4 7    SER 7    7    7   SER SER H . n 
D 4 8    GLY 8    8    8   GLY GLY H . n 
D 4 9    PRO 9    9    9   PRO PRO H . n 
D 4 10   THR 10   10   10  THR THR H . n 
D 4 11   LEU 11   11   11  LEU LEU H . n 
D 4 12   VAL 12   12   12  VAL VAL H . n 
D 4 13   LYS 13   13   13  LYS LYS H . n 
D 4 14   PRO 14   14   14  PRO PRO H . n 
D 4 15   THR 15   15   15  THR THR H . n 
D 4 16   GLN 16   16   16  GLN GLN H . n 
D 4 17   THR 17   17   17  THR THR H . n 
D 4 18   LEU 18   18   18  LEU LEU H . n 
D 4 19   THR 19   19   19  THR THR H . n 
D 4 20   LEU 20   20   20  LEU LEU H . n 
D 4 21   THR 21   21   21  THR THR H . n 
D 4 22   CYS 22   22   22  CYS CYS H . n 
D 4 23   LYS 23   23   23  LYS LYS H . n 
D 4 24   LEU 24   24   24  LEU LEU H . n 
D 4 25   SER 25   25   25  SER SER H . n 
D 4 26   GLY 26   26   26  GLY GLY H . n 
D 4 27   PHE 27   27   27  PHE PHE H . n 
D 4 28   SER 28   28   28  SER SER H . n 
D 4 29   VAL 29   29   29  VAL VAL H . n 
D 4 30   ASN 30   30   30  ASN ASN H . n 
D 4 31   THR 31   31   31  THR THR H . n 
D 4 32   GLY 32   32   32  GLY GLY H . n 
D 4 33   GLY 33   33   33  GLY GLY H . n 
D 4 34   VAL 34   34   34  VAL VAL H . n 
D 4 35   GLY 35   35   35  GLY GLY H . n 
D 4 36   VAL 36   36   36  VAL VAL H . n 
D 4 37   GLY 37   37   37  GLY GLY H . n 
D 4 38   TRP 38   38   38  TRP TRP H . n 
D 4 39   ILE 39   39   39  ILE ILE H . n 
D 4 40   ARG 40   40   40  ARG ARG H . n 
D 4 41   GLN 41   41   41  GLN GLN H . n 
D 4 42   PRO 42   42   42  PRO PRO H . n 
D 4 43   PRO 43   43   43  PRO PRO H . n 
D 4 44   GLY 44   44   44  GLY GLY H . n 
D 4 45   LYS 45   45   45  LYS LYS H . n 
D 4 46   ALA 46   46   46  ALA ALA H . n 
D 4 47   LEU 47   47   47  LEU LEU H . n 
D 4 48   GLU 48   48   48  GLU GLU H . n 
D 4 49   TRP 49   49   49  TRP TRP H . n 
D 4 50   LEU 50   50   50  LEU LEU H . n 
D 4 51   ALA 51   51   51  ALA ALA H . n 
D 4 52   LEU 52   52   52  LEU LEU H . n 
D 4 53   ILE 53   53   53  ILE ILE H . n 
D 4 54   TYR 54   54   54  TYR TYR H . n 
D 4 55   TRP 55   55   55  TRP TRP H . n 
D 4 56   ASN 56   56   56  ASN ASN H . n 
D 4 57   ASP 57   57   57  ASP ASP H . n 
D 4 58   ASP 58   58   58  ASP ASP H . n 
D 4 59   LYS 59   59   59  LYS LYS H . n 
D 4 60   LEU 60   60   60  LEU LEU H . n 
D 4 61   TYR 61   61   61  TYR TYR H . n 
D 4 62   SER 62   62   62  SER SER H . n 
D 4 63   PRO 63   63   63  PRO PRO H . n 
D 4 64   SER 64   64   64  SER SER H . n 
D 4 65   LEU 65   65   65  LEU LEU H . n 
D 4 66   LYS 66   66   66  LYS LYS H . n 
D 4 67   SER 67   67   67  SER SER H . n 
D 4 68   ARG 68   68   68  ARG ARG H . n 
D 4 69   LEU 69   69   69  LEU LEU H . n 
D 4 70   THR 70   70   70  THR THR H . n 
D 4 71   VAL 71   71   71  VAL VAL H . n 
D 4 72   THR 72   72   72  THR THR H . n 
D 4 73   LYS 73   73   73  LYS LYS H . n 
D 4 74   ASP 74   74   74  ASP ASP H . n 
D 4 75   THR 75   75   75  THR THR H . n 
D 4 76   SER 76   76   76  SER SER H . n 
D 4 77   LYS 77   77   77  LYS LYS H . n 
D 4 78   ASN 78   78   78  ASN ASN H . n 
D 4 79   GLN 79   79   79  GLN GLN H . n 
D 4 80   VAL 80   80   80  VAL VAL H . n 
D 4 81   VAL 81   81   81  VAL VAL H . n 
D 4 82   LEU 82   82   82  LEU LEU H . n 
D 4 83   THR 83   83   83  THR THR H . n 
D 4 84   MET 84   84   84  MET MET H . n 
D 4 85   THR 85   85   85  THR THR H . n 
D 4 86   ASN 86   86   86  ASN ASN H . n 
D 4 87   MET 87   87   87  MET MET H . n 
D 4 88   ASP 88   88   88  ASP ASP H . n 
D 4 89   PRO 89   89   89  PRO PRO H . n 
D 4 90   VAL 90   90   90  VAL VAL H . n 
D 4 91   ASP 91   91   91  ASP ASP H . n 
D 4 92   THR 92   92   92  THR THR H . n 
D 4 93   ALA 93   93   93  ALA ALA H . n 
D 4 94   THR 94   94   94  THR THR H . n 
D 4 95   TYR 95   95   95  TYR TYR H . n 
D 4 96   TYR 96   96   96  TYR TYR H . n 
D 4 97   CYS 97   97   97  CYS CYS H . n 
D 4 98   ALA 98   98   98  ALA ALA H . n 
D 4 99   HIS 99   99   99  HIS HIS H . n 
D 4 100  VAL 100  100  100 VAL VAL H . n 
D 4 101  LEU 101  101  101 LEU LEU H . n 
D 4 102  VAL 102  102  102 VAL VAL H . n 
D 4 103  TRP 103  103  103 TRP TRP H . n 
D 4 104  PHE 104  104  104 PHE PHE H . n 
D 4 105  GLY 105  105  105 GLY GLY H . n 
D 4 106  GLU 106  106  106 GLU GLU H . n 
D 4 107  VAL 107  107  107 VAL VAL H . n 
D 4 108  LEU 108  108  108 LEU LEU H . n 
D 4 109  PRO 109  109  109 PRO PRO H . n 
D 4 110  ASP 110  110  110 ASP ASP H . n 
D 4 111  ALA 111  111  111 ALA ALA H . n 
D 4 112  PHE 112  112  112 PHE PHE H . n 
D 4 113  ASP 113  113  113 ASP ASP H . n 
D 4 114  VAL 114  114  114 VAL VAL H . n 
D 4 115  TRP 115  115  115 TRP TRP H . n 
D 4 116  GLY 116  116  116 GLY GLY H . n 
D 4 117  GLN 117  117  117 GLN GLN H . n 
D 4 118  GLY 118  118  118 GLY GLY H . n 
D 4 119  THR 119  119  119 THR THR H . n 
D 4 120  MET 120  120  120 MET MET H . n 
D 4 121  VAL 121  121  121 VAL VAL H . n 
D 4 122  THR 122  122  122 THR THR H . n 
D 4 123  VAL 123  123  123 VAL VAL H . n 
D 4 124  SER 124  124  ?   ?   ?   H . n 
D 4 125  SER 125  125  ?   ?   ?   H . n 
E 5 1    SER 1    1    1   SER SER L . n 
E 5 2    TYR 2    2    2   TYR TYR L . n 
E 5 3    GLU 3    3    3   GLU GLU L . n 
E 5 4    LEU 4    4    4   LEU LEU L . n 
E 5 5    THR 5    5    5   THR THR L . n 
E 5 6    GLN 6    6    6   GLN GLN L . n 
E 5 7    PRO 7    7    7   PRO PRO L . n 
E 5 8    PRO 8    8    8   PRO PRO L . n 
E 5 9    SER 9    9    9   SER SER L . n 
E 5 10   VAL 10   10   10  VAL VAL L . n 
E 5 11   SER 11   11   11  SER SER L . n 
E 5 12   VAL 12   12   12  VAL VAL L . n 
E 5 13   SER 13   13   13  SER SER L . n 
E 5 14   PRO 14   14   14  PRO PRO L . n 
E 5 15   GLY 15   15   15  GLY GLY L . n 
E 5 16   GLN 16   16   16  GLN GLN L . n 
E 5 17   THR 17   17   17  THR THR L . n 
E 5 18   ALA 18   18   18  ALA ALA L . n 
E 5 19   SER 19   19   19  SER SER L . n 
E 5 20   ILE 20   20   20  ILE ILE L . n 
E 5 21   THR 21   21   21  THR THR L . n 
E 5 22   CYS 22   22   22  CYS CYS L . n 
E 5 23   SER 23   23   23  SER SER L . n 
E 5 24   GLY 24   24   24  GLY GLY L . n 
E 5 25   ASP 25   25   25  ASP ASP L . n 
E 5 26   LYS 26   26   26  LYS LYS L . n 
E 5 27   LEU 27   27   27  LEU LEU L . n 
E 5 28   GLY 28   28   28  GLY GLY L . n 
E 5 29   GLU 29   29   29  GLU GLU L . n 
E 5 30   THR 30   30   30  THR THR L . n 
E 5 31   TYR 31   31   31  TYR TYR L . n 
E 5 32   ALA 32   32   32  ALA ALA L . n 
E 5 33   SER 33   33   33  SER SER L . n 
E 5 34   TRP 34   34   34  TRP TRP L . n 
E 5 35   TYR 35   35   35  TYR TYR L . n 
E 5 36   GLN 36   36   36  GLN GLN L . n 
E 5 37   GLN 37   37   37  GLN GLN L . n 
E 5 38   LYS 38   38   38  LYS LYS L . n 
E 5 39   PRO 39   39   39  PRO PRO L . n 
E 5 40   GLY 40   40   40  GLY GLY L . n 
E 5 41   GLN 41   41   41  GLN GLN L . n 
E 5 42   SER 42   42   42  SER SER L . n 
E 5 43   PRO 43   43   43  PRO PRO L . n 
E 5 44   ILE 44   44   44  ILE ILE L . n 
E 5 45   LEU 45   45   45  LEU LEU L . n 
E 5 46   VAL 46   46   46  VAL VAL L . n 
E 5 47   ILE 47   47   47  ILE ILE L . n 
E 5 48   TYR 48   48   48  TYR TYR L . n 
E 5 49   GLN 49   49   49  GLN GLN L . n 
E 5 50   ASP 50   50   50  ASP ASP L . n 
E 5 51   ASN 51   51   51  ASN ASN L . n 
E 5 52   LYS 52   52   52  LYS LYS L . n 
E 5 53   ARG 53   53   53  ARG ARG L . n 
E 5 54   PRO 54   54   54  PRO PRO L . n 
E 5 55   SER 55   55   55  SER SER L . n 
E 5 56   GLY 56   56   56  GLY GLY L . n 
E 5 57   ILE 57   57   57  ILE ILE L . n 
E 5 58   PRO 58   58   58  PRO PRO L . n 
E 5 59   GLU 59   59   59  GLU GLU L . n 
E 5 60   ARG 60   60   60  ARG ARG L . n 
E 5 61   PHE 61   61   61  PHE PHE L . n 
E 5 62   SER 62   62   62  SER SER L . n 
E 5 63   GLY 63   63   63  GLY GLY L . n 
E 5 64   SER 64   64   64  SER SER L . n 
E 5 65   ASN 65   65   65  ASN ASN L . n 
E 5 66   SER 66   66   66  SER SER L . n 
E 5 67   GLU 67   67   67  GLU GLU L . n 
E 5 68   ASN 68   68   68  ASN ASN L . n 
E 5 69   THR 69   69   69  THR THR L . n 
E 5 70   ALA 70   70   70  ALA ALA L . n 
E 5 71   THR 71   71   71  THR THR L . n 
E 5 72   LEU 72   72   72  LEU LEU L . n 
E 5 73   THR 73   73   73  THR THR L . n 
E 5 74   ILE 74   74   74  ILE ILE L . n 
E 5 75   SER 75   75   75  SER SER L . n 
E 5 76   GLY 76   76   76  GLY GLY L . n 
E 5 77   THR 77   77   77  THR THR L . n 
E 5 78   GLN 78   78   78  GLN GLN L . n 
E 5 79   THR 79   79   79  THR THR L . n 
E 5 80   MET 80   80   80  MET MET L . n 
E 5 81   ASP 81   81   81  ASP ASP L . n 
E 5 82   GLU 82   82   82  GLU GLU L . n 
E 5 83   ALA 83   83   83  ALA ALA L . n 
E 5 84   ASP 84   84   84  ASP ASP L . n 
E 5 85   TYR 85   85   85  TYR TYR L . n 
E 5 86   TYR 86   86   86  TYR TYR L . n 
E 5 87   CYS 87   87   87  CYS CYS L . n 
E 5 88   GLN 88   88   88  GLN GLN L . n 
E 5 89   ALA 89   89   89  ALA ALA L . n 
E 5 90   TRP 90   90   90  TRP TRP L . n 
E 5 91   ASP 91   91   91  ASP ASP L . n 
E 5 92   LYS 92   92   92  LYS LYS L . n 
E 5 93   THR 93   93   93  THR THR L . n 
E 5 94   ILE 94   94   94  ILE ILE L . n 
E 5 95   ALA 95   95   95  ALA ALA L . n 
E 5 96   GLY 96   96   96  GLY GLY L . n 
E 5 97   PHE 97   97   97  PHE PHE L . n 
E 5 98   GLY 98   98   98  GLY GLY L . n 
E 5 99   GLY 99   99   99  GLY GLY L . n 
E 5 100  GLY 100  100  100 GLY GLY L . n 
E 5 101  THR 101  101  101 THR THR L . n 
E 5 102  LYS 102  102  102 LYS LYS L . n 
E 5 103  LEU 103  103  103 LEU LEU L . n 
E 5 104  THR 104  104  104 THR THR L . n 
E 5 105  VAL 105  105  105 VAL VAL L . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
F 6 NAG 1 D NAG 1 A NAG 800 n 
F 6 NAG 2 D NAG 2 A NAG 801 n 
F 6 BMA 3 D BMA 3 A BMA 802 n 
G 7 NAG 1 E NAG 1 A NAG 808 n 
G 7 NAG 2 E NAG 2 A NAG 809 n 
H 7 NAG 1 F NAG 1 A NAG 812 n 
H 7 NAG 2 F NAG 2 A NAG 813 n 
# 
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 
I 8 NAG 1 1301 797 NAG NAG A . 
J 8 NAG 1 1302 803 NAG NAG A . 
K 8 NAG 1 1303 805 NAG NAG A . 
L 8 NAG 1 1304 806 NAG NAG A . 
M 8 NAG 1 1305 810 NAG NAG A . 
# 
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 A GLN 14  ? CG  ? A GLN 14  CG  
2   1 Y 1 A GLN 14  ? CD  ? A GLN 14  CD  
3   1 Y 1 A GLN 14  ? OE1 ? A GLN 14  OE1 
4   1 Y 1 A GLN 14  ? NE2 ? A GLN 14  NE2 
5   1 Y 1 A ARG 21  ? CG  ? A ARG 21  CG  
6   1 Y 1 A ARG 21  ? CD  ? A ARG 21  CD  
7   1 Y 1 A ARG 21  ? NE  ? A ARG 21  NE  
8   1 Y 1 A ARG 21  ? CZ  ? A ARG 21  CZ  
9   1 Y 1 A ARG 21  ? NH1 ? A ARG 21  NH1 
10  1 Y 1 A ARG 21  ? NH2 ? A ARG 21  NH2 
11  1 Y 1 A THR 22  ? OG1 ? A THR 22  OG1 
12  1 Y 1 A THR 22  ? CG2 ? A THR 22  CG2 
13  1 Y 1 A GLN 23  ? CG  ? A GLN 23  CG  
14  1 Y 1 A GLN 23  ? CD  ? A GLN 23  CD  
15  1 Y 1 A GLN 23  ? OE1 ? A GLN 23  OE1 
16  1 Y 1 A GLN 23  ? NE2 ? A GLN 23  NE2 
17  1 Y 1 A LEU 24  ? CG  ? A LEU 24  CG  
18  1 Y 1 A LEU 24  ? CD1 ? A LEU 24  CD1 
19  1 Y 1 A LEU 24  ? CD2 ? A LEU 24  CD2 
20  1 Y 1 A PHE 79  ? CG  ? A PHE 79  CG  
21  1 Y 1 A PHE 79  ? CD1 ? A PHE 79  CD1 
22  1 Y 1 A PHE 79  ? CD2 ? A PHE 79  CD2 
23  1 Y 1 A PHE 79  ? CE1 ? A PHE 79  CE1 
24  1 Y 1 A PHE 79  ? CE2 ? A PHE 79  CE2 
25  1 Y 1 A PHE 79  ? CZ  ? A PHE 79  CZ  
26  1 Y 1 A LYS 147 ? CG  ? A LYS 147 CG  
27  1 Y 1 A LYS 147 ? CD  ? A LYS 147 CD  
28  1 Y 1 A LYS 147 ? CE  ? A LYS 147 CE  
29  1 Y 1 A LYS 147 ? NZ  ? A LYS 147 NZ  
30  1 Y 1 A ASN 148 ? CG  ? A ASN 148 CG  
31  1 Y 1 A ASN 148 ? OD1 ? A ASN 148 OD1 
32  1 Y 1 A ASN 148 ? ND2 ? A ASN 148 ND2 
33  1 Y 1 A LYS 150 ? CG  ? A LYS 150 CG  
34  1 Y 1 A LYS 150 ? CD  ? A LYS 150 CD  
35  1 Y 1 A LYS 150 ? CE  ? A LYS 150 CE  
36  1 Y 1 A LYS 150 ? NZ  ? A LYS 150 NZ  
37  1 Y 1 A GLU 154 ? CG  ? A GLU 154 CG  
38  1 Y 1 A GLU 154 ? CD  ? A GLU 154 CD  
39  1 Y 1 A GLU 154 ? OE1 ? A GLU 154 OE1 
40  1 Y 1 A GLU 154 ? OE2 ? A GLU 154 OE2 
41  1 Y 1 A PHE 186 ? CG  ? A PHE 186 CG  
42  1 Y 1 A PHE 186 ? CD1 ? A PHE 186 CD1 
43  1 Y 1 A PHE 186 ? CD2 ? A PHE 186 CD2 
44  1 Y 1 A PHE 186 ? CE1 ? A PHE 186 CE1 
45  1 Y 1 A PHE 186 ? CE2 ? A PHE 186 CE2 
46  1 Y 1 A PHE 186 ? CZ  ? A PHE 186 CZ  
47  1 Y 1 A VAL 213 ? CG1 ? A VAL 213 CG1 
48  1 Y 1 A VAL 213 ? CG2 ? A VAL 213 CG2 
49  1 Y 1 A ARG 214 ? CG  ? A ARG 214 CG  
50  1 Y 1 A ARG 214 ? CD  ? A ARG 214 CD  
51  1 Y 1 A ARG 214 ? NE  ? A ARG 214 NE  
52  1 Y 1 A ARG 214 ? CZ  ? A ARG 214 CZ  
53  1 Y 1 A ARG 214 ? NH1 ? A ARG 214 NH1 
54  1 Y 1 A ARG 214 ? NH2 ? A ARG 214 NH2 
55  1 Y 1 A SER 247 ? OG  ? A SER 247 OG  
56  1 Y 1 A SER 248 ? OG  ? A SER 248 OG  
57  1 Y 1 A SER 249 ? OG  ? A SER 249 OG  
58  1 Y 1 B GLU 1   ? CG  ? B GLU 1   CG  
59  1 Y 1 B GLU 1   ? CD  ? B GLU 1   CD  
60  1 Y 1 B GLU 1   ? OE1 ? B GLU 1   OE1 
61  1 Y 1 B GLU 1   ? OE2 ? B GLU 1   OE2 
62  1 Y 1 B LYS 65  ? CG  ? B LYS 65  CG  
63  1 Y 1 B LYS 65  ? CD  ? B LYS 65  CD  
64  1 Y 1 B LYS 65  ? CE  ? B LYS 65  CE  
65  1 Y 1 B LYS 65  ? NZ  ? B LYS 65  NZ  
66  1 Y 1 B GLU 89  ? CG  ? B GLU 89  CG  
67  1 Y 1 B GLU 89  ? CD  ? B GLU 89  CD  
68  1 Y 1 B GLU 89  ? OE1 ? B GLU 89  OE1 
69  1 Y 1 B GLU 89  ? OE2 ? B GLU 89  OE2 
70  1 Y 1 C ILE 2   ? CG1 ? C ILE 2   CG1 
71  1 Y 1 C ILE 2   ? CG2 ? C ILE 2   CG2 
72  1 Y 1 C ILE 2   ? CD1 ? C ILE 2   CD1 
73  1 Y 1 C TRP 3   ? CG  ? C TRP 3   CG  
74  1 Y 1 C TRP 3   ? CD1 ? C TRP 3   CD1 
75  1 Y 1 C TRP 3   ? CD2 ? C TRP 3   CD2 
76  1 Y 1 C TRP 3   ? NE1 ? C TRP 3   NE1 
77  1 Y 1 C TRP 3   ? CE2 ? C TRP 3   CE2 
78  1 Y 1 C TRP 3   ? CE3 ? C TRP 3   CE3 
79  1 Y 1 C TRP 3   ? CZ2 ? C TRP 3   CZ2 
80  1 Y 1 C TRP 3   ? CZ3 ? C TRP 3   CZ3 
81  1 Y 1 C TRP 3   ? CH2 ? C TRP 3   CH2 
82  1 Y 1 C SER 7   ? OG  ? C SER 7   OG  
83  1 Y 1 C SER 9   ? OG  ? C SER 9   OG  
84  1 Y 1 C ASP 70  ? CG  ? C ASP 70  CG  
85  1 Y 1 C ASP 70  ? OD1 ? C ASP 70  OD1 
86  1 Y 1 C ASP 70  ? OD2 ? C ASP 70  OD2 
87  1 Y 1 C SER 77  ? OG  ? C SER 77  OG  
88  1 Y 1 C LYS 103 ? CG  ? C LYS 103 CG  
89  1 Y 1 C LYS 103 ? CD  ? C LYS 103 CD  
90  1 Y 1 C LYS 103 ? CE  ? C LYS 103 CE  
91  1 Y 1 C LYS 103 ? NZ  ? C LYS 103 NZ  
92  1 Y 1 C ASP 105 ? CG  ? C ASP 105 CG  
93  1 Y 1 C ASP 105 ? OD1 ? C ASP 105 OD1 
94  1 Y 1 C ASP 105 ? OD2 ? C ASP 105 OD2 
95  1 Y 1 C PHE 106 ? CG  ? C PHE 106 CG  
96  1 Y 1 C PHE 106 ? CD1 ? C PHE 106 CD1 
97  1 Y 1 C PHE 106 ? CD2 ? C PHE 106 CD2 
98  1 Y 1 C PHE 106 ? CE1 ? C PHE 106 CE1 
99  1 Y 1 C PHE 106 ? CE2 ? C PHE 106 CE2 
100 1 Y 1 C PHE 106 ? CZ  ? C PHE 106 CZ  
101 1 Y 1 H LYS 5   ? CG  ? D LYS 5   CG  
102 1 Y 1 H LYS 5   ? CD  ? D LYS 5   CD  
103 1 Y 1 H LYS 5   ? CE  ? D LYS 5   CE  
104 1 Y 1 H LYS 5   ? NZ  ? D LYS 5   NZ  
105 1 Y 1 H GLU 6   ? CG  ? D GLU 6   CG  
106 1 Y 1 H GLU 6   ? CD  ? D GLU 6   CD  
107 1 Y 1 H GLU 6   ? OE1 ? D GLU 6   OE1 
108 1 Y 1 H GLU 6   ? OE2 ? D GLU 6   OE2 
109 1 Y 1 H SER 7   ? OG  ? D SER 7   OG  
110 1 Y 1 H THR 10  ? OG1 ? D THR 10  OG1 
111 1 Y 1 H THR 10  ? CG2 ? D THR 10  CG2 
112 1 Y 1 H LEU 11  ? CG  ? D LEU 11  CG  
113 1 Y 1 H LEU 11  ? CD1 ? D LEU 11  CD1 
114 1 Y 1 H LEU 11  ? CD2 ? D LEU 11  CD2 
115 1 Y 1 H VAL 12  ? CG1 ? D VAL 12  CG1 
116 1 Y 1 H VAL 12  ? CG2 ? D VAL 12  CG2 
117 1 Y 1 H LYS 13  ? CG  ? D LYS 13  CG  
118 1 Y 1 H LYS 13  ? CD  ? D LYS 13  CD  
119 1 Y 1 H LYS 13  ? CE  ? D LYS 13  CE  
120 1 Y 1 H LYS 13  ? NZ  ? D LYS 13  NZ  
121 1 Y 1 H THR 15  ? OG1 ? D THR 15  OG1 
122 1 Y 1 H THR 15  ? CG2 ? D THR 15  CG2 
123 1 Y 1 H GLN 16  ? CG  ? D GLN 16  CG  
124 1 Y 1 H GLN 16  ? CD  ? D GLN 16  CD  
125 1 Y 1 H GLN 16  ? OE1 ? D GLN 16  OE1 
126 1 Y 1 H GLN 16  ? NE2 ? D GLN 16  NE2 
127 1 Y 1 H THR 17  ? OG1 ? D THR 17  OG1 
128 1 Y 1 H THR 17  ? CG2 ? D THR 17  CG2 
129 1 Y 1 H LEU 18  ? CG  ? D LEU 18  CG  
130 1 Y 1 H LEU 18  ? CD1 ? D LEU 18  CD1 
131 1 Y 1 H LEU 18  ? CD2 ? D LEU 18  CD2 
132 1 Y 1 H THR 19  ? OG1 ? D THR 19  OG1 
133 1 Y 1 H THR 19  ? CG2 ? D THR 19  CG2 
134 1 Y 1 H LEU 20  ? CG  ? D LEU 20  CG  
135 1 Y 1 H LEU 20  ? CD1 ? D LEU 20  CD1 
136 1 Y 1 H LEU 20  ? CD2 ? D LEU 20  CD2 
137 1 Y 1 H THR 21  ? OG1 ? D THR 21  OG1 
138 1 Y 1 H THR 21  ? CG2 ? D THR 21  CG2 
139 1 Y 1 H LYS 23  ? CG  ? D LYS 23  CG  
140 1 Y 1 H LYS 23  ? CD  ? D LYS 23  CD  
141 1 Y 1 H LYS 23  ? CE  ? D LYS 23  CE  
142 1 Y 1 H LYS 23  ? NZ  ? D LYS 23  NZ  
143 1 Y 1 H LEU 24  ? CG  ? D LEU 24  CG  
144 1 Y 1 H LEU 24  ? CD1 ? D LEU 24  CD1 
145 1 Y 1 H LEU 24  ? CD2 ? D LEU 24  CD2 
146 1 Y 1 H SER 25  ? OG  ? D SER 25  OG  
147 1 Y 1 H PHE 27  ? CG  ? D PHE 27  CG  
148 1 Y 1 H PHE 27  ? CD1 ? D PHE 27  CD1 
149 1 Y 1 H PHE 27  ? CD2 ? D PHE 27  CD2 
150 1 Y 1 H PHE 27  ? CE1 ? D PHE 27  CE1 
151 1 Y 1 H PHE 27  ? CE2 ? D PHE 27  CE2 
152 1 Y 1 H PHE 27  ? CZ  ? D PHE 27  CZ  
153 1 Y 1 H SER 28  ? OG  ? D SER 28  OG  
154 1 Y 1 H VAL 29  ? CG1 ? D VAL 29  CG1 
155 1 Y 1 H VAL 29  ? CG2 ? D VAL 29  CG2 
156 1 Y 1 H ASN 30  ? CG  ? D ASN 30  CG  
157 1 Y 1 H ASN 30  ? OD1 ? D ASN 30  OD1 
158 1 Y 1 H ASN 30  ? ND2 ? D ASN 30  ND2 
159 1 Y 1 H THR 31  ? OG1 ? D THR 31  OG1 
160 1 Y 1 H THR 31  ? CG2 ? D THR 31  CG2 
161 1 Y 1 H VAL 34  ? CG1 ? D VAL 34  CG1 
162 1 Y 1 H VAL 34  ? CG2 ? D VAL 34  CG2 
163 1 Y 1 H VAL 36  ? CG1 ? D VAL 36  CG1 
164 1 Y 1 H VAL 36  ? CG2 ? D VAL 36  CG2 
165 1 Y 1 H TRP 38  ? CG  ? D TRP 38  CG  
166 1 Y 1 H TRP 38  ? CD1 ? D TRP 38  CD1 
167 1 Y 1 H TRP 38  ? CD2 ? D TRP 38  CD2 
168 1 Y 1 H TRP 38  ? NE1 ? D TRP 38  NE1 
169 1 Y 1 H TRP 38  ? CE2 ? D TRP 38  CE2 
170 1 Y 1 H TRP 38  ? CE3 ? D TRP 38  CE3 
171 1 Y 1 H TRP 38  ? CZ2 ? D TRP 38  CZ2 
172 1 Y 1 H TRP 38  ? CZ3 ? D TRP 38  CZ3 
173 1 Y 1 H TRP 38  ? CH2 ? D TRP 38  CH2 
174 1 Y 1 H ILE 39  ? CG1 ? D ILE 39  CG1 
175 1 Y 1 H ILE 39  ? CG2 ? D ILE 39  CG2 
176 1 Y 1 H ILE 39  ? CD1 ? D ILE 39  CD1 
177 1 Y 1 H ARG 40  ? CG  ? D ARG 40  CG  
178 1 Y 1 H ARG 40  ? CD  ? D ARG 40  CD  
179 1 Y 1 H ARG 40  ? NE  ? D ARG 40  NE  
180 1 Y 1 H ARG 40  ? CZ  ? D ARG 40  CZ  
181 1 Y 1 H ARG 40  ? NH1 ? D ARG 40  NH1 
182 1 Y 1 H ARG 40  ? NH2 ? D ARG 40  NH2 
183 1 Y 1 H GLN 41  ? CG  ? D GLN 41  CG  
184 1 Y 1 H GLN 41  ? CD  ? D GLN 41  CD  
185 1 Y 1 H GLN 41  ? OE1 ? D GLN 41  OE1 
186 1 Y 1 H GLN 41  ? NE2 ? D GLN 41  NE2 
187 1 Y 1 H LYS 45  ? CG  ? D LYS 45  CG  
188 1 Y 1 H LYS 45  ? CD  ? D LYS 45  CD  
189 1 Y 1 H LYS 45  ? CE  ? D LYS 45  CE  
190 1 Y 1 H LYS 45  ? NZ  ? D LYS 45  NZ  
191 1 Y 1 H LEU 47  ? CG  ? D LEU 47  CG  
192 1 Y 1 H LEU 47  ? CD1 ? D LEU 47  CD1 
193 1 Y 1 H LEU 47  ? CD2 ? D LEU 47  CD2 
194 1 Y 1 H GLU 48  ? CG  ? D GLU 48  CG  
195 1 Y 1 H GLU 48  ? CD  ? D GLU 48  CD  
196 1 Y 1 H GLU 48  ? OE1 ? D GLU 48  OE1 
197 1 Y 1 H GLU 48  ? OE2 ? D GLU 48  OE2 
198 1 Y 1 H TRP 49  ? CG  ? D TRP 49  CG  
199 1 Y 1 H TRP 49  ? CD1 ? D TRP 49  CD1 
200 1 Y 1 H TRP 49  ? CD2 ? D TRP 49  CD2 
201 1 Y 1 H TRP 49  ? NE1 ? D TRP 49  NE1 
202 1 Y 1 H TRP 49  ? CE2 ? D TRP 49  CE2 
203 1 Y 1 H TRP 49  ? CE3 ? D TRP 49  CE3 
204 1 Y 1 H TRP 49  ? CZ2 ? D TRP 49  CZ2 
205 1 Y 1 H TRP 49  ? CZ3 ? D TRP 49  CZ3 
206 1 Y 1 H TRP 49  ? CH2 ? D TRP 49  CH2 
207 1 Y 1 H LEU 50  ? CG  ? D LEU 50  CG  
208 1 Y 1 H LEU 50  ? CD1 ? D LEU 50  CD1 
209 1 Y 1 H LEU 50  ? CD2 ? D LEU 50  CD2 
210 1 Y 1 H LEU 52  ? CG  ? D LEU 52  CG  
211 1 Y 1 H LEU 52  ? CD1 ? D LEU 52  CD1 
212 1 Y 1 H LEU 52  ? CD2 ? D LEU 52  CD2 
213 1 Y 1 H ILE 53  ? CG1 ? D ILE 53  CG1 
214 1 Y 1 H ILE 53  ? CG2 ? D ILE 53  CG2 
215 1 Y 1 H ILE 53  ? CD1 ? D ILE 53  CD1 
216 1 Y 1 H TYR 54  ? CG  ? D TYR 54  CG  
217 1 Y 1 H TYR 54  ? CD1 ? D TYR 54  CD1 
218 1 Y 1 H TYR 54  ? CD2 ? D TYR 54  CD2 
219 1 Y 1 H TYR 54  ? CE1 ? D TYR 54  CE1 
220 1 Y 1 H TYR 54  ? CE2 ? D TYR 54  CE2 
221 1 Y 1 H TYR 54  ? CZ  ? D TYR 54  CZ  
222 1 Y 1 H TYR 54  ? OH  ? D TYR 54  OH  
223 1 Y 1 H ASN 56  ? CG  ? D ASN 56  CG  
224 1 Y 1 H ASN 56  ? OD1 ? D ASN 56  OD1 
225 1 Y 1 H ASN 56  ? ND2 ? D ASN 56  ND2 
226 1 Y 1 H ASP 57  ? CG  ? D ASP 57  CG  
227 1 Y 1 H ASP 57  ? OD1 ? D ASP 57  OD1 
228 1 Y 1 H ASP 57  ? OD2 ? D ASP 57  OD2 
229 1 Y 1 H ASP 58  ? CG  ? D ASP 58  CG  
230 1 Y 1 H ASP 58  ? OD1 ? D ASP 58  OD1 
231 1 Y 1 H ASP 58  ? OD2 ? D ASP 58  OD2 
232 1 Y 1 H LYS 59  ? CG  ? D LYS 59  CG  
233 1 Y 1 H LYS 59  ? CD  ? D LYS 59  CD  
234 1 Y 1 H LYS 59  ? CE  ? D LYS 59  CE  
235 1 Y 1 H LYS 59  ? NZ  ? D LYS 59  NZ  
236 1 Y 1 H LEU 60  ? CG  ? D LEU 60  CG  
237 1 Y 1 H LEU 60  ? CD1 ? D LEU 60  CD1 
238 1 Y 1 H LEU 60  ? CD2 ? D LEU 60  CD2 
239 1 Y 1 H TYR 61  ? CG  ? D TYR 61  CG  
240 1 Y 1 H TYR 61  ? CD1 ? D TYR 61  CD1 
241 1 Y 1 H TYR 61  ? CD2 ? D TYR 61  CD2 
242 1 Y 1 H TYR 61  ? CE1 ? D TYR 61  CE1 
243 1 Y 1 H TYR 61  ? CE2 ? D TYR 61  CE2 
244 1 Y 1 H TYR 61  ? CZ  ? D TYR 61  CZ  
245 1 Y 1 H TYR 61  ? OH  ? D TYR 61  OH  
246 1 Y 1 H SER 62  ? OG  ? D SER 62  OG  
247 1 Y 1 H SER 64  ? OG  ? D SER 64  OG  
248 1 Y 1 H LEU 65  ? CG  ? D LEU 65  CG  
249 1 Y 1 H LEU 65  ? CD1 ? D LEU 65  CD1 
250 1 Y 1 H LEU 65  ? CD2 ? D LEU 65  CD2 
251 1 Y 1 H LYS 66  ? CG  ? D LYS 66  CG  
252 1 Y 1 H LYS 66  ? CD  ? D LYS 66  CD  
253 1 Y 1 H LYS 66  ? CE  ? D LYS 66  CE  
254 1 Y 1 H LYS 66  ? NZ  ? D LYS 66  NZ  
255 1 Y 1 H SER 67  ? OG  ? D SER 67  OG  
256 1 Y 1 H ARG 68  ? CG  ? D ARG 68  CG  
257 1 Y 1 H ARG 68  ? CD  ? D ARG 68  CD  
258 1 Y 1 H ARG 68  ? NE  ? D ARG 68  NE  
259 1 Y 1 H ARG 68  ? CZ  ? D ARG 68  CZ  
260 1 Y 1 H ARG 68  ? NH1 ? D ARG 68  NH1 
261 1 Y 1 H ARG 68  ? NH2 ? D ARG 68  NH2 
262 1 Y 1 H LEU 69  ? CG  ? D LEU 69  CG  
263 1 Y 1 H LEU 69  ? CD1 ? D LEU 69  CD1 
264 1 Y 1 H LEU 69  ? CD2 ? D LEU 69  CD2 
265 1 Y 1 H THR 70  ? OG1 ? D THR 70  OG1 
266 1 Y 1 H THR 70  ? CG2 ? D THR 70  CG2 
267 1 Y 1 H VAL 71  ? CG1 ? D VAL 71  CG1 
268 1 Y 1 H VAL 71  ? CG2 ? D VAL 71  CG2 
269 1 Y 1 H THR 72  ? OG1 ? D THR 72  OG1 
270 1 Y 1 H THR 72  ? CG2 ? D THR 72  CG2 
271 1 Y 1 H LYS 73  ? CG  ? D LYS 73  CG  
272 1 Y 1 H LYS 73  ? CD  ? D LYS 73  CD  
273 1 Y 1 H LYS 73  ? CE  ? D LYS 73  CE  
274 1 Y 1 H LYS 73  ? NZ  ? D LYS 73  NZ  
275 1 Y 1 H ASP 74  ? CG  ? D ASP 74  CG  
276 1 Y 1 H ASP 74  ? OD1 ? D ASP 74  OD1 
277 1 Y 1 H ASP 74  ? OD2 ? D ASP 74  OD2 
278 1 Y 1 H THR 75  ? OG1 ? D THR 75  OG1 
279 1 Y 1 H THR 75  ? CG2 ? D THR 75  CG2 
280 1 Y 1 H SER 76  ? OG  ? D SER 76  OG  
281 1 Y 1 H LYS 77  ? CG  ? D LYS 77  CG  
282 1 Y 1 H LYS 77  ? CD  ? D LYS 77  CD  
283 1 Y 1 H LYS 77  ? CE  ? D LYS 77  CE  
284 1 Y 1 H LYS 77  ? NZ  ? D LYS 77  NZ  
285 1 Y 1 H ASN 78  ? CG  ? D ASN 78  CG  
286 1 Y 1 H ASN 78  ? OD1 ? D ASN 78  OD1 
287 1 Y 1 H ASN 78  ? ND2 ? D ASN 78  ND2 
288 1 Y 1 H GLN 79  ? CG  ? D GLN 79  CG  
289 1 Y 1 H GLN 79  ? CD  ? D GLN 79  CD  
290 1 Y 1 H GLN 79  ? OE1 ? D GLN 79  OE1 
291 1 Y 1 H GLN 79  ? NE2 ? D GLN 79  NE2 
292 1 Y 1 H VAL 80  ? CG1 ? D VAL 80  CG1 
293 1 Y 1 H VAL 80  ? CG2 ? D VAL 80  CG2 
294 1 Y 1 H VAL 81  ? CG1 ? D VAL 81  CG1 
295 1 Y 1 H VAL 81  ? CG2 ? D VAL 81  CG2 
296 1 Y 1 H LEU 82  ? CG  ? D LEU 82  CG  
297 1 Y 1 H LEU 82  ? CD1 ? D LEU 82  CD1 
298 1 Y 1 H LEU 82  ? CD2 ? D LEU 82  CD2 
299 1 Y 1 H THR 83  ? OG1 ? D THR 83  OG1 
300 1 Y 1 H THR 83  ? CG2 ? D THR 83  CG2 
301 1 Y 1 H MET 84  ? CG  ? D MET 84  CG  
302 1 Y 1 H MET 84  ? SD  ? D MET 84  SD  
303 1 Y 1 H MET 84  ? CE  ? D MET 84  CE  
304 1 Y 1 H THR 85  ? OG1 ? D THR 85  OG1 
305 1 Y 1 H THR 85  ? CG2 ? D THR 85  CG2 
306 1 Y 1 H ASN 86  ? CG  ? D ASN 86  CG  
307 1 Y 1 H ASN 86  ? OD1 ? D ASN 86  OD1 
308 1 Y 1 H ASN 86  ? ND2 ? D ASN 86  ND2 
309 1 Y 1 H MET 87  ? CG  ? D MET 87  CG  
310 1 Y 1 H MET 87  ? SD  ? D MET 87  SD  
311 1 Y 1 H MET 87  ? CE  ? D MET 87  CE  
312 1 Y 1 H ASP 88  ? CG  ? D ASP 88  CG  
313 1 Y 1 H ASP 88  ? OD1 ? D ASP 88  OD1 
314 1 Y 1 H ASP 88  ? OD2 ? D ASP 88  OD2 
315 1 Y 1 H VAL 90  ? CG1 ? D VAL 90  CG1 
316 1 Y 1 H VAL 90  ? CG2 ? D VAL 90  CG2 
317 1 Y 1 H ASP 91  ? CG  ? D ASP 91  CG  
318 1 Y 1 H ASP 91  ? OD1 ? D ASP 91  OD1 
319 1 Y 1 H ASP 91  ? OD2 ? D ASP 91  OD2 
320 1 Y 1 H THR 92  ? OG1 ? D THR 92  OG1 
321 1 Y 1 H THR 92  ? CG2 ? D THR 92  CG2 
322 1 Y 1 H THR 94  ? OG1 ? D THR 94  OG1 
323 1 Y 1 H THR 94  ? CG2 ? D THR 94  CG2 
324 1 Y 1 H TYR 95  ? CG  ? D TYR 95  CG  
325 1 Y 1 H TYR 95  ? CD1 ? D TYR 95  CD1 
326 1 Y 1 H TYR 95  ? CD2 ? D TYR 95  CD2 
327 1 Y 1 H TYR 95  ? CE1 ? D TYR 95  CE1 
328 1 Y 1 H TYR 95  ? CE2 ? D TYR 95  CE2 
329 1 Y 1 H TYR 95  ? CZ  ? D TYR 95  CZ  
330 1 Y 1 H TYR 95  ? OH  ? D TYR 95  OH  
331 1 Y 1 H TYR 96  ? CG  ? D TYR 96  CG  
332 1 Y 1 H TYR 96  ? CD1 ? D TYR 96  CD1 
333 1 Y 1 H TYR 96  ? CD2 ? D TYR 96  CD2 
334 1 Y 1 H TYR 96  ? CE1 ? D TYR 96  CE1 
335 1 Y 1 H TYR 96  ? CE2 ? D TYR 96  CE2 
336 1 Y 1 H TYR 96  ? CZ  ? D TYR 96  CZ  
337 1 Y 1 H TYR 96  ? OH  ? D TYR 96  OH  
338 1 Y 1 H HIS 99  ? CG  ? D HIS 99  CG  
339 1 Y 1 H HIS 99  ? ND1 ? D HIS 99  ND1 
340 1 Y 1 H HIS 99  ? CD2 ? D HIS 99  CD2 
341 1 Y 1 H HIS 99  ? CE1 ? D HIS 99  CE1 
342 1 Y 1 H HIS 99  ? NE2 ? D HIS 99  NE2 
343 1 Y 1 H VAL 100 ? CG1 ? D VAL 100 CG1 
344 1 Y 1 H VAL 100 ? CG2 ? D VAL 100 CG2 
345 1 Y 1 H LEU 101 ? CG  ? D LEU 101 CG  
346 1 Y 1 H LEU 101 ? CD1 ? D LEU 101 CD1 
347 1 Y 1 H LEU 101 ? CD2 ? D LEU 101 CD2 
348 1 Y 1 H VAL 102 ? CG1 ? D VAL 102 CG1 
349 1 Y 1 H VAL 102 ? CG2 ? D VAL 102 CG2 
350 1 Y 1 H GLU 106 ? CG  ? D GLU 106 CG  
351 1 Y 1 H GLU 106 ? CD  ? D GLU 106 CD  
352 1 Y 1 H GLU 106 ? OE1 ? D GLU 106 OE1 
353 1 Y 1 H GLU 106 ? OE2 ? D GLU 106 OE2 
354 1 Y 1 H VAL 107 ? CG1 ? D VAL 107 CG1 
355 1 Y 1 H VAL 107 ? CG2 ? D VAL 107 CG2 
356 1 Y 1 H ASP 110 ? CG  ? D ASP 110 CG  
357 1 Y 1 H ASP 110 ? OD1 ? D ASP 110 OD1 
358 1 Y 1 H ASP 110 ? OD2 ? D ASP 110 OD2 
359 1 Y 1 H PHE 112 ? CG  ? D PHE 112 CG  
360 1 Y 1 H PHE 112 ? CD1 ? D PHE 112 CD1 
361 1 Y 1 H PHE 112 ? CD2 ? D PHE 112 CD2 
362 1 Y 1 H PHE 112 ? CE1 ? D PHE 112 CE1 
363 1 Y 1 H PHE 112 ? CE2 ? D PHE 112 CE2 
364 1 Y 1 H PHE 112 ? CZ  ? D PHE 112 CZ  
365 1 Y 1 H ASP 113 ? CG  ? D ASP 113 CG  
366 1 Y 1 H ASP 113 ? OD1 ? D ASP 113 OD1 
367 1 Y 1 H ASP 113 ? OD2 ? D ASP 113 OD2 
368 1 Y 1 H VAL 114 ? CG1 ? D VAL 114 CG1 
369 1 Y 1 H VAL 114 ? CG2 ? D VAL 114 CG2 
370 1 Y 1 H TRP 115 ? CG  ? D TRP 115 CG  
371 1 Y 1 H TRP 115 ? CD1 ? D TRP 115 CD1 
372 1 Y 1 H TRP 115 ? CD2 ? D TRP 115 CD2 
373 1 Y 1 H TRP 115 ? NE1 ? D TRP 115 NE1 
374 1 Y 1 H TRP 115 ? CE2 ? D TRP 115 CE2 
375 1 Y 1 H TRP 115 ? CE3 ? D TRP 115 CE3 
376 1 Y 1 H TRP 115 ? CZ2 ? D TRP 115 CZ2 
377 1 Y 1 H TRP 115 ? CZ3 ? D TRP 115 CZ3 
378 1 Y 1 H TRP 115 ? CH2 ? D TRP 115 CH2 
379 1 Y 1 H GLN 117 ? CG  ? D GLN 117 CG  
380 1 Y 1 H GLN 117 ? CD  ? D GLN 117 CD  
381 1 Y 1 H GLN 117 ? OE1 ? D GLN 117 OE1 
382 1 Y 1 H GLN 117 ? NE2 ? D GLN 117 NE2 
383 1 Y 1 H THR 119 ? OG1 ? D THR 119 OG1 
384 1 Y 1 H THR 119 ? CG2 ? D THR 119 CG2 
385 1 Y 1 H MET 120 ? CG  ? D MET 120 CG  
386 1 Y 1 H MET 120 ? SD  ? D MET 120 SD  
387 1 Y 1 H MET 120 ? CE  ? D MET 120 CE  
388 1 Y 1 H VAL 121 ? CG1 ? D VAL 121 CG1 
389 1 Y 1 H VAL 121 ? CG2 ? D VAL 121 CG2 
390 1 Y 1 H THR 122 ? OG1 ? D THR 122 OG1 
391 1 Y 1 H THR 122 ? CG2 ? D THR 122 CG2 
392 1 Y 1 H VAL 123 ? CG1 ? D VAL 123 CG1 
393 1 Y 1 H VAL 123 ? CG2 ? D VAL 123 CG2 
394 1 Y 1 L SER 1   ? OG  ? E SER 1   OG  
395 1 Y 1 L TYR 2   ? CG  ? E TYR 2   CG  
396 1 Y 1 L TYR 2   ? CD1 ? E TYR 2   CD1 
397 1 Y 1 L TYR 2   ? CD2 ? E TYR 2   CD2 
398 1 Y 1 L TYR 2   ? CE1 ? E TYR 2   CE1 
399 1 Y 1 L TYR 2   ? CE2 ? E TYR 2   CE2 
400 1 Y 1 L TYR 2   ? CZ  ? E TYR 2   CZ  
401 1 Y 1 L TYR 2   ? OH  ? E TYR 2   OH  
402 1 Y 1 L GLU 3   ? CG  ? E GLU 3   CG  
403 1 Y 1 L GLU 3   ? CD  ? E GLU 3   CD  
404 1 Y 1 L GLU 3   ? OE1 ? E GLU 3   OE1 
405 1 Y 1 L GLU 3   ? OE2 ? E GLU 3   OE2 
406 1 Y 1 L LEU 4   ? CG  ? E LEU 4   CG  
407 1 Y 1 L LEU 4   ? CD1 ? E LEU 4   CD1 
408 1 Y 1 L LEU 4   ? CD2 ? E LEU 4   CD2 
409 1 Y 1 L THR 5   ? OG1 ? E THR 5   OG1 
410 1 Y 1 L THR 5   ? CG2 ? E THR 5   CG2 
411 1 Y 1 L GLN 6   ? CG  ? E GLN 6   CG  
412 1 Y 1 L GLN 6   ? CD  ? E GLN 6   CD  
413 1 Y 1 L GLN 6   ? OE1 ? E GLN 6   OE1 
414 1 Y 1 L GLN 6   ? NE2 ? E GLN 6   NE2 
415 1 Y 1 L SER 9   ? OG  ? E SER 9   OG  
416 1 Y 1 L VAL 10  ? CG1 ? E VAL 10  CG1 
417 1 Y 1 L VAL 10  ? CG2 ? E VAL 10  CG2 
418 1 Y 1 L SER 11  ? OG  ? E SER 11  OG  
419 1 Y 1 L VAL 12  ? CG1 ? E VAL 12  CG1 
420 1 Y 1 L VAL 12  ? CG2 ? E VAL 12  CG2 
421 1 Y 1 L SER 13  ? OG  ? E SER 13  OG  
422 1 Y 1 L GLN 16  ? CG  ? E GLN 16  CG  
423 1 Y 1 L GLN 16  ? CD  ? E GLN 16  CD  
424 1 Y 1 L GLN 16  ? OE1 ? E GLN 16  OE1 
425 1 Y 1 L GLN 16  ? NE2 ? E GLN 16  NE2 
426 1 Y 1 L THR 17  ? OG1 ? E THR 17  OG1 
427 1 Y 1 L THR 17  ? CG2 ? E THR 17  CG2 
428 1 Y 1 L SER 19  ? OG  ? E SER 19  OG  
429 1 Y 1 L ILE 20  ? CG1 ? E ILE 20  CG1 
430 1 Y 1 L ILE 20  ? CG2 ? E ILE 20  CG2 
431 1 Y 1 L ILE 20  ? CD1 ? E ILE 20  CD1 
432 1 Y 1 L THR 21  ? OG1 ? E THR 21  OG1 
433 1 Y 1 L THR 21  ? CG2 ? E THR 21  CG2 
434 1 Y 1 L SER 23  ? OG  ? E SER 23  OG  
435 1 Y 1 L ASP 25  ? CG  ? E ASP 25  CG  
436 1 Y 1 L ASP 25  ? OD1 ? E ASP 25  OD1 
437 1 Y 1 L ASP 25  ? OD2 ? E ASP 25  OD2 
438 1 Y 1 L LYS 26  ? CG  ? E LYS 26  CG  
439 1 Y 1 L LYS 26  ? CD  ? E LYS 26  CD  
440 1 Y 1 L LYS 26  ? CE  ? E LYS 26  CE  
441 1 Y 1 L LYS 26  ? NZ  ? E LYS 26  NZ  
442 1 Y 1 L LEU 27  ? CG  ? E LEU 27  CG  
443 1 Y 1 L LEU 27  ? CD1 ? E LEU 27  CD1 
444 1 Y 1 L LEU 27  ? CD2 ? E LEU 27  CD2 
445 1 Y 1 L GLU 29  ? CG  ? E GLU 29  CG  
446 1 Y 1 L GLU 29  ? CD  ? E GLU 29  CD  
447 1 Y 1 L GLU 29  ? OE1 ? E GLU 29  OE1 
448 1 Y 1 L GLU 29  ? OE2 ? E GLU 29  OE2 
449 1 Y 1 L THR 30  ? OG1 ? E THR 30  OG1 
450 1 Y 1 L THR 30  ? CG2 ? E THR 30  CG2 
451 1 Y 1 L TYR 31  ? CG  ? E TYR 31  CG  
452 1 Y 1 L TYR 31  ? CD1 ? E TYR 31  CD1 
453 1 Y 1 L TYR 31  ? CD2 ? E TYR 31  CD2 
454 1 Y 1 L TYR 31  ? CE1 ? E TYR 31  CE1 
455 1 Y 1 L TYR 31  ? CE2 ? E TYR 31  CE2 
456 1 Y 1 L TYR 31  ? CZ  ? E TYR 31  CZ  
457 1 Y 1 L TYR 31  ? OH  ? E TYR 31  OH  
458 1 Y 1 L SER 33  ? OG  ? E SER 33  OG  
459 1 Y 1 L TRP 34  ? CG  ? E TRP 34  CG  
460 1 Y 1 L TRP 34  ? CD1 ? E TRP 34  CD1 
461 1 Y 1 L TRP 34  ? CD2 ? E TRP 34  CD2 
462 1 Y 1 L TRP 34  ? NE1 ? E TRP 34  NE1 
463 1 Y 1 L TRP 34  ? CE2 ? E TRP 34  CE2 
464 1 Y 1 L TRP 34  ? CE3 ? E TRP 34  CE3 
465 1 Y 1 L TRP 34  ? CZ2 ? E TRP 34  CZ2 
466 1 Y 1 L TRP 34  ? CZ3 ? E TRP 34  CZ3 
467 1 Y 1 L TRP 34  ? CH2 ? E TRP 34  CH2 
468 1 Y 1 L TYR 35  ? CG  ? E TYR 35  CG  
469 1 Y 1 L TYR 35  ? CD1 ? E TYR 35  CD1 
470 1 Y 1 L TYR 35  ? CD2 ? E TYR 35  CD2 
471 1 Y 1 L TYR 35  ? CE1 ? E TYR 35  CE1 
472 1 Y 1 L TYR 35  ? CE2 ? E TYR 35  CE2 
473 1 Y 1 L TYR 35  ? CZ  ? E TYR 35  CZ  
474 1 Y 1 L TYR 35  ? OH  ? E TYR 35  OH  
475 1 Y 1 L GLN 36  ? CG  ? E GLN 36  CG  
476 1 Y 1 L GLN 36  ? CD  ? E GLN 36  CD  
477 1 Y 1 L GLN 36  ? OE1 ? E GLN 36  OE1 
478 1 Y 1 L GLN 36  ? NE2 ? E GLN 36  NE2 
479 1 Y 1 L GLN 37  ? CG  ? E GLN 37  CG  
480 1 Y 1 L GLN 37  ? CD  ? E GLN 37  CD  
481 1 Y 1 L GLN 37  ? OE1 ? E GLN 37  OE1 
482 1 Y 1 L GLN 37  ? NE2 ? E GLN 37  NE2 
483 1 Y 1 L LYS 38  ? CG  ? E LYS 38  CG  
484 1 Y 1 L LYS 38  ? CD  ? E LYS 38  CD  
485 1 Y 1 L LYS 38  ? CE  ? E LYS 38  CE  
486 1 Y 1 L LYS 38  ? NZ  ? E LYS 38  NZ  
487 1 Y 1 L GLN 41  ? CG  ? E GLN 41  CG  
488 1 Y 1 L GLN 41  ? CD  ? E GLN 41  CD  
489 1 Y 1 L GLN 41  ? OE1 ? E GLN 41  OE1 
490 1 Y 1 L GLN 41  ? NE2 ? E GLN 41  NE2 
491 1 Y 1 L SER 42  ? OG  ? E SER 42  OG  
492 1 Y 1 L ILE 44  ? CG1 ? E ILE 44  CG1 
493 1 Y 1 L ILE 44  ? CG2 ? E ILE 44  CG2 
494 1 Y 1 L ILE 44  ? CD1 ? E ILE 44  CD1 
495 1 Y 1 L LEU 45  ? CG  ? E LEU 45  CG  
496 1 Y 1 L LEU 45  ? CD1 ? E LEU 45  CD1 
497 1 Y 1 L LEU 45  ? CD2 ? E LEU 45  CD2 
498 1 Y 1 L VAL 46  ? CG1 ? E VAL 46  CG1 
499 1 Y 1 L VAL 46  ? CG2 ? E VAL 46  CG2 
500 1 Y 1 L ILE 47  ? CG1 ? E ILE 47  CG1 
501 1 Y 1 L ILE 47  ? CG2 ? E ILE 47  CG2 
502 1 Y 1 L ILE 47  ? CD1 ? E ILE 47  CD1 
503 1 Y 1 L TYR 48  ? CG  ? E TYR 48  CG  
504 1 Y 1 L TYR 48  ? CD1 ? E TYR 48  CD1 
505 1 Y 1 L TYR 48  ? CD2 ? E TYR 48  CD2 
506 1 Y 1 L TYR 48  ? CE1 ? E TYR 48  CE1 
507 1 Y 1 L TYR 48  ? CE2 ? E TYR 48  CE2 
508 1 Y 1 L TYR 48  ? CZ  ? E TYR 48  CZ  
509 1 Y 1 L TYR 48  ? OH  ? E TYR 48  OH  
510 1 Y 1 L GLN 49  ? CG  ? E GLN 49  CG  
511 1 Y 1 L GLN 49  ? CD  ? E GLN 49  CD  
512 1 Y 1 L GLN 49  ? OE1 ? E GLN 49  OE1 
513 1 Y 1 L GLN 49  ? NE2 ? E GLN 49  NE2 
514 1 Y 1 L ASP 50  ? CG  ? E ASP 50  CG  
515 1 Y 1 L ASP 50  ? OD1 ? E ASP 50  OD1 
516 1 Y 1 L ASP 50  ? OD2 ? E ASP 50  OD2 
517 1 Y 1 L ASN 51  ? CG  ? E ASN 51  CG  
518 1 Y 1 L ASN 51  ? OD1 ? E ASN 51  OD1 
519 1 Y 1 L ASN 51  ? ND2 ? E ASN 51  ND2 
520 1 Y 1 L LYS 52  ? CG  ? E LYS 52  CG  
521 1 Y 1 L LYS 52  ? CD  ? E LYS 52  CD  
522 1 Y 1 L LYS 52  ? CE  ? E LYS 52  CE  
523 1 Y 1 L LYS 52  ? NZ  ? E LYS 52  NZ  
524 1 Y 1 L ARG 53  ? CG  ? E ARG 53  CG  
525 1 Y 1 L ARG 53  ? CD  ? E ARG 53  CD  
526 1 Y 1 L ARG 53  ? NE  ? E ARG 53  NE  
527 1 Y 1 L ARG 53  ? CZ  ? E ARG 53  CZ  
528 1 Y 1 L ARG 53  ? NH1 ? E ARG 53  NH1 
529 1 Y 1 L ARG 53  ? NH2 ? E ARG 53  NH2 
530 1 Y 1 L SER 55  ? OG  ? E SER 55  OG  
531 1 Y 1 L ILE 57  ? CG1 ? E ILE 57  CG1 
532 1 Y 1 L ILE 57  ? CG2 ? E ILE 57  CG2 
533 1 Y 1 L ILE 57  ? CD1 ? E ILE 57  CD1 
534 1 Y 1 L GLU 59  ? CG  ? E GLU 59  CG  
535 1 Y 1 L GLU 59  ? CD  ? E GLU 59  CD  
536 1 Y 1 L GLU 59  ? OE1 ? E GLU 59  OE1 
537 1 Y 1 L GLU 59  ? OE2 ? E GLU 59  OE2 
538 1 Y 1 L ARG 60  ? CG  ? E ARG 60  CG  
539 1 Y 1 L ARG 60  ? CD  ? E ARG 60  CD  
540 1 Y 1 L ARG 60  ? NE  ? E ARG 60  NE  
541 1 Y 1 L ARG 60  ? CZ  ? E ARG 60  CZ  
542 1 Y 1 L ARG 60  ? NH1 ? E ARG 60  NH1 
543 1 Y 1 L ARG 60  ? NH2 ? E ARG 60  NH2 
544 1 Y 1 L PHE 61  ? CG  ? E PHE 61  CG  
545 1 Y 1 L PHE 61  ? CD1 ? E PHE 61  CD1 
546 1 Y 1 L PHE 61  ? CD2 ? E PHE 61  CD2 
547 1 Y 1 L PHE 61  ? CE1 ? E PHE 61  CE1 
548 1 Y 1 L PHE 61  ? CE2 ? E PHE 61  CE2 
549 1 Y 1 L PHE 61  ? CZ  ? E PHE 61  CZ  
550 1 Y 1 L SER 62  ? OG  ? E SER 62  OG  
551 1 Y 1 L SER 64  ? OG  ? E SER 64  OG  
552 1 Y 1 L ASN 65  ? CG  ? E ASN 65  CG  
553 1 Y 1 L ASN 65  ? OD1 ? E ASN 65  OD1 
554 1 Y 1 L ASN 65  ? ND2 ? E ASN 65  ND2 
555 1 Y 1 L SER 66  ? OG  ? E SER 66  OG  
556 1 Y 1 L GLU 67  ? CG  ? E GLU 67  CG  
557 1 Y 1 L GLU 67  ? CD  ? E GLU 67  CD  
558 1 Y 1 L GLU 67  ? OE1 ? E GLU 67  OE1 
559 1 Y 1 L GLU 67  ? OE2 ? E GLU 67  OE2 
560 1 Y 1 L ASN 68  ? CG  ? E ASN 68  CG  
561 1 Y 1 L ASN 68  ? OD1 ? E ASN 68  OD1 
562 1 Y 1 L ASN 68  ? ND2 ? E ASN 68  ND2 
563 1 Y 1 L THR 69  ? OG1 ? E THR 69  OG1 
564 1 Y 1 L THR 69  ? CG2 ? E THR 69  CG2 
565 1 Y 1 L THR 71  ? OG1 ? E THR 71  OG1 
566 1 Y 1 L THR 71  ? CG2 ? E THR 71  CG2 
567 1 Y 1 L LEU 72  ? CG  ? E LEU 72  CG  
568 1 Y 1 L LEU 72  ? CD1 ? E LEU 72  CD1 
569 1 Y 1 L LEU 72  ? CD2 ? E LEU 72  CD2 
570 1 Y 1 L THR 73  ? OG1 ? E THR 73  OG1 
571 1 Y 1 L THR 73  ? CG2 ? E THR 73  CG2 
572 1 Y 1 L ILE 74  ? CG1 ? E ILE 74  CG1 
573 1 Y 1 L ILE 74  ? CG2 ? E ILE 74  CG2 
574 1 Y 1 L ILE 74  ? CD1 ? E ILE 74  CD1 
575 1 Y 1 L SER 75  ? OG  ? E SER 75  OG  
576 1 Y 1 L THR 77  ? OG1 ? E THR 77  OG1 
577 1 Y 1 L THR 77  ? CG2 ? E THR 77  CG2 
578 1 Y 1 L GLN 78  ? CG  ? E GLN 78  CG  
579 1 Y 1 L GLN 78  ? CD  ? E GLN 78  CD  
580 1 Y 1 L GLN 78  ? OE1 ? E GLN 78  OE1 
581 1 Y 1 L GLN 78  ? NE2 ? E GLN 78  NE2 
582 1 Y 1 L THR 79  ? OG1 ? E THR 79  OG1 
583 1 Y 1 L THR 79  ? CG2 ? E THR 79  CG2 
584 1 Y 1 L MET 80  ? CG  ? E MET 80  CG  
585 1 Y 1 L MET 80  ? SD  ? E MET 80  SD  
586 1 Y 1 L MET 80  ? CE  ? E MET 80  CE  
587 1 Y 1 L ASP 81  ? CG  ? E ASP 81  CG  
588 1 Y 1 L ASP 81  ? OD1 ? E ASP 81  OD1 
589 1 Y 1 L ASP 81  ? OD2 ? E ASP 81  OD2 
590 1 Y 1 L GLU 82  ? CG  ? E GLU 82  CG  
591 1 Y 1 L GLU 82  ? CD  ? E GLU 82  CD  
592 1 Y 1 L GLU 82  ? OE1 ? E GLU 82  OE1 
593 1 Y 1 L GLU 82  ? OE2 ? E GLU 82  OE2 
594 1 Y 1 L ASP 84  ? CG  ? E ASP 84  CG  
595 1 Y 1 L ASP 84  ? OD1 ? E ASP 84  OD1 
596 1 Y 1 L ASP 84  ? OD2 ? E ASP 84  OD2 
597 1 Y 1 L TYR 85  ? CG  ? E TYR 85  CG  
598 1 Y 1 L TYR 85  ? CD1 ? E TYR 85  CD1 
599 1 Y 1 L TYR 85  ? CD2 ? E TYR 85  CD2 
600 1 Y 1 L TYR 85  ? CE1 ? E TYR 85  CE1 
601 1 Y 1 L TYR 85  ? CE2 ? E TYR 85  CE2 
602 1 Y 1 L TYR 85  ? CZ  ? E TYR 85  CZ  
603 1 Y 1 L TYR 85  ? OH  ? E TYR 85  OH  
604 1 Y 1 L TYR 86  ? CG  ? E TYR 86  CG  
605 1 Y 1 L TYR 86  ? CD1 ? E TYR 86  CD1 
606 1 Y 1 L TYR 86  ? CD2 ? E TYR 86  CD2 
607 1 Y 1 L TYR 86  ? CE1 ? E TYR 86  CE1 
608 1 Y 1 L TYR 86  ? CE2 ? E TYR 86  CE2 
609 1 Y 1 L TYR 86  ? CZ  ? E TYR 86  CZ  
610 1 Y 1 L TYR 86  ? OH  ? E TYR 86  OH  
611 1 Y 1 L GLN 88  ? CG  ? E GLN 88  CG  
612 1 Y 1 L GLN 88  ? CD  ? E GLN 88  CD  
613 1 Y 1 L GLN 88  ? OE1 ? E GLN 88  OE1 
614 1 Y 1 L GLN 88  ? NE2 ? E GLN 88  NE2 
615 1 Y 1 L TRP 90  ? CG  ? E TRP 90  CG  
616 1 Y 1 L TRP 90  ? CD1 ? E TRP 90  CD1 
617 1 Y 1 L TRP 90  ? CD2 ? E TRP 90  CD2 
618 1 Y 1 L TRP 90  ? NE1 ? E TRP 90  NE1 
619 1 Y 1 L TRP 90  ? CE2 ? E TRP 90  CE2 
620 1 Y 1 L TRP 90  ? CE3 ? E TRP 90  CE3 
621 1 Y 1 L TRP 90  ? CZ2 ? E TRP 90  CZ2 
622 1 Y 1 L TRP 90  ? CZ3 ? E TRP 90  CZ3 
623 1 Y 1 L TRP 90  ? CH2 ? E TRP 90  CH2 
624 1 Y 1 L ASP 91  ? CG  ? E ASP 91  CG  
625 1 Y 1 L ASP 91  ? OD1 ? E ASP 91  OD1 
626 1 Y 1 L ASP 91  ? OD2 ? E ASP 91  OD2 
627 1 Y 1 L LYS 92  ? CG  ? E LYS 92  CG  
628 1 Y 1 L LYS 92  ? CD  ? E LYS 92  CD  
629 1 Y 1 L LYS 92  ? CE  ? E LYS 92  CE  
630 1 Y 1 L LYS 92  ? NZ  ? E LYS 92  NZ  
631 1 Y 1 L THR 93  ? OG1 ? E THR 93  OG1 
632 1 Y 1 L THR 93  ? CG2 ? E THR 93  CG2 
633 1 Y 1 L ILE 94  ? CG1 ? E ILE 94  CG1 
634 1 Y 1 L ILE 94  ? CG2 ? E ILE 94  CG2 
635 1 Y 1 L ILE 94  ? CD1 ? E ILE 94  CD1 
636 1 Y 1 L PHE 97  ? CG  ? E PHE 97  CG  
637 1 Y 1 L PHE 97  ? CD1 ? E PHE 97  CD1 
638 1 Y 1 L PHE 97  ? CD2 ? E PHE 97  CD2 
639 1 Y 1 L PHE 97  ? CE1 ? E PHE 97  CE1 
640 1 Y 1 L PHE 97  ? CE2 ? E PHE 97  CE2 
641 1 Y 1 L PHE 97  ? CZ  ? E PHE 97  CZ  
642 1 Y 1 L THR 101 ? OG1 ? E THR 101 OG1 
643 1 Y 1 L THR 101 ? CG2 ? E THR 101 CG2 
644 1 Y 1 L LYS 102 ? CG  ? E LYS 102 CG  
645 1 Y 1 L LYS 102 ? CD  ? E LYS 102 CD  
646 1 Y 1 L LYS 102 ? CE  ? E LYS 102 CE  
647 1 Y 1 L LYS 102 ? NZ  ? E LYS 102 NZ  
648 1 Y 1 L LEU 103 ? CG  ? E LEU 103 CG  
649 1 Y 1 L LEU 103 ? CD1 ? E LEU 103 CD1 
650 1 Y 1 L LEU 103 ? CD2 ? E LEU 103 CD2 
651 1 Y 1 L THR 104 ? OG1 ? E THR 104 OG1 
652 1 Y 1 L THR 104 ? CG2 ? E THR 104 CG2 
653 1 Y 1 L VAL 105 ? CG1 ? E VAL 105 CG1 
654 1 Y 1 L VAL 105 ? CG2 ? E VAL 105 CG2 
# 
_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                   8VYF 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     8VYF 
_struct.title                        'SARS-CoV-2 S NTD (C.37 Lambda variant) plus S2L20 and S2X303 Fabs, 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        8VYF 
_struct_keywords.text            
;sars-cov-2, coronavirus, lambda, s2l20, s2x303, C.37, antibody, Fab, S protein, spike, fusion protein, Structural Genomics, Seattle Structural Genomics Center for Infectious Disease, SSGCID, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM complex
;
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN/IMMUNE SYSTEM' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 7 ? 
H N N 7 ? 
I N N 8 ? 
J N N 8 ? 
K N N 8 ? 
L N N 8 ? 
M N N 8 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP SPIKE_SARS2 P0DTC2 ? 1 
;MFVFLVLLPLVSSQCVNLTTRTQLPPAYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFHAIHVSGTNGTKRFD
NPVLPFNDGVYFASTEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVVIKVCEFQFCNDPFLGVYYHKNNKSWMESEFRVY
SSANNCTFEYVSQPFLMDLEGKQGNFKNLREFVFKNIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGINITRFQT
LLALHRSYLTPGDSSSGWTAGAAAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQTSNFRV
QPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSF
VIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPC
NGVEGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFNFNGLTGTGVLTESNKKFL
PFQQFGRDIADTTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNQVAVLYQDVNCTEVPVAIHADQLTPTWRVYSTGS
NVFQTRAGCLIGAEHVNNSYECDIPIGAGICASYQTQTNSPRRARSVASQSIIAYTMSLGAENSVAYSNNSIAIPTNFTI
SVTTEILPVSMTKTSVDCTMYICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKDFGGF
NFSQILPDPSKPSKRSFIEDLLFNKVTLADAGFIKQYGDCLGDIAARDLICAQKFNGLTVLPPLLTDEMIAQYTSALLAG
TITSGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKLIANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALN
TLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRV
DFCGKGYHLMSFPQSAPHGVVFLHVTYVPAQEKNFTTAPAICHDGKAHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNT
FVSGNCDVVIGIVNNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDL
QELGKYEQ
;
1 
2 PDB 8VYF        8VYF   ? 2 ? 1 
3 PDB 8VYF        8VYF   ? 3 ? 1 
4 PDB 8VYF        8VYF   ? 4 ? 1 
5 PDB 8VYF        8VYF   ? 5 ? 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 8VYF A 1 ? 1201 ? P0DTC2 1 ? 1208 ? 1 1201 
2 2 8VYF B 1 ? 122  ? 8VYF   1 ? 122  ? 1 122  
3 3 8VYF C 1 ? 107  ? 8VYF   1 ? 107  ? 1 107  
4 4 8VYF H 1 ? 125  ? 8VYF   1 ? 125  ? 1 125  
5 5 8VYF L 1 ? 105  ? 8VYF   1 ? 105  ? 1 105  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8VYF VAL A 75   ? UNP P0DTC2 GLY 75  variant          75   1  
1 8VYF ILE A 76   ? UNP P0DTC2 THR 76  variant          76   2  
1 8VYF ?   A ?    ? UNP P0DTC2 ARG 246 deletion         ?    3  
1 8VYF ?   A ?    ? UNP P0DTC2 SER 247 deletion         ?    4  
1 8VYF ?   A ?    ? UNP P0DTC2 TYR 248 deletion         ?    5  
1 8VYF ?   A ?    ? UNP P0DTC2 LEU 249 deletion         ?    6  
1 8VYF ?   A ?    ? UNP P0DTC2 THR 250 deletion         ?    7  
1 8VYF ?   A ?    ? UNP P0DTC2 PRO 251 deletion         ?    8  
1 8VYF ?   A ?    ? UNP P0DTC2 GLY 252 deletion         ?    9  
1 8VYF ASN A 246  ? UNP P0DTC2 ASP 253 variant          246  10 
1 8VYF CYS A 376  ? UNP P0DTC2 SER 383 conflict         376  11 
1 8VYF GLN A 445  ? UNP P0DTC2 LEU 452 variant          445  12 
1 8VYF SER A 483  ? UNP P0DTC2 PHE 490 variant          483  13 
1 8VYF GLY A 607  ? UNP P0DTC2 ASP 614 variant          607  14 
1 8VYF PRO A 810  ? UNP P0DTC2 PHE 817 conflict         810  15 
1 8VYF ASN A 852  ? UNP P0DTC2 THR 859 variant          852  16 
1 8VYF PRO A 885  ? UNP P0DTC2 ALA 892 conflict         885  17 
1 8VYF PRO A 892  ? UNP P0DTC2 ALA 899 conflict         892  18 
1 8VYF PRO A 935  ? UNP P0DTC2 ALA 942 conflict         935  19 
1 8VYF CYS A 978  ? UNP P0DTC2 ASP 985 conflict         978  20 
1 8VYF PRO A 979  ? UNP P0DTC2 LYS 986 conflict         979  21 
1 8VYF PRO A 980  ? UNP P0DTC2 VAL 987 conflict         980  22 
1 8VYF GLY A 1202 ? UNP P0DTC2 ?   ?   'expression tag' 1202 23 
1 8VYF SER A 1203 ? UNP P0DTC2 ?   ?   'expression tag' 1203 24 
1 8VYF GLY A 1204 ? UNP P0DTC2 ?   ?   'expression tag' 1204 25 
1 8VYF TYR A 1205 ? UNP P0DTC2 ?   ?   'expression tag' 1205 26 
1 8VYF ILE A 1206 ? UNP P0DTC2 ?   ?   'expression tag' 1206 27 
1 8VYF PRO A 1207 ? UNP P0DTC2 ?   ?   'expression tag' 1207 28 
1 8VYF GLU A 1208 ? UNP P0DTC2 ?   ?   'expression tag' 1208 29 
1 8VYF ALA A 1209 ? UNP P0DTC2 ?   ?   'expression tag' 1209 30 
1 8VYF PRO A 1210 ? UNP P0DTC2 ?   ?   'expression tag' 1210 31 
1 8VYF ARG A 1211 ? UNP P0DTC2 ?   ?   'expression tag' 1211 32 
1 8VYF ASP A 1212 ? UNP P0DTC2 ?   ?   'expression tag' 1212 33 
1 8VYF GLY A 1213 ? UNP P0DTC2 ?   ?   'expression tag' 1213 34 
1 8VYF GLN A 1214 ? UNP P0DTC2 ?   ?   'expression tag' 1214 35 
1 8VYF ALA A 1215 ? UNP P0DTC2 ?   ?   'expression tag' 1215 36 
1 8VYF TYR A 1216 ? UNP P0DTC2 ?   ?   'expression tag' 1216 37 
1 8VYF VAL A 1217 ? UNP P0DTC2 ?   ?   'expression tag' 1217 38 
1 8VYF ARG A 1218 ? UNP P0DTC2 ?   ?   'expression tag' 1218 39 
1 8VYF LYS A 1219 ? UNP P0DTC2 ?   ?   'expression tag' 1219 40 
1 8VYF ASP A 1220 ? UNP P0DTC2 ?   ?   'expression tag' 1220 41 
1 8VYF GLY A 1221 ? UNP P0DTC2 ?   ?   'expression tag' 1221 42 
1 8VYF GLU A 1222 ? UNP P0DTC2 ?   ?   'expression tag' 1222 43 
1 8VYF TRP A 1223 ? UNP P0DTC2 ?   ?   'expression tag' 1223 44 
1 8VYF VAL A 1224 ? UNP P0DTC2 ?   ?   'expression tag' 1224 45 
1 8VYF LEU A 1225 ? UNP P0DTC2 ?   ?   'expression tag' 1225 46 
1 8VYF LEU A 1226 ? UNP P0DTC2 ?   ?   'expression tag' 1226 47 
1 8VYF SER A 1227 ? UNP P0DTC2 ?   ?   'expression tag' 1227 48 
1 8VYF THR A 1228 ? UNP P0DTC2 ?   ?   'expression tag' 1228 49 
1 8VYF PHE A 1229 ? UNP P0DTC2 ?   ?   'expression tag' 1229 50 
1 8VYF LEU A 1230 ? UNP P0DTC2 ?   ?   'expression tag' 1230 51 
1 8VYF GLY A 1231 ? UNP P0DTC2 ?   ?   'expression tag' 1231 52 
1 8VYF ARG A 1232 ? UNP P0DTC2 ?   ?   'expression tag' 1232 53 
1 8VYF SER A 1233 ? UNP P0DTC2 ?   ?   'expression tag' 1233 54 
1 8VYF LEU A 1234 ? UNP P0DTC2 ?   ?   'expression tag' 1234 55 
1 8VYF GLU A 1235 ? UNP P0DTC2 ?   ?   'expression tag' 1235 56 
1 8VYF VAL A 1236 ? UNP P0DTC2 ?   ?   'expression tag' 1236 57 
1 8VYF LEU A 1237 ? UNP P0DTC2 ?   ?   'expression tag' 1237 58 
1 8VYF PHE A 1238 ? UNP P0DTC2 ?   ?   'expression tag' 1238 59 
1 8VYF GLN A 1239 ? UNP P0DTC2 ?   ?   'expression tag' 1239 60 
1 8VYF GLY A 1240 ? UNP P0DTC2 ?   ?   'expression tag' 1240 61 
1 8VYF PRO A 1241 ? UNP P0DTC2 ?   ?   'expression tag' 1241 62 
1 8VYF GLY A 1242 ? UNP P0DTC2 ?   ?   'expression tag' 1242 63 
1 8VYF SER A 1243 ? UNP P0DTC2 ?   ?   'expression tag' 1243 64 
1 8VYF GLY A 1244 ? UNP P0DTC2 ?   ?   'expression tag' 1244 65 
1 8VYF GLY A 1245 ? UNP P0DTC2 ?   ?   'expression tag' 1245 66 
1 8VYF LEU A 1246 ? UNP P0DTC2 ?   ?   'expression tag' 1246 67 
1 8VYF ASN A 1247 ? UNP P0DTC2 ?   ?   'expression tag' 1247 68 
1 8VYF ASP A 1248 ? UNP P0DTC2 ?   ?   'expression tag' 1248 69 
1 8VYF ILE A 1249 ? UNP P0DTC2 ?   ?   'expression tag' 1249 70 
1 8VYF PHE A 1250 ? UNP P0DTC2 ?   ?   'expression tag' 1250 71 
1 8VYF GLU A 1251 ? UNP P0DTC2 ?   ?   'expression tag' 1251 72 
1 8VYF ALA A 1252 ? UNP P0DTC2 ?   ?   'expression tag' 1252 73 
1 8VYF GLN A 1253 ? UNP P0DTC2 ?   ?   'expression tag' 1253 74 
1 8VYF LYS A 1254 ? UNP P0DTC2 ?   ?   'expression tag' 1254 75 
1 8VYF ILE A 1255 ? UNP P0DTC2 ?   ?   'expression tag' 1255 76 
1 8VYF GLU A 1256 ? UNP P0DTC2 ?   ?   'expression tag' 1256 77 
1 8VYF TRP A 1257 ? UNP P0DTC2 ?   ?   'expression tag' 1257 78 
1 8VYF HIS A 1258 ? UNP P0DTC2 ?   ?   'expression tag' 1258 79 
1 8VYF GLU A 1259 ? UNP P0DTC2 ?   ?   'expression tag' 1259 80 
1 8VYF GLY A 1260 ? UNP P0DTC2 ?   ?   'expression tag' 1260 81 
1 8VYF SER A 1261 ? UNP P0DTC2 ?   ?   'expression tag' 1261 82 
1 8VYF GLY A 1262 ? UNP P0DTC2 ?   ?   'expression tag' 1262 83 
1 8VYF HIS A 1263 ? UNP P0DTC2 ?   ?   'expression tag' 1263 84 
1 8VYF HIS A 1264 ? UNP P0DTC2 ?   ?   'expression tag' 1264 85 
1 8VYF HIS A 1265 ? UNP P0DTC2 ?   ?   'expression tag' 1265 86 
1 8VYF HIS A 1266 ? UNP P0DTC2 ?   ?   'expression tag' 1266 87 
1 8VYF HIS A 1267 ? UNP P0DTC2 ?   ?   'expression tag' 1267 88 
1 8VYF HIS A 1268 ? UNP P0DTC2 ?   ?   'expression tag' 1268 89 
1 8VYF HIS A 1269 ? UNP P0DTC2 ?   ?   'expression tag' 1269 90 
1 8VYF HIS A 1270 ? UNP P0DTC2 ?   ?   'expression tag' 1270 91 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   pentameric 
_pdbx_struct_assembly.oligomeric_count     5 
# 
_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,K,L,M 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
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 ASP A 287 ? LEU A 296 ? ASP A 287 LEU A 296 1 ? 10 
HELX_P HELX_P2 AA2 THR B 28  ? TYR B 32  ? THR B 28  TYR B 32  5 ? 5  
HELX_P HELX_P3 AA3 ARG B 87  ? THR B 91  ? ARG B 87  THR B 91  5 ? 5  
HELX_P HELX_P4 AA4 LEU D 65  ? SER D 67  ? LEU H 65  SER H 67  5 ? 3  
HELX_P HELX_P5 AA5 ASP D 88  ? THR D 92  ? ASP H 88  THR H 92  5 ? 5  
HELX_P HELX_P6 AA6 LYS E 26  ? THR E 30  ? LYS L 26  THR L 30  5 ? 5  
HELX_P HELX_P7 AA7 GLN E 78  ? GLU E 82  ? GLN L 78  GLU L 82  5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A CYS 15  SG  ? ? ? 1_555 A CYS 136 SG ? ? A CYS 15  A CYS 136  1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf2  disulf ?    ? A CYS 131 SG  ? ? ? 1_555 A CYS 166 SG ? ? A CYS 131 A CYS 166  1_555 ? ? ? ? ? ? ? 2.038 ? ?               
disulf3  disulf ?    ? A CYS 284 SG  ? ? ? 1_555 A CYS 294 SG ? ? A CYS 284 A CYS 294  1_555 ? ? ? ? ? ? ? 2.026 ? ?               
disulf4  disulf ?    ? B CYS 22  SG  ? ? ? 1_555 B CYS 96  SG ? ? B CYS 22  B CYS 96   1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf5  disulf ?    ? C CYS 23  SG  ? ? ? 1_555 C CYS 88  SG ? ? C CYS 23  C CYS 88   1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf6  disulf ?    ? D CYS 22  SG  ? ? ? 1_555 D CYS 97  SG ? ? H CYS 22  H CYS 97   1_555 ? ? ? ? ? ? ? 2.028 ? ?               
disulf7  disulf ?    ? E CYS 22  SG  ? ? ? 1_555 E CYS 87  SG ? ? L CYS 22  L CYS 87   1_555 ? ? ? ? ? ? ? 2.024 ? ?               
covale1  covale one  ? A ASN 17  ND2 ? ? ? 1_555 L NAG .   C1 ? ? A ASN 17  A NAG 1304 1_555 ? ? ? ? ? ? ? 1.494 ? N-Glycosylation 
covale2  covale one  ? A ASN 61  ND2 ? ? ? 1_555 H NAG .   C1 ? ? A ASN 61  F NAG 1    1_555 ? ? ? ? ? ? ? 1.491 ? N-Glycosylation 
covale3  covale one  ? A ASN 122 ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 122 D NAG 1    1_555 ? ? ? ? ? ? ? 1.494 ? N-Glycosylation 
covale4  covale one  ? A ASN 149 ND2 ? ? ? 1_555 K NAG .   C1 ? ? A ASN 149 A NAG 1303 1_555 ? ? ? ? ? ? ? 1.496 ? N-Glycosylation 
covale5  covale one  ? A ASN 165 ND2 ? ? ? 1_555 J NAG .   C1 ? ? A ASN 165 A NAG 1302 1_555 ? ? ? ? ? ? ? 1.493 ? N-Glycosylation 
covale6  covale one  ? A ASN 234 ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 234 E NAG 1    1_555 ? ? ? ? ? ? ? 1.494 ? N-Glycosylation 
covale7  covale one  ? A ASN 246 ND2 ? ? ? 1_555 M NAG .   C1 ? ? A ASN 246 A NAG 1305 1_555 ? ? ? ? ? ? ? 1.491 ? N-Glycosylation 
covale8  covale one  ? A ASN 275 ND2 ? ? ? 1_555 I NAG .   C1 ? ? A ASN 275 A NAG 1301 1_555 ? ? ? ? ? ? ? 1.500 ? N-Glycosylation 
covale9  covale both ? F NAG .   O4  ? ? ? 1_555 F NAG .   C1 ? ? D NAG 1   D NAG 2    1_555 ? ? ? ? ? ? ? 1.504 ? ?               
covale10 covale both ? F NAG .   O4  ? ? ? 1_555 F BMA .   C1 ? ? D NAG 2   D BMA 3    1_555 ? ? ? ? ? ? ? 1.498 ? ?               
covale11 covale both ? G NAG .   O4  ? ? ? 1_555 G NAG .   C1 ? ? E NAG 1   E NAG 2    1_555 ? ? ? ? ? ? ? 1.503 ? ?               
covale12 covale both ? H NAG .   O4  ? ? ? 1_555 H NAG .   C1 ? ? F NAG 1   F NAG 2    1_555 ? ? ? ? ? ? ? 1.504 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 7  C . ? SER 7  C PRO 8  C ? PRO 8  C 1 -1.80 
2 LEU 94 C . ? LEU 94 C PRO 95 C ? PRO 95 C 1 -1.60 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 3 ? 
AA3 ? 7 ? 
AA4 ? 4 ? 
AA5 ? 7 ? 
AA6 ? 4 ? 
AA7 ? 7 ? 
AA8 ? 4 ? 
AA9 ? 6 ? 
AB1 ? 5 ? 
AB2 ? 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 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 6 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 2 6 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 4 6 ? parallel      
AA3 6 7 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 7 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 2 5 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 5 7 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 7 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 2 5 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA7 5 7 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 1 4 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AA9 4 6 ? anti-parallel 
AB1 1 2 ? parallel      
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 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 ALA A 27  ? ASN A 30  ? ALA A 27  ASN A 30  
AA1 2 ASN A 61  ? HIS A 66  ? ASN A 61  HIS A 66  
AA1 3 ALA A 257 ? TYR A 262 ? ALA A 257 TYR A 262 
AA1 4 VAL A 90  ? THR A 95  ? VAL A 90  THR A 95  
AA1 5 LYS A 187 ? ILE A 197 ? LYS A 187 ILE A 197 
AA1 6 TYR A 200 ? ILE A 210 ? TYR A 200 ILE A 210 
AA1 7 GLU A 224 ? PRO A 230 ? GLU A 224 PRO A 230 
AA2 1 VAL A 47  ? PHE A 55  ? VAL A 47  PHE A 55  
AA2 2 GLN A 264 ? TYR A 272 ? GLN A 264 TYR A 272 
AA2 3 ILE A 278 ? ASP A 283 ? ILE A 278 ASP A 283 
AA3 1 LEU A 84  ? PRO A 85  ? LEU A 84  PRO A 85  
AA3 2 ILE A 101 ? GLY A 107 ? ILE A 101 GLY A 107 
AA3 3 SER A 116 ? ASN A 121 ? SER A 116 ASN A 121 
AA3 4 VAL A 126 ? TYR A 145 ? VAL A 126 TYR A 145 
AA3 5 TRP A 152 ? SER A 172 ? TRP A 152 SER A 172 
AA3 6 ARG A 237 ? SER A 247 ? ARG A 237 SER A 247 
AA3 7 GLY A 250 ? THR A 252 ? GLY A 250 THR A 252 
AA4 1 GLN B 3   ? SER B 7   ? GLN B 3   SER B 7   
AA4 2 LEU B 18  ? SER B 25  ? LEU B 18  SER B 25  
AA4 3 THR B 78  ? MET B 83  ? THR B 78  MET B 83  
AA4 4 PHE B 68  ? ASP B 73  ? PHE B 68  ASP B 73  
AA5 1 GLY B 10  ? VAL B 12  ? GLY B 10  VAL B 12  
AA5 2 MET B 34  ? GLN B 39  ? MET B 34  GLN B 39  
AA5 3 GLU B 46  ? ILE B 51  ? GLU B 46  ILE B 51  
AA5 4 LYS B 58  ? TYR B 60  ? LYS B 58  TYR B 60  
AA5 5 ALA B 92  ? ASN B 98  ? ALA B 92  ASN B 98  
AA5 6 TYR B 111 ? TRP B 112 ? TYR B 111 TRP B 112 
AA5 7 THR B 116 ? VAL B 120 ? THR B 116 VAL B 120 
AA6 1 MET C 4   ? SER C 7   ? MET C 4   SER C 7   
AA6 2 VAL C 19  ? ALA C 25  ? VAL C 19  ALA C 25  
AA6 3 ASP C 70  ? ILE C 75  ? ASP C 70  ILE C 75  
AA6 4 PHE C 62  ? SER C 67  ? PHE C 62  SER C 67  
AA7 1 SER C 10  ? SER C 12  ? SER C 10  SER C 12  
AA7 2 LEU C 33  ? GLN C 38  ? LEU C 33  GLN C 38  
AA7 3 LYS C 45  ? SER C 49  ? LYS C 45  SER C 49  
AA7 4 ASN C 53  ? MET C 54  ? ASN C 53  MET C 54  
AA7 5 THR C 85  ? GLN C 90  ? THR C 85  GLN C 90  
AA7 6 THR C 97  ? PHE C 98  ? THR C 97  PHE C 98  
AA7 7 THR C 102 ? ASP C 105 ? THR C 102 ASP C 105 
AA8 1 GLU D 6   ? SER D 7   ? GLU H 6   SER H 7   
AA8 2 LEU D 18  ? LYS D 23  ? LEU H 18  LYS H 23  
AA8 3 GLN D 79  ? MET D 84  ? GLN H 79  MET H 84  
AA8 4 LEU D 69  ? ASP D 74  ? LEU H 69  ASP H 74  
AA9 1 GLY D 35  ? GLN D 41  ? GLY H 35  GLN H 41  
AA9 2 GLU D 48  ? TYR D 54  ? GLU H 48  TYR H 54  
AA9 3 LYS D 59  ? TYR D 61  ? LYS H 59  TYR H 61  
AA9 4 ALA D 93  ? VAL D 102 ? ALA H 93  VAL H 102 
AA9 5 PRO D 109 ? TRP D 115 ? PRO H 109 TRP H 115 
AA9 6 THR D 119 ? VAL D 121 ? THR H 119 VAL H 121 
AB1 1 SER E 9   ? SER E 11  ? SER L 9   SER L 11  
AB1 2 THR E 101 ? THR E 104 ? THR L 101 THR L 104 
AB1 3 ASP E 84  ? GLN E 88  ? ASP L 84  GLN L 88  
AB1 4 SER E 33  ? GLN E 37  ? SER L 33  GLN L 37  
AB1 5 ILE E 44  ? ILE E 47  ? ILE L 44  ILE L 47  
AB2 1 ALA E 18  ? SER E 23  ? ALA L 18  SER L 23  
AB2 2 THR E 69  ? ILE E 74  ? THR L 69  ILE L 74  
AB2 3 PHE E 61  ? SER E 66  ? PHE L 61  SER L 66  
# 
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 ALA A 27  ? N ALA A 27  O TRP A 64  ? O TRP A 64  
AA1 2 3 N PHE A 65  ? N PHE A 65  O TYR A 258 ? O TYR A 258 
AA1 3 4 O TYR A 259 ? O TYR A 259 N ALA A 93  ? N ALA A 93  
AA1 4 5 N PHE A 92  ? N PHE A 92  O PHE A 192 ? O PHE A 192 
AA1 5 6 N LEU A 189 ? N LEU A 189 O THR A 208 ? O THR A 208 
AA1 6 7 N ILE A 203 ? N ILE A 203 O LEU A 226 ? O LEU A 226 
AA2 1 2 N HIS A 49  ? N HIS A 49  O LEU A 270 ? O LEU A 270 
AA2 2 3 N LYS A 271 ? N LYS A 271 O THR A 279 ? O THR A 279 
AA3 1 6 N LEU A 84  ? N LEU A 84  O PHE A 238 ? O PHE A 238 
AA3 2 3 N PHE A 106 ? N PHE A 106 O LEU A 117 ? O LEU A 117 
AA3 2 6 N GLY A 103 ? N GLY A 103 O LEU A 241 ? O LEU A 241 
AA3 3 4 N LEU A 118 ? N LEU A 118 O LYS A 129 ? O LYS A 129 
AA3 4 5 N ILE A 128 ? N ILE A 128 O TYR A 170 ? O TYR A 170 
AA3 4 6 N LEU A 141 ? N LEU A 141 O LEU A 244 ? O LEU A 244 
AA3 6 7 N HIS A 245 ? N HIS A 245 O THR A 252 ? O THR A 252 
AA4 1 2 N VAL B 5   ? N VAL B 5   O ALA B 23  ? O ALA B 23  
AA4 2 3 N LEU B 20  ? N LEU B 20  O LEU B 81  ? O LEU B 81  
AA4 3 4 O TYR B 80  ? O TYR B 80  N SER B 71  ? N SER B 71  
AA5 1 7 N VAL B 12  ? N VAL B 12  O THR B 119 ? O THR B 119 
AA5 2 3 N ARG B 38  ? N ARG B 38  O GLU B 46  ? O GLU B 46  
AA5 2 5 N VAL B 37  ? N VAL B 37  O TYR B 95  ? O TYR B 95  
AA5 3 4 N PHE B 50  ? N PHE B 50  O TYR B 59  ? O TYR B 59  
AA5 5 6 N ASN B 98  ? N ASN B 98  O TYR B 111 ? O TYR B 111 
AA5 5 7 N TYR B 94  ? N TYR B 94  O THR B 116 ? O THR B 116 
AA6 1 2 N THR C 5   ? N THR C 5   O GLN C 24  ? O GLN C 24  
AA6 2 3 N CYS C 23  ? N CYS C 23  O PHE C 71  ? O PHE C 71  
AA6 3 4 O THR C 72  ? O THR C 72  N SER C 65  ? N SER C 65  
AA7 1 7 N LEU C 11  ? N LEU C 11  O ASP C 105 ? O ASP C 105 
AA7 2 3 N TRP C 35  ? N TRP C 35  O ILE C 48  ? O ILE C 48  
AA7 2 5 N ASN C 34  ? N ASN C 34  O GLN C 89  ? O GLN C 89  
AA7 3 4 N SER C 49  ? N SER C 49  O ASN C 53  ? O ASN C 53  
AA7 5 6 N GLN C 90  ? N GLN C 90  O THR C 97  ? O THR C 97  
AA7 5 7 N TYR C 86  ? N TYR C 86  O THR C 102 ? O THR C 102 
AA8 1 2 N SER D 7   ? N SER H 7   O THR D 21  ? O THR H 21  
AA8 2 3 N CYS D 22  ? N CYS H 22  O VAL D 80  ? O VAL H 80  
AA8 3 4 O GLN D 79  ? O GLN H 79  N ASP D 74  ? N ASP H 74  
AA9 1 2 N TRP D 38  ? N TRP H 38  O ALA D 51  ? O ALA H 51  
AA9 1 4 N ILE D 39  ? N ILE H 39  O TYR D 96  ? O TYR H 96  
AA9 2 3 N LEU D 52  ? N LEU H 52  O LEU D 60  ? O LEU H 60  
AA9 4 5 N HIS D 99  ? N HIS H 99  O VAL D 114 ? O VAL H 114 
AA9 4 6 N TYR D 95  ? N TYR H 95  O THR D 119 ? O THR H 119 
AB1 1 2 N VAL E 10  ? N VAL L 10  O THR E 104 ? O THR L 104 
AB1 2 3 O THR E 101 ? O THR L 101 N TYR E 85  ? N TYR L 85  
AB1 3 4 O ASP E 84  ? O ASP L 84  N GLN E 37  ? N GLN L 37  
AB1 4 5 N TRP E 34  ? N TRP L 34  O ILE E 47  ? O ILE L 47  
AB2 1 2 N ILE E 20  ? N ILE L 20  O LEU E 72  ? O LEU L 72  
AB2 2 3 O THR E 73  ? O THR L 73  N SER E 62  ? N SER L 62  
# 
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 PHE A 32  ? ? 50.03   -117.43 
2  1 ASN A 87  ? ? 52.21   -125.11 
3  1 THR A 108 ? ? -117.36 -82.57  
4  1 ASN A 122 ? ? -129.23 -164.61 
5  1 ASP A 138 ? ? -151.71 79.59   
6  1 ARG A 214 ? ? -150.72 56.47   
7  1 ARG C 30  ? ? 46.95   -114.65 
8  1 TYR C 32  ? ? -107.61 71.51   
9  1 ALA C 51  ? ? 73.69   -55.64  
10 1 LEU H 50  ? ? -102.05 -63.51  
11 1 ASP H 110 ? ? -123.87 -82.26  
12 1 ASP L 50  ? ? 73.76   -58.57  
# 
_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 
# 
_pdbx_entry_details.entry_id                 8VYF 
_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.id                1 
_em_3d_fitting.entry_id          8VYF 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    8VYF 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.2 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               95557 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            8 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 
'SARS-CoV-2 S C.37 (Lambda variant) plus S309, S2L20, and S2X303 Fabs. Local refinement of NTD with S2L20 and S2X303 Fabs.' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       '1, 2, 3, 4, 5' 
# 
_em_imaging.entry_id                        8VYF 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             2000 
_em_imaging.nominal_defocus_max             30000 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              8VYF 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                8VYF 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1    1 Y 1 A MET 1    ? A MET 1    
2    1 Y 1 A PHE 2    ? A PHE 2    
3    1 Y 1 A VAL 3    ? A VAL 3    
4    1 Y 1 A PHE 4    ? A PHE 4    
5    1 Y 1 A LEU 5    ? A LEU 5    
6    1 Y 1 A VAL 6    ? A VAL 6    
7    1 Y 1 A LEU 7    ? A LEU 7    
8    1 Y 1 A LEU 8    ? A LEU 8    
9    1 Y 1 A PRO 9    ? A PRO 9    
10   1 Y 1 A LEU 10   ? A LEU 10   
11   1 Y 1 A VAL 11   ? A VAL 11   
12   1 Y 1 A SER 12   ? A SER 12   
13   1 Y 1 A SER 13   ? A SER 13   
14   1 Y 1 A THR 19   ? A THR 19   
15   1 Y 1 A THR 20   ? A THR 20   
16   1 Y 1 A VAL 70   ? A VAL 70   
17   1 Y 1 A SER 71   ? A SER 71   
18   1 Y 1 A GLY 72   ? A GLY 72   
19   1 Y 1 A THR 73   ? A THR 73   
20   1 Y 1 A ASN 74   ? A ASN 74   
21   1 Y 1 A VAL 75   ? A VAL 75   
22   1 Y 1 A ILE 76   ? A ILE 76   
23   1 Y 1 A LYS 77   ? A LYS 77   
24   1 Y 1 A ARG 78   ? A ARG 78   
25   1 Y 1 A MET 177  ? A MET 177  
26   1 Y 1 A ASP 178  ? A ASP 178  
27   1 Y 1 A LEU 179  ? A LEU 179  
28   1 Y 1 A GLU 180  ? A GLU 180  
29   1 Y 1 A GLY 181  ? A GLY 181  
30   1 Y 1 A LYS 182  ? A LYS 182  
31   1 Y 1 A GLN 183  ? A GLN 183  
32   1 Y 1 A GLY 184  ? A GLY 184  
33   1 Y 1 A ASN 185  ? A ASN 185  
34   1 Y 1 A PHE 299  ? A PHE 299  
35   1 Y 1 A THR 300  ? A THR 300  
36   1 Y 1 A VAL 301  ? A VAL 301  
37   1 Y 1 A GLU 302  ? A GLU 302  
38   1 Y 1 A LYS 303  ? A LYS 303  
39   1 Y 1 A GLY 304  ? A GLY 304  
40   1 Y 1 A ILE 305  ? A ILE 305  
41   1 Y 1 A TYR 306  ? A TYR 306  
42   1 Y 1 A GLN 307  ? A GLN 307  
43   1 Y 1 A THR 308  ? A THR 308  
44   1 Y 1 A SER 309  ? A SER 309  
45   1 Y 1 A ASN 310  ? A ASN 310  
46   1 Y 1 A PHE 311  ? A PHE 311  
47   1 Y 1 A ARG 312  ? A ARG 312  
48   1 Y 1 A VAL 313  ? A VAL 313  
49   1 Y 1 A GLN 314  ? A GLN 314  
50   1 Y 1 A PRO 315  ? A PRO 315  
51   1 Y 1 A THR 316  ? A THR 316  
52   1 Y 1 A GLU 317  ? A GLU 317  
53   1 Y 1 A SER 318  ? A SER 318  
54   1 Y 1 A ILE 319  ? A ILE 319  
55   1 Y 1 A VAL 320  ? A VAL 320  
56   1 Y 1 A ARG 321  ? A ARG 321  
57   1 Y 1 A PHE 322  ? A PHE 322  
58   1 Y 1 A PRO 323  ? A PRO 323  
59   1 Y 1 A ASN 324  ? A ASN 324  
60   1 Y 1 A ILE 325  ? A ILE 325  
61   1 Y 1 A THR 326  ? A THR 326  
62   1 Y 1 A ASN 327  ? A ASN 327  
63   1 Y 1 A LEU 328  ? A LEU 328  
64   1 Y 1 A CYS 329  ? A CYS 329  
65   1 Y 1 A PRO 330  ? A PRO 330  
66   1 Y 1 A PHE 331  ? A PHE 331  
67   1 Y 1 A GLY 332  ? A GLY 332  
68   1 Y 1 A GLU 333  ? A GLU 333  
69   1 Y 1 A VAL 334  ? A VAL 334  
70   1 Y 1 A PHE 335  ? A PHE 335  
71   1 Y 1 A ASN 336  ? A ASN 336  
72   1 Y 1 A ALA 337  ? A ALA 337  
73   1 Y 1 A THR 338  ? A THR 338  
74   1 Y 1 A ARG 339  ? A ARG 339  
75   1 Y 1 A PHE 340  ? A PHE 340  
76   1 Y 1 A ALA 341  ? A ALA 341  
77   1 Y 1 A SER 342  ? A SER 342  
78   1 Y 1 A VAL 343  ? A VAL 343  
79   1 Y 1 A TYR 344  ? A TYR 344  
80   1 Y 1 A ALA 345  ? A ALA 345  
81   1 Y 1 A TRP 346  ? A TRP 346  
82   1 Y 1 A ASN 347  ? A ASN 347  
83   1 Y 1 A ARG 348  ? A ARG 348  
84   1 Y 1 A LYS 349  ? A LYS 349  
85   1 Y 1 A ARG 350  ? A ARG 350  
86   1 Y 1 A ILE 351  ? A ILE 351  
87   1 Y 1 A SER 352  ? A SER 352  
88   1 Y 1 A ASN 353  ? A ASN 353  
89   1 Y 1 A CYS 354  ? A CYS 354  
90   1 Y 1 A VAL 355  ? A VAL 355  
91   1 Y 1 A ALA 356  ? A ALA 356  
92   1 Y 1 A ASP 357  ? A ASP 357  
93   1 Y 1 A TYR 358  ? A TYR 358  
94   1 Y 1 A SER 359  ? A SER 359  
95   1 Y 1 A VAL 360  ? A VAL 360  
96   1 Y 1 A LEU 361  ? A LEU 361  
97   1 Y 1 A TYR 362  ? A TYR 362  
98   1 Y 1 A ASN 363  ? A ASN 363  
99   1 Y 1 A SER 364  ? A SER 364  
100  1 Y 1 A ALA 365  ? A ALA 365  
101  1 Y 1 A SER 366  ? A SER 366  
102  1 Y 1 A PHE 367  ? A PHE 367  
103  1 Y 1 A SER 368  ? A SER 368  
104  1 Y 1 A THR 369  ? A THR 369  
105  1 Y 1 A PHE 370  ? A PHE 370  
106  1 Y 1 A LYS 371  ? A LYS 371  
107  1 Y 1 A CYS 372  ? A CYS 372  
108  1 Y 1 A TYR 373  ? A TYR 373  
109  1 Y 1 A GLY 374  ? A GLY 374  
110  1 Y 1 A VAL 375  ? A VAL 375  
111  1 Y 1 A CYS 376  ? A CYS 376  
112  1 Y 1 A PRO 377  ? A PRO 377  
113  1 Y 1 A THR 378  ? A THR 378  
114  1 Y 1 A LYS 379  ? A LYS 379  
115  1 Y 1 A LEU 380  ? A LEU 380  
116  1 Y 1 A ASN 381  ? A ASN 381  
117  1 Y 1 A ASP 382  ? A ASP 382  
118  1 Y 1 A LEU 383  ? A LEU 383  
119  1 Y 1 A CYS 384  ? A CYS 384  
120  1 Y 1 A PHE 385  ? A PHE 385  
121  1 Y 1 A THR 386  ? A THR 386  
122  1 Y 1 A ASN 387  ? A ASN 387  
123  1 Y 1 A VAL 388  ? A VAL 388  
124  1 Y 1 A TYR 389  ? A TYR 389  
125  1 Y 1 A ALA 390  ? A ALA 390  
126  1 Y 1 A ASP 391  ? A ASP 391  
127  1 Y 1 A SER 392  ? A SER 392  
128  1 Y 1 A PHE 393  ? A PHE 393  
129  1 Y 1 A VAL 394  ? A VAL 394  
130  1 Y 1 A ILE 395  ? A ILE 395  
131  1 Y 1 A ARG 396  ? A ARG 396  
132  1 Y 1 A GLY 397  ? A GLY 397  
133  1 Y 1 A ASP 398  ? A ASP 398  
134  1 Y 1 A GLU 399  ? A GLU 399  
135  1 Y 1 A VAL 400  ? A VAL 400  
136  1 Y 1 A ARG 401  ? A ARG 401  
137  1 Y 1 A GLN 402  ? A GLN 402  
138  1 Y 1 A ILE 403  ? A ILE 403  
139  1 Y 1 A ALA 404  ? A ALA 404  
140  1 Y 1 A PRO 405  ? A PRO 405  
141  1 Y 1 A GLY 406  ? A GLY 406  
142  1 Y 1 A GLN 407  ? A GLN 407  
143  1 Y 1 A THR 408  ? A THR 408  
144  1 Y 1 A GLY 409  ? A GLY 409  
145  1 Y 1 A LYS 410  ? A LYS 410  
146  1 Y 1 A ILE 411  ? A ILE 411  
147  1 Y 1 A ALA 412  ? A ALA 412  
148  1 Y 1 A ASP 413  ? A ASP 413  
149  1 Y 1 A TYR 414  ? A TYR 414  
150  1 Y 1 A ASN 415  ? A ASN 415  
151  1 Y 1 A TYR 416  ? A TYR 416  
152  1 Y 1 A LYS 417  ? A LYS 417  
153  1 Y 1 A LEU 418  ? A LEU 418  
154  1 Y 1 A PRO 419  ? A PRO 419  
155  1 Y 1 A ASP 420  ? A ASP 420  
156  1 Y 1 A ASP 421  ? A ASP 421  
157  1 Y 1 A PHE 422  ? A PHE 422  
158  1 Y 1 A THR 423  ? A THR 423  
159  1 Y 1 A GLY 424  ? A GLY 424  
160  1 Y 1 A CYS 425  ? A CYS 425  
161  1 Y 1 A VAL 426  ? A VAL 426  
162  1 Y 1 A ILE 427  ? A ILE 427  
163  1 Y 1 A ALA 428  ? A ALA 428  
164  1 Y 1 A TRP 429  ? A TRP 429  
165  1 Y 1 A ASN 430  ? A ASN 430  
166  1 Y 1 A SER 431  ? A SER 431  
167  1 Y 1 A ASN 432  ? A ASN 432  
168  1 Y 1 A ASN 433  ? A ASN 433  
169  1 Y 1 A LEU 434  ? A LEU 434  
170  1 Y 1 A ASP 435  ? A ASP 435  
171  1 Y 1 A SER 436  ? A SER 436  
172  1 Y 1 A LYS 437  ? A LYS 437  
173  1 Y 1 A VAL 438  ? A VAL 438  
174  1 Y 1 A GLY 439  ? A GLY 439  
175  1 Y 1 A GLY 440  ? A GLY 440  
176  1 Y 1 A ASN 441  ? A ASN 441  
177  1 Y 1 A TYR 442  ? A TYR 442  
178  1 Y 1 A ASN 443  ? A ASN 443  
179  1 Y 1 A TYR 444  ? A TYR 444  
180  1 Y 1 A GLN 445  ? A GLN 445  
181  1 Y 1 A TYR 446  ? A TYR 446  
182  1 Y 1 A ARG 447  ? A ARG 447  
183  1 Y 1 A LEU 448  ? A LEU 448  
184  1 Y 1 A PHE 449  ? A PHE 449  
185  1 Y 1 A ARG 450  ? A ARG 450  
186  1 Y 1 A LYS 451  ? A LYS 451  
187  1 Y 1 A SER 452  ? A SER 452  
188  1 Y 1 A ASN 453  ? A ASN 453  
189  1 Y 1 A LEU 454  ? A LEU 454  
190  1 Y 1 A LYS 455  ? A LYS 455  
191  1 Y 1 A PRO 456  ? A PRO 456  
192  1 Y 1 A PHE 457  ? A PHE 457  
193  1 Y 1 A GLU 458  ? A GLU 458  
194  1 Y 1 A ARG 459  ? A ARG 459  
195  1 Y 1 A ASP 460  ? A ASP 460  
196  1 Y 1 A ILE 461  ? A ILE 461  
197  1 Y 1 A SER 462  ? A SER 462  
198  1 Y 1 A THR 463  ? A THR 463  
199  1 Y 1 A GLU 464  ? A GLU 464  
200  1 Y 1 A ILE 465  ? A ILE 465  
201  1 Y 1 A TYR 466  ? A TYR 466  
202  1 Y 1 A GLN 467  ? A GLN 467  
203  1 Y 1 A ALA 468  ? A ALA 468  
204  1 Y 1 A GLY 469  ? A GLY 469  
205  1 Y 1 A SER 470  ? A SER 470  
206  1 Y 1 A THR 471  ? A THR 471  
207  1 Y 1 A PRO 472  ? A PRO 472  
208  1 Y 1 A CYS 473  ? A CYS 473  
209  1 Y 1 A ASN 474  ? A ASN 474  
210  1 Y 1 A GLY 475  ? A GLY 475  
211  1 Y 1 A VAL 476  ? A VAL 476  
212  1 Y 1 A GLU 477  ? A GLU 477  
213  1 Y 1 A GLY 478  ? A GLY 478  
214  1 Y 1 A PHE 479  ? A PHE 479  
215  1 Y 1 A ASN 480  ? A ASN 480  
216  1 Y 1 A CYS 481  ? A CYS 481  
217  1 Y 1 A TYR 482  ? A TYR 482  
218  1 Y 1 A SER 483  ? A SER 483  
219  1 Y 1 A PRO 484  ? A PRO 484  
220  1 Y 1 A LEU 485  ? A LEU 485  
221  1 Y 1 A GLN 486  ? A GLN 486  
222  1 Y 1 A SER 487  ? A SER 487  
223  1 Y 1 A TYR 488  ? A TYR 488  
224  1 Y 1 A GLY 489  ? A GLY 489  
225  1 Y 1 A PHE 490  ? A PHE 490  
226  1 Y 1 A GLN 491  ? A GLN 491  
227  1 Y 1 A PRO 492  ? A PRO 492  
228  1 Y 1 A THR 493  ? A THR 493  
229  1 Y 1 A ASN 494  ? A ASN 494  
230  1 Y 1 A GLY 495  ? A GLY 495  
231  1 Y 1 A VAL 496  ? A VAL 496  
232  1 Y 1 A GLY 497  ? A GLY 497  
233  1 Y 1 A TYR 498  ? A TYR 498  
234  1 Y 1 A GLN 499  ? A GLN 499  
235  1 Y 1 A PRO 500  ? A PRO 500  
236  1 Y 1 A TYR 501  ? A TYR 501  
237  1 Y 1 A ARG 502  ? A ARG 502  
238  1 Y 1 A VAL 503  ? A VAL 503  
239  1 Y 1 A VAL 504  ? A VAL 504  
240  1 Y 1 A VAL 505  ? A VAL 505  
241  1 Y 1 A LEU 506  ? A LEU 506  
242  1 Y 1 A SER 507  ? A SER 507  
243  1 Y 1 A PHE 508  ? A PHE 508  
244  1 Y 1 A GLU 509  ? A GLU 509  
245  1 Y 1 A LEU 510  ? A LEU 510  
246  1 Y 1 A LEU 511  ? A LEU 511  
247  1 Y 1 A HIS 512  ? A HIS 512  
248  1 Y 1 A ALA 513  ? A ALA 513  
249  1 Y 1 A PRO 514  ? A PRO 514  
250  1 Y 1 A ALA 515  ? A ALA 515  
251  1 Y 1 A THR 516  ? A THR 516  
252  1 Y 1 A VAL 517  ? A VAL 517  
253  1 Y 1 A CYS 518  ? A CYS 518  
254  1 Y 1 A GLY 519  ? A GLY 519  
255  1 Y 1 A PRO 520  ? A PRO 520  
256  1 Y 1 A LYS 521  ? A LYS 521  
257  1 Y 1 A LYS 522  ? A LYS 522  
258  1 Y 1 A SER 523  ? A SER 523  
259  1 Y 1 A THR 524  ? A THR 524  
260  1 Y 1 A ASN 525  ? A ASN 525  
261  1 Y 1 A LEU 526  ? A LEU 526  
262  1 Y 1 A VAL 527  ? A VAL 527  
263  1 Y 1 A LYS 528  ? A LYS 528  
264  1 Y 1 A ASN 529  ? A ASN 529  
265  1 Y 1 A LYS 530  ? A LYS 530  
266  1 Y 1 A CYS 531  ? A CYS 531  
267  1 Y 1 A VAL 532  ? A VAL 532  
268  1 Y 1 A ASN 533  ? A ASN 533  
269  1 Y 1 A PHE 534  ? A PHE 534  
270  1 Y 1 A ASN 535  ? A ASN 535  
271  1 Y 1 A PHE 536  ? A PHE 536  
272  1 Y 1 A ASN 537  ? A ASN 537  
273  1 Y 1 A GLY 538  ? A GLY 538  
274  1 Y 1 A LEU 539  ? A LEU 539  
275  1 Y 1 A THR 540  ? A THR 540  
276  1 Y 1 A GLY 541  ? A GLY 541  
277  1 Y 1 A THR 542  ? A THR 542  
278  1 Y 1 A GLY 543  ? A GLY 543  
279  1 Y 1 A VAL 544  ? A VAL 544  
280  1 Y 1 A LEU 545  ? A LEU 545  
281  1 Y 1 A THR 546  ? A THR 546  
282  1 Y 1 A GLU 547  ? A GLU 547  
283  1 Y 1 A SER 548  ? A SER 548  
284  1 Y 1 A ASN 549  ? A ASN 549  
285  1 Y 1 A LYS 550  ? A LYS 550  
286  1 Y 1 A LYS 551  ? A LYS 551  
287  1 Y 1 A PHE 552  ? A PHE 552  
288  1 Y 1 A LEU 553  ? A LEU 553  
289  1 Y 1 A PRO 554  ? A PRO 554  
290  1 Y 1 A PHE 555  ? A PHE 555  
291  1 Y 1 A GLN 556  ? A GLN 556  
292  1 Y 1 A GLN 557  ? A GLN 557  
293  1 Y 1 A PHE 558  ? A PHE 558  
294  1 Y 1 A GLY 559  ? A GLY 559  
295  1 Y 1 A ARG 560  ? A ARG 560  
296  1 Y 1 A ASP 561  ? A ASP 561  
297  1 Y 1 A ILE 562  ? A ILE 562  
298  1 Y 1 A ALA 563  ? A ALA 563  
299  1 Y 1 A ASP 564  ? A ASP 564  
300  1 Y 1 A THR 565  ? A THR 565  
301  1 Y 1 A THR 566  ? A THR 566  
302  1 Y 1 A ASP 567  ? A ASP 567  
303  1 Y 1 A ALA 568  ? A ALA 568  
304  1 Y 1 A VAL 569  ? A VAL 569  
305  1 Y 1 A ARG 570  ? A ARG 570  
306  1 Y 1 A ASP 571  ? A ASP 571  
307  1 Y 1 A PRO 572  ? A PRO 572  
308  1 Y 1 A GLN 573  ? A GLN 573  
309  1 Y 1 A THR 574  ? A THR 574  
310  1 Y 1 A LEU 575  ? A LEU 575  
311  1 Y 1 A GLU 576  ? A GLU 576  
312  1 Y 1 A ILE 577  ? A ILE 577  
313  1 Y 1 A LEU 578  ? A LEU 578  
314  1 Y 1 A ASP 579  ? A ASP 579  
315  1 Y 1 A ILE 580  ? A ILE 580  
316  1 Y 1 A THR 581  ? A THR 581  
317  1 Y 1 A PRO 582  ? A PRO 582  
318  1 Y 1 A CYS 583  ? A CYS 583  
319  1 Y 1 A SER 584  ? A SER 584  
320  1 Y 1 A PHE 585  ? A PHE 585  
321  1 Y 1 A GLY 586  ? A GLY 586  
322  1 Y 1 A GLY 587  ? A GLY 587  
323  1 Y 1 A VAL 588  ? A VAL 588  
324  1 Y 1 A SER 589  ? A SER 589  
325  1 Y 1 A VAL 590  ? A VAL 590  
326  1 Y 1 A ILE 591  ? A ILE 591  
327  1 Y 1 A THR 592  ? A THR 592  
328  1 Y 1 A PRO 593  ? A PRO 593  
329  1 Y 1 A GLY 594  ? A GLY 594  
330  1 Y 1 A THR 595  ? A THR 595  
331  1 Y 1 A ASN 596  ? A ASN 596  
332  1 Y 1 A THR 597  ? A THR 597  
333  1 Y 1 A SER 598  ? A SER 598  
334  1 Y 1 A ASN 599  ? A ASN 599  
335  1 Y 1 A GLN 600  ? A GLN 600  
336  1 Y 1 A VAL 601  ? A VAL 601  
337  1 Y 1 A ALA 602  ? A ALA 602  
338  1 Y 1 A VAL 603  ? A VAL 603  
339  1 Y 1 A LEU 604  ? A LEU 604  
340  1 Y 1 A TYR 605  ? A TYR 605  
341  1 Y 1 A GLN 606  ? A GLN 606  
342  1 Y 1 A GLY 607  ? A GLY 607  
343  1 Y 1 A VAL 608  ? A VAL 608  
344  1 Y 1 A ASN 609  ? A ASN 609  
345  1 Y 1 A CYS 610  ? A CYS 610  
346  1 Y 1 A THR 611  ? A THR 611  
347  1 Y 1 A GLU 612  ? A GLU 612  
348  1 Y 1 A VAL 613  ? A VAL 613  
349  1 Y 1 A PRO 614  ? A PRO 614  
350  1 Y 1 A VAL 615  ? A VAL 615  
351  1 Y 1 A ALA 616  ? A ALA 616  
352  1 Y 1 A ILE 617  ? A ILE 617  
353  1 Y 1 A HIS 618  ? A HIS 618  
354  1 Y 1 A ALA 619  ? A ALA 619  
355  1 Y 1 A ASP 620  ? A ASP 620  
356  1 Y 1 A GLN 621  ? A GLN 621  
357  1 Y 1 A LEU 622  ? A LEU 622  
358  1 Y 1 A THR 623  ? A THR 623  
359  1 Y 1 A PRO 624  ? A PRO 624  
360  1 Y 1 A THR 625  ? A THR 625  
361  1 Y 1 A TRP 626  ? A TRP 626  
362  1 Y 1 A ARG 627  ? A ARG 627  
363  1 Y 1 A VAL 628  ? A VAL 628  
364  1 Y 1 A TYR 629  ? A TYR 629  
365  1 Y 1 A SER 630  ? A SER 630  
366  1 Y 1 A THR 631  ? A THR 631  
367  1 Y 1 A GLY 632  ? A GLY 632  
368  1 Y 1 A SER 633  ? A SER 633  
369  1 Y 1 A ASN 634  ? A ASN 634  
370  1 Y 1 A VAL 635  ? A VAL 635  
371  1 Y 1 A PHE 636  ? A PHE 636  
372  1 Y 1 A GLN 637  ? A GLN 637  
373  1 Y 1 A THR 638  ? A THR 638  
374  1 Y 1 A ARG 639  ? A ARG 639  
375  1 Y 1 A ALA 640  ? A ALA 640  
376  1 Y 1 A GLY 641  ? A GLY 641  
377  1 Y 1 A CYS 642  ? A CYS 642  
378  1 Y 1 A LEU 643  ? A LEU 643  
379  1 Y 1 A ILE 644  ? A ILE 644  
380  1 Y 1 A GLY 645  ? A GLY 645  
381  1 Y 1 A ALA 646  ? A ALA 646  
382  1 Y 1 A GLU 647  ? A GLU 647  
383  1 Y 1 A HIS 648  ? A HIS 648  
384  1 Y 1 A VAL 649  ? A VAL 649  
385  1 Y 1 A ASN 650  ? A ASN 650  
386  1 Y 1 A ASN 651  ? A ASN 651  
387  1 Y 1 A SER 652  ? A SER 652  
388  1 Y 1 A TYR 653  ? A TYR 653  
389  1 Y 1 A GLU 654  ? A GLU 654  
390  1 Y 1 A CYS 655  ? A CYS 655  
391  1 Y 1 A ASP 656  ? A ASP 656  
392  1 Y 1 A ILE 657  ? A ILE 657  
393  1 Y 1 A PRO 658  ? A PRO 658  
394  1 Y 1 A ILE 659  ? A ILE 659  
395  1 Y 1 A GLY 660  ? A GLY 660  
396  1 Y 1 A ALA 661  ? A ALA 661  
397  1 Y 1 A GLY 662  ? A GLY 662  
398  1 Y 1 A ILE 663  ? A ILE 663  
399  1 Y 1 A CYS 664  ? A CYS 664  
400  1 Y 1 A ALA 665  ? A ALA 665  
401  1 Y 1 A SER 666  ? A SER 666  
402  1 Y 1 A TYR 667  ? A TYR 667  
403  1 Y 1 A GLN 668  ? A GLN 668  
404  1 Y 1 A THR 669  ? A THR 669  
405  1 Y 1 A GLN 670  ? A GLN 670  
406  1 Y 1 A THR 671  ? A THR 671  
407  1 Y 1 A ASN 672  ? A ASN 672  
408  1 Y 1 A SER 673  ? A SER 673  
409  1 Y 1 A PRO 674  ? A PRO 674  
410  1 Y 1 A ARG 675  ? A ARG 675  
411  1 Y 1 A ARG 676  ? A ARG 676  
412  1 Y 1 A ALA 677  ? A ALA 677  
413  1 Y 1 A ARG 678  ? A ARG 678  
414  1 Y 1 A SER 679  ? A SER 679  
415  1 Y 1 A VAL 680  ? A VAL 680  
416  1 Y 1 A ALA 681  ? A ALA 681  
417  1 Y 1 A SER 682  ? A SER 682  
418  1 Y 1 A GLN 683  ? A GLN 683  
419  1 Y 1 A SER 684  ? A SER 684  
420  1 Y 1 A ILE 685  ? A ILE 685  
421  1 Y 1 A ILE 686  ? A ILE 686  
422  1 Y 1 A ALA 687  ? A ALA 687  
423  1 Y 1 A TYR 688  ? A TYR 688  
424  1 Y 1 A THR 689  ? A THR 689  
425  1 Y 1 A MET 690  ? A MET 690  
426  1 Y 1 A SER 691  ? A SER 691  
427  1 Y 1 A LEU 692  ? A LEU 692  
428  1 Y 1 A GLY 693  ? A GLY 693  
429  1 Y 1 A ALA 694  ? A ALA 694  
430  1 Y 1 A GLU 695  ? A GLU 695  
431  1 Y 1 A ASN 696  ? A ASN 696  
432  1 Y 1 A SER 697  ? A SER 697  
433  1 Y 1 A VAL 698  ? A VAL 698  
434  1 Y 1 A ALA 699  ? A ALA 699  
435  1 Y 1 A TYR 700  ? A TYR 700  
436  1 Y 1 A SER 701  ? A SER 701  
437  1 Y 1 A ASN 702  ? A ASN 702  
438  1 Y 1 A ASN 703  ? A ASN 703  
439  1 Y 1 A SER 704  ? A SER 704  
440  1 Y 1 A ILE 705  ? A ILE 705  
441  1 Y 1 A ALA 706  ? A ALA 706  
442  1 Y 1 A ILE 707  ? A ILE 707  
443  1 Y 1 A PRO 708  ? A PRO 708  
444  1 Y 1 A THR 709  ? A THR 709  
445  1 Y 1 A ASN 710  ? A ASN 710  
446  1 Y 1 A PHE 711  ? A PHE 711  
447  1 Y 1 A THR 712  ? A THR 712  
448  1 Y 1 A ILE 713  ? A ILE 713  
449  1 Y 1 A SER 714  ? A SER 714  
450  1 Y 1 A VAL 715  ? A VAL 715  
451  1 Y 1 A THR 716  ? A THR 716  
452  1 Y 1 A THR 717  ? A THR 717  
453  1 Y 1 A GLU 718  ? A GLU 718  
454  1 Y 1 A ILE 719  ? A ILE 719  
455  1 Y 1 A LEU 720  ? A LEU 720  
456  1 Y 1 A PRO 721  ? A PRO 721  
457  1 Y 1 A VAL 722  ? A VAL 722  
458  1 Y 1 A SER 723  ? A SER 723  
459  1 Y 1 A MET 724  ? A MET 724  
460  1 Y 1 A THR 725  ? A THR 725  
461  1 Y 1 A LYS 726  ? A LYS 726  
462  1 Y 1 A THR 727  ? A THR 727  
463  1 Y 1 A SER 728  ? A SER 728  
464  1 Y 1 A VAL 729  ? A VAL 729  
465  1 Y 1 A ASP 730  ? A ASP 730  
466  1 Y 1 A CYS 731  ? A CYS 731  
467  1 Y 1 A THR 732  ? A THR 732  
468  1 Y 1 A MET 733  ? A MET 733  
469  1 Y 1 A TYR 734  ? A TYR 734  
470  1 Y 1 A ILE 735  ? A ILE 735  
471  1 Y 1 A CYS 736  ? A CYS 736  
472  1 Y 1 A GLY 737  ? A GLY 737  
473  1 Y 1 A ASP 738  ? A ASP 738  
474  1 Y 1 A SER 739  ? A SER 739  
475  1 Y 1 A THR 740  ? A THR 740  
476  1 Y 1 A GLU 741  ? A GLU 741  
477  1 Y 1 A CYS 742  ? A CYS 742  
478  1 Y 1 A SER 743  ? A SER 743  
479  1 Y 1 A ASN 744  ? A ASN 744  
480  1 Y 1 A LEU 745  ? A LEU 745  
481  1 Y 1 A LEU 746  ? A LEU 746  
482  1 Y 1 A LEU 747  ? A LEU 747  
483  1 Y 1 A GLN 748  ? A GLN 748  
484  1 Y 1 A TYR 749  ? A TYR 749  
485  1 Y 1 A GLY 750  ? A GLY 750  
486  1 Y 1 A SER 751  ? A SER 751  
487  1 Y 1 A PHE 752  ? A PHE 752  
488  1 Y 1 A CYS 753  ? A CYS 753  
489  1 Y 1 A THR 754  ? A THR 754  
490  1 Y 1 A GLN 755  ? A GLN 755  
491  1 Y 1 A LEU 756  ? A LEU 756  
492  1 Y 1 A ASN 757  ? A ASN 757  
493  1 Y 1 A ARG 758  ? A ARG 758  
494  1 Y 1 A ALA 759  ? A ALA 759  
495  1 Y 1 A LEU 760  ? A LEU 760  
496  1 Y 1 A THR 761  ? A THR 761  
497  1 Y 1 A GLY 762  ? A GLY 762  
498  1 Y 1 A ILE 763  ? A ILE 763  
499  1 Y 1 A ALA 764  ? A ALA 764  
500  1 Y 1 A VAL 765  ? A VAL 765  
501  1 Y 1 A GLU 766  ? A GLU 766  
502  1 Y 1 A GLN 767  ? A GLN 767  
503  1 Y 1 A ASP 768  ? A ASP 768  
504  1 Y 1 A LYS 769  ? A LYS 769  
505  1 Y 1 A ASN 770  ? A ASN 770  
506  1 Y 1 A THR 771  ? A THR 771  
507  1 Y 1 A GLN 772  ? A GLN 772  
508  1 Y 1 A GLU 773  ? A GLU 773  
509  1 Y 1 A VAL 774  ? A VAL 774  
510  1 Y 1 A PHE 775  ? A PHE 775  
511  1 Y 1 A ALA 776  ? A ALA 776  
512  1 Y 1 A GLN 777  ? A GLN 777  
513  1 Y 1 A VAL 778  ? A VAL 778  
514  1 Y 1 A LYS 779  ? A LYS 779  
515  1 Y 1 A GLN 780  ? A GLN 780  
516  1 Y 1 A ILE 781  ? A ILE 781  
517  1 Y 1 A TYR 782  ? A TYR 782  
518  1 Y 1 A LYS 783  ? A LYS 783  
519  1 Y 1 A THR 784  ? A THR 784  
520  1 Y 1 A PRO 785  ? A PRO 785  
521  1 Y 1 A PRO 786  ? A PRO 786  
522  1 Y 1 A ILE 787  ? A ILE 787  
523  1 Y 1 A LYS 788  ? A LYS 788  
524  1 Y 1 A ASP 789  ? A ASP 789  
525  1 Y 1 A PHE 790  ? A PHE 790  
526  1 Y 1 A GLY 791  ? A GLY 791  
527  1 Y 1 A GLY 792  ? A GLY 792  
528  1 Y 1 A PHE 793  ? A PHE 793  
529  1 Y 1 A ASN 794  ? A ASN 794  
530  1 Y 1 A PHE 795  ? A PHE 795  
531  1 Y 1 A SER 796  ? A SER 796  
532  1 Y 1 A GLN 797  ? A GLN 797  
533  1 Y 1 A ILE 798  ? A ILE 798  
534  1 Y 1 A LEU 799  ? A LEU 799  
535  1 Y 1 A PRO 800  ? A PRO 800  
536  1 Y 1 A ASP 801  ? A ASP 801  
537  1 Y 1 A PRO 802  ? A PRO 802  
538  1 Y 1 A SER 803  ? A SER 803  
539  1 Y 1 A LYS 804  ? A LYS 804  
540  1 Y 1 A PRO 805  ? A PRO 805  
541  1 Y 1 A SER 806  ? A SER 806  
542  1 Y 1 A LYS 807  ? A LYS 807  
543  1 Y 1 A ARG 808  ? A ARG 808  
544  1 Y 1 A SER 809  ? A SER 809  
545  1 Y 1 A PRO 810  ? A PRO 810  
546  1 Y 1 A ILE 811  ? A ILE 811  
547  1 Y 1 A GLU 812  ? A GLU 812  
548  1 Y 1 A ASP 813  ? A ASP 813  
549  1 Y 1 A LEU 814  ? A LEU 814  
550  1 Y 1 A LEU 815  ? A LEU 815  
551  1 Y 1 A PHE 816  ? A PHE 816  
552  1 Y 1 A ASN 817  ? A ASN 817  
553  1 Y 1 A LYS 818  ? A LYS 818  
554  1 Y 1 A VAL 819  ? A VAL 819  
555  1 Y 1 A THR 820  ? A THR 820  
556  1 Y 1 A LEU 821  ? A LEU 821  
557  1 Y 1 A ALA 822  ? A ALA 822  
558  1 Y 1 A ASP 823  ? A ASP 823  
559  1 Y 1 A ALA 824  ? A ALA 824  
560  1 Y 1 A GLY 825  ? A GLY 825  
561  1 Y 1 A PHE 826  ? A PHE 826  
562  1 Y 1 A ILE 827  ? A ILE 827  
563  1 Y 1 A LYS 828  ? A LYS 828  
564  1 Y 1 A GLN 829  ? A GLN 829  
565  1 Y 1 A TYR 830  ? A TYR 830  
566  1 Y 1 A GLY 831  ? A GLY 831  
567  1 Y 1 A ASP 832  ? A ASP 832  
568  1 Y 1 A CYS 833  ? A CYS 833  
569  1 Y 1 A LEU 834  ? A LEU 834  
570  1 Y 1 A GLY 835  ? A GLY 835  
571  1 Y 1 A ASP 836  ? A ASP 836  
572  1 Y 1 A ILE 837  ? A ILE 837  
573  1 Y 1 A ALA 838  ? A ALA 838  
574  1 Y 1 A ALA 839  ? A ALA 839  
575  1 Y 1 A ARG 840  ? A ARG 840  
576  1 Y 1 A ASP 841  ? A ASP 841  
577  1 Y 1 A LEU 842  ? A LEU 842  
578  1 Y 1 A ILE 843  ? A ILE 843  
579  1 Y 1 A CYS 844  ? A CYS 844  
580  1 Y 1 A ALA 845  ? A ALA 845  
581  1 Y 1 A GLN 846  ? A GLN 846  
582  1 Y 1 A LYS 847  ? A LYS 847  
583  1 Y 1 A PHE 848  ? A PHE 848  
584  1 Y 1 A ASN 849  ? A ASN 849  
585  1 Y 1 A GLY 850  ? A GLY 850  
586  1 Y 1 A LEU 851  ? A LEU 851  
587  1 Y 1 A ASN 852  ? A ASN 852  
588  1 Y 1 A VAL 853  ? A VAL 853  
589  1 Y 1 A LEU 854  ? A LEU 854  
590  1 Y 1 A PRO 855  ? A PRO 855  
591  1 Y 1 A PRO 856  ? A PRO 856  
592  1 Y 1 A LEU 857  ? A LEU 857  
593  1 Y 1 A LEU 858  ? A LEU 858  
594  1 Y 1 A THR 859  ? A THR 859  
595  1 Y 1 A ASP 860  ? A ASP 860  
596  1 Y 1 A GLU 861  ? A GLU 861  
597  1 Y 1 A MET 862  ? A MET 862  
598  1 Y 1 A ILE 863  ? A ILE 863  
599  1 Y 1 A ALA 864  ? A ALA 864  
600  1 Y 1 A GLN 865  ? A GLN 865  
601  1 Y 1 A TYR 866  ? A TYR 866  
602  1 Y 1 A THR 867  ? A THR 867  
603  1 Y 1 A SER 868  ? A SER 868  
604  1 Y 1 A ALA 869  ? A ALA 869  
605  1 Y 1 A LEU 870  ? A LEU 870  
606  1 Y 1 A LEU 871  ? A LEU 871  
607  1 Y 1 A ALA 872  ? A ALA 872  
608  1 Y 1 A GLY 873  ? A GLY 873  
609  1 Y 1 A THR 874  ? A THR 874  
610  1 Y 1 A ILE 875  ? A ILE 875  
611  1 Y 1 A THR 876  ? A THR 876  
612  1 Y 1 A SER 877  ? A SER 877  
613  1 Y 1 A GLY 878  ? A GLY 878  
614  1 Y 1 A TRP 879  ? A TRP 879  
615  1 Y 1 A THR 880  ? A THR 880  
616  1 Y 1 A PHE 881  ? A PHE 881  
617  1 Y 1 A GLY 882  ? A GLY 882  
618  1 Y 1 A ALA 883  ? A ALA 883  
619  1 Y 1 A GLY 884  ? A GLY 884  
620  1 Y 1 A PRO 885  ? A PRO 885  
621  1 Y 1 A ALA 886  ? A ALA 886  
622  1 Y 1 A LEU 887  ? A LEU 887  
623  1 Y 1 A GLN 888  ? A GLN 888  
624  1 Y 1 A ILE 889  ? A ILE 889  
625  1 Y 1 A PRO 890  ? A PRO 890  
626  1 Y 1 A PHE 891  ? A PHE 891  
627  1 Y 1 A PRO 892  ? A PRO 892  
628  1 Y 1 A MET 893  ? A MET 893  
629  1 Y 1 A GLN 894  ? A GLN 894  
630  1 Y 1 A MET 895  ? A MET 895  
631  1 Y 1 A ALA 896  ? A ALA 896  
632  1 Y 1 A TYR 897  ? A TYR 897  
633  1 Y 1 A ARG 898  ? A ARG 898  
634  1 Y 1 A PHE 899  ? A PHE 899  
635  1 Y 1 A ASN 900  ? A ASN 900  
636  1 Y 1 A GLY 901  ? A GLY 901  
637  1 Y 1 A ILE 902  ? A ILE 902  
638  1 Y 1 A GLY 903  ? A GLY 903  
639  1 Y 1 A VAL 904  ? A VAL 904  
640  1 Y 1 A THR 905  ? A THR 905  
641  1 Y 1 A GLN 906  ? A GLN 906  
642  1 Y 1 A ASN 907  ? A ASN 907  
643  1 Y 1 A VAL 908  ? A VAL 908  
644  1 Y 1 A LEU 909  ? A LEU 909  
645  1 Y 1 A TYR 910  ? A TYR 910  
646  1 Y 1 A GLU 911  ? A GLU 911  
647  1 Y 1 A ASN 912  ? A ASN 912  
648  1 Y 1 A GLN 913  ? A GLN 913  
649  1 Y 1 A LYS 914  ? A LYS 914  
650  1 Y 1 A LEU 915  ? A LEU 915  
651  1 Y 1 A ILE 916  ? A ILE 916  
652  1 Y 1 A ALA 917  ? A ALA 917  
653  1 Y 1 A ASN 918  ? A ASN 918  
654  1 Y 1 A GLN 919  ? A GLN 919  
655  1 Y 1 A PHE 920  ? A PHE 920  
656  1 Y 1 A ASN 921  ? A ASN 921  
657  1 Y 1 A SER 922  ? A SER 922  
658  1 Y 1 A ALA 923  ? A ALA 923  
659  1 Y 1 A ILE 924  ? A ILE 924  
660  1 Y 1 A GLY 925  ? A GLY 925  
661  1 Y 1 A LYS 926  ? A LYS 926  
662  1 Y 1 A ILE 927  ? A ILE 927  
663  1 Y 1 A GLN 928  ? A GLN 928  
664  1 Y 1 A ASP 929  ? A ASP 929  
665  1 Y 1 A SER 930  ? A SER 930  
666  1 Y 1 A LEU 931  ? A LEU 931  
667  1 Y 1 A SER 932  ? A SER 932  
668  1 Y 1 A SER 933  ? A SER 933  
669  1 Y 1 A THR 934  ? A THR 934  
670  1 Y 1 A PRO 935  ? A PRO 935  
671  1 Y 1 A SER 936  ? A SER 936  
672  1 Y 1 A ALA 937  ? A ALA 937  
673  1 Y 1 A LEU 938  ? A LEU 938  
674  1 Y 1 A GLY 939  ? A GLY 939  
675  1 Y 1 A LYS 940  ? A LYS 940  
676  1 Y 1 A LEU 941  ? A LEU 941  
677  1 Y 1 A GLN 942  ? A GLN 942  
678  1 Y 1 A ASP 943  ? A ASP 943  
679  1 Y 1 A VAL 944  ? A VAL 944  
680  1 Y 1 A VAL 945  ? A VAL 945  
681  1 Y 1 A ASN 946  ? A ASN 946  
682  1 Y 1 A GLN 947  ? A GLN 947  
683  1 Y 1 A ASN 948  ? A ASN 948  
684  1 Y 1 A ALA 949  ? A ALA 949  
685  1 Y 1 A GLN 950  ? A GLN 950  
686  1 Y 1 A ALA 951  ? A ALA 951  
687  1 Y 1 A LEU 952  ? A LEU 952  
688  1 Y 1 A ASN 953  ? A ASN 953  
689  1 Y 1 A THR 954  ? A THR 954  
690  1 Y 1 A LEU 955  ? A LEU 955  
691  1 Y 1 A VAL 956  ? A VAL 956  
692  1 Y 1 A LYS 957  ? A LYS 957  
693  1 Y 1 A GLN 958  ? A GLN 958  
694  1 Y 1 A LEU 959  ? A LEU 959  
695  1 Y 1 A SER 960  ? A SER 960  
696  1 Y 1 A SER 961  ? A SER 961  
697  1 Y 1 A ASN 962  ? A ASN 962  
698  1 Y 1 A PHE 963  ? A PHE 963  
699  1 Y 1 A GLY 964  ? A GLY 964  
700  1 Y 1 A ALA 965  ? A ALA 965  
701  1 Y 1 A ILE 966  ? A ILE 966  
702  1 Y 1 A SER 967  ? A SER 967  
703  1 Y 1 A SER 968  ? A SER 968  
704  1 Y 1 A VAL 969  ? A VAL 969  
705  1 Y 1 A LEU 970  ? A LEU 970  
706  1 Y 1 A ASN 971  ? A ASN 971  
707  1 Y 1 A ASP 972  ? A ASP 972  
708  1 Y 1 A ILE 973  ? A ILE 973  
709  1 Y 1 A LEU 974  ? A LEU 974  
710  1 Y 1 A SER 975  ? A SER 975  
711  1 Y 1 A ARG 976  ? A ARG 976  
712  1 Y 1 A LEU 977  ? A LEU 977  
713  1 Y 1 A CYS 978  ? A CYS 978  
714  1 Y 1 A PRO 979  ? A PRO 979  
715  1 Y 1 A PRO 980  ? A PRO 980  
716  1 Y 1 A GLU 981  ? A GLU 981  
717  1 Y 1 A ALA 982  ? A ALA 982  
718  1 Y 1 A GLU 983  ? A GLU 983  
719  1 Y 1 A VAL 984  ? A VAL 984  
720  1 Y 1 A GLN 985  ? A GLN 985  
721  1 Y 1 A ILE 986  ? A ILE 986  
722  1 Y 1 A ASP 987  ? A ASP 987  
723  1 Y 1 A ARG 988  ? A ARG 988  
724  1 Y 1 A LEU 989  ? A LEU 989  
725  1 Y 1 A ILE 990  ? A ILE 990  
726  1 Y 1 A THR 991  ? A THR 991  
727  1 Y 1 A GLY 992  ? A GLY 992  
728  1 Y 1 A ARG 993  ? A ARG 993  
729  1 Y 1 A LEU 994  ? A LEU 994  
730  1 Y 1 A GLN 995  ? A GLN 995  
731  1 Y 1 A SER 996  ? A SER 996  
732  1 Y 1 A LEU 997  ? A LEU 997  
733  1 Y 1 A GLN 998  ? A GLN 998  
734  1 Y 1 A THR 999  ? A THR 999  
735  1 Y 1 A TYR 1000 ? A TYR 1000 
736  1 Y 1 A VAL 1001 ? A VAL 1001 
737  1 Y 1 A THR 1002 ? A THR 1002 
738  1 Y 1 A GLN 1003 ? A GLN 1003 
739  1 Y 1 A GLN 1004 ? A GLN 1004 
740  1 Y 1 A LEU 1005 ? A LEU 1005 
741  1 Y 1 A ILE 1006 ? A ILE 1006 
742  1 Y 1 A ARG 1007 ? A ARG 1007 
743  1 Y 1 A ALA 1008 ? A ALA 1008 
744  1 Y 1 A ALA 1009 ? A ALA 1009 
745  1 Y 1 A GLU 1010 ? A GLU 1010 
746  1 Y 1 A ILE 1011 ? A ILE 1011 
747  1 Y 1 A ARG 1012 ? A ARG 1012 
748  1 Y 1 A ALA 1013 ? A ALA 1013 
749  1 Y 1 A SER 1014 ? A SER 1014 
750  1 Y 1 A ALA 1015 ? A ALA 1015 
751  1 Y 1 A ASN 1016 ? A ASN 1016 
752  1 Y 1 A LEU 1017 ? A LEU 1017 
753  1 Y 1 A ALA 1018 ? A ALA 1018 
754  1 Y 1 A ALA 1019 ? A ALA 1019 
755  1 Y 1 A THR 1020 ? A THR 1020 
756  1 Y 1 A LYS 1021 ? A LYS 1021 
757  1 Y 1 A MET 1022 ? A MET 1022 
758  1 Y 1 A SER 1023 ? A SER 1023 
759  1 Y 1 A GLU 1024 ? A GLU 1024 
760  1 Y 1 A CYS 1025 ? A CYS 1025 
761  1 Y 1 A VAL 1026 ? A VAL 1026 
762  1 Y 1 A LEU 1027 ? A LEU 1027 
763  1 Y 1 A GLY 1028 ? A GLY 1028 
764  1 Y 1 A GLN 1029 ? A GLN 1029 
765  1 Y 1 A SER 1030 ? A SER 1030 
766  1 Y 1 A LYS 1031 ? A LYS 1031 
767  1 Y 1 A ARG 1032 ? A ARG 1032 
768  1 Y 1 A VAL 1033 ? A VAL 1033 
769  1 Y 1 A ASP 1034 ? A ASP 1034 
770  1 Y 1 A PHE 1035 ? A PHE 1035 
771  1 Y 1 A CYS 1036 ? A CYS 1036 
772  1 Y 1 A GLY 1037 ? A GLY 1037 
773  1 Y 1 A LYS 1038 ? A LYS 1038 
774  1 Y 1 A GLY 1039 ? A GLY 1039 
775  1 Y 1 A TYR 1040 ? A TYR 1040 
776  1 Y 1 A HIS 1041 ? A HIS 1041 
777  1 Y 1 A LEU 1042 ? A LEU 1042 
778  1 Y 1 A MET 1043 ? A MET 1043 
779  1 Y 1 A SER 1044 ? A SER 1044 
780  1 Y 1 A PHE 1045 ? A PHE 1045 
781  1 Y 1 A PRO 1046 ? A PRO 1046 
782  1 Y 1 A GLN 1047 ? A GLN 1047 
783  1 Y 1 A SER 1048 ? A SER 1048 
784  1 Y 1 A ALA 1049 ? A ALA 1049 
785  1 Y 1 A PRO 1050 ? A PRO 1050 
786  1 Y 1 A HIS 1051 ? A HIS 1051 
787  1 Y 1 A GLY 1052 ? A GLY 1052 
788  1 Y 1 A VAL 1053 ? A VAL 1053 
789  1 Y 1 A VAL 1054 ? A VAL 1054 
790  1 Y 1 A PHE 1055 ? A PHE 1055 
791  1 Y 1 A LEU 1056 ? A LEU 1056 
792  1 Y 1 A HIS 1057 ? A HIS 1057 
793  1 Y 1 A VAL 1058 ? A VAL 1058 
794  1 Y 1 A THR 1059 ? A THR 1059 
795  1 Y 1 A TYR 1060 ? A TYR 1060 
796  1 Y 1 A VAL 1061 ? A VAL 1061 
797  1 Y 1 A PRO 1062 ? A PRO 1062 
798  1 Y 1 A ALA 1063 ? A ALA 1063 
799  1 Y 1 A GLN 1064 ? A GLN 1064 
800  1 Y 1 A GLU 1065 ? A GLU 1065 
801  1 Y 1 A LYS 1066 ? A LYS 1066 
802  1 Y 1 A ASN 1067 ? A ASN 1067 
803  1 Y 1 A PHE 1068 ? A PHE 1068 
804  1 Y 1 A THR 1069 ? A THR 1069 
805  1 Y 1 A THR 1070 ? A THR 1070 
806  1 Y 1 A ALA 1071 ? A ALA 1071 
807  1 Y 1 A PRO 1072 ? A PRO 1072 
808  1 Y 1 A ALA 1073 ? A ALA 1073 
809  1 Y 1 A ILE 1074 ? A ILE 1074 
810  1 Y 1 A CYS 1075 ? A CYS 1075 
811  1 Y 1 A HIS 1076 ? A HIS 1076 
812  1 Y 1 A ASP 1077 ? A ASP 1077 
813  1 Y 1 A GLY 1078 ? A GLY 1078 
814  1 Y 1 A LYS 1079 ? A LYS 1079 
815  1 Y 1 A ALA 1080 ? A ALA 1080 
816  1 Y 1 A HIS 1081 ? A HIS 1081 
817  1 Y 1 A PHE 1082 ? A PHE 1082 
818  1 Y 1 A PRO 1083 ? A PRO 1083 
819  1 Y 1 A ARG 1084 ? A ARG 1084 
820  1 Y 1 A GLU 1085 ? A GLU 1085 
821  1 Y 1 A GLY 1086 ? A GLY 1086 
822  1 Y 1 A VAL 1087 ? A VAL 1087 
823  1 Y 1 A PHE 1088 ? A PHE 1088 
824  1 Y 1 A VAL 1089 ? A VAL 1089 
825  1 Y 1 A SER 1090 ? A SER 1090 
826  1 Y 1 A ASN 1091 ? A ASN 1091 
827  1 Y 1 A GLY 1092 ? A GLY 1092 
828  1 Y 1 A THR 1093 ? A THR 1093 
829  1 Y 1 A HIS 1094 ? A HIS 1094 
830  1 Y 1 A TRP 1095 ? A TRP 1095 
831  1 Y 1 A PHE 1096 ? A PHE 1096 
832  1 Y 1 A VAL 1097 ? A VAL 1097 
833  1 Y 1 A THR 1098 ? A THR 1098 
834  1 Y 1 A GLN 1099 ? A GLN 1099 
835  1 Y 1 A ARG 1100 ? A ARG 1100 
836  1 Y 1 A ASN 1101 ? A ASN 1101 
837  1 Y 1 A PHE 1102 ? A PHE 1102 
838  1 Y 1 A TYR 1103 ? A TYR 1103 
839  1 Y 1 A GLU 1104 ? A GLU 1104 
840  1 Y 1 A PRO 1105 ? A PRO 1105 
841  1 Y 1 A GLN 1106 ? A GLN 1106 
842  1 Y 1 A ILE 1107 ? A ILE 1107 
843  1 Y 1 A ILE 1108 ? A ILE 1108 
844  1 Y 1 A THR 1109 ? A THR 1109 
845  1 Y 1 A THR 1110 ? A THR 1110 
846  1 Y 1 A ASP 1111 ? A ASP 1111 
847  1 Y 1 A ASN 1112 ? A ASN 1112 
848  1 Y 1 A THR 1113 ? A THR 1113 
849  1 Y 1 A PHE 1114 ? A PHE 1114 
850  1 Y 1 A VAL 1115 ? A VAL 1115 
851  1 Y 1 A SER 1116 ? A SER 1116 
852  1 Y 1 A GLY 1117 ? A GLY 1117 
853  1 Y 1 A ASN 1118 ? A ASN 1118 
854  1 Y 1 A CYS 1119 ? A CYS 1119 
855  1 Y 1 A ASP 1120 ? A ASP 1120 
856  1 Y 1 A VAL 1121 ? A VAL 1121 
857  1 Y 1 A VAL 1122 ? A VAL 1122 
858  1 Y 1 A ILE 1123 ? A ILE 1123 
859  1 Y 1 A GLY 1124 ? A GLY 1124 
860  1 Y 1 A ILE 1125 ? A ILE 1125 
861  1 Y 1 A VAL 1126 ? A VAL 1126 
862  1 Y 1 A ASN 1127 ? A ASN 1127 
863  1 Y 1 A ASN 1128 ? A ASN 1128 
864  1 Y 1 A THR 1129 ? A THR 1129 
865  1 Y 1 A VAL 1130 ? A VAL 1130 
866  1 Y 1 A TYR 1131 ? A TYR 1131 
867  1 Y 1 A ASP 1132 ? A ASP 1132 
868  1 Y 1 A PRO 1133 ? A PRO 1133 
869  1 Y 1 A LEU 1134 ? A LEU 1134 
870  1 Y 1 A GLN 1135 ? A GLN 1135 
871  1 Y 1 A PRO 1136 ? A PRO 1136 
872  1 Y 1 A GLU 1137 ? A GLU 1137 
873  1 Y 1 A LEU 1138 ? A LEU 1138 
874  1 Y 1 A ASP 1139 ? A ASP 1139 
875  1 Y 1 A SER 1140 ? A SER 1140 
876  1 Y 1 A PHE 1141 ? A PHE 1141 
877  1 Y 1 A LYS 1142 ? A LYS 1142 
878  1 Y 1 A GLU 1143 ? A GLU 1143 
879  1 Y 1 A GLU 1144 ? A GLU 1144 
880  1 Y 1 A LEU 1145 ? A LEU 1145 
881  1 Y 1 A ASP 1146 ? A ASP 1146 
882  1 Y 1 A LYS 1147 ? A LYS 1147 
883  1 Y 1 A TYR 1148 ? A TYR 1148 
884  1 Y 1 A PHE 1149 ? A PHE 1149 
885  1 Y 1 A LYS 1150 ? A LYS 1150 
886  1 Y 1 A ASN 1151 ? A ASN 1151 
887  1 Y 1 A HIS 1152 ? A HIS 1152 
888  1 Y 1 A THR 1153 ? A THR 1153 
889  1 Y 1 A SER 1154 ? A SER 1154 
890  1 Y 1 A PRO 1155 ? A PRO 1155 
891  1 Y 1 A ASP 1156 ? A ASP 1156 
892  1 Y 1 A VAL 1157 ? A VAL 1157 
893  1 Y 1 A ASP 1158 ? A ASP 1158 
894  1 Y 1 A LEU 1159 ? A LEU 1159 
895  1 Y 1 A GLY 1160 ? A GLY 1160 
896  1 Y 1 A ASP 1161 ? A ASP 1161 
897  1 Y 1 A ILE 1162 ? A ILE 1162 
898  1 Y 1 A SER 1163 ? A SER 1163 
899  1 Y 1 A GLY 1164 ? A GLY 1164 
900  1 Y 1 A ILE 1165 ? A ILE 1165 
901  1 Y 1 A ASN 1166 ? A ASN 1166 
902  1 Y 1 A ALA 1167 ? A ALA 1167 
903  1 Y 1 A SER 1168 ? A SER 1168 
904  1 Y 1 A VAL 1169 ? A VAL 1169 
905  1 Y 1 A VAL 1170 ? A VAL 1170 
906  1 Y 1 A ASN 1171 ? A ASN 1171 
907  1 Y 1 A ILE 1172 ? A ILE 1172 
908  1 Y 1 A GLN 1173 ? A GLN 1173 
909  1 Y 1 A LYS 1174 ? A LYS 1174 
910  1 Y 1 A GLU 1175 ? A GLU 1175 
911  1 Y 1 A ILE 1176 ? A ILE 1176 
912  1 Y 1 A ASP 1177 ? A ASP 1177 
913  1 Y 1 A ARG 1178 ? A ARG 1178 
914  1 Y 1 A LEU 1179 ? A LEU 1179 
915  1 Y 1 A ASN 1180 ? A ASN 1180 
916  1 Y 1 A GLU 1181 ? A GLU 1181 
917  1 Y 1 A VAL 1182 ? A VAL 1182 
918  1 Y 1 A ALA 1183 ? A ALA 1183 
919  1 Y 1 A LYS 1184 ? A LYS 1184 
920  1 Y 1 A ASN 1185 ? A ASN 1185 
921  1 Y 1 A LEU 1186 ? A LEU 1186 
922  1 Y 1 A ASN 1187 ? A ASN 1187 
923  1 Y 1 A GLU 1188 ? A GLU 1188 
924  1 Y 1 A SER 1189 ? A SER 1189 
925  1 Y 1 A LEU 1190 ? A LEU 1190 
926  1 Y 1 A ILE 1191 ? A ILE 1191 
927  1 Y 1 A ASP 1192 ? A ASP 1192 
928  1 Y 1 A LEU 1193 ? A LEU 1193 
929  1 Y 1 A GLN 1194 ? A GLN 1194 
930  1 Y 1 A GLU 1195 ? A GLU 1195 
931  1 Y 1 A LEU 1196 ? A LEU 1196 
932  1 Y 1 A GLY 1197 ? A GLY 1197 
933  1 Y 1 A LYS 1198 ? A LYS 1198 
934  1 Y 1 A TYR 1199 ? A TYR 1199 
935  1 Y 1 A GLU 1200 ? A GLU 1200 
936  1 Y 1 A GLN 1201 ? A GLN 1201 
937  1 Y 1 A GLY 1202 ? A GLY 1202 
938  1 Y 1 A SER 1203 ? A SER 1203 
939  1 Y 1 A GLY 1204 ? A GLY 1204 
940  1 Y 1 A TYR 1205 ? A TYR 1205 
941  1 Y 1 A ILE 1206 ? A ILE 1206 
942  1 Y 1 A PRO 1207 ? A PRO 1207 
943  1 Y 1 A GLU 1208 ? A GLU 1208 
944  1 Y 1 A ALA 1209 ? A ALA 1209 
945  1 Y 1 A PRO 1210 ? A PRO 1210 
946  1 Y 1 A ARG 1211 ? A ARG 1211 
947  1 Y 1 A ASP 1212 ? A ASP 1212 
948  1 Y 1 A GLY 1213 ? A GLY 1213 
949  1 Y 1 A GLN 1214 ? A GLN 1214 
950  1 Y 1 A ALA 1215 ? A ALA 1215 
951  1 Y 1 A TYR 1216 ? A TYR 1216 
952  1 Y 1 A VAL 1217 ? A VAL 1217 
953  1 Y 1 A ARG 1218 ? A ARG 1218 
954  1 Y 1 A LYS 1219 ? A LYS 1219 
955  1 Y 1 A ASP 1220 ? A ASP 1220 
956  1 Y 1 A GLY 1221 ? A GLY 1221 
957  1 Y 1 A GLU 1222 ? A GLU 1222 
958  1 Y 1 A TRP 1223 ? A TRP 1223 
959  1 Y 1 A VAL 1224 ? A VAL 1224 
960  1 Y 1 A LEU 1225 ? A LEU 1225 
961  1 Y 1 A LEU 1226 ? A LEU 1226 
962  1 Y 1 A SER 1227 ? A SER 1227 
963  1 Y 1 A THR 1228 ? A THR 1228 
964  1 Y 1 A PHE 1229 ? A PHE 1229 
965  1 Y 1 A LEU 1230 ? A LEU 1230 
966  1 Y 1 A GLY 1231 ? A GLY 1231 
967  1 Y 1 A ARG 1232 ? A ARG 1232 
968  1 Y 1 A SER 1233 ? A SER 1233 
969  1 Y 1 A LEU 1234 ? A LEU 1234 
970  1 Y 1 A GLU 1235 ? A GLU 1235 
971  1 Y 1 A VAL 1236 ? A VAL 1236 
972  1 Y 1 A LEU 1237 ? A LEU 1237 
973  1 Y 1 A PHE 1238 ? A PHE 1238 
974  1 Y 1 A GLN 1239 ? A GLN 1239 
975  1 Y 1 A GLY 1240 ? A GLY 1240 
976  1 Y 1 A PRO 1241 ? A PRO 1241 
977  1 Y 1 A GLY 1242 ? A GLY 1242 
978  1 Y 1 A SER 1243 ? A SER 1243 
979  1 Y 1 A GLY 1244 ? A GLY 1244 
980  1 Y 1 A GLY 1245 ? A GLY 1245 
981  1 Y 1 A LEU 1246 ? A LEU 1246 
982  1 Y 1 A ASN 1247 ? A ASN 1247 
983  1 Y 1 A ASP 1248 ? A ASP 1248 
984  1 Y 1 A ILE 1249 ? A ILE 1249 
985  1 Y 1 A PHE 1250 ? A PHE 1250 
986  1 Y 1 A GLU 1251 ? A GLU 1251 
987  1 Y 1 A ALA 1252 ? A ALA 1252 
988  1 Y 1 A GLN 1253 ? A GLN 1253 
989  1 Y 1 A LYS 1254 ? A LYS 1254 
990  1 Y 1 A ILE 1255 ? A ILE 1255 
991  1 Y 1 A GLU 1256 ? A GLU 1256 
992  1 Y 1 A TRP 1257 ? A TRP 1257 
993  1 Y 1 A HIS 1258 ? A HIS 1258 
994  1 Y 1 A GLU 1259 ? A GLU 1259 
995  1 Y 1 A GLY 1260 ? A GLY 1260 
996  1 Y 1 A SER 1261 ? A SER 1261 
997  1 Y 1 A GLY 1262 ? A GLY 1262 
998  1 Y 1 A HIS 1263 ? A HIS 1263 
999  1 Y 1 A HIS 1264 ? A HIS 1264 
1000 1 Y 1 A HIS 1265 ? A HIS 1265 
1001 1 Y 1 A HIS 1266 ? A HIS 1266 
1002 1 Y 1 A HIS 1267 ? A HIS 1267 
1003 1 Y 1 A HIS 1268 ? A HIS 1268 
1004 1 Y 1 A HIS 1269 ? A HIS 1269 
1005 1 Y 1 A HIS 1270 ? A HIS 1270 
1006 1 Y 1 B SER 122  ? B SER 122  
1007 1 Y 1 C VAL 1    ? C VAL 1    
1008 1 Y 1 C LYS 107  ? C LYS 107  
1009 1 Y 1 H GLN 1    ? D GLN 1    
1010 1 Y 1 H ILE 2    ? D ILE 2    
1011 1 Y 1 H THR 3    ? D THR 3    
1012 1 Y 1 H LEU 4    ? D LEU 4    
1013 1 Y 1 H SER 124  ? D SER 124  
1014 1 Y 1 H SER 125  ? D SER 125  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
BMA C1   C N R 74  
BMA C2   C N S 75  
BMA C3   C N S 76  
BMA C4   C N S 77  
BMA C5   C N R 78  
BMA C6   C N N 79  
BMA O1   O N N 80  
BMA O2   O N N 81  
BMA O3   O N N 82  
BMA O4   O N N 83  
BMA O5   O N N 84  
BMA O6   O N N 85  
BMA H1   H N N 86  
BMA H2   H N N 87  
BMA H3   H N N 88  
BMA H4   H N N 89  
BMA H5   H N N 90  
BMA H61  H N N 91  
BMA H62  H N N 92  
BMA HO1  H N N 93  
BMA HO2  H N N 94  
BMA HO3  H N N 95  
BMA HO4  H N N 96  
BMA HO6  H N N 97  
CYS N    N N N 98  
CYS CA   C N R 99  
CYS C    C N N 100 
CYS O    O N N 101 
CYS CB   C N N 102 
CYS SG   S N N 103 
CYS OXT  O N N 104 
CYS H    H N N 105 
CYS H2   H N N 106 
CYS HA   H N N 107 
CYS HB2  H N N 108 
CYS HB3  H N N 109 
CYS HG   H N N 110 
CYS HXT  H N N 111 
GLN N    N N N 112 
GLN CA   C N S 113 
GLN C    C N N 114 
GLN O    O N N 115 
GLN CB   C N N 116 
GLN CG   C N N 117 
GLN CD   C N N 118 
GLN OE1  O N N 119 
GLN NE2  N N N 120 
GLN OXT  O N N 121 
GLN H    H N N 122 
GLN H2   H N N 123 
GLN HA   H N N 124 
GLN HB2  H N N 125 
GLN HB3  H N N 126 
GLN HG2  H N N 127 
GLN HG3  H N N 128 
GLN HE21 H N N 129 
GLN HE22 H N N 130 
GLN HXT  H N N 131 
GLU N    N N N 132 
GLU CA   C N S 133 
GLU C    C N N 134 
GLU O    O N N 135 
GLU CB   C N N 136 
GLU CG   C N N 137 
GLU CD   C N N 138 
GLU OE1  O N N 139 
GLU OE2  O N N 140 
GLU OXT  O N N 141 
GLU H    H N N 142 
GLU H2   H N N 143 
GLU HA   H N N 144 
GLU HB2  H N N 145 
GLU HB3  H N N 146 
GLU HG2  H N N 147 
GLU HG3  H N N 148 
GLU HE2  H N N 149 
GLU HXT  H N N 150 
GLY N    N N N 151 
GLY CA   C N N 152 
GLY C    C N N 153 
GLY O    O N N 154 
GLY OXT  O N N 155 
GLY H    H N N 156 
GLY H2   H N N 157 
GLY HA2  H N N 158 
GLY HA3  H N N 159 
GLY HXT  H N N 160 
HIS N    N N N 161 
HIS CA   C N S 162 
HIS C    C N N 163 
HIS O    O N N 164 
HIS CB   C N N 165 
HIS CG   C Y N 166 
HIS ND1  N Y N 167 
HIS CD2  C Y N 168 
HIS CE1  C Y N 169 
HIS NE2  N Y N 170 
HIS OXT  O N N 171 
HIS H    H N N 172 
HIS H2   H N N 173 
HIS HA   H N N 174 
HIS HB2  H N N 175 
HIS HB3  H N N 176 
HIS HD1  H N N 177 
HIS HD2  H N N 178 
HIS HE1  H N N 179 
HIS HE2  H N N 180 
HIS HXT  H N N 181 
ILE N    N N N 182 
ILE CA   C N S 183 
ILE C    C N N 184 
ILE O    O N N 185 
ILE CB   C N S 186 
ILE CG1  C N N 187 
ILE CG2  C N N 188 
ILE CD1  C N N 189 
ILE OXT  O N N 190 
ILE H    H N N 191 
ILE H2   H N N 192 
ILE HA   H N N 193 
ILE HB   H N N 194 
ILE HG12 H N N 195 
ILE HG13 H N N 196 
ILE HG21 H N N 197 
ILE HG22 H N N 198 
ILE HG23 H N N 199 
ILE HD11 H N N 200 
ILE HD12 H N N 201 
ILE HD13 H N N 202 
ILE HXT  H N N 203 
LEU N    N N N 204 
LEU CA   C N S 205 
LEU C    C N N 206 
LEU O    O N N 207 
LEU CB   C N N 208 
LEU CG   C N N 209 
LEU CD1  C N N 210 
LEU CD2  C N N 211 
LEU OXT  O N N 212 
LEU H    H N N 213 
LEU H2   H N N 214 
LEU HA   H N N 215 
LEU HB2  H N N 216 
LEU HB3  H N N 217 
LEU HG   H N N 218 
LEU HD11 H N N 219 
LEU HD12 H N N 220 
LEU HD13 H N N 221 
LEU HD21 H N N 222 
LEU HD22 H N N 223 
LEU HD23 H N N 224 
LEU HXT  H N N 225 
LYS N    N N N 226 
LYS CA   C N S 227 
LYS C    C N N 228 
LYS O    O N N 229 
LYS CB   C N N 230 
LYS CG   C N N 231 
LYS CD   C N N 232 
LYS CE   C N N 233 
LYS NZ   N N N 234 
LYS OXT  O N N 235 
LYS H    H N N 236 
LYS H2   H N N 237 
LYS HA   H N N 238 
LYS HB2  H N N 239 
LYS HB3  H N N 240 
LYS HG2  H N N 241 
LYS HG3  H N N 242 
LYS HD2  H N N 243 
LYS HD3  H N N 244 
LYS HE2  H N N 245 
LYS HE3  H N N 246 
LYS HZ1  H N N 247 
LYS HZ2  H N N 248 
LYS HZ3  H N N 249 
LYS HXT  H N N 250 
MET N    N N N 251 
MET CA   C N S 252 
MET C    C N N 253 
MET O    O N N 254 
MET CB   C N N 255 
MET CG   C N N 256 
MET SD   S N N 257 
MET CE   C N N 258 
MET OXT  O N N 259 
MET H    H N N 260 
MET H2   H N N 261 
MET HA   H N N 262 
MET HB2  H N N 263 
MET HB3  H N N 264 
MET HG2  H N N 265 
MET HG3  H N N 266 
MET HE1  H N N 267 
MET HE2  H N N 268 
MET HE3  H N N 269 
MET HXT  H N N 270 
NAG C1   C N R 271 
NAG C2   C N R 272 
NAG C3   C N R 273 
NAG C4   C N S 274 
NAG C5   C N R 275 
NAG C6   C N N 276 
NAG C7   C N N 277 
NAG C8   C N N 278 
NAG N2   N N N 279 
NAG O1   O N N 280 
NAG O3   O N N 281 
NAG O4   O N N 282 
NAG O5   O N N 283 
NAG O6   O N N 284 
NAG O7   O N N 285 
NAG H1   H N N 286 
NAG H2   H N N 287 
NAG H3   H N N 288 
NAG H4   H N N 289 
NAG H5   H N N 290 
NAG H61  H N N 291 
NAG H62  H N N 292 
NAG H81  H N N 293 
NAG H82  H N N 294 
NAG H83  H N N 295 
NAG HN2  H N N 296 
NAG HO1  H N N 297 
NAG HO3  H N N 298 
NAG HO4  H N N 299 
NAG HO6  H N N 300 
PHE N    N N N 301 
PHE CA   C N S 302 
PHE C    C N N 303 
PHE O    O N N 304 
PHE CB   C N N 305 
PHE CG   C Y N 306 
PHE CD1  C Y N 307 
PHE CD2  C Y N 308 
PHE CE1  C Y N 309 
PHE CE2  C Y N 310 
PHE CZ   C Y N 311 
PHE OXT  O N N 312 
PHE H    H N N 313 
PHE H2   H N N 314 
PHE HA   H N N 315 
PHE HB2  H N N 316 
PHE HB3  H N N 317 
PHE HD1  H N N 318 
PHE HD2  H N N 319 
PHE HE1  H N N 320 
PHE HE2  H N N 321 
PHE HZ   H N N 322 
PHE HXT  H N N 323 
PRO N    N N N 324 
PRO CA   C N S 325 
PRO C    C N N 326 
PRO O    O N N 327 
PRO CB   C N N 328 
PRO CG   C N N 329 
PRO CD   C N N 330 
PRO OXT  O N N 331 
PRO H    H N N 332 
PRO HA   H N N 333 
PRO HB2  H N N 334 
PRO HB3  H N N 335 
PRO HG2  H N N 336 
PRO HG3  H N N 337 
PRO HD2  H N N 338 
PRO HD3  H N N 339 
PRO HXT  H N N 340 
SER N    N N N 341 
SER CA   C N S 342 
SER C    C N N 343 
SER O    O N N 344 
SER CB   C N N 345 
SER OG   O N N 346 
SER OXT  O N N 347 
SER H    H N N 348 
SER H2   H N N 349 
SER HA   H N N 350 
SER HB2  H N N 351 
SER HB3  H N N 352 
SER HG   H N N 353 
SER HXT  H N N 354 
THR N    N N N 355 
THR CA   C N S 356 
THR C    C N N 357 
THR O    O N N 358 
THR CB   C N R 359 
THR OG1  O N N 360 
THR CG2  C N N 361 
THR OXT  O N N 362 
THR H    H N N 363 
THR H2   H N N 364 
THR HA   H N N 365 
THR HB   H N N 366 
THR HG1  H N N 367 
THR HG21 H N N 368 
THR HG22 H N N 369 
THR HG23 H N N 370 
THR HXT  H N N 371 
TRP N    N N N 372 
TRP CA   C N S 373 
TRP C    C N N 374 
TRP O    O N N 375 
TRP CB   C N N 376 
TRP CG   C Y N 377 
TRP CD1  C Y N 378 
TRP CD2  C Y N 379 
TRP NE1  N Y N 380 
TRP CE2  C Y N 381 
TRP CE3  C Y N 382 
TRP CZ2  C Y N 383 
TRP CZ3  C Y N 384 
TRP CH2  C Y N 385 
TRP OXT  O N N 386 
TRP H    H N N 387 
TRP H2   H N N 388 
TRP HA   H N N 389 
TRP HB2  H N N 390 
TRP HB3  H N N 391 
TRP HD1  H N N 392 
TRP HE1  H N N 393 
TRP HE3  H N N 394 
TRP HZ2  H N N 395 
TRP HZ3  H N N 396 
TRP HH2  H N N 397 
TRP HXT  H N N 398 
TYR N    N N N 399 
TYR CA   C N S 400 
TYR C    C N N 401 
TYR O    O N N 402 
TYR CB   C N N 403 
TYR CG   C Y N 404 
TYR CD1  C Y N 405 
TYR CD2  C Y N 406 
TYR CE1  C Y N 407 
TYR CE2  C Y N 408 
TYR CZ   C Y N 409 
TYR OH   O N N 410 
TYR OXT  O N N 411 
TYR H    H N N 412 
TYR H2   H N N 413 
TYR HA   H N N 414 
TYR HB2  H N N 415 
TYR HB3  H N N 416 
TYR HD1  H N N 417 
TYR HD2  H N N 418 
TYR HE1  H N N 419 
TYR HE2  H N N 420 
TYR HH   H N N 421 
TYR HXT  H N N 422 
VAL N    N N N 423 
VAL CA   C N S 424 
VAL C    C N N 425 
VAL O    O N N 426 
VAL CB   C N N 427 
VAL CG1  C N N 428 
VAL CG2  C N N 429 
VAL OXT  O N N 430 
VAL H    H N N 431 
VAL H2   H N N 432 
VAL HA   H N N 433 
VAL HB   H N N 434 
VAL HG11 H N N 435 
VAL HG12 H N N 436 
VAL HG13 H N N 437 
VAL HG21 H N N 438 
VAL HG22 H N N 439 
VAL HG23 H N N 440 
VAL HXT  H N N 441 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BMA C1  C2   sing N N 70  
BMA C1  O1   sing N N 71  
BMA C1  O5   sing N N 72  
BMA C1  H1   sing N N 73  
BMA C2  C3   sing N N 74  
BMA C2  O2   sing N N 75  
BMA C2  H2   sing N N 76  
BMA C3  C4   sing N N 77  
BMA C3  O3   sing N N 78  
BMA C3  H3   sing N N 79  
BMA C4  C5   sing N N 80  
BMA C4  O4   sing N N 81  
BMA C4  H4   sing N N 82  
BMA C5  C6   sing N N 83  
BMA C5  O5   sing N N 84  
BMA C5  H5   sing N N 85  
BMA C6  O6   sing N N 86  
BMA C6  H61  sing N N 87  
BMA C6  H62  sing N N 88  
BMA O1  HO1  sing N N 89  
BMA O2  HO2  sing N N 90  
BMA O3  HO3  sing N N 91  
BMA O4  HO4  sing N N 92  
BMA O6  HO6  sing N N 93  
CYS N   CA   sing N N 94  
CYS N   H    sing N N 95  
CYS N   H2   sing N N 96  
CYS CA  C    sing N N 97  
CYS CA  CB   sing N N 98  
CYS CA  HA   sing N N 99  
CYS C   O    doub N N 100 
CYS C   OXT  sing N N 101 
CYS CB  SG   sing N N 102 
CYS CB  HB2  sing N N 103 
CYS CB  HB3  sing N N 104 
CYS SG  HG   sing N N 105 
CYS OXT HXT  sing N N 106 
GLN N   CA   sing N N 107 
GLN N   H    sing N N 108 
GLN N   H2   sing N N 109 
GLN CA  C    sing N N 110 
GLN CA  CB   sing N N 111 
GLN CA  HA   sing N N 112 
GLN C   O    doub N N 113 
GLN C   OXT  sing N N 114 
GLN CB  CG   sing N N 115 
GLN CB  HB2  sing N N 116 
GLN CB  HB3  sing N N 117 
GLN CG  CD   sing N N 118 
GLN CG  HG2  sing N N 119 
GLN CG  HG3  sing N N 120 
GLN CD  OE1  doub N N 121 
GLN CD  NE2  sing N N 122 
GLN NE2 HE21 sing N N 123 
GLN NE2 HE22 sing N N 124 
GLN OXT HXT  sing N N 125 
GLU N   CA   sing N N 126 
GLU N   H    sing N N 127 
GLU N   H2   sing N N 128 
GLU CA  C    sing N N 129 
GLU CA  CB   sing N N 130 
GLU CA  HA   sing N N 131 
GLU C   O    doub N N 132 
GLU C   OXT  sing N N 133 
GLU CB  CG   sing N N 134 
GLU CB  HB2  sing N N 135 
GLU CB  HB3  sing N N 136 
GLU CG  CD   sing N N 137 
GLU CG  HG2  sing N N 138 
GLU CG  HG3  sing N N 139 
GLU CD  OE1  doub N N 140 
GLU CD  OE2  sing N N 141 
GLU OE2 HE2  sing N N 142 
GLU OXT HXT  sing N N 143 
GLY N   CA   sing N N 144 
GLY N   H    sing N N 145 
GLY N   H2   sing N N 146 
GLY CA  C    sing N N 147 
GLY CA  HA2  sing N N 148 
GLY CA  HA3  sing N N 149 
GLY C   O    doub N N 150 
GLY C   OXT  sing N N 151 
GLY OXT HXT  sing N N 152 
HIS N   CA   sing N N 153 
HIS N   H    sing N N 154 
HIS N   H2   sing N N 155 
HIS CA  C    sing N N 156 
HIS CA  CB   sing N N 157 
HIS CA  HA   sing N N 158 
HIS C   O    doub N N 159 
HIS C   OXT  sing N N 160 
HIS CB  CG   sing N N 161 
HIS CB  HB2  sing N N 162 
HIS CB  HB3  sing N N 163 
HIS CG  ND1  sing Y N 164 
HIS CG  CD2  doub Y N 165 
HIS ND1 CE1  doub Y N 166 
HIS ND1 HD1  sing N N 167 
HIS CD2 NE2  sing Y N 168 
HIS CD2 HD2  sing N N 169 
HIS CE1 NE2  sing Y N 170 
HIS CE1 HE1  sing N N 171 
HIS NE2 HE2  sing N N 172 
HIS OXT HXT  sing N N 173 
ILE N   CA   sing N N 174 
ILE N   H    sing N N 175 
ILE N   H2   sing N N 176 
ILE CA  C    sing N N 177 
ILE CA  CB   sing N N 178 
ILE CA  HA   sing N N 179 
ILE C   O    doub N N 180 
ILE C   OXT  sing N N 181 
ILE CB  CG1  sing N N 182 
ILE CB  CG2  sing N N 183 
ILE CB  HB   sing N N 184 
ILE CG1 CD1  sing N N 185 
ILE CG1 HG12 sing N N 186 
ILE CG1 HG13 sing N N 187 
ILE CG2 HG21 sing N N 188 
ILE CG2 HG22 sing N N 189 
ILE CG2 HG23 sing N N 190 
ILE CD1 HD11 sing N N 191 
ILE CD1 HD12 sing N N 192 
ILE CD1 HD13 sing N N 193 
ILE OXT HXT  sing N N 194 
LEU N   CA   sing N N 195 
LEU N   H    sing N N 196 
LEU N   H2   sing N N 197 
LEU CA  C    sing N N 198 
LEU CA  CB   sing N N 199 
LEU CA  HA   sing N N 200 
LEU C   O    doub N N 201 
LEU C   OXT  sing N N 202 
LEU CB  CG   sing N N 203 
LEU CB  HB2  sing N N 204 
LEU CB  HB3  sing N N 205 
LEU CG  CD1  sing N N 206 
LEU CG  CD2  sing N N 207 
LEU CG  HG   sing N N 208 
LEU CD1 HD11 sing N N 209 
LEU CD1 HD12 sing N N 210 
LEU CD1 HD13 sing N N 211 
LEU CD2 HD21 sing N N 212 
LEU CD2 HD22 sing N N 213 
LEU CD2 HD23 sing N N 214 
LEU OXT HXT  sing N N 215 
LYS N   CA   sing N N 216 
LYS N   H    sing N N 217 
LYS N   H2   sing N N 218 
LYS CA  C    sing N N 219 
LYS CA  CB   sing N N 220 
LYS CA  HA   sing N N 221 
LYS C   O    doub N N 222 
LYS C   OXT  sing N N 223 
LYS CB  CG   sing N N 224 
LYS CB  HB2  sing N N 225 
LYS CB  HB3  sing N N 226 
LYS CG  CD   sing N N 227 
LYS CG  HG2  sing N N 228 
LYS CG  HG3  sing N N 229 
LYS CD  CE   sing N N 230 
LYS CD  HD2  sing N N 231 
LYS CD  HD3  sing N N 232 
LYS CE  NZ   sing N N 233 
LYS CE  HE2  sing N N 234 
LYS CE  HE3  sing N N 235 
LYS NZ  HZ1  sing N N 236 
LYS NZ  HZ2  sing N N 237 
LYS NZ  HZ3  sing N N 238 
LYS OXT HXT  sing N N 239 
MET N   CA   sing N N 240 
MET N   H    sing N N 241 
MET N   H2   sing N N 242 
MET CA  C    sing N N 243 
MET CA  CB   sing N N 244 
MET CA  HA   sing N N 245 
MET C   O    doub N N 246 
MET C   OXT  sing N N 247 
MET CB  CG   sing N N 248 
MET CB  HB2  sing N N 249 
MET CB  HB3  sing N N 250 
MET CG  SD   sing N N 251 
MET CG  HG2  sing N N 252 
MET CG  HG3  sing N N 253 
MET SD  CE   sing N N 254 
MET CE  HE1  sing N N 255 
MET CE  HE2  sing N N 256 
MET CE  HE3  sing N N 257 
MET OXT HXT  sing N N 258 
NAG C1  C2   sing N N 259 
NAG C1  O1   sing N N 260 
NAG C1  O5   sing N N 261 
NAG C1  H1   sing N N 262 
NAG C2  C3   sing N N 263 
NAG C2  N2   sing N N 264 
NAG C2  H2   sing N N 265 
NAG C3  C4   sing N N 266 
NAG C3  O3   sing N N 267 
NAG C3  H3   sing N N 268 
NAG C4  C5   sing N N 269 
NAG C4  O4   sing N N 270 
NAG C4  H4   sing N N 271 
NAG C5  C6   sing N N 272 
NAG C5  O5   sing N N 273 
NAG C5  H5   sing N N 274 
NAG C6  O6   sing N N 275 
NAG C6  H61  sing N N 276 
NAG C6  H62  sing N N 277 
NAG C7  C8   sing N N 278 
NAG C7  N2   sing N N 279 
NAG C7  O7   doub N N 280 
NAG C8  H81  sing N N 281 
NAG C8  H82  sing N N 282 
NAG C8  H83  sing N N 283 
NAG N2  HN2  sing N N 284 
NAG O1  HO1  sing N N 285 
NAG O3  HO3  sing N N 286 
NAG O4  HO4  sing N N 287 
NAG O6  HO6  sing N N 288 
PHE N   CA   sing N N 289 
PHE N   H    sing N N 290 
PHE N   H2   sing N N 291 
PHE CA  C    sing N N 292 
PHE CA  CB   sing N N 293 
PHE CA  HA   sing N N 294 
PHE C   O    doub N N 295 
PHE C   OXT  sing N N 296 
PHE CB  CG   sing N N 297 
PHE CB  HB2  sing N N 298 
PHE CB  HB3  sing N N 299 
PHE CG  CD1  doub Y N 300 
PHE CG  CD2  sing Y N 301 
PHE CD1 CE1  sing Y N 302 
PHE CD1 HD1  sing N N 303 
PHE CD2 CE2  doub Y N 304 
PHE CD2 HD2  sing N N 305 
PHE CE1 CZ   doub Y N 306 
PHE CE1 HE1  sing N N 307 
PHE CE2 CZ   sing Y N 308 
PHE CE2 HE2  sing N N 309 
PHE CZ  HZ   sing N N 310 
PHE OXT HXT  sing N N 311 
PRO N   CA   sing N N 312 
PRO N   CD   sing N N 313 
PRO N   H    sing N N 314 
PRO CA  C    sing N N 315 
PRO CA  CB   sing N N 316 
PRO CA  HA   sing N N 317 
PRO C   O    doub N N 318 
PRO C   OXT  sing N N 319 
PRO CB  CG   sing N N 320 
PRO CB  HB2  sing N N 321 
PRO CB  HB3  sing N N 322 
PRO CG  CD   sing N N 323 
PRO CG  HG2  sing N N 324 
PRO CG  HG3  sing N N 325 
PRO CD  HD2  sing N N 326 
PRO CD  HD3  sing N N 327 
PRO OXT HXT  sing N N 328 
SER N   CA   sing N N 329 
SER N   H    sing N N 330 
SER N   H2   sing N N 331 
SER CA  C    sing N N 332 
SER CA  CB   sing N N 333 
SER CA  HA   sing N N 334 
SER C   O    doub N N 335 
SER C   OXT  sing N N 336 
SER CB  OG   sing N N 337 
SER CB  HB2  sing N N 338 
SER CB  HB3  sing N N 339 
SER OG  HG   sing N N 340 
SER OXT HXT  sing N N 341 
THR N   CA   sing N N 342 
THR N   H    sing N N 343 
THR N   H2   sing N N 344 
THR CA  C    sing N N 345 
THR CA  CB   sing N N 346 
THR CA  HA   sing N N 347 
THR C   O    doub N N 348 
THR C   OXT  sing N N 349 
THR CB  OG1  sing N N 350 
THR CB  CG2  sing N N 351 
THR CB  HB   sing N N 352 
THR OG1 HG1  sing N N 353 
THR CG2 HG21 sing N N 354 
THR CG2 HG22 sing N N 355 
THR CG2 HG23 sing N N 356 
THR OXT HXT  sing N N 357 
TRP N   CA   sing N N 358 
TRP N   H    sing N N 359 
TRP N   H2   sing N N 360 
TRP CA  C    sing N N 361 
TRP CA  CB   sing N N 362 
TRP CA  HA   sing N N 363 
TRP C   O    doub N N 364 
TRP C   OXT  sing N N 365 
TRP CB  CG   sing N N 366 
TRP CB  HB2  sing N N 367 
TRP CB  HB3  sing N N 368 
TRP CG  CD1  doub Y N 369 
TRP CG  CD2  sing Y N 370 
TRP CD1 NE1  sing Y N 371 
TRP CD1 HD1  sing N N 372 
TRP CD2 CE2  doub Y N 373 
TRP CD2 CE3  sing Y N 374 
TRP NE1 CE2  sing Y N 375 
TRP NE1 HE1  sing N N 376 
TRP CE2 CZ2  sing Y N 377 
TRP CE3 CZ3  doub Y N 378 
TRP CE3 HE3  sing N N 379 
TRP CZ2 CH2  doub Y N 380 
TRP CZ2 HZ2  sing N N 381 
TRP CZ3 CH2  sing Y N 382 
TRP CZ3 HZ3  sing N N 383 
TRP CH2 HH2  sing N N 384 
TRP OXT HXT  sing N N 385 
TYR N   CA   sing N N 386 
TYR N   H    sing N N 387 
TYR N   H2   sing N N 388 
TYR CA  C    sing N N 389 
TYR CA  CB   sing N N 390 
TYR CA  HA   sing N N 391 
TYR C   O    doub N N 392 
TYR C   OXT  sing N N 393 
TYR CB  CG   sing N N 394 
TYR CB  HB2  sing N N 395 
TYR CB  HB3  sing N N 396 
TYR CG  CD1  doub Y N 397 
TYR CG  CD2  sing Y N 398 
TYR CD1 CE1  sing Y N 399 
TYR CD1 HD1  sing N N 400 
TYR CD2 CE2  doub Y N 401 
TYR CD2 HD2  sing N N 402 
TYR CE1 CZ   doub Y N 403 
TYR CE1 HE1  sing N N 404 
TYR CE2 CZ   sing Y N 405 
TYR CE2 HE2  sing N N 406 
TYR CZ  OH   sing N N 407 
TYR OH  HH   sing N N 408 
TYR OXT HXT  sing N N 409 
VAL N   CA   sing N N 410 
VAL N   H    sing N N 411 
VAL N   H2   sing N N 412 
VAL CA  C    sing N N 413 
VAL CA  CB   sing N N 414 
VAL CA  HA   sing N N 415 
VAL C   O    doub N N 416 
VAL C   OXT  sing N N 417 
VAL CB  CG1  sing N N 418 
VAL CB  CG2  sing N N 419 
VAL CB  HB   sing N N 420 
VAL CG1 HG11 sing N N 421 
VAL CG1 HG12 sing N N 422 
VAL CG1 HG13 sing N N 423 
VAL CG2 HG21 sing N N 424 
VAL CG2 HG22 sing N N 425 
VAL CG2 HG23 sing N N 426 
VAL OXT HXT  sing N N 427 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          2697049 
_em_entity_assembly_naturalsource.organism             'Severe acute respiratory syndrome coronavirus 2' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         63 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ? 1  1 ? ? ? ? 
'IMAGE ACQUISITION'             ? 2  ? ? 1 ? ? 
MASKING                         ? 3  ? ? ? ? ? 
'CTF CORRECTION'                ? 4  1 ? ? ? ? 
'LAYERLINE INDEXING'            ? 5  ? ? ? ? ? 
'DIFFRACTION INDEXING'          ? 6  ? ? ? ? ? 
'MODEL FITTING'                 ? 7  ? ? ? ? ? 
'MODEL REFINEMENT'              ? 8  ? ? ? ? ? 
OTHER                           ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? ? ? 
CLASSIFICATION                  ? 12 1 ? ? ? ? 
RECONSTRUCTION                  ? 13 1 ? ? ? ? 
'VOLUME SELECTION'              ? 14 1 1 1 ? ? 
'SERIES ALIGNMENT'              ? 15 1 1 1 ? ? 
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ? ? 
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ? ? 
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ? ? 
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 1 ? ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'Howard Hughes Medical Institute (HHMI)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
6 NAG 1 n 
6 NAG 2 n 
6 BMA 3 n 
7 NAG 1 n 
7 NAG 2 n 
# 
_atom_sites.entry_id                    8VYF 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLN A 1 14  ? 253.661 270.011 195.910 1.00 23.72  ? 14   GLN A N   1 
ATOM   2    C CA  . GLN A 1 14  ? 252.865 269.929 197.130 1.00 23.86  ? 14   GLN A CA  1 
ATOM   3    C C   . GLN A 1 14  ? 253.661 269.301 198.279 1.00 23.97  ? 14   GLN A C   1 
ATOM   4    O O   . GLN A 1 14  ? 253.754 269.880 199.366 1.00 23.76  ? 14   GLN A O   1 
ATOM   5    C CB  . GLN A 1 14  ? 251.558 269.143 196.883 1.00 22.06  ? 14   GLN A CB  1 
ATOM   6    N N   . CYS A 1 15  ? 254.240 268.116 198.035 1.00 25.47  ? 15   CYS A N   1 
ATOM   7    C CA  . CYS A 1 15  ? 255.019 267.401 199.038 1.00 25.29  ? 15   CYS A CA  1 
ATOM   8    C C   . CYS A 1 15  ? 256.327 268.124 199.346 1.00 25.55  ? 15   CYS A C   1 
ATOM   9    O O   . CYS A 1 15  ? 256.962 268.693 198.453 1.00 25.81  ? 15   CYS A O   1 
ATOM   10   C CB  . CYS A 1 15  ? 255.330 265.967 198.571 1.00 25.43  ? 15   CYS A CB  1 
ATOM   11   S SG  . CYS A 1 15  ? 253.873 264.904 198.379 1.00 21.86  ? 15   CYS A SG  1 
ATOM   12   N N   . VAL A 1 16  ? 256.731 268.087 200.610 1.00 25.18  ? 16   VAL A N   1 
ATOM   13   C CA  . VAL A 1 16  ? 257.983 268.690 201.057 1.00 25.15  ? 16   VAL A CA  1 
ATOM   14   C C   . VAL A 1 16  ? 258.889 267.657 201.727 1.00 25.85  ? 16   VAL A C   1 
ATOM   15   O O   . VAL A 1 16  ? 258.467 266.949 202.640 1.00 24.71  ? 16   VAL A O   1 
ATOM   16   C CB  . VAL A 1 16  ? 257.689 269.829 202.049 1.00 26.26  ? 16   VAL A CB  1 
ATOM   17   C CG1 . VAL A 1 16  ? 258.981 270.419 202.582 1.00 26.98  ? 16   VAL A CG1 1 
ATOM   18   C CG2 . VAL A 1 16  ? 256.862 270.891 201.359 1.00 25.28  ? 16   VAL A CG2 1 
ATOM   19   N N   . ASN A 1 17  ? 260.147 267.592 201.278 1.00 26.51  ? 17   ASN A N   1 
ATOM   20   C CA  . ASN A 1 17  ? 261.136 266.692 201.848 1.00 27.07  ? 17   ASN A CA  1 
ATOM   21   C C   . ASN A 1 17  ? 261.748 267.304 203.112 1.00 27.10  ? 17   ASN A C   1 
ATOM   22   O O   . ASN A 1 17  ? 262.329 268.395 203.069 1.00 26.89  ? 17   ASN A O   1 
ATOM   23   C CB  . ASN A 1 17  ? 262.240 266.375 200.821 1.00 28.03  ? 17   ASN A CB  1 
ATOM   24   C CG  . ASN A 1 17  ? 261.919 265.158 199.948 1.00 29.10  ? 17   ASN A CG  1 
ATOM   25   O OD1 . ASN A 1 17  ? 260.980 264.397 200.206 1.00 28.68  ? 17   ASN A OD1 1 
ATOM   26   N ND2 . ASN A 1 17  ? 262.721 264.995 198.915 1.00 30.14  ? 17   ASN A ND2 1 
ATOM   27   N N   . LEU A 1 18  ? 261.599 266.605 204.239 1.00 26.88  ? 18   LEU A N   1 
ATOM   28   C CA  . LEU A 1 18  ? 262.064 267.078 205.542 1.00 25.21  ? 18   LEU A CA  1 
ATOM   29   C C   . LEU A 1 18  ? 263.150 266.154 206.078 1.00 25.33  ? 18   LEU A C   1 
ATOM   30   O O   . LEU A 1 18  ? 263.392 265.075 205.538 1.00 25.86  ? 18   LEU A O   1 
ATOM   31   C CB  . LEU A 1 18  ? 260.892 267.152 206.545 1.00 25.16  ? 18   LEU A CB  1 
ATOM   32   C CG  . LEU A 1 18  ? 259.689 268.095 206.149 1.00 25.81  ? 18   LEU A CG  1 
ATOM   33   C CD1 . LEU A 1 18  ? 258.572 267.988 207.212 1.00 22.67  ? 18   LEU A CD1 1 
ATOM   34   C CD2 . LEU A 1 18  ? 260.184 269.557 206.010 1.00 28.27  ? 18   LEU A CD2 1 
ATOM   35   N N   . ARG A 1 21  ? 265.851 264.343 210.203 1.00 21.41  ? 21   ARG A N   1 
ATOM   36   C CA  . ARG A 1 21  ? 264.977 263.570 211.078 1.00 20.64  ? 21   ARG A CA  1 
ATOM   37   C C   . ARG A 1 21  ? 265.798 262.689 212.026 1.00 21.30  ? 21   ARG A C   1 
ATOM   38   O O   . ARG A 1 21  ? 266.418 261.715 211.597 1.00 22.22  ? 21   ARG A O   1 
ATOM   39   C CB  . ARG A 1 21  ? 264.009 262.709 210.257 1.00 20.46  ? 21   ARG A CB  1 
ATOM   40   N N   . THR A 1 22  ? 265.807 263.052 213.316 1.00 21.47  ? 22   THR A N   1 
ATOM   41   C CA  . THR A 1 22  ? 266.551 262.329 214.352 1.00 21.97  ? 22   THR A CA  1 
ATOM   42   C C   . THR A 1 22  ? 265.622 261.481 215.211 1.00 21.37  ? 22   THR A C   1 
ATOM   43   O O   . THR A 1 22  ? 264.635 261.973 215.758 1.00 20.64  ? 22   THR A O   1 
ATOM   44   C CB  . THR A 1 22  ? 267.334 263.300 215.251 1.00 22.43  ? 22   THR A CB  1 
ATOM   45   N N   . GLN A 1 23  ? 265.963 260.201 215.355 1.00 21.65  ? 23   GLN A N   1 
ATOM   46   C CA  . GLN A 1 23  ? 265.171 259.303 216.185 1.00 20.55  ? 23   GLN A CA  1 
ATOM   47   C C   . GLN A 1 23  ? 265.820 259.112 217.549 1.00 18.89  ? 23   GLN A C   1 
ATOM   48   O O   . GLN A 1 23  ? 267.029 258.871 217.646 1.00 18.77  ? 23   GLN A O   1 
ATOM   49   C CB  . GLN A 1 23  ? 265.002 257.942 215.499 1.00 20.48  ? 23   GLN A CB  1 
ATOM   50   N N   . LEU A 1 24  ? 265.021 259.216 218.599 1.00 19.08  ? 24   LEU A N   1 
ATOM   51   C CA  . LEU A 1 24  ? 265.466 258.985 219.968 1.00 16.95  ? 24   LEU A CA  1 
ATOM   52   C C   . LEU A 1 24  ? 264.837 257.696 220.486 1.00 15.46  ? 24   LEU A C   1 
ATOM   53   O O   . LEU A 1 24  ? 263.802 257.277 219.970 1.00 14.89  ? 24   LEU A O   1 
ATOM   54   C CB  . LEU A 1 24  ? 265.068 260.173 220.858 1.00 17.03  ? 24   LEU A CB  1 
ATOM   55   N N   . PRO A 1 25  ? 265.444 257.044 221.485 1.00 15.13  ? 25   PRO A N   1 
ATOM   56   C CA  . PRO A 1 25  ? 264.911 255.890 222.180 1.00 12.84  ? 25   PRO A CA  1 
ATOM   57   C C   . PRO A 1 25  ? 263.619 256.280 222.889 1.00 12.12  ? 25   PRO A C   1 
ATOM   58   O O   . PRO A 1 25  ? 263.469 257.430 223.304 1.00 12.28  ? 25   PRO A O   1 
ATOM   59   C CB  . PRO A 1 25  ? 266.046 255.523 223.150 1.00 12.87  ? 25   PRO A CB  1 
ATOM   60   C CG  . PRO A 1 25  ? 266.875 256.790 223.285 1.00 13.98  ? 25   PRO A CG  1 
ATOM   61   C CD  . PRO A 1 25  ? 266.769 257.476 221.937 1.00 14.88  ? 25   PRO A CD  1 
ATOM   62   N N   . PRO A 1 26  ? 262.683 255.340 223.026 1.00 11.27  ? 26   PRO A N   1 
ATOM   63   C CA  . PRO A 1 26  ? 261.340 255.505 223.551 1.00 10.02  ? 26   PRO A CA  1 
ATOM   64   C C   . PRO A 1 26  ? 261.308 255.741 225.051 1.00 9.50   ? 26   PRO A C   1 
ATOM   65   O O   . PRO A 1 26  ? 262.144 255.223 225.792 1.00 9.98   ? 26   PRO A O   1 
ATOM   66   C CB  . PRO A 1 26  ? 260.693 254.163 223.201 1.00 8.93   ? 26   PRO A CB  1 
ATOM   67   C CG  . PRO A 1 26  ? 261.849 253.183 223.177 1.00 9.08   ? 26   PRO A CG  1 
ATOM   68   C CD  . PRO A 1 26  ? 263.014 253.972 222.630 1.00 10.49  ? 26   PRO A CD  1 
ATOM   69   N N   . ALA A 1 27  ? 260.286 256.461 225.494 1.00 8.52   ? 27   ALA A N   1 
ATOM   70   C CA  . ALA A 1 27  ? 259.993 256.616 226.908 1.00 7.37   ? 27   ALA A CA  1 
ATOM   71   C C   . ALA A 1 27  ? 258.680 255.917 227.211 1.00 7.20   ? 27   ALA A C   1 
ATOM   72   O O   . ALA A 1 27  ? 257.878 255.696 226.305 1.00 7.23   ? 27   ALA A O   1 
ATOM   73   C CB  . ALA A 1 27  ? 259.927 258.087 227.283 1.00 8.69   ? 27   ALA A CB  1 
ATOM   74   N N   . TYR A 1 28  ? 258.469 255.533 228.464 1.00 7.30   ? 28   TYR A N   1 
ATOM   75   C CA  . TYR A 1 28  ? 257.250 254.816 228.816 1.00 6.21   ? 28   TYR A CA  1 
ATOM   76   C C   . TYR A 1 28  ? 256.541 255.428 230.016 1.00 6.09   ? 28   TYR A C   1 
ATOM   77   O O   . TYR A 1 28  ? 257.179 255.964 230.921 1.00 6.74   ? 28   TYR A O   1 
ATOM   78   C CB  . TYR A 1 28  ? 257.573 253.349 229.089 1.00 6.48   ? 28   TYR A CB  1 
ATOM   79   C CG  . TYR A 1 28  ? 258.196 252.650 227.908 1.00 6.72   ? 28   TYR A CG  1 
ATOM   80   C CD1 . TYR A 1 28  ? 257.400 252.001 226.982 1.00 6.62   ? 28   TYR A CD1 1 
ATOM   81   C CD2 . TYR A 1 28  ? 259.571 252.666 227.748 1.00 7.70   ? 28   TYR A CD2 1 
ATOM   82   C CE1 . TYR A 1 28  ? 257.980 251.366 225.903 1.00 6.65   ? 28   TYR A CE1 1 
ATOM   83   C CE2 . TYR A 1 28  ? 260.148 252.035 226.671 1.00 7.66   ? 28   TYR A CE2 1 
ATOM   84   C CZ  . TYR A 1 28  ? 259.359 251.386 225.753 1.00 7.22   ? 28   TYR A CZ  1 
ATOM   85   O OH  . TYR A 1 28  ? 259.938 250.753 224.681 1.00 7.26   ? 28   TYR A OH  1 
ATOM   86   N N   . THR A 1 29  ? 255.217 255.308 230.028 1.00 5.79   ? 29   THR A N   1 
ATOM   87   C CA  . THR A 1 29  ? 254.409 255.762 231.152 1.00 5.29   ? 29   THR A CA  1 
ATOM   88   C C   . THR A 1 29  ? 253.436 254.676 231.606 1.00 5.34   ? 29   THR A C   1 
ATOM   89   O O   . THR A 1 29  ? 253.277 253.653 230.942 1.00 5.19   ? 29   THR A O   1 
ATOM   90   C CB  . THR A 1 29  ? 253.635 257.041 230.792 1.00 5.72   ? 29   THR A CB  1 
ATOM   91   O OG1 . THR A 1 29  ? 253.035 257.582 231.972 1.00 6.62   ? 29   THR A OG1 1 
ATOM   92   C CG2 . THR A 1 29  ? 252.554 256.738 229.778 1.00 6.18   ? 29   THR A CG2 1 
ATOM   93   N N   . ASN A 1 30  ? 252.787 254.915 232.741 1.00 5.15   ? 30   ASN A N   1 
ATOM   94   C CA  . ASN A 1 30  ? 251.858 253.963 233.344 1.00 4.82   ? 30   ASN A CA  1 
ATOM   95   C C   . ASN A 1 30  ? 250.412 254.288 232.973 1.00 4.99   ? 30   ASN A C   1 
ATOM   96   O O   . ASN A 1 30  ? 249.915 255.371 233.285 1.00 4.97   ? 30   ASN A O   1 
ATOM   97   C CB  . ASN A 1 30  ? 252.051 253.951 234.851 1.00 4.88   ? 30   ASN A CB  1 
ATOM   98   C CG  . ASN A 1 30  ? 251.346 252.831 235.548 1.00 4.53   ? 30   ASN A CG  1 
ATOM   99   O OD1 . ASN A 1 30  ? 250.305 252.337 235.106 1.00 4.45   ? 30   ASN A OD1 1 
ATOM   100  N ND2 . ASN A 1 30  ? 251.909 252.412 236.655 1.00 4.56   ? 30   ASN A ND2 1 
ATOM   101  N N   . SER A 1 31  ? 249.749 253.369 232.280 1.00 4.73   ? 31   SER A N   1 
ATOM   102  C CA  . SER A 1 31  ? 248.374 253.576 231.827 1.00 4.30   ? 31   SER A CA  1 
ATOM   103  C C   . SER A 1 31  ? 247.362 253.550 232.963 1.00 4.69   ? 31   SER A C   1 
ATOM   104  O O   . SER A 1 31  ? 246.203 253.933 232.782 1.00 4.80   ? 31   SER A O   1 
ATOM   105  C CB  . SER A 1 31  ? 247.987 252.514 230.832 1.00 4.40   ? 31   SER A CB  1 
ATOM   106  O OG  . SER A 1 31  ? 247.943 251.258 231.439 1.00 4.79   ? 31   SER A OG  1 
ATOM   107  N N   . PHE A 1 32  ? 247.782 253.058 234.118 1.00 4.59   ? 32   PHE A N   1 
ATOM   108  C CA  . PHE A 1 32  ? 246.898 252.899 235.261 1.00 4.62   ? 32   PHE A CA  1 
ATOM   109  C C   . PHE A 1 32  ? 245.615 252.173 234.876 1.00 4.45   ? 32   PHE A C   1 
ATOM   110  O O   . PHE A 1 32  ? 245.650 251.013 234.469 1.00 4.45   ? 32   PHE A O   1 
ATOM   111  C CB  . PHE A 1 32  ? 246.574 254.256 235.886 1.00 4.61   ? 32   PHE A CB  1 
ATOM   112  C CG  . PHE A 1 32  ? 247.753 254.899 236.538 1.00 4.63   ? 32   PHE A CG  1 
ATOM   113  C CD1 . PHE A 1 32  ? 248.185 254.480 237.781 1.00 4.44   ? 32   PHE A CD1 1 
ATOM   114  C CD2 . PHE A 1 32  ? 248.432 255.924 235.913 1.00 5.06   ? 32   PHE A CD2 1 
ATOM   115  C CE1 . PHE A 1 32  ? 249.275 255.070 238.382 1.00 4.36   ? 32   PHE A CE1 1 
ATOM   116  C CE2 . PHE A 1 32  ? 249.520 256.517 236.509 1.00 4.95   ? 32   PHE A CE2 1 
ATOM   117  C CZ  . PHE A 1 32  ? 249.943 256.088 237.746 1.00 4.41   ? 32   PHE A CZ  1 
ATOM   118  N N   . THR A 1 33  ? 244.480 252.846 235.016 1.00 4.35   ? 33   THR A N   1 
ATOM   119  C CA  . THR A 1 33  ? 243.193 252.215 234.762 1.00 4.38   ? 33   THR A CA  1 
ATOM   120  C C   . THR A 1 33  ? 242.415 252.903 233.646 1.00 4.25   ? 33   THR A C   1 
ATOM   121  O O   . THR A 1 33  ? 241.183 252.890 233.634 1.00 4.61   ? 33   THR A O   1 
ATOM   122  C CB  . THR A 1 33  ? 242.352 252.194 236.043 1.00 4.60   ? 33   THR A CB  1 
ATOM   123  O OG1 . THR A 1 33  ? 242.192 253.532 236.527 1.00 5.01   ? 33   THR A OG1 1 
ATOM   124  C CG2 . THR A 1 33  ? 243.046 251.357 237.103 1.00 4.69   ? 33   THR A CG2 1 
ATOM   125  N N   . ARG A 1 34  ? 243.131 253.525 232.719 1.00 4.11   ? 34   ARG A N   1 
ATOM   126  C CA  . ARG A 1 34  ? 242.499 254.253 231.627 1.00 3.59   ? 34   ARG A CA  1 
ATOM   127  C C   . ARG A 1 34  ? 242.410 253.415 230.357 1.00 3.29   ? 34   ARG A C   1 
ATOM   128  O O   . ARG A 1 34  ? 243.118 252.422 230.210 1.00 3.40   ? 34   ARG A O   1 
ATOM   129  C CB  . ARG A 1 34  ? 243.264 255.528 231.340 1.00 3.80   ? 34   ARG A CB  1 
ATOM   130  C CG  . ARG A 1 34  ? 243.398 256.432 232.537 1.00 4.53   ? 34   ARG A CG  1 
ATOM   131  C CD  . ARG A 1 34  ? 243.853 257.772 232.171 1.00 5.05   ? 34   ARG A CD  1 
ATOM   132  N NE  . ARG A 1 34  ? 242.783 258.550 231.571 1.00 5.11   ? 34   ARG A NE  1 
ATOM   133  C CZ  . ARG A 1 34  ? 241.835 259.214 232.266 1.00 5.14   ? 34   ARG A CZ  1 
ATOM   134  N NH1 . ARG A 1 34  ? 240.924 259.906 231.626 1.00 5.40   ? 34   ARG A NH1 1 
ATOM   135  N NH2 . ARG A 1 34  ? 241.823 259.169 233.589 1.00 5.42   ? 34   ARG A NH2 1 
ATOM   136  N N   . GLY A 1 35  ? 241.540 253.826 229.434 1.00 3.18   ? 35   GLY A N   1 
ATOM   137  C CA  . GLY A 1 35  ? 241.403 253.142 228.149 1.00 2.63   ? 35   GLY A CA  1 
ATOM   138  C C   . GLY A 1 35  ? 240.130 252.302 228.074 1.00 3.21   ? 35   GLY A C   1 
ATOM   139  O O   . GLY A 1 35  ? 239.925 251.555 227.117 1.00 3.34   ? 35   GLY A O   1 
ATOM   140  N N   . VAL A 1 36  ? 239.280 252.433 229.086 1.00 3.56   ? 36   VAL A N   1 
ATOM   141  C CA  . VAL A 1 36  ? 238.003 251.730 229.138 1.00 3.65   ? 36   VAL A CA  1 
ATOM   142  C C   . VAL A 1 36  ? 236.935 252.508 228.383 1.00 3.77   ? 36   VAL A C   1 
ATOM   143  O O   . VAL A 1 36  ? 236.919 253.736 228.412 1.00 3.90   ? 36   VAL A O   1 
ATOM   144  C CB  . VAL A 1 36  ? 237.573 251.495 230.599 1.00 3.91   ? 36   VAL A CB  1 
ATOM   145  C CG1 . VAL A 1 36  ? 236.181 250.874 230.658 1.00 4.69   ? 36   VAL A CG1 1 
ATOM   146  C CG2 . VAL A 1 36  ? 238.585 250.580 231.269 1.00 4.47   ? 36   VAL A CG2 1 
ATOM   147  N N   . TYR A 1 37  ? 236.077 251.789 227.672 1.00 4.06   ? 37   TYR A N   1 
ATOM   148  C CA  . TYR A 1 37  ? 235.027 252.398 226.866 1.00 4.13   ? 37   TYR A CA  1 
ATOM   149  C C   . TYR A 1 37  ? 233.742 251.588 226.933 1.00 4.65   ? 37   TYR A C   1 
ATOM   150  O O   . TYR A 1 37  ? 233.756 250.417 227.310 1.00 4.97   ? 37   TYR A O   1 
ATOM   151  C CB  . TYR A 1 37  ? 235.489 252.525 225.418 1.00 3.83   ? 37   TYR A CB  1 
ATOM   152  C CG  . TYR A 1 37  ? 235.786 251.207 224.783 1.00 3.84   ? 37   TYR A CG  1 
ATOM   153  C CD1 . TYR A 1 37  ? 234.788 250.509 224.146 1.00 4.21   ? 37   TYR A CD1 1 
ATOM   154  C CD2 . TYR A 1 37  ? 237.062 250.690 224.843 1.00 3.67   ? 37   TYR A CD2 1 
ATOM   155  C CE1 . TYR A 1 37  ? 235.058 249.294 223.576 1.00 4.03   ? 37   TYR A CE1 1 
ATOM   156  C CE2 . TYR A 1 37  ? 237.335 249.475 224.272 1.00 3.64   ? 37   TYR A CE2 1 
ATOM   157  C CZ  . TYR A 1 37  ? 236.335 248.777 223.642 1.00 3.61   ? 37   TYR A CZ  1 
ATOM   158  O OH  . TYR A 1 37  ? 236.599 247.560 223.077 1.00 3.82   ? 37   TYR A OH  1 
ATOM   159  N N   . TYR A 1 38  ? 232.632 252.210 226.547 1.00 4.74   ? 38   TYR A N   1 
ATOM   160  C CA  . TYR A 1 38  ? 231.343 251.525 226.516 1.00 5.22   ? 38   TYR A CA  1 
ATOM   161  C C   . TYR A 1 38  ? 231.323 250.484 225.397 1.00 5.52   ? 38   TYR A C   1 
ATOM   162  O O   . TYR A 1 38  ? 231.402 250.850 224.226 1.00 5.33   ? 38   TYR A O   1 
ATOM   163  C CB  . TYR A 1 38  ? 230.211 252.528 226.288 1.00 4.98   ? 38   TYR A CB  1 
ATOM   164  C CG  . TYR A 1 38  ? 229.928 253.436 227.453 1.00 5.13   ? 38   TYR A CG  1 
ATOM   165  C CD1 . TYR A 1 38  ? 230.670 254.581 227.626 1.00 4.65   ? 38   TYR A CD1 1 
ATOM   166  C CD2 . TYR A 1 38  ? 228.912 253.137 228.335 1.00 6.22   ? 38   TYR A CD2 1 
ATOM   167  C CE1 . TYR A 1 38  ? 230.410 255.423 228.677 1.00 4.72   ? 38   TYR A CE1 1 
ATOM   168  C CE2 . TYR A 1 38  ? 228.648 253.984 229.388 1.00 8.59   ? 38   TYR A CE2 1 
ATOM   169  C CZ  . TYR A 1 38  ? 229.396 255.120 229.558 1.00 7.15   ? 38   TYR A CZ  1 
ATOM   170  O OH  . TYR A 1 38  ? 229.131 255.962 230.600 1.00 8.99   ? 38   TYR A OH  1 
ATOM   171  N N   . PRO A 1 39  ? 231.193 249.193 225.726 1.00 6.00   ? 39   PRO A N   1 
ATOM   172  C CA  . PRO A 1 39  ? 231.310 248.063 224.819 1.00 6.17   ? 39   PRO A CA  1 
ATOM   173  C C   . PRO A 1 39  ? 230.186 248.023 223.787 1.00 6.99   ? 39   PRO A C   1 
ATOM   174  O O   . PRO A 1 39  ? 230.354 247.477 222.697 1.00 7.08   ? 39   PRO A O   1 
ATOM   175  C CB  . PRO A 1 39  ? 231.242 246.867 225.775 1.00 6.37   ? 39   PRO A CB  1 
ATOM   176  C CG  . PRO A 1 39  ? 230.482 247.378 226.984 1.00 6.81   ? 39   PRO A CG  1 
ATOM   177  C CD  . PRO A 1 39  ? 230.857 248.837 227.104 1.00 6.38   ? 39   PRO A CD  1 
ATOM   178  N N   . ASP A 1 40  ? 229.049 248.625 224.119 1.00 7.21   ? 40   ASP A N   1 
ATOM   179  C CA  . ASP A 1 40  ? 227.919 248.682 223.203 1.00 7.68   ? 40   ASP A CA  1 
ATOM   180  C C   . ASP A 1 40  ? 227.034 249.881 223.519 1.00 7.95   ? 40   ASP A C   1 
ATOM   181  O O   . ASP A 1 40  ? 227.391 250.729 224.337 1.00 7.50   ? 40   ASP A O   1 
ATOM   182  C CB  . ASP A 1 40  ? 227.114 247.376 223.231 1.00 7.60   ? 40   ASP A CB  1 
ATOM   183  C CG  . ASP A 1 40  ? 226.467 247.080 224.565 1.00 8.54   ? 40   ASP A CG  1 
ATOM   184  O OD1 . ASP A 1 40  ? 226.241 248.001 225.312 1.00 8.75   ? 40   ASP A OD1 1 
ATOM   185  O OD2 . ASP A 1 40  ? 226.190 245.930 224.826 1.00 9.22   ? 40   ASP A OD2 1 
ATOM   186  N N   . LYS A 1 41  ? 225.899 249.974 222.837 1.00 8.29   ? 41   LYS A N   1 
ATOM   187  C CA  . LYS A 1 41  ? 225.019 251.128 222.969 1.00 8.70   ? 41   LYS A CA  1 
ATOM   188  C C   . LYS A 1 41  ? 223.791 250.837 223.824 1.00 9.32   ? 41   LYS A C   1 
ATOM   189  O O   . LYS A 1 41  ? 222.806 251.573 223.775 1.00 10.33  ? 41   LYS A O   1 
ATOM   190  C CB  . LYS A 1 41  ? 224.587 251.613 221.587 1.00 9.23   ? 41   LYS A CB  1 
ATOM   191  C CG  . LYS A 1 41  ? 225.731 252.113 220.720 1.00 8.67   ? 41   LYS A CG  1 
ATOM   192  C CD  . LYS A 1 41  ? 225.230 252.597 219.371 1.00 8.82   ? 41   LYS A CD  1 
ATOM   193  C CE  . LYS A 1 41  ? 226.373 253.095 218.501 1.00 8.24   ? 41   LYS A CE  1 
ATOM   194  N NZ  . LYS A 1 41  ? 225.895 253.544 217.165 1.00 8.06   ? 41   LYS A NZ  1 
ATOM   195  N N   . VAL A 1 42  ? 223.835 249.747 224.579 1.00 9.33   ? 42   VAL A N   1 
ATOM   196  C CA  . VAL A 1 42  ? 222.706 249.365 225.416 1.00 10.49  ? 42   VAL A CA  1 
ATOM   197  C C   . VAL A 1 42  ? 222.779 250.051 226.770 1.00 11.16  ? 42   VAL A C   1 
ATOM   198  O O   . VAL A 1 42  ? 223.811 250.018 227.439 1.00 11.02  ? 42   VAL A O   1 
ATOM   199  C CB  . VAL A 1 42  ? 222.675 247.838 225.599 1.00 10.36  ? 42   VAL A CB  1 
ATOM   200  C CG1 . VAL A 1 42  ? 221.556 247.436 226.550 1.00 11.45  ? 42   VAL A CG1 1 
ATOM   201  C CG2 . VAL A 1 42  ? 222.491 247.176 224.245 1.00 9.44   ? 42   VAL A CG2 1 
ATOM   202  N N   . PHE A 1 43  ? 221.685 250.682 227.175 1.00 11.57  ? 43   PHE A N   1 
ATOM   203  C CA  . PHE A 1 43  ? 221.655 251.360 228.462 1.00 12.55  ? 43   PHE A CA  1 
ATOM   204  C C   . PHE A 1 43  ? 221.573 250.369 229.610 1.00 12.90  ? 43   PHE A C   1 
ATOM   205  O O   . PHE A 1 43  ? 220.733 249.469 229.612 1.00 13.26  ? 43   PHE A O   1 
ATOM   206  C CB  . PHE A 1 43  ? 220.471 252.320 228.554 1.00 12.29  ? 43   PHE A CB  1 
ATOM   207  C CG  . PHE A 1 43  ? 220.414 253.046 229.868 1.00 13.00  ? 43   PHE A CG  1 
ATOM   208  C CD1 . PHE A 1 43  ? 221.206 254.158 230.099 1.00 13.44  ? 43   PHE A CD1 1 
ATOM   209  C CD2 . PHE A 1 43  ? 219.580 252.607 230.884 1.00 13.71  ? 43   PHE A CD2 1 
ATOM   210  C CE1 . PHE A 1 43  ? 221.163 254.816 231.311 1.00 13.77  ? 43   PHE A CE1 1 
ATOM   211  C CE2 . PHE A 1 43  ? 219.537 253.263 232.097 1.00 14.04  ? 43   PHE A CE2 1 
ATOM   212  C CZ  . PHE A 1 43  ? 220.330 254.369 232.309 1.00 14.02  ? 43   PHE A CZ  1 
ATOM   213  N N   . ARG A 1 44  ? 222.432 250.563 230.600 1.00 13.29  ? 44   ARG A N   1 
ATOM   214  C CA  . ARG A 1 44  ? 222.428 249.756 231.810 1.00 13.77  ? 44   ARG A CA  1 
ATOM   215  C C   . ARG A 1 44  ? 222.614 250.664 233.009 1.00 14.02  ? 44   ARG A C   1 
ATOM   216  O O   . ARG A 1 44  ? 223.252 251.706 232.893 1.00 14.72  ? 44   ARG A O   1 
ATOM   217  C CB  . ARG A 1 44  ? 223.543 248.726 231.780 1.00 13.43  ? 44   ARG A CB  1 
ATOM   218  C CG  . ARG A 1 44  ? 223.460 247.720 230.654 1.00 12.79  ? 44   ARG A CG  1 
ATOM   219  C CD  . ARG A 1 44  ? 224.597 246.772 230.700 1.00 12.39  ? 44   ARG A CD  1 
ATOM   220  N NE  . ARG A 1 44  ? 224.550 245.810 229.617 1.00 11.05  ? 44   ARG A NE  1 
ATOM   221  C CZ  . ARG A 1 44  ? 224.976 246.060 228.361 1.00 10.92  ? 44   ARG A CZ  1 
ATOM   222  N NH1 . ARG A 1 44  ? 224.914 245.123 227.443 1.00 10.70  ? 44   ARG A NH1 1 
ATOM   223  N NH2 . ARG A 1 44  ? 225.458 247.252 228.052 1.00 10.90  ? 44   ARG A NH2 1 
ATOM   224  N N   . SER A 1 45  ? 222.078 250.270 234.158 1.00 14.57  ? 45   SER A N   1 
ATOM   225  C CA  . SER A 1 45  ? 222.261 251.056 235.373 1.00 14.73  ? 45   SER A CA  1 
ATOM   226  C C   . SER A 1 45  ? 222.239 250.190 236.622 1.00 14.62  ? 45   SER A C   1 
ATOM   227  O O   . SER A 1 45  ? 221.603 249.136 236.649 1.00 14.85  ? 45   SER A O   1 
ATOM   228  C CB  . SER A 1 45  ? 221.191 252.127 235.465 1.00 14.85  ? 45   SER A CB  1 
ATOM   229  O OG  . SER A 1 45  ? 219.909 251.560 235.534 1.00 14.88  ? 45   SER A OG  1 
ATOM   230  N N   . SER A 1 46  ? 222.922 250.659 237.663 1.00 15.55  ? 46   SER A N   1 
ATOM   231  C CA  . SER A 1 46  ? 222.943 249.979 238.955 1.00 16.02  ? 46   SER A CA  1 
ATOM   232  C C   . SER A 1 46  ? 223.249 248.494 238.803 1.00 15.02  ? 46   SER A C   1 
ATOM   233  O O   . SER A 1 46  ? 222.523 247.646 239.323 1.00 15.39  ? 46   SER A O   1 
ATOM   234  C CB  . SER A 1 46  ? 221.611 250.159 239.660 1.00 14.94  ? 46   SER A CB  1 
ATOM   235  O OG  . SER A 1 46  ? 221.356 251.512 239.908 1.00 15.41  ? 46   SER A OG  1 
ATOM   236  N N   . VAL A 1 47  ? 224.299 248.179 238.053 1.00 15.11  ? 47   VAL A N   1 
ATOM   237  C CA  . VAL A 1 47  ? 224.617 246.787 237.764 1.00 14.98  ? 47   VAL A CA  1 
ATOM   238  C C   . VAL A 1 47  ? 226.097 246.563 237.489 1.00 13.59  ? 47   VAL A C   1 
ATOM   239  O O   . VAL A 1 47  ? 226.766 247.405 236.887 1.00 15.29  ? 47   VAL A O   1 
ATOM   240  C CB  . VAL A 1 47  ? 223.776 246.309 236.556 1.00 14.53  ? 47   VAL A CB  1 
ATOM   241  C CG1 . VAL A 1 47  ? 224.152 247.093 235.305 1.00 14.00  ? 47   VAL A CG1 1 
ATOM   242  C CG2 . VAL A 1 47  ? 223.975 244.811 236.323 1.00 14.64  ? 47   VAL A CG2 1 
ATOM   243  N N   . LEU A 1 48  ? 226.587 245.389 237.871 1.00 13.79  ? 48   LEU A N   1 
ATOM   244  C CA  . LEU A 1 48  ? 227.930 244.967 237.501 1.00 13.11  ? 48   LEU A CA  1 
ATOM   245  C C   . LEU A 1 48  ? 227.854 244.053 236.285 1.00 12.31  ? 48   LEU A C   1 
ATOM   246  O O   . LEU A 1 48  ? 227.285 242.962 236.350 1.00 12.36  ? 48   LEU A O   1 
ATOM   247  C CB  . LEU A 1 48  ? 228.609 244.234 238.662 1.00 13.19  ? 48   LEU A CB  1 
ATOM   248  C CG  . LEU A 1 48  ? 228.717 245.002 239.986 1.00 14.17  ? 48   LEU A CG  1 
ATOM   249  C CD1 . LEU A 1 48  ? 229.394 244.113 241.017 1.00 16.34  ? 48   LEU A CD1 1 
ATOM   250  C CD2 . LEU A 1 48  ? 229.506 246.281 239.771 1.00 13.81  ? 48   LEU A CD2 1 
ATOM   251  N N   . HIS A 1 49  ? 228.387 244.522 235.166 1.00 11.47  ? 49   HIS A N   1 
ATOM   252  C CA  . HIS A 1 49  ? 228.271 243.809 233.900 1.00 11.36  ? 49   HIS A CA  1 
ATOM   253  C C   . HIS A 1 49  ? 229.611 243.269 233.428 1.00 9.93   ? 49   HIS A C   1 
ATOM   254  O O   . HIS A 1 49  ? 230.587 244.011 233.312 1.00 11.61  ? 49   HIS A O   1 
ATOM   255  C CB  . HIS A 1 49  ? 227.680 244.730 232.831 1.00 10.77  ? 49   HIS A CB  1 
ATOM   256  C CG  . HIS A 1 49  ? 227.561 244.102 231.484 1.00 10.38  ? 49   HIS A CG  1 
ATOM   257  N ND1 . HIS A 1 49  ? 226.646 243.111 231.203 1.00 10.51  ? 49   HIS A ND1 1 
ATOM   258  C CD2 . HIS A 1 49  ? 228.236 244.330 230.334 1.00 10.14  ? 49   HIS A CD2 1 
ATOM   259  C CE1 . HIS A 1 49  ? 226.768 242.752 229.936 1.00 11.27  ? 49   HIS A CE1 1 
ATOM   260  N NE2 . HIS A 1 49  ? 227.724 243.478 229.388 1.00 9.92   ? 49   HIS A NE2 1 
ATOM   261  N N   . SER A 1 50  ? 229.663 241.970 233.165 1.00 10.33  ? 50   SER A N   1 
ATOM   262  C CA  . SER A 1 50  ? 230.892 241.336 232.705 1.00 9.47   ? 50   SER A CA  1 
ATOM   263  C C   . SER A 1 50  ? 230.910 241.228 231.187 1.00 8.92   ? 50   SER A C   1 
ATOM   264  O O   . SER A 1 50  ? 229.964 240.723 230.581 1.00 9.29   ? 50   SER A O   1 
ATOM   265  C CB  . SER A 1 50  ? 231.042 239.962 233.326 1.00 9.95   ? 50   SER A CB  1 
ATOM   266  O OG  . SER A 1 50  ? 232.191 239.318 232.848 1.00 9.19   ? 50   SER A OG  1 
ATOM   267  N N   . THR A 1 51  ? 231.983 241.718 230.572 1.00 8.22   ? 51   THR A N   1 
ATOM   268  C CA  . THR A 1 51  ? 232.096 241.694 229.120 1.00 7.98   ? 51   THR A CA  1 
ATOM   269  C C   . THR A 1 51  ? 233.508 241.360 228.657 1.00 7.07   ? 51   THR A C   1 
ATOM   270  O O   . THR A 1 51  ? 234.492 241.710 229.311 1.00 7.28   ? 51   THR A O   1 
ATOM   271  C CB  . THR A 1 51  ? 231.674 243.050 228.521 1.00 7.38   ? 51   THR A CB  1 
ATOM   272  O OG1 . THR A 1 51  ? 231.698 242.967 227.094 1.00 7.23   ? 51   THR A OG1 1 
ATOM   273  C CG2 . THR A 1 51  ? 232.619 244.156 228.978 1.00 6.99   ? 51   THR A CG2 1 
ATOM   274  N N   . GLN A 1 52  ? 233.604 240.705 227.503 1.00 6.56   ? 52   GLN A N   1 
ATOM   275  C CA  . GLN A 1 52  ? 234.892 240.397 226.898 1.00 5.12   ? 52   GLN A CA  1 
ATOM   276  C C   . GLN A 1 52  ? 235.068 241.178 225.607 1.00 4.95   ? 52   GLN A C   1 
ATOM   277  O O   . GLN A 1 52  ? 234.253 241.072 224.690 1.00 5.26   ? 52   GLN A O   1 
ATOM   278  C CB  . GLN A 1 52  ? 235.023 238.897 226.628 1.00 5.26   ? 52   GLN A CB  1 
ATOM   279  C CG  . GLN A 1 52  ? 236.366 238.485 226.051 1.00 4.88   ? 52   GLN A CG  1 
ATOM   280  C CD  . GLN A 1 52  ? 236.470 236.988 225.853 1.00 4.57   ? 52   GLN A CD  1 
ATOM   281  O OE1 . GLN A 1 52  ? 235.465 236.309 225.629 1.00 4.00   ? 52   GLN A OE1 1 
ATOM   282  N NE2 . GLN A 1 52  ? 237.686 236.460 225.935 1.00 3.57   ? 52   GLN A NE2 1 
ATOM   283  N N   . ASP A 1 53  ? 236.116 241.988 225.554 1.00 4.79   ? 53   ASP A N   1 
ATOM   284  C CA  . ASP A 1 53  ? 236.369 242.838 224.397 1.00 4.31   ? 53   ASP A CA  1 
ATOM   285  C C   . ASP A 1 53  ? 237.823 243.288 224.379 1.00 3.72   ? 53   ASP A C   1 
ATOM   286  O O   . ASP A 1 53  ? 238.602 242.933 225.265 1.00 4.22   ? 53   ASP A O   1 
ATOM   287  C CB  . ASP A 1 53  ? 235.427 244.049 224.405 1.00 4.12   ? 53   ASP A CB  1 
ATOM   288  C CG  . ASP A 1 53  ? 235.066 244.558 223.014 1.00 4.08   ? 53   ASP A CG  1 
ATOM   289  O OD1 . ASP A 1 53  ? 235.861 244.405 222.117 1.00 4.09   ? 53   ASP A OD1 1 
ATOM   290  O OD2 . ASP A 1 53  ? 234.000 245.104 222.865 1.00 4.61   ? 53   ASP A OD2 1 
ATOM   291  N N   . LEU A 1 54  ? 238.188 244.077 223.380 1.00 3.74   ? 54   LEU A N   1 
ATOM   292  C CA  . LEU A 1 54  ? 239.545 244.589 223.291 1.00 3.44   ? 54   LEU A CA  1 
ATOM   293  C C   . LEU A 1 54  ? 239.706 245.838 224.142 1.00 3.38   ? 54   LEU A C   1 
ATOM   294  O O   . LEU A 1 54  ? 239.125 246.882 223.854 1.00 3.41   ? 54   LEU A O   1 
ATOM   295  C CB  . LEU A 1 54  ? 239.890 244.913 221.833 1.00 3.18   ? 54   LEU A CB  1 
ATOM   296  C CG  . LEU A 1 54  ? 239.850 243.741 220.845 1.00 3.03   ? 54   LEU A CG  1 
ATOM   297  C CD1 . LEU A 1 54  ? 240.026 244.279 219.440 1.00 2.67   ? 54   LEU A CD1 1 
ATOM   298  C CD2 . LEU A 1 54  ? 240.956 242.750 221.182 1.00 2.96   ? 54   LEU A CD2 1 
ATOM   299  N N   . PHE A 1 55  ? 240.484 245.716 225.206 1.00 3.26   ? 55   PHE A N   1 
ATOM   300  C CA  . PHE A 1 55  ? 240.685 246.805 226.150 1.00 3.49   ? 55   PHE A CA  1 
ATOM   301  C C   . PHE A 1 55  ? 242.164 247.017 226.395 1.00 3.19   ? 55   PHE A C   1 
ATOM   302  O O   . PHE A 1 55  ? 242.959 246.095 226.234 1.00 3.21   ? 55   PHE A O   1 
ATOM   303  C CB  . PHE A 1 55  ? 240.009 246.514 227.489 1.00 4.67   ? 55   PHE A CB  1 
ATOM   304  C CG  . PHE A 1 55  ? 238.506 246.434 227.469 1.00 4.63   ? 55   PHE A CG  1 
ATOM   305  C CD1 . PHE A 1 55  ? 237.736 247.584 227.485 1.00 4.62   ? 55   PHE A CD1 1 
ATOM   306  C CD2 . PHE A 1 55  ? 237.864 245.213 227.479 1.00 4.71   ? 55   PHE A CD2 1 
ATOM   307  C CE1 . PHE A 1 55  ? 236.359 247.511 227.499 1.00 4.40   ? 55   PHE A CE1 1 
ATOM   308  C CE2 . PHE A 1 55  ? 236.493 245.137 227.499 1.00 4.84   ? 55   PHE A CE2 1 
ATOM   309  C CZ  . PHE A 1 55  ? 235.739 246.289 227.508 1.00 5.10   ? 55   PHE A CZ  1 
ATOM   310  N N   . LEU A 1 56  ? 242.535 248.223 226.803 1.00 3.16   ? 56   LEU A N   1 
ATOM   311  C CA  . LEU A 1 56  ? 243.912 248.477 227.196 1.00 3.20   ? 56   LEU A CA  1 
ATOM   312  C C   . LEU A 1 56  ? 244.138 247.841 228.572 1.00 3.71   ? 56   LEU A C   1 
ATOM   313  O O   . LEU A 1 56  ? 243.451 248.209 229.523 1.00 4.06   ? 56   LEU A O   1 
ATOM   314  C CB  . LEU A 1 56  ? 244.162 249.991 227.273 1.00 2.97   ? 56   LEU A CB  1 
ATOM   315  C CG  . LEU A 1 56  ? 245.611 250.440 227.530 1.00 2.79   ? 56   LEU A CG  1 
ATOM   316  C CD1 . LEU A 1 56  ? 246.465 250.131 226.314 1.00 2.65   ? 56   LEU A CD1 1 
ATOM   317  C CD2 . LEU A 1 56  ? 245.628 251.922 227.832 1.00 2.76   ? 56   LEU A CD2 1 
ATOM   318  N N   . PRO A 1 57  ? 245.062 246.880 228.707 1.00 3.78   ? 57   PRO A N   1 
ATOM   319  C CA  . PRO A 1 57  ? 245.364 246.162 229.929 1.00 4.02   ? 57   PRO A CA  1 
ATOM   320  C C   . PRO A 1 57  ? 245.716 247.124 231.046 1.00 4.33   ? 57   PRO A C   1 
ATOM   321  O O   . PRO A 1 57  ? 246.419 248.112 230.823 1.00 4.30   ? 57   PRO A O   1 
ATOM   322  C CB  . PRO A 1 57  ? 246.572 245.314 229.525 1.00 4.36   ? 57   PRO A CB  1 
ATOM   323  C CG  . PRO A 1 57  ? 246.431 245.136 228.041 1.00 3.81   ? 57   PRO A CG  1 
ATOM   324  C CD  . PRO A 1 57  ? 245.843 246.437 227.547 1.00 3.57   ? 57   PRO A CD  1 
ATOM   325  N N   . PHE A 1 58  ? 245.245 246.835 232.251 1.00 4.81   ? 58   PHE A N   1 
ATOM   326  C CA  . PHE A 1 58  ? 245.531 247.717 233.370 1.00 5.04   ? 58   PHE A CA  1 
ATOM   327  C C   . PHE A 1 58  ? 247.010 247.729 233.715 1.00 4.89   ? 58   PHE A C   1 
ATOM   328  O O   . PHE A 1 58  ? 247.684 246.698 233.680 1.00 5.27   ? 58   PHE A O   1 
ATOM   329  C CB  . PHE A 1 58  ? 244.713 247.327 234.600 1.00 5.53   ? 58   PHE A CB  1 
ATOM   330  C CG  . PHE A 1 58  ? 243.303 247.850 234.630 1.00 5.83   ? 58   PHE A CG  1 
ATOM   331  C CD1 . PHE A 1 58  ? 242.745 248.541 233.565 1.00 5.62   ? 58   PHE A CD1 1 
ATOM   332  C CD2 . PHE A 1 58  ? 242.535 247.664 235.760 1.00 6.69   ? 58   PHE A CD2 1 
ATOM   333  C CE1 . PHE A 1 58  ? 241.466 249.027 233.645 1.00 5.41   ? 58   PHE A CE1 1 
ATOM   334  C CE2 . PHE A 1 58  ? 241.254 248.147 235.830 1.00 7.31   ? 58   PHE A CE2 1 
ATOM   335  C CZ  . PHE A 1 58  ? 240.723 248.830 234.773 1.00 6.42   ? 58   PHE A CZ  1 
ATOM   336  N N   . PHE A 1 59  ? 247.502 248.921 234.033 1.00 4.74   ? 59   PHE A N   1 
ATOM   337  C CA  . PHE A 1 59  ? 248.879 249.163 234.440 1.00 4.77   ? 59   PHE A CA  1 
ATOM   338  C C   . PHE A 1 59  ? 249.900 248.767 233.382 1.00 4.84   ? 59   PHE A C   1 
ATOM   339  O O   . PHE A 1 59  ? 251.067 248.545 233.699 1.00 5.31   ? 59   PHE A O   1 
ATOM   340  C CB  . PHE A 1 59  ? 249.174 248.447 235.753 1.00 4.81   ? 59   PHE A CB  1 
ATOM   341  C CG  . PHE A 1 59  ? 248.263 248.881 236.851 1.00 4.79   ? 59   PHE A CG  1 
ATOM   342  C CD1 . PHE A 1 59  ? 248.447 250.095 237.483 1.00 4.81   ? 59   PHE A CD1 1 
ATOM   343  C CD2 . PHE A 1 59  ? 247.208 248.090 237.240 1.00 5.35   ? 59   PHE A CD2 1 
ATOM   344  C CE1 . PHE A 1 59  ? 247.591 250.503 238.483 1.00 4.73   ? 59   PHE A CE1 1 
ATOM   345  C CE2 . PHE A 1 59  ? 246.350 248.495 238.235 1.00 5.41   ? 59   PHE A CE2 1 
ATOM   346  C CZ  . PHE A 1 59  ? 246.541 249.703 238.856 1.00 4.81   ? 59   PHE A CZ  1 
ATOM   347  N N   . SER A 1 60  ? 249.484 248.733 232.123 1.00 4.85   ? 60   SER A N   1 
ATOM   348  C CA  . SER A 1 60  ? 250.408 248.451 231.033 1.00 4.99   ? 60   SER A CA  1 
ATOM   349  C C   . SER A 1 60  ? 251.356 249.625 230.782 1.00 5.52   ? 60   SER A C   1 
ATOM   350  O O   . SER A 1 60  ? 251.084 250.753 231.201 1.00 4.82   ? 60   SER A O   1 
ATOM   351  C CB  . SER A 1 60  ? 249.649 248.125 229.759 1.00 4.68   ? 60   SER A CB  1 
ATOM   352  O OG  . SER A 1 60  ? 248.955 249.242 229.280 1.00 4.49   ? 60   SER A OG  1 
ATOM   353  N N   . ASN A 1 61  ? 252.463 249.330 230.077 1.00 6.00   ? 61   ASN A N   1 
ATOM   354  C CA  . ASN A 1 61  ? 253.452 250.334 229.667 1.00 5.28   ? 61   ASN A CA  1 
ATOM   355  C C   . ASN A 1 61  ? 253.074 250.962 228.324 1.00 5.75   ? 61   ASN A C   1 
ATOM   356  O O   . ASN A 1 61  ? 252.987 250.276 227.310 1.00 6.02   ? 61   ASN A O   1 
ATOM   357  C CB  . ASN A 1 61  ? 254.844 249.712 229.591 1.00 6.37   ? 61   ASN A CB  1 
ATOM   358  C CG  . ASN A 1 61  ? 255.566 249.686 230.926 1.00 7.67   ? 61   ASN A CG  1 
ATOM   359  O OD1 . ASN A 1 61  ? 255.564 250.687 231.664 1.00 7.70   ? 61   ASN A OD1 1 
ATOM   360  N ND2 . ASN A 1 61  ? 256.180 248.568 231.253 1.00 8.75   ? 61   ASN A ND2 1 
ATOM   361  N N   . VAL A 1 62  ? 252.839 252.276 228.342 1.00 5.60   ? 62   VAL A N   1 
ATOM   362  C CA  . VAL A 1 62  ? 252.418 253.052 227.171 1.00 4.92   ? 62   VAL A CA  1 
ATOM   363  C C   . VAL A 1 62  ? 253.572 253.881 226.645 1.00 5.49   ? 62   VAL A C   1 
ATOM   364  O O   . VAL A 1 62  ? 254.302 254.496 227.419 1.00 5.41   ? 62   VAL A O   1 
ATOM   365  C CB  . VAL A 1 62  ? 251.227 253.948 227.542 1.00 4.52   ? 62   VAL A CB  1 
ATOM   366  C CG1 . VAL A 1 62  ? 250.859 254.851 226.406 1.00 4.87   ? 62   VAL A CG1 1 
ATOM   367  C CG2 . VAL A 1 62  ? 250.069 253.074 227.889 1.00 4.58   ? 62   VAL A CG2 1 
ATOM   368  N N   . THR A 1 63  ? 253.775 253.862 225.333 1.00 5.31   ? 63   THR A N   1 
ATOM   369  C CA  . THR A 1 63  ? 254.906 254.567 224.751 1.00 5.39   ? 63   THR A CA  1 
ATOM   370  C C   . THR A 1 63  ? 254.624 256.055 224.658 1.00 5.92   ? 63   THR A C   1 
ATOM   371  O O   . THR A 1 63  ? 253.571 256.472 224.179 1.00 5.16   ? 63   THR A O   1 
ATOM   372  C CB  . THR A 1 63  ? 255.253 254.033 223.356 1.00 5.35   ? 63   THR A CB  1 
ATOM   373  O OG1 . THR A 1 63  ? 255.523 252.630 223.431 1.00 6.01   ? 63   THR A OG1 1 
ATOM   374  C CG2 . THR A 1 63  ? 256.490 254.751 222.827 1.00 6.49   ? 63   THR A CG2 1 
ATOM   375  N N   . TRP A 1 64  ? 255.571 256.849 225.125 1.00 6.59   ? 64   TRP A N   1 
ATOM   376  C CA  . TRP A 1 64  ? 255.449 258.299 225.130 1.00 6.94   ? 64   TRP A CA  1 
ATOM   377  C C   . TRP A 1 64  ? 256.295 258.930 224.032 1.00 7.50   ? 64   TRP A C   1 
ATOM   378  O O   . TRP A 1 64  ? 257.523 258.850 224.056 1.00 7.85   ? 64   TRP A O   1 
ATOM   379  C CB  . TRP A 1 64  ? 255.871 258.829 226.492 1.00 7.15   ? 64   TRP A CB  1 
ATOM   380  C CG  . TRP A 1 64  ? 255.691 260.283 226.683 1.00 8.08   ? 64   TRP A CG  1 
ATOM   381  C CD1 . TRP A 1 64  ? 254.938 261.144 225.946 1.00 8.05   ? 64   TRP A CD1 1 
ATOM   382  C CD2 . TRP A 1 64  ? 256.280 261.063 227.729 1.00 8.46   ? 64   TRP A CD2 1 
ATOM   383  N NE1 . TRP A 1 64  ? 255.024 262.404 226.468 1.00 8.28   ? 64   TRP A NE1 1 
ATOM   384  C CE2 . TRP A 1 64  ? 255.840 262.372 227.561 1.00 8.93   ? 64   TRP A CE2 1 
ATOM   385  C CE3 . TRP A 1 64  ? 257.134 260.756 228.786 1.00 8.08   ? 64   TRP A CE3 1 
ATOM   386  C CZ2 . TRP A 1 64  ? 256.224 263.383 228.416 1.00 9.71   ? 64   TRP A CZ2 1 
ATOM   387  C CZ3 . TRP A 1 64  ? 257.522 261.766 229.642 1.00 8.91   ? 64   TRP A CZ3 1 
ATOM   388  C CH2 . TRP A 1 64  ? 257.079 263.045 229.463 1.00 10.31  ? 64   TRP A CH2 1 
ATOM   389  N N   . PHE A 1 65  ? 255.630 259.534 223.053 1.00 7.39   ? 65   PHE A N   1 
ATOM   390  C CA  . PHE A 1 65  ? 256.312 260.122 221.909 1.00 7.88   ? 65   PHE A CA  1 
ATOM   391  C C   . PHE A 1 65  ? 256.369 261.636 222.004 1.00 8.52   ? 65   PHE A C   1 
ATOM   392  O O   . PHE A 1 65  ? 255.405 262.280 222.417 1.00 9.10   ? 65   PHE A O   1 
ATOM   393  C CB  . PHE A 1 65  ? 255.603 259.751 220.610 1.00 7.21   ? 65   PHE A CB  1 
ATOM   394  C CG  . PHE A 1 65  ? 255.713 258.320 220.224 1.00 6.63   ? 65   PHE A CG  1 
ATOM   395  C CD1 . PHE A 1 65  ? 256.801 257.869 219.503 1.00 6.85   ? 65   PHE A CD1 1 
ATOM   396  C CD2 . PHE A 1 65  ? 254.724 257.422 220.563 1.00 6.17   ? 65   PHE A CD2 1 
ATOM   397  C CE1 . PHE A 1 65  ? 256.898 256.549 219.131 1.00 5.95   ? 65   PHE A CE1 1 
ATOM   398  C CE2 . PHE A 1 65  ? 254.819 256.104 220.190 1.00 5.41   ? 65   PHE A CE2 1 
ATOM   399  C CZ  . PHE A 1 65  ? 255.907 255.668 219.474 1.00 5.48   ? 65   PHE A CZ  1 
ATOM   400  N N   . HIS A 1 66  ? 257.475 262.205 221.540 1.00 9.57   ? 66   HIS A N   1 
ATOM   401  C CA  . HIS A 1 66  ? 257.625 263.651 221.445 1.00 10.75  ? 66   HIS A CA  1 
ATOM   402  C C   . HIS A 1 66  ? 257.823 264.046 219.992 1.00 12.12  ? 66   HIS A C   1 
ATOM   403  O O   . HIS A 1 66  ? 258.851 263.728 219.397 1.00 13.48  ? 66   HIS A O   1 
ATOM   404  C CB  . HIS A 1 66  ? 258.830 264.137 222.251 1.00 11.19  ? 66   HIS A CB  1 
ATOM   405  C CG  . HIS A 1 66  ? 258.758 263.856 223.708 1.00 9.89   ? 66   HIS A CG  1 
ATOM   406  N ND1 . HIS A 1 66  ? 258.236 264.753 224.609 1.00 9.47   ? 66   HIS A ND1 1 
ATOM   407  C CD2 . HIS A 1 66  ? 259.158 262.785 224.428 1.00 9.68   ? 66   HIS A CD2 1 
ATOM   408  C CE1 . HIS A 1 66  ? 258.321 264.249 225.823 1.00 9.31   ? 66   HIS A CE1 1 
ATOM   409  N NE2 . HIS A 1 66  ? 258.878 263.055 225.740 1.00 9.40   ? 66   HIS A NE2 1 
ATOM   410  N N   . ALA A 1 67  ? 256.819 264.690 219.404 1.00 12.56  ? 67   ALA A N   1 
ATOM   411  C CA  . ALA A 1 67  ? 256.886 265.044 217.990 1.00 14.73  ? 67   ALA A CA  1 
ATOM   412  C C   . ALA A 1 67  ? 257.970 266.080 217.765 1.00 15.47  ? 67   ALA A C   1 
ATOM   413  O O   . ALA A 1 67  ? 258.735 266.007 216.801 1.00 16.15  ? 67   ALA A O   1 
ATOM   414  C CB  . ALA A 1 67  ? 255.550 265.581 217.517 1.00 13.91  ? 67   ALA A CB  1 
ATOM   415  N N   . ILE A 1 68  ? 258.036 267.037 218.678 1.00 15.91  ? 68   ILE A N   1 
ATOM   416  C CA  . ILE A 1 68  ? 259.056 268.074 218.631 1.00 17.03  ? 68   ILE A CA  1 
ATOM   417  C C   . ILE A 1 68  ? 259.985 267.933 219.837 1.00 16.91  ? 68   ILE A C   1 
ATOM   418  O O   . ILE A 1 68  ? 259.537 268.012 220.982 1.00 16.67  ? 68   ILE A O   1 
ATOM   419  C CB  . ILE A 1 68  ? 258.407 269.474 218.604 1.00 17.35  ? 68   ILE A CB  1 
ATOM   420  C CG1 . ILE A 1 68  ? 257.421 269.589 217.407 1.00 17.80  ? 68   ILE A CG1 1 
ATOM   421  C CG2 . ILE A 1 68  ? 259.465 270.561 218.549 1.00 18.13  ? 68   ILE A CG2 1 
ATOM   422  C CD1 . ILE A 1 68  ? 258.044 269.412 216.024 1.00 18.64  ? 68   ILE A CD1 1 
ATOM   423  N N   . HIS A 1 69  ? 261.278 267.715 219.573 1.00 18.06  ? 69   HIS A N   1 
ATOM   424  C CA  . HIS A 1 69  ? 262.278 267.470 220.612 1.00 19.62  ? 69   HIS A CA  1 
ATOM   425  C C   . HIS A 1 69  ? 262.497 268.716 221.471 1.00 18.81  ? 69   HIS A C   1 
ATOM   426  O O   . HIS A 1 69  ? 263.406 269.512 221.226 1.00 20.10  ? 69   HIS A O   1 
ATOM   427  C CB  . HIS A 1 69  ? 263.625 267.008 219.998 1.00 20.36  ? 69   HIS A CB  1 
ATOM   428  C CG  . HIS A 1 69  ? 263.565 265.698 219.225 1.00 20.09  ? 69   HIS A CG  1 
ATOM   429  N ND1 . HIS A 1 69  ? 263.060 264.542 219.764 1.00 19.40  ? 69   HIS A ND1 1 
ATOM   430  C CD2 . HIS A 1 69  ? 263.986 265.377 217.970 1.00 20.13  ? 69   HIS A CD2 1 
ATOM   431  C CE1 . HIS A 1 69  ? 263.150 263.562 218.871 1.00 20.02  ? 69   HIS A CE1 1 
ATOM   432  N NE2 . HIS A 1 69  ? 263.708 264.045 217.780 1.00 20.15  ? 69   HIS A NE2 1 
ATOM   433  N N   . PHE A 1 79  ? 263.584 265.969 214.480 1.00 19.66  ? 79   PHE A N   1 
ATOM   434  C CA  . PHE A 1 79  ? 262.134 265.891 214.623 1.00 18.50  ? 79   PHE A CA  1 
ATOM   435  C C   . PHE A 1 79  ? 261.602 264.787 213.704 1.00 17.40  ? 79   PHE A C   1 
ATOM   436  O O   . PHE A 1 79  ? 261.871 264.804 212.501 1.00 17.50  ? 79   PHE A O   1 
ATOM   437  C CB  . PHE A 1 79  ? 261.468 267.242 214.241 1.00 18.47  ? 79   PHE A CB  1 
ATOM   438  N N   . ASP A 1 80  ? 260.842 263.832 214.265 1.00 16.72  ? 80   ASP A N   1 
ATOM   439  C CA  . ASP A 1 80  ? 260.261 262.737 213.477 1.00 15.47  ? 80   ASP A CA  1 
ATOM   440  C C   . ASP A 1 80  ? 258.941 262.246 214.065 1.00 13.52  ? 80   ASP A C   1 
ATOM   441  O O   . ASP A 1 80  ? 258.685 262.380 215.262 1.00 13.84  ? 80   ASP A O   1 
ATOM   442  C CB  . ASP A 1 80  ? 261.246 261.560 213.360 1.00 17.59  ? 80   ASP A CB  1 
ATOM   443  C CG  . ASP A 1 80  ? 260.908 260.606 212.206 1.00 15.17  ? 80   ASP A CG  1 
ATOM   444  O OD1 . ASP A 1 80  ? 259.890 260.796 211.578 1.00 14.52  ? 80   ASP A OD1 1 
ATOM   445  O OD2 . ASP A 1 80  ? 261.680 259.707 211.957 1.00 17.60  ? 80   ASP A OD2 1 
ATOM   446  N N   . ASN A 1 81  ? 258.120 261.667 213.200 1.00 13.26  ? 81   ASN A N   1 
ATOM   447  C CA  . ASN A 1 81  ? 256.819 261.114 213.548 1.00 11.61  ? 81   ASN A CA  1 
ATOM   448  C C   . ASN A 1 81  ? 256.657 259.748 212.890 1.00 10.20  ? 81   ASN A C   1 
ATOM   449  O O   . ASN A 1 81  ? 256.115 259.651 211.789 1.00 9.83   ? 81   ASN A O   1 
ATOM   450  C CB  . ASN A 1 81  ? 255.707 262.049 213.118 1.00 10.16  ? 81   ASN A CB  1 
ATOM   451  C CG  . ASN A 1 81  ? 255.737 263.341 213.866 1.00 12.22  ? 81   ASN A CG  1 
ATOM   452  O OD1 . ASN A 1 81  ? 255.337 263.395 215.033 1.00 12.53  ? 81   ASN A OD1 1 
ATOM   453  N ND2 . ASN A 1 81  ? 256.207 264.384 213.226 1.00 13.94  ? 81   ASN A ND2 1 
ATOM   454  N N   . PRO A 1 82  ? 257.141 258.691 213.540 1.00 9.41   ? 82   PRO A N   1 
ATOM   455  C CA  . PRO A 1 82  ? 257.391 257.376 212.988 1.00 8.11   ? 82   PRO A CA  1 
ATOM   456  C C   . PRO A 1 82  ? 256.103 256.656 212.645 1.00 6.73   ? 82   PRO A C   1 
ATOM   457  O O   . PRO A 1 82  ? 255.068 256.890 213.268 1.00 6.54   ? 82   PRO A O   1 
ATOM   458  C CB  . PRO A 1 82  ? 258.133 256.681 214.135 1.00 7.82   ? 82   PRO A CB  1 
ATOM   459  C CG  . PRO A 1 82  ? 257.639 257.375 215.389 1.00 7.61   ? 82   PRO A CG  1 
ATOM   460  C CD  . PRO A 1 82  ? 257.383 258.807 214.977 1.00 8.93   ? 82   PRO A CD  1 
ATOM   461  N N   . VAL A 1 83  ? 256.184 255.747 211.681 1.00 6.02   ? 83   VAL A N   1 
ATOM   462  C CA  . VAL A 1 83  ? 255.059 254.883 211.359 1.00 5.01   ? 83   VAL A CA  1 
ATOM   463  C C   . VAL A 1 83  ? 254.990 253.750 212.369 1.00 4.84   ? 83   VAL A C   1 
ATOM   464  O O   . VAL A 1 83  ? 255.982 253.067 212.619 1.00 5.06   ? 83   VAL A O   1 
ATOM   465  C CB  . VAL A 1 83  ? 255.200 254.316 209.937 1.00 4.63   ? 83   VAL A CB  1 
ATOM   466  C CG1 . VAL A 1 83  ? 254.071 253.341 209.642 1.00 4.51   ? 83   VAL A CG1 1 
ATOM   467  C CG2 . VAL A 1 83  ? 255.187 255.454 208.937 1.00 5.50   ? 83   VAL A CG2 1 
ATOM   468  N N   . LEU A 1 84  ? 253.824 253.581 212.974 1.00 4.29   ? 84   LEU A N   1 
ATOM   469  C CA  . LEU A 1 84  ? 253.636 252.591 214.020 1.00 3.81   ? 84   LEU A CA  1 
ATOM   470  C C   . LEU A 1 84  ? 252.710 251.480 213.546 1.00 3.62   ? 84   LEU A C   1 
ATOM   471  O O   . LEU A 1 84  ? 251.876 251.710 212.673 1.00 3.49   ? 84   LEU A O   1 
ATOM   472  C CB  . LEU A 1 84  ? 253.043 253.280 215.255 1.00 3.57   ? 84   LEU A CB  1 
ATOM   473  C CG  . LEU A 1 84  ? 253.849 254.461 215.812 1.00 4.05   ? 84   LEU A CG  1 
ATOM   474  C CD1 . LEU A 1 84  ? 253.070 255.100 216.938 1.00 3.89   ? 84   LEU A CD1 1 
ATOM   475  C CD2 . LEU A 1 84  ? 255.204 253.978 216.298 1.00 4.44   ? 84   LEU A CD2 1 
ATOM   476  N N   . PRO A 1 85  ? 252.836 250.275 214.104 1.00 3.49   ? 85   PRO A N   1 
ATOM   477  C CA  . PRO A 1 85  ? 251.950 249.147 213.902 1.00 3.32   ? 85   PRO A CA  1 
ATOM   478  C C   . PRO A 1 85  ? 250.584 249.438 214.503 1.00 3.03   ? 85   PRO A C   1 
ATOM   479  O O   . PRO A 1 85  ? 250.478 250.165 215.487 1.00 3.07   ? 85   PRO A O   1 
ATOM   480  C CB  . PRO A 1 85  ? 252.676 248.012 214.635 1.00 3.23   ? 85   PRO A CB  1 
ATOM   481  C CG  . PRO A 1 85  ? 253.571 248.702 215.642 1.00 3.25   ? 85   PRO A CG  1 
ATOM   482  C CD  . PRO A 1 85  ? 253.965 250.011 214.996 1.00 3.63   ? 85   PRO A CD  1 
ATOM   483  N N   . PHE A 1 86  ? 249.545 248.865 213.916 1.00 2.89   ? 86   PHE A N   1 
ATOM   484  C CA  . PHE A 1 86  ? 248.187 249.019 214.421 1.00 2.67   ? 86   PHE A CA  1 
ATOM   485  C C   . PHE A 1 86  ? 247.799 247.837 215.300 1.00 2.47   ? 86   PHE A C   1 
ATOM   486  O O   . PHE A 1 86  ? 246.971 247.963 216.202 1.00 2.17   ? 86   PHE A O   1 
ATOM   487  C CB  . PHE A 1 86  ? 247.205 249.150 213.256 1.00 3.03   ? 86   PHE A CB  1 
ATOM   488  C CG  . PHE A 1 86  ? 245.803 249.511 213.648 1.00 2.67   ? 86   PHE A CG  1 
ATOM   489  C CD1 . PHE A 1 86  ? 245.476 250.811 213.992 1.00 2.66   ? 86   PHE A CD1 1 
ATOM   490  C CD2 . PHE A 1 86  ? 244.806 248.556 213.661 1.00 2.54   ? 86   PHE A CD2 1 
ATOM   491  C CE1 . PHE A 1 86  ? 244.184 251.143 214.342 1.00 2.53   ? 86   PHE A CE1 1 
ATOM   492  C CE2 . PHE A 1 86  ? 243.515 248.886 214.009 1.00 2.65   ? 86   PHE A CE2 1 
ATOM   493  C CZ  . PHE A 1 86  ? 243.205 250.182 214.351 1.00 2.68   ? 86   PHE A CZ  1 
ATOM   494  N N   . ASN A 1 87  ? 248.387 246.682 215.013 1.00 2.53   ? 87   ASN A N   1 
ATOM   495  C CA  . ASN A 1 87  ? 248.068 245.450 215.716 1.00 2.06   ? 87   ASN A CA  1 
ATOM   496  C C   . ASN A 1 87  ? 246.566 245.188 215.721 1.00 2.06   ? 87   ASN A C   1 
ATOM   497  O O   . ASN A 1 87  ? 245.947 245.137 214.657 1.00 2.25   ? 87   ASN A O   1 
ATOM   498  C CB  . ASN A 1 87  ? 248.660 245.463 217.113 1.00 2.20   ? 87   ASN A CB  1 
ATOM   499  C CG  . ASN A 1 87  ? 250.173 245.486 217.078 1.00 2.48   ? 87   ASN A CG  1 
ATOM   500  O OD1 . ASN A 1 87  ? 250.771 245.068 216.082 1.00 2.82   ? 87   ASN A OD1 1 
ATOM   501  N ND2 . ASN A 1 87  ? 250.796 245.947 218.133 1.00 2.79   ? 87   ASN A ND2 1 
ATOM   502  N N   . ASP A 1 88  ? 245.975 245.003 216.899 1.00 1.98   ? 88   ASP A N   1 
ATOM   503  C CA  . ASP A 1 88  ? 244.558 244.666 216.978 1.00 1.83   ? 88   ASP A CA  1 
ATOM   504  C C   . ASP A 1 88  ? 243.706 245.833 217.452 1.00 1.71   ? 88   ASP A C   1 
ATOM   505  O O   . ASP A 1 88  ? 242.533 245.661 217.777 1.00 2.00   ? 88   ASP A O   1 
ATOM   506  C CB  . ASP A 1 88  ? 244.339 243.459 217.894 1.00 1.82   ? 88   ASP A CB  1 
ATOM   507  C CG  . ASP A 1 88  ? 244.961 242.176 217.336 1.00 1.98   ? 88   ASP A CG  1 
ATOM   508  O OD1 . ASP A 1 88  ? 245.254 242.143 216.166 1.00 2.14   ? 88   ASP A OD1 1 
ATOM   509  O OD2 . ASP A 1 88  ? 245.133 241.242 218.081 1.00 2.02   ? 88   ASP A OD2 1 
ATOM   510  N N   . GLY A 1 89  ? 244.291 247.018 217.488 1.00 1.97   ? 89   GLY A N   1 
ATOM   511  C CA  . GLY A 1 89  ? 243.588 248.205 217.950 1.00 1.89   ? 89   GLY A CA  1 
ATOM   512  C C   . GLY A 1 89  ? 244.534 249.111 218.714 1.00 1.96   ? 89   GLY A C   1 
ATOM   513  O O   . GLY A 1 89  ? 245.504 248.649 219.319 1.00 2.13   ? 89   GLY A O   1 
ATOM   514  N N   . VAL A 1 90  ? 244.256 250.408 218.681 1.00 2.00   ? 90   VAL A N   1 
ATOM   515  C CA  . VAL A 1 90  ? 245.161 251.382 219.271 1.00 1.74   ? 90   VAL A CA  1 
ATOM   516  C C   . VAL A 1 90  ? 244.496 252.346 220.241 1.00 1.79   ? 90   VAL A C   1 
ATOM   517  O O   . VAL A 1 90  ? 243.454 252.931 219.951 1.00 2.12   ? 90   VAL A O   1 
ATOM   518  C CB  . VAL A 1 90  ? 245.847 252.193 218.154 1.00 1.81   ? 90   VAL A CB  1 
ATOM   519  C CG1 . VAL A 1 90  ? 246.739 253.267 218.746 1.00 1.96   ? 90   VAL A CG1 1 
ATOM   520  C CG2 . VAL A 1 90  ? 246.662 251.260 217.287 1.00 2.18   ? 90   VAL A CG2 1 
ATOM   521  N N   . TYR A 1 91  ? 245.156 252.551 221.373 1.00 1.89   ? 91   TYR A N   1 
ATOM   522  C CA  . TYR A 1 91  ? 244.785 253.597 222.316 1.00 1.88   ? 91   TYR A CA  1 
ATOM   523  C C   . TYR A 1 91  ? 245.689 254.802 222.110 1.00 2.16   ? 91   TYR A C   1 
ATOM   524  O O   . TYR A 1 91  ? 246.912 254.688 222.175 1.00 2.62   ? 91   TYR A O   1 
ATOM   525  C CB  . TYR A 1 91  ? 244.888 253.099 223.754 1.00 1.97   ? 91   TYR A CB  1 
ATOM   526  C CG  . TYR A 1 91  ? 244.828 254.203 224.792 1.00 2.07   ? 91   TYR A CG  1 
ATOM   527  C CD1 . TYR A 1 91  ? 246.003 254.641 225.379 1.00 2.17   ? 91   TYR A CD1 1 
ATOM   528  C CD2 . TYR A 1 91  ? 243.618 254.771 225.161 1.00 2.04   ? 91   TYR A CD2 1 
ATOM   529  C CE1 . TYR A 1 91  ? 245.975 255.632 226.326 1.00 2.09   ? 91   TYR A CE1 1 
ATOM   530  C CE2 . TYR A 1 91  ? 243.592 255.773 226.117 1.00 2.21   ? 91   TYR A CE2 1 
ATOM   531  C CZ  . TYR A 1 91  ? 244.769 256.198 226.696 1.00 2.46   ? 91   TYR A CZ  1 
ATOM   532  O OH  . TYR A 1 91  ? 244.764 257.187 227.648 1.00 3.58   ? 91   TYR A OH  1 
ATOM   533  N N   . PHE A 1 92  ? 245.091 255.951 221.846 1.00 2.43   ? 92   PHE A N   1 
ATOM   534  C CA  . PHE A 1 92  ? 245.851 257.159 221.555 1.00 2.76   ? 92   PHE A CA  1 
ATOM   535  C C   . PHE A 1 92  ? 245.428 258.294 222.471 1.00 2.99   ? 92   PHE A C   1 
ATOM   536  O O   . PHE A 1 92  ? 244.239 258.531 222.668 1.00 3.41   ? 92   PHE A O   1 
ATOM   537  C CB  . PHE A 1 92  ? 245.638 257.567 220.096 1.00 2.94   ? 92   PHE A CB  1 
ATOM   538  C CG  . PHE A 1 92  ? 246.444 258.751 219.646 1.00 3.40   ? 92   PHE A CG  1 
ATOM   539  C CD1 . PHE A 1 92  ? 245.980 260.041 219.834 1.00 3.68   ? 92   PHE A CD1 1 
ATOM   540  C CD2 . PHE A 1 92  ? 247.661 258.573 219.012 1.00 3.76   ? 92   PHE A CD2 1 
ATOM   541  C CE1 . PHE A 1 92  ? 246.718 261.124 219.407 1.00 4.31   ? 92   PHE A CE1 1 
ATOM   542  C CE2 . PHE A 1 92  ? 248.395 259.653 218.583 1.00 4.34   ? 92   PHE A CE2 1 
ATOM   543  C CZ  . PHE A 1 92  ? 247.924 260.929 218.783 1.00 4.63   ? 92   PHE A CZ  1 
ATOM   544  N N   . ALA A 1 93  ? 246.394 259.013 223.020 1.00 3.71   ? 93   ALA A N   1 
ATOM   545  C CA  . ALA A 1 93  ? 246.074 260.144 223.880 1.00 4.33   ? 93   ALA A CA  1 
ATOM   546  C C   . ALA A 1 93  ? 247.060 261.278 223.676 1.00 5.48   ? 93   ALA A C   1 
ATOM   547  O O   . ALA A 1 93  ? 248.226 261.051 223.362 1.00 4.96   ? 93   ALA A O   1 
ATOM   548  C CB  . ALA A 1 93  ? 246.061 259.713 225.336 1.00 4.51   ? 93   ALA A CB  1 
ATOM   549  N N   . SER A 1 94  ? 246.604 262.506 223.881 1.00 6.04   ? 94   SER A N   1 
ATOM   550  C CA  . SER A 1 94  ? 247.487 263.658 223.742 1.00 6.64   ? 94   SER A CA  1 
ATOM   551  C C   . SER A 1 94  ? 247.139 264.765 224.726 1.00 7.99   ? 94   SER A C   1 
ATOM   552  O O   . SER A 1 94  ? 246.002 264.867 225.184 1.00 7.95   ? 94   SER A O   1 
ATOM   553  C CB  . SER A 1 94  ? 247.420 264.192 222.325 1.00 6.94   ? 94   SER A CB  1 
ATOM   554  O OG  . SER A 1 94  ? 246.144 264.702 222.038 1.00 8.22   ? 94   SER A OG  1 
ATOM   555  N N   . THR A 1 95  ? 248.129 265.600 225.043 1.00 8.55   ? 95   THR A N   1 
ATOM   556  C CA  . THR A 1 95  ? 247.926 266.734 225.942 1.00 9.31   ? 95   THR A CA  1 
ATOM   557  C C   . THR A 1 95  ? 248.549 268.005 225.388 1.00 10.00  ? 95   THR A C   1 
ATOM   558  O O   . THR A 1 95  ? 249.620 268.429 225.825 1.00 11.21  ? 95   THR A O   1 
ATOM   559  C CB  . THR A 1 95  ? 248.485 266.450 227.350 1.00 9.13   ? 95   THR A CB  1 
ATOM   560  O OG1 . THR A 1 95  ? 249.863 266.083 227.261 1.00 9.24   ? 95   THR A OG1 1 
ATOM   561  C CG2 . THR A 1 95  ? 247.711 265.336 228.019 1.00 9.87   ? 95   THR A CG2 1 
ATOM   562  N N   . GLU A 1 96  ? 247.881 268.607 224.415 1.00 10.69  ? 96   GLU A N   1 
ATOM   563  C CA  . GLU A 1 96  ? 248.375 269.820 223.781 1.00 11.84  ? 96   GLU A CA  1 
ATOM   564  C C   . GLU A 1 96  ? 247.234 270.802 223.518 1.00 12.21  ? 96   GLU A C   1 
ATOM   565  O O   . GLU A 1 96  ? 246.104 270.402 223.233 1.00 11.78  ? 96   GLU A O   1 
ATOM   566  C CB  . GLU A 1 96  ? 249.149 269.463 222.502 1.00 11.46  ? 96   GLU A CB  1 
ATOM   567  C CG  . GLU A 1 96  ? 248.389 268.601 221.486 1.00 11.73  ? 96   GLU A CG  1 
ATOM   568  C CD  . GLU A 1 96  ? 247.898 269.369 220.291 1.00 12.70  ? 96   GLU A CD  1 
ATOM   569  O OE1 . GLU A 1 96  ? 248.342 270.474 220.098 1.00 13.11  ? 96   GLU A OE1 1 
ATOM   570  O OE2 . GLU A 1 96  ? 247.095 268.844 219.555 1.00 12.65  ? 96   GLU A OE2 1 
ATOM   571  N N   . LYS A 1 97  ? 247.533 272.094 223.655 1.00 12.66  ? 97   LYS A N   1 
ATOM   572  C CA  . LYS A 1 97  ? 246.525 273.145 223.524 1.00 12.72  ? 97   LYS A CA  1 
ATOM   573  C C   . LYS A 1 97  ? 246.690 273.953 222.242 1.00 13.34  ? 97   LYS A C   1 
ATOM   574  O O   . LYS A 1 97  ? 245.901 274.856 221.963 1.00 13.46  ? 97   LYS A O   1 
ATOM   575  C CB  . LYS A 1 97  ? 246.603 274.091 224.722 1.00 12.66  ? 97   LYS A CB  1 
ATOM   576  C CG  . LYS A 1 97  ? 246.414 273.417 226.072 1.00 13.46  ? 97   LYS A CG  1 
ATOM   577  C CD  . LYS A 1 97  ? 246.691 274.383 227.225 1.00 14.67  ? 97   LYS A CD  1 
ATOM   578  C CE  . LYS A 1 97  ? 245.521 275.331 227.469 1.00 16.00  ? 97   LYS A CE  1 
ATOM   579  N NZ  . LYS A 1 97  ? 245.719 276.143 228.702 1.00 15.92  ? 97   LYS A NZ  1 
ATOM   580  N N   . SER A 1 98  ? 247.732 273.648 221.482 1.00 13.72  ? 98   SER A N   1 
ATOM   581  C CA  . SER A 1 98  ? 248.079 274.422 220.298 1.00 14.11  ? 98   SER A CA  1 
ATOM   582  C C   . SER A 1 98  ? 247.404 273.895 219.035 1.00 13.90  ? 98   SER A C   1 
ATOM   583  O O   . SER A 1 98  ? 247.592 274.444 217.949 1.00 14.36  ? 98   SER A O   1 
ATOM   584  C CB  . SER A 1 98  ? 249.582 274.427 220.112 1.00 14.36  ? 98   SER A CB  1 
ATOM   585  O OG  . SER A 1 98  ? 250.221 275.045 221.194 1.00 15.82  ? 98   SER A OG  1 
ATOM   586  N N   . ASN A 1 99  ? 246.631 272.823 219.175 1.00 13.99  ? 99   ASN A N   1 
ATOM   587  C CA  . ASN A 1 99  ? 245.958 272.200 218.039 1.00 14.38  ? 99   ASN A CA  1 
ATOM   588  C C   . ASN A 1 99  ? 246.948 271.819 216.945 1.00 13.88  ? 99   ASN A C   1 
ATOM   589  O O   . ASN A 1 99  ? 246.712 272.063 215.761 1.00 14.70  ? 99   ASN A O   1 
ATOM   590  C CB  . ASN A 1 99  ? 244.868 273.107 217.498 1.00 12.66  ? 99   ASN A CB  1 
ATOM   591  C CG  . ASN A 1 99  ? 243.761 273.319 218.495 1.00 14.01  ? 99   ASN A CG  1 
ATOM   592  O OD1 . ASN A 1 99  ? 243.293 272.366 219.130 1.00 13.73  ? 99   ASN A OD1 1 
ATOM   593  N ND2 . ASN A 1 99  ? 243.336 274.546 218.650 1.00 15.61  ? 99   ASN A ND2 1 
ATOM   594  N N   . ILE A 1 100 ? 248.057 271.215 217.358 1.00 14.05  ? 100  ILE A N   1 
ATOM   595  C CA  . ILE A 1 100 ? 249.085 270.752 216.437 1.00 14.38  ? 100  ILE A CA  1 
ATOM   596  C C   . ILE A 1 100 ? 248.691 269.431 215.796 1.00 13.27  ? 100  ILE A C   1 
ATOM   597  O O   . ILE A 1 100 ? 248.936 269.215 214.611 1.00 14.57  ? 100  ILE A O   1 
ATOM   598  C CB  . ILE A 1 100 ? 250.440 270.613 217.144 1.00 14.26  ? 100  ILE A CB  1 
ATOM   599  C CG1 . ILE A 1 100 ? 250.913 271.991 217.590 1.00 15.22  ? 100  ILE A CG1 1 
ATOM   600  C CG2 . ILE A 1 100 ? 251.455 269.980 216.195 1.00 14.45  ? 100  ILE A CG2 1 
ATOM   601  C CD1 . ILE A 1 100 ? 252.045 271.967 218.591 1.00 16.58  ? 100  ILE A CD1 1 
ATOM   602  N N   . ILE A 1 101 ? 248.109 268.527 216.577 1.00 12.73  ? 101  ILE A N   1 
ATOM   603  C CA  . ILE A 1 101 ? 247.682 267.250 216.020 1.00 12.16  ? 101  ILE A CA  1 
ATOM   604  C C   . ILE A 1 101 ? 246.371 267.446 215.273 1.00 12.21  ? 101  ILE A C   1 
ATOM   605  O O   . ILE A 1 101 ? 245.427 268.026 215.808 1.00 12.10  ? 101  ILE A O   1 
ATOM   606  C CB  . ILE A 1 101 ? 247.532 266.182 217.119 1.00 11.64  ? 101  ILE A CB  1 
ATOM   607  C CG1 . ILE A 1 101 ? 248.909 265.919 217.766 1.00 10.97  ? 101  ILE A CG1 1 
ATOM   608  C CG2 . ILE A 1 101 ? 246.949 264.896 216.528 1.00 9.79   ? 101  ILE A CG2 1 
ATOM   609  C CD1 . ILE A 1 101 ? 248.857 265.120 219.046 1.00 8.71   ? 101  ILE A CD1 1 
ATOM   610  N N   . ARG A 1 102 ? 246.326 267.009 214.019 1.00 11.58  ? 102  ARG A N   1 
ATOM   611  C CA  . ARG A 1 102 ? 245.136 267.216 213.207 1.00 11.58  ? 102  ARG A CA  1 
ATOM   612  C C   . ARG A 1 102 ? 244.447 265.923 212.809 1.00 10.99  ? 102  ARG A C   1 
ATOM   613  O O   . ARG A 1 102 ? 243.231 265.901 212.623 1.00 11.34  ? 102  ARG A O   1 
ATOM   614  C CB  . ARG A 1 102 ? 245.471 268.013 211.956 1.00 12.49  ? 102  ARG A CB  1 
ATOM   615  C CG  . ARG A 1 102 ? 245.994 269.418 212.213 1.00 14.74  ? 102  ARG A CG  1 
ATOM   616  C CD  . ARG A 1 102 ? 244.962 270.296 212.842 1.00 15.33  ? 102  ARG A CD  1 
ATOM   617  N NE  . ARG A 1 102 ? 245.471 271.631 213.109 1.00 16.74  ? 102  ARG A NE  1 
ATOM   618  C CZ  . ARG A 1 102 ? 245.443 272.661 212.241 1.00 24.33  ? 102  ARG A CZ  1 
ATOM   619  N NH1 . ARG A 1 102 ? 245.940 273.822 212.598 1.00 30.68  ? 102  ARG A NH1 1 
ATOM   620  N NH2 . ARG A 1 102 ? 244.920 272.509 211.035 1.00 23.42  ? 102  ARG A NH2 1 
ATOM   621  N N   . GLY A 1 103 ? 245.203 264.849 212.644 1.00 9.45   ? 103  GLY A N   1 
ATOM   622  C CA  . GLY A 1 103 ? 244.575 263.636 212.143 1.00 7.95   ? 103  GLY A CA  1 
ATOM   623  C C   . GLY A 1 103 ? 245.511 262.449 212.059 1.00 7.13   ? 103  GLY A C   1 
ATOM   624  O O   . GLY A 1 103 ? 246.628 262.481 212.574 1.00 7.01   ? 103  GLY A O   1 
ATOM   625  N N   . TRP A 1 104 ? 245.021 261.382 211.439 1.00 6.43   ? 104  TRP A N   1 
ATOM   626  C CA  . TRP A 1 104 ? 245.755 260.131 211.348 1.00 5.86   ? 104  TRP A CA  1 
ATOM   627  C C   . TRP A 1 104 ? 245.618 259.487 209.973 1.00 6.32   ? 104  TRP A C   1 
ATOM   628  O O   . TRP A 1 104 ? 244.589 259.619 209.309 1.00 6.68   ? 104  TRP A O   1 
ATOM   629  C CB  . TRP A 1 104 ? 245.250 259.141 212.397 1.00 5.27   ? 104  TRP A CB  1 
ATOM   630  C CG  . TRP A 1 104 ? 245.296 259.648 213.803 1.00 4.56   ? 104  TRP A CG  1 
ATOM   631  C CD1 . TRP A 1 104 ? 246.316 259.510 214.688 1.00 4.27   ? 104  TRP A CD1 1 
ATOM   632  C CD2 . TRP A 1 104 ? 244.255 260.370 214.503 1.00 4.27   ? 104  TRP A CD2 1 
ATOM   633  N NE1 . TRP A 1 104 ? 245.989 260.099 215.877 1.00 4.31   ? 104  TRP A NE1 1 
ATOM   634  C CE2 . TRP A 1 104 ? 244.733 260.631 215.781 1.00 3.97   ? 104  TRP A CE2 1 
ATOM   635  C CE3 . TRP A 1 104 ? 242.976 260.809 214.148 1.00 4.67   ? 104  TRP A CE3 1 
ATOM   636  C CZ2 . TRP A 1 104 ? 243.981 261.316 216.716 1.00 3.79   ? 104  TRP A CZ2 1 
ATOM   637  C CZ3 . TRP A 1 104 ? 242.222 261.496 215.087 1.00 4.26   ? 104  TRP A CZ3 1 
ATOM   638  C CH2 . TRP A 1 104 ? 242.714 261.744 216.336 1.00 3.69   ? 104  TRP A CH2 1 
ATOM   639  N N   . ILE A 1 105 ? 246.636 258.731 209.586 1.00 5.96   ? 105  ILE A N   1 
ATOM   640  C CA  . ILE A 1 105 ? 246.585 257.908 208.386 1.00 5.74   ? 105  ILE A CA  1 
ATOM   641  C C   . ILE A 1 105 ? 246.617 256.437 208.758 1.00 5.38   ? 105  ILE A C   1 
ATOM   642  O O   . ILE A 1 105 ? 247.525 255.994 209.455 1.00 4.74   ? 105  ILE A O   1 
ATOM   643  C CB  . ILE A 1 105 ? 247.771 258.204 207.454 1.00 6.00   ? 105  ILE A CB  1 
ATOM   644  C CG1 . ILE A 1 105 ? 247.734 259.655 207.001 1.00 7.30   ? 105  ILE A CG1 1 
ATOM   645  C CG2 . ILE A 1 105 ? 247.724 257.263 206.260 1.00 7.28   ? 105  ILE A CG2 1 
ATOM   646  C CD1 . ILE A 1 105 ? 248.995 260.112 206.302 1.00 9.33   ? 105  ILE A CD1 1 
ATOM   647  N N   . PHE A 1 106 ? 245.636 255.679 208.285 1.00 5.45   ? 106  PHE A N   1 
ATOM   648  C CA  . PHE A 1 106 ? 245.583 254.248 208.560 1.00 5.17   ? 106  PHE A CA  1 
ATOM   649  C C   . PHE A 1 106 ? 245.624 253.454 207.263 1.00 5.72   ? 106  PHE A C   1 
ATOM   650  O O   . PHE A 1 106 ? 244.916 253.774 206.310 1.00 6.41   ? 106  PHE A O   1 
ATOM   651  C CB  . PHE A 1 106 ? 244.300 253.894 209.313 1.00 5.06   ? 106  PHE A CB  1 
ATOM   652  C CG  . PHE A 1 106 ? 244.159 254.538 210.651 1.00 4.58   ? 106  PHE A CG  1 
ATOM   653  C CD1 . PHE A 1 106 ? 243.466 255.724 210.791 1.00 4.87   ? 106  PHE A CD1 1 
ATOM   654  C CD2 . PHE A 1 106 ? 244.712 253.960 211.773 1.00 3.84   ? 106  PHE A CD2 1 
ATOM   655  C CE1 . PHE A 1 106 ? 243.333 256.316 212.024 1.00 4.18   ? 106  PHE A CE1 1 
ATOM   656  C CE2 . PHE A 1 106 ? 244.585 254.554 213.006 1.00 3.41   ? 106  PHE A CE2 1 
ATOM   657  C CZ  . PHE A 1 106 ? 243.894 255.734 213.130 1.00 3.31   ? 106  PHE A CZ  1 
ATOM   658  N N   . GLY A 1 107 ? 246.418 252.393 207.227 1.00 5.31   ? 107  GLY A N   1 
ATOM   659  C CA  . GLY A 1 107 ? 246.474 251.568 206.027 1.00 5.69   ? 107  GLY A CA  1 
ATOM   660  C C   . GLY A 1 107 ? 247.495 250.448 206.142 1.00 5.57   ? 107  GLY A C   1 
ATOM   661  O O   . GLY A 1 107 ? 247.825 250.002 207.240 1.00 5.06   ? 107  GLY A O   1 
ATOM   662  N N   . THR A 1 108 ? 247.969 249.976 204.993 1.00 6.28   ? 108  THR A N   1 
ATOM   663  C CA  . THR A 1 108 ? 248.930 248.881 204.940 1.00 6.10   ? 108  THR A CA  1 
ATOM   664  C C   . THR A 1 108 ? 250.245 249.335 204.318 1.00 6.47   ? 108  THR A C   1 
ATOM   665  O O   . THR A 1 108 ? 251.186 249.682 205.031 1.00 6.30   ? 108  THR A O   1 
ATOM   666  C CB  . THR A 1 108 ? 248.367 247.681 204.160 1.00 6.30   ? 108  THR A CB  1 
ATOM   667  O OG1 . THR A 1 108 ? 247.974 248.094 202.846 1.00 7.50   ? 108  THR A OG1 1 
ATOM   668  C CG2 . THR A 1 108 ? 247.170 247.092 204.883 1.00 6.25   ? 108  THR A CG2 1 
ATOM   669  N N   . THR A 1 109 ? 250.302 249.354 202.988 1.00 6.91   ? 109  THR A N   1 
ATOM   670  C CA  . THR A 1 109 ? 251.503 249.790 202.282 1.00 7.31   ? 109  THR A CA  1 
ATOM   671  C C   . THR A 1 109 ? 251.601 251.312 202.260 1.00 7.76   ? 109  THR A C   1 
ATOM   672  O O   . THR A 1 109 ? 252.658 251.875 201.977 1.00 8.16   ? 109  THR A O   1 
ATOM   673  C CB  . THR A 1 109 ? 251.533 249.228 200.850 1.00 7.94   ? 109  THR A CB  1 
ATOM   674  O OG1 . THR A 1 109 ? 250.413 249.729 200.108 1.00 8.54   ? 109  THR A OG1 1 
ATOM   675  C CG2 . THR A 1 109 ? 251.473 247.710 200.891 1.00 7.97   ? 109  THR A CG2 1 
ATOM   676  N N   . LEU A 1 110 ? 250.496 251.975 202.585 1.00 7.88   ? 110  LEU A N   1 
ATOM   677  C CA  . LEU A 1 110 ? 250.442 253.431 202.665 1.00 8.22   ? 110  LEU A CA  1 
ATOM   678  C C   . LEU A 1 110 ? 250.921 254.092 201.380 1.00 9.05   ? 110  LEU A C   1 
ATOM   679  O O   . LEU A 1 110 ? 251.619 255.107 201.417 1.00 9.87   ? 110  LEU A O   1 
ATOM   680  C CB  . LEU A 1 110 ? 251.275 253.927 203.858 1.00 8.03   ? 110  LEU A CB  1 
ATOM   681  C CG  . LEU A 1 110 ? 250.878 253.359 205.250 1.00 6.50   ? 110  LEU A CG  1 
ATOM   682  C CD1 . LEU A 1 110 ? 251.851 253.863 206.304 1.00 6.24   ? 110  LEU A CD1 1 
ATOM   683  C CD2 . LEU A 1 110 ? 249.459 253.779 205.597 1.00 6.51   ? 110  LEU A CD2 1 
ATOM   684  N N   . ASP A 1 111 ? 250.531 253.524 200.245 1.00 9.14   ? 111  ASP A N   1 
ATOM   685  C CA  . ASP A 1 111 ? 250.845 254.093 198.944 1.00 10.00  ? 111  ASP A CA  1 
ATOM   686  C C   . ASP A 1 111 ? 249.736 253.751 197.952 1.00 9.92   ? 111  ASP A C   1 
ATOM   687  O O   . ASP A 1 111 ? 248.716 253.175 198.329 1.00 10.19  ? 111  ASP A O   1 
ATOM   688  C CB  . ASP A 1 111 ? 252.204 253.604 198.431 1.00 10.08  ? 111  ASP A CB  1 
ATOM   689  C CG  . ASP A 1 111 ? 252.242 252.124 198.101 1.00 9.64   ? 111  ASP A CG  1 
ATOM   690  O OD1 . ASP A 1 111 ? 251.205 251.505 198.127 1.00 10.36  ? 111  ASP A OD1 1 
ATOM   691  O OD2 . ASP A 1 111 ? 253.311 251.622 197.806 1.00 9.81   ? 111  ASP A OD2 1 
ATOM   692  N N   . SER A 1 112 ? 249.947 254.107 196.689 1.00 10.87  ? 112  SER A N   1 
ATOM   693  C CA  . SER A 1 112 ? 248.928 253.965 195.651 1.00 10.70  ? 112  SER A CA  1 
ATOM   694  C C   . SER A 1 112 ? 248.526 252.524 195.341 1.00 10.33  ? 112  SER A C   1 
ATOM   695  O O   . SER A 1 112 ? 247.609 252.300 194.552 1.00 10.77  ? 112  SER A O   1 
ATOM   696  C CB  . SER A 1 112 ? 249.402 254.627 194.376 1.00 11.19  ? 112  SER A CB  1 
ATOM   697  O OG  . SER A 1 112 ? 250.511 253.957 193.842 1.00 11.05  ? 112  SER A OG  1 
ATOM   698  N N   . LYS A 1 113 ? 249.227 251.546 195.910 1.00 10.05  ? 113  LYS A N   1 
ATOM   699  C CA  . LYS A 1 113 ? 248.916 250.146 195.638 1.00 9.81   ? 113  LYS A CA  1 
ATOM   700  C C   . LYS A 1 113 ? 247.630 249.681 196.319 1.00 9.68   ? 113  LYS A C   1 
ATOM   701  O O   . LYS A 1 113 ? 246.978 248.753 195.840 1.00 10.29  ? 113  LYS A O   1 
ATOM   702  C CB  . LYS A 1 113 ? 250.065 249.245 196.080 1.00 9.90   ? 113  LYS A CB  1 
ATOM   703  C CG  . LYS A 1 113 ? 251.326 249.400 195.271 1.00 9.45   ? 113  LYS A CG  1 
ATOM   704  C CD  . LYS A 1 113 ? 252.446 248.558 195.857 1.00 9.95   ? 113  LYS A CD  1 
ATOM   705  C CE  . LYS A 1 113 ? 253.787 248.881 195.225 1.00 10.58  ? 113  LYS A CE  1 
ATOM   706  N NZ  . LYS A 1 113 ? 254.077 250.337 195.285 1.00 10.87  ? 113  LYS A NZ  1 
ATOM   707  N N   . THR A 1 114 ? 247.289 250.281 197.459 1.00 9.77   ? 114  THR A N   1 
ATOM   708  C CA  . THR A 1 114 ? 246.121 249.837 198.214 1.00 10.04  ? 114  THR A CA  1 
ATOM   709  C C   . THR A 1 114 ? 245.276 251.008 198.691 1.00 9.80   ? 114  THR A C   1 
ATOM   710  O O   . THR A 1 114 ? 245.722 252.154 198.684 1.00 10.36  ? 114  THR A O   1 
ATOM   711  C CB  . THR A 1 114 ? 246.526 248.999 199.438 1.00 9.86   ? 114  THR A CB  1 
ATOM   712  O OG1 . THR A 1 114 ? 247.139 249.848 200.416 1.00 9.05   ? 114  THR A OG1 1 
ATOM   713  C CG2 . THR A 1 114 ? 247.507 247.909 199.040 1.00 9.53   ? 114  THR A CG2 1 
ATOM   714  N N   . GLN A 1 115 ? 244.069 250.713 199.156 1.00 9.81   ? 115  GLN A N   1 
ATOM   715  C CA  . GLN A 1 115 ? 243.218 251.747 199.727 1.00 9.77   ? 115  GLN A CA  1 
ATOM   716  C C   . GLN A 1 115 ? 243.692 252.112 201.124 1.00 9.41   ? 115  GLN A C   1 
ATOM   717  O O   . GLN A 1 115 ? 244.061 251.238 201.909 1.00 9.49   ? 115  GLN A O   1 
ATOM   718  C CB  . GLN A 1 115 ? 241.764 251.282 199.779 1.00 9.05   ? 115  GLN A CB  1 
ATOM   719  C CG  . GLN A 1 115 ? 241.121 251.098 198.424 1.00 9.24   ? 115  GLN A CG  1 
ATOM   720  C CD  . GLN A 1 115 ? 239.716 250.571 198.539 1.00 10.08  ? 115  GLN A CD  1 
ATOM   721  O OE1 . GLN A 1 115 ? 238.991 250.918 199.475 1.00 10.19  ? 115  GLN A OE1 1 
ATOM   722  N NE2 . GLN A 1 115 ? 239.319 249.727 197.596 1.00 10.90  ? 115  GLN A NE2 1 
ATOM   723  N N   . SER A 1 116 ? 243.661 253.401 201.436 1.00 9.32   ? 116  SER A N   1 
ATOM   724  C CA  . SER A 1 116 ? 244.041 253.878 202.759 1.00 8.31   ? 116  SER A CA  1 
ATOM   725  C C   . SER A 1 116 ? 242.993 254.821 203.323 1.00 8.21   ? 116  SER A C   1 
ATOM   726  O O   . SER A 1 116 ? 242.268 255.484 202.578 1.00 8.74   ? 116  SER A O   1 
ATOM   727  C CB  . SER A 1 116 ? 245.380 254.585 202.706 1.00 8.95   ? 116  SER A CB  1 
ATOM   728  O OG  . SER A 1 116 ? 246.396 253.720 202.283 1.00 9.27   ? 116  SER A OG  1 
ATOM   729  N N   . LEU A 1 117 ? 242.916 254.871 204.646 1.00 7.43   ? 117  LEU A N   1 
ATOM   730  C CA  . LEU A 1 117 ? 241.975 255.722 205.358 1.00 7.27   ? 117  LEU A CA  1 
ATOM   731  C C   . LEU A 1 117 ? 242.632 256.988 205.885 1.00 7.10   ? 117  LEU A C   1 
ATOM   732  O O   . LEU A 1 117 ? 243.568 256.935 206.682 1.00 6.52   ? 117  LEU A O   1 
ATOM   733  C CB  . LEU A 1 117 ? 241.349 254.926 206.510 1.00 6.69   ? 117  LEU A CB  1 
ATOM   734  C CG  . LEU A 1 117 ? 240.544 255.710 207.549 1.00 6.55   ? 117  LEU A CG  1 
ATOM   735  C CD1 . LEU A 1 117 ? 239.344 256.361 206.899 1.00 7.41   ? 117  LEU A CD1 1 
ATOM   736  C CD2 . LEU A 1 117 ? 240.107 254.753 208.644 1.00 5.52   ? 117  LEU A CD2 1 
ATOM   737  N N   . LEU A 1 118 ? 242.138 258.129 205.430 1.00 7.71   ? 118  LEU A N   1 
ATOM   738  C CA  . LEU A 1 118 ? 242.676 259.417 205.838 1.00 7.74   ? 118  LEU A CA  1 
ATOM   739  C C   . LEU A 1 118 ? 241.667 260.197 206.674 1.00 8.23   ? 118  LEU A C   1 
ATOM   740  O O   . LEU A 1 118 ? 240.612 260.591 206.176 1.00 8.47   ? 118  LEU A O   1 
ATOM   741  C CB  . LEU A 1 118 ? 243.060 260.224 204.589 1.00 8.90   ? 118  LEU A CB  1 
ATOM   742  C CG  . LEU A 1 118 ? 243.581 261.648 204.816 1.00 8.66   ? 118  LEU A CG  1 
ATOM   743  C CD1 . LEU A 1 118 ? 244.884 261.598 205.588 1.00 8.85   ? 118  LEU A CD1 1 
ATOM   744  C CD2 . LEU A 1 118 ? 243.786 262.322 203.471 1.00 10.65  ? 118  LEU A CD2 1 
ATOM   745  N N   . ILE A 1 119 ? 241.994 260.424 207.946 1.00 7.89   ? 119  ILE A N   1 
ATOM   746  C CA  . ILE A 1 119 ? 241.124 261.185 208.839 1.00 8.12   ? 119  ILE A CA  1 
ATOM   747  C C   . ILE A 1 119 ? 241.787 262.488 209.236 1.00 8.79   ? 119  ILE A C   1 
ATOM   748  O O   . ILE A 1 119 ? 242.748 262.482 210.005 1.00 8.55   ? 119  ILE A O   1 
ATOM   749  C CB  . ILE A 1 119 ? 240.793 260.390 210.117 1.00 7.65   ? 119  ILE A CB  1 
ATOM   750  C CG1 . ILE A 1 119 ? 240.060 259.092 209.753 1.00 7.79   ? 119  ILE A CG1 1 
ATOM   751  C CG2 . ILE A 1 119 ? 239.970 261.252 211.083 1.00 7.89   ? 119  ILE A CG2 1 
ATOM   752  C CD1 . ILE A 1 119 ? 239.868 258.139 210.908 1.00 6.37   ? 119  ILE A CD1 1 
ATOM   753  N N   . VAL A 1 120 ? 241.300 263.606 208.705 1.00 9.81   ? 120  VAL A N   1 
ATOM   754  C CA  . VAL A 1 120 ? 241.939 264.884 208.987 1.00 10.63  ? 120  VAL A CA  1 
ATOM   755  C C   . VAL A 1 120 ? 240.969 265.971 209.417 1.00 12.08  ? 120  VAL A C   1 
ATOM   756  O O   . VAL A 1 120 ? 239.985 266.251 208.730 1.00 12.56  ? 120  VAL A O   1 
ATOM   757  C CB  . VAL A 1 120 ? 242.729 265.367 207.760 1.00 10.79  ? 120  VAL A CB  1 
ATOM   758  C CG1 . VAL A 1 120 ? 243.355 266.712 208.038 1.00 13.52  ? 120  VAL A CG1 1 
ATOM   759  C CG2 . VAL A 1 120 ? 243.803 264.365 207.434 1.00 10.34  ? 120  VAL A CG2 1 
ATOM   760  N N   . ASN A 1 121 ? 241.294 266.624 210.528 1.00 12.53  ? 121  ASN A N   1 
ATOM   761  C CA  . ASN A 1 121 ? 240.546 267.780 210.995 1.00 14.59  ? 121  ASN A CA  1 
ATOM   762  C C   . ASN A 1 121 ? 241.154 269.054 210.416 1.00 16.97  ? 121  ASN A C   1 
ATOM   763  O O   . ASN A 1 121 ? 242.376 269.165 210.317 1.00 16.24  ? 121  ASN A O   1 
ATOM   764  C CB  . ASN A 1 121 ? 240.563 267.852 212.509 1.00 13.39  ? 121  ASN A CB  1 
ATOM   765  C CG  . ASN A 1 121 ? 239.781 266.767 213.163 1.00 11.60  ? 121  ASN A CG  1 
ATOM   766  O OD1 . ASN A 1 121 ? 238.561 266.881 213.317 1.00 11.67  ? 121  ASN A OD1 1 
ATOM   767  N ND2 . ASN A 1 121 ? 240.451 265.713 213.547 1.00 10.44  ? 121  ASN A ND2 1 
ATOM   768  N N   . ASN A 1 122 ? 240.297 270.032 210.102 1.00 19.93  ? 122  ASN A N   1 
ATOM   769  C CA  . ASN A 1 122 ? 240.753 271.358 209.675 1.00 24.98  ? 122  ASN A CA  1 
ATOM   770  C C   . ASN A 1 122 ? 240.051 272.437 210.498 1.00 27.19  ? 122  ASN A C   1 
ATOM   771  O O   . ASN A 1 122 ? 239.493 272.152 211.558 1.00 25.65  ? 122  ASN A O   1 
ATOM   772  C CB  . ASN A 1 122 ? 240.558 271.535 208.164 1.00 27.74  ? 122  ASN A CB  1 
ATOM   773  C CG  . ASN A 1 122 ? 239.123 271.855 207.706 1.00 28.19  ? 122  ASN A CG  1 
ATOM   774  O OD1 . ASN A 1 122 ? 238.198 272.029 208.510 1.00 29.31  ? 122  ASN A OD1 1 
ATOM   775  N ND2 . ASN A 1 122 ? 238.955 271.940 206.396 1.00 31.22  ? 122  ASN A ND2 1 
ATOM   776  N N   . ALA A 1 123 ? 240.108 273.688 210.035 1.00 32.28  ? 123  ALA A N   1 
ATOM   777  C CA  . ALA A 1 123 ? 239.604 274.834 210.784 1.00 34.54  ? 123  ALA A CA  1 
ATOM   778  C C   . ALA A 1 123 ? 238.125 274.734 211.178 1.00 32.27  ? 123  ALA A C   1 
ATOM   779  O O   . ALA A 1 123 ? 237.731 275.272 212.213 1.00 33.30  ? 123  ALA A O   1 
ATOM   780  C CB  . ALA A 1 123 ? 239.814 276.100 209.981 1.00 41.02  ? 123  ALA A CB  1 
ATOM   781  N N   . THR A 1 124 ? 237.292 274.105 210.346 1.00 30.54  ? 124  THR A N   1 
ATOM   782  C CA  . THR A 1 124 ? 235.858 274.110 210.633 1.00 31.07  ? 124  THR A CA  1 
ATOM   783  C C   . THR A 1 124 ? 235.199 272.730 210.670 1.00 26.38  ? 124  THR A C   1 
ATOM   784  O O   . THR A 1 124 ? 234.111 272.583 211.226 1.00 23.77  ? 124  THR A O   1 
ATOM   785  C CB  . THR A 1 124 ? 235.111 274.985 209.614 1.00 38.60  ? 124  THR A CB  1 
ATOM   786  O OG1 . THR A 1 124 ? 235.177 274.377 208.320 1.00 34.80  ? 124  THR A OG1 1 
ATOM   787  C CG2 . THR A 1 124 ? 235.759 276.368 209.547 1.00 50.31  ? 124  THR A CG2 1 
ATOM   788  N N   . ASN A 1 125 ? 235.826 271.726 210.058 1.00 26.84  ? 125  ASN A N   1 
ATOM   789  C CA  . ASN A 1 125 ? 235.191 270.414 209.926 1.00 20.41  ? 125  ASN A CA  1 
ATOM   790  C C   . ASN A 1 125 ? 236.192 269.263 209.956 1.00 16.17  ? 125  ASN A C   1 
ATOM   791  O O   . ASN A 1 125 ? 237.404 269.476 210.002 1.00 20.85  ? 125  ASN A O   1 
ATOM   792  C CB  . ASN A 1 125 ? 234.400 270.345 208.629 1.00 22.55  ? 125  ASN A CB  1 
ATOM   793  C CG  . ASN A 1 125 ? 233.175 271.207 208.633 1.00 24.07  ? 125  ASN A CG  1 
ATOM   794  O OD1 . ASN A 1 125 ? 233.194 272.348 208.154 1.00 27.61  ? 125  ASN A OD1 1 
ATOM   795  N ND2 . ASN A 1 125 ? 232.100 270.682 209.156 1.00 19.76  ? 125  ASN A ND2 1 
ATOM   796  N N   . VAL A 1 126 ? 235.673 268.039 209.875 1.00 15.06  ? 126  VAL A N   1 
ATOM   797  C CA  . VAL A 1 126 ? 236.517 266.855 209.746 1.00 13.85  ? 126  VAL A CA  1 
ATOM   798  C C   . VAL A 1 126 ? 236.165 266.096 208.481 1.00 12.95  ? 126  VAL A C   1 
ATOM   799  O O   . VAL A 1 126 ? 234.993 265.837 208.200 1.00 12.58  ? 126  VAL A O   1 
ATOM   800  C CB  . VAL A 1 126 ? 236.378 265.926 210.974 1.00 12.31  ? 126  VAL A CB  1 
ATOM   801  C CG1 . VAL A 1 126 ? 234.957 265.431 211.120 1.00 11.59  ? 126  VAL A CG1 1 
ATOM   802  C CG2 . VAL A 1 126 ? 237.339 264.746 210.848 1.00 11.18  ? 126  VAL A CG2 1 
ATOM   803  N N   . VAL A 1 127 ? 237.183 265.738 207.715 1.00 11.95  ? 127  VAL A N   1 
ATOM   804  C CA  . VAL A 1 127 ? 236.971 265.023 206.469 1.00 11.12  ? 127  VAL A CA  1 
ATOM   805  C C   . VAL A 1 127 ? 237.609 263.648 206.503 1.00 10.37  ? 127  VAL A C   1 
ATOM   806  O O   . VAL A 1 127 ? 238.809 263.510 206.741 1.00 10.16  ? 127  VAL A O   1 
ATOM   807  C CB  . VAL A 1 127 ? 237.545 265.825 205.290 1.00 11.47  ? 127  VAL A CB  1 
ATOM   808  C CG1 . VAL A 1 127 ? 237.348 265.061 203.990 1.00 11.50  ? 127  VAL A CG1 1 
ATOM   809  C CG2 . VAL A 1 127 ? 236.862 267.175 205.224 1.00 15.52  ? 127  VAL A CG2 1 
ATOM   810  N N   . ILE A 1 128 ? 236.797 262.631 206.257 1.00 9.96   ? 128  ILE A N   1 
ATOM   811  C CA  . ILE A 1 128 ? 237.275 261.262 206.240 1.00 9.31   ? 128  ILE A CA  1 
ATOM   812  C C   . ILE A 1 128 ? 237.117 260.647 204.858 1.00 9.16   ? 128  ILE A C   1 
ATOM   813  O O   . ILE A 1 128 ? 236.013 260.578 204.321 1.00 9.27   ? 128  ILE A O   1 
ATOM   814  C CB  . ILE A 1 128 ? 236.532 260.416 207.282 1.00 8.70   ? 128  ILE A CB  1 
ATOM   815  C CG1 . ILE A 1 128 ? 236.757 261.026 208.678 1.00 8.89   ? 128  ILE A CG1 1 
ATOM   816  C CG2 . ILE A 1 128 ? 237.002 258.980 207.209 1.00 8.60   ? 128  ILE A CG2 1 
ATOM   817  C CD1 . ILE A 1 128 ? 236.060 260.305 209.812 1.00 8.01   ? 128  ILE A CD1 1 
ATOM   818  N N   . LYS A 1 129 ? 238.226 260.207 204.278 1.00 9.06   ? 129  LYS A N   1 
ATOM   819  C CA  . LYS A 1 129 ? 238.196 259.640 202.935 1.00 8.89   ? 129  LYS A CA  1 
ATOM   820  C C   . LYS A 1 129 ? 238.943 258.323 202.845 1.00 8.83   ? 129  LYS A C   1 
ATOM   821  O O   . LYS A 1 129 ? 239.982 258.139 203.481 1.00 8.75   ? 129  LYS A O   1 
ATOM   822  C CB  . LYS A 1 129 ? 238.793 260.621 201.927 1.00 9.26   ? 129  LYS A CB  1 
ATOM   823  C CG  . LYS A 1 129 ? 237.951 261.851 201.668 1.00 9.57   ? 129  LYS A CG  1 
ATOM   824  C CD  . LYS A 1 129 ? 238.651 262.824 200.725 1.00 8.73   ? 129  LYS A CD  1 
ATOM   825  C CE  . LYS A 1 129 ? 238.595 262.343 199.281 1.00 9.35   ? 129  LYS A CE  1 
ATOM   826  N NZ  . LYS A 1 129 ? 238.990 263.413 198.325 1.00 10.03  ? 129  LYS A NZ  1 
ATOM   827  N N   . VAL A 1 130 ? 238.443 257.425 202.005 1.00 9.55   ? 130  VAL A N   1 
ATOM   828  C CA  . VAL A 1 130 ? 239.154 256.193 201.705 1.00 9.39   ? 130  VAL A CA  1 
ATOM   829  C C   . VAL A 1 130 ? 239.422 256.103 200.207 1.00 10.01  ? 130  VAL A C   1 
ATOM   830  O O   . VAL A 1 130 ? 238.482 256.018 199.409 1.00 10.52  ? 130  VAL A O   1 
ATOM   831  C CB  . VAL A 1 130 ? 238.355 254.974 202.179 1.00 8.84   ? 130  VAL A CB  1 
ATOM   832  C CG1 . VAL A 1 130 ? 239.122 253.689 201.894 1.00 8.73   ? 130  VAL A CG1 1 
ATOM   833  C CG2 . VAL A 1 130 ? 238.075 255.124 203.659 1.00 8.23   ? 130  VAL A CG2 1 
ATOM   834  N N   . CYS A 1 131 ? 240.703 256.166 199.839 1.00 10.46  ? 131  CYS A N   1 
ATOM   835  C CA  . CYS A 1 131 ? 241.158 256.240 198.455 1.00 11.03  ? 131  CYS A CA  1 
ATOM   836  C C   . CYS A 1 131 ? 242.507 255.560 198.291 1.00 10.55  ? 131  CYS A C   1 
ATOM   837  O O   . CYS A 1 131 ? 243.174 255.244 199.278 1.00 11.15  ? 131  CYS A O   1 
ATOM   838  C CB  . CYS A 1 131 ? 241.293 257.709 197.993 1.00 12.05  ? 131  CYS A CB  1 
ATOM   839  S SG  . CYS A 1 131 ? 239.817 258.733 198.240 1.00 11.60  ? 131  CYS A SG  1 
ATOM   840  N N   . GLU A 1 132 ? 242.930 255.373 197.054 1.00 11.47  ? 132  GLU A N   1 
ATOM   841  C CA  . GLU A 1 132 ? 244.274 254.869 196.809 1.00 11.26  ? 132  GLU A CA  1 
ATOM   842  C C   . GLU A 1 132 ? 245.241 256.039 196.813 1.00 11.50  ? 132  GLU A C   1 
ATOM   843  O O   . GLU A 1 132 ? 245.660 256.529 195.765 1.00 11.74  ? 132  GLU A O   1 
ATOM   844  C CB  . GLU A 1 132 ? 244.336 254.095 195.492 1.00 11.62  ? 132  GLU A CB  1 
ATOM   845  C CG  . GLU A 1 132 ? 243.512 252.808 195.496 1.00 11.35  ? 132  GLU A CG  1 
ATOM   846  C CD  . GLU A 1 132 ? 243.636 252.020 194.223 1.00 12.71  ? 132  GLU A CD  1 
ATOM   847  O OE1 . GLU A 1 132 ? 244.257 252.501 193.307 1.00 13.70  ? 132  GLU A OE1 1 
ATOM   848  O OE2 . GLU A 1 132 ? 243.109 250.933 194.165 1.00 12.28  ? 132  GLU A OE2 1 
ATOM   849  N N   . PHE A 1 133 ? 245.541 256.518 198.016 1.00 11.56  ? 133  PHE A N   1 
ATOM   850  C CA  . PHE A 1 133 ? 246.344 257.714 198.205 1.00 12.20  ? 133  PHE A CA  1 
ATOM   851  C C   . PHE A 1 133 ? 247.812 257.444 197.948 1.00 11.92  ? 133  PHE A C   1 
ATOM   852  O O   . PHE A 1 133 ? 248.360 256.449 198.415 1.00 11.96  ? 133  PHE A O   1 
ATOM   853  C CB  . PHE A 1 133 ? 246.219 258.226 199.642 1.00 12.09  ? 133  PHE A CB  1 
ATOM   854  C CG  . PHE A 1 133 ? 244.910 258.849 199.998 1.00 11.96  ? 133  PHE A CG  1 
ATOM   855  C CD1 . PHE A 1 133 ? 244.600 260.117 199.573 1.00 12.53  ? 133  PHE A CD1 1 
ATOM   856  C CD2 . PHE A 1 133 ? 243.997 258.175 200.782 1.00 11.23  ? 133  PHE A CD2 1 
ATOM   857  C CE1 . PHE A 1 133 ? 243.400 260.701 199.910 1.00 12.66  ? 133  PHE A CE1 1 
ATOM   858  C CE2 . PHE A 1 133 ? 242.800 258.754 201.128 1.00 10.74  ? 133  PHE A CE2 1 
ATOM   859  C CZ  . PHE A 1 133 ? 242.500 260.019 200.687 1.00 11.25  ? 133  PHE A CZ  1 
ATOM   860  N N   . GLN A 1 134 ? 248.467 258.382 197.282 1.00 12.45  ? 134  GLN A N   1 
ATOM   861  C CA  . GLN A 1 134 ? 249.915 258.350 197.185 1.00 12.50  ? 134  GLN A CA  1 
ATOM   862  C C   . GLN A 1 134 ? 250.477 259.416 198.108 1.00 12.68  ? 134  GLN A C   1 
ATOM   863  O O   . GLN A 1 134 ? 250.498 260.604 197.769 1.00 15.32  ? 134  GLN A O   1 
ATOM   864  C CB  . GLN A 1 134 ? 250.379 258.567 195.746 1.00 12.64  ? 134  GLN A CB  1 
ATOM   865  C CG  . GLN A 1 134 ? 251.887 258.524 195.564 1.00 13.01  ? 134  GLN A CG  1 
ATOM   866  C CD  . GLN A 1 134 ? 252.494 257.196 196.002 1.00 12.26  ? 134  GLN A CD  1 
ATOM   867  O OE1 . GLN A 1 134 ? 251.935 256.115 195.761 1.00 11.92  ? 134  GLN A OE1 1 
ATOM   868  N NE2 . GLN A 1 134 ? 253.653 257.273 196.646 1.00 12.03  ? 134  GLN A NE2 1 
ATOM   869  N N   . PHE A 1 135 ? 250.862 258.985 199.305 1.00 13.24  ? 135  PHE A N   1 
ATOM   870  C CA  . PHE A 1 135 ? 251.231 259.888 200.385 1.00 14.12  ? 135  PHE A CA  1 
ATOM   871  C C   . PHE A 1 135 ? 252.631 260.454 200.209 1.00 16.06  ? 135  PHE A C   1 
ATOM   872  O O   . PHE A 1 135 ? 253.492 259.815 199.599 1.00 15.79  ? 135  PHE A O   1 
ATOM   873  C CB  . PHE A 1 135 ? 251.127 259.168 201.732 1.00 13.55  ? 135  PHE A CB  1 
ATOM   874  C CG  . PHE A 1 135 ? 249.713 258.898 202.161 1.00 12.51  ? 135  PHE A CG  1 
ATOM   875  C CD1 . PHE A 1 135 ? 248.868 259.940 202.490 1.00 12.82  ? 135  PHE A CD1 1 
ATOM   876  C CD2 . PHE A 1 135 ? 249.230 257.607 202.243 1.00 11.57  ? 135  PHE A CD2 1 
ATOM   877  C CE1 . PHE A 1 135 ? 247.568 259.702 202.883 1.00 11.59  ? 135  PHE A CE1 1 
ATOM   878  C CE2 . PHE A 1 135 ? 247.934 257.363 202.639 1.00 10.97  ? 135  PHE A CE2 1 
ATOM   879  C CZ  . PHE A 1 135 ? 247.100 258.415 202.959 1.00 11.09  ? 135  PHE A CZ  1 
ATOM   880  N N   . CYS A 1 136 ? 252.855 261.647 200.770 1.00 16.63  ? 136  CYS A N   1 
ATOM   881  C CA  . CYS A 1 136 ? 254.157 262.309 200.767 1.00 18.70  ? 136  CYS A CA  1 
ATOM   882  C C   . CYS A 1 136 ? 255.148 261.568 201.670 1.00 18.49  ? 136  CYS A C   1 
ATOM   883  O O   . CYS A 1 136 ? 254.756 260.789 202.540 1.00 17.49  ? 136  CYS A O   1 
ATOM   884  C CB  . CYS A 1 136 ? 254.028 263.765 201.243 1.00 19.46  ? 136  CYS A CB  1 
ATOM   885  S SG  . CYS A 1 136 ? 252.983 264.825 200.201 1.00 19.71  ? 136  CYS A SG  1 
ATOM   886  N N   . ASN A 1 137 ? 256.437 261.830 201.472 1.00 19.03  ? 137  ASN A N   1 
ATOM   887  C CA  . ASN A 1 137 ? 257.481 261.172 202.256 1.00 19.36  ? 137  ASN A CA  1 
ATOM   888  C C   . ASN A 1 137 ? 257.370 261.502 203.739 1.00 19.43  ? 137  ASN A C   1 
ATOM   889  O O   . ASN A 1 137 ? 257.719 260.688 204.595 1.00 19.76  ? 137  ASN A O   1 
ATOM   890  C CB  . ASN A 1 137 ? 258.849 261.560 201.731 1.00 20.03  ? 137  ASN A CB  1 
ATOM   891  C CG  . ASN A 1 137 ? 259.164 260.907 200.424 1.00 22.20  ? 137  ASN A CG  1 
ATOM   892  O OD1 . ASN A 1 137 ? 258.698 259.798 200.139 1.00 20.37  ? 137  ASN A OD1 1 
ATOM   893  N ND2 . ASN A 1 137 ? 259.938 261.576 199.610 1.00 26.15  ? 137  ASN A ND2 1 
ATOM   894  N N   . ASP A 1 138 ? 256.876 262.696 204.038 1.00 19.60  ? 138  ASP A N   1 
ATOM   895  C CA  . ASP A 1 138 ? 256.674 263.129 205.411 1.00 19.77  ? 138  ASP A CA  1 
ATOM   896  C C   . ASP A 1 138 ? 255.525 264.131 205.453 1.00 19.43  ? 138  ASP A C   1 
ATOM   897  O O   . ASP A 1 138 ? 255.759 265.337 205.466 1.00 19.86  ? 138  ASP A O   1 
ATOM   898  C CB  . ASP A 1 138 ? 257.947 263.766 205.974 1.00 21.09  ? 138  ASP A CB  1 
ATOM   899  C CG  . ASP A 1 138 ? 257.876 264.016 207.482 1.00 21.39  ? 138  ASP A CG  1 
ATOM   900  O OD1 . ASP A 1 138 ? 256.885 263.669 208.082 1.00 20.59  ? 138  ASP A OD1 1 
ATOM   901  O OD2 . ASP A 1 138 ? 258.820 264.548 208.021 1.00 22.71  ? 138  ASP A OD2 1 
ATOM   902  N N   . PRO A 1 139 ? 254.281 263.642 205.422 1.00 19.58  ? 139  PRO A N   1 
ATOM   903  C CA  . PRO A 1 139 ? 253.055 264.377 205.170 1.00 18.13  ? 139  PRO A CA  1 
ATOM   904  C C   . PRO A 1 139 ? 252.696 265.290 206.330 1.00 19.79  ? 139  PRO A C   1 
ATOM   905  O O   . PRO A 1 139 ? 252.911 264.936 207.489 1.00 18.77  ? 139  PRO A O   1 
ATOM   906  C CB  . PRO A 1 139 ? 252.038 263.246 205.006 1.00 17.48  ? 139  PRO A CB  1 
ATOM   907  C CG  . PRO A 1 139 ? 252.583 262.113 205.843 1.00 15.47  ? 139  PRO A CG  1 
ATOM   908  C CD  . PRO A 1 139 ? 254.087 262.227 205.735 1.00 17.26  ? 139  PRO A CD  1 
ATOM   909  N N   . PHE A 1 140 ? 252.120 266.447 206.019 1.00 20.46  ? 140  PHE A N   1 
ATOM   910  C CA  . PHE A 1 140 ? 251.673 267.378 207.051 1.00 20.37  ? 140  PHE A CA  1 
ATOM   911  C C   . PHE A 1 140 ? 250.720 268.433 206.501 1.00 20.80  ? 140  PHE A C   1 
ATOM   912  O O   . PHE A 1 140 ? 250.513 268.538 205.292 1.00 21.79  ? 140  PHE A O   1 
ATOM   913  C CB  . PHE A 1 140 ? 252.865 268.059 207.737 1.00 21.70  ? 140  PHE A CB  1 
ATOM   914  C CG  . PHE A 1 140 ? 253.731 268.904 206.839 1.00 22.01  ? 140  PHE A CG  1 
ATOM   915  C CD1 . PHE A 1 140 ? 254.778 268.343 206.147 1.00 22.12  ? 140  PHE A CD1 1 
ATOM   916  C CD2 . PHE A 1 140 ? 253.511 270.264 206.709 1.00 23.83  ? 140  PHE A CD2 1 
ATOM   917  C CE1 . PHE A 1 140 ? 255.586 269.111 205.339 1.00 24.19  ? 140  PHE A CE1 1 
ATOM   918  C CE2 . PHE A 1 140 ? 254.316 271.037 205.904 1.00 25.27  ? 140  PHE A CE2 1 
ATOM   919  C CZ  . PHE A 1 140 ? 255.357 270.460 205.217 1.00 26.42  ? 140  PHE A CZ  1 
ATOM   920  N N   . LEU A 1 141 ? 250.156 269.226 207.404 1.00 20.73  ? 141  LEU A N   1 
ATOM   921  C CA  . LEU A 1 141 ? 249.335 270.366 207.020 1.00 21.99  ? 141  LEU A CA  1 
ATOM   922  C C   . LEU A 1 141 ? 250.106 271.649 207.292 1.00 23.11  ? 141  LEU A C   1 
ATOM   923  O O   . LEU A 1 141 ? 250.791 271.756 208.309 1.00 24.53  ? 141  LEU A O   1 
ATOM   924  C CB  . LEU A 1 141 ? 248.021 270.370 207.812 1.00 19.89  ? 141  LEU A CB  1 
ATOM   925  C CG  . LEU A 1 141 ? 246.918 269.416 207.318 1.00 18.47  ? 141  LEU A CG  1 
ATOM   926  C CD1 . LEU A 1 141 ? 247.208 267.988 207.787 1.00 17.08  ? 141  LEU A CD1 1 
ATOM   927  C CD2 . LEU A 1 141 ? 245.582 269.897 207.851 1.00 17.46  ? 141  LEU A CD2 1 
ATOM   928  N N   . GLY A 1 142 ? 250.041 272.605 206.373 1.00 26.40  ? 142  GLY A N   1 
ATOM   929  C CA  . GLY A 1 142 ? 250.772 273.854 206.547 1.00 30.12  ? 142  GLY A CA  1 
ATOM   930  C C   . GLY A 1 142 ? 249.884 274.964 207.086 1.00 33.60  ? 142  GLY A C   1 
ATOM   931  O O   . GLY A 1 142 ? 248.779 275.186 206.583 1.00 34.33  ? 142  GLY A O   1 
ATOM   932  N N   . VAL A 1 143 ? 250.399 275.689 208.075 1.00 34.64  ? 143  VAL A N   1 
ATOM   933  C CA  . VAL A 1 143 ? 249.720 276.843 208.653 1.00 39.41  ? 143  VAL A CA  1 
ATOM   934  C C   . VAL A 1 143 ? 250.679 278.022 208.782 1.00 41.49  ? 143  VAL A C   1 
ATOM   935  O O   . VAL A 1 143 ? 251.894 277.852 208.696 1.00 39.10  ? 143  VAL A O   1 
ATOM   936  C CB  . VAL A 1 143 ? 249.139 276.496 210.040 1.00 38.10  ? 143  VAL A CB  1 
ATOM   937  C CG1 . VAL A 1 143 ? 248.136 275.361 209.917 1.00 34.50  ? 143  VAL A CG1 1 
ATOM   938  C CG2 . VAL A 1 143 ? 250.264 276.113 210.990 1.00 34.43  ? 143  VAL A CG2 1 
ATOM   939  N N   . TYR A 1 144 ? 250.135 279.206 209.034 1.00 46.00  ? 144  TYR A N   1 
ATOM   940  C CA  . TYR A 1 144 ? 250.965 280.357 209.373 1.00 50.55  ? 144  TYR A CA  1 
ATOM   941  C C   . TYR A 1 144 ? 250.310 281.178 210.472 1.00 55.63  ? 144  TYR A C   1 
ATOM   942  O O   . TYR A 1 144 ? 249.114 281.043 210.734 1.00 55.19  ? 144  TYR A O   1 
ATOM   943  C CB  . TYR A 1 144 ? 251.271 281.211 208.143 1.00 53.11  ? 144  TYR A CB  1 
ATOM   944  C CG  . TYR A 1 144 ? 250.096 281.924 207.539 1.00 55.48  ? 144  TYR A CG  1 
ATOM   945  C CD1 . TYR A 1 144 ? 249.806 283.225 207.911 1.00 60.94  ? 144  TYR A CD1 1 
ATOM   946  C CD2 . TYR A 1 144 ? 249.324 281.289 206.591 1.00 52.09  ? 144  TYR A CD2 1 
ATOM   947  C CE1 . TYR A 1 144 ? 248.751 283.883 207.326 1.00 65.04  ? 144  TYR A CE1 1 
ATOM   948  C CE2 . TYR A 1 144 ? 248.270 281.945 206.007 1.00 55.83  ? 144  TYR A CE2 1 
ATOM   949  C CZ  . TYR A 1 144 ? 247.985 283.238 206.367 1.00 64.85  ? 144  TYR A CZ  1 
ATOM   950  O OH  . TYR A 1 144 ? 246.942 283.898 205.772 1.00 69.25  ? 144  TYR A OH  1 
ATOM   951  N N   . TYR A 1 145 ? 251.109 281.988 211.154 1.00 57.56  ? 145  TYR A N   1 
ATOM   952  C CA  . TYR A 1 145 ? 250.632 282.709 212.327 1.00 62.01  ? 145  TYR A CA  1 
ATOM   953  C C   . TYR A 1 145 ? 250.517 284.213 212.129 1.00 67.65  ? 145  TYR A C   1 
ATOM   954  O O   . TYR A 1 145 ? 251.181 284.802 211.276 1.00 68.49  ? 145  TYR A O   1 
ATOM   955  C CB  . TYR A 1 145 ? 251.524 282.396 213.526 1.00 61.12  ? 145  TYR A CB  1 
ATOM   956  C CG  . TYR A 1 145 ? 251.317 281.001 214.063 1.00 56.67  ? 145  TYR A CG  1 
ATOM   957  C CD1 . TYR A 1 145 ? 251.995 279.927 213.509 1.00 48.44  ? 145  TYR A CD1 1 
ATOM   958  C CD2 . TYR A 1 145 ? 250.437 280.798 215.110 1.00 57.75  ? 145  TYR A CD2 1 
ATOM   959  C CE1 . TYR A 1 145 ? 251.787 278.657 214.004 1.00 45.19  ? 145  TYR A CE1 1 
ATOM   960  C CE2 . TYR A 1 145 ? 250.232 279.531 215.604 1.00 55.34  ? 145  TYR A CE2 1 
ATOM   961  C CZ  . TYR A 1 145 ? 250.902 278.462 215.053 1.00 46.90  ? 145  TYR A CZ  1 
ATOM   962  O OH  . TYR A 1 145 ? 250.694 277.194 215.543 1.00 44.25  ? 145  TYR A OH  1 
ATOM   963  N N   . HIS A 1 146 ? 249.662 284.814 212.950 1.00 71.78  ? 146  HIS A N   1 
ATOM   964  C CA  . HIS A 1 146 ? 249.424 286.251 213.000 1.00 75.57  ? 146  HIS A CA  1 
ATOM   965  C C   . HIS A 1 146 ? 250.655 286.969 213.543 1.00 79.92  ? 146  HIS A C   1 
ATOM   966  O O   . HIS A 1 146 ? 251.660 286.333 213.864 1.00 79.40  ? 146  HIS A O   1 
ATOM   967  C CB  . HIS A 1 146 ? 248.207 286.525 213.899 1.00 77.11  ? 146  HIS A CB  1 
ATOM   968  C CG  . HIS A 1 146 ? 247.676 287.925 213.879 1.00 91.28  ? 146  HIS A CG  1 
ATOM   969  N ND1 . HIS A 1 146 ? 248.317 288.976 214.501 1.00 82.45  ? 146  HIS A ND1 1 
ATOM   970  C CD2 . HIS A 1 146 ? 246.551 288.440 213.335 1.00 81.52  ? 146  HIS A CD2 1 
ATOM   971  C CE1 . HIS A 1 146 ? 247.610 290.082 214.327 1.00 87.16  ? 146  HIS A CE1 1 
ATOM   972  N NE2 . HIS A 1 146 ? 246.536 289.781 213.623 1.00 84.95  ? 146  HIS A NE2 1 
ATOM   973  N N   . LYS A 1 147 ? 250.586 288.295 213.644 1.00 82.75  ? 147  LYS A N   1 
ATOM   974  C CA  . LYS A 1 147 ? 251.675 289.050 214.254 1.00 84.68  ? 147  LYS A CA  1 
ATOM   975  C C   . LYS A 1 147 ? 251.829 288.605 215.703 1.00 82.08  ? 147  LYS A C   1 
ATOM   976  O O   . LYS A 1 147 ? 252.939 288.538 216.233 1.00 83.33  ? 147  LYS A O   1 
ATOM   977  C CB  . LYS A 1 147 ? 251.413 290.561 214.183 1.00 91.00  ? 147  LYS A CB  1 
ATOM   978  N N   . ASN A 1 148 ? 250.702 288.278 216.330 1.00 81.77  ? 148  ASN A N   1 
ATOM   979  C CA  . ASN A 1 148 ? 250.696 287.748 217.688 1.00 80.92  ? 148  ASN A CA  1 
ATOM   980  C C   . ASN A 1 148 ? 250.729 286.215 217.655 1.00 86.36  ? 148  ASN A C   1 
ATOM   981  O O   . ASN A 1 148 ? 250.668 285.614 216.585 1.00 78.88  ? 148  ASN A O   1 
ATOM   982  C CB  . ASN A 1 148 ? 249.493 288.280 218.453 1.00 80.28  ? 148  ASN A CB  1 
ATOM   983  N N   . ASN A 1 149 ? 250.825 285.589 218.840 1.00 79.73  ? 149  ASN A N   1 
ATOM   984  C CA  . ASN A 1 149 ? 250.939 284.131 218.950 1.00 80.65  ? 149  ASN A CA  1 
ATOM   985  C C   . ASN A 1 149 ? 249.617 283.489 219.417 1.00 79.81  ? 149  ASN A C   1 
ATOM   986  O O   . ASN A 1 149 ? 249.621 282.359 219.909 1.00 79.52  ? 149  ASN A O   1 
ATOM   987  C CB  . ASN A 1 149 ? 252.077 283.757 219.898 1.00 81.29  ? 149  ASN A CB  1 
ATOM   988  C CG  . ASN A 1 149 ? 253.422 284.359 219.480 1.00 82.71  ? 149  ASN A CG  1 
ATOM   989  O OD1 . ASN A 1 149 ? 253.955 284.035 218.411 1.00 82.33  ? 149  ASN A OD1 1 
ATOM   990  N ND2 . ASN A 1 149 ? 253.965 285.223 220.317 1.00 84.22  ? 149  ASN A ND2 1 
ATOM   991  N N   . LYS A 1 150 ? 248.498 284.209 219.265 1.00 79.22  ? 150  LYS A N   1 
ATOM   992  C CA  . LYS A 1 150 ? 247.176 283.733 219.691 1.00 80.02  ? 150  LYS A CA  1 
ATOM   993  C C   . LYS A 1 150 ? 246.247 283.479 218.511 1.00 78.30  ? 150  LYS A C   1 
ATOM   994  O O   . LYS A 1 150 ? 245.065 283.190 218.696 1.00 77.55  ? 150  LYS A O   1 
ATOM   995  C CB  . LYS A 1 150 ? 246.532 284.744 220.639 1.00 81.82  ? 150  LYS A CB  1 
ATOM   996  N N   . SER A 1 151 ? 246.769 283.606 217.298 1.00 76.88  ? 151  SER A N   1 
ATOM   997  C CA  . SER A 1 151 ? 245.936 283.485 216.108 1.00 74.29  ? 151  SER A CA  1 
ATOM   998  C C   . SER A 1 151 ? 246.699 282.875 214.941 1.00 71.40  ? 151  SER A C   1 
ATOM   999  O O   . SER A 1 151 ? 247.896 283.116 214.773 1.00 67.45  ? 151  SER A O   1 
ATOM   1000 C CB  . SER A 1 151 ? 245.401 284.849 215.719 1.00 77.40  ? 151  SER A CB  1 
ATOM   1001 O OG  . SER A 1 151 ? 244.566 284.769 214.597 1.00 73.95  ? 151  SER A OG  1 
ATOM   1002 N N   . TRP A 1 152 ? 245.996 282.073 214.144 1.00 65.93  ? 152  TRP A N   1 
ATOM   1003 C CA  . TRP A 1 152 ? 246.585 281.411 212.987 1.00 62.87  ? 152  TRP A CA  1 
ATOM   1004 C C   . TRP A 1 152 ? 245.589 281.253 211.848 1.00 61.75  ? 152  TRP A C   1 
ATOM   1005 O O   . TRP A 1 152 ? 244.374 281.355 212.042 1.00 67.31  ? 152  TRP A O   1 
ATOM   1006 C CB  . TRP A 1 152 ? 247.131 280.034 213.370 1.00 59.24  ? 152  TRP A CB  1 
ATOM   1007 C CG  . TRP A 1 152 ? 246.104 279.122 213.958 1.00 59.74  ? 152  TRP A CG  1 
ATOM   1008 C CD1 . TRP A 1 152 ? 245.852 278.958 215.280 1.00 60.93  ? 152  TRP A CD1 1 
ATOM   1009 C CD2 . TRP A 1 152 ? 245.178 278.246 213.262 1.00 57.68  ? 152  TRP A CD2 1 
ATOM   1010 N NE1 . TRP A 1 152 ? 244.843 278.051 215.459 1.00 58.39  ? 152  TRP A NE1 1 
ATOM   1011 C CE2 . TRP A 1 152 ? 244.416 277.609 214.237 1.00 57.93  ? 152  TRP A CE2 1 
ATOM   1012 C CE3 . TRP A 1 152 ? 244.940 277.958 211.914 1.00 54.00  ? 152  TRP A CE3 1 
ATOM   1013 C CZ2 . TRP A 1 152 ? 243.422 276.702 213.915 1.00 55.40  ? 152  TRP A CZ2 1 
ATOM   1014 C CZ3 . TRP A 1 152 ? 243.944 277.048 211.591 1.00 49.75  ? 152  TRP A CZ3 1 
ATOM   1015 C CH2 . TRP A 1 152 ? 243.204 276.438 212.566 1.00 49.89  ? 152  TRP A CH2 1 
ATOM   1016 N N   . MET A 1 153 ? 246.124 280.999 210.659 1.00 58.54  ? 153  MET A N   1 
ATOM   1017 C CA  . MET A 1 153 ? 245.324 280.760 209.466 1.00 57.48  ? 153  MET A CA  1 
ATOM   1018 C C   . MET A 1 153 ? 245.949 279.638 208.640 1.00 52.45  ? 153  MET A C   1 
ATOM   1019 O O   . MET A 1 153 ? 247.156 279.409 208.705 1.00 48.22  ? 153  MET A O   1 
ATOM   1020 C CB  . MET A 1 153 ? 245.200 282.049 208.657 1.00 61.62  ? 153  MET A CB  1 
ATOM   1021 C CG  . MET A 1 153 ? 244.262 281.969 207.456 1.00 61.26  ? 153  MET A CG  1 
ATOM   1022 S SD  . MET A 1 153 ? 244.112 283.539 206.565 1.00 69.13  ? 153  MET A SD  1 
ATOM   1023 C CE  . MET A 1 153 ? 243.298 284.589 207.758 1.00 82.81  ? 153  MET A CE  1 
ATOM   1024 N N   . GLU A 1 154 ? 245.122 278.916 207.891 1.00 50.50  ? 154  GLU A N   1 
ATOM   1025 C CA  . GLU A 1 154 ? 245.596 277.794 207.087 1.00 44.59  ? 154  GLU A CA  1 
ATOM   1026 C C   . GLU A 1 154 ? 246.389 278.256 205.872 1.00 43.18  ? 154  GLU A C   1 
ATOM   1027 O O   . GLU A 1 154 ? 246.133 279.329 205.326 1.00 46.15  ? 154  GLU A O   1 
ATOM   1028 C CB  . GLU A 1 154 ? 244.417 276.935 206.631 1.00 41.80  ? 154  GLU A CB  1 
ATOM   1029 N N   . SER A 1 155 ? 247.342 277.430 205.440 1.00 39.67  ? 155  SER A N   1 
ATOM   1030 C CA  . SER A 1 155 ? 248.163 277.748 204.276 1.00 37.68  ? 155  SER A CA  1 
ATOM   1031 C C   . SER A 1 155 ? 247.931 276.782 203.118 1.00 35.25  ? 155  SER A C   1 
ATOM   1032 O O   . SER A 1 155 ? 247.459 277.180 202.053 1.00 35.14  ? 155  SER A O   1 
ATOM   1033 C CB  . SER A 1 155 ? 249.633 277.724 204.649 1.00 38.91  ? 155  SER A CB  1 
ATOM   1034 O OG  . SER A 1 155 ? 250.432 278.069 203.555 1.00 37.20  ? 155  SER A OG  1 
ATOM   1035 N N   . GLU A 1 156 ? 248.311 275.520 203.314 1.00 33.14  ? 156  GLU A N   1 
ATOM   1036 C CA  . GLU A 1 156 ? 248.257 274.527 202.242 1.00 30.32  ? 156  GLU A CA  1 
ATOM   1037 C C   . GLU A 1 156 ? 248.109 273.111 202.796 1.00 27.23  ? 156  GLU A C   1 
ATOM   1038 O O   . GLU A 1 156 ? 248.497 272.831 203.931 1.00 26.98  ? 156  GLU A O   1 
ATOM   1039 C CB  . GLU A 1 156 ? 249.516 274.636 201.365 1.00 29.82  ? 156  GLU A CB  1 
ATOM   1040 C CG  . GLU A 1 156 ? 249.565 273.705 200.142 1.00 27.90  ? 156  GLU A CG  1 
ATOM   1041 C CD  . GLU A 1 156 ? 248.417 273.904 199.185 1.00 28.89  ? 156  GLU A CD  1 
ATOM   1042 O OE1 . GLU A 1 156 ? 247.338 273.446 199.482 1.00 28.86  ? 156  GLU A OE1 1 
ATOM   1043 O OE2 . GLU A 1 156 ? 248.621 274.508 198.158 1.00 29.60  ? 156  GLU A OE2 1 
ATOM   1044 N N   . PHE A 1 157 ? 247.556 272.217 201.985 1.00 26.25  ? 157  PHE A N   1 
ATOM   1045 C CA  . PHE A 1 157 ? 247.373 270.824 202.377 1.00 24.62  ? 157  PHE A CA  1 
ATOM   1046 C C   . PHE A 1 157 ? 248.437 269.953 201.714 1.00 23.51  ? 157  PHE A C   1 
ATOM   1047 O O   . PHE A 1 157 ? 248.449 269.806 200.493 1.00 23.74  ? 157  PHE A O   1 
ATOM   1048 C CB  . PHE A 1 157 ? 245.975 270.363 201.968 1.00 22.97  ? 157  PHE A CB  1 
ATOM   1049 C CG  . PHE A 1 157 ? 245.518 269.117 202.631 1.00 20.88  ? 157  PHE A CG  1 
ATOM   1050 C CD1 . PHE A 1 157 ? 244.905 269.189 203.864 1.00 19.94  ? 157  PHE A CD1 1 
ATOM   1051 C CD2 . PHE A 1 157 ? 245.679 267.883 202.039 1.00 20.09  ? 157  PHE A CD2 1 
ATOM   1052 C CE1 . PHE A 1 157 ? 244.463 268.060 204.495 1.00 18.36  ? 157  PHE A CE1 1 
ATOM   1053 C CE2 . PHE A 1 157 ? 245.235 266.744 202.674 1.00 19.24  ? 157  PHE A CE2 1 
ATOM   1054 C CZ  . PHE A 1 157 ? 244.625 266.834 203.905 1.00 18.27  ? 157  PHE A CZ  1 
ATOM   1055 N N   . ARG A 1 158 ? 249.361 269.412 202.509 1.00 22.50  ? 158  ARG A N   1 
ATOM   1056 C CA  . ARG A 1 158 ? 250.516 268.712 201.955 1.00 22.23  ? 158  ARG A CA  1 
ATOM   1057 C C   . ARG A 1 158 ? 250.636 267.296 202.508 1.00 20.67  ? 158  ARG A C   1 
ATOM   1058 O O   . ARG A 1 158 ? 251.673 266.919 203.054 1.00 20.45  ? 158  ARG A O   1 
ATOM   1059 C CB  . ARG A 1 158 ? 251.786 269.478 202.285 1.00 24.16  ? 158  ARG A CB  1 
ATOM   1060 C CG  . ARG A 1 158 ? 251.828 270.902 201.753 1.00 24.99  ? 158  ARG A CG  1 
ATOM   1061 C CD  . ARG A 1 158 ? 253.059 271.604 202.177 1.00 25.85  ? 158  ARG A CD  1 
ATOM   1062 N NE  . ARG A 1 158 ? 253.033 273.020 201.832 1.00 27.15  ? 158  ARG A NE  1 
ATOM   1063 C CZ  . ARG A 1 158 ? 253.393 273.535 200.639 1.00 26.80  ? 158  ARG A CZ  1 
ATOM   1064 N NH1 . ARG A 1 158 ? 253.337 274.834 200.445 1.00 28.33  ? 158  ARG A NH1 1 
ATOM   1065 N NH2 . ARG A 1 158 ? 253.798 272.742 199.663 1.00 25.99  ? 158  ARG A NH2 1 
ATOM   1066 N N   . VAL A 1 159 ? 249.565 266.523 202.380 1.00 19.78  ? 159  VAL A N   1 
ATOM   1067 C CA  . VAL A 1 159 ? 249.525 265.174 202.926 1.00 18.18  ? 159  VAL A CA  1 
ATOM   1068 C C   . VAL A 1 159 ? 249.816 264.130 201.859 1.00 16.82  ? 159  VAL A C   1 
ATOM   1069 O O   . VAL A 1 159 ? 250.545 263.168 202.101 1.00 16.61  ? 159  VAL A O   1 
ATOM   1070 C CB  . VAL A 1 159 ? 248.156 264.903 203.571 1.00 17.26  ? 159  VAL A CB  1 
ATOM   1071 C CG1 . VAL A 1 159 ? 248.061 263.465 204.034 1.00 14.51  ? 159  VAL A CG1 1 
ATOM   1072 C CG2 . VAL A 1 159 ? 247.963 265.851 204.743 1.00 17.83  ? 159  VAL A CG2 1 
ATOM   1073 N N   . TYR A 1 160 ? 249.218 264.306 200.688 1.00 16.45  ? 160  TYR A N   1 
ATOM   1074 C CA  . TYR A 1 160 ? 249.395 263.362 199.595 1.00 15.59  ? 160  TYR A CA  1 
ATOM   1075 C C   . TYR A 1 160 ? 249.579 264.087 198.273 1.00 15.48  ? 160  TYR A C   1 
ATOM   1076 O O   . TYR A 1 160 ? 249.124 265.218 198.109 1.00 16.57  ? 160  TYR A O   1 
ATOM   1077 C CB  . TYR A 1 160 ? 248.207 262.396 199.524 1.00 15.17  ? 160  TYR A CB  1 
ATOM   1078 C CG  . TYR A 1 160 ? 246.872 263.067 199.332 1.00 13.78  ? 160  TYR A CG  1 
ATOM   1079 C CD1 . TYR A 1 160 ? 246.409 263.348 198.061 1.00 13.92  ? 160  TYR A CD1 1 
ATOM   1080 C CD2 . TYR A 1 160 ? 246.103 263.391 200.433 1.00 14.58  ? 160  TYR A CD2 1 
ATOM   1081 C CE1 . TYR A 1 160 ? 245.186 263.955 197.890 1.00 13.79  ? 160  TYR A CE1 1 
ATOM   1082 C CE2 . TYR A 1 160 ? 244.879 263.997 200.262 1.00 14.46  ? 160  TYR A CE2 1 
ATOM   1083 C CZ  . TYR A 1 160 ? 244.421 264.280 198.999 1.00 13.92  ? 160  TYR A CZ  1 
ATOM   1084 O OH  . TYR A 1 160 ? 243.199 264.888 198.833 1.00 13.05  ? 160  TYR A OH  1 
ATOM   1085 N N   . SER A 1 161 ? 250.256 263.427 197.336 1.00 15.44  ? 161  SER A N   1 
ATOM   1086 C CA  . SER A 1 161 ? 250.507 263.994 196.016 1.00 15.58  ? 161  SER A CA  1 
ATOM   1087 C C   . SER A 1 161 ? 249.356 263.730 195.056 1.00 14.37  ? 161  SER A C   1 
ATOM   1088 O O   . SER A 1 161 ? 249.105 264.511 194.138 1.00 15.11  ? 161  SER A O   1 
ATOM   1089 C CB  . SER A 1 161 ? 251.778 263.406 195.442 1.00 15.01  ? 161  SER A CB  1 
ATOM   1090 O OG  . SER A 1 161 ? 251.633 262.029 195.217 1.00 14.50  ? 161  SER A OG  1 
ATOM   1091 N N   . SER A 1 162 ? 248.654 262.627 195.276 1.00 14.00  ? 162  SER A N   1 
ATOM   1092 C CA  . SER A 1 162 ? 247.515 262.275 194.433 1.00 13.96  ? 162  SER A CA  1 
ATOM   1093 C C   . SER A 1 162 ? 246.576 261.299 195.133 1.00 12.99  ? 162  SER A C   1 
ATOM   1094 O O   . SER A 1 162 ? 246.963 260.616 196.082 1.00 15.66  ? 162  SER A O   1 
ATOM   1095 C CB  . SER A 1 162 ? 247.995 261.683 193.122 1.00 13.49  ? 162  SER A CB  1 
ATOM   1096 O OG  . SER A 1 162 ? 248.640 260.461 193.330 1.00 13.84  ? 162  SER A OG  1 
ATOM   1097 N N   . ALA A 1 163 ? 245.344 261.209 194.634 1.00 13.34  ? 163  ALA A N   1 
ATOM   1098 C CA  . ALA A 1 163 ? 244.377 260.236 195.133 1.00 13.18  ? 163  ALA A CA  1 
ATOM   1099 C C   . ALA A 1 163 ? 243.407 259.839 194.035 1.00 13.69  ? 163  ALA A C   1 
ATOM   1100 O O   . ALA A 1 163 ? 242.937 260.690 193.280 1.00 14.62  ? 163  ALA A O   1 
ATOM   1101 C CB  . ALA A 1 163 ? 243.608 260.809 196.308 1.00 13.73  ? 163  ALA A CB  1 
ATOM   1102 N N   . ASN A 1 164 ? 243.078 258.555 193.973 1.00 13.11  ? 164  ASN A N   1 
ATOM   1103 C CA  . ASN A 1 164 ? 242.125 258.054 192.992 1.00 13.38  ? 164  ASN A CA  1 
ATOM   1104 C C   . ASN A 1 164 ? 241.343 256.878 193.567 1.00 11.93  ? 164  ASN A C   1 
ATOM   1105 O O   . ASN A 1 164 ? 241.601 256.452 194.693 1.00 14.30  ? 164  ASN A O   1 
ATOM   1106 C CB  . ASN A 1 164 ? 242.858 257.647 191.722 1.00 13.12  ? 164  ASN A CB  1 
ATOM   1107 C CG  . ASN A 1 164 ? 243.460 258.805 191.003 1.00 13.68  ? 164  ASN A CG  1 
ATOM   1108 O OD1 . ASN A 1 164 ? 242.750 259.591 190.367 1.00 14.86  ? 164  ASN A OD1 1 
ATOM   1109 N ND2 . ASN A 1 164 ? 244.759 258.933 191.084 1.00 13.22  ? 164  ASN A ND2 1 
ATOM   1110 N N   . ASN A 1 165 ? 240.398 256.339 192.778 1.00 12.49  ? 165  ASN A N   1 
ATOM   1111 C CA  . ASN A 1 165 ? 239.643 255.140 193.143 1.00 11.42  ? 165  ASN A CA  1 
ATOM   1112 C C   . ASN A 1 165 ? 239.005 255.269 194.542 1.00 11.56  ? 165  ASN A C   1 
ATOM   1113 O O   . ASN A 1 165 ? 239.127 254.365 195.363 1.00 11.01  ? 165  ASN A O   1 
ATOM   1114 C CB  . ASN A 1 165 ? 240.522 253.896 193.070 1.00 12.65  ? 165  ASN A CB  1 
ATOM   1115 C CG  . ASN A 1 165 ? 241.347 253.797 191.789 1.00 13.29  ? 165  ASN A CG  1 
ATOM   1116 O OD1 . ASN A 1 165 ? 242.383 254.464 191.655 1.00 13.29  ? 165  ASN A OD1 1 
ATOM   1117 N ND2 . ASN A 1 165 ? 240.908 252.971 190.863 1.00 15.51  ? 165  ASN A ND2 1 
ATOM   1118 N N   . CYS A 1 166 ? 238.357 256.408 194.806 1.00 11.75  ? 166  CYS A N   1 
ATOM   1119 C CA  . CYS A 1 166 ? 237.764 256.673 196.123 1.00 11.80  ? 166  CYS A CA  1 
ATOM   1120 C C   . CYS A 1 166 ? 236.466 255.895 196.328 1.00 11.25  ? 166  CYS A C   1 
ATOM   1121 O O   . CYS A 1 166 ? 235.584 255.888 195.467 1.00 11.57  ? 166  CYS A O   1 
ATOM   1122 C CB  . CYS A 1 166 ? 237.526 258.179 196.309 1.00 12.12  ? 166  CYS A CB  1 
ATOM   1123 S SG  . CYS A 1 166 ? 239.060 259.161 196.397 1.00 12.86  ? 166  CYS A SG  1 
ATOM   1124 N N   . THR A 1 167 ? 236.361 255.225 197.479 1.00 10.66  ? 167  THR A N   1 
ATOM   1125 C CA  . THR A 1 167 ? 235.209 254.377 197.773 1.00 9.30   ? 167  THR A CA  1 
ATOM   1126 C C   . THR A 1 167 ? 234.349 254.902 198.916 1.00 9.67   ? 167  THR A C   1 
ATOM   1127 O O   . THR A 1 167 ? 233.193 254.507 199.057 1.00 10.94  ? 167  THR A O   1 
ATOM   1128 C CB  . THR A 1 167 ? 235.653 252.949 198.134 1.00 9.72   ? 167  THR A CB  1 
ATOM   1129 O OG1 . THR A 1 167 ? 236.436 252.994 199.332 1.00 10.02  ? 167  THR A OG1 1 
ATOM   1130 C CG2 . THR A 1 167 ? 236.486 252.345 197.015 1.00 10.14  ? 167  THR A CG2 1 
ATOM   1131 N N   . PHE A 1 168 ? 234.913 255.765 199.754 1.00 9.63   ? 168  PHE A N   1 
ATOM   1132 C CA  . PHE A 1 168 ? 234.180 256.251 200.921 1.00 9.20   ? 168  PHE A CA  1 
ATOM   1133 C C   . PHE A 1 168 ? 234.503 257.706 201.230 1.00 9.01   ? 168  PHE A C   1 
ATOM   1134 O O   . PHE A 1 168 ? 235.665 258.115 201.196 1.00 9.28   ? 168  PHE A O   1 
ATOM   1135 C CB  . PHE A 1 168 ? 234.491 255.384 202.145 1.00 8.92   ? 168  PHE A CB  1 
ATOM   1136 C CG  . PHE A 1 168 ? 233.775 255.786 203.392 1.00 9.00   ? 168  PHE A CG  1 
ATOM   1137 C CD1 . PHE A 1 168 ? 234.368 256.652 204.292 1.00 8.85   ? 168  PHE A CD1 1 
ATOM   1138 C CD2 . PHE A 1 168 ? 232.519 255.287 203.680 1.00 8.66   ? 168  PHE A CD2 1 
ATOM   1139 C CE1 . PHE A 1 168 ? 233.719 257.017 205.448 1.00 8.27   ? 168  PHE A CE1 1 
ATOM   1140 C CE2 . PHE A 1 168 ? 231.867 255.650 204.835 1.00 8.21   ? 168  PHE A CE2 1 
ATOM   1141 C CZ  . PHE A 1 168 ? 232.467 256.516 205.719 1.00 7.70   ? 168  PHE A CZ  1 
ATOM   1142 N N   . GLU A 1 169 ? 233.474 258.478 201.563 1.00 9.15   ? 169  GLU A N   1 
ATOM   1143 C CA  . GLU A 1 169 ? 233.666 259.857 201.995 1.00 9.24   ? 169  GLU A CA  1 
ATOM   1144 C C   . GLU A 1 169 ? 232.656 260.243 203.067 1.00 9.21   ? 169  GLU A C   1 
ATOM   1145 O O   . GLU A 1 169 ? 231.461 259.982 202.935 1.00 9.61   ? 169  GLU A O   1 
ATOM   1146 C CB  . GLU A 1 169 ? 233.565 260.820 200.812 1.00 8.81   ? 169  GLU A CB  1 
ATOM   1147 C CG  . GLU A 1 169 ? 233.821 262.280 201.179 1.00 9.11   ? 169  GLU A CG  1 
ATOM   1148 C CD  . GLU A 1 169 ? 233.854 263.193 199.992 1.00 8.82   ? 169  GLU A CD  1 
ATOM   1149 O OE1 . GLU A 1 169 ? 233.702 262.718 198.893 1.00 8.66   ? 169  GLU A OE1 1 
ATOM   1150 O OE2 . GLU A 1 169 ? 234.036 264.372 200.183 1.00 8.87   ? 169  GLU A OE2 1 
ATOM   1151 N N   . TYR A 1 170 ? 233.146 260.884 204.121 1.00 9.34   ? 170  TYR A N   1 
ATOM   1152 C CA  . TYR A 1 170 ? 232.311 261.319 205.231 1.00 9.68   ? 170  TYR A CA  1 
ATOM   1153 C C   . TYR A 1 170 ? 232.758 262.677 205.758 1.00 10.01  ? 170  TYR A C   1 
ATOM   1154 O O   . TYR A 1 170 ? 233.951 262.924 205.932 1.00 10.50  ? 170  TYR A O   1 
ATOM   1155 C CB  . TYR A 1 170 ? 232.360 260.262 206.334 1.00 9.02   ? 170  TYR A CB  1 
ATOM   1156 C CG  . TYR A 1 170 ? 231.695 260.636 207.627 1.00 9.22   ? 170  TYR A CG  1 
ATOM   1157 C CD1 . TYR A 1 170 ? 232.444 261.202 208.639 1.00 9.16   ? 170  TYR A CD1 1 
ATOM   1158 C CD2 . TYR A 1 170 ? 230.352 260.382 207.819 1.00 9.61   ? 170  TYR A CD2 1 
ATOM   1159 C CE1 . TYR A 1 170 ? 231.857 261.515 209.839 1.00 9.17   ? 170  TYR A CE1 1 
ATOM   1160 C CE2 . TYR A 1 170 ? 229.760 260.697 209.021 1.00 9.22   ? 170  TYR A CE2 1 
ATOM   1161 C CZ  . TYR A 1 170 ? 230.509 261.259 210.030 1.00 9.05   ? 170  TYR A CZ  1 
ATOM   1162 O OH  . TYR A 1 170 ? 229.921 261.567 211.234 1.00 8.86   ? 170  TYR A OH  1 
ATOM   1163 N N   . VAL A 1 171 ? 231.800 263.567 205.998 1.00 10.65  ? 171  VAL A N   1 
ATOM   1164 C CA  . VAL A 1 171 ? 232.106 264.887 206.542 1.00 11.22  ? 171  VAL A CA  1 
ATOM   1165 C C   . VAL A 1 171 ? 231.208 265.213 207.729 1.00 11.28  ? 171  VAL A C   1 
ATOM   1166 O O   . VAL A 1 171 ? 229.992 265.041 207.663 1.00 11.56  ? 171  VAL A O   1 
ATOM   1167 C CB  . VAL A 1 171 ? 231.957 265.974 205.456 1.00 11.75  ? 171  VAL A CB  1 
ATOM   1168 C CG1 . VAL A 1 171 ? 232.272 267.355 206.042 1.00 14.87  ? 171  VAL A CG1 1 
ATOM   1169 C CG2 . VAL A 1 171 ? 232.895 265.664 204.298 1.00 12.43  ? 171  VAL A CG2 1 
ATOM   1170 N N   . SER A 1 172 ? 231.814 265.688 208.813 1.00 11.64  ? 172  SER A N   1 
ATOM   1171 C CA  . SER A 1 172 ? 231.068 266.049 210.016 1.00 11.86  ? 172  SER A CA  1 
ATOM   1172 C C   . SER A 1 172 ? 231.779 267.127 210.825 1.00 13.12  ? 172  SER A C   1 
ATOM   1173 O O   . SER A 1 172 ? 232.649 267.834 210.312 1.00 14.67  ? 172  SER A O   1 
ATOM   1174 C CB  . SER A 1 172 ? 230.843 264.817 210.870 1.00 11.26  ? 172  SER A CB  1 
ATOM   1175 O OG  . SER A 1 172 ? 229.955 265.080 211.925 1.00 12.28  ? 172  SER A OG  1 
ATOM   1176 N N   . GLN A 1 173 ? 231.393 267.259 212.090 1.00 12.67  ? 173  GLN A N   1 
ATOM   1177 C CA  . GLN A 1 173 ? 231.990 268.248 212.979 1.00 13.11  ? 173  GLN A CA  1 
ATOM   1178 C C   . GLN A 1 173 ? 233.349 267.755 213.480 1.00 12.86  ? 173  GLN A C   1 
ATOM   1179 O O   . GLN A 1 173 ? 233.558 266.546 213.576 1.00 11.58  ? 173  GLN A O   1 
ATOM   1180 C CB  . GLN A 1 173 ? 231.053 268.530 214.156 1.00 12.54  ? 173  GLN A CB  1 
ATOM   1181 C CG  . GLN A 1 173 ? 229.755 269.200 213.760 1.00 13.28  ? 173  GLN A CG  1 
ATOM   1182 C CD  . GLN A 1 173 ? 229.990 270.553 213.131 1.00 13.81  ? 173  GLN A CD  1 
ATOM   1183 O OE1 . GLN A 1 173 ? 230.672 271.405 213.707 1.00 13.85  ? 173  GLN A OE1 1 
ATOM   1184 N NE2 . GLN A 1 173 ? 229.431 270.762 211.947 1.00 12.98  ? 173  GLN A NE2 1 
ATOM   1185 N N   . PRO A 1 174 ? 234.275 268.661 213.829 1.00 13.26  ? 174  PRO A N   1 
ATOM   1186 C CA  . PRO A 1 174 ? 235.633 268.387 214.269 1.00 12.28  ? 174  PRO A CA  1 
ATOM   1187 C C   . PRO A 1 174 ? 235.704 267.432 215.455 1.00 10.88  ? 174  PRO A C   1 
ATOM   1188 O O   . PRO A 1 174 ? 234.877 267.491 216.364 1.00 11.40  ? 174  PRO A O   1 
ATOM   1189 C CB  . PRO A 1 174 ? 236.130 269.778 214.682 1.00 12.75  ? 174  PRO A CB  1 
ATOM   1190 C CG  . PRO A 1 174 ? 235.315 270.737 213.860 1.00 15.54  ? 174  PRO A CG  1 
ATOM   1191 C CD  . PRO A 1 174 ? 233.951 270.102 213.758 1.00 14.51  ? 174  PRO A CD  1 
ATOM   1192 N N   . PHE A 1 175 ? 236.729 266.582 215.455 1.00 10.29  ? 175  PHE A N   1 
ATOM   1193 C CA  . PHE A 1 175 ? 236.992 265.664 216.566 1.00 9.25   ? 175  PHE A CA  1 
ATOM   1194 C C   . PHE A 1 175 ? 237.919 266.286 217.619 1.00 8.82   ? 175  PHE A C   1 
ATOM   1195 O O   . PHE A 1 175 ? 237.873 265.903 218.789 1.00 8.29   ? 175  PHE A O   1 
ATOM   1196 C CB  . PHE A 1 175 ? 237.657 264.377 216.063 1.00 7.57   ? 175  PHE A CB  1 
ATOM   1197 C CG  . PHE A 1 175 ? 236.825 263.507 215.156 1.00 7.92   ? 175  PHE A CG  1 
ATOM   1198 C CD1 . PHE A 1 175 ? 235.478 263.760 214.919 1.00 8.20   ? 175  PHE A CD1 1 
ATOM   1199 C CD2 . PHE A 1 175 ? 237.405 262.408 214.541 1.00 6.34   ? 175  PHE A CD2 1 
ATOM   1200 C CE1 . PHE A 1 175 ? 234.744 262.934 214.091 1.00 8.08   ? 175  PHE A CE1 1 
ATOM   1201 C CE2 . PHE A 1 175 ? 236.672 261.585 213.716 1.00 6.67   ? 175  PHE A CE2 1 
ATOM   1202 C CZ  . PHE A 1 175 ? 235.340 261.849 213.491 1.00 6.87   ? 175  PHE A CZ  1 
ATOM   1203 N N   . LEU A 1 176 ? 238.788 267.212 217.187 1.00 9.14   ? 176  LEU A N   1 
ATOM   1204 C CA  . LEU A 1 176 ? 239.823 267.821 218.022 1.00 8.68   ? 176  LEU A CA  1 
ATOM   1205 C C   . LEU A 1 176 ? 239.569 269.316 218.182 1.00 8.75   ? 176  LEU A C   1 
ATOM   1206 O O   . LEU A 1 176 ? 239.443 270.047 217.197 1.00 9.04   ? 176  LEU A O   1 
ATOM   1207 C CB  . LEU A 1 176 ? 241.218 267.588 217.393 1.00 8.74   ? 176  LEU A CB  1 
ATOM   1208 C CG  . LEU A 1 176 ? 241.675 266.080 217.213 1.00 7.88   ? 176  LEU A CG  1 
ATOM   1209 C CD1 . LEU A 1 176 ? 242.956 266.023 216.356 1.00 9.92   ? 176  LEU A CD1 1 
ATOM   1210 C CD2 . LEU A 1 176 ? 241.927 265.441 218.589 1.00 6.90   ? 176  LEU A CD2 1 
ATOM   1211 N N   . PHE A 1 186 ? 245.525 275.060 233.118 1.00 16.47  ? 186  PHE A N   1 
ATOM   1212 C CA  . PHE A 1 186 ? 245.403 273.615 232.949 1.00 16.06  ? 186  PHE A CA  1 
ATOM   1213 C C   . PHE A 1 186 ? 245.678 273.205 231.497 1.00 14.89  ? 186  PHE A C   1 
ATOM   1214 O O   . PHE A 1 186 ? 245.901 274.059 230.631 1.00 15.94  ? 186  PHE A O   1 
ATOM   1215 C CB  . PHE A 1 186 ? 243.991 273.149 233.386 1.00 16.02  ? 186  PHE A CB  1 
ATOM   1216 N N   . LYS A 1 187 ? 245.630 271.890 231.234 1.00 15.83  ? 187  LYS A N   1 
ATOM   1217 C CA  . LYS A 1 187 ? 245.817 271.330 229.895 1.00 15.23  ? 187  LYS A CA  1 
ATOM   1218 C C   . LYS A 1 187 ? 244.601 270.526 229.457 1.00 14.41  ? 187  LYS A C   1 
ATOM   1219 O O   . LYS A 1 187 ? 243.812 270.062 230.282 1.00 12.65  ? 187  LYS A O   1 
ATOM   1220 C CB  . LYS A 1 187 ? 247.075 270.463 229.844 1.00 14.07  ? 187  LYS A CB  1 
ATOM   1221 C CG  . LYS A 1 187 ? 248.370 271.229 230.044 1.00 15.51  ? 187  LYS A CG  1 
ATOM   1222 C CD  . LYS A 1 187 ? 249.587 270.323 229.873 1.00 14.38  ? 187  LYS A CD  1 
ATOM   1223 C CE  . LYS A 1 187 ? 250.880 271.116 230.015 1.00 17.00  ? 187  LYS A CE  1 
ATOM   1224 N NZ  . LYS A 1 187 ? 252.089 270.281 229.750 1.00 17.73  ? 187  LYS A NZ  1 
ATOM   1225 N N   . ASN A 1 188 ? 244.459 270.363 228.148 1.00 13.39  ? 188  ASN A N   1 
ATOM   1226 C CA  . ASN A 1 188 ? 243.364 269.594 227.576 1.00 11.76  ? 188  ASN A CA  1 
ATOM   1227 C C   . ASN A 1 188 ? 243.801 268.182 227.211 1.00 10.00  ? 188  ASN A C   1 
ATOM   1228 O O   . ASN A 1 188 ? 244.657 268.000 226.346 1.00 10.12  ? 188  ASN A O   1 
ATOM   1229 C CB  . ASN A 1 188 ? 242.816 270.302 226.354 1.00 11.70  ? 188  ASN A CB  1 
ATOM   1230 C CG  . ASN A 1 188 ? 242.166 271.614 226.688 1.00 12.11  ? 188  ASN A CG  1 
ATOM   1231 O OD1 . ASN A 1 188 ? 241.446 271.728 227.686 1.00 13.20  ? 188  ASN A OD1 1 
ATOM   1232 N ND2 . ASN A 1 188 ? 242.402 272.608 225.870 1.00 12.65  ? 188  ASN A ND2 1 
ATOM   1233 N N   . LEU A 1 189 ? 243.210 267.185 227.865 1.00 10.21  ? 189  LEU A N   1 
ATOM   1234 C CA  . LEU A 1 189 ? 243.532 265.788 227.592 1.00 9.06   ? 189  LEU A CA  1 
ATOM   1235 C C   . LEU A 1 189 ? 242.501 265.156 226.674 1.00 8.40   ? 189  LEU A C   1 
ATOM   1236 O O   . LEU A 1 189 ? 241.309 265.119 226.987 1.00 8.15   ? 189  LEU A O   1 
ATOM   1237 C CB  . LEU A 1 189 ? 243.615 264.987 228.898 1.00 9.56   ? 189  LEU A CB  1 
ATOM   1238 C CG  . LEU A 1 189 ? 243.759 263.447 228.754 1.00 8.34   ? 189  LEU A CG  1 
ATOM   1239 C CD1 . LEU A 1 189 ? 245.088 263.093 228.106 1.00 7.82   ? 189  LEU A CD1 1 
ATOM   1240 C CD2 . LEU A 1 189 ? 243.655 262.813 230.122 1.00 8.05   ? 189  LEU A CD2 1 
ATOM   1241 N N   . ARG A 1 190 ? 242.959 264.653 225.537 1.00 7.78   ? 190  ARG A N   1 
ATOM   1242 C CA  . ARG A 1 190 ? 242.066 264.022 224.578 1.00 7.11   ? 190  ARG A CA  1 
ATOM   1243 C C   . ARG A 1 190 ? 242.448 262.568 224.384 1.00 6.34   ? 190  ARG A C   1 
ATOM   1244 O O   . ARG A 1 190 ? 243.614 262.252 224.144 1.00 5.80   ? 190  ARG A O   1 
ATOM   1245 C CB  . ARG A 1 190 ? 242.110 264.741 223.243 1.00 7.62   ? 190  ARG A CB  1 
ATOM   1246 C CG  . ARG A 1 190 ? 241.677 266.188 223.293 1.00 8.54   ? 190  ARG A CG  1 
ATOM   1247 C CD  . ARG A 1 190 ? 241.696 266.810 221.955 1.00 8.05   ? 190  ARG A CD  1 
ATOM   1248 N NE  . ARG A 1 190 ? 241.353 268.217 222.011 1.00 8.53   ? 190  ARG A NE  1 
ATOM   1249 C CZ  . ARG A 1 190 ? 242.235 269.207 222.254 1.00 10.01  ? 190  ARG A CZ  1 
ATOM   1250 N NH1 . ARG A 1 190 ? 241.827 270.456 222.285 1.00 10.06  ? 190  ARG A NH1 1 
ATOM   1251 N NH2 . ARG A 1 190 ? 243.513 268.917 222.463 1.00 11.16  ? 190  ARG A NH2 1 
ATOM   1252 N N   . GLU A 1 191 ? 241.469 261.682 224.504 1.00 5.25   ? 191  GLU A N   1 
ATOM   1253 C CA  . GLU A 1 191 ? 241.716 260.252 224.382 1.00 3.93   ? 191  GLU A CA  1 
ATOM   1254 C C   . GLU A 1 191 ? 240.857 259.624 223.298 1.00 3.56   ? 191  GLU A C   1 
ATOM   1255 O O   . GLU A 1 191 ? 239.668 259.918 223.190 1.00 3.62   ? 191  GLU A O   1 
ATOM   1256 C CB  . GLU A 1 191 ? 241.454 259.568 225.721 1.00 4.27   ? 191  GLU A CB  1 
ATOM   1257 C CG  . GLU A 1 191 ? 242.396 259.999 226.829 1.00 4.70   ? 191  GLU A CG  1 
ATOM   1258 C CD  . GLU A 1 191 ? 241.991 259.491 228.168 1.00 4.66   ? 191  GLU A CD  1 
ATOM   1259 O OE1 . GLU A 1 191 ? 242.534 258.508 228.608 1.00 4.49   ? 191  GLU A OE1 1 
ATOM   1260 O OE2 . GLU A 1 191 ? 241.139 260.097 228.768 1.00 5.06   ? 191  GLU A OE2 1 
ATOM   1261 N N   . PHE A 1 192 ? 241.470 258.748 222.508 1.00 3.27   ? 192  PHE A N   1 
ATOM   1262 C CA  . PHE A 1 192 ? 240.791 258.040 221.431 1.00 2.82   ? 192  PHE A CA  1 
ATOM   1263 C C   . PHE A 1 192 ? 241.097 256.550 221.440 1.00 2.43   ? 192  PHE A C   1 
ATOM   1264 O O   . PHE A 1 192 ? 242.206 256.132 221.772 1.00 2.59   ? 192  PHE A O   1 
ATOM   1265 C CB  . PHE A 1 192 ? 241.206 258.604 220.070 1.00 2.93   ? 192  PHE A CB  1 
ATOM   1266 C CG  . PHE A 1 192 ? 240.795 260.013 219.836 1.00 3.12   ? 192  PHE A CG  1 
ATOM   1267 C CD1 . PHE A 1 192 ? 239.606 260.294 219.195 1.00 3.18   ? 192  PHE A CD1 1 
ATOM   1268 C CD2 . PHE A 1 192 ? 241.587 261.060 220.255 1.00 3.65   ? 192  PHE A CD2 1 
ATOM   1269 C CE1 . PHE A 1 192 ? 239.213 261.591 218.977 1.00 3.80   ? 192  PHE A CE1 1 
ATOM   1270 C CE2 . PHE A 1 192 ? 241.198 262.357 220.042 1.00 4.19   ? 192  PHE A CE2 1 
ATOM   1271 C CZ  . PHE A 1 192 ? 240.005 262.623 219.401 1.00 4.17   ? 192  PHE A CZ  1 
ATOM   1272 N N   . VAL A 1 193 ? 240.132 255.757 221.003 1.00 2.43   ? 193  VAL A N   1 
ATOM   1273 C CA  . VAL A 1 193 ? 240.356 254.336 220.763 1.00 2.15   ? 193  VAL A CA  1 
ATOM   1274 C C   . VAL A 1 193 ? 239.966 253.967 219.345 1.00 2.26   ? 193  VAL A C   1 
ATOM   1275 O O   . VAL A 1 193 ? 238.862 254.274 218.894 1.00 2.61   ? 193  VAL A O   1 
ATOM   1276 C CB  . VAL A 1 193 ? 239.579 253.474 221.774 1.00 2.28   ? 193  VAL A CB  1 
ATOM   1277 C CG1 . VAL A 1 193 ? 239.714 252.009 221.434 1.00 2.41   ? 193  VAL A CG1 1 
ATOM   1278 C CG2 . VAL A 1 193 ? 240.125 253.721 223.156 1.00 2.27   ? 193  VAL A CG2 1 
ATOM   1279 N N   . PHE A 1 194 ? 240.885 253.321 218.636 1.00 2.29   ? 194  PHE A N   1 
ATOM   1280 C CA  . PHE A 1 194 ? 240.662 252.938 217.250 1.00 2.40   ? 194  PHE A CA  1 
ATOM   1281 C C   . PHE A 1 194 ? 240.590 251.426 217.086 1.00 2.54   ? 194  PHE A C   1 
ATOM   1282 O O   . PHE A 1 194 ? 241.564 250.715 217.341 1.00 2.61   ? 194  PHE A O   1 
ATOM   1283 C CB  . PHE A 1 194 ? 241.787 253.480 216.369 1.00 2.43   ? 194  PHE A CB  1 
ATOM   1284 C CG  . PHE A 1 194 ? 241.915 254.973 216.396 1.00 2.23   ? 194  PHE A CG  1 
ATOM   1285 C CD1 . PHE A 1 194 ? 241.058 255.767 215.666 1.00 2.57   ? 194  PHE A CD1 1 
ATOM   1286 C CD2 . PHE A 1 194 ? 242.903 255.582 217.147 1.00 1.93   ? 194  PHE A CD2 1 
ATOM   1287 C CE1 . PHE A 1 194 ? 241.175 257.138 215.687 1.00 2.61   ? 194  PHE A CE1 1 
ATOM   1288 C CE2 . PHE A 1 194 ? 243.025 256.953 217.169 1.00 2.39   ? 194  PHE A CE2 1 
ATOM   1289 C CZ  . PHE A 1 194 ? 242.157 257.730 216.440 1.00 2.62   ? 194  PHE A CZ  1 
ATOM   1290 N N   . LYS A 1 195 ? 239.439 250.936 216.638 1.00 2.96   ? 195  LYS A N   1 
ATOM   1291 C CA  . LYS A 1 195 ? 239.239 249.508 216.408 1.00 3.18   ? 195  LYS A CA  1 
ATOM   1292 C C   . LYS A 1 195 ? 238.811 249.241 214.973 1.00 3.78   ? 195  LYS A C   1 
ATOM   1293 O O   . LYS A 1 195 ? 238.201 250.095 214.334 1.00 3.74   ? 195  LYS A O   1 
ATOM   1294 C CB  . LYS A 1 195 ? 238.188 248.948 217.363 1.00 3.39   ? 195  LYS A CB  1 
ATOM   1295 C CG  . LYS A 1 195 ? 238.622 248.858 218.813 1.00 3.13   ? 195  LYS A CG  1 
ATOM   1296 C CD  . LYS A 1 195 ? 237.420 248.727 219.732 1.00 3.30   ? 195  LYS A CD  1 
ATOM   1297 C CE  . LYS A 1 195 ? 236.662 247.430 219.494 1.00 3.37   ? 195  LYS A CE  1 
ATOM   1298 N NZ  . LYS A 1 195 ? 235.509 247.287 220.418 1.00 3.78   ? 195  LYS A NZ  1 
ATOM   1299 N N   . ASN A 1 196 ? 239.105 248.047 214.473 1.00 3.79   ? 196  ASN A N   1 
ATOM   1300 C CA  . ASN A 1 196 ? 238.696 247.668 213.124 1.00 4.08   ? 196  ASN A CA  1 
ATOM   1301 C C   . ASN A 1 196 ? 238.166 246.240 213.106 1.00 4.47   ? 196  ASN A C   1 
ATOM   1302 O O   . ASN A 1 196 ? 238.936 245.284 213.016 1.00 4.93   ? 196  ASN A O   1 
ATOM   1303 C CB  . ASN A 1 196 ? 239.855 247.828 212.157 1.00 4.33   ? 196  ASN A CB  1 
ATOM   1304 C CG  . ASN A 1 196 ? 239.465 247.616 210.716 1.00 4.61   ? 196  ASN A CG  1 
ATOM   1305 O OD1 . ASN A 1 196 ? 238.280 247.564 210.369 1.00 5.51   ? 196  ASN A OD1 1 
ATOM   1306 N ND2 . ASN A 1 196 ? 240.454 247.493 209.869 1.00 5.14   ? 196  ASN A ND2 1 
ATOM   1307 N N   . ILE A 1 197 ? 236.852 246.098 213.253 1.00 4.37   ? 197  ILE A N   1 
ATOM   1308 C CA  . ILE A 1 197 ? 236.246 244.778 213.378 1.00 4.43   ? 197  ILE A CA  1 
ATOM   1309 C C   . ILE A 1 197 ? 235.196 244.522 212.310 1.00 4.29   ? 197  ILE A C   1 
ATOM   1310 O O   . ILE A 1 197 ? 234.224 245.264 212.182 1.00 4.57   ? 197  ILE A O   1 
ATOM   1311 C CB  . ILE A 1 197 ? 235.623 244.591 214.772 1.00 3.99   ? 197  ILE A CB  1 
ATOM   1312 C CG1 . ILE A 1 197 ? 236.719 244.710 215.839 1.00 4.22   ? 197  ILE A CG1 1 
ATOM   1313 C CG2 . ILE A 1 197 ? 234.911 243.243 214.856 1.00 5.33   ? 197  ILE A CG2 1 
ATOM   1314 C CD1 . ILE A 1 197 ? 236.204 244.718 217.255 1.00 4.15   ? 197  ILE A CD1 1 
ATOM   1315 N N   . ASP A 1 198 ? 235.385 243.441 211.563 1.00 4.63   ? 198  ASP A N   1 
ATOM   1316 C CA  . ASP A 1 198 ? 234.457 243.032 210.517 1.00 4.62   ? 198  ASP A CA  1 
ATOM   1317 C C   . ASP A 1 198 ? 234.208 244.145 209.507 1.00 4.97   ? 198  ASP A C   1 
ATOM   1318 O O   . ASP A 1 198 ? 233.101 244.295 208.991 1.00 4.96   ? 198  ASP A O   1 
ATOM   1319 C CB  . ASP A 1 198 ? 233.130 242.577 211.129 1.00 4.36   ? 198  ASP A CB  1 
ATOM   1320 C CG  . ASP A 1 198 ? 233.290 241.360 212.034 1.00 4.96   ? 198  ASP A CG  1 
ATOM   1321 O OD1 . ASP A 1 198 ? 234.169 240.567 211.781 1.00 5.17   ? 198  ASP A OD1 1 
ATOM   1322 O OD2 . ASP A 1 198 ? 232.536 241.236 212.969 1.00 4.80   ? 198  ASP A OD2 1 
ATOM   1323 N N   . GLY A 1 199 ? 235.250 244.911 209.208 1.00 5.10   ? 199  GLY A N   1 
ATOM   1324 C CA  . GLY A 1 199 ? 235.166 245.962 208.205 1.00 5.60   ? 199  GLY A CA  1 
ATOM   1325 C C   . GLY A 1 199 ? 234.734 247.310 208.775 1.00 5.11   ? 199  GLY A C   1 
ATOM   1326 O O   . GLY A 1 199 ? 234.766 248.323 208.071 1.00 5.52   ? 199  GLY A O   1 
ATOM   1327 N N   . TYR A 1 200 ? 234.332 247.339 210.038 1.00 5.16   ? 200  TYR A N   1 
ATOM   1328 C CA  . TYR A 1 200 ? 233.879 248.585 210.640 1.00 5.22   ? 200  TYR A CA  1 
ATOM   1329 C C   . TYR A 1 200 ? 234.982 249.253 211.441 1.00 4.64   ? 200  TYR A C   1 
ATOM   1330 O O   . TYR A 1 200 ? 235.532 248.662 212.373 1.00 4.81   ? 200  TYR A O   1 
ATOM   1331 C CB  . TYR A 1 200 ? 232.663 248.335 211.526 1.00 5.33   ? 200  TYR A CB  1 
ATOM   1332 C CG  . TYR A 1 200 ? 231.425 247.970 210.758 1.00 5.04   ? 200  TYR A CG  1 
ATOM   1333 C CD1 . TYR A 1 200 ? 231.197 246.654 210.402 1.00 4.97   ? 200  TYR A CD1 1 
ATOM   1334 C CD2 . TYR A 1 200 ? 230.512 248.951 210.410 1.00 5.10   ? 200  TYR A CD2 1 
ATOM   1335 C CE1 . TYR A 1 200 ? 230.061 246.319 209.698 1.00 5.33   ? 200  TYR A CE1 1 
ATOM   1336 C CE2 . TYR A 1 200 ? 229.375 248.616 209.709 1.00 5.18   ? 200  TYR A CE2 1 
ATOM   1337 C CZ  . TYR A 1 200 ? 229.148 247.306 209.351 1.00 5.43   ? 200  TYR A CZ  1 
ATOM   1338 O OH  . TYR A 1 200 ? 228.015 246.970 208.649 1.00 5.09   ? 200  TYR A OH  1 
ATOM   1339 N N   . PHE A 1 201 ? 235.288 250.495 211.087 1.00 5.00   ? 201  PHE A N   1 
ATOM   1340 C CA  . PHE A 1 201 ? 236.292 251.257 211.809 1.00 4.72   ? 201  PHE A CA  1 
ATOM   1341 C C   . PHE A 1 201 ? 235.601 252.086 212.876 1.00 4.42   ? 201  PHE A C   1 
ATOM   1342 O O   . PHE A 1 201 ? 234.839 253.006 212.572 1.00 4.21   ? 201  PHE A O   1 
ATOM   1343 C CB  . PHE A 1 201 ? 237.092 252.151 210.865 1.00 4.91   ? 201  PHE A CB  1 
ATOM   1344 C CG  . PHE A 1 201 ? 238.316 252.745 211.493 1.00 4.42   ? 201  PHE A CG  1 
ATOM   1345 C CD1 . PHE A 1 201 ? 239.449 251.976 211.670 1.00 4.17   ? 201  PHE A CD1 1 
ATOM   1346 C CD2 . PHE A 1 201 ? 238.343 254.062 211.905 1.00 4.08   ? 201  PHE A CD2 1 
ATOM   1347 C CE1 . PHE A 1 201 ? 240.580 252.506 212.242 1.00 3.66   ? 201  PHE A CE1 1 
ATOM   1348 C CE2 . PHE A 1 201 ? 239.477 254.593 212.475 1.00 3.72   ? 201  PHE A CE2 1 
ATOM   1349 C CZ  . PHE A 1 201 ? 240.593 253.813 212.642 1.00 3.63   ? 201  PHE A CZ  1 
ATOM   1350 N N   . LYS A 1 202 ? 235.811 251.706 214.125 1.00 4.13   ? 202  LYS A N   1 
ATOM   1351 C CA  . LYS A 1 202 ? 235.082 252.296 215.234 1.00 3.85   ? 202  LYS A CA  1 
ATOM   1352 C C   . LYS A 1 202 ? 235.957 253.246 216.027 1.00 3.47   ? 202  LYS A C   1 
ATOM   1353 O O   . LYS A 1 202 ? 237.075 252.900 216.417 1.00 3.31   ? 202  LYS A O   1 
ATOM   1354 C CB  . LYS A 1 202 ? 234.550 251.194 216.149 1.00 3.72   ? 202  LYS A CB  1 
ATOM   1355 C CG  . LYS A 1 202 ? 233.536 250.265 215.494 1.00 4.15   ? 202  LYS A CG  1 
ATOM   1356 C CD  . LYS A 1 202 ? 233.137 249.139 216.434 1.00 4.01   ? 202  LYS A CD  1 
ATOM   1357 C CE  . LYS A 1 202 ? 232.268 248.095 215.733 1.00 4.37   ? 202  LYS A CE  1 
ATOM   1358 N NZ  . LYS A 1 202 ? 230.855 248.547 215.569 1.00 4.38   ? 202  LYS A NZ  1 
ATOM   1359 N N   . ILE A 1 203 ? 235.444 254.440 216.284 1.00 3.31   ? 203  ILE A N   1 
ATOM   1360 C CA  . ILE A 1 203 ? 236.180 255.416 217.068 1.00 2.94   ? 203  ILE A CA  1 
ATOM   1361 C C   . ILE A 1 203 ? 235.425 255.788 218.334 1.00 3.09   ? 203  ILE A C   1 
ATOM   1362 O O   . ILE A 1 203 ? 234.248 256.151 218.285 1.00 2.73   ? 203  ILE A O   1 
ATOM   1363 C CB  . ILE A 1 203 ? 236.470 256.693 216.258 1.00 2.97   ? 203  ILE A CB  1 
ATOM   1364 C CG1 . ILE A 1 203 ? 237.248 256.343 214.983 1.00 3.25   ? 203  ILE A CG1 1 
ATOM   1365 C CG2 . ILE A 1 203 ? 237.266 257.677 217.116 1.00 2.98   ? 203  ILE A CG2 1 
ATOM   1366 C CD1 . ILE A 1 203 ? 237.408 257.501 214.010 1.00 3.91   ? 203  ILE A CD1 1 
ATOM   1367 N N   . TYR A 1 204 ? 236.128 255.726 219.459 1.00 2.95   ? 204  TYR A N   1 
ATOM   1368 C CA  . TYR A 1 204 ? 235.609 256.168 220.750 1.00 2.77   ? 204  TYR A CA  1 
ATOM   1369 C C   . TYR A 1 204 ? 236.443 257.348 221.214 1.00 2.90   ? 204  TYR A C   1 
ATOM   1370 O O   . TYR A 1 204 ? 237.618 257.443 220.855 1.00 2.98   ? 204  TYR A O   1 
ATOM   1371 C CB  . TYR A 1 204 ? 235.689 255.049 221.787 1.00 2.94   ? 204  TYR A CB  1 
ATOM   1372 C CG  . TYR A 1 204 ? 234.924 253.805 221.436 1.00 2.98   ? 204  TYR A CG  1 
ATOM   1373 C CD1 . TYR A 1 204 ? 235.457 252.890 220.546 1.00 2.96   ? 204  TYR A CD1 1 
ATOM   1374 C CD2 . TYR A 1 204 ? 233.700 253.565 222.021 1.00 3.22   ? 204  TYR A CD2 1 
ATOM   1375 C CE1 . TYR A 1 204 ? 234.760 251.748 220.237 1.00 3.19   ? 204  TYR A CE1 1 
ATOM   1376 C CE2 . TYR A 1 204 ? 233.007 252.420 221.714 1.00 3.34   ? 204  TYR A CE2 1 
ATOM   1377 C CZ  . TYR A 1 204 ? 233.531 251.515 220.826 1.00 3.36   ? 204  TYR A CZ  1 
ATOM   1378 O OH  . TYR A 1 204 ? 232.833 250.370 220.525 1.00 3.78   ? 204  TYR A OH  1 
ATOM   1379 N N   . SER A 1 205 ? 235.866 258.244 222.009 1.00 3.06   ? 205  SER A N   1 
ATOM   1380 C CA  . SER A 1 205 ? 236.641 259.384 222.482 1.00 3.23   ? 205  SER A CA  1 
ATOM   1381 C C   . SER A 1 205 ? 236.150 259.976 223.797 1.00 3.55   ? 205  SER A C   1 
ATOM   1382 O O   . SER A 1 205 ? 235.000 259.783 224.200 1.00 3.84   ? 205  SER A O   1 
ATOM   1383 C CB  . SER A 1 205 ? 236.647 260.470 221.428 1.00 3.42   ? 205  SER A CB  1 
ATOM   1384 O OG  . SER A 1 205 ? 235.370 261.015 221.267 1.00 3.35   ? 205  SER A OG  1 
ATOM   1385 N N   . LYS A 1 206 ? 237.038 260.723 224.449 1.00 3.96   ? 206  LYS A N   1 
ATOM   1386 C CA  . LYS A 1 206 ? 236.710 261.486 225.648 1.00 4.62   ? 206  LYS A CA  1 
ATOM   1387 C C   . LYS A 1 206 ? 237.587 262.732 225.747 1.00 6.17   ? 206  LYS A C   1 
ATOM   1388 O O   . LYS A 1 206 ? 238.764 262.703 225.387 1.00 6.15   ? 206  LYS A O   1 
ATOM   1389 C CB  . LYS A 1 206 ? 236.869 260.623 226.902 1.00 4.55   ? 206  LYS A CB  1 
ATOM   1390 C CG  . LYS A 1 206 ? 236.329 261.244 228.187 1.00 4.72   ? 206  LYS A CG  1 
ATOM   1391 C CD  . LYS A 1 206 ? 234.807 261.172 228.245 1.00 4.18   ? 206  LYS A CD  1 
ATOM   1392 C CE  . LYS A 1 206 ? 234.268 261.769 229.533 1.00 3.98   ? 206  LYS A CE  1 
ATOM   1393 N NZ  . LYS A 1 206 ? 232.776 261.759 229.566 1.00 2.03   ? 206  LYS A NZ  1 
ATOM   1394 N N   . HIS A 1 207 ? 237.015 263.828 226.236 1.00 6.85   ? 207  HIS A N   1 
ATOM   1395 C CA  . HIS A 1 207 ? 237.764 265.065 226.427 1.00 7.91   ? 207  HIS A CA  1 
ATOM   1396 C C   . HIS A 1 207 ? 237.591 265.601 227.846 1.00 8.70   ? 207  HIS A C   1 
ATOM   1397 O O   . HIS A 1 207 ? 236.485 265.962 228.249 1.00 9.26   ? 207  HIS A O   1 
ATOM   1398 C CB  . HIS A 1 207 ? 237.312 266.117 225.409 1.00 7.83   ? 207  HIS A CB  1 
ATOM   1399 C CG  . HIS A 1 207 ? 238.057 267.417 225.480 1.00 8.77   ? 207  HIS A CG  1 
ATOM   1400 N ND1 . HIS A 1 207 ? 237.604 268.562 224.856 1.00 9.51   ? 207  HIS A ND1 1 
ATOM   1401 C CD2 . HIS A 1 207 ? 239.215 267.761 226.095 1.00 9.24   ? 207  HIS A CD2 1 
ATOM   1402 C CE1 . HIS A 1 207 ? 238.447 269.549 225.090 1.00 10.06  ? 207  HIS A CE1 1 
ATOM   1403 N NE2 . HIS A 1 207 ? 239.428 269.090 225.838 1.00 9.91   ? 207  HIS A NE2 1 
ATOM   1404 N N   . THR A 1 208 ? 238.684 265.623 228.606 1.00 9.05   ? 208  THR A N   1 
ATOM   1405 C CA  . THR A 1 208 ? 238.662 266.092 229.989 1.00 10.02  ? 208  THR A CA  1 
ATOM   1406 C C   . THR A 1 208 ? 239.833 267.040 230.239 1.00 9.82   ? 208  THR A C   1 
ATOM   1407 O O   . THR A 1 208 ? 240.824 266.990 229.513 1.00 10.90  ? 208  THR A O   1 
ATOM   1408 C CB  . THR A 1 208 ? 238.741 264.902 230.970 1.00 9.06   ? 208  THR A CB  1 
ATOM   1409 O OG1 . THR A 1 208 ? 239.995 264.231 230.811 1.00 9.32   ? 208  THR A OG1 1 
ATOM   1410 C CG2 . THR A 1 208 ? 237.622 263.920 230.703 1.00 8.65   ? 208  THR A CG2 1 
ATOM   1411 N N   . PRO A 1 209 ? 239.733 267.923 231.237 1.00 11.41  ? 209  PRO A N   1 
ATOM   1412 C CA  . PRO A 1 209 ? 240.806 268.752 231.763 1.00 12.02  ? 209  PRO A CA  1 
ATOM   1413 C C   . PRO A 1 209 ? 241.792 267.923 232.579 1.00 12.44  ? 209  PRO A C   1 
ATOM   1414 O O   . PRO A 1 209 ? 241.403 266.957 233.235 1.00 12.64  ? 209  PRO A O   1 
ATOM   1415 C CB  . PRO A 1 209 ? 240.045 269.760 232.632 1.00 12.75  ? 209  PRO A CB  1 
ATOM   1416 C CG  . PRO A 1 209 ? 238.776 269.035 233.043 1.00 11.20  ? 209  PRO A CG  1 
ATOM   1417 C CD  . PRO A 1 209 ? 238.424 268.152 231.859 1.00 11.55  ? 209  PRO A CD  1 
ATOM   1418 N N   . ILE A 1 210 ? 243.058 268.327 232.559 1.00 12.84  ? 210  ILE A N   1 
ATOM   1419 C CA  . ILE A 1 210 ? 244.091 267.684 233.363 1.00 14.74  ? 210  ILE A CA  1 
ATOM   1420 C C   . ILE A 1 210 ? 245.004 268.720 234.022 1.00 14.45  ? 210  ILE A C   1 
ATOM   1421 O O   . ILE A 1 210 ? 245.315 269.757 233.430 1.00 14.71  ? 210  ILE A O   1 
ATOM   1422 C CB  . ILE A 1 210 ? 244.904 266.694 232.501 1.00 13.52  ? 210  ILE A CB  1 
ATOM   1423 C CG1 . ILE A 1 210 ? 245.886 265.914 233.373 1.00 13.82  ? 210  ILE A CG1 1 
ATOM   1424 C CG2 . ILE A 1 210 ? 245.633 267.427 231.394 1.00 13.19  ? 210  ILE A CG2 1 
ATOM   1425 C CD1 . ILE A 1 210 ? 246.464 264.706 232.698 1.00 11.94  ? 210  ILE A CD1 1 
ATOM   1426 N N   . ASN A 1 211 ? 245.433 268.441 235.252 1.00 14.69  ? 211  ASN A N   1 
ATOM   1427 C CA  . ASN A 1 211 ? 246.287 269.362 236.001 1.00 15.35  ? 211  ASN A CA  1 
ATOM   1428 C C   . ASN A 1 211 ? 247.701 268.828 236.231 1.00 15.42  ? 211  ASN A C   1 
ATOM   1429 O O   . ASN A 1 211 ? 248.374 269.229 237.180 1.00 15.52  ? 211  ASN A O   1 
ATOM   1430 C CB  . ASN A 1 211 ? 245.642 269.708 237.326 1.00 15.08  ? 211  ASN A CB  1 
ATOM   1431 C CG  . ASN A 1 211 ? 245.459 268.502 238.199 1.00 17.11  ? 211  ASN A CG  1 
ATOM   1432 O OD1 . ASN A 1 211 ? 245.410 267.367 237.703 1.00 16.38  ? 211  ASN A OD1 1 
ATOM   1433 N ND2 . ASN A 1 211 ? 245.355 268.719 239.486 1.00 16.66  ? 211  ASN A ND2 1 
ATOM   1434 N N   . LEU A 1 212 ? 248.149 267.929 235.365 1.00 14.88  ? 212  LEU A N   1 
ATOM   1435 C CA  . LEU A 1 212 ? 249.499 267.385 235.460 1.00 15.10  ? 212  LEU A CA  1 
ATOM   1436 C C   . LEU A 1 212 ? 250.398 268.009 234.410 1.00 15.28  ? 212  LEU A C   1 
ATOM   1437 O O   . LEU A 1 212 ? 249.926 268.482 233.377 1.00 15.35  ? 212  LEU A O   1 
ATOM   1438 C CB  . LEU A 1 212 ? 249.495 265.862 235.291 1.00 14.45  ? 212  LEU A CB  1 
ATOM   1439 C CG  . LEU A 1 212 ? 248.612 265.071 236.264 1.00 14.56  ? 212  LEU A CG  1 
ATOM   1440 C CD1 . LEU A 1 212 ? 248.772 263.589 235.975 1.00 11.53  ? 212  LEU A CD1 1 
ATOM   1441 C CD2 . LEU A 1 212 ? 249.002 265.390 237.702 1.00 16.09  ? 212  LEU A CD2 1 
ATOM   1442 N N   . VAL A 1 213 ? 251.697 268.013 234.675 1.00 15.13  ? 213  VAL A N   1 
ATOM   1443 C CA  . VAL A 1 213 ? 252.643 268.618 233.749 1.00 14.87  ? 213  VAL A CA  1 
ATOM   1444 C C   . VAL A 1 213 ? 252.976 267.704 232.575 1.00 13.84  ? 213  VAL A C   1 
ATOM   1445 O O   . VAL A 1 213 ? 252.888 268.117 231.417 1.00 15.04  ? 213  VAL A O   1 
ATOM   1446 C CB  . VAL A 1 213 ? 253.938 268.995 234.497 1.00 15.33  ? 213  VAL A CB  1 
ATOM   1447 N N   . ARG A 1 214 ? 253.385 266.472 232.868 1.00 14.82  ? 214  ARG A N   1 
ATOM   1448 C CA  . ARG A 1 214 ? 253.819 265.565 231.812 1.00 13.13  ? 214  ARG A CA  1 
ATOM   1449 C C   . ARG A 1 214 ? 253.576 264.096 232.146 1.00 11.75  ? 214  ARG A C   1 
ATOM   1450 O O   . ARG A 1 214 ? 254.508 263.294 232.142 1.00 11.47  ? 214  ARG A O   1 
ATOM   1451 C CB  . ARG A 1 214 ? 255.295 265.793 231.510 1.00 13.56  ? 214  ARG A CB  1 
ATOM   1452 N N   . ASP A 1 215 ? 252.329 263.745 232.440 1.00 10.92  ? 215  ASP A N   1 
ATOM   1453 C CA  . ASP A 1 215 ? 252.004 262.366 232.796 1.00 10.73  ? 215  ASP A CA  1 
ATOM   1454 C C   . ASP A 1 215 ? 250.537 262.051 232.510 1.00 9.98   ? 215  ASP A C   1 
ATOM   1455 O O   . ASP A 1 215 ? 249.772 262.930 232.113 1.00 9.71   ? 215  ASP A O   1 
ATOM   1456 C CB  . ASP A 1 215 ? 252.313 262.137 234.284 1.00 10.33  ? 215  ASP A CB  1 
ATOM   1457 C CG  . ASP A 1 215 ? 252.706 260.705 234.631 1.00 9.99   ? 215  ASP A CG  1 
ATOM   1458 O OD1 . ASP A 1 215 ? 252.349 259.815 233.900 1.00 9.64   ? 215  ASP A OD1 1 
ATOM   1459 O OD2 . ASP A 1 215 ? 253.367 260.518 235.625 1.00 9.56   ? 215  ASP A OD2 1 
ATOM   1460 N N   . LEU A 1 216 ? 250.141 260.806 232.752 1.00 9.15   ? 216  LEU A N   1 
ATOM   1461 C CA  . LEU A 1 216 ? 248.742 260.409 232.638 1.00 8.81   ? 216  LEU A CA  1 
ATOM   1462 C C   . LEU A 1 216 ? 248.090 260.469 234.015 1.00 8.49   ? 216  LEU A C   1 
ATOM   1463 O O   . LEU A 1 216 ? 248.727 260.134 235.012 1.00 8.13   ? 216  LEU A O   1 
ATOM   1464 C CB  . LEU A 1 216 ? 248.620 258.991 232.050 1.00 7.85   ? 216  LEU A CB  1 
ATOM   1465 C CG  . LEU A 1 216 ? 249.078 258.805 230.584 1.00 7.53   ? 216  LEU A CG  1 
ATOM   1466 C CD1 . LEU A 1 216 ? 249.003 257.327 230.221 1.00 5.73   ? 216  LEU A CD1 1 
ATOM   1467 C CD2 . LEU A 1 216 ? 248.186 259.623 229.655 1.00 7.54   ? 216  LEU A CD2 1 
ATOM   1468 N N   . PRO A 1 217 ? 246.829 260.892 234.094 1.00 8.38   ? 217  PRO A N   1 
ATOM   1469 C CA  . PRO A 1 217 ? 246.063 261.061 235.309 1.00 7.53   ? 217  PRO A CA  1 
ATOM   1470 C C   . PRO A 1 217 ? 245.707 259.718 235.919 1.00 6.84   ? 217  PRO A C   1 
ATOM   1471 O O   . PRO A 1 217 ? 245.449 258.752 235.202 1.00 6.33   ? 217  PRO A O   1 
ATOM   1472 C CB  . PRO A 1 217 ? 244.832 261.826 234.816 1.00 7.69   ? 217  PRO A CB  1 
ATOM   1473 C CG  . PRO A 1 217 ? 244.686 261.426 233.365 1.00 8.37   ? 217  PRO A CG  1 
ATOM   1474 C CD  . PRO A 1 217 ? 246.098 261.174 232.863 1.00 8.29   ? 217  PRO A CD  1 
ATOM   1475 N N   . GLN A 1 218 ? 245.654 259.669 237.244 1.00 6.57   ? 218  GLN A N   1 
ATOM   1476 C CA  . GLN A 1 218 ? 245.260 258.454 237.938 1.00 5.35   ? 218  GLN A CA  1 
ATOM   1477 C C   . GLN A 1 218 ? 243.822 258.561 238.414 1.00 5.65   ? 218  GLN A C   1 
ATOM   1478 O O   . GLN A 1 218 ? 243.524 259.252 239.388 1.00 5.85   ? 218  GLN A O   1 
ATOM   1479 C CB  . GLN A 1 218 ? 246.199 258.176 239.114 1.00 4.36   ? 218  GLN A CB  1 
ATOM   1480 C CG  . GLN A 1 218 ? 245.929 256.869 239.830 1.00 3.97   ? 218  GLN A CG  1 
ATOM   1481 C CD  . GLN A 1 218 ? 247.008 256.536 240.836 1.00 4.74   ? 218  GLN A CD  1 
ATOM   1482 O OE1 . GLN A 1 218 ? 247.941 257.315 241.046 1.00 4.33   ? 218  GLN A OE1 1 
ATOM   1483 N NE2 . GLN A 1 218 ? 246.891 255.373 241.468 1.00 5.12   ? 218  GLN A NE2 1 
ATOM   1484 N N   . GLY A 1 219 ? 242.931 257.890 237.699 1.00 5.95   ? 219  GLY A N   1 
ATOM   1485 C CA  . GLY A 1 219 ? 241.500 257.957 237.958 1.00 5.41   ? 219  GLY A CA  1 
ATOM   1486 C C   . GLY A 1 219 ? 240.762 257.144 236.909 1.00 5.03   ? 219  GLY A C   1 
ATOM   1487 O O   . GLY A 1 219 ? 241.383 256.414 236.139 1.00 5.21   ? 219  GLY A O   1 
ATOM   1488 N N   . PHE A 1 220 ? 239.440 257.256 236.879 1.00 5.41   ? 220  PHE A N   1 
ATOM   1489 C CA  . PHE A 1 220 ? 238.664 256.466 235.933 1.00 5.52   ? 220  PHE A CA  1 
ATOM   1490 C C   . PHE A 1 220 ? 237.664 257.307 235.153 1.00 5.67   ? 220  PHE A C   1 
ATOM   1491 O O   . PHE A 1 220 ? 236.926 258.109 235.726 1.00 5.72   ? 220  PHE A O   1 
ATOM   1492 C CB  . PHE A 1 220 ? 237.916 255.348 236.652 1.00 6.20   ? 220  PHE A CB  1 
ATOM   1493 C CG  . PHE A 1 220 ? 237.209 254.449 235.709 1.00 6.61   ? 220  PHE A CG  1 
ATOM   1494 C CD1 . PHE A 1 220 ? 235.939 254.750 235.276 1.00 7.15   ? 220  PHE A CD1 1 
ATOM   1495 C CD2 . PHE A 1 220 ? 237.815 253.301 235.241 1.00 6.85   ? 220  PHE A CD2 1 
ATOM   1496 C CE1 . PHE A 1 220 ? 235.289 253.934 234.391 1.00 7.32   ? 220  PHE A CE1 1 
ATOM   1497 C CE2 . PHE A 1 220 ? 237.163 252.479 234.359 1.00 7.40   ? 220  PHE A CE2 1 
ATOM   1498 C CZ  . PHE A 1 220 ? 235.897 252.798 233.932 1.00 7.40   ? 220  PHE A CZ  1 
ATOM   1499 N N   . SER A 1 221 ? 237.633 257.094 233.842 1.00 5.51   ? 221  SER A N   1 
ATOM   1500 C CA  . SER A 1 221 ? 236.668 257.737 232.960 1.00 4.94   ? 221  SER A CA  1 
ATOM   1501 C C   . SER A 1 221 ? 236.503 256.909 231.690 1.00 4.86   ? 221  SER A C   1 
ATOM   1502 O O   . SER A 1 221 ? 237.489 256.580 231.030 1.00 4.73   ? 221  SER A O   1 
ATOM   1503 C CB  . SER A 1 221 ? 237.126 259.139 232.616 1.00 4.65   ? 221  SER A CB  1 
ATOM   1504 O OG  . SER A 1 221 ? 236.200 259.785 231.793 1.00 4.81   ? 221  SER A OG  1 
ATOM   1505 N N   . ALA A 1 222 ? 235.266 256.545 231.365 1.00 4.86   ? 222  ALA A N   1 
ATOM   1506 C CA  . ALA A 1 222 ? 235.010 255.715 230.193 1.00 4.33   ? 222  ALA A CA  1 
ATOM   1507 C C   . ALA A 1 222 ? 234.839 256.568 228.943 1.00 4.10   ? 222  ALA A C   1 
ATOM   1508 O O   . ALA A 1 222 ? 234.257 257.651 228.994 1.00 4.23   ? 222  ALA A O   1 
ATOM   1509 C CB  . ALA A 1 222 ? 233.778 254.851 230.413 1.00 5.23   ? 222  ALA A CB  1 
ATOM   1510 N N   . LEU A 1 223 ? 235.318 256.051 227.817 1.00 3.97   ? 223  LEU A N   1 
ATOM   1511 C CA  . LEU A 1 223 ? 235.195 256.720 226.527 1.00 3.56   ? 223  LEU A CA  1 
ATOM   1512 C C   . LEU A 1 223 ? 233.882 256.367 225.842 1.00 3.68   ? 223  LEU A C   1 
ATOM   1513 O O   . LEU A 1 223 ? 233.401 255.238 225.943 1.00 3.80   ? 223  LEU A O   1 
ATOM   1514 C CB  . LEU A 1 223 ? 236.367 256.330 225.621 1.00 3.46   ? 223  LEU A CB  1 
ATOM   1515 C CG  . LEU A 1 223 ? 237.670 257.132 225.786 1.00 3.41   ? 223  LEU A CG  1 
ATOM   1516 C CD1 . LEU A 1 223 ? 238.214 256.975 227.197 1.00 3.82   ? 223  LEU A CD1 1 
ATOM   1517 C CD2 . LEU A 1 223 ? 238.667 256.635 224.782 1.00 3.17   ? 223  LEU A CD2 1 
ATOM   1518 N N   . GLU A 1 224 ? 233.302 257.339 225.144 1.00 3.25   ? 224  GLU A N   1 
ATOM   1519 C CA  . GLU A 1 224 ? 232.019 257.148 224.475 1.00 2.92   ? 224  GLU A CA  1 
ATOM   1520 C C   . GLU A 1 224 ? 232.208 256.994 222.968 1.00 2.91   ? 224  GLU A C   1 
ATOM   1521 O O   . GLU A 1 224 ? 233.166 257.530 222.415 1.00 2.81   ? 224  GLU A O   1 
ATOM   1522 C CB  . GLU A 1 224 ? 231.105 258.339 224.759 1.00 2.76   ? 224  GLU A CB  1 
ATOM   1523 C CG  . GLU A 1 224 ? 230.737 258.513 226.221 1.00 2.83   ? 224  GLU A CG  1 
ATOM   1524 C CD  . GLU A 1 224 ? 229.953 259.769 226.479 1.00 1.56   ? 224  GLU A CD  1 
ATOM   1525 O OE1 . GLU A 1 224 ? 229.713 260.495 225.547 1.00 1.40   ? 224  GLU A OE1 1 
ATOM   1526 O OE2 . GLU A 1 224 ? 229.600 260.007 227.611 1.00 1.50   ? 224  GLU A OE2 1 
ATOM   1527 N N   . PRO A 1 225 ? 231.314 256.272 222.283 1.00 2.82   ? 225  PRO A N   1 
ATOM   1528 C CA  . PRO A 1 225 ? 231.255 256.127 220.841 1.00 2.68   ? 225  PRO A CA  1 
ATOM   1529 C C   . PRO A 1 225 ? 231.209 257.480 220.152 1.00 2.68   ? 225  PRO A C   1 
ATOM   1530 O O   . PRO A 1 225 ? 230.466 258.370 220.565 1.00 2.83   ? 225  PRO A O   1 
ATOM   1531 C CB  . PRO A 1 225 ? 229.941 255.365 220.647 1.00 2.75   ? 225  PRO A CB  1 
ATOM   1532 C CG  . PRO A 1 225 ? 229.768 254.582 221.921 1.00 2.97   ? 225  PRO A CG  1 
ATOM   1533 C CD  . PRO A 1 225 ? 230.316 255.482 223.009 1.00 3.26   ? 225  PRO A CD  1 
ATOM   1534 N N   . LEU A 1 226 ? 231.989 257.622 219.088 1.00 2.78   ? 226  LEU A N   1 
ATOM   1535 C CA  . LEU A 1 226 ? 232.038 258.858 218.321 1.00 2.74   ? 226  LEU A CA  1 
ATOM   1536 C C   . LEU A 1 226 ? 231.475 258.656 216.922 1.00 3.03   ? 226  LEU A C   1 
ATOM   1537 O O   . LEU A 1 226 ? 230.567 259.373 216.498 1.00 3.34   ? 226  LEU A O   1 
ATOM   1538 C CB  . LEU A 1 226 ? 233.487 259.352 218.232 1.00 2.80   ? 226  LEU A CB  1 
ATOM   1539 C CG  . LEU A 1 226 ? 233.741 260.628 217.429 1.00 3.25   ? 226  LEU A CG  1 
ATOM   1540 C CD1 . LEU A 1 226 ? 233.013 261.796 218.063 1.00 3.29   ? 226  LEU A CD1 1 
ATOM   1541 C CD2 . LEU A 1 226 ? 235.233 260.882 217.391 1.00 3.82   ? 226  LEU A CD2 1 
ATOM   1542 N N   . VAL A 1 227 ? 232.032 257.690 216.202 1.00 3.05   ? 227  VAL A N   1 
ATOM   1543 C CA  . VAL A 1 227 ? 231.607 257.405 214.836 1.00 3.13   ? 227  VAL A CA  1 
ATOM   1544 C C   . VAL A 1 227 ? 231.922 255.961 214.452 1.00 3.80   ? 227  VAL A C   1 
ATOM   1545 O O   . VAL A 1 227 ? 232.903 255.384 214.924 1.00 3.65   ? 227  VAL A O   1 
ATOM   1546 C CB  . VAL A 1 227 ? 232.269 258.400 213.856 1.00 3.44   ? 227  VAL A CB  1 
ATOM   1547 C CG1 . VAL A 1 227 ? 233.766 258.226 213.862 1.00 3.79   ? 227  VAL A CG1 1 
ATOM   1548 C CG2 . VAL A 1 227 ? 231.719 258.206 212.453 1.00 5.34   ? 227  VAL A CG2 1 
ATOM   1549 N N   . ASP A 1 228 ? 231.084 255.379 213.598 1.00 4.27   ? 228  ASP A N   1 
ATOM   1550 C CA  . ASP A 1 228 ? 231.279 254.008 213.132 1.00 4.37   ? 228  ASP A CA  1 
ATOM   1551 C C   . ASP A 1 228 ? 231.236 253.957 211.605 1.00 4.89   ? 228  ASP A C   1 
ATOM   1552 O O   . ASP A 1 228 ? 230.191 254.195 210.996 1.00 5.51   ? 228  ASP A O   1 
ATOM   1553 C CB  . ASP A 1 228 ? 230.216 253.092 213.737 1.00 4.05   ? 228  ASP A CB  1 
ATOM   1554 C CG  . ASP A 1 228 ? 230.472 251.632 213.471 1.00 4.49   ? 228  ASP A CG  1 
ATOM   1555 O OD1 . ASP A 1 228 ? 231.181 251.334 212.547 1.00 4.60   ? 228  ASP A OD1 1 
ATOM   1556 O OD2 . ASP A 1 228 ? 229.977 250.816 214.216 1.00 4.93   ? 228  ASP A OD2 1 
ATOM   1557 N N   . LEU A 1 229 ? 232.397 253.739 210.994 1.00 4.88   ? 229  LEU A N   1 
ATOM   1558 C CA  . LEU A 1 229 ? 232.557 253.861 209.547 1.00 5.42   ? 229  LEU A CA  1 
ATOM   1559 C C   . LEU A 1 229 ? 232.619 252.500 208.834 1.00 5.13   ? 229  LEU A C   1 
ATOM   1560 O O   . LEU A 1 229 ? 233.576 251.745 209.023 1.00 5.93   ? 229  LEU A O   1 
ATOM   1561 C CB  . LEU A 1 229 ? 233.851 254.623 209.260 1.00 5.23   ? 229  LEU A CB  1 
ATOM   1562 C CG  . LEU A 1 229 ? 234.025 255.956 209.998 1.00 5.21   ? 229  LEU A CG  1 
ATOM   1563 C CD1 . LEU A 1 229 ? 235.459 256.406 209.857 1.00 5.95   ? 229  LEU A CD1 1 
ATOM   1564 C CD2 . LEU A 1 229 ? 233.082 256.998 209.414 1.00 6.34   ? 229  LEU A CD2 1 
ATOM   1565 N N   . PRO A 1 230 ? 231.647 252.189 207.966 1.00 5.72   ? 230  PRO A N   1 
ATOM   1566 C CA  . PRO A 1 230 ? 231.513 250.954 207.212 1.00 5.70   ? 230  PRO A CA  1 
ATOM   1567 C C   . PRO A 1 230 ? 232.438 250.950 206.001 1.00 6.38   ? 230  PRO A C   1 
ATOM   1568 O O   . PRO A 1 230 ? 231.988 251.117 204.868 1.00 6.95   ? 230  PRO A O   1 
ATOM   1569 C CB  . PRO A 1 230 ? 230.042 250.995 206.795 1.00 5.64   ? 230  PRO A CB  1 
ATOM   1570 C CG  . PRO A 1 230 ? 229.743 252.471 206.641 1.00 6.29   ? 230  PRO A CG  1 
ATOM   1571 C CD  . PRO A 1 230 ? 230.580 253.162 207.713 1.00 6.26   ? 230  PRO A CD  1 
ATOM   1572 N N   . ILE A 1 231 ? 233.736 250.828 206.255 1.00 6.15   ? 231  ILE A N   1 
ATOM   1573 C CA  . ILE A 1 231 ? 234.742 250.994 205.210 1.00 6.20   ? 231  ILE A CA  1 
ATOM   1574 C C   . ILE A 1 231 ? 235.151 249.686 204.524 1.00 6.74   ? 231  ILE A C   1 
ATOM   1575 O O   . ILE A 1 231 ? 235.218 249.628 203.297 1.00 7.29   ? 231  ILE A O   1 
ATOM   1576 C CB  . ILE A 1 231 ? 235.978 251.691 205.778 1.00 6.18   ? 231  ILE A CB  1 
ATOM   1577 C CG1 . ILE A 1 231 ? 235.600 253.093 206.239 1.00 6.50   ? 231  ILE A CG1 1 
ATOM   1578 C CG2 . ILE A 1 231 ? 237.046 251.743 204.722 1.00 7.40   ? 231  ILE A CG2 1 
ATOM   1579 C CD1 . ILE A 1 231 ? 236.639 253.744 207.098 1.00 6.31   ? 231  ILE A CD1 1 
ATOM   1580 N N   . GLY A 1 232 ? 235.442 248.652 205.308 1.00 6.62   ? 232  GLY A N   1 
ATOM   1581 C CA  . GLY A 1 232 ? 235.793 247.348 204.742 1.00 6.22   ? 232  GLY A CA  1 
ATOM   1582 C C   . GLY A 1 232 ? 237.234 247.205 204.232 1.00 6.52   ? 232  GLY A C   1 
ATOM   1583 O O   . GLY A 1 232 ? 237.464 246.510 203.242 1.00 7.42   ? 232  GLY A O   1 
ATOM   1584 N N   . ILE A 1 233 ? 238.207 247.832 204.896 1.00 6.70   ? 233  ILE A N   1 
ATOM   1585 C CA  . ILE A 1 233 ? 239.603 247.684 204.463 1.00 6.98   ? 233  ILE A CA  1 
ATOM   1586 C C   . ILE A 1 233 ? 240.493 247.184 205.605 1.00 7.30   ? 233  ILE A C   1 
ATOM   1587 O O   . ILE A 1 233 ? 240.128 247.297 206.773 1.00 7.39   ? 233  ILE A O   1 
ATOM   1588 C CB  . ILE A 1 233 ? 240.182 249.008 203.918 1.00 7.46   ? 233  ILE A CB  1 
ATOM   1589 C CG1 . ILE A 1 233 ? 240.225 250.068 205.038 1.00 7.10   ? 233  ILE A CG1 1 
ATOM   1590 C CG2 . ILE A 1 233 ? 239.373 249.481 202.706 1.00 7.96   ? 233  ILE A CG2 1 
ATOM   1591 C CD1 . ILE A 1 233 ? 240.956 251.340 204.657 1.00 7.92   ? 233  ILE A CD1 1 
ATOM   1592 N N   . ASN A 1 234 ? 241.675 246.647 205.230 1.00 7.44   ? 234  ASN A N   1 
ATOM   1593 C CA  . ASN A 1 234 ? 242.682 246.194 206.193 1.00 6.99   ? 234  ASN A CA  1 
ATOM   1594 C C   . ASN A 1 234 ? 243.563 247.341 206.656 1.00 6.93   ? 234  ASN A C   1 
ATOM   1595 O O   . ASN A 1 234 ? 243.987 248.181 205.845 1.00 6.79   ? 234  ASN A O   1 
ATOM   1596 C CB  . ASN A 1 234 ? 243.551 245.093 205.563 1.00 9.22   ? 234  ASN A CB  1 
ATOM   1597 C CG  . ASN A 1 234 ? 242.871 243.736 205.522 1.00 11.14  ? 234  ASN A CG  1 
ATOM   1598 O OD1 . ASN A 1 234 ? 242.089 243.385 206.415 1.00 12.12  ? 234  ASN A OD1 1 
ATOM   1599 N ND2 . ASN A 1 234 ? 243.178 242.964 204.493 1.00 12.32  ? 234  ASN A ND2 1 
ATOM   1600 N N   . ILE A 1 235 ? 243.871 247.373 207.957 1.00 6.29   ? 235  ILE A N   1 
ATOM   1601 C CA  . ILE A 1 235 ? 244.797 248.331 208.564 1.00 5.17   ? 235  ILE A CA  1 
ATOM   1602 C C   . ILE A 1 235 ? 245.862 247.597 209.366 1.00 4.80   ? 235  ILE A C   1 
ATOM   1603 O O   . ILE A 1 235 ? 245.537 246.810 210.255 1.00 4.62   ? 235  ILE A O   1 
ATOM   1604 C CB  . ILE A 1 235 ? 244.047 249.312 209.484 1.00 4.63   ? 235  ILE A CB  1 
ATOM   1605 C CG1 . ILE A 1 235 ? 243.012 250.108 208.670 1.00 5.20   ? 235  ILE A CG1 1 
ATOM   1606 C CG2 . ILE A 1 235 ? 245.041 250.240 210.178 1.00 4.50   ? 235  ILE A CG2 1 
ATOM   1607 C CD1 . ILE A 1 235 ? 242.030 250.884 209.512 1.00 5.03   ? 235  ILE A CD1 1 
ATOM   1608 N N   . THR A 1 236 ? 247.129 247.855 209.064 1.00 4.88   ? 236  THR A N   1 
ATOM   1609 C CA  . THR A 1 236 ? 248.222 247.229 209.797 1.00 4.23   ? 236  THR A CA  1 
ATOM   1610 C C   . THR A 1 236 ? 249.184 248.256 210.376 1.00 4.07   ? 236  THR A C   1 
ATOM   1611 O O   . THR A 1 236 ? 249.915 247.960 211.322 1.00 3.80   ? 236  THR A O   1 
ATOM   1612 C CB  . THR A 1 236 ? 249.002 246.249 208.909 1.00 4.67   ? 236  THR A CB  1 
ATOM   1613 O OG1 . THR A 1 236 ? 249.537 246.951 207.785 1.00 5.25   ? 236  THR A OG1 1 
ATOM   1614 C CG2 . THR A 1 236 ? 248.099 245.132 208.428 1.00 5.16   ? 236  THR A CG2 1 
ATOM   1615 N N   . ARG A 1 237 ? 249.193 249.453 209.800 1.00 4.21   ? 237  ARG A N   1 
ATOM   1616 C CA  . ARG A 1 237 ? 250.095 250.521 210.222 1.00 3.86   ? 237  ARG A CA  1 
ATOM   1617 C C   . ARG A 1 237 ? 249.385 251.868 210.222 1.00 3.92   ? 237  ARG A C   1 
ATOM   1618 O O   . ARG A 1 237 ? 248.429 252.069 209.471 1.00 4.38   ? 237  ARG A O   1 
ATOM   1619 C CB  . ARG A 1 237 ? 251.314 250.575 209.311 1.00 4.30   ? 237  ARG A CB  1 
ATOM   1620 C CG  . ARG A 1 237 ? 252.164 249.321 209.349 1.00 4.54   ? 237  ARG A CG  1 
ATOM   1621 C CD  . ARG A 1 237 ? 253.426 249.438 208.587 1.00 5.00   ? 237  ARG A CD  1 
ATOM   1622 N NE  . ARG A 1 237 ? 253.209 249.464 207.153 1.00 5.13   ? 237  ARG A NE  1 
ATOM   1623 C CZ  . ARG A 1 237 ? 254.120 249.083 206.236 1.00 5.12   ? 237  ARG A CZ  1 
ATOM   1624 N NH1 . ARG A 1 237 ? 253.828 249.171 204.968 1.00 6.63   ? 237  ARG A NH1 1 
ATOM   1625 N NH2 . ARG A 1 237 ? 255.296 248.620 206.605 1.00 5.44   ? 237  ARG A NH2 1 
ATOM   1626 N N   . PHE A 1 238 ? 249.871 252.806 211.032 1.00 3.62   ? 238  PHE A N   1 
ATOM   1627 C CA  . PHE A 1 238 ? 249.297 254.144 211.031 1.00 3.76   ? 238  PHE A CA  1 
ATOM   1628 C C   . PHE A 1 238 ? 250.325 255.221 211.356 1.00 3.92   ? 238  PHE A C   1 
ATOM   1629 O O   . PHE A 1 238 ? 251.380 254.945 211.929 1.00 3.96   ? 238  PHE A O   1 
ATOM   1630 C CB  . PHE A 1 238 ? 248.135 254.231 212.024 1.00 3.74   ? 238  PHE A CB  1 
ATOM   1631 C CG  . PHE A 1 238 ? 248.543 254.296 213.460 1.00 3.18   ? 238  PHE A CG  1 
ATOM   1632 C CD1 . PHE A 1 238 ? 248.905 253.159 214.152 1.00 3.17   ? 238  PHE A CD1 1 
ATOM   1633 C CD2 . PHE A 1 238 ? 248.543 255.508 214.129 1.00 3.32   ? 238  PHE A CD2 1 
ATOM   1634 C CE1 . PHE A 1 238 ? 249.270 253.234 215.478 1.00 2.90   ? 238  PHE A CE1 1 
ATOM   1635 C CE2 . PHE A 1 238 ? 248.904 255.584 215.453 1.00 2.69   ? 238  PHE A CE2 1 
ATOM   1636 C CZ  . PHE A 1 238 ? 249.270 254.446 216.127 1.00 2.70   ? 238  PHE A CZ  1 
ATOM   1637 N N   . GLN A 1 239 ? 250.002 256.456 210.987 1.00 4.41   ? 239  GLN A N   1 
ATOM   1638 C CA  . GLN A 1 239 ? 250.873 257.603 211.222 1.00 4.90   ? 239  GLN A CA  1 
ATOM   1639 C C   . GLN A 1 239 ? 250.064 258.823 211.658 1.00 5.37   ? 239  GLN A C   1 
ATOM   1640 O O   . GLN A 1 239 ? 248.916 258.990 211.252 1.00 5.57   ? 239  GLN A O   1 
ATOM   1641 C CB  . GLN A 1 239 ? 251.678 257.914 209.960 1.00 5.50   ? 239  GLN A CB  1 
ATOM   1642 C CG  . GLN A 1 239 ? 252.744 258.972 210.137 1.00 6.21   ? 239  GLN A CG  1 
ATOM   1643 C CD  . GLN A 1 239 ? 253.626 259.087 208.923 1.00 7.31   ? 239  GLN A CD  1 
ATOM   1644 O OE1 . GLN A 1 239 ? 253.162 258.907 207.794 1.00 7.54   ? 239  GLN A OE1 1 
ATOM   1645 N NE2 . GLN A 1 239 ? 254.902 259.382 209.134 1.00 8.61   ? 239  GLN A NE2 1 
ATOM   1646 N N   . THR A 1 240 ? 250.658 259.669 212.495 1.00 5.83   ? 240  THR A N   1 
ATOM   1647 C CA  . THR A 1 240 ? 249.977 260.868 212.985 1.00 6.18   ? 240  THR A CA  1 
ATOM   1648 C C   . THR A 1 240 ? 250.329 262.101 212.153 1.00 7.83   ? 240  THR A C   1 
ATOM   1649 O O   . THR A 1 240 ? 251.499 262.354 211.865 1.00 8.32   ? 240  THR A O   1 
ATOM   1650 C CB  . THR A 1 240 ? 250.319 261.120 214.466 1.00 5.96   ? 240  THR A CB  1 
ATOM   1651 O OG1 . THR A 1 240 ? 249.909 259.989 215.243 1.00 5.58   ? 240  THR A OG1 1 
ATOM   1652 C CG2 . THR A 1 240 ? 249.601 262.359 214.981 1.00 6.97   ? 240  THR A CG2 1 
ATOM   1653 N N   . LEU A 1 241 ? 249.306 262.863 211.767 1.00 8.17   ? 241  LEU A N   1 
ATOM   1654 C CA  . LEU A 1 241 ? 249.482 264.093 210.996 1.00 9.68   ? 241  LEU A CA  1 
ATOM   1655 C C   . LEU A 1 241 ? 249.460 265.336 211.872 1.00 10.55  ? 241  LEU A C   1 
ATOM   1656 O O   . LEU A 1 241 ? 248.521 265.551 212.645 1.00 10.64  ? 241  LEU A O   1 
ATOM   1657 C CB  . LEU A 1 241 ? 248.386 264.221 209.931 1.00 8.99   ? 241  LEU A CB  1 
ATOM   1658 C CG  . LEU A 1 241 ? 248.455 263.242 208.770 1.00 9.03   ? 241  LEU A CG  1 
ATOM   1659 C CD1 . LEU A 1 241 ? 247.176 263.336 207.971 1.00 9.18   ? 241  LEU A CD1 1 
ATOM   1660 C CD2 . LEU A 1 241 ? 249.653 263.587 207.892 1.00 13.02  ? 241  LEU A CD2 1 
ATOM   1661 N N   . LEU A 1 242 ? 250.492 266.162 211.725 1.00 12.24  ? 242  LEU A N   1 
ATOM   1662 C CA  . LEU A 1 242 ? 250.627 267.401 212.481 1.00 13.59  ? 242  LEU A CA  1 
ATOM   1663 C C   . LEU A 1 242 ? 250.511 268.624 211.578 1.00 16.18  ? 242  LEU A C   1 
ATOM   1664 O O   . LEU A 1 242 ? 250.803 268.551 210.385 1.00 17.46  ? 242  LEU A O   1 
ATOM   1665 C CB  . LEU A 1 242 ? 251.986 267.439 213.181 1.00 14.35  ? 242  LEU A CB  1 
ATOM   1666 C CG  . LEU A 1 242 ? 252.355 266.209 214.010 1.00 12.15  ? 242  LEU A CG  1 
ATOM   1667 C CD1 . LEU A 1 242 ? 253.727 266.409 214.582 1.00 12.10  ? 242  LEU A CD1 1 
ATOM   1668 C CD2 . LEU A 1 242 ? 251.339 265.988 215.114 1.00 12.04  ? 242  LEU A CD2 1 
ATOM   1669 N N   . ALA A 1 243 ? 250.134 269.756 212.168 1.00 16.45  ? 243  ALA A N   1 
ATOM   1670 C CA  . ALA A 1 243 ? 250.151 271.037 211.472 1.00 19.51  ? 243  ALA A CA  1 
ATOM   1671 C C   . ALA A 1 243 ? 251.449 271.779 211.765 1.00 21.16  ? 243  ALA A C   1 
ATOM   1672 O O   . ALA A 1 243 ? 251.745 272.098 212.917 1.00 20.09  ? 243  ALA A O   1 
ATOM   1673 C CB  . ALA A 1 243 ? 248.962 271.884 211.887 1.00 20.12  ? 243  ALA A CB  1 
ATOM   1674 N N   . LEU A 1 244 ? 252.231 272.028 210.722 1.00 23.91  ? 244  LEU A N   1 
ATOM   1675 C CA  . LEU A 1 244 ? 253.529 272.678 210.863 1.00 24.17  ? 244  LEU A CA  1 
ATOM   1676 C C   . LEU A 1 244 ? 253.511 274.080 210.274 1.00 26.87  ? 244  LEU A C   1 
ATOM   1677 O O   . LEU A 1 244 ? 252.781 274.354 209.321 1.00 28.48  ? 244  LEU A O   1 
ATOM   1678 C CB  . LEU A 1 244 ? 254.622 271.866 210.157 1.00 24.67  ? 244  LEU A CB  1 
ATOM   1679 C CG  . LEU A 1 244 ? 254.728 270.379 210.523 1.00 22.85  ? 244  LEU A CG  1 
ATOM   1680 C CD1 . LEU A 1 244 ? 255.866 269.760 209.726 1.00 24.23  ? 244  LEU A CD1 1 
ATOM   1681 C CD2 . LEU A 1 244 ? 254.956 270.223 212.011 1.00 21.51  ? 244  LEU A CD2 1 
ATOM   1682 N N   . HIS A 1 245 ? 254.363 274.949 210.802 1.00 27.48  ? 245  HIS A N   1 
ATOM   1683 C CA  . HIS A 1 245 ? 254.551 276.272 210.224 1.00 28.86  ? 245  HIS A CA  1 
ATOM   1684 C C   . HIS A 1 245 ? 255.992 276.428 209.747 1.00 26.97  ? 245  HIS A C   1 
ATOM   1685 O O   . HIS A 1 245 ? 256.878 275.700 210.205 1.00 38.50  ? 245  HIS A O   1 
ATOM   1686 C CB  . HIS A 1 245 ? 254.184 277.369 211.230 1.00 31.97  ? 245  HIS A CB  1 
ATOM   1687 C CG  . HIS A 1 245 ? 255.034 277.400 212.454 1.00 30.48  ? 245  HIS A CG  1 
ATOM   1688 N ND1 . HIS A 1 245 ? 254.776 276.617 213.559 1.00 29.49  ? 245  HIS A ND1 1 
ATOM   1689 C CD2 . HIS A 1 245 ? 256.126 278.134 212.759 1.00 30.02  ? 245  HIS A CD2 1 
ATOM   1690 C CE1 . HIS A 1 245 ? 255.676 276.869 214.491 1.00 27.29  ? 245  HIS A CE1 1 
ATOM   1691 N NE2 . HIS A 1 245 ? 256.505 277.786 214.032 1.00 28.64  ? 245  HIS A NE2 1 
ATOM   1692 N N   . ASN A 1 246 ? 256.218 277.332 208.792 1.00 28.82  ? 246  ASN A N   1 
ATOM   1693 C CA  . ASN A 1 246 ? 257.537 277.544 208.199 1.00 27.81  ? 246  ASN A CA  1 
ATOM   1694 C C   . ASN A 1 246 ? 258.288 278.664 208.914 1.00 30.55  ? 246  ASN A C   1 
ATOM   1695 O O   . ASN A 1 246 ? 257.924 279.833 208.812 1.00 30.28  ? 246  ASN A O   1 
ATOM   1696 C CB  . ASN A 1 246 ? 257.416 277.834 206.707 1.00 29.24  ? 246  ASN A CB  1 
ATOM   1697 C CG  . ASN A 1 246 ? 258.732 277.672 205.958 1.00 30.44  ? 246  ASN A CG  1 
ATOM   1698 O OD1 . ASN A 1 246 ? 259.651 276.980 206.424 1.00 28.95  ? 246  ASN A OD1 1 
ATOM   1699 N ND2 . ASN A 1 246 ? 258.837 278.299 204.806 1.00 30.41  ? 246  ASN A ND2 1 
ATOM   1700 N N   . SER A 1 247 ? 259.341 278.286 209.653 1.00 30.13  ? 247  SER A N   1 
ATOM   1701 C CA  . SER A 1 247 ? 260.182 279.212 210.408 1.00 30.97  ? 247  SER A CA  1 
ATOM   1702 C C   . SER A 1 247 ? 261.498 279.434 209.674 1.00 31.90  ? 247  SER A C   1 
ATOM   1703 O O   . SER A 1 247 ? 261.797 278.747 208.697 1.00 31.23  ? 247  SER A O   1 
ATOM   1704 C CB  . SER A 1 247 ? 260.457 278.667 211.797 1.00 31.62  ? 247  SER A CB  1 
ATOM   1705 N N   . SER A 1 248 ? 262.301 280.369 210.162 1.00 31.44  ? 248  SER A N   1 
ATOM   1706 C CA  . SER A 1 248 ? 263.598 280.653 209.554 1.00 31.53  ? 248  SER A CA  1 
ATOM   1707 C C   . SER A 1 248 ? 264.547 279.462 209.666 1.00 32.15  ? 248  SER A C   1 
ATOM   1708 O O   . SER A 1 248 ? 265.547 279.384 208.951 1.00 32.30  ? 248  SER A O   1 
ATOM   1709 C CB  . SER A 1 248 ? 264.222 281.867 210.212 1.00 32.65  ? 248  SER A CB  1 
ATOM   1710 N N   . SER A 1 249 ? 264.225 278.537 210.563 1.00 32.46  ? 249  SER A N   1 
ATOM   1711 C CA  . SER A 1 249 ? 265.028 277.343 210.786 1.00 32.69  ? 249  SER A CA  1 
ATOM   1712 C C   . SER A 1 249 ? 264.439 276.125 210.079 1.00 31.01  ? 249  SER A C   1 
ATOM   1713 O O   . SER A 1 249 ? 264.937 275.009 210.232 1.00 31.78  ? 249  SER A O   1 
ATOM   1714 C CB  . SER A 1 249 ? 265.132 277.068 212.271 1.00 30.60  ? 249  SER A CB  1 
ATOM   1715 N N   . GLY A 1 250 ? 263.365 276.336 209.319 1.00 30.36  ? 250  GLY A N   1 
ATOM   1716 C CA  . GLY A 1 250 ? 262.683 275.247 208.630 1.00 30.06  ? 250  GLY A CA  1 
ATOM   1717 C C   . GLY A 1 250 ? 261.302 274.988 209.224 1.00 28.98  ? 250  GLY A C   1 
ATOM   1718 O O   . GLY A 1 250 ? 260.839 275.730 210.092 1.00 29.84  ? 250  GLY A O   1 
ATOM   1719 N N   . TRP A 1 251 ? 260.646 273.933 208.751 1.00 28.00  ? 251  TRP A N   1 
ATOM   1720 C CA  . TRP A 1 251 ? 259.302 273.601 209.209 1.00 27.37  ? 251  TRP A CA  1 
ATOM   1721 C C   . TRP A 1 251 ? 259.345 273.060 210.631 1.00 26.56  ? 251  TRP A C   1 
ATOM   1722 O O   . TRP A 1 251 ? 260.164 272.198 210.950 1.00 26.38  ? 251  TRP A O   1 
ATOM   1723 C CB  . TRP A 1 251 ? 258.676 272.557 208.287 1.00 27.64  ? 251  TRP A CB  1 
ATOM   1724 C CG  . TRP A 1 251 ? 258.312 273.086 206.940 1.00 27.77  ? 251  TRP A CG  1 
ATOM   1725 C CD1 . TRP A 1 251 ? 259.060 273.016 205.805 1.00 28.44  ? 251  TRP A CD1 1 
ATOM   1726 C CD2 . TRP A 1 251 ? 257.090 273.756 206.573 1.00 27.28  ? 251  TRP A CD2 1 
ATOM   1727 N NE1 . TRP A 1 251 ? 258.390 273.599 204.763 1.00 28.31  ? 251  TRP A NE1 1 
ATOM   1728 C CE2 . TRP A 1 251 ? 257.181 274.054 205.213 1.00 28.14  ? 251  TRP A CE2 1 
ATOM   1729 C CE3 . TRP A 1 251 ? 255.940 274.118 207.276 1.00 27.34  ? 251  TRP A CE3 1 
ATOM   1730 C CZ2 . TRP A 1 251 ? 256.165 274.699 204.538 1.00 28.68  ? 251  TRP A CZ2 1 
ATOM   1731 C CZ3 . TRP A 1 251 ? 254.920 274.767 206.598 1.00 27.77  ? 251  TRP A CZ3 1 
ATOM   1732 C CH2 . TRP A 1 251 ? 255.030 275.050 205.263 1.00 28.73  ? 251  TRP A CH2 1 
ATOM   1733 N N   . THR A 1 252 ? 258.470 273.572 211.487 1.00 26.15  ? 252  THR A N   1 
ATOM   1734 C CA  . THR A 1 252 ? 258.452 273.145 212.879 1.00 25.26  ? 252  THR A CA  1 
ATOM   1735 C C   . THR A 1 252 ? 257.072 273.294 213.510 1.00 24.43  ? 252  THR A C   1 
ATOM   1736 O O   . THR A 1 252 ? 256.087 273.575 212.827 1.00 26.22  ? 252  THR A O   1 
ATOM   1737 C CB  . THR A 1 252 ? 259.496 273.930 213.695 1.00 25.25  ? 252  THR A CB  1 
ATOM   1738 O OG1 . THR A 1 252 ? 259.637 273.333 214.991 1.00 23.67  ? 252  THR A OG1 1 
ATOM   1739 C CG2 . THR A 1 252 ? 259.074 275.383 213.842 1.00 25.85  ? 252  THR A CG2 1 
ATOM   1740 N N   . ALA A 1 253 ? 257.006 273.081 214.817 1.00 23.12  ? 253  ALA A N   1 
ATOM   1741 C CA  . ALA A 1 253 ? 255.754 273.141 215.560 1.00 22.43  ? 253  ALA A CA  1 
ATOM   1742 C C   . ALA A 1 253 ? 256.035 273.329 217.042 1.00 21.11  ? 253  ALA A C   1 
ATOM   1743 O O   . ALA A 1 253 ? 257.188 273.304 217.470 1.00 21.05  ? 253  ALA A O   1 
ATOM   1744 C CB  . ALA A 1 253 ? 254.930 271.886 215.329 1.00 20.66  ? 253  ALA A CB  1 
ATOM   1745 N N   . GLY A 1 254 ? 254.977 273.523 217.820 1.00 19.72  ? 254  GLY A N   1 
ATOM   1746 C CA  . GLY A 1 254 ? 255.119 273.656 219.265 1.00 18.71  ? 254  GLY A CA  1 
ATOM   1747 C C   . GLY A 1 254 ? 255.377 272.291 219.892 1.00 17.60  ? 254  GLY A C   1 
ATOM   1748 O O   . GLY A 1 254 ? 255.562 271.301 219.188 1.00 17.39  ? 254  GLY A O   1 
ATOM   1749 N N   . ALA A 1 255 ? 255.397 272.239 221.219 1.00 17.06  ? 255  ALA A N   1 
ATOM   1750 C CA  . ALA A 1 255 ? 255.778 271.016 221.920 1.00 16.00  ? 255  ALA A CA  1 
ATOM   1751 C C   . ALA A 1 255 ? 254.651 269.989 221.943 1.00 15.47  ? 255  ALA A C   1 
ATOM   1752 O O   . ALA A 1 255 ? 254.078 269.705 222.994 1.00 14.45  ? 255  ALA A O   1 
ATOM   1753 C CB  . ALA A 1 255 ? 256.200 271.343 223.343 1.00 17.17  ? 255  ALA A CB  1 
ATOM   1754 N N   . ALA A 1 256 ? 254.354 269.423 220.779 1.00 14.96  ? 256  ALA A N   1 
ATOM   1755 C CA  . ALA A 1 256 ? 253.341 268.380 220.672 1.00 13.66  ? 256  ALA A CA  1 
ATOM   1756 C C   . ALA A 1 256 ? 253.903 267.040 221.129 1.00 12.55  ? 256  ALA A C   1 
ATOM   1757 O O   . ALA A 1 256 ? 255.054 266.701 220.836 1.00 12.45  ? 256  ALA A O   1 
ATOM   1758 C CB  . ALA A 1 256 ? 252.833 268.270 219.244 1.00 14.07  ? 256  ALA A CB  1 
ATOM   1759 N N   . ALA A 1 257 ? 253.069 266.275 221.827 1.00 10.82  ? 257  ALA A N   1 
ATOM   1760 C CA  . ALA A 1 257 ? 253.429 264.951 222.312 1.00 9.46   ? 257  ALA A CA  1 
ATOM   1761 C C   . ALA A 1 257 ? 252.182 264.087 222.417 1.00 8.05   ? 257  ALA A C   1 
ATOM   1762 O O   . ALA A 1 257 ? 251.071 264.604 222.528 1.00 8.43   ? 257  ALA A O   1 
ATOM   1763 C CB  . ALA A 1 257 ? 254.123 265.046 223.661 1.00 9.65   ? 257  ALA A CB  1 
ATOM   1764 N N   . TYR A 1 258 ? 252.368 262.776 222.374 1.00 7.49   ? 258  TYR A N   1 
ATOM   1765 C CA  . TYR A 1 258 ? 251.243 261.855 222.457 1.00 6.56   ? 258  TYR A CA  1 
ATOM   1766 C C   . TYR A 1 258 ? 251.648 260.489 222.989 1.00 6.31   ? 258  TYR A C   1 
ATOM   1767 O O   . TYR A 1 258 ? 252.828 260.139 223.016 1.00 6.38   ? 258  TYR A O   1 
ATOM   1768 C CB  . TYR A 1 258 ? 250.562 261.731 221.094 1.00 5.97   ? 258  TYR A CB  1 
ATOM   1769 C CG  . TYR A 1 258 ? 251.480 261.322 219.971 1.00 6.32   ? 258  TYR A CG  1 
ATOM   1770 C CD1 . TYR A 1 258 ? 252.156 262.290 219.246 1.00 6.56   ? 258  TYR A CD1 1 
ATOM   1771 C CD2 . TYR A 1 258 ? 251.637 259.989 219.656 1.00 5.91   ? 258  TYR A CD2 1 
ATOM   1772 C CE1 . TYR A 1 258 ? 252.987 261.920 218.210 1.00 6.89   ? 258  TYR A CE1 1 
ATOM   1773 C CE2 . TYR A 1 258 ? 252.467 259.617 218.620 1.00 5.84   ? 258  TYR A CE2 1 
ATOM   1774 C CZ  . TYR A 1 258 ? 253.139 260.578 217.898 1.00 6.42   ? 258  TYR A CZ  1 
ATOM   1775 O OH  . TYR A 1 258 ? 253.965 260.208 216.865 1.00 7.65   ? 258  TYR A OH  1 
ATOM   1776 N N   . TYR A 1 259 ? 250.656 259.722 223.419 1.00 5.65   ? 259  TYR A N   1 
ATOM   1777 C CA  . TYR A 1 259 ? 250.874 258.402 223.986 1.00 5.11   ? 259  TYR A CA  1 
ATOM   1778 C C   . TYR A 1 259 ? 250.214 257.332 223.127 1.00 4.25   ? 259  TYR A C   1 
ATOM   1779 O O   . TYR A 1 259 ? 249.090 257.516 222.659 1.00 4.09   ? 259  TYR A O   1 
ATOM   1780 C CB  . TYR A 1 259 ? 250.286 258.343 225.394 1.00 5.28   ? 259  TYR A CB  1 
ATOM   1781 C CG  . TYR A 1 259 ? 250.827 259.364 226.358 1.00 6.22   ? 259  TYR A CG  1 
ATOM   1782 C CD1 . TYR A 1 259 ? 251.945 259.081 227.114 1.00 6.56   ? 259  TYR A CD1 1 
ATOM   1783 C CD2 . TYR A 1 259 ? 250.184 260.580 226.504 1.00 6.38   ? 259  TYR A CD2 1 
ATOM   1784 C CE1 . TYR A 1 259 ? 252.420 260.009 228.015 1.00 6.97   ? 259  TYR A CE1 1 
ATOM   1785 C CE2 . TYR A 1 259 ? 250.656 261.507 227.405 1.00 6.96   ? 259  TYR A CE2 1 
ATOM   1786 C CZ  . TYR A 1 259 ? 251.771 261.223 228.160 1.00 7.86   ? 259  TYR A CZ  1 
ATOM   1787 O OH  . TYR A 1 259 ? 252.243 262.143 229.067 1.00 8.85   ? 259  TYR A OH  1 
ATOM   1788 N N   . VAL A 1 260 ? 250.896 256.204 222.937 1.00 4.18   ? 260  VAL A N   1 
ATOM   1789 C CA  . VAL A 1 260 ? 250.320 255.104 222.167 1.00 3.40   ? 260  VAL A CA  1 
ATOM   1790 C C   . VAL A 1 260 ? 250.369 253.774 222.912 1.00 3.36   ? 260  VAL A C   1 
ATOM   1791 O O   . VAL A 1 260 ? 251.439 253.306 223.310 1.00 3.83   ? 260  VAL A O   1 
ATOM   1792 C CB  . VAL A 1 260 ? 251.046 254.953 220.816 1.00 3.45   ? 260  VAL A CB  1 
ATOM   1793 C CG1 . VAL A 1 260 ? 250.446 253.802 220.019 1.00 2.90   ? 260  VAL A CG1 1 
ATOM   1794 C CG2 . VAL A 1 260 ? 250.938 256.249 220.036 1.00 3.88   ? 260  VAL A CG2 1 
ATOM   1795 N N   . GLY A 1 261 ? 249.206 253.149 223.061 1.00 2.63   ? 261  GLY A N   1 
ATOM   1796 C CA  . GLY A 1 261 ? 249.102 251.834 223.680 1.00 2.41   ? 261  GLY A CA  1 
ATOM   1797 C C   . GLY A 1 261 ? 248.369 250.884 222.745 1.00 2.04   ? 261  GLY A C   1 
ATOM   1798 O O   . GLY A 1 261 ? 247.864 251.303 221.706 1.00 2.27   ? 261  GLY A O   1 
ATOM   1799 N N   . TYR A 1 262 ? 248.301 249.610 223.113 1.00 2.12   ? 262  TYR A N   1 
ATOM   1800 C CA  . TYR A 1 262 ? 247.630 248.628 222.265 1.00 2.21   ? 262  TYR A CA  1 
ATOM   1801 C C   . TYR A 1 262 ? 246.636 247.801 223.054 1.00 2.32   ? 262  TYR A C   1 
ATOM   1802 O O   . TYR A 1 262 ? 246.857 247.494 224.225 1.00 2.68   ? 262  TYR A O   1 
ATOM   1803 C CB  . TYR A 1 262 ? 248.658 247.734 221.573 1.00 2.32   ? 262  TYR A CB  1 
ATOM   1804 C CG  . TYR A 1 262 ? 249.596 248.515 220.699 1.00 2.24   ? 262  TYR A CG  1 
ATOM   1805 C CD1 . TYR A 1 262 ? 249.237 248.822 219.404 1.00 2.20   ? 262  TYR A CD1 1 
ATOM   1806 C CD2 . TYR A 1 262 ? 250.805 248.947 221.200 1.00 2.49   ? 262  TYR A CD2 1 
ATOM   1807 C CE1 . TYR A 1 262 ? 250.082 249.561 218.616 1.00 2.28   ? 262  TYR A CE1 1 
ATOM   1808 C CE2 . TYR A 1 262 ? 251.650 249.687 220.409 1.00 2.58   ? 262  TYR A CE2 1 
ATOM   1809 C CZ  . TYR A 1 262 ? 251.292 249.995 219.124 1.00 2.45   ? 262  TYR A CZ  1 
ATOM   1810 O OH  . TYR A 1 262 ? 252.134 250.744 218.342 1.00 3.01   ? 262  TYR A OH  1 
ATOM   1811 N N   . LEU A 1 263 ? 245.543 247.434 222.399 1.00 2.30   ? 263  LEU A N   1 
ATOM   1812 C CA  . LEU A 1 263 ? 244.467 246.707 223.054 1.00 2.48   ? 263  LEU A CA  1 
ATOM   1813 C C   . LEU A 1 263 ? 244.710 245.206 223.036 1.00 2.69   ? 263  LEU A C   1 
ATOM   1814 O O   . LEU A 1 263 ? 245.352 244.680 222.127 1.00 2.86   ? 263  LEU A O   1 
ATOM   1815 C CB  . LEU A 1 263 ? 243.139 246.997 222.351 1.00 2.60   ? 263  LEU A CB  1 
ATOM   1816 C CG  . LEU A 1 263 ? 242.760 248.472 222.169 1.00 2.39   ? 263  LEU A CG  1 
ATOM   1817 C CD1 . LEU A 1 263 ? 241.442 248.543 221.424 1.00 2.59   ? 263  LEU A CD1 1 
ATOM   1818 C CD2 . LEU A 1 263 ? 242.656 249.159 223.511 1.00 2.69   ? 263  LEU A CD2 1 
ATOM   1819 N N   . GLN A 1 264 ? 244.166 244.515 224.031 1.00 2.81   ? 264  GLN A N   1 
ATOM   1820 C CA  . GLN A 1 264 ? 244.215 243.060 224.089 1.00 2.86   ? 264  GLN A CA  1 
ATOM   1821 C C   . GLN A 1 264 ? 242.844 242.500 224.455 1.00 3.00   ? 264  GLN A C   1 
ATOM   1822 O O   . GLN A 1 264 ? 242.061 243.173 225.123 1.00 3.19   ? 264  GLN A O   1 
ATOM   1823 C CB  . GLN A 1 264 ? 245.262 242.598 225.108 1.00 3.11   ? 264  GLN A CB  1 
ATOM   1824 C CG  . GLN A 1 264 ? 246.688 242.929 224.730 1.00 2.89   ? 264  GLN A CG  1 
ATOM   1825 C CD  . GLN A 1 264 ? 247.690 242.285 225.659 1.00 3.03   ? 264  GLN A CD  1 
ATOM   1826 O OE1 . GLN A 1 264 ? 247.373 241.321 226.361 1.00 3.54   ? 264  GLN A OE1 1 
ATOM   1827 N NE2 . GLN A 1 264 ? 248.907 242.809 225.671 1.00 3.19   ? 264  GLN A NE2 1 
ATOM   1828 N N   . PRO A 1 265 ? 242.533 241.273 224.027 1.00 3.09   ? 265  PRO A N   1 
ATOM   1829 C CA  . PRO A 1 265 ? 241.328 240.532 224.347 1.00 3.42   ? 265  PRO A CA  1 
ATOM   1830 C C   . PRO A 1 265 ? 241.327 240.097 225.804 1.00 3.80   ? 265  PRO A C   1 
ATOM   1831 O O   . PRO A 1 265 ? 241.984 239.123 226.172 1.00 3.93   ? 265  PRO A O   1 
ATOM   1832 C CB  . PRO A 1 265 ? 241.404 239.342 223.384 1.00 3.23   ? 265  PRO A CB  1 
ATOM   1833 C CG  . PRO A 1 265 ? 242.882 239.172 223.092 1.00 2.83   ? 265  PRO A CG  1 
ATOM   1834 C CD  . PRO A 1 265 ? 243.460 240.573 223.132 1.00 2.96   ? 265  PRO A CD  1 
ATOM   1835 N N   . ARG A 1 266 ? 240.617 240.852 226.633 1.00 4.04   ? 266  ARG A N   1 
ATOM   1836 C CA  . ARG A 1 266 ? 240.568 240.602 228.066 1.00 4.75   ? 266  ARG A CA  1 
ATOM   1837 C C   . ARG A 1 266 ? 239.156 240.743 228.611 1.00 5.29   ? 266  ARG A C   1 
ATOM   1838 O O   . ARG A 1 266 ? 238.291 241.355 227.980 1.00 5.16   ? 266  ARG A O   1 
ATOM   1839 C CB  . ARG A 1 266 ? 241.510 241.531 228.813 1.00 4.60   ? 266  ARG A CB  1 
ATOM   1840 C CG  . ARG A 1 266 ? 242.976 241.206 228.630 1.00 4.74   ? 266  ARG A CG  1 
ATOM   1841 C CD  . ARG A 1 266 ? 243.830 241.906 229.618 1.00 5.41   ? 266  ARG A CD  1 
ATOM   1842 N NE  . ARG A 1 266 ? 245.186 241.384 229.604 1.00 5.62   ? 266  ARG A NE  1 
ATOM   1843 C CZ  . ARG A 1 266 ? 246.109 241.586 230.567 1.00 6.09   ? 266  ARG A CZ  1 
ATOM   1844 N NH1 . ARG A 1 266 ? 247.302 241.048 230.446 1.00 5.86   ? 266  ARG A NH1 1 
ATOM   1845 N NH2 . ARG A 1 266 ? 245.827 242.320 231.632 1.00 6.60   ? 266  ARG A NH2 1 
ATOM   1846 N N   . THR A 1 267 ? 238.920 240.159 229.780 1.00 6.07   ? 267  THR A N   1 
ATOM   1847 C CA  . THR A 1 267 ? 237.612 240.234 230.415 1.00 6.76   ? 267  THR A CA  1 
ATOM   1848 C C   . THR A 1 267 ? 237.587 241.315 231.481 1.00 7.13   ? 267  THR A C   1 
ATOM   1849 O O   . THR A 1 267 ? 238.439 241.350 232.370 1.00 8.14   ? 267  THR A O   1 
ATOM   1850 C CB  . THR A 1 267 ? 237.212 238.883 231.032 1.00 6.65   ? 267  THR A CB  1 
ATOM   1851 O OG1 . THR A 1 267 ? 237.159 237.889 230.003 1.00 5.83   ? 267  THR A OG1 1 
ATOM   1852 C CG2 . THR A 1 267 ? 235.845 238.990 231.695 1.00 7.38   ? 267  THR A CG2 1 
ATOM   1853 N N   . PHE A 1 268 ? 236.615 242.208 231.369 1.00 7.56   ? 268  PHE A N   1 
ATOM   1854 C CA  . PHE A 1 268 ? 236.443 243.298 232.315 1.00 8.15   ? 268  PHE A CA  1 
ATOM   1855 C C   . PHE A 1 268 ? 235.099 243.237 233.018 1.00 8.47   ? 268  PHE A C   1 
ATOM   1856 O O   . PHE A 1 268 ? 234.076 242.922 232.406 1.00 8.38   ? 268  PHE A O   1 
ATOM   1857 C CB  . PHE A 1 268 ? 236.576 244.650 231.609 1.00 7.30   ? 268  PHE A CB  1 
ATOM   1858 C CG  . PHE A 1 268 ? 237.986 245.103 231.374 1.00 6.99   ? 268  PHE A CG  1 
ATOM   1859 C CD1 . PHE A 1 268 ? 238.879 244.363 230.623 1.00 6.62   ? 268  PHE A CD1 1 
ATOM   1860 C CD2 . PHE A 1 268 ? 238.409 246.299 231.896 1.00 6.96   ? 268  PHE A CD2 1 
ATOM   1861 C CE1 . PHE A 1 268 ? 240.166 244.810 230.422 1.00 6.71   ? 268  PHE A CE1 1 
ATOM   1862 C CE2 . PHE A 1 268 ? 239.681 246.747 231.687 1.00 7.32   ? 268  PHE A CE2 1 
ATOM   1863 C CZ  . PHE A 1 268 ? 240.565 246.003 230.953 1.00 6.34   ? 268  PHE A CZ  1 
ATOM   1864 N N   . LEU A 1 269 ? 235.096 243.609 234.290 1.00 9.24   ? 269  LEU A N   1 
ATOM   1865 C CA  . LEU A 1 269 ? 233.851 243.794 235.021 1.00 9.77   ? 269  LEU A CA  1 
ATOM   1866 C C   . LEU A 1 269 ? 233.575 245.287 235.138 1.00 9.69   ? 269  LEU A C   1 
ATOM   1867 O O   . LEU A 1 269 ? 234.361 246.022 235.738 1.00 9.44   ? 269  LEU A O   1 
ATOM   1868 C CB  . LEU A 1 269 ? 233.943 243.148 236.413 1.00 10.36  ? 269  LEU A CB  1 
ATOM   1869 C CG  . LEU A 1 269 ? 232.674 243.222 237.297 1.00 10.72  ? 269  LEU A CG  1 
ATOM   1870 C CD1 . LEU A 1 269 ? 231.551 242.405 236.650 1.00 11.04  ? 269  LEU A CD1 1 
ATOM   1871 C CD2 . LEU A 1 269 ? 232.999 242.691 238.691 1.00 13.51  ? 269  LEU A CD2 1 
ATOM   1872 N N   . LEU A 1 270 ? 232.495 245.745 234.515 1.00 10.23  ? 270  LEU A N   1 
ATOM   1873 C CA  . LEU A 1 270 ? 232.187 247.171 234.456 1.00 10.57  ? 270  LEU A CA  1 
ATOM   1874 C C   . LEU A 1 270 ? 231.092 247.549 235.440 1.00 10.81  ? 270  LEU A C   1 
ATOM   1875 O O   . LEU A 1 270 ? 230.039 246.911 235.492 1.00 12.71  ? 270  LEU A O   1 
ATOM   1876 C CB  . LEU A 1 270 ? 231.752 247.556 233.037 1.00 10.64  ? 270  LEU A CB  1 
ATOM   1877 C CG  . LEU A 1 270 ? 232.746 247.227 231.907 1.00 8.87   ? 270  LEU A CG  1 
ATOM   1878 C CD1 . LEU A 1 270 ? 232.114 247.581 230.576 1.00 10.47  ? 270  LEU A CD1 1 
ATOM   1879 C CD2 . LEU A 1 270 ? 234.039 248.003 232.113 1.00 9.77   ? 270  LEU A CD2 1 
ATOM   1880 N N   . LYS A 1 271 ? 231.340 248.597 236.215 1.00 11.46  ? 271  LYS A N   1 
ATOM   1881 C CA  . LYS A 1 271 ? 230.379 249.052 237.210 1.00 12.51  ? 271  LYS A CA  1 
ATOM   1882 C C   . LYS A 1 271 ? 229.552 250.236 236.726 1.00 11.76  ? 271  LYS A C   1 
ATOM   1883 O O   . LYS A 1 271 ? 230.067 251.346 236.588 1.00 13.73  ? 271  LYS A O   1 
ATOM   1884 C CB  . LYS A 1 271 ? 231.108 249.422 238.503 1.00 11.81  ? 271  LYS A CB  1 
ATOM   1885 C CG  . LYS A 1 271 ? 230.206 249.892 239.635 1.00 12.49  ? 271  LYS A CG  1 
ATOM   1886 C CD  . LYS A 1 271 ? 231.011 250.167 240.897 1.00 11.06  ? 271  LYS A CD  1 
ATOM   1887 C CE  . LYS A 1 271 ? 230.122 250.637 242.035 1.00 11.73  ? 271  LYS A CE  1 
ATOM   1888 N NZ  . LYS A 1 271 ? 230.904 250.898 243.273 1.00 12.24  ? 271  LYS A NZ  1 
ATOM   1889 N N   . TYR A 1 272 ? 228.261 250.000 236.498 1.00 13.86  ? 272  TYR A N   1 
ATOM   1890 C CA  . TYR A 1 272 ? 227.340 251.050 236.072 1.00 13.31  ? 272  TYR A CA  1 
ATOM   1891 C C   . TYR A 1 272 ? 226.631 251.639 237.286 1.00 14.11  ? 272  TYR A C   1 
ATOM   1892 O O   . TYR A 1 272 ? 226.005 250.912 238.059 1.00 13.98  ? 272  TYR A O   1 
ATOM   1893 C CB  . TYR A 1 272 ? 226.298 250.499 235.095 1.00 13.81  ? 272  TYR A CB  1 
ATOM   1894 C CG  . TYR A 1 272 ? 226.829 250.142 233.730 1.00 13.98  ? 272  TYR A CG  1 
ATOM   1895 C CD1 . TYR A 1 272 ? 227.387 248.900 233.503 1.00 13.58  ? 272  TYR A CD1 1 
ATOM   1896 C CD2 . TYR A 1 272 ? 226.734 251.054 232.698 1.00 13.37  ? 272  TYR A CD2 1 
ATOM   1897 C CE1 . TYR A 1 272 ? 227.854 248.578 232.248 1.00 13.80  ? 272  TYR A CE1 1 
ATOM   1898 C CE2 . TYR A 1 272 ? 227.199 250.729 231.445 1.00 13.54  ? 272  TYR A CE2 1 
ATOM   1899 C CZ  . TYR A 1 272 ? 227.757 249.496 231.220 1.00 14.00  ? 272  TYR A CZ  1 
ATOM   1900 O OH  . TYR A 1 272 ? 228.222 249.167 229.970 1.00 14.02  ? 272  TYR A OH  1 
ATOM   1901 N N   . ASN A 1 273 ? 226.709 252.956 237.444 1.00 13.80  ? 273  ASN A N   1 
ATOM   1902 C CA  . ASN A 1 273 ? 226.086 253.613 238.586 1.00 13.93  ? 273  ASN A CA  1 
ATOM   1903 C C   . ASN A 1 273 ? 224.606 253.854 238.330 1.00 16.03  ? 273  ASN A C   1 
ATOM   1904 O O   . ASN A 1 273 ? 224.045 253.359 237.350 1.00 14.42  ? 273  ASN A O   1 
ATOM   1905 C CB  . ASN A 1 273 ? 226.790 254.915 238.932 1.00 15.14  ? 273  ASN A CB  1 
ATOM   1906 C CG  . ASN A 1 273 ? 226.564 256.006 237.921 1.00 13.80  ? 273  ASN A CG  1 
ATOM   1907 O OD1 . ASN A 1 273 ? 225.820 255.830 236.949 1.00 14.86  ? 273  ASN A OD1 1 
ATOM   1908 N ND2 . ASN A 1 273 ? 227.174 257.142 238.146 1.00 14.59  ? 273  ASN A ND2 1 
ATOM   1909 N N   . GLU A 1 274 ? 223.968 254.591 239.227 1.00 15.89  ? 274  GLU A N   1 
ATOM   1910 C CA  . GLU A 1 274 ? 222.531 254.836 239.147 1.00 16.32  ? 274  GLU A CA  1 
ATOM   1911 C C   . GLU A 1 274 ? 222.096 255.526 237.844 1.00 15.83  ? 274  GLU A C   1 
ATOM   1912 O O   . GLU A 1 274 ? 221.001 255.261 237.346 1.00 15.32  ? 274  GLU A O   1 
ATOM   1913 C CB  . GLU A 1 274 ? 222.080 255.670 240.350 1.00 16.58  ? 274  GLU A CB  1 
ATOM   1914 C CG  . GLU A 1 274 ? 222.205 254.951 241.694 1.00 17.11  ? 274  GLU A CG  1 
ATOM   1915 C CD  . GLU A 1 274 ? 223.596 255.007 242.272 1.00 17.78  ? 274  GLU A CD  1 
ATOM   1916 O OE1 . GLU A 1 274 ? 224.448 255.603 241.658 1.00 17.17  ? 274  GLU A OE1 1 
ATOM   1917 O OE2 . GLU A 1 274 ? 223.806 254.451 243.322 1.00 19.16  ? 274  GLU A OE2 1 
ATOM   1918 N N   . ASN A 1 275 ? 222.953 256.397 237.301 1.00 16.21  ? 275  ASN A N   1 
ATOM   1919 C CA  . ASN A 1 275 ? 222.644 257.166 236.085 1.00 16.23  ? 275  ASN A CA  1 
ATOM   1920 C C   . ASN A 1 275 ? 223.153 256.460 234.807 1.00 15.54  ? 275  ASN A C   1 
ATOM   1921 O O   . ASN A 1 275 ? 223.098 257.034 233.731 1.00 14.87  ? 275  ASN A O   1 
ATOM   1922 C CB  . ASN A 1 275 ? 223.219 258.571 236.184 1.00 17.24  ? 275  ASN A CB  1 
ATOM   1923 C CG  . ASN A 1 275 ? 222.553 259.423 237.267 1.00 17.58  ? 275  ASN A CG  1 
ATOM   1924 O OD1 . ASN A 1 275 ? 221.584 258.996 237.910 1.00 18.61  ? 275  ASN A OD1 1 
ATOM   1925 N ND2 . ASN A 1 275 ? 223.071 260.617 237.462 1.00 20.48  ? 275  ASN A ND2 1 
ATOM   1926 N N   . GLY A 1 276 ? 223.627 255.212 234.946 1.00 13.76  ? 276  GLY A N   1 
ATOM   1927 C CA  . GLY A 1 276 ? 224.071 254.401 233.808 1.00 13.30  ? 276  GLY A CA  1 
ATOM   1928 C C   . GLY A 1 276 ? 225.455 254.777 233.287 1.00 13.51  ? 276  GLY A C   1 
ATOM   1929 O O   . GLY A 1 276 ? 225.783 254.518 232.128 1.00 12.87  ? 276  GLY A O   1 
ATOM   1930 N N   . THR A 1 277 ? 226.266 255.381 234.139 1.00 12.82  ? 277  THR A N   1 
ATOM   1931 C CA  . THR A 1 277 ? 227.618 255.763 233.769 1.00 12.11  ? 277  THR A CA  1 
ATOM   1932 C C   . THR A 1 277 ? 228.607 254.783 234.371 1.00 10.54  ? 277  THR A C   1 
ATOM   1933 O O   . THR A 1 277 ? 228.454 254.372 235.522 1.00 15.33  ? 277  THR A O   1 
ATOM   1934 C CB  . THR A 1 277 ? 227.932 257.198 234.226 1.00 12.34  ? 277  THR A CB  1 
ATOM   1935 O OG1 . THR A 1 277 ? 227.057 258.110 233.548 1.00 12.67  ? 277  THR A OG1 1 
ATOM   1936 C CG2 . THR A 1 277 ? 229.376 257.567 233.925 1.00 12.70  ? 277  THR A CG2 1 
ATOM   1937 N N   . ILE A 1 278 ? 229.611 254.388 233.601 1.00 11.03  ? 278  ILE A N   1 
ATOM   1938 C CA  . ILE A 1 278 ? 230.613 253.478 234.132 1.00 10.68  ? 278  ILE A CA  1 
ATOM   1939 C C   . ILE A 1 278 ? 231.554 254.268 235.029 1.00 10.32  ? 278  ILE A C   1 
ATOM   1940 O O   . ILE A 1 278 ? 232.144 255.259 234.600 1.00 10.07  ? 278  ILE A O   1 
ATOM   1941 C CB  . ILE A 1 278 ? 231.413 252.796 233.008 1.00 9.46   ? 278  ILE A CB  1 
ATOM   1942 C CG1 . ILE A 1 278 ? 230.481 252.022 232.088 1.00 10.60  ? 278  ILE A CG1 1 
ATOM   1943 C CG2 . ILE A 1 278 ? 232.421 251.841 233.620 1.00 9.75   ? 278  ILE A CG2 1 
ATOM   1944 C CD1 . ILE A 1 278 ? 231.130 251.581 230.793 1.00 9.41   ? 278  ILE A CD1 1 
ATOM   1945 N N   . THR A 1 279 ? 231.664 253.858 236.286 1.00 10.00  ? 279  THR A N   1 
ATOM   1946 C CA  . THR A 1 279 ? 232.459 254.609 237.250 1.00 9.51   ? 279  THR A CA  1 
ATOM   1947 C C   . THR A 1 279 ? 233.687 253.848 237.715 1.00 9.44   ? 279  THR A C   1 
ATOM   1948 O O   . THR A 1 279 ? 234.555 254.410 238.381 1.00 9.59   ? 279  THR A O   1 
ATOM   1949 C CB  . THR A 1 279 ? 231.617 255.004 238.471 1.00 10.06  ? 279  THR A CB  1 
ATOM   1950 O OG1 . THR A 1 279 ? 231.158 253.822 239.135 1.00 11.17  ? 279  THR A OG1 1 
ATOM   1951 C CG2 . THR A 1 279 ? 230.425 255.834 238.033 1.00 11.94  ? 279  THR A CG2 1 
ATOM   1952 N N   . ASP A 1 280 ? 233.754 252.568 237.384 1.00 9.79   ? 280  ASP A N   1 
ATOM   1953 C CA  . ASP A 1 280 ? 234.894 251.750 237.771 1.00 8.96   ? 280  ASP A CA  1 
ATOM   1954 C C   . ASP A 1 280 ? 235.013 250.540 236.857 1.00 8.96   ? 280  ASP A C   1 
ATOM   1955 O O   . ASP A 1 280 ? 234.128 250.286 236.035 1.00 9.62   ? 280  ASP A O   1 
ATOM   1956 C CB  . ASP A 1 280 ? 234.744 251.299 239.230 1.00 8.98   ? 280  ASP A CB  1 
ATOM   1957 C CG  . ASP A 1 280 ? 236.068 251.033 239.933 1.00 10.05  ? 280  ASP A CG  1 
ATOM   1958 O OD1 . ASP A 1 280 ? 237.060 250.880 239.260 1.00 10.35  ? 280  ASP A OD1 1 
ATOM   1959 O OD2 . ASP A 1 280 ? 236.073 250.980 241.140 1.00 10.91  ? 280  ASP A OD2 1 
ATOM   1960 N N   . ALA A 1 281 ? 236.086 249.777 237.022 1.00 8.64   ? 281  ALA A N   1 
ATOM   1961 C CA  . ALA A 1 281 ? 236.270 248.550 236.259 1.00 8.96   ? 281  ALA A CA  1 
ATOM   1962 C C   . ALA A 1 281 ? 237.336 247.662 236.885 1.00 8.86   ? 281  ALA A C   1 
ATOM   1963 O O   . ALA A 1 281 ? 238.291 248.147 237.491 1.00 9.03   ? 281  ALA A O   1 
ATOM   1964 C CB  . ALA A 1 281 ? 236.640 248.872 234.820 1.00 8.21   ? 281  ALA A CB  1 
ATOM   1965 N N   . VAL A 1 282 ? 237.200 246.358 236.678 1.00 8.71   ? 282  VAL A N   1 
ATOM   1966 C CA  . VAL A 1 282 ? 238.213 245.403 237.106 1.00 8.76   ? 282  VAL A CA  1 
ATOM   1967 C C   . VAL A 1 282 ? 238.745 244.585 235.939 1.00 8.66   ? 282  VAL A C   1 
ATOM   1968 O O   . VAL A 1 282 ? 237.980 243.939 235.223 1.00 9.36   ? 282  VAL A O   1 
ATOM   1969 C CB  . VAL A 1 282 ? 237.635 244.447 238.170 1.00 10.00  ? 282  VAL A CB  1 
ATOM   1970 C CG1 . VAL A 1 282 ? 238.680 243.413 238.582 1.00 11.72  ? 282  VAL A CG1 1 
ATOM   1971 C CG2 . VAL A 1 282 ? 237.175 245.248 239.375 1.00 10.72  ? 282  VAL A CG2 1 
ATOM   1972 N N   . ASP A 1 283 ? 240.063 244.584 235.775 1.00 8.23   ? 283  ASP A N   1 
ATOM   1973 C CA  . ASP A 1 283 ? 240.713 243.761 234.761 1.00 8.38   ? 283  ASP A CA  1 
ATOM   1974 C C   . ASP A 1 283 ? 240.954 242.369 235.329 1.00 9.64   ? 283  ASP A C   1 
ATOM   1975 O O   . ASP A 1 283 ? 241.809 242.191 236.203 1.00 9.85   ? 283  ASP A O   1 
ATOM   1976 C CB  . ASP A 1 283 ? 242.027 244.399 234.304 1.00 7.79   ? 283  ASP A CB  1 
ATOM   1977 C CG  . ASP A 1 283 ? 242.753 243.583 233.242 1.00 7.73   ? 283  ASP A CG  1 
ATOM   1978 O OD1 . ASP A 1 283 ? 242.431 242.424 233.086 1.00 7.97   ? 283  ASP A OD1 1 
ATOM   1979 O OD2 . ASP A 1 283 ? 243.634 244.117 232.597 1.00 6.95   ? 283  ASP A OD2 1 
ATOM   1980 N N   . CYS A 1 284 ? 240.166 241.392 234.888 1.00 9.55   ? 284  CYS A N   1 
ATOM   1981 C CA  . CYS A 1 284 ? 240.088 240.065 235.480 1.00 10.87  ? 284  CYS A CA  1 
ATOM   1982 C C   . CYS A 1 284 ? 241.364 239.263 235.233 1.00 11.05  ? 284  CYS A C   1 
ATOM   1983 O O   . CYS A 1 284 ? 241.533 238.168 235.781 1.00 12.04  ? 284  CYS A O   1 
ATOM   1984 C CB  . CYS A 1 284 ? 238.894 239.287 234.926 1.00 10.43  ? 284  CYS A CB  1 
ATOM   1985 S SG  . CYS A 1 284 ? 237.281 240.080 235.205 1.00 11.15  ? 284  CYS A SG  1 
ATOM   1986 N N   . ALA A 1 285 ? 242.238 239.765 234.371 1.00 9.66   ? 285  ALA A N   1 
ATOM   1987 C CA  . ALA A 1 285 ? 243.467 239.053 234.036 1.00 9.27   ? 285  ALA A CA  1 
ATOM   1988 C C   . ALA A 1 285 ? 244.687 239.715 234.664 1.00 9.81   ? 285  ALA A C   1 
ATOM   1989 O O   . ALA A 1 285 ? 245.821 239.312 234.405 1.00 9.55   ? 285  ALA A O   1 
ATOM   1990 C CB  . ALA A 1 285 ? 243.632 238.984 232.529 1.00 8.23   ? 285  ALA A CB  1 
ATOM   1991 N N   . LEU A 1 286 ? 244.456 240.740 235.474 1.00 10.29  ? 286  LEU A N   1 
ATOM   1992 C CA  . LEU A 1 286 ? 245.540 241.503 236.080 1.00 11.11  ? 286  LEU A CA  1 
ATOM   1993 C C   . LEU A 1 286 ? 246.288 240.722 237.155 1.00 12.82  ? 286  LEU A C   1 
ATOM   1994 O O   . LEU A 1 286 ? 247.514 240.798 237.245 1.00 13.82  ? 286  LEU A O   1 
ATOM   1995 C CB  . LEU A 1 286 ? 244.980 242.793 236.686 1.00 10.41  ? 286  LEU A CB  1 
ATOM   1996 C CG  . LEU A 1 286 ? 245.984 243.722 237.367 1.00 9.63   ? 286  LEU A CG  1 
ATOM   1997 C CD1 . LEU A 1 286 ? 247.038 244.167 236.371 1.00 9.09   ? 286  LEU A CD1 1 
ATOM   1998 C CD2 . LEU A 1 286 ? 245.238 244.909 237.932 1.00 10.98  ? 286  LEU A CD2 1 
ATOM   1999 N N   . ASP A 1 287 ? 245.547 239.996 237.986 1.00 12.81  ? 287  ASP A N   1 
ATOM   2000 C CA  . ASP A 1 287 ? 246.122 239.290 239.126 1.00 14.17  ? 287  ASP A CA  1 
ATOM   2001 C C   . ASP A 1 287 ? 245.047 238.446 239.833 1.00 14.89  ? 287  ASP A C   1 
ATOM   2002 O O   . ASP A 1 287 ? 243.857 238.640 239.582 1.00 16.61  ? 287  ASP A O   1 
ATOM   2003 C CB  . ASP A 1 287 ? 246.764 240.312 240.087 1.00 14.60  ? 287  ASP A CB  1 
ATOM   2004 C CG  . ASP A 1 287 ? 245.812 241.412 240.546 1.00 14.39  ? 287  ASP A CG  1 
ATOM   2005 O OD1 . ASP A 1 287 ? 244.623 241.193 240.529 1.00 14.95  ? 287  ASP A OD1 1 
ATOM   2006 O OD2 . ASP A 1 287 ? 246.285 242.457 240.925 1.00 13.97  ? 287  ASP A OD2 1 
ATOM   2007 N N   . PRO A 1 288 ? 245.445 237.492 240.694 1.00 14.66  ? 288  PRO A N   1 
ATOM   2008 C CA  . PRO A 1 288 ? 244.593 236.657 241.533 1.00 16.05  ? 288  PRO A CA  1 
ATOM   2009 C C   . PRO A 1 288 ? 243.558 237.439 242.338 1.00 15.22  ? 288  PRO A C   1 
ATOM   2010 O O   . PRO A 1 288 ? 242.444 236.956 242.555 1.00 16.58  ? 288  PRO A O   1 
ATOM   2011 C CB  . PRO A 1 288 ? 245.619 235.975 242.440 1.00 14.98  ? 288  PRO A CB  1 
ATOM   2012 C CG  . PRO A 1 288 ? 246.856 235.868 241.582 1.00 15.20  ? 288  PRO A CG  1 
ATOM   2013 C CD  . PRO A 1 288 ? 246.882 237.148 240.785 1.00 15.79  ? 288  PRO A CD  1 
ATOM   2014 N N   . LEU A 1 289 ? 243.907 238.645 242.777 1.00 16.21  ? 289  LEU A N   1 
ATOM   2015 C CA  . LEU A 1 289 ? 242.958 239.456 243.528 1.00 16.23  ? 289  LEU A CA  1 
ATOM   2016 C C   . LEU A 1 289 ? 241.803 239.896 242.639 1.00 17.46  ? 289  LEU A C   1 
ATOM   2017 O O   . LEU A 1 289 ? 240.637 239.815 243.031 1.00 17.93  ? 289  LEU A O   1 
ATOM   2018 C CB  . LEU A 1 289 ? 243.656 240.682 244.130 1.00 16.02  ? 289  LEU A CB  1 
ATOM   2019 C CG  . LEU A 1 289 ? 242.753 241.662 244.911 1.00 17.58  ? 289  LEU A CG  1 
ATOM   2020 C CD1 . LEU A 1 289 ? 242.092 240.944 246.084 1.00 17.92  ? 289  LEU A CD1 1 
ATOM   2021 C CD2 . LEU A 1 289 ? 243.593 242.832 245.398 1.00 18.77  ? 289  LEU A CD2 1 
ATOM   2022 N N   . SER A 1 290 ? 242.130 240.340 241.430 1.00 16.15  ? 290  SER A N   1 
ATOM   2023 C CA  . SER A 1 290 ? 241.112 240.766 240.481 1.00 14.83  ? 290  SER A CA  1 
ATOM   2024 C C   . SER A 1 290 ? 240.269 239.582 240.031 1.00 12.83  ? 290  SER A C   1 
ATOM   2025 O O   . SER A 1 290 ? 239.058 239.706 239.847 1.00 17.04  ? 290  SER A O   1 
ATOM   2026 C CB  . SER A 1 290 ? 241.759 241.435 239.289 1.00 14.33  ? 290  SER A CB  1 
ATOM   2027 O OG  . SER A 1 290 ? 242.386 242.629 239.670 1.00 13.62  ? 290  SER A OG  1 
ATOM   2028 N N   . GLU A 1 291 ? 240.902 238.418 239.899 1.00 13.14  ? 291  GLU A N   1 
ATOM   2029 C CA  . GLU A 1 291 ? 240.178 237.213 239.519 1.00 14.45  ? 291  GLU A CA  1 
ATOM   2030 C C   . GLU A 1 291 ? 239.113 236.887 240.559 1.00 18.81  ? 291  GLU A C   1 
ATOM   2031 O O   . GLU A 1 291 ? 237.984 236.532 240.214 1.00 17.28  ? 291  GLU A O   1 
ATOM   2032 C CB  . GLU A 1 291 ? 241.133 236.028 239.379 1.00 16.92  ? 291  GLU A CB  1 
ATOM   2033 C CG  . GLU A 1 291 ? 242.067 236.102 238.181 1.00 15.73  ? 291  GLU A CG  1 
ATOM   2034 C CD  . GLU A 1 291 ? 243.090 234.993 238.172 1.00 16.12  ? 291  GLU A CD  1 
ATOM   2035 O OE1 . GLU A 1 291 ? 243.125 234.243 239.117 1.00 16.58  ? 291  GLU A OE1 1 
ATOM   2036 O OE2 . GLU A 1 291 ? 243.837 234.898 237.225 1.00 14.38  ? 291  GLU A OE2 1 
ATOM   2037 N N   . THR A 1 292 ? 239.466 237.050 241.835 1.00 18.40  ? 292  THR A N   1 
ATOM   2038 C CA  . THR A 1 292 ? 238.526 236.819 242.924 1.00 17.07  ? 292  THR A CA  1 
ATOM   2039 C C   . THR A 1 292 ? 237.364 237.802 242.852 1.00 15.40  ? 292  THR A C   1 
ATOM   2040 O O   . THR A 1 292 ? 236.205 237.411 242.988 1.00 19.18  ? 292  THR A O   1 
ATOM   2041 C CB  . THR A 1 292 ? 239.220 236.936 244.295 1.00 17.37  ? 292  THR A CB  1 
ATOM   2042 O OG1 . THR A 1 292 ? 240.246 235.937 244.399 1.00 17.50  ? 292  THR A OG1 1 
ATOM   2043 C CG2 . THR A 1 292 ? 238.210 236.738 245.417 1.00 19.43  ? 292  THR A CG2 1 
ATOM   2044 N N   . LYS A 1 293 ? 237.676 239.077 242.622 1.00 17.24  ? 293  LYS A N   1 
ATOM   2045 C CA  . LYS A 1 293 ? 236.641 240.103 242.513 1.00 17.50  ? 293  LYS A CA  1 
ATOM   2046 C C   . LYS A 1 293 ? 235.672 239.833 241.358 1.00 15.23  ? 293  LYS A C   1 
ATOM   2047 O O   . LYS A 1 293 ? 234.461 240.015 241.511 1.00 19.47  ? 293  LYS A O   1 
ATOM   2048 C CB  . LYS A 1 293 ? 237.272 241.488 242.345 1.00 17.13  ? 293  LYS A CB  1 
ATOM   2049 C CG  . LYS A 1 293 ? 237.942 242.033 243.595 1.00 17.14  ? 293  LYS A CG  1 
ATOM   2050 C CD  . LYS A 1 293 ? 238.555 243.404 243.340 1.00 16.87  ? 293  LYS A CD  1 
ATOM   2051 C CE  . LYS A 1 293 ? 239.228 243.953 244.586 1.00 19.21  ? 293  LYS A CE  1 
ATOM   2052 N NZ  . LYS A 1 293 ? 239.856 245.281 244.337 1.00 18.30  ? 293  LYS A NZ  1 
ATOM   2053 N N   . CYS A 1 294 ? 236.202 239.391 240.208 1.00 17.73  ? 294  CYS A N   1 
ATOM   2054 C CA  . CYS A 1 294 ? 235.399 239.077 239.024 1.00 17.89  ? 294  CYS A CA  1 
ATOM   2055 C C   . CYS A 1 294 ? 234.532 237.838 239.251 1.00 17.72  ? 294  CYS A C   1 
ATOM   2056 O O   . CYS A 1 294 ? 233.385 237.779 238.796 1.00 18.55  ? 294  CYS A O   1 
ATOM   2057 C CB  . CYS A 1 294 ? 236.302 238.866 237.798 1.00 17.46  ? 294  CYS A CB  1 
ATOM   2058 S SG  . CYS A 1 294 ? 237.108 240.385 237.200 1.00 14.52  ? 294  CYS A SG  1 
ATOM   2059 N N   . THR A 1 295 ? 235.078 236.857 239.963 1.00 18.08  ? 295  THR A N   1 
ATOM   2060 C CA  . THR A 1 295 ? 234.354 235.627 240.271 1.00 18.05  ? 295  THR A CA  1 
ATOM   2061 C C   . THR A 1 295 ? 233.175 235.892 241.200 1.00 19.03  ? 295  THR A C   1 
ATOM   2062 O O   . THR A 1 295 ? 232.082 235.364 240.996 1.00 19.35  ? 295  THR A O   1 
ATOM   2063 C CB  . THR A 1 295 ? 235.283 234.585 240.920 1.00 19.10  ? 295  THR A CB  1 
ATOM   2064 O OG1 . THR A 1 295 ? 236.336 234.249 240.007 1.00 19.03  ? 295  THR A OG1 1 
ATOM   2065 C CG2 . THR A 1 295 ? 234.504 233.329 241.277 1.00 19.56  ? 295  THR A CG2 1 
ATOM   2066 N N   . LEU A 1 296 ? 233.403 236.712 242.221 1.00 19.44  ? 296  LEU A N   1 
ATOM   2067 C CA  . LEU A 1 296 ? 232.391 236.996 243.231 1.00 19.68  ? 296  LEU A CA  1 
ATOM   2068 C C   . LEU A 1 296 ? 231.548 238.213 242.871 1.00 19.48  ? 296  LEU A C   1 
ATOM   2069 O O   . LEU A 1 296 ? 230.679 238.622 243.640 1.00 19.62  ? 296  LEU A O   1 
ATOM   2070 C CB  . LEU A 1 296 ? 233.064 237.239 244.586 1.00 20.15  ? 296  LEU A CB  1 
ATOM   2071 C CG  . LEU A 1 296 ? 233.923 236.085 245.138 1.00 20.42  ? 296  LEU A CG  1 
ATOM   2072 C CD1 . LEU A 1 296 ? 234.611 236.551 246.410 1.00 19.83  ? 296  LEU A CD1 1 
ATOM   2073 C CD2 . LEU A 1 296 ? 233.051 234.865 245.410 1.00 21.29  ? 296  LEU A CD2 1 
ATOM   2074 N N   . LYS A 1 297 ? 231.830 238.810 241.720 1.00 19.11  ? 297  LYS A N   1 
ATOM   2075 C CA  . LYS A 1 297 ? 231.137 240.018 241.274 1.00 19.25  ? 297  LYS A CA  1 
ATOM   2076 C C   . LYS A 1 297 ? 231.155 241.114 242.341 1.00 19.31  ? 297  LYS A C   1 
ATOM   2077 O O   . LYS A 1 297 ? 230.112 241.675 242.680 1.00 18.51  ? 297  LYS A O   1 
ATOM   2078 C CB  . LYS A 1 297 ? 229.694 239.693 240.876 1.00 18.27  ? 297  LYS A CB  1 
ATOM   2079 C CG  . LYS A 1 297 ? 229.568 238.589 239.835 1.00 18.85  ? 297  LYS A CG  1 
ATOM   2080 C CD  . LYS A 1 297 ? 230.147 239.019 238.490 1.00 18.70  ? 297  LYS A CD  1 
ATOM   2081 C CE  . LYS A 1 297 ? 230.073 237.900 237.460 1.00 18.40  ? 297  LYS A CE  1 
ATOM   2082 N NZ  . LYS A 1 297 ? 230.856 236.709 237.891 1.00 19.79  ? 297  LYS A NZ  1 
ATOM   2083 N N   . SER A 1 298 ? 232.351 241.407 242.866 1.00 19.39  ? 298  SER A N   1 
ATOM   2084 C CA  . SER A 1 298 ? 232.562 242.425 243.894 1.00 19.76  ? 298  SER A CA  1 
ATOM   2085 C C   . SER A 1 298 ? 233.342 243.606 243.307 1.00 18.69  ? 298  SER A C   1 
ATOM   2086 O O   . SER A 1 298 ? 234.396 244.004 243.813 1.00 19.43  ? 298  SER A O   1 
ATOM   2087 C CB  . SER A 1 298 ? 233.283 241.812 245.092 1.00 20.36  ? 298  SER A CB  1 
ATOM   2088 O OG  . SER A 1 298 ? 233.523 242.765 246.089 1.00 22.31  ? 298  SER A OG  1 
ATOM   2089 N N   . GLU B 2 1   ? 271.524 252.714 217.932 1.00 11.63  ? 1    GLU B N   1 
ATOM   2090 C CA  . GLU B 2 1   ? 270.792 252.693 219.198 1.00 11.81  ? 1    GLU B CA  1 
ATOM   2091 C C   . GLU B 2 1   ? 269.948 251.424 219.366 1.00 10.86  ? 1    GLU B C   1 
ATOM   2092 O O   . GLU B 2 1   ? 269.731 250.971 220.492 1.00 10.54  ? 1    GLU B O   1 
ATOM   2093 C CB  . GLU B 2 1   ? 269.897 253.941 219.327 1.00 13.16  ? 1    GLU B CB  1 
ATOM   2094 N N   . VAL B 2 2   ? 269.471 250.859 218.250 1.00 10.45  ? 2    VAL B N   1 
ATOM   2095 C CA  . VAL B 2 2   ? 268.673 249.632 218.261 1.00 10.07  ? 2    VAL B CA  1 
ATOM   2096 C C   . VAL B 2 2   ? 269.565 248.402 218.249 1.00 9.81   ? 2    VAL B C   1 
ATOM   2097 O O   . VAL B 2 2   ? 270.416 248.250 217.374 1.00 9.93   ? 2    VAL B O   1 
ATOM   2098 C CB  . VAL B 2 2   ? 267.724 249.591 217.052 1.00 9.42   ? 2    VAL B CB  1 
ATOM   2099 C CG1 . VAL B 2 2   ? 266.985 248.267 217.019 1.00 8.70   ? 2    VAL B CG1 1 
ATOM   2100 C CG2 . VAL B 2 2   ? 266.736 250.741 217.149 1.00 9.59   ? 2    VAL B CG2 1 
ATOM   2101 N N   . GLN B 2 3   ? 269.364 247.526 219.226 1.00 9.42   ? 3    GLN B N   1 
ATOM   2102 C CA  . GLN B 2 3   ? 270.186 246.334 219.358 1.00 9.59   ? 3    GLN B CA  1 
ATOM   2103 C C   . GLN B 2 3   ? 269.359 245.072 219.551 1.00 9.13   ? 3    GLN B C   1 
ATOM   2104 O O   . GLN B 2 3   ? 268.335 245.075 220.237 1.00 9.09   ? 3    GLN B O   1 
ATOM   2105 C CB  . GLN B 2 3   ? 271.151 246.482 220.538 1.00 9.38   ? 3    GLN B CB  1 
ATOM   2106 C CG  . GLN B 2 3   ? 272.158 247.609 220.399 1.00 9.82   ? 3    GLN B CG  1 
ATOM   2107 C CD  . GLN B 2 3   ? 273.226 247.301 219.373 1.00 10.05  ? 3    GLN B CD  1 
ATOM   2108 O OE1 . GLN B 2 3   ? 273.595 246.140 219.175 1.00 9.20   ? 3    GLN B OE1 1 
ATOM   2109 N NE2 . GLN B 2 3   ? 273.732 248.335 218.715 1.00 10.15  ? 3    GLN B NE2 1 
ATOM   2110 N N   . LEU B 2 4   ? 269.860 243.982 218.987 1.00 9.39   ? 4    LEU B N   1 
ATOM   2111 C CA  . LEU B 2 4   ? 269.341 242.643 219.225 1.00 9.41   ? 4    LEU B CA  1 
ATOM   2112 C C   . LEU B 2 4   ? 270.518 241.704 219.453 1.00 9.35   ? 4    LEU B C   1 
ATOM   2113 O O   . LEU B 2 4   ? 271.383 241.568 218.588 1.00 9.25   ? 4    LEU B O   1 
ATOM   2114 C CB  . LEU B 2 4   ? 268.509 242.164 218.025 1.00 9.38   ? 4    LEU B CB  1 
ATOM   2115 C CG  . LEU B 2 4   ? 267.163 242.863 217.782 1.00 8.90   ? 4    LEU B CG  1 
ATOM   2116 C CD1 . LEU B 2 4   ? 266.622 242.447 216.416 1.00 8.90   ? 4    LEU B CD1 1 
ATOM   2117 C CD2 . LEU B 2 4   ? 266.187 242.469 218.874 1.00 9.81   ? 4    LEU B CD2 1 
ATOM   2118 N N   . VAL B 2 5   ? 270.585 241.098 220.631 1.00 9.40   ? 5    VAL B N   1 
ATOM   2119 C CA  . VAL B 2 5   ? 271.738 240.268 220.964 1.00 9.79   ? 5    VAL B CA  1 
ATOM   2120 C C   . VAL B 2 5   ? 271.359 238.841 221.327 1.00 9.51   ? 5    VAL B C   1 
ATOM   2121 O O   . VAL B 2 5   ? 270.721 238.600 222.352 1.00 9.71   ? 5    VAL B O   1 
ATOM   2122 C CB  . VAL B 2 5   ? 272.514 240.898 222.135 1.00 8.85   ? 5    VAL B CB  1 
ATOM   2123 C CG1 . VAL B 2 5   ? 273.713 240.035 222.495 1.00 10.23  ? 5    VAL B CG1 1 
ATOM   2124 C CG2 . VAL B 2 5   ? 272.958 242.302 221.746 1.00 9.56   ? 5    VAL B CG2 1 
ATOM   2125 N N   . GLU B 2 6   ? 271.793 237.896 220.498 1.00 9.85   ? 6    GLU B N   1 
ATOM   2126 C CA  . GLU B 2 6   ? 271.538 236.482 220.732 1.00 10.29  ? 6    GLU B CA  1 
ATOM   2127 C C   . GLU B 2 6   ? 272.557 235.878 221.686 1.00 10.48  ? 6    GLU B C   1 
ATOM   2128 O O   . GLU B 2 6   ? 273.732 236.248 221.675 1.00 10.39  ? 6    GLU B O   1 
ATOM   2129 C CB  . GLU B 2 6   ? 271.561 235.702 219.419 1.00 10.23  ? 6    GLU B CB  1 
ATOM   2130 C CG  . GLU B 2 6   ? 270.519 236.127 218.419 1.00 9.90   ? 6    GLU B CG  1 
ATOM   2131 C CD  . GLU B 2 6   ? 270.989 237.224 217.517 1.00 9.45   ? 6    GLU B CD  1 
ATOM   2132 O OE1 . GLU B 2 6   ? 272.012 237.813 217.793 1.00 10.01  ? 6    GLU B OE1 1 
ATOM   2133 O OE2 . GLU B 2 6   ? 270.337 237.464 216.533 1.00 9.81   ? 6    GLU B OE2 1 
ATOM   2134 N N   . SER B 2 7   ? 272.114 234.896 222.458 1.00 10.55  ? 7    SER B N   1 
ATOM   2135 C CA  . SER B 2 7   ? 272.992 234.138 223.337 1.00 10.97  ? 7    SER B CA  1 
ATOM   2136 C C   . SER B 2 7   ? 272.426 232.748 223.598 1.00 11.11  ? 7    SER B C   1 
ATOM   2137 O O   . SER B 2 7   ? 271.263 232.474 223.297 1.00 11.04  ? 7    SER B O   1 
ATOM   2138 C CB  . SER B 2 7   ? 273.191 234.878 224.646 1.00 10.79  ? 7    SER B CB  1 
ATOM   2139 O OG  . SER B 2 7   ? 271.990 234.967 225.363 1.00 11.53  ? 7    SER B OG  1 
ATOM   2140 N N   . GLY B 2 8   ? 273.246 231.872 224.174 1.00 11.91  ? 8    GLY B N   1 
ATOM   2141 C CA  . GLY B 2 8   ? 272.794 230.527 224.518 1.00 11.48  ? 8    GLY B CA  1 
ATOM   2142 C C   . GLY B 2 8   ? 273.223 229.481 223.493 1.00 12.43  ? 8    GLY B C   1 
ATOM   2143 O O   . GLY B 2 8   ? 272.754 228.345 223.526 1.00 12.26  ? 8    GLY B O   1 
ATOM   2144 N N   . GLY B 2 9   ? 274.124 229.854 222.593 1.00 12.27  ? 9    GLY B N   1 
ATOM   2145 C CA  . GLY B 2 9   ? 274.610 228.916 221.586 1.00 12.99  ? 9    GLY B CA  1 
ATOM   2146 C C   . GLY B 2 9   ? 275.615 227.957 222.210 1.00 13.72  ? 9    GLY B C   1 
ATOM   2147 O O   . GLY B 2 9   ? 275.817 227.968 223.424 1.00 14.40  ? 9    GLY B O   1 
ATOM   2148 N N   . GLY B 2 10  ? 276.227 227.110 221.388 1.00 13.59  ? 10   GLY B N   1 
ATOM   2149 C CA  . GLY B 2 10  ? 277.157 226.113 221.909 1.00 14.14  ? 10   GLY B CA  1 
ATOM   2150 C C   . GLY B 2 10  ? 277.029 224.777 221.187 1.00 14.96  ? 10   GLY B C   1 
ATOM   2151 O O   . GLY B 2 10  ? 276.467 224.702 220.092 1.00 14.92  ? 10   GLY B O   1 
ATOM   2152 N N   . VAL B 2 11  ? 277.583 223.730 221.794 1.00 15.40  ? 11   VAL B N   1 
ATOM   2153 C CA  . VAL B 2 11  ? 277.592 222.405 221.185 1.00 15.87  ? 11   VAL B CA  1 
ATOM   2154 C C   . VAL B 2 11  ? 276.768 221.419 222.004 1.00 16.53  ? 11   VAL B C   1 
ATOM   2155 O O   . VAL B 2 11  ? 276.967 221.281 223.210 1.00 17.63  ? 11   VAL B O   1 
ATOM   2156 C CB  . VAL B 2 11  ? 279.033 221.874 221.064 1.00 15.73  ? 11   VAL B CB  1 
ATOM   2157 C CG1 . VAL B 2 11  ? 279.030 220.499 220.394 1.00 15.49  ? 11   VAL B CG1 1 
ATOM   2158 C CG2 . VAL B 2 11  ? 279.881 222.862 220.275 1.00 16.84  ? 11   VAL B CG2 1 
ATOM   2159 N N   . VAL B 2 12  ? 275.846 220.735 221.338 1.00 16.86  ? 12   VAL B N   1 
ATOM   2160 C CA  . VAL B 2 12  ? 274.993 219.750 221.991 1.00 16.59  ? 12   VAL B CA  1 
ATOM   2161 C C   . VAL B 2 12  ? 275.029 218.417 221.258 1.00 15.33  ? 12   VAL B C   1 
ATOM   2162 O O   . VAL B 2 12  ? 275.470 218.342 220.111 1.00 17.86  ? 12   VAL B O   1 
ATOM   2163 C CB  . VAL B 2 12  ? 273.542 220.254 222.064 1.00 17.18  ? 12   VAL B CB  1 
ATOM   2164 C CG1 . VAL B 2 12  ? 273.474 221.546 222.860 1.00 16.92  ? 12   VAL B CG1 1 
ATOM   2165 C CG2 . VAL B 2 12  ? 273.009 220.465 220.667 1.00 16.53  ? 12   VAL B CG2 1 
ATOM   2166 N N   . GLN B 2 13  ? 274.543 217.370 221.913 1.00 16.88  ? 13   GLN B N   1 
ATOM   2167 C CA  . GLN B 2 13  ? 274.474 216.053 221.295 1.00 17.68  ? 13   GLN B CA  1 
ATOM   2168 C C   . GLN B 2 13  ? 273.110 215.853 220.632 1.00 17.09  ? 13   GLN B C   1 
ATOM   2169 O O   . GLN B 2 13  ? 272.128 216.458 221.061 1.00 16.53  ? 13   GLN B O   1 
ATOM   2170 C CB  . GLN B 2 13  ? 274.709 214.970 222.350 1.00 17.11  ? 13   GLN B CB  1 
ATOM   2171 C CG  . GLN B 2 13  ? 276.028 215.101 223.092 1.00 17.27  ? 13   GLN B CG  1 
ATOM   2172 C CD  . GLN B 2 13  ? 277.227 214.988 222.176 1.00 17.90  ? 13   GLN B CD  1 
ATOM   2173 O OE1 . GLN B 2 13  ? 277.352 214.028 221.412 1.00 18.16  ? 13   GLN B OE1 1 
ATOM   2174 N NE2 . GLN B 2 13  ? 278.117 215.970 222.246 1.00 16.59  ? 13   GLN B NE2 1 
ATOM   2175 N N   . PRO B 2 14  ? 273.024 215.010 219.597 1.00 17.41  ? 14   PRO B N   1 
ATOM   2176 C CA  . PRO B 2 14  ? 271.806 214.595 218.928 1.00 17.02  ? 14   PRO B CA  1 
ATOM   2177 C C   . PRO B 2 14  ? 270.793 214.061 219.923 1.00 16.87  ? 14   PRO B C   1 
ATOM   2178 O O   . PRO B 2 14  ? 271.125 213.256 220.794 1.00 17.31  ? 14   PRO B O   1 
ATOM   2179 C CB  . PRO B 2 14  ? 272.312 213.488 217.998 1.00 17.37  ? 14   PRO B CB  1 
ATOM   2180 C CG  . PRO B 2 14  ? 273.740 213.872 217.707 1.00 17.09  ? 14   PRO B CG  1 
ATOM   2181 C CD  . PRO B 2 14  ? 274.249 214.483 218.997 1.00 17.46  ? 14   PRO B CD  1 
ATOM   2182 N N   . GLY B 2 15  ? 269.553 214.514 219.788 1.00 16.72  ? 15   GLY B N   1 
ATOM   2183 C CA  . GLY B 2 15  ? 268.476 214.097 220.673 1.00 16.34  ? 15   GLY B CA  1 
ATOM   2184 C C   . GLY B 2 15  ? 268.374 215.005 221.893 1.00 16.34  ? 15   GLY B C   1 
ATOM   2185 O O   . GLY B 2 15  ? 267.427 214.902 222.674 1.00 15.83  ? 15   GLY B O   1 
ATOM   2186 N N   . GLY B 2 16  ? 269.342 215.905 222.047 1.00 15.88  ? 16   GLY B N   1 
ATOM   2187 C CA  . GLY B 2 16  ? 269.376 216.806 223.190 1.00 15.41  ? 16   GLY B CA  1 
ATOM   2188 C C   . GLY B 2 16  ? 268.541 218.053 222.942 1.00 14.56  ? 16   GLY B C   1 
ATOM   2189 O O   . GLY B 2 16  ? 267.720 218.092 222.023 1.00 14.33  ? 16   GLY B O   1 
ATOM   2190 N N   . SER B 2 17  ? 268.741 219.066 223.778 1.00 14.26  ? 17   SER B N   1 
ATOM   2191 C CA  . SER B 2 17  ? 267.956 220.289 223.691 1.00 13.54  ? 17   SER B CA  1 
ATOM   2192 C C   . SER B 2 17  ? 268.803 221.511 224.006 1.00 13.50  ? 17   SER B C   1 
ATOM   2193 O O   . SER B 2 17  ? 269.849 221.408 224.648 1.00 13.82  ? 17   SER B O   1 
ATOM   2194 C CB  . SER B 2 17  ? 266.781 220.223 224.646 1.00 13.24  ? 17   SER B CB  1 
ATOM   2195 O OG  . SER B 2 17  ? 267.217 220.172 225.975 1.00 13.30  ? 17   SER B OG  1 
ATOM   2196 N N   . LEU B 2 18  ? 268.345 222.668 223.544 1.00 12.82  ? 18   LEU B N   1 
ATOM   2197 C CA  . LEU B 2 18  ? 269.052 223.919 223.782 1.00 12.53  ? 18   LEU B CA  1 
ATOM   2198 C C   . LEU B 2 18  ? 268.086 225.098 223.798 1.00 12.10  ? 18   LEU B C   1 
ATOM   2199 O O   . LEU B 2 18  ? 267.211 225.206 222.938 1.00 12.31  ? 18   LEU B O   1 
ATOM   2200 C CB  . LEU B 2 18  ? 270.115 224.122 222.696 1.00 12.26  ? 18   LEU B CB  1 
ATOM   2201 C CG  . LEU B 2 18  ? 271.032 225.339 222.845 1.00 12.79  ? 18   LEU B CG  1 
ATOM   2202 C CD1 . LEU B 2 18  ? 271.929 225.163 224.062 1.00 14.40  ? 18   LEU B CD1 1 
ATOM   2203 C CD2 . LEU B 2 18  ? 271.864 225.475 221.594 1.00 13.55  ? 18   LEU B CD2 1 
ATOM   2204 N N   . ARG B 2 19  ? 268.234 225.971 224.788 1.00 12.08  ? 19   ARG B N   1 
ATOM   2205 C CA  . ARG B 2 19  ? 267.383 227.149 224.899 1.00 11.58  ? 19   ARG B CA  1 
ATOM   2206 C C   . ARG B 2 19  ? 268.133 228.416 224.510 1.00 11.41  ? 19   ARG B C   1 
ATOM   2207 O O   . ARG B 2 19  ? 269.088 228.809 225.178 1.00 11.57  ? 19   ARG B O   1 
ATOM   2208 C CB  . ARG B 2 19  ? 266.867 227.291 226.320 1.00 11.38  ? 19   ARG B CB  1 
ATOM   2209 C CG  . ARG B 2 19  ? 265.861 228.408 226.544 1.00 11.09  ? 19   ARG B CG  1 
ATOM   2210 C CD  . ARG B 2 19  ? 265.341 228.376 227.935 1.00 10.85  ? 19   ARG B CD  1 
ATOM   2211 N NE  . ARG B 2 19  ? 264.365 229.421 228.189 1.00 10.55  ? 19   ARG B NE  1 
ATOM   2212 C CZ  . ARG B 2 19  ? 263.046 229.325 227.926 1.00 10.32  ? 19   ARG B CZ  1 
ATOM   2213 N NH1 . ARG B 2 19  ? 262.249 230.329 228.216 1.00 10.45  ? 19   ARG B NH1 1 
ATOM   2214 N NH2 . ARG B 2 19  ? 262.548 228.224 227.382 1.00 10.73  ? 19   ARG B NH2 1 
ATOM   2215 N N   . LEU B 2 20  ? 267.692 229.055 223.433 1.00 11.22  ? 20   LEU B N   1 
ATOM   2216 C CA  . LEU B 2 20  ? 268.320 230.285 222.966 1.00 11.06  ? 20   LEU B CA  1 
ATOM   2217 C C   . LEU B 2 20  ? 267.527 231.492 223.429 1.00 10.21  ? 20   LEU B C   1 
ATOM   2218 O O   . LEU B 2 20  ? 266.314 231.409 223.630 1.00 10.04  ? 20   LEU B O   1 
ATOM   2219 C CB  . LEU B 2 20  ? 268.411 230.318 221.434 1.00 10.96  ? 20   LEU B CB  1 
ATOM   2220 C CG  . LEU B 2 20  ? 269.161 229.170 220.760 1.00 11.92  ? 20   LEU B CG  1 
ATOM   2221 C CD1 . LEU B 2 20  ? 269.096 229.362 219.250 1.00 11.67  ? 20   LEU B CD1 1 
ATOM   2222 C CD2 . LEU B 2 20  ? 270.600 229.138 221.241 1.00 12.25  ? 20   LEU B CD2 1 
ATOM   2223 N N   . SER B 2 21  ? 268.201 232.625 223.550 1.00 10.18  ? 21   SER B N   1 
ATOM   2224 C CA  . SER B 2 21  ? 267.521 233.860 223.905 1.00 9.68   ? 21   SER B CA  1 
ATOM   2225 C C   . SER B 2 21  ? 268.080 235.044 223.125 1.00 9.43   ? 21   SER B C   1 
ATOM   2226 O O   . SER B 2 21  ? 269.223 235.008 222.664 1.00 9.86   ? 21   SER B O   1 
ATOM   2227 C CB  . SER B 2 21  ? 267.649 234.113 225.396 1.00 9.70   ? 21   SER B CB  1 
ATOM   2228 O OG  . SER B 2 21  ? 268.986 234.319 225.758 1.00 10.42  ? 21   SER B OG  1 
ATOM   2229 N N   . CYS B 2 22  ? 267.267 236.095 222.995 1.00 9.12   ? 22   CYS B N   1 
ATOM   2230 C CA  . CYS B 2 22  ? 267.646 237.345 222.345 1.00 9.14   ? 22   CYS B CA  1 
ATOM   2231 C C   . CYS B 2 22  ? 267.202 238.542 223.173 1.00 8.77   ? 22   CYS B C   1 
ATOM   2232 O O   . CYS B 2 22  ? 266.017 238.700 223.480 1.00 8.62   ? 22   CYS B O   1 
ATOM   2233 C CB  . CYS B 2 22  ? 267.035 237.426 220.938 1.00 8.95   ? 22   CYS B CB  1 
ATOM   2234 S SG  . CYS B 2 22  ? 267.367 238.972 220.053 1.00 9.65   ? 22   CYS B SG  1 
ATOM   2235 N N   . ALA B 2 23  ? 268.160 239.384 223.543 1.00 8.80   ? 23   ALA B N   1 
ATOM   2236 C CA  . ALA B 2 23  ? 267.875 240.577 224.326 1.00 8.29   ? 23   ALA B CA  1 
ATOM   2237 C C   . ALA B 2 23  ? 267.635 241.762 223.407 1.00 8.71   ? 23   ALA B C   1 
ATOM   2238 O O   . ALA B 2 23  ? 268.464 242.073 222.551 1.00 8.82   ? 23   ALA B O   1 
ATOM   2239 C CB  . ALA B 2 23  ? 269.024 240.872 225.277 1.00 8.64   ? 23   ALA B CB  1 
ATOM   2240 N N   . ALA B 2 24  ? 266.495 242.421 223.577 1.00 8.43   ? 24   ALA B N   1 
ATOM   2241 C CA  . ALA B 2 24  ? 266.149 243.554 222.731 1.00 8.48   ? 24   ALA B CA  1 
ATOM   2242 C C   . ALA B 2 24  ? 266.227 244.861 223.500 1.00 8.28   ? 24   ALA B C   1 
ATOM   2243 O O   . ALA B 2 24  ? 265.841 244.933 224.666 1.00 8.36   ? 24   ALA B O   1 
ATOM   2244 C CB  . ALA B 2 24  ? 264.751 243.369 222.166 1.00 7.98   ? 24   ALA B CB  1 
ATOM   2245 N N   . SER B 2 25  ? 266.692 245.907 222.826 1.00 8.46   ? 25   SER B N   1 
ATOM   2246 C CA  . SER B 2 25  ? 266.710 247.244 223.405 1.00 8.21   ? 25   SER B CA  1 
ATOM   2247 C C   . SER B 2 25  ? 266.734 248.318 222.323 1.00 8.54   ? 25   SER B C   1 
ATOM   2248 O O   . SER B 2 25  ? 267.098 248.052 221.178 1.00 8.94   ? 25   SER B O   1 
ATOM   2249 C CB  . SER B 2 25  ? 267.909 247.400 224.318 1.00 7.89   ? 25   SER B CB  1 
ATOM   2250 O OG  . SER B 2 25  ? 269.103 247.319 223.596 1.00 9.38   ? 25   SER B OG  1 
ATOM   2251 N N   . GLY B 2 26  ? 266.359 249.541 222.695 1.00 8.48   ? 26   GLY B N   1 
ATOM   2252 C CA  . GLY B 2 26  ? 266.428 250.680 221.783 1.00 8.91   ? 26   GLY B CA  1 
ATOM   2253 C C   . GLY B 2 26  ? 265.126 250.914 221.018 1.00 8.71   ? 26   GLY B C   1 
ATOM   2254 O O   . GLY B 2 26  ? 265.006 251.886 220.272 1.00 9.31   ? 26   GLY B O   1 
ATOM   2255 N N   . PHE B 2 27  ? 264.152 250.031 221.201 1.00 8.15   ? 27   PHE B N   1 
ATOM   2256 C CA  . PHE B 2 27  ? 262.880 250.161 220.501 1.00 7.56   ? 27   PHE B CA  1 
ATOM   2257 C C   . PHE B 2 27  ? 261.737 249.559 221.306 1.00 7.23   ? 27   PHE B C   1 
ATOM   2258 O O   . PHE B 2 27  ? 261.956 248.864 222.301 1.00 7.13   ? 27   PHE B O   1 
ATOM   2259 C CB  . PHE B 2 27  ? 262.961 249.518 219.114 1.00 7.87   ? 27   PHE B CB  1 
ATOM   2260 C CG  . PHE B 2 27  ? 263.086 248.022 219.109 1.00 7.97   ? 27   PHE B CG  1 
ATOM   2261 C CD1 . PHE B 2 27  ? 264.288 247.410 219.399 1.00 8.21   ? 27   PHE B CD1 1 
ATOM   2262 C CD2 . PHE B 2 27  ? 262.006 247.227 218.773 1.00 7.30   ? 27   PHE B CD2 1 
ATOM   2263 C CE1 . PHE B 2 27  ? 264.407 246.039 219.364 1.00 8.38   ? 27   PHE B CE1 1 
ATOM   2264 C CE2 . PHE B 2 27  ? 262.120 245.856 218.735 1.00 7.06   ? 27   PHE B CE2 1 
ATOM   2265 C CZ  . PHE B 2 27  ? 263.320 245.262 219.032 1.00 8.23   ? 27   PHE B CZ  1 
ATOM   2266 N N   . THR B 2 28  ? 260.510 249.842 220.884 1.00 6.84   ? 28   THR B N   1 
ATOM   2267 C CA  . THR B 2 28  ? 259.325 249.368 221.587 1.00 6.48   ? 28   THR B CA  1 
ATOM   2268 C C   . THR B 2 28  ? 259.066 247.894 221.317 1.00 5.80   ? 28   THR B C   1 
ATOM   2269 O O   . THR B 2 28  ? 258.134 247.532 220.600 1.00 6.01   ? 28   THR B O   1 
ATOM   2270 C CB  . THR B 2 28  ? 258.091 250.193 221.193 1.00 6.16   ? 28   THR B CB  1 
ATOM   2271 O OG1 . THR B 2 28  ? 257.930 250.158 219.770 1.00 6.33   ? 28   THR B OG1 1 
ATOM   2272 C CG2 . THR B 2 28  ? 258.258 251.632 221.643 1.00 6.30   ? 28   THR B CG2 1 
ATOM   2273 N N   . PHE B 2 29  ? 259.892 247.048 221.919 1.00 6.53   ? 29   PHE B N   1 
ATOM   2274 C CA  . PHE B 2 29  ? 259.853 245.603 221.720 1.00 6.45   ? 29   PHE B CA  1 
ATOM   2275 C C   . PHE B 2 29  ? 258.451 245.026 221.859 1.00 5.86   ? 29   PHE B C   1 
ATOM   2276 O O   . PHE B 2 29  ? 258.047 244.168 221.076 1.00 5.65   ? 29   PHE B O   1 
ATOM   2277 C CB  . PHE B 2 29  ? 260.790 244.919 222.718 1.00 6.80   ? 29   PHE B CB  1 
ATOM   2278 C CG  . PHE B 2 29  ? 260.796 243.419 222.648 1.00 7.10   ? 29   PHE B CG  1 
ATOM   2279 C CD1 . PHE B 2 29  ? 261.523 242.758 221.677 1.00 7.36   ? 29   PHE B CD1 1 
ATOM   2280 C CD2 . PHE B 2 29  ? 260.086 242.666 223.565 1.00 6.71   ? 29   PHE B CD2 1 
ATOM   2281 C CE1 . PHE B 2 29  ? 261.542 241.381 221.624 1.00 7.39   ? 29   PHE B CE1 1 
ATOM   2282 C CE2 . PHE B 2 29  ? 260.104 241.289 223.514 1.00 6.96   ? 29   PHE B CE2 1 
ATOM   2283 C CZ  . PHE B 2 29  ? 260.832 240.646 222.542 1.00 7.15   ? 29   PHE B CZ  1 
ATOM   2284 N N   . ASN B 2 30  ? 257.708 245.485 222.859 1.00 6.03   ? 30   ASN B N   1 
ATOM   2285 C CA  . ASN B 2 30  ? 256.405 244.902 223.168 1.00 5.76   ? 30   ASN B CA  1 
ATOM   2286 C C   . ASN B 2 30  ? 255.313 245.315 222.183 1.00 5.27   ? 30   ASN B C   1 
ATOM   2287 O O   . ASN B 2 30  ? 254.155 244.926 222.335 1.00 4.98   ? 30   ASN B O   1 
ATOM   2288 C CB  . ASN B 2 30  ? 255.993 245.270 224.579 1.00 5.55   ? 30   ASN B CB  1 
ATOM   2289 C CG  . ASN B 2 30  ? 255.789 246.747 224.743 1.00 5.85   ? 30   ASN B CG  1 
ATOM   2290 O OD1 . ASN B 2 30  ? 256.021 247.520 223.804 1.00 6.21   ? 30   ASN B OD1 1 
ATOM   2291 N ND2 . ASN B 2 30  ? 255.359 247.158 225.908 1.00 6.44   ? 30   ASN B ND2 1 
ATOM   2292 N N   . SER B 2 31  ? 255.680 246.094 221.172 1.00 5.32   ? 31   SER B N   1 
ATOM   2293 C CA  . SER B 2 31  ? 254.734 246.523 220.153 1.00 4.84   ? 31   SER B CA  1 
ATOM   2294 C C   . SER B 2 31  ? 254.870 245.714 218.871 1.00 4.86   ? 31   SER B C   1 
ATOM   2295 O O   . SER B 2 31  ? 253.996 245.765 218.004 1.00 4.80   ? 31   SER B O   1 
ATOM   2296 C CB  . SER B 2 31  ? 254.946 247.989 219.844 1.00 4.43   ? 31   SER B CB  1 
ATOM   2297 O OG  . SER B 2 31  ? 254.697 248.776 220.973 1.00 5.22   ? 31   SER B OG  1 
ATOM   2298 N N   . TYR B 2 32  ? 255.974 244.978 218.741 1.00 4.90   ? 32   TYR B N   1 
ATOM   2299 C CA  . TYR B 2 32  ? 256.276 244.264 217.504 1.00 4.94   ? 32   TYR B CA  1 
ATOM   2300 C C   . TYR B 2 32  ? 256.276 242.756 217.691 1.00 5.02   ? 32   TYR B C   1 
ATOM   2301 O O   . TYR B 2 32  ? 256.641 242.248 218.752 1.00 5.26   ? 32   TYR B O   1 
ATOM   2302 C CB  . TYR B 2 32  ? 257.651 244.666 216.966 1.00 5.33   ? 32   TYR B CB  1 
ATOM   2303 C CG  . TYR B 2 32  ? 257.797 246.107 216.569 1.00 5.38   ? 32   TYR B CG  1 
ATOM   2304 C CD1 . TYR B 2 32  ? 257.327 246.542 215.345 1.00 5.03   ? 32   TYR B CD1 1 
ATOM   2305 C CD2 . TYR B 2 32  ? 258.432 246.989 217.418 1.00 5.41   ? 32   TYR B CD2 1 
ATOM   2306 C CE1 . TYR B 2 32  ? 257.488 247.859 214.975 1.00 4.91   ? 32   TYR B CE1 1 
ATOM   2307 C CE2 . TYR B 2 32  ? 258.594 248.303 217.051 1.00 5.52   ? 32   TYR B CE2 1 
ATOM   2308 C CZ  . TYR B 2 32  ? 258.125 248.739 215.834 1.00 4.97   ? 32   TYR B CZ  1 
ATOM   2309 O OH  . TYR B 2 32  ? 258.293 250.050 215.465 1.00 5.17   ? 32   TYR B OH  1 
ATOM   2310 N N   . GLY B 2 33  ? 255.944 242.036 216.626 1.00 5.13   ? 33   GLY B N   1 
ATOM   2311 C CA  . GLY B 2 33  ? 256.140 240.595 216.602 1.00 5.25   ? 33   GLY B CA  1 
ATOM   2312 C C   . GLY B 2 33  ? 257.607 240.320 216.314 1.00 5.60   ? 33   GLY B C   1 
ATOM   2313 O O   . GLY B 2 33  ? 258.348 241.237 215.965 1.00 6.27   ? 33   GLY B O   1 
ATOM   2314 N N   . MET B 2 34  ? 258.034 239.073 216.468 1.00 5.81   ? 34   MET B N   1 
ATOM   2315 C CA  . MET B 2 34  ? 259.436 238.736 216.242 1.00 6.04   ? 34   MET B CA  1 
ATOM   2316 C C   . MET B 2 34  ? 259.608 237.429 215.487 1.00 6.62   ? 34   MET B C   1 
ATOM   2317 O O   . MET B 2 34  ? 258.790 236.516 215.605 1.00 6.55   ? 34   MET B O   1 
ATOM   2318 C CB  . MET B 2 34  ? 260.192 238.665 217.561 1.00 6.35   ? 34   MET B CB  1 
ATOM   2319 C CG  . MET B 2 34  ? 260.304 239.982 218.324 1.00 6.27   ? 34   MET B CG  1 
ATOM   2320 S SD  . MET B 2 34  ? 261.374 241.198 217.506 1.00 6.91   ? 34   MET B SD  1 
ATOM   2321 C CE  . MET B 2 34  ? 263.015 240.501 217.736 1.00 7.64   ? 34   MET B CE  1 
ATOM   2322 N N   . HIS B 2 35  ? 260.695 237.338 214.725 1.00 7.01   ? 35   HIS B N   1 
ATOM   2323 C CA  . HIS B 2 35  ? 260.997 236.151 213.939 1.00 7.14   ? 35   HIS B CA  1 
ATOM   2324 C C   . HIS B 2 35  ? 262.327 235.524 214.330 1.00 7.48   ? 35   HIS B C   1 
ATOM   2325 O O   . HIS B 2 35  ? 263.266 236.220 214.721 1.00 7.72   ? 35   HIS B O   1 
ATOM   2326 C CB  . HIS B 2 35  ? 261.077 236.503 212.449 1.00 7.29   ? 35   HIS B CB  1 
ATOM   2327 C CG  . HIS B 2 35  ? 259.839 237.082 211.886 1.00 6.84   ? 35   HIS B CG  1 
ATOM   2328 N ND1 . HIS B 2 35  ? 258.938 236.345 211.157 1.00 7.40   ? 35   HIS B ND1 1 
ATOM   2329 C CD2 . HIS B 2 35  ? 259.345 238.337 211.940 1.00 6.70   ? 35   HIS B CD2 1 
ATOM   2330 C CE1 . HIS B 2 35  ? 257.939 237.123 210.787 1.00 7.46   ? 35   HIS B CE1 1 
ATOM   2331 N NE2 . HIS B 2 35  ? 258.165 238.336 211.249 1.00 7.17   ? 35   HIS B NE2 1 
ATOM   2332 N N   . TRP B 2 36  ? 262.423 234.212 214.141 1.00 7.75   ? 36   TRP B N   1 
ATOM   2333 C CA  . TRP B 2 36  ? 263.707 233.526 214.170 1.00 8.16   ? 36   TRP B CA  1 
ATOM   2334 C C   . TRP B 2 36  ? 264.052 233.042 212.769 1.00 8.35   ? 36   TRP B C   1 
ATOM   2335 O O   . TRP B 2 36  ? 263.207 232.470 212.077 1.00 8.52   ? 36   TRP B O   1 
ATOM   2336 C CB  . TRP B 2 36  ? 263.696 232.338 215.136 1.00 8.25   ? 36   TRP B CB  1 
ATOM   2337 C CG  . TRP B 2 36  ? 263.749 232.721 216.584 1.00 8.62   ? 36   TRP B CG  1 
ATOM   2338 C CD1 . TRP B 2 36  ? 262.695 232.847 217.420 1.00 8.63   ? 36   TRP B CD1 1 
ATOM   2339 C CD2 . TRP B 2 36  ? 264.926 233.026 217.375 1.00 8.61   ? 36   TRP B CD2 1 
ATOM   2340 N NE1 . TRP B 2 36  ? 263.121 233.205 218.670 1.00 8.79   ? 36   TRP B NE1 1 
ATOM   2341 C CE2 . TRP B 2 36  ? 264.484 233.320 218.659 1.00 8.78   ? 36   TRP B CE2 1 
ATOM   2342 C CE3 . TRP B 2 36  ? 266.293 233.070 217.096 1.00 9.13   ? 36   TRP B CE3 1 
ATOM   2343 C CZ2 . TRP B 2 36  ? 265.360 233.658 219.677 1.00 8.92   ? 36   TRP B CZ2 1 
ATOM   2344 C CZ3 . TRP B 2 36  ? 267.172 233.410 218.116 1.00 9.12   ? 36   TRP B CZ3 1 
ATOM   2345 C CH2 . TRP B 2 36  ? 266.715 233.696 219.373 1.00 8.70   ? 36   TRP B CH2 1 
ATOM   2346 N N   . VAL B 2 37  ? 265.294 233.282 212.365 1.00 8.92   ? 37   VAL B N   1 
ATOM   2347 C CA  . VAL B 2 37  ? 265.811 232.865 211.064 1.00 9.31   ? 37   VAL B CA  1 
ATOM   2348 C C   . VAL B 2 37  ? 267.157 232.178 211.256 1.00 9.88   ? 37   VAL B C   1 
ATOM   2349 O O   . VAL B 2 37  ? 267.974 232.635 212.052 1.00 10.26  ? 37   VAL B O   1 
ATOM   2350 C CB  . VAL B 2 37  ? 265.970 234.087 210.127 1.00 9.22   ? 37   VAL B CB  1 
ATOM   2351 C CG1 . VAL B 2 37  ? 266.525 233.656 208.769 1.00 10.27  ? 37   VAL B CG1 1 
ATOM   2352 C CG2 . VAL B 2 37  ? 264.621 234.780 209.953 1.00 8.84   ? 37   VAL B CG2 1 
ATOM   2353 N N   . ARG B 2 38  ? 267.398 231.081 210.550 1.00 10.16  ? 38   ARG B N   1 
ATOM   2354 C CA  . ARG B 2 38  ? 268.674 230.393 210.703 1.00 10.74  ? 38   ARG B CA  1 
ATOM   2355 C C   . ARG B 2 38  ? 269.386 230.226 209.374 1.00 10.97  ? 38   ARG B C   1 
ATOM   2356 O O   . ARG B 2 38  ? 268.752 230.132 208.324 1.00 11.01  ? 38   ARG B O   1 
ATOM   2357 C CB  . ARG B 2 38  ? 268.489 229.028 211.342 1.00 11.01  ? 38   ARG B CB  1 
ATOM   2358 C CG  . ARG B 2 38  ? 267.797 227.999 210.476 1.00 11.08  ? 38   ARG B CG  1 
ATOM   2359 C CD  . ARG B 2 38  ? 267.642 226.711 211.186 1.00 11.44  ? 38   ARG B CD  1 
ATOM   2360 N NE  . ARG B 2 38  ? 267.014 225.707 210.349 1.00 11.00  ? 38   ARG B NE  1 
ATOM   2361 C CZ  . ARG B 2 38  ? 266.785 224.433 210.715 1.00 11.64  ? 38   ARG B CZ  1 
ATOM   2362 N NH1 . ARG B 2 38  ? 266.208 223.613 209.868 1.00 11.93  ? 38   ARG B NH1 1 
ATOM   2363 N NH2 . ARG B 2 38  ? 267.139 224.006 211.913 1.00 13.01  ? 38   ARG B NH2 1 
ATOM   2364 N N   . GLN B 2 39  ? 270.711 230.178 209.426 1.00 11.38  ? 39   GLN B N   1 
ATOM   2365 C CA  . GLN B 2 39  ? 271.506 229.966 208.227 1.00 11.96  ? 39   GLN B CA  1 
ATOM   2366 C C   . GLN B 2 39  ? 272.660 229.006 208.473 1.00 12.48  ? 39   GLN B C   1 
ATOM   2367 O O   . GLN B 2 39  ? 273.604 229.328 209.194 1.00 12.45  ? 39   GLN B O   1 
ATOM   2368 C CB  . GLN B 2 39  ? 272.043 231.302 207.723 1.00 11.88  ? 39   GLN B CB  1 
ATOM   2369 C CG  . GLN B 2 39  ? 272.839 231.220 206.444 1.00 12.65  ? 39   GLN B CG  1 
ATOM   2370 C CD  . GLN B 2 39  ? 273.124 232.589 205.881 1.00 13.08  ? 39   GLN B CD  1 
ATOM   2371 O OE1 . GLN B 2 39  ? 273.148 233.577 206.625 1.00 13.14  ? 39   GLN B OE1 1 
ATOM   2372 N NE2 . GLN B 2 39  ? 273.331 232.669 204.573 1.00 13.41  ? 39   GLN B NE2 1 
ATOM   2373 N N   . ALA B 2 40  ? 272.591 227.833 207.855 1.00 12.69  ? 40   ALA B N   1 
ATOM   2374 C CA  . ALA B 2 40  ? 273.671 226.864 207.963 1.00 13.61  ? 40   ALA B CA  1 
ATOM   2375 C C   . ALA B 2 40  ? 274.841 227.338 207.109 1.00 13.15  ? 40   ALA B C   1 
ATOM   2376 O O   . ALA B 2 40  ? 274.619 227.958 206.071 1.00 13.69  ? 40   ALA B O   1 
ATOM   2377 C CB  . ALA B 2 40  ? 273.203 225.487 207.523 1.00 13.79  ? 40   ALA B CB  1 
ATOM   2378 N N   . PRO B 2 41  ? 276.084 227.050 207.499 1.00 13.77  ? 41   PRO B N   1 
ATOM   2379 C CA  . PRO B 2 41  ? 277.285 227.350 206.749 1.00 13.93  ? 41   PRO B CA  1 
ATOM   2380 C C   . PRO B 2 41  ? 277.180 226.826 205.323 1.00 13.98  ? 41   PRO B C   1 
ATOM   2381 O O   . PRO B 2 41  ? 276.896 225.648 205.108 1.00 14.03  ? 41   PRO B O   1 
ATOM   2382 C CB  . PRO B 2 41  ? 278.354 226.596 207.549 1.00 13.88  ? 41   PRO B CB  1 
ATOM   2383 C CG  . PRO B 2 41  ? 277.817 226.582 208.968 1.00 13.22  ? 41   PRO B CG  1 
ATOM   2384 C CD  . PRO B 2 41  ? 276.318 226.427 208.811 1.00 14.10  ? 41   PRO B CD  1 
ATOM   2385 N N   . GLY B 2 42  ? 277.420 227.705 204.355 1.00 13.98  ? 42   GLY B N   1 
ATOM   2386 C CA  . GLY B 2 42  ? 277.387 227.334 202.943 1.00 13.72  ? 42   GLY B CA  1 
ATOM   2387 C C   . GLY B 2 42  ? 275.973 227.318 202.363 1.00 13.88  ? 42   GLY B C   1 
ATOM   2388 O O   . GLY B 2 42  ? 275.787 227.004 201.186 1.00 13.82  ? 42   GLY B O   1 
ATOM   2389 N N   . LYS B 2 43  ? 274.978 227.642 203.184 1.00 13.95  ? 43   LYS B N   1 
ATOM   2390 C CA  . LYS B 2 43  ? 273.585 227.601 202.750 1.00 14.03  ? 43   LYS B CA  1 
ATOM   2391 C C   . LYS B 2 43  ? 272.933 228.979 202.778 1.00 13.93  ? 43   LYS B C   1 
ATOM   2392 O O   . LYS B 2 43  ? 273.508 229.945 203.281 1.00 13.82  ? 43   LYS B O   1 
ATOM   2393 C CB  . LYS B 2 43  ? 272.786 226.627 203.616 1.00 13.80  ? 43   LYS B CB  1 
ATOM   2394 C CG  . LYS B 2 43  ? 273.339 225.201 203.645 1.00 13.96  ? 43   LYS B CG  1 
ATOM   2395 C CD  . LYS B 2 43  ? 273.250 224.527 202.282 1.00 13.63  ? 43   LYS B CD  1 
ATOM   2396 C CE  . LYS B 2 43  ? 273.690 223.073 202.358 1.00 14.94  ? 43   LYS B CE  1 
ATOM   2397 N NZ  . LYS B 2 43  ? 273.654 222.410 201.024 1.00 15.21  ? 43   LYS B NZ  1 
ATOM   2398 N N   . GLY B 2 44  ? 271.725 229.064 202.226 1.00 13.98  ? 44   GLY B N   1 
ATOM   2399 C CA  . GLY B 2 44  ? 270.972 230.312 202.213 1.00 13.87  ? 44   GLY B CA  1 
ATOM   2400 C C   . GLY B 2 44  ? 270.166 230.473 203.496 1.00 13.22  ? 44   GLY B C   1 
ATOM   2401 O O   . GLY B 2 44  ? 270.360 229.728 204.455 1.00 12.75  ? 44   GLY B O   1 
ATOM   2402 N N   . LEU B 2 45  ? 269.277 231.458 203.513 1.00 13.12  ? 45   LEU B N   1 
ATOM   2403 C CA  . LEU B 2 45  ? 268.493 231.765 204.702 1.00 12.47  ? 45   LEU B CA  1 
ATOM   2404 C C   . LEU B 2 45  ? 267.266 230.871 204.797 1.00 12.29  ? 45   LEU B C   1 
ATOM   2405 O O   . LEU B 2 45  ? 266.618 230.592 203.789 1.00 12.73  ? 45   LEU B O   1 
ATOM   2406 C CB  . LEU B 2 45  ? 268.030 233.225 204.647 1.00 12.50  ? 45   LEU B CB  1 
ATOM   2407 C CG  . LEU B 2 45  ? 269.130 234.287 204.541 1.00 12.82  ? 45   LEU B CG  1 
ATOM   2408 C CD1 . LEU B 2 45  ? 268.488 235.630 204.243 1.00 13.15  ? 45   LEU B CD1 1 
ATOM   2409 C CD2 . LEU B 2 45  ? 269.915 234.347 205.836 1.00 11.67  ? 45   LEU B CD2 1 
ATOM   2410 N N   . GLU B 2 46  ? 266.924 230.459 206.014 1.00 11.55  ? 46   GLU B N   1 
ATOM   2411 C CA  . GLU B 2 46  ? 265.709 229.690 206.239 1.00 11.37  ? 46   GLU B CA  1 
ATOM   2412 C C   . GLU B 2 46  ? 264.915 230.238 207.419 1.00 10.68  ? 46   GLU B C   1 
ATOM   2413 O O   . GLU B 2 46  ? 265.451 230.436 208.508 1.00 10.36  ? 46   GLU B O   1 
ATOM   2414 C CB  . GLU B 2 46  ? 266.050 228.217 206.470 1.00 11.04  ? 46   GLU B CB  1 
ATOM   2415 C CG  . GLU B 2 46  ? 264.844 227.317 206.666 1.00 11.40  ? 46   GLU B CG  1 
ATOM   2416 C CD  . GLU B 2 46  ? 265.207 225.864 206.753 1.00 11.56  ? 46   GLU B CD  1 
ATOM   2417 O OE1 . GLU B 2 46  ? 265.871 225.490 207.690 1.00 11.73  ? 46   GLU B OE1 1 
ATOM   2418 O OE2 . GLU B 2 46  ? 264.824 225.126 205.878 1.00 12.31  ? 46   GLU B OE2 1 
ATOM   2419 N N   . TRP B 2 47  ? 263.632 230.482 207.193 1.00 10.72  ? 47   TRP B N   1 
ATOM   2420 C CA  . TRP B 2 47  ? 262.744 231.001 208.228 1.00 9.64   ? 47   TRP B CA  1 
ATOM   2421 C C   . TRP B 2 47  ? 262.364 229.894 209.205 1.00 9.33   ? 47   TRP B C   1 
ATOM   2422 O O   . TRP B 2 47  ? 262.106 228.764 208.793 1.00 9.76   ? 47   TRP B O   1 
ATOM   2423 C CB  . TRP B 2 47  ? 261.507 231.596 207.564 1.00 9.43   ? 47   TRP B CB  1 
ATOM   2424 C CG  . TRP B 2 47  ? 260.522 232.193 208.491 1.00 8.96   ? 47   TRP B CG  1 
ATOM   2425 C CD1 . TRP B 2 47  ? 260.517 233.459 208.981 1.00 8.64   ? 47   TRP B CD1 1 
ATOM   2426 C CD2 . TRP B 2 47  ? 259.353 231.552 209.025 1.00 8.68   ? 47   TRP B CD2 1 
ATOM   2427 N NE1 . TRP B 2 47  ? 259.426 233.646 209.781 1.00 8.10   ? 47   TRP B NE1 1 
ATOM   2428 C CE2 . TRP B 2 47  ? 258.700 232.485 209.811 1.00 8.31   ? 47   TRP B CE2 1 
ATOM   2429 C CE3 . TRP B 2 47  ? 258.815 230.279 208.894 1.00 8.75   ? 47   TRP B CE3 1 
ATOM   2430 C CZ2 . TRP B 2 47  ? 257.528 232.188 210.461 1.00 7.82   ? 47   TRP B CZ2 1 
ATOM   2431 C CZ3 . TRP B 2 47  ? 257.644 229.982 209.557 1.00 8.42   ? 47   TRP B CZ3 1 
ATOM   2432 C CH2 . TRP B 2 47  ? 257.015 230.913 210.318 1.00 7.90   ? 47   TRP B CH2 1 
ATOM   2433 N N   . VAL B 2 48  ? 262.349 230.207 210.501 1.00 8.81   ? 48   VAL B N   1 
ATOM   2434 C CA  . VAL B 2 48  ? 262.075 229.194 211.515 1.00 8.61   ? 48   VAL B CA  1 
ATOM   2435 C C   . VAL B 2 48  ? 260.730 229.377 212.214 1.00 8.18   ? 48   VAL B C   1 
ATOM   2436 O O   . VAL B 2 48  ? 259.922 228.449 212.255 1.00 8.26   ? 48   VAL B O   1 
ATOM   2437 C CB  . VAL B 2 48  ? 263.200 229.191 212.571 1.00 7.94   ? 48   VAL B CB  1 
ATOM   2438 C CG1 . VAL B 2 48  ? 262.905 228.181 213.666 1.00 8.55   ? 48   VAL B CG1 1 
ATOM   2439 C CG2 . VAL B 2 48  ? 264.520 228.869 211.897 1.00 9.37   ? 48   VAL B CG2 1 
ATOM   2440 N N   . ALA B 2 49  ? 260.508 230.544 212.814 1.00 8.01   ? 49   ALA B N   1 
ATOM   2441 C CA  . ALA B 2 49  ? 259.290 230.743 213.604 1.00 7.58   ? 49   ALA B CA  1 
ATOM   2442 C C   . ALA B 2 49  ? 258.930 232.217 213.768 1.00 7.29   ? 49   ALA B C   1 
ATOM   2443 O O   . ALA B 2 49  ? 259.788 233.095 213.677 1.00 7.54   ? 49   ALA B O   1 
ATOM   2444 C CB  . ALA B 2 49  ? 259.447 230.095 214.970 1.00 7.69   ? 49   ALA B CB  1 
ATOM   2445 N N   . PHE B 2 50  ? 257.651 232.472 214.048 1.00 6.95   ? 50   PHE B N   1 
ATOM   2446 C CA  . PHE B 2 50  ? 257.140 233.824 214.284 1.00 6.69   ? 50   PHE B CA  1 
ATOM   2447 C C   . PHE B 2 50  ? 256.173 233.879 215.456 1.00 5.99   ? 50   PHE B C   1 
ATOM   2448 O O   . PHE B 2 50  ? 255.315 233.008 215.610 1.00 6.36   ? 50   PHE B O   1 
ATOM   2449 C CB  . PHE B 2 50  ? 256.450 234.352 213.025 1.00 6.70   ? 50   PHE B CB  1 
ATOM   2450 C CG  . PHE B 2 50  ? 255.640 235.598 213.206 1.00 6.52   ? 50   PHE B CG  1 
ATOM   2451 C CD1 . PHE B 2 50  ? 256.232 236.796 213.546 1.00 6.21   ? 50   PHE B CD1 1 
ATOM   2452 C CD2 . PHE B 2 50  ? 254.276 235.574 213.000 1.00 6.16   ? 50   PHE B CD2 1 
ATOM   2453 C CE1 . PHE B 2 50  ? 255.480 237.939 213.688 1.00 5.92   ? 50   PHE B CE1 1 
ATOM   2454 C CE2 . PHE B 2 50  ? 253.519 236.712 213.140 1.00 5.85   ? 50   PHE B CE2 1 
ATOM   2455 C CZ  . PHE B 2 50  ? 254.122 237.897 213.486 1.00 5.53   ? 50   PHE B CZ  1 
ATOM   2456 N N   . ILE B 2 51  ? 256.315 234.908 216.284 1.00 6.11   ? 51   ILE B N   1 
ATOM   2457 C CA  . ILE B 2 51  ? 255.414 235.118 217.412 1.00 5.83   ? 51   ILE B CA  1 
ATOM   2458 C C   . ILE B 2 51  ? 254.843 236.532 217.394 1.00 5.53   ? 51   ILE B C   1 
ATOM   2459 O O   . ILE B 2 51  ? 255.559 237.497 217.121 1.00 5.27   ? 51   ILE B O   1 
ATOM   2460 C CB  . ILE B 2 51  ? 256.147 234.844 218.738 1.00 6.01   ? 51   ILE B CB  1 
ATOM   2461 C CG1 . ILE B 2 51  ? 255.177 234.896 219.910 1.00 5.44   ? 51   ILE B CG1 1 
ATOM   2462 C CG2 . ILE B 2 51  ? 257.284 235.847 218.930 1.00 6.34   ? 51   ILE B CG2 1 
ATOM   2463 C CD1 . ILE B 2 51  ? 255.725 234.253 221.168 1.00 5.97   ? 51   ILE B CD1 1 
ATOM   2464 N N   . ARG B 2 52  ? 253.554 236.659 217.697 1.00 5.12   ? 52   ARG B N   1 
ATOM   2465 C CA  . ARG B 2 52  ? 252.907 237.968 217.698 1.00 4.66   ? 52   ARG B CA  1 
ATOM   2466 C C   . ARG B 2 52  ? 253.282 238.801 218.920 1.00 4.66   ? 52   ARG B C   1 
ATOM   2467 O O   . ARG B 2 52  ? 253.778 238.282 219.918 1.00 4.41   ? 52   ARG B O   1 
ATOM   2468 C CB  . ARG B 2 52  ? 251.397 237.834 217.630 1.00 4.23   ? 52   ARG B CB  1 
ATOM   2469 C CG  . ARG B 2 52  ? 250.868 237.260 216.336 1.00 4.36   ? 52   ARG B CG  1 
ATOM   2470 C CD  . ARG B 2 52  ? 249.407 237.474 216.213 1.00 3.68   ? 52   ARG B CD  1 
ATOM   2471 N NE  . ARG B 2 52  ? 249.091 238.840 215.826 1.00 2.99   ? 52   ARG B NE  1 
ATOM   2472 C CZ  . ARG B 2 52  ? 247.989 239.526 216.205 1.00 2.30   ? 52   ARG B CZ  1 
ATOM   2473 N NH1 . ARG B 2 52  ? 247.801 240.747 215.762 1.00 2.14   ? 52   ARG B NH1 1 
ATOM   2474 N NH2 . ARG B 2 52  ? 247.096 238.982 217.016 1.00 2.83   ? 52   ARG B NH2 1 
ATOM   2475 N N   . TYR B 2 53  ? 253.043 240.106 218.823 1.00 4.74   ? 53   TYR B N   1 
ATOM   2476 C CA  . TYR B 2 53  ? 253.430 241.074 219.848 1.00 4.57   ? 53   TYR B CA  1 
ATOM   2477 C C   . TYR B 2 53  ? 252.943 240.733 221.256 1.00 4.41   ? 53   TYR B C   1 
ATOM   2478 O O   . TYR B 2 53  ? 253.622 241.041 222.236 1.00 4.81   ? 53   TYR B O   1 
ATOM   2479 C CB  . TYR B 2 53  ? 252.920 242.461 219.458 1.00 4.26   ? 53   TYR B CB  1 
ATOM   2480 C CG  . TYR B 2 53  ? 251.452 242.672 219.735 1.00 3.73   ? 53   TYR B CG  1 
ATOM   2481 C CD1 . TYR B 2 53  ? 250.504 242.213 218.840 1.00 3.40   ? 53   TYR B CD1 1 
ATOM   2482 C CD2 . TYR B 2 53  ? 251.055 243.339 220.879 1.00 3.73   ? 53   TYR B CD2 1 
ATOM   2483 C CE1 . TYR B 2 53  ? 249.166 242.410 219.095 1.00 2.92   ? 53   TYR B CE1 1 
ATOM   2484 C CE2 . TYR B 2 53  ? 249.714 243.541 221.130 1.00 3.26   ? 53   TYR B CE2 1 
ATOM   2485 C CZ  . TYR B 2 53  ? 248.773 243.077 220.243 1.00 2.82   ? 53   TYR B CZ  1 
ATOM   2486 O OH  . TYR B 2 53  ? 247.439 243.277 220.487 1.00 2.69   ? 53   TYR B OH  1 
ATOM   2487 N N   . ASP B 2 54  ? 251.768 240.118 221.369 1.00 4.02   ? 54   ASP B N   1 
ATOM   2488 C CA  . ASP B 2 54  ? 251.201 239.834 222.682 1.00 3.99   ? 54   ASP B CA  1 
ATOM   2489 C C   . ASP B 2 54  ? 251.621 238.474 223.219 1.00 4.31   ? 54   ASP B C   1 
ATOM   2490 O O   . ASP B 2 54  ? 251.210 238.077 224.309 1.00 4.36   ? 54   ASP B O   1 
ATOM   2491 C CB  . ASP B 2 54  ? 249.676 239.907 222.629 1.00 3.43   ? 54   ASP B CB  1 
ATOM   2492 C CG  . ASP B 2 54  ? 249.067 238.893 221.672 1.00 3.84   ? 54   ASP B CG  1 
ATOM   2493 O OD1 . ASP B 2 54  ? 249.807 238.192 221.013 1.00 4.05   ? 54   ASP B OD1 1 
ATOM   2494 O OD2 . ASP B 2 54  ? 247.866 238.820 221.609 1.00 3.77   ? 54   ASP B OD2 1 
ATOM   2495 N N   . GLY B 2 55  ? 252.438 237.761 222.456 1.00 4.42   ? 55   GLY B N   1 
ATOM   2496 C CA  . GLY B 2 55  ? 252.915 236.448 222.864 1.00 4.40   ? 55   GLY B CA  1 
ATOM   2497 C C   . GLY B 2 55  ? 251.846 235.376 222.695 1.00 4.23   ? 55   GLY B C   1 
ATOM   2498 O O   . GLY B 2 55  ? 251.975 234.276 223.233 1.00 4.92   ? 55   GLY B O   1 
ATOM   2499 N N   . GLY B 2 56  ? 250.796 235.695 221.946 1.00 4.13   ? 56   GLY B N   1 
ATOM   2500 C CA  . GLY B 2 56  ? 249.681 234.778 221.751 1.00 4.22   ? 56   GLY B CA  1 
ATOM   2501 C C   . GLY B 2 56  ? 249.930 233.803 220.609 1.00 4.71   ? 56   GLY B C   1 
ATOM   2502 O O   . GLY B 2 56  ? 250.491 232.724 220.810 1.00 5.32   ? 56   GLY B O   1 
ATOM   2503 N N   . ASN B 2 57  ? 249.484 234.167 219.411 1.00 4.36   ? 57   ASN B N   1 
ATOM   2504 C CA  . ASN B 2 57  ? 249.596 233.277 218.261 1.00 4.32   ? 57   ASN B CA  1 
ATOM   2505 C C   . ASN B 2 57  ? 251.049 232.994 217.908 1.00 4.85   ? 57   ASN B C   1 
ATOM   2506 O O   . ASN B 2 57  ? 251.897 233.889 217.942 1.00 4.78   ? 57   ASN B O   1 
ATOM   2507 C CB  . ASN B 2 57  ? 248.860 233.842 217.066 1.00 4.35   ? 57   ASN B CB  1 
ATOM   2508 C CG  . ASN B 2 57  ? 247.381 233.901 217.280 1.00 4.27   ? 57   ASN B CG  1 
ATOM   2509 O OD1 . ASN B 2 57  ? 246.839 233.219 218.156 1.00 4.29   ? 57   ASN B OD1 1 
ATOM   2510 N ND2 . ASN B 2 57  ? 246.710 234.700 216.495 1.00 3.89   ? 57   ASN B ND2 1 
ATOM   2511 N N   . LYS B 2 58  ? 251.325 231.737 217.568 1.00 5.29   ? 58   LYS B N   1 
ATOM   2512 C CA  . LYS B 2 58  ? 252.668 231.295 217.219 1.00 5.54   ? 58   LYS B CA  1 
ATOM   2513 C C   . LYS B 2 58  ? 252.649 230.493 215.925 1.00 5.90   ? 58   LYS B C   1 
ATOM   2514 O O   . LYS B 2 58  ? 251.730 229.710 215.686 1.00 6.28   ? 58   LYS B O   1 
ATOM   2515 C CB  . LYS B 2 58  ? 253.240 230.442 218.347 1.00 5.62   ? 58   LYS B CB  1 
ATOM   2516 C CG  . LYS B 2 58  ? 253.319 231.157 219.684 1.00 5.69   ? 58   LYS B CG  1 
ATOM   2517 C CD  . LYS B 2 58  ? 253.690 230.207 220.803 1.00 6.15   ? 58   LYS B CD  1 
ATOM   2518 C CE  . LYS B 2 58  ? 253.635 230.896 222.162 1.00 5.67   ? 58   LYS B CE  1 
ATOM   2519 N NZ  . LYS B 2 58  ? 252.227 231.124 222.627 1.00 5.14   ? 58   LYS B NZ  1 
ATOM   2520 N N   . TYR B 2 59  ? 253.672 230.681 215.100 1.00 6.01   ? 59   TYR B N   1 
ATOM   2521 C CA  . TYR B 2 59  ? 253.773 229.975 213.829 1.00 6.45   ? 59   TYR B CA  1 
ATOM   2522 C C   . TYR B 2 59  ? 255.146 229.337 213.668 1.00 7.07   ? 59   TYR B C   1 
ATOM   2523 O O   . TYR B 2 59  ? 256.154 229.902 214.093 1.00 7.23   ? 59   TYR B O   1 
ATOM   2524 C CB  . TYR B 2 59  ? 253.497 230.946 212.686 1.00 6.13   ? 59   TYR B CB  1 
ATOM   2525 C CG  . TYR B 2 59  ? 252.177 231.662 212.826 1.00 5.83   ? 59   TYR B CG  1 
ATOM   2526 C CD1 . TYR B 2 59  ? 252.094 232.804 213.608 1.00 5.66   ? 59   TYR B CD1 1 
ATOM   2527 C CD2 . TYR B 2 59  ? 251.054 231.189 212.178 1.00 5.93   ? 59   TYR B CD2 1 
ATOM   2528 C CE1 . TYR B 2 59  ? 250.899 233.468 213.741 1.00 5.35   ? 59   TYR B CE1 1 
ATOM   2529 C CE2 . TYR B 2 59  ? 249.853 231.856 212.311 1.00 5.69   ? 59   TYR B CE2 1 
ATOM   2530 C CZ  . TYR B 2 59  ? 249.775 232.992 213.090 1.00 5.29   ? 59   TYR B CZ  1 
ATOM   2531 O OH  . TYR B 2 59  ? 248.580 233.657 213.220 1.00 5.27   ? 59   TYR B OH  1 
ATOM   2532 N N   . TYR B 2 60  ? 255.186 228.163 213.043 1.00 7.55   ? 60   TYR B N   1 
ATOM   2533 C CA  . TYR B 2 60  ? 256.445 227.451 212.849 1.00 7.99   ? 60   TYR B CA  1 
ATOM   2534 C C   . TYR B 2 60  ? 256.610 226.955 211.422 1.00 8.51   ? 60   TYR B C   1 
ATOM   2535 O O   . TYR B 2 60  ? 255.630 226.624 210.755 1.00 8.67   ? 60   TYR B O   1 
ATOM   2536 C CB  . TYR B 2 60  ? 256.526 226.252 213.791 1.00 8.06   ? 60   TYR B CB  1 
ATOM   2537 C CG  . TYR B 2 60  ? 256.384 226.597 215.241 1.00 7.96   ? 60   TYR B CG  1 
ATOM   2538 C CD1 . TYR B 2 60  ? 257.498 226.912 215.993 1.00 8.17   ? 60   TYR B CD1 1 
ATOM   2539 C CD2 . TYR B 2 60  ? 255.131 226.592 215.823 1.00 7.83   ? 60   TYR B CD2 1 
ATOM   2540 C CE1 . TYR B 2 60  ? 257.357 227.221 217.324 1.00 8.25   ? 60   TYR B CE1 1 
ATOM   2541 C CE2 . TYR B 2 60  ? 254.989 226.899 217.154 1.00 7.26   ? 60   TYR B CE2 1 
ATOM   2542 C CZ  . TYR B 2 60  ? 256.092 227.211 217.905 1.00 7.86   ? 60   TYR B CZ  1 
ATOM   2543 O OH  . TYR B 2 60  ? 255.944 227.513 219.237 1.00 8.52   ? 60   TYR B OH  1 
ATOM   2544 N N   . ALA B 2 61  ? 257.860 226.848 210.983 1.00 8.52   ? 61   ALA B N   1 
ATOM   2545 C CA  . ALA B 2 61  ? 258.183 226.194 209.723 1.00 8.90   ? 61   ALA B CA  1 
ATOM   2546 C C   . ALA B 2 61  ? 257.950 224.695 209.846 1.00 8.93   ? 61   ALA B C   1 
ATOM   2547 O O   . ALA B 2 61  ? 258.135 224.116 210.917 1.00 10.08  ? 61   ALA B O   1 
ATOM   2548 C CB  . ALA B 2 61  ? 259.625 226.474 209.331 1.00 9.37   ? 61   ALA B CB  1 
ATOM   2549 N N   . ASP B 2 62  ? 257.573 224.058 208.745 1.00 9.25   ? 62   ASP B N   1 
ATOM   2550 C CA  . ASP B 2 62  ? 257.275 222.629 208.759 1.00 9.31   ? 62   ASP B CA  1 
ATOM   2551 C C   . ASP B 2 62  ? 258.454 221.786 209.230 1.00 9.72   ? 62   ASP B C   1 
ATOM   2552 O O   . ASP B 2 62  ? 258.264 220.730 209.832 1.00 9.84   ? 62   ASP B O   1 
ATOM   2553 C CB  . ASP B 2 62  ? 256.847 222.162 207.367 1.00 9.48   ? 62   ASP B CB  1 
ATOM   2554 C CG  . ASP B 2 62  ? 255.454 222.641 206.970 1.00 9.96   ? 62   ASP B CG  1 
ATOM   2555 O OD1 . ASP B 2 62  ? 254.712 223.057 207.831 1.00 9.99   ? 62   ASP B OD1 1 
ATOM   2556 O OD2 . ASP B 2 62  ? 255.149 222.591 205.806 1.00 9.39   ? 62   ASP B OD2 1 
ATOM   2557 N N   . SER B 2 63  ? 259.669 222.242 208.950 1.00 9.54   ? 63   SER B N   1 
ATOM   2558 C CA  . SER B 2 63  ? 260.869 221.483 209.283 1.00 9.68   ? 63   SER B CA  1 
ATOM   2559 C C   . SER B 2 63  ? 261.180 221.464 210.780 1.00 10.16  ? 63   SER B C   1 
ATOM   2560 O O   . SER B 2 63  ? 261.990 220.655 211.233 1.00 10.80  ? 63   SER B O   1 
ATOM   2561 C CB  . SER B 2 63  ? 262.055 222.043 208.528 1.00 10.21  ? 63   SER B CB  1 
ATOM   2562 O OG  . SER B 2 63  ? 262.397 223.316 209.000 1.00 10.80  ? 63   SER B OG  1 
ATOM   2563 N N   . VAL B 2 64  ? 260.568 222.368 211.542 1.00 10.05  ? 64   VAL B N   1 
ATOM   2564 C CA  . VAL B 2 64  ? 260.816 222.437 212.981 1.00 10.31  ? 64   VAL B CA  1 
ATOM   2565 C C   . VAL B 2 64  ? 259.533 222.249 213.780 1.00 10.04  ? 64   VAL B C   1 
ATOM   2566 O O   . VAL B 2 64  ? 259.560 222.132 215.008 1.00 10.60  ? 64   VAL B O   1 
ATOM   2567 C CB  . VAL B 2 64  ? 261.460 223.781 213.359 1.00 10.31  ? 64   VAL B CB  1 
ATOM   2568 C CG1 . VAL B 2 64  ? 262.785 223.947 212.632 1.00 10.69  ? 64   VAL B CG1 1 
ATOM   2569 C CG2 . VAL B 2 64  ? 260.514 224.916 213.029 1.00 9.35   ? 64   VAL B CG2 1 
ATOM   2570 N N   . LYS B 2 65  ? 258.406 222.243 213.085 1.00 10.02  ? 65   LYS B N   1 
ATOM   2571 C CA  . LYS B 2 65  ? 257.112 222.108 213.730 1.00 9.89   ? 65   LYS B CA  1 
ATOM   2572 C C   . LYS B 2 65  ? 257.047 220.820 214.534 1.00 10.84  ? 65   LYS B C   1 
ATOM   2573 O O   . LYS B 2 65  ? 257.339 219.741 214.021 1.00 11.33  ? 65   LYS B O   1 
ATOM   2574 C CB  . LYS B 2 65  ? 256.008 222.133 212.677 1.00 9.64   ? 65   LYS B CB  1 
ATOM   2575 N N   . GLY B 2 66  ? 256.659 220.939 215.797 1.00 11.14  ? 66   GLY B N   1 
ATOM   2576 C CA  . GLY B 2 66  ? 256.542 219.783 216.678 1.00 10.99  ? 66   GLY B CA  1 
ATOM   2577 C C   . GLY B 2 66  ? 257.789 219.577 217.532 1.00 10.52  ? 66   GLY B C   1 
ATOM   2578 O O   . GLY B 2 66  ? 257.773 218.792 218.479 1.00 11.83  ? 66   GLY B O   1 
ATOM   2579 N N   . ARG B 2 67  ? 258.868 220.281 217.203 1.00 10.82  ? 67   ARG B N   1 
ATOM   2580 C CA  . ARG B 2 67  ? 260.108 220.151 217.958 1.00 10.96  ? 67   ARG B CA  1 
ATOM   2581 C C   . ARG B 2 67  ? 260.498 221.457 218.638 1.00 10.95  ? 67   ARG B C   1 
ATOM   2582 O O   . ARG B 2 67  ? 260.969 221.458 219.776 1.00 11.21  ? 67   ARG B O   1 
ATOM   2583 C CB  . ARG B 2 67  ? 261.246 219.719 217.050 1.00 11.62  ? 67   ARG B CB  1 
ATOM   2584 C CG  . ARG B 2 67  ? 261.110 218.334 216.455 1.00 12.40  ? 67   ARG B CG  1 
ATOM   2585 C CD  . ARG B 2 67  ? 262.362 217.927 215.775 1.00 13.30  ? 67   ARG B CD  1 
ATOM   2586 N NE  . ARG B 2 67  ? 262.652 218.777 214.631 1.00 12.46  ? 67   ARG B NE  1 
ATOM   2587 C CZ  . ARG B 2 67  ? 263.884 219.207 214.281 1.00 13.67  ? 67   ARG B CZ  1 
ATOM   2588 N NH1 . ARG B 2 67  ? 264.036 219.981 213.227 1.00 13.31  ? 67   ARG B NH1 1 
ATOM   2589 N NH2 . ARG B 2 67  ? 264.946 218.860 214.993 1.00 14.52  ? 67   ARG B NH2 1 
ATOM   2590 N N   . PHE B 2 68  ? 260.314 222.569 217.933 1.00 10.52  ? 68   PHE B N   1 
ATOM   2591 C CA  . PHE B 2 68  ? 260.704 223.874 218.457 1.00 10.35  ? 68   PHE B CA  1 
ATOM   2592 C C   . PHE B 2 68  ? 259.514 224.602 219.072 1.00 9.75   ? 68   PHE B C   1 
ATOM   2593 O O   . PHE B 2 68  ? 258.381 224.457 218.614 1.00 9.52   ? 68   PHE B O   1 
ATOM   2594 C CB  . PHE B 2 68  ? 261.301 224.753 217.353 1.00 10.20  ? 68   PHE B CB  1 
ATOM   2595 C CG  . PHE B 2 68  ? 262.667 224.333 216.820 1.00 10.75  ? 68   PHE B CG  1 
ATOM   2596 C CD1 . PHE B 2 68  ? 263.241 223.099 217.114 1.00 11.11  ? 68   PHE B CD1 1 
ATOM   2597 C CD2 . PHE B 2 68  ? 263.372 225.197 215.999 1.00 10.57  ? 68   PHE B CD2 1 
ATOM   2598 C CE1 . PHE B 2 68  ? 264.470 222.751 216.594 1.00 12.17  ? 68   PHE B CE1 1 
ATOM   2599 C CE2 . PHE B 2 68  ? 264.600 224.847 215.483 1.00 11.28  ? 68   PHE B CE2 1 
ATOM   2600 C CZ  . PHE B 2 68  ? 265.148 223.622 215.780 1.00 12.44  ? 68   PHE B CZ  1 
ATOM   2601 N N   . THR B 2 69  ? 259.785 225.404 220.099 1.00 9.78   ? 69   THR B N   1 
ATOM   2602 C CA  . THR B 2 69  ? 258.775 226.271 220.698 1.00 9.55   ? 69   THR B CA  1 
ATOM   2603 C C   . THR B 2 69  ? 259.263 227.716 220.781 1.00 9.20   ? 69   THR B C   1 
ATOM   2604 O O   . THR B 2 69  ? 260.379 227.983 221.225 1.00 9.54   ? 69   THR B O   1 
ATOM   2605 C CB  . THR B 2 69  ? 258.371 225.777 222.100 1.00 9.69   ? 69   THR B CB  1 
ATOM   2606 O OG1 . THR B 2 69  ? 257.800 224.468 221.997 1.00 10.29  ? 69   THR B OG1 1 
ATOM   2607 C CG2 . THR B 2 69  ? 257.352 226.721 222.729 1.00 9.94   ? 69   THR B CG2 1 
ATOM   2608 N N   . ILE B 2 70  ? 258.413 228.650 220.367 1.00 8.74   ? 70   ILE B N   1 
ATOM   2609 C CA  . ILE B 2 70  ? 258.757 230.069 220.411 1.00 8.50   ? 70   ILE B CA  1 
ATOM   2610 C C   . ILE B 2 70  ? 257.987 230.759 221.529 1.00 8.03   ? 70   ILE B C   1 
ATOM   2611 O O   . ILE B 2 70  ? 256.810 230.474 221.747 1.00 7.91   ? 70   ILE B O   1 
ATOM   2612 C CB  . ILE B 2 70  ? 258.462 230.758 219.060 1.00 7.69   ? 70   ILE B CB  1 
ATOM   2613 C CG1 . ILE B 2 70  ? 259.039 232.182 219.054 1.00 7.61   ? 70   ILE B CG1 1 
ATOM   2614 C CG2 . ILE B 2 70  ? 256.963 230.796 218.791 1.00 7.01   ? 70   ILE B CG2 1 
ATOM   2615 C CD1 . ILE B 2 70  ? 259.064 232.828 217.681 1.00 7.41   ? 70   ILE B CD1 1 
ATOM   2616 N N   . SER B 2 71  ? 258.661 231.640 222.256 1.00 7.86   ? 71   SER B N   1 
ATOM   2617 C CA  . SER B 2 71  ? 258.019 232.364 223.346 1.00 7.39   ? 71   SER B CA  1 
ATOM   2618 C C   . SER B 2 71  ? 258.711 233.694 223.597 1.00 7.75   ? 71   SER B C   1 
ATOM   2619 O O   . SER B 2 71  ? 259.791 233.946 223.067 1.00 7.84   ? 71   SER B O   1 
ATOM   2620 C CB  . SER B 2 71  ? 258.022 231.526 224.608 1.00 7.36   ? 71   SER B CB  1 
ATOM   2621 O OG  . SER B 2 71  ? 259.320 231.341 225.086 1.00 8.53   ? 71   SER B OG  1 
ATOM   2622 N N   . ARG B 2 72  ? 258.079 234.552 224.389 1.00 7.50   ? 72   ARG B N   1 
ATOM   2623 C CA  . ARG B 2 72  ? 258.659 235.851 224.707 1.00 7.22   ? 72   ARG B CA  1 
ATOM   2624 C C   . ARG B 2 72  ? 258.199 236.356 226.063 1.00 7.42   ? 72   ARG B C   1 
ATOM   2625 O O   . ARG B 2 72  ? 257.146 235.959 226.561 1.00 8.62   ? 72   ARG B O   1 
ATOM   2626 C CB  . ARG B 2 72  ? 258.288 236.872 223.646 1.00 6.92   ? 72   ARG B CB  1 
ATOM   2627 C CG  . ARG B 2 72  ? 256.802 237.133 223.511 1.00 6.37   ? 72   ARG B CG  1 
ATOM   2628 C CD  . ARG B 2 72  ? 256.493 237.903 222.288 1.00 5.93   ? 72   ARG B CD  1 
ATOM   2629 N NE  . ARG B 2 72  ? 256.870 239.293 222.407 1.00 5.70   ? 72   ARG B NE  1 
ATOM   2630 C CZ  . ARG B 2 72  ? 256.980 240.143 221.376 1.00 5.59   ? 72   ARG B CZ  1 
ATOM   2631 N NH1 . ARG B 2 72  ? 257.294 241.390 221.598 1.00 5.81   ? 72   ARG B NH1 1 
ATOM   2632 N NH2 . ARG B 2 72  ? 256.766 239.737 220.145 1.00 5.54   ? 72   ARG B NH2 1 
ATOM   2633 N N   . ASP B 2 73  ? 258.972 237.271 226.631 1.00 7.60   ? 73   ASP B N   1 
ATOM   2634 C CA  . ASP B 2 73  ? 258.606 237.931 227.876 1.00 7.70   ? 73   ASP B CA  1 
ATOM   2635 C C   . ASP B 2 73  ? 258.764 239.438 227.733 1.00 7.32   ? 73   ASP B C   1 
ATOM   2636 O O   . ASP B 2 73  ? 259.879 239.958 227.662 1.00 8.71   ? 73   ASP B O   1 
ATOM   2637 C CB  . ASP B 2 73  ? 259.452 237.413 229.038 1.00 8.21   ? 73   ASP B CB  1 
ATOM   2638 C CG  . ASP B 2 73  ? 259.005 237.977 230.374 1.00 8.44   ? 73   ASP B CG  1 
ATOM   2639 O OD1 . ASP B 2 73  ? 258.248 238.925 230.368 1.00 8.50   ? 73   ASP B OD1 1 
ATOM   2640 O OD2 . ASP B 2 73  ? 259.419 237.462 231.388 1.00 8.31   ? 73   ASP B OD2 1 
ATOM   2641 N N   . ASN B 2 74  ? 257.639 240.137 227.637 1.00 7.85   ? 74   ASN B N   1 
ATOM   2642 C CA  . ASN B 2 74  ? 257.653 241.558 227.315 1.00 7.67   ? 74   ASN B CA  1 
ATOM   2643 C C   . ASN B 2 74  ? 258.051 242.438 228.492 1.00 7.98   ? 74   ASN B C   1 
ATOM   2644 O O   . ASN B 2 74  ? 258.238 243.642 228.327 1.00 7.94   ? 74   ASN B O   1 
ATOM   2645 C CB  . ASN B 2 74  ? 256.308 241.991 226.768 1.00 7.52   ? 74   ASN B CB  1 
ATOM   2646 C CG  . ASN B 2 74  ? 256.077 241.523 225.358 1.00 6.70   ? 74   ASN B CG  1 
ATOM   2647 O OD1 . ASN B 2 74  ? 257.032 241.236 224.622 1.00 6.57   ? 74   ASN B OD1 1 
ATOM   2648 N ND2 . ASN B 2 74  ? 254.828 241.450 224.970 1.00 5.63   ? 74   ASN B ND2 1 
ATOM   2649 N N   . SER B 2 75  ? 258.186 241.855 229.679 1.00 7.97   ? 75   SER B N   1 
ATOM   2650 C CA  . SER B 2 75  ? 258.594 242.650 230.833 1.00 8.25   ? 75   SER B CA  1 
ATOM   2651 C C   . SER B 2 75  ? 260.113 242.693 230.950 1.00 8.56   ? 75   SER B C   1 
ATOM   2652 O O   . SER B 2 75  ? 260.661 243.453 231.748 1.00 9.22   ? 75   SER B O   1 
ATOM   2653 C CB  . SER B 2 75  ? 257.988 242.108 232.112 1.00 8.17   ? 75   SER B CB  1 
ATOM   2654 O OG  . SER B 2 75  ? 258.579 240.898 232.481 1.00 8.92   ? 75   SER B OG  1 
ATOM   2655 N N   . LYS B 2 76  ? 260.790 241.860 230.163 1.00 8.27   ? 76   LYS B N   1 
ATOM   2656 C CA  . LYS B 2 76  ? 262.245 241.781 230.182 1.00 8.31   ? 76   LYS B CA  1 
ATOM   2657 C C   . LYS B 2 76  ? 262.825 242.090 228.808 1.00 7.96   ? 76   LYS B C   1 
ATOM   2658 O O   . LYS B 2 76  ? 264.039 242.053 228.611 1.00 8.23   ? 76   LYS B O   1 
ATOM   2659 C CB  . LYS B 2 76  ? 262.696 240.394 230.634 1.00 8.21   ? 76   LYS B CB  1 
ATOM   2660 C CG  . LYS B 2 76  ? 262.288 240.030 232.051 1.00 8.47   ? 76   LYS B CG  1 
ATOM   2661 C CD  . LYS B 2 76  ? 262.780 238.642 232.425 1.00 7.75   ? 76   LYS B CD  1 
ATOM   2662 C CE  . LYS B 2 76  ? 262.361 238.268 233.837 1.00 7.93   ? 76   LYS B CE  1 
ATOM   2663 N NZ  . LYS B 2 76  ? 262.774 236.883 234.190 1.00 7.25   ? 76   LYS B NZ  1 
ATOM   2664 N N   . ASN B 2 77  ? 261.941 242.346 227.849 1.00 7.94   ? 77   ASN B N   1 
ATOM   2665 C CA  . ASN B 2 77  ? 262.323 242.542 226.456 1.00 7.74   ? 77   ASN B CA  1 
ATOM   2666 C C   . ASN B 2 77  ? 263.171 241.388 225.934 1.00 7.36   ? 77   ASN B C   1 
ATOM   2667 O O   . ASN B 2 77  ? 264.187 241.601 225.270 1.00 8.24   ? 77   ASN B O   1 
ATOM   2668 C CB  . ASN B 2 77  ? 263.043 243.863 226.275 1.00 7.49   ? 77   ASN B CB  1 
ATOM   2669 C CG  . ASN B 2 77  ? 262.171 245.034 226.594 1.00 7.69   ? 77   ASN B CG  1 
ATOM   2670 O OD1 . ASN B 2 77  ? 260.950 244.989 226.397 1.00 7.89   ? 77   ASN B OD1 1 
ATOM   2671 N ND2 . ASN B 2 77  ? 262.769 246.090 227.080 1.00 7.78   ? 77   ASN B ND2 1 
ATOM   2672 N N   . THR B 2 78  ? 262.759 240.159 226.237 1.00 7.89   ? 78   THR B N   1 
ATOM   2673 C CA  . THR B 2 78  ? 263.529 239.000 225.801 1.00 8.09   ? 78   THR B CA  1 
ATOM   2674 C C   . THR B 2 78  ? 262.709 238.026 224.962 1.00 7.99   ? 78   THR B C   1 
ATOM   2675 O O   . THR B 2 78  ? 261.598 237.639 225.328 1.00 7.95   ? 78   THR B O   1 
ATOM   2676 C CB  . THR B 2 78  ? 264.135 238.247 226.999 1.00 8.30   ? 78   THR B CB  1 
ATOM   2677 O OG1 . THR B 2 78  ? 264.962 239.136 227.756 1.00 8.32   ? 78   THR B OG1 1 
ATOM   2678 C CG2 . THR B 2 78  ? 264.985 237.079 226.516 1.00 8.62   ? 78   THR B CG2 1 
ATOM   2679 N N   . LEU B 2 79  ? 263.291 237.611 223.843 1.00 8.43   ? 79   LEU B N   1 
ATOM   2680 C CA  . LEU B 2 79  ? 262.706 236.612 222.957 1.00 8.41   ? 79   LEU B CA  1 
ATOM   2681 C C   . LEU B 2 79  ? 263.400 235.268 223.169 1.00 8.34   ? 79   LEU B C   1 
ATOM   2682 O O   . LEU B 2 79  ? 264.622 235.215 223.307 1.00 9.44   ? 79   LEU B O   1 
ATOM   2683 C CB  . LEU B 2 79  ? 262.866 237.068 221.500 1.00 8.70   ? 79   LEU B CB  1 
ATOM   2684 C CG  . LEU B 2 79  ? 262.307 236.151 220.408 1.00 8.32   ? 79   LEU B CG  1 
ATOM   2685 C CD1 . LEU B 2 79  ? 260.790 236.194 220.428 1.00 7.76   ? 79   LEU B CD1 1 
ATOM   2686 C CD2 . LEU B 2 79  ? 262.856 236.603 219.069 1.00 7.91   ? 79   LEU B CD2 1 
ATOM   2687 N N   . TYR B 2 80  ? 262.631 234.183 223.206 1.00 8.55   ? 80   TYR B N   1 
ATOM   2688 C CA  . TYR B 2 80  ? 263.208 232.861 223.433 1.00 8.96   ? 80   TYR B CA  1 
ATOM   2689 C C   . TYR B 2 80  ? 262.885 231.869 222.322 1.00 9.09   ? 80   TYR B C   1 
ATOM   2690 O O   . TYR B 2 80  ? 261.810 231.911 221.721 1.00 9.04   ? 80   TYR B O   1 
ATOM   2691 C CB  . TYR B 2 80  ? 262.707 232.278 224.753 1.00 8.85   ? 80   TYR B CB  1 
ATOM   2692 C CG  . TYR B 2 80  ? 263.055 233.074 225.974 1.00 8.80   ? 80   TYR B CG  1 
ATOM   2693 C CD1 . TYR B 2 80  ? 264.285 232.911 226.576 1.00 9.09   ? 80   TYR B CD1 1 
ATOM   2694 C CD2 . TYR B 2 80  ? 262.129 233.951 226.509 1.00 8.48   ? 80   TYR B CD2 1 
ATOM   2695 C CE1 . TYR B 2 80  ? 264.593 233.623 227.713 1.00 8.79   ? 80   TYR B CE1 1 
ATOM   2696 C CE2 . TYR B 2 80  ? 262.435 234.664 227.646 1.00 8.47   ? 80   TYR B CE2 1 
ATOM   2697 C CZ  . TYR B 2 80  ? 263.661 234.501 228.249 1.00 8.81   ? 80   TYR B CZ  1 
ATOM   2698 O OH  . TYR B 2 80  ? 263.965 235.209 229.389 1.00 9.00   ? 80   TYR B OH  1 
ATOM   2699 N N   . LEU B 2 81  ? 263.795 230.920 222.118 1.00 9.72   ? 81   LEU B N   1 
ATOM   2700 C CA  . LEU B 2 81  ? 263.540 229.767 221.260 1.00 9.98   ? 81   LEU B CA  1 
ATOM   2701 C C   . LEU B 2 81  ? 263.994 228.489 221.950 1.00 10.25  ? 81   LEU B C   1 
ATOM   2702 O O   . LEU B 2 81  ? 265.179 228.310 222.236 1.00 10.59  ? 81   LEU B O   1 
ATOM   2703 C CB  . LEU B 2 81  ? 264.264 229.914 219.913 1.00 10.00  ? 81   LEU B CB  1 
ATOM   2704 C CG  . LEU B 2 81  ? 264.149 228.719 218.933 1.00 9.74   ? 81   LEU B CG  1 
ATOM   2705 C CD1 . LEU B 2 81  ? 262.698 228.532 218.511 1.00 9.66   ? 81   LEU B CD1 1 
ATOM   2706 C CD2 . LEU B 2 81  ? 265.030 228.977 217.720 1.00 10.05  ? 81   LEU B CD2 1 
ATOM   2707 N N   . GLN B 2 82  ? 263.051 227.598 222.219 1.00 10.43  ? 82   GLN B N   1 
ATOM   2708 C CA  . GLN B 2 82  ? 263.360 226.349 222.901 1.00 10.85  ? 82   GLN B CA  1 
ATOM   2709 C C   . GLN B 2 82  ? 263.370 225.199 221.913 1.00 10.78  ? 82   GLN B C   1 
ATOM   2710 O O   . GLN B 2 82  ? 262.345 224.879 221.311 1.00 10.98  ? 82   GLN B O   1 
ATOM   2711 C CB  . GLN B 2 82  ? 262.345 226.080 224.014 1.00 10.48  ? 82   GLN B CB  1 
ATOM   2712 C CG  . GLN B 2 82  ? 262.561 224.776 224.770 1.00 10.73  ? 82   GLN B CG  1 
ATOM   2713 C CD  . GLN B 2 82  ? 263.808 224.801 225.635 1.00 11.57  ? 82   GLN B CD  1 
ATOM   2714 O OE1 . GLN B 2 82  ? 263.962 225.668 226.501 1.00 11.81  ? 82   GLN B OE1 1 
ATOM   2715 N NE2 . GLN B 2 82  ? 264.704 223.847 225.410 1.00 11.89  ? 82   GLN B NE2 1 
ATOM   2716 N N   . MET B 2 83  ? 264.533 224.594 221.717 1.00 11.45  ? 83   MET B N   1 
ATOM   2717 C CA  . MET B 2 83  ? 264.653 223.530 220.734 1.00 11.61  ? 83   MET B CA  1 
ATOM   2718 C C   . MET B 2 83  ? 264.847 222.177 221.398 1.00 12.21  ? 83   MET B C   1 
ATOM   2719 O O   . MET B 2 83  ? 265.776 221.989 222.183 1.00 12.66  ? 83   MET B O   1 
ATOM   2720 C CB  . MET B 2 83  ? 265.821 223.823 219.806 1.00 12.13  ? 83   MET B CB  1 
ATOM   2721 C CG  . MET B 2 83  ? 265.763 225.186 219.144 1.00 11.49  ? 83   MET B CG  1 
ATOM   2722 S SD  . MET B 2 83  ? 267.115 225.472 217.991 1.00 12.36  ? 83   MET B SD  1 
ATOM   2723 C CE  . MET B 2 83  ? 268.496 225.674 219.098 1.00 12.19  ? 83   MET B CE  1 
ATOM   2724 N N   . LYS B 2 84  ? 263.990 221.221 221.055 1.00 12.44  ? 84   LYS B N   1 
ATOM   2725 C CA  . LYS B 2 84  ? 264.118 219.863 221.566 1.00 13.30  ? 84   LYS B CA  1 
ATOM   2726 C C   . LYS B 2 84  ? 264.373 218.881 220.434 1.00 13.26  ? 84   LYS B C   1 
ATOM   2727 O O   . LYS B 2 84  ? 264.120 219.184 219.269 1.00 14.28  ? 84   LYS B O   1 
ATOM   2728 C CB  . LYS B 2 84  ? 262.871 219.464 222.353 1.00 12.78  ? 84   LYS B CB  1 
ATOM   2729 C CG  . LYS B 2 84  ? 262.665 220.265 223.630 1.00 13.02  ? 84   LYS B CG  1 
ATOM   2730 C CD  . LYS B 2 84  ? 261.477 219.749 224.424 1.00 14.80  ? 84   LYS B CD  1 
ATOM   2731 C CE  . LYS B 2 84  ? 261.281 220.547 225.706 1.00 14.01  ? 84   LYS B CE  1 
ATOM   2732 N NZ  . LYS B 2 84  ? 260.118 220.053 226.496 1.00 14.05  ? 84   LYS B NZ  1 
ATOM   2733 N N   . SER B 2 85  ? 264.893 217.706 220.776 1.00 13.99  ? 85   SER B N   1 
ATOM   2734 C CA  . SER B 2 85  ? 265.164 216.669 219.787 1.00 14.72  ? 85   SER B CA  1 
ATOM   2735 C C   . SER B 2 85  ? 265.984 217.213 218.624 1.00 15.17  ? 85   SER B C   1 
ATOM   2736 O O   . SER B 2 85  ? 265.622 217.030 217.459 1.00 14.83  ? 85   SER B O   1 
ATOM   2737 C CB  . SER B 2 85  ? 263.866 216.078 219.272 1.00 13.17  ? 85   SER B CB  1 
ATOM   2738 O OG  . SER B 2 85  ? 263.134 215.493 220.314 1.00 13.97  ? 85   SER B OG  1 
ATOM   2739 N N   . LEU B 2 86  ? 267.082 217.890 218.950 1.00 15.31  ? 86   LEU B N   1 
ATOM   2740 C CA  . LEU B 2 86  ? 267.967 218.466 217.942 1.00 15.85  ? 86   LEU B CA  1 
ATOM   2741 C C   . LEU B 2 86  ? 268.685 217.402 217.124 1.00 15.67  ? 86   LEU B C   1 
ATOM   2742 O O   . LEU B 2 86  ? 269.091 216.361 217.644 1.00 15.85  ? 86   LEU B O   1 
ATOM   2743 C CB  . LEU B 2 86  ? 268.982 219.400 218.609 1.00 15.85  ? 86   LEU B CB  1 
ATOM   2744 C CG  . LEU B 2 86  ? 268.423 220.744 219.101 1.00 14.90  ? 86   LEU B CG  1 
ATOM   2745 C CD1 . LEU B 2 86  ? 269.422 221.410 220.021 1.00 14.70  ? 86   LEU B CD1 1 
ATOM   2746 C CD2 . LEU B 2 86  ? 268.158 221.640 217.896 1.00 14.72  ? 86   LEU B CD2 1 
ATOM   2747 N N   . ARG B 2 87  ? 268.840 217.676 215.833 1.00 15.70  ? 87   ARG B N   1 
ATOM   2748 C CA  . ARG B 2 87  ? 269.474 216.755 214.897 1.00 16.01  ? 87   ARG B CA  1 
ATOM   2749 C C   . ARG B 2 87  ? 270.680 217.400 214.227 1.00 15.09  ? 87   ARG B C   1 
ATOM   2750 O O   . ARG B 2 87  ? 270.863 218.613 214.294 1.00 17.61  ? 87   ARG B O   1 
ATOM   2751 C CB  . ARG B 2 87  ? 268.476 216.324 213.835 1.00 16.42  ? 87   ARG B CB  1 
ATOM   2752 C CG  . ARG B 2 87  ? 267.243 215.621 214.371 1.00 16.33  ? 87   ARG B CG  1 
ATOM   2753 C CD  . ARG B 2 87  ? 266.265 215.334 213.298 1.00 16.24  ? 87   ARG B CD  1 
ATOM   2754 N NE  . ARG B 2 87  ? 265.049 214.742 213.826 1.00 15.23  ? 87   ARG B NE  1 
ATOM   2755 C CZ  . ARG B 2 87  ? 263.945 214.479 213.102 1.00 15.56  ? 87   ARG B CZ  1 
ATOM   2756 N NH1 . ARG B 2 87  ? 262.895 213.942 213.683 1.00 15.59  ? 87   ARG B NH1 1 
ATOM   2757 N NH2 . ARG B 2 87  ? 263.915 214.762 211.811 1.00 15.69  ? 87   ARG B NH2 1 
ATOM   2758 N N   . ALA B 2 88  ? 271.499 216.592 213.563 1.00 16.60  ? 88   ALA B N   1 
ATOM   2759 C CA  . ALA B 2 88  ? 272.686 217.106 212.883 1.00 16.98  ? 88   ALA B CA  1 
ATOM   2760 C C   . ALA B 2 88  ? 272.318 218.179 211.859 1.00 16.18  ? 88   ALA B C   1 
ATOM   2761 O O   . ALA B 2 88  ? 273.061 219.141 211.656 1.00 16.06  ? 88   ALA B O   1 
ATOM   2762 C CB  . ALA B 2 88  ? 273.429 215.972 212.199 1.00 17.42  ? 88   ALA B CB  1 
ATOM   2763 N N   . GLU B 2 89  ? 271.159 218.020 211.233 1.00 15.97  ? 89   GLU B N   1 
ATOM   2764 C CA  . GLU B 2 89  ? 270.684 218.935 210.203 1.00 15.83  ? 89   GLU B CA  1 
ATOM   2765 C C   . GLU B 2 89  ? 270.346 220.322 210.747 1.00 15.19  ? 89   GLU B C   1 
ATOM   2766 O O   . GLU B 2 89  ? 270.131 221.258 209.977 1.00 15.24  ? 89   GLU B O   1 
ATOM   2767 C CB  . GLU B 2 89  ? 269.459 218.342 209.506 1.00 15.42  ? 89   GLU B CB  1 
ATOM   2768 N N   . ASP B 2 90  ? 270.272 220.450 212.068 1.00 16.21  ? 90   ASP B N   1 
ATOM   2769 C CA  . ASP B 2 90  ? 269.890 221.709 212.693 1.00 15.04  ? 90   ASP B CA  1 
ATOM   2770 C C   . ASP B 2 90  ? 271.090 222.601 212.978 1.00 14.56  ? 90   ASP B C   1 
ATOM   2771 O O   . ASP B 2 90  ? 270.937 223.680 213.551 1.00 14.27  ? 90   ASP B O   1 
ATOM   2772 C CB  . ASP B 2 90  ? 269.145 221.459 214.006 1.00 14.55  ? 90   ASP B CB  1 
ATOM   2773 C CG  . ASP B 2 90  ? 267.791 220.789 213.833 1.00 14.77  ? 90   ASP B CG  1 
ATOM   2774 O OD1 . ASP B 2 90  ? 267.014 221.212 213.003 1.00 14.57  ? 90   ASP B OD1 1 
ATOM   2775 O OD2 . ASP B 2 90  ? 267.543 219.846 214.546 1.00 14.96  ? 90   ASP B OD2 1 
ATOM   2776 N N   . THR B 2 91  ? 272.283 222.169 212.579 1.00 15.32  ? 91   THR B N   1 
ATOM   2777 C CA  . THR B 2 91  ? 273.457 223.008 212.781 1.00 15.36  ? 91   THR B CA  1 
ATOM   2778 C C   . THR B 2 91  ? 273.349 224.258 211.924 1.00 14.63  ? 91   THR B C   1 
ATOM   2779 O O   . THR B 2 91  ? 273.237 224.175 210.700 1.00 15.01  ? 91   THR B O   1 
ATOM   2780 C CB  . THR B 2 91  ? 274.757 222.254 212.443 1.00 15.52  ? 91   THR B CB  1 
ATOM   2781 O OG1 . THR B 2 91  ? 274.901 221.126 213.321 1.00 15.88  ? 91   THR B OG1 1 
ATOM   2782 C CG2 . THR B 2 91  ? 275.967 223.178 212.582 1.00 16.03  ? 91   THR B CG2 1 
ATOM   2783 N N   . ALA B 2 92  ? 273.365 225.415 212.574 1.00 14.30  ? 92   ALA B N   1 
ATOM   2784 C CA  . ALA B 2 92  ? 273.188 226.682 211.875 1.00 13.40  ? 92   ALA B CA  1 
ATOM   2785 C C   . ALA B 2 92  ? 273.450 227.862 212.791 1.00 12.39  ? 92   ALA B C   1 
ATOM   2786 O O   . ALA B 2 92  ? 273.450 227.720 214.013 1.00 13.38  ? 92   ALA B O   1 
ATOM   2787 C CB  . ALA B 2 92  ? 271.779 226.777 211.308 1.00 12.67  ? 92   ALA B CB  1 
ATOM   2788 N N   . VAL B 2 93  ? 273.608 229.040 212.199 1.00 12.29  ? 93   VAL B N   1 
ATOM   2789 C CA  . VAL B 2 93  ? 273.635 230.273 212.972 1.00 12.07  ? 93   VAL B CA  1 
ATOM   2790 C C   . VAL B 2 93  ? 272.229 230.835 213.093 1.00 11.28  ? 93   VAL B C   1 
ATOM   2791 O O   . VAL B 2 93  ? 271.555 231.060 212.089 1.00 11.54  ? 93   VAL B O   1 
ATOM   2792 C CB  . VAL B 2 93  ? 274.554 231.312 212.311 1.00 11.73  ? 93   VAL B CB  1 
ATOM   2793 C CG1 . VAL B 2 93  ? 274.516 232.620 213.095 1.00 11.37  ? 93   VAL B CG1 1 
ATOM   2794 C CG2 . VAL B 2 93  ? 275.966 230.767 212.257 1.00 12.42  ? 93   VAL B CG2 1 
ATOM   2795 N N   . TYR B 2 94  ? 271.780 231.032 214.323 1.00 11.51  ? 94   TYR B N   1 
ATOM   2796 C CA  . TYR B 2 94  ? 270.429 231.504 214.579 1.00 11.15  ? 94   TYR B CA  1 
ATOM   2797 C C   . TYR B 2 94  ? 270.388 232.998 214.837 1.00 10.65  ? 94   TYR B C   1 
ATOM   2798 O O   . TYR B 2 94  ? 271.129 233.517 215.672 1.00 10.70  ? 94   TYR B O   1 
ATOM   2799 C CB  . TYR B 2 94  ? 269.824 230.747 215.759 1.00 11.30  ? 94   TYR B CB  1 
ATOM   2800 C CG  . TYR B 2 94  ? 269.395 229.346 215.421 1.00 11.58  ? 94   TYR B CG  1 
ATOM   2801 C CD1 . TYR B 2 94  ? 270.333 228.332 215.314 1.00 11.91  ? 94   TYR B CD1 1 
ATOM   2802 C CD2 . TYR B 2 94  ? 268.054 229.072 215.226 1.00 11.64  ? 94   TYR B CD2 1 
ATOM   2803 C CE1 . TYR B 2 94  ? 269.926 227.051 215.006 1.00 12.29  ? 94   TYR B CE1 1 
ATOM   2804 C CE2 . TYR B 2 94  ? 267.649 227.793 214.922 1.00 11.85  ? 94   TYR B CE2 1 
ATOM   2805 C CZ  . TYR B 2 94  ? 268.579 226.787 214.810 1.00 12.06  ? 94   TYR B CZ  1 
ATOM   2806 O OH  . TYR B 2 94  ? 268.170 225.512 214.511 1.00 12.76  ? 94   TYR B OH  1 
ATOM   2807 N N   . TYR B 2 95  ? 269.493 233.679 214.133 1.00 10.44  ? 95   TYR B N   1 
ATOM   2808 C CA  . TYR B 2 95  ? 269.291 235.110 214.290 1.00 9.93   ? 95   TYR B CA  1 
ATOM   2809 C C   . TYR B 2 95  ? 267.901 235.397 214.842 1.00 9.48   ? 95   TYR B C   1 
ATOM   2810 O O   . TYR B 2 95  ? 266.926 234.757 214.440 1.00 9.16   ? 95   TYR B O   1 
ATOM   2811 C CB  . TYR B 2 95  ? 269.397 235.829 212.935 1.00 9.94   ? 95   TYR B CB  1 
ATOM   2812 C CG  . TYR B 2 95  ? 270.732 235.773 212.244 1.00 10.42  ? 95   TYR B CG  1 
ATOM   2813 C CD1 . TYR B 2 95  ? 271.665 236.775 212.452 1.00 10.24  ? 95   TYR B CD1 1 
ATOM   2814 C CD2 . TYR B 2 95  ? 271.011 234.735 211.374 1.00 10.64  ? 95   TYR B CD2 1 
ATOM   2815 C CE1 . TYR B 2 95  ? 272.874 236.733 211.794 1.00 9.91   ? 95   TYR B CE1 1 
ATOM   2816 C CE2 . TYR B 2 95  ? 272.221 234.693 210.718 1.00 10.68  ? 95   TYR B CE2 1 
ATOM   2817 C CZ  . TYR B 2 95  ? 273.149 235.688 210.926 1.00 10.45  ? 95   TYR B CZ  1 
ATOM   2818 O OH  . TYR B 2 95  ? 274.356 235.645 210.272 1.00 12.33  ? 95   TYR B OH  1 
ATOM   2819 N N   . CYS B 2 96  ? 267.798 236.441 215.663 1.00 9.24   ? 96   CYS B N   1 
ATOM   2820 C CA  . CYS B 2 96  ? 266.517 237.051 216.004 1.00 8.69   ? 96   CYS B CA  1 
ATOM   2821 C C   . CYS B 2 96  ? 266.370 238.297 215.143 1.00 8.41   ? 96   CYS B C   1 
ATOM   2822 O O   . CYS B 2 96  ? 267.349 239.003 214.883 1.00 8.64   ? 96   CYS B O   1 
ATOM   2823 C CB  . CYS B 2 96  ? 266.432 237.385 217.504 1.00 8.54   ? 96   CYS B CB  1 
ATOM   2824 S SG  . CYS B 2 96  ? 267.746 238.470 218.124 1.00 9.68   ? 96   CYS B SG  1 
ATOM   2825 N N   . ALA B 2 97  ? 265.161 238.555 214.666 1.00 8.22   ? 97   ALA B N   1 
ATOM   2826 C CA  . ALA B 2 97  ? 264.969 239.683 213.770 1.00 7.62   ? 97   ALA B CA  1 
ATOM   2827 C C   . ALA B 2 97  ? 263.554 240.229 213.808 1.00 7.47   ? 97   ALA B C   1 
ATOM   2828 O O   . ALA B 2 97  ? 262.593 239.518 214.104 1.00 7.21   ? 97   ALA B O   1 
ATOM   2829 C CB  . ALA B 2 97  ? 265.311 239.273 212.345 1.00 8.01   ? 97   ALA B CB  1 
ATOM   2830 N N   . ASN B 2 98  ? 263.437 241.497 213.448 1.00 7.41   ? 98   ASN B N   1 
ATOM   2831 C CA  . ASN B 2 98  ? 262.156 242.149 213.246 1.00 7.22   ? 98   ASN B CA  1 
ATOM   2832 C C   . ASN B 2 98  ? 262.027 242.478 211.770 1.00 7.08   ? 98   ASN B C   1 
ATOM   2833 O O   . ASN B 2 98  ? 262.583 243.470 211.303 1.00 7.27   ? 98   ASN B O   1 
ATOM   2834 C CB  . ASN B 2 98  ? 262.049 243.405 214.092 1.00 6.91   ? 98   ASN B CB  1 
ATOM   2835 C CG  . ASN B 2 98  ? 260.694 244.030 214.020 1.00 6.28   ? 98   ASN B CG  1 
ATOM   2836 O OD1 . ASN B 2 98  ? 259.704 243.332 213.785 1.00 6.56   ? 98   ASN B OD1 1 
ATOM   2837 N ND2 . ASN B 2 98  ? 260.626 245.323 214.218 1.00 6.24   ? 98   ASN B ND2 1 
ATOM   2838 N N   . LEU B 2 99  ? 261.370 241.605 211.019 1.00 7.12   ? 99   LEU B N   1 
ATOM   2839 C CA  . LEU B 2 99  ? 261.359 241.735 209.568 1.00 7.05   ? 99   LEU B CA  1 
ATOM   2840 C C   . LEU B 2 99  ? 260.281 242.705 209.114 1.00 7.12   ? 99   LEU B C   1 
ATOM   2841 O O   . LEU B 2 99  ? 259.175 242.710 209.656 1.00 6.85   ? 99   LEU B O   1 
ATOM   2842 C CB  . LEU B 2 99  ? 261.118 240.364 208.922 1.00 7.26   ? 99   LEU B CB  1 
ATOM   2843 C CG  . LEU B 2 99  ? 262.124 239.251 209.290 1.00 7.58   ? 99   LEU B CG  1 
ATOM   2844 C CD1 . LEU B 2 99  ? 261.686 237.944 208.644 1.00 8.05   ? 99   LEU B CD1 1 
ATOM   2845 C CD2 . LEU B 2 99  ? 263.518 239.639 208.829 1.00 8.35   ? 99   LEU B CD2 1 
ATOM   2846 N N   . LYS B 2 100 ? 260.591 243.502 208.095 1.00 7.13   ? 100  LYS B N   1 
ATOM   2847 C CA  . LYS B 2 100 ? 259.609 244.435 207.553 1.00 6.92   ? 100  LYS B CA  1 
ATOM   2848 C C   . LYS B 2 100 ? 258.480 243.669 206.874 1.00 6.60   ? 100  LYS B C   1 
ATOM   2849 O O   . LYS B 2 100 ? 258.716 242.785 206.048 1.00 7.86   ? 100  LYS B O   1 
ATOM   2850 C CB  . LYS B 2 100 ? 260.279 245.433 206.614 1.00 6.83   ? 100  LYS B CB  1 
ATOM   2851 C CG  . LYS B 2 100 ? 259.367 246.529 206.112 1.00 7.03   ? 100  LYS B CG  1 
ATOM   2852 C CD  . LYS B 2 100 ? 260.164 247.762 205.727 1.00 7.26   ? 100  LYS B CD  1 
ATOM   2853 C CE  . LYS B 2 100 ? 259.268 248.863 205.209 1.00 6.89   ? 100  LYS B CE  1 
ATOM   2854 N NZ  . LYS B 2 100 ? 259.942 250.185 205.260 1.00 6.85   ? 100  LYS B NZ  1 
ATOM   2855 N N   . ASP B 2 101 ? 257.256 243.954 207.307 1.00 6.62   ? 101  ASP B N   1 
ATOM   2856 C CA  . ASP B 2 101 ? 256.094 243.143 206.964 1.00 6.82   ? 101  ASP B CA  1 
ATOM   2857 C C   . ASP B 2 101 ? 254.790 243.930 207.058 1.00 6.27   ? 101  ASP B C   1 
ATOM   2858 O O   . ASP B 2 101 ? 254.348 244.294 208.152 1.00 5.89   ? 101  ASP B O   1 
ATOM   2859 C CB  . ASP B 2 101 ? 256.057 241.927 207.890 1.00 6.91   ? 101  ASP B CB  1 
ATOM   2860 C CG  . ASP B 2 101 ? 254.869 241.018 207.699 1.00 6.79   ? 101  ASP B CG  1 
ATOM   2861 O OD1 . ASP B 2 101 ? 253.956 241.378 206.992 1.00 6.97   ? 101  ASP B OD1 1 
ATOM   2862 O OD2 . ASP B 2 101 ? 254.851 239.986 208.323 1.00 7.22   ? 101  ASP B OD2 1 
ATOM   2863 N N   . SER B 2 102 ? 254.185 244.209 205.906 1.00 6.66   ? 102  SER B N   1 
ATOM   2864 C CA  . SER B 2 102 ? 252.998 245.057 205.837 1.00 6.51   ? 102  SER B CA  1 
ATOM   2865 C C   . SER B 2 102 ? 251.693 244.270 205.914 1.00 6.44   ? 102  SER B C   1 
ATOM   2866 O O   . SER B 2 102 ? 250.620 244.827 205.687 1.00 6.59   ? 102  SER B O   1 
ATOM   2867 C CB  . SER B 2 102 ? 253.005 245.870 204.558 1.00 6.79   ? 102  SER B CB  1 
ATOM   2868 O OG  . SER B 2 102 ? 252.889 245.045 203.436 1.00 8.03   ? 102  SER B OG  1 
ATOM   2869 N N   . ARG B 2 103 ? 251.776 242.971 206.193 1.00 6.65   ? 103  ARG B N   1 
ATOM   2870 C CA  . ARG B 2 103 ? 250.569 242.155 206.268 1.00 7.04   ? 103  ARG B CA  1 
ATOM   2871 C C   . ARG B 2 103 ? 250.322 241.552 207.642 1.00 6.82   ? 103  ARG B C   1 
ATOM   2872 O O   . ARG B 2 103 ? 249.186 241.532 208.115 1.00 6.84   ? 103  ARG B O   1 
ATOM   2873 C CB  . ARG B 2 103 ? 250.607 241.045 205.237 1.00 7.84   ? 103  ARG B CB  1 
ATOM   2874 C CG  . ARG B 2 103 ? 250.381 241.514 203.829 1.00 8.58   ? 103  ARG B CG  1 
ATOM   2875 C CD  . ARG B 2 103 ? 250.448 240.411 202.856 1.00 9.42   ? 103  ARG B CD  1 
ATOM   2876 N NE  . ARG B 2 103 ? 249.486 239.355 203.138 1.00 9.71   ? 103  ARG B NE  1 
ATOM   2877 C CZ  . ARG B 2 103 ? 248.164 239.433 202.898 1.00 10.14  ? 103  ARG B CZ  1 
ATOM   2878 N NH1 . ARG B 2 103 ? 247.395 238.404 203.168 1.00 10.83  ? 103  ARG B NH1 1 
ATOM   2879 N NH2 . ARG B 2 103 ? 247.640 240.536 202.394 1.00 11.11  ? 103  ARG B NH2 1 
ATOM   2880 N N   . TYR B 2 104 ? 251.363 241.020 208.269 1.00 6.62   ? 104  TYR B N   1 
ATOM   2881 C CA  . TYR B 2 104 ? 251.167 240.316 209.532 1.00 6.50   ? 104  TYR B CA  1 
ATOM   2882 C C   . TYR B 2 104 ? 251.700 241.074 210.742 1.00 5.98   ? 104  TYR B C   1 
ATOM   2883 O O   . TYR B 2 104 ? 251.057 241.091 211.791 1.00 6.08   ? 104  TYR B O   1 
ATOM   2884 C CB  . TYR B 2 104 ? 251.784 238.921 209.452 1.00 6.87   ? 104  TYR B CB  1 
ATOM   2885 C CG  . TYR B 2 104 ? 251.095 238.051 208.435 1.00 7.45   ? 104  TYR B CG  1 
ATOM   2886 C CD1 . TYR B 2 104 ? 249.970 237.332 208.790 1.00 7.32   ? 104  TYR B CD1 1 
ATOM   2887 C CD2 . TYR B 2 104 ? 251.568 237.998 207.141 1.00 7.79   ? 104  TYR B CD2 1 
ATOM   2888 C CE1 . TYR B 2 104 ? 249.322 236.564 207.850 1.00 7.73   ? 104  TYR B CE1 1 
ATOM   2889 C CE2 . TYR B 2 104 ? 250.922 237.234 206.204 1.00 8.56   ? 104  TYR B CE2 1 
ATOM   2890 C CZ  . TYR B 2 104 ? 249.802 236.521 206.553 1.00 8.62   ? 104  TYR B CZ  1 
ATOM   2891 O OH  . TYR B 2 104 ? 249.148 235.774 205.608 1.00 9.66   ? 104  TYR B OH  1 
ATOM   2892 N N   . SER B 2 105 ? 252.873 241.681 210.617 1.00 5.84   ? 105  SER B N   1 
ATOM   2893 C CA  . SER B 2 105 ? 253.471 242.346 211.771 1.00 5.30   ? 105  SER B CA  1 
ATOM   2894 C C   . SER B 2 105 ? 253.143 243.833 211.835 1.00 5.44   ? 105  SER B C   1 
ATOM   2895 O O   . SER B 2 105 ? 253.025 244.397 212.922 1.00 5.35   ? 105  SER B O   1 
ATOM   2896 C CB  . SER B 2 105 ? 254.971 242.160 211.767 1.00 5.27   ? 105  SER B CB  1 
ATOM   2897 O OG  . SER B 2 105 ? 255.310 240.807 211.876 1.00 6.51   ? 105  SER B OG  1 
ATOM   2898 N N   . GLY B 2 106 ? 253.016 244.475 210.677 1.00 5.44   ? 106  GLY B N   1 
ATOM   2899 C CA  . GLY B 2 106 ? 252.788 245.914 210.638 1.00 4.87   ? 106  GLY B CA  1 
ATOM   2900 C C   . GLY B 2 106 ? 254.070 246.665 210.974 1.00 4.93   ? 106  GLY B C   1 
ATOM   2901 O O   . GLY B 2 106 ? 254.041 247.727 211.596 1.00 4.97   ? 106  GLY B O   1 
ATOM   2902 N N   . SER B 2 107 ? 255.199 246.080 210.600 1.00 5.13   ? 107  SER B N   1 
ATOM   2903 C CA  . SER B 2 107 ? 256.503 246.655 210.902 1.00 5.20   ? 107  SER B CA  1 
ATOM   2904 C C   . SER B 2 107 ? 257.001 247.512 209.754 1.00 5.68   ? 107  SER B C   1 
ATOM   2905 O O   . SER B 2 107 ? 257.006 247.077 208.603 1.00 5.46   ? 107  SER B O   1 
ATOM   2906 C CB  . SER B 2 107 ? 257.501 245.558 211.197 1.00 5.51   ? 107  SER B CB  1 
ATOM   2907 O OG  . SER B 2 107 ? 257.154 244.874 212.363 1.00 5.89   ? 107  SER B OG  1 
ATOM   2908 N N   . TYR B 2 108 ? 257.430 248.728 210.071 1.00 5.79   ? 108  TYR B N   1 
ATOM   2909 C CA  . TYR B 2 108 ? 257.935 249.654 209.064 1.00 5.78   ? 108  TYR B CA  1 
ATOM   2910 C C   . TYR B 2 108 ? 259.461 249.693 209.060 1.00 5.84   ? 108  TYR B C   1 
ATOM   2911 O O   . TYR B 2 108 ? 260.078 250.355 208.220 1.00 5.93   ? 108  TYR B O   1 
ATOM   2912 C CB  . TYR B 2 108 ? 257.370 251.051 209.320 1.00 5.40   ? 108  TYR B CB  1 
ATOM   2913 C CG  . TYR B 2 108 ? 257.491 251.995 208.157 1.00 5.48   ? 108  TYR B CG  1 
ATOM   2914 C CD1 . TYR B 2 108 ? 256.586 251.920 207.115 1.00 5.38   ? 108  TYR B CD1 1 
ATOM   2915 C CD2 . TYR B 2 108 ? 258.495 252.942 208.135 1.00 5.46   ? 108  TYR B CD2 1 
ATOM   2916 C CE1 . TYR B 2 108 ? 256.684 252.785 206.052 1.00 5.05   ? 108  TYR B CE1 1 
ATOM   2917 C CE2 . TYR B 2 108 ? 258.596 253.810 207.072 1.00 5.32   ? 108  TYR B CE2 1 
ATOM   2918 C CZ  . TYR B 2 108 ? 257.694 253.733 206.031 1.00 5.07   ? 108  TYR B CZ  1 
ATOM   2919 O OH  . TYR B 2 108 ? 257.792 254.600 204.969 1.00 5.35   ? 108  TYR B OH  1 
ATOM   2920 N N   . TYR B 2 109 ? 260.067 248.981 210.004 1.00 5.76   ? 109  TYR B N   1 
ATOM   2921 C CA  . TYR B 2 109 ? 261.515 248.980 210.158 1.00 5.72   ? 109  TYR B CA  1 
ATOM   2922 C C   . TYR B 2 109 ? 262.048 247.556 210.167 1.00 6.45   ? 109  TYR B C   1 
ATOM   2923 O O   . TYR B 2 109 ? 261.357 246.634 210.595 1.00 6.49   ? 109  TYR B O   1 
ATOM   2924 C CB  . TYR B 2 109 ? 261.906 249.703 211.443 1.00 5.89   ? 109  TYR B CB  1 
ATOM   2925 C CG  . TYR B 2 109 ? 261.354 251.101 211.526 1.00 5.90   ? 109  TYR B CG  1 
ATOM   2926 C CD1 . TYR B 2 109 ? 262.030 252.153 210.936 1.00 5.88   ? 109  TYR B CD1 1 
ATOM   2927 C CD2 . TYR B 2 109 ? 260.163 251.330 212.192 1.00 5.81   ? 109  TYR B CD2 1 
ATOM   2928 C CE1 . TYR B 2 109 ? 261.513 253.430 211.010 1.00 5.56   ? 109  TYR B CE1 1 
ATOM   2929 C CE2 . TYR B 2 109 ? 259.647 252.605 212.267 1.00 5.64   ? 109  TYR B CE2 1 
ATOM   2930 C CZ  . TYR B 2 109 ? 260.317 253.651 211.679 1.00 5.50   ? 109  TYR B CZ  1 
ATOM   2931 O OH  . TYR B 2 109 ? 259.801 254.920 211.757 1.00 6.01   ? 109  TYR B OH  1 
ATOM   2932 N N   . ASP B 2 110 ? 263.276 247.375 209.692 1.00 6.83   ? 110  ASP B N   1 
ATOM   2933 C CA  . ASP B 2 110 ? 263.867 246.044 209.609 1.00 7.03   ? 110  ASP B CA  1 
ATOM   2934 C C   . ASP B 2 110 ? 265.120 245.949 210.481 1.00 7.38   ? 110  ASP B C   1 
ATOM   2935 O O   . ASP B 2 110 ? 266.101 246.657 210.249 1.00 7.92   ? 110  ASP B O   1 
ATOM   2936 C CB  . ASP B 2 110 ? 264.197 245.723 208.142 1.00 7.75   ? 110  ASP B CB  1 
ATOM   2937 C CG  . ASP B 2 110 ? 264.530 244.257 207.876 1.00 8.23   ? 110  ASP B CG  1 
ATOM   2938 O OD1 . ASP B 2 110 ? 265.690 243.937 207.761 1.00 8.92   ? 110  ASP B OD1 1 
ATOM   2939 O OD2 . ASP B 2 110 ? 263.611 243.474 207.753 1.00 7.98   ? 110  ASP B OD2 1 
ATOM   2940 N N   . TYR B 2 111 ? 265.070 245.097 211.505 1.00 7.45   ? 111  TYR B N   1 
ATOM   2941 C CA  . TYR B 2 111 ? 266.187 244.954 212.441 1.00 7.71   ? 111  TYR B CA  1 
ATOM   2942 C C   . TYR B 2 111 ? 266.697 243.518 212.500 1.00 7.79   ? 111  TYR B C   1 
ATOM   2943 O O   . TYR B 2 111 ? 265.913 242.572 212.501 1.00 7.96   ? 111  TYR B O   1 
ATOM   2944 C CB  . TYR B 2 111 ? 265.773 245.386 213.850 1.00 7.24   ? 111  TYR B CB  1 
ATOM   2945 C CG  . TYR B 2 111 ? 265.235 246.793 213.950 1.00 7.13   ? 111  TYR B CG  1 
ATOM   2946 C CD1 . TYR B 2 111 ? 265.949 247.858 213.428 1.00 7.27   ? 111  TYR B CD1 1 
ATOM   2947 C CD2 . TYR B 2 111 ? 264.025 247.018 214.588 1.00 7.14   ? 111  TYR B CD2 1 
ATOM   2948 C CE1 . TYR B 2 111 ? 265.451 249.140 213.541 1.00 7.26   ? 111  TYR B CE1 1 
ATOM   2949 C CE2 . TYR B 2 111 ? 263.530 248.298 214.701 1.00 7.03   ? 111  TYR B CE2 1 
ATOM   2950 C CZ  . TYR B 2 111 ? 264.239 249.356 214.180 1.00 6.74   ? 111  TYR B CZ  1 
ATOM   2951 O OH  . TYR B 2 111 ? 263.748 250.634 214.295 1.00 7.30   ? 111  TYR B OH  1 
ATOM   2952 N N   . TRP B 2 112 ? 268.014 243.360 212.606 1.00 8.24   ? 112  TRP B N   1 
ATOM   2953 C CA  . TRP B 2 112 ? 268.630 242.040 212.739 1.00 8.45   ? 112  TRP B CA  1 
ATOM   2954 C C   . TRP B 2 112 ? 269.619 241.994 213.895 1.00 8.69   ? 112  TRP B C   1 
ATOM   2955 O O   . TRP B 2 112 ? 270.261 242.994 214.213 1.00 9.48   ? 112  TRP B O   1 
ATOM   2956 C CB  . TRP B 2 112 ? 269.356 241.652 211.451 1.00 9.04   ? 112  TRP B CB  1 
ATOM   2957 C CG  . TRP B 2 112 ? 268.449 241.358 210.306 1.00 8.86   ? 112  TRP B CG  1 
ATOM   2958 C CD1 . TRP B 2 112 ? 267.771 242.264 209.560 1.00 8.81   ? 112  TRP B CD1 1 
ATOM   2959 C CD2 . TRP B 2 112 ? 268.134 240.062 209.748 1.00 9.52   ? 112  TRP B CD2 1 
ATOM   2960 N NE1 . TRP B 2 112 ? 267.050 241.634 208.590 1.00 9.15   ? 112  TRP B NE1 1 
ATOM   2961 C CE2 . TRP B 2 112 ? 267.264 240.283 208.683 1.00 9.56   ? 112  TRP B CE2 1 
ATOM   2962 C CE3 . TRP B 2 112 ? 268.518 238.753 210.060 1.00 9.92   ? 112  TRP B CE3 1 
ATOM   2963 C CZ2 . TRP B 2 112 ? 266.764 239.244 207.916 1.00 9.74   ? 112  TRP B CZ2 1 
ATOM   2964 C CZ3 . TRP B 2 112 ? 268.016 237.710 209.293 1.00 9.73   ? 112  TRP B CZ3 1 
ATOM   2965 C CH2 . TRP B 2 112 ? 267.162 237.950 208.247 1.00 10.16  ? 112  TRP B CH2 1 
ATOM   2966 N N   . GLY B 2 113 ? 269.771 240.815 214.489 1.00 9.15   ? 113  GLY B N   1 
ATOM   2967 C CA  . GLY B 2 113 ? 270.759 240.600 215.537 1.00 9.44   ? 113  GLY B CA  1 
ATOM   2968 C C   . GLY B 2 113 ? 272.112 240.192 214.963 1.00 9.61   ? 113  GLY B C   1 
ATOM   2969 O O   . GLY B 2 113 ? 272.415 240.468 213.801 1.00 9.91   ? 113  GLY B O   1 
ATOM   2970 N N   . GLN B 2 114 ? 272.944 239.578 215.802 1.00 9.45   ? 114  GLN B N   1 
ATOM   2971 C CA  . GLN B 2 114 ? 274.315 239.246 215.431 1.00 9.76   ? 114  GLN B CA  1 
ATOM   2972 C C   . GLN B 2 114 ? 274.430 237.815 214.928 1.00 9.84   ? 114  GLN B C   1 
ATOM   2973 O O   . GLN B 2 114 ? 275.185 237.532 213.998 1.00 10.54  ? 114  GLN B O   1 
ATOM   2974 C CB  . GLN B 2 114 ? 275.238 239.440 216.635 1.00 8.97   ? 114  GLN B CB  1 
ATOM   2975 C CG  . GLN B 2 114 ? 275.320 240.875 217.132 1.00 9.20   ? 114  GLN B CG  1 
ATOM   2976 C CD  . GLN B 2 114 ? 276.132 241.000 218.407 1.00 9.07   ? 114  GLN B CD  1 
ATOM   2977 O OE1 . GLN B 2 114 ? 276.492 239.997 219.029 1.00 7.80   ? 114  GLN B OE1 1 
ATOM   2978 N NE2 . GLN B 2 114 ? 276.423 242.232 218.804 1.00 7.92   ? 114  GLN B NE2 1 
ATOM   2979 N N   . GLY B 2 115 ? 273.677 236.917 215.554 1.00 10.21  ? 115  GLY B N   1 
ATOM   2980 C CA  . GLY B 2 115 ? 273.683 235.506 215.187 1.00 10.17  ? 115  GLY B CA  1 
ATOM   2981 C C   . GLY B 2 115 ? 274.492 234.658 216.166 1.00 10.76  ? 115  GLY B C   1 
ATOM   2982 O O   . GLY B 2 115 ? 275.644 234.971 216.470 1.00 11.13  ? 115  GLY B O   1 
ATOM   2983 N N   . THR B 2 116 ? 273.893 233.567 216.639 1.00 11.07  ? 116  THR B N   1 
ATOM   2984 C CA  . THR B 2 116 ? 274.574 232.657 217.557 1.00 11.13  ? 116  THR B CA  1 
ATOM   2985 C C   . THR B 2 116 ? 274.641 231.253 216.965 1.00 11.38  ? 116  THR B C   1 
ATOM   2986 O O   . THR B 2 116 ? 273.654 230.744 216.435 1.00 12.65  ? 116  THR B O   1 
ATOM   2987 C CB  . THR B 2 116 ? 273.888 232.623 218.939 1.00 11.06  ? 116  THR B CB  1 
ATOM   2988 O OG1 . THR B 2 116 ? 274.683 231.846 219.841 1.00 11.46  ? 116  THR B OG1 1 
ATOM   2989 C CG2 . THR B 2 116 ? 272.490 232.011 218.852 1.00 11.23  ? 116  THR B CG2 1 
ATOM   2990 N N   . LEU B 2 117 ? 275.818 230.639 217.023 1.00 11.80  ? 117  LEU B N   1 
ATOM   2991 C CA  . LEU B 2 117 ? 276.015 229.339 216.392 1.00 12.41  ? 117  LEU B CA  1 
ATOM   2992 C C   . LEU B 2 117 ? 275.618 228.169 217.280 1.00 13.04  ? 117  LEU B C   1 
ATOM   2993 O O   . LEU B 2 117 ? 276.087 228.036 218.412 1.00 13.06  ? 117  LEU B O   1 
ATOM   2994 C CB  . LEU B 2 117 ? 277.480 229.180 215.965 1.00 12.08  ? 117  LEU B CB  1 
ATOM   2995 C CG  . LEU B 2 117 ? 277.868 227.812 215.354 1.00 13.25  ? 117  LEU B CG  1 
ATOM   2996 C CD1 . LEU B 2 117 ? 277.125 227.593 214.038 1.00 13.53  ? 117  LEU B CD1 1 
ATOM   2997 C CD2 . LEU B 2 117 ? 279.370 227.780 215.131 1.00 11.83  ? 117  LEU B CD2 1 
ATOM   2998 N N   . VAL B 2 118 ? 274.780 227.300 216.726 1.00 13.30  ? 118  VAL B N   1 
ATOM   2999 C CA  . VAL B 2 118 ? 274.371 226.071 217.384 1.00 14.07  ? 118  VAL B CA  1 
ATOM   3000 C C   . VAL B 2 118 ? 274.869 224.865 216.605 1.00 14.05  ? 118  VAL B C   1 
ATOM   3001 O O   . VAL B 2 118 ? 274.552 224.701 215.426 1.00 15.70  ? 118  VAL B O   1 
ATOM   3002 C CB  . VAL B 2 118 ? 272.839 226.012 217.498 1.00 12.94  ? 118  VAL B CB  1 
ATOM   3003 C CG1 . VAL B 2 118 ? 272.407 224.695 218.134 1.00 14.28  ? 118  VAL B CG1 1 
ATOM   3004 C CG2 . VAL B 2 118 ? 272.357 227.195 218.314 1.00 13.08  ? 118  VAL B CG2 1 
ATOM   3005 N N   . THR B 2 119 ? 275.649 224.018 217.266 1.00 15.12  ? 119  THR B N   1 
ATOM   3006 C CA  . THR B 2 119 ? 276.204 222.837 216.618 1.00 16.13  ? 119  THR B CA  1 
ATOM   3007 C C   . THR B 2 119 ? 275.717 221.559 217.272 1.00 15.21  ? 119  THR B C   1 
ATOM   3008 O O   . THR B 2 119 ? 275.760 221.419 218.494 1.00 17.27  ? 119  THR B O   1 
ATOM   3009 C CB  . THR B 2 119 ? 277.743 222.865 216.643 1.00 16.18  ? 119  THR B CB  1 
ATOM   3010 O OG1 . THR B 2 119 ? 278.211 224.014 215.931 1.00 16.56  ? 119  THR B OG1 1 
ATOM   3011 C CG2 . THR B 2 119 ? 278.314 221.608 216.002 1.00 16.30  ? 119  THR B CG2 1 
ATOM   3012 N N   . VAL B 2 120 ? 275.267 220.619 216.452 1.00 16.24  ? 120  VAL B N   1 
ATOM   3013 C CA  . VAL B 2 120 ? 274.838 219.323 216.955 1.00 16.59  ? 120  VAL B CA  1 
ATOM   3014 C C   . VAL B 2 120 ? 275.843 218.251 216.535 1.00 16.84  ? 120  VAL B C   1 
ATOM   3015 O O   . VAL B 2 120 ? 276.101 218.073 215.344 1.00 17.80  ? 120  VAL B O   1 
ATOM   3016 C CB  . VAL B 2 120 ? 273.435 218.979 216.426 1.00 16.68  ? 120  VAL B CB  1 
ATOM   3017 C CG1 . VAL B 2 120 ? 272.993 217.626 216.964 1.00 15.88  ? 120  VAL B CG1 1 
ATOM   3018 C CG2 . VAL B 2 120 ? 272.459 220.066 216.837 1.00 15.84  ? 120  VAL B CG2 1 
ATOM   3019 N N   . SER B 2 121 ? 276.440 217.574 217.523 1.00 16.61  ? 121  SER B N   1 
ATOM   3020 C CA  . SER B 2 121 ? 277.512 216.604 217.286 1.00 16.52  ? 121  SER B CA  1 
ATOM   3021 C C   . SER B 2 121 ? 277.505 215.502 218.340 1.00 17.22  ? 121  SER B C   1 
ATOM   3022 O O   . SER B 2 121 ? 277.206 214.345 218.038 1.00 17.84  ? 121  SER B O   1 
ATOM   3023 C CB  . SER B 2 121 ? 278.863 217.312 217.281 1.00 16.69  ? 121  SER B CB  1 
ATOM   3024 O OG  . SER B 2 121 ? 279.913 216.403 217.093 1.00 16.85  ? 121  SER B OG  1 
ATOM   3025 N N   . ILE C 3 2   ? 254.323 228.095 199.851 1.00 14.72  ? 2    ILE C N   1 
ATOM   3026 C CA  . ILE C 3 2   ? 254.775 228.849 198.687 1.00 13.99  ? 2    ILE C CA  1 
ATOM   3027 C C   . ILE C 3 2   ? 256.267 228.589 198.465 1.00 14.86  ? 2    ILE C C   1 
ATOM   3028 O O   . ILE C 3 2   ? 257.088 228.874 199.340 1.00 14.87  ? 2    ILE C O   1 
ATOM   3029 C CB  . ILE C 3 2   ? 254.511 230.382 198.863 1.00 13.42  ? 2    ILE C CB  1 
ATOM   3030 N N   . TRP C 3 3   ? 256.611 228.047 197.292 1.00 15.19  ? 3    TRP C N   1 
ATOM   3031 C CA  . TRP C 3 3   ? 257.998 227.780 196.920 1.00 16.28  ? 3    TRP C CA  1 
ATOM   3032 C C   . TRP C 3 3   ? 258.602 228.974 196.197 1.00 15.57  ? 3    TRP C C   1 
ATOM   3033 O O   . TRP C 3 3   ? 257.942 229.614 195.376 1.00 15.67  ? 3    TRP C O   1 
ATOM   3034 C CB  . TRP C 3 3   ? 258.082 226.542 196.032 1.00 16.12  ? 3    TRP C CB  1 
ATOM   3035 N N   . MET C 3 4   ? 259.862 229.265 196.497 1.00 15.81  ? 4    MET C N   1 
ATOM   3036 C CA  . MET C 3 4   ? 260.561 230.376 195.865 1.00 16.04  ? 4    MET C CA  1 
ATOM   3037 C C   . MET C 3 4   ? 261.780 229.883 195.103 1.00 16.36  ? 4    MET C C   1 
ATOM   3038 O O   . MET C 3 4   ? 262.462 228.954 195.539 1.00 16.58  ? 4    MET C O   1 
ATOM   3039 C CB  . MET C 3 4   ? 260.975 231.399 196.920 1.00 15.91  ? 4    MET C CB  1 
ATOM   3040 C CG  . MET C 3 4   ? 259.825 231.947 197.760 1.00 14.68  ? 4    MET C CG  1 
ATOM   3041 S SD  . MET C 3 4   ? 258.652 232.932 196.810 1.00 15.51  ? 4    MET C SD  1 
ATOM   3042 C CE  . MET C 3 4   ? 259.613 234.398 196.472 1.00 14.33  ? 4    MET C CE  1 
ATOM   3043 N N   . THR C 3 5   ? 262.071 230.526 193.980 1.00 16.23  ? 5    THR C N   1 
ATOM   3044 C CA  . THR C 3 5   ? 263.262 230.199 193.206 1.00 16.58  ? 5    THR C CA  1 
ATOM   3045 C C   . THR C 3 5   ? 263.879 231.455 192.607 1.00 16.39  ? 5    THR C C   1 
ATOM   3046 O O   . THR C 3 5   ? 263.190 232.450 192.385 1.00 18.18  ? 5    THR C O   1 
ATOM   3047 C CB  . THR C 3 5   ? 262.942 229.184 192.093 1.00 17.26  ? 5    THR C CB  1 
ATOM   3048 O OG1 . THR C 3 5   ? 264.160 228.754 191.479 1.00 18.55  ? 5    THR C OG1 1 
ATOM   3049 C CG2 . THR C 3 5   ? 262.044 229.808 191.041 1.00 17.29  ? 5    THR C CG2 1 
ATOM   3050 N N   . GLN C 3 6   ? 265.181 231.411 192.354 1.00 16.61  ? 6    GLN C N   1 
ATOM   3051 C CA  . GLN C 3 6   ? 265.881 232.544 191.763 1.00 17.46  ? 6    GLN C CA  1 
ATOM   3052 C C   . GLN C 3 6   ? 266.791 232.103 190.625 1.00 18.47  ? 6    GLN C C   1 
ATOM   3053 O O   . GLN C 3 6   ? 267.286 230.975 190.614 1.00 18.63  ? 6    GLN C O   1 
ATOM   3054 C CB  . GLN C 3 6   ? 266.678 233.305 192.827 1.00 16.74  ? 6    GLN C CB  1 
ATOM   3055 C CG  . GLN C 3 6   ? 265.808 234.040 193.843 1.00 16.41  ? 6    GLN C CG  1 
ATOM   3056 C CD  . GLN C 3 6   ? 266.616 234.805 194.885 1.00 15.43  ? 6    GLN C CD  1 
ATOM   3057 O OE1 . GLN C 3 6   ? 266.526 234.528 196.089 1.00 15.00  ? 6    GLN C OE1 1 
ATOM   3058 N NE2 . GLN C 3 6   ? 267.407 235.771 194.429 1.00 15.68  ? 6    GLN C NE2 1 
ATOM   3059 N N   . SER C 3 7   ? 267.005 233.000 189.668 1.00 18.44  ? 7    SER C N   1 
ATOM   3060 C CA  . SER C 3 7   ? 267.845 232.707 188.514 1.00 19.30  ? 7    SER C CA  1 
ATOM   3061 C C   . SER C 3 7   ? 268.534 233.965 187.987 1.00 19.33  ? 7    SER C C   1 
ATOM   3062 O O   . SER C 3 7   ? 267.925 235.034 187.926 1.00 19.23  ? 7    SER C O   1 
ATOM   3063 C CB  . SER C 3 7   ? 267.007 232.087 187.413 1.00 19.86  ? 7    SER C CB  1 
ATOM   3064 N N   . PRO C 3 8   ? 269.809 233.849 187.615 1.00 20.26  ? 8    PRO C N   1 
ATOM   3065 C CA  . PRO C 3 8   ? 270.684 232.690 187.664 1.00 20.22  ? 8    PRO C CA  1 
ATOM   3066 C C   . PRO C 3 8   ? 271.121 232.417 189.090 1.00 19.71  ? 8    PRO C C   1 
ATOM   3067 O O   . PRO C 3 8   ? 271.006 233.290 189.945 1.00 19.95  ? 8    PRO C O   1 
ATOM   3068 C CB  . PRO C 3 8   ? 271.855 233.139 186.788 1.00 20.63  ? 8    PRO C CB  1 
ATOM   3069 C CG  . PRO C 3 8   ? 271.898 234.636 186.972 1.00 20.86  ? 8    PRO C CG  1 
ATOM   3070 C CD  . PRO C 3 8   ? 270.444 235.056 187.102 1.00 19.33  ? 8    PRO C CD  1 
ATOM   3071 N N   . SER C 3 9   ? 271.643 231.222 189.347 1.00 20.48  ? 9    SER C N   1 
ATOM   3072 C CA  . SER C 3 9   ? 272.160 230.910 190.675 1.00 21.27  ? 9    SER C CA  1 
ATOM   3073 C C   . SER C 3 9   ? 273.373 231.773 190.998 1.00 20.48  ? 9    SER C C   1 
ATOM   3074 O O   . SER C 3 9   ? 273.625 232.104 192.159 1.00 19.97  ? 9    SER C O   1 
ATOM   3075 C CB  . SER C 3 9   ? 272.542 229.447 190.752 1.00 20.86  ? 9    SER C CB  1 
ATOM   3076 N N   . SER C 3 10  ? 274.110 232.151 189.960 1.00 21.96  ? 10   SER C N   1 
ATOM   3077 C CA  . SER C 3 10  ? 275.260 233.026 190.111 1.00 21.35  ? 10   SER C CA  1 
ATOM   3078 C C   . SER C 3 10  ? 275.549 233.763 188.813 1.00 22.05  ? 10   SER C C   1 
ATOM   3079 O O   . SER C 3 10  ? 275.261 233.263 187.724 1.00 21.72  ? 10   SER C O   1 
ATOM   3080 C CB  . SER C 3 10  ? 276.478 232.228 190.534 1.00 21.55  ? 10   SER C CB  1 
ATOM   3081 O OG  . SER C 3 10  ? 276.875 231.342 189.525 1.00 21.76  ? 10   SER C OG  1 
ATOM   3082 N N   . LEU C 3 11  ? 276.153 234.937 188.934 1.00 23.49  ? 11   LEU C N   1 
ATOM   3083 C CA  . LEU C 3 11  ? 276.579 235.717 187.781 1.00 23.63  ? 11   LEU C CA  1 
ATOM   3084 C C   . LEU C 3 11  ? 277.794 236.554 188.141 1.00 22.93  ? 11   LEU C C   1 
ATOM   3085 O O   . LEU C 3 11  ? 278.048 236.804 189.320 1.00 23.61  ? 11   LEU C O   1 
ATOM   3086 C CB  . LEU C 3 11  ? 275.439 236.626 187.296 1.00 23.22  ? 11   LEU C CB  1 
ATOM   3087 C CG  . LEU C 3 11  ? 275.006 237.748 188.261 1.00 23.31  ? 11   LEU C CG  1 
ATOM   3088 C CD1 . LEU C 3 11  ? 275.708 239.054 187.877 1.00 23.17  ? 11   LEU C CD1 1 
ATOM   3089 C CD2 . LEU C 3 11  ? 273.490 237.913 188.210 1.00 23.46  ? 11   LEU C CD2 1 
ATOM   3090 N N   . SER C 3 12  ? 278.523 237.014 187.135 1.00 23.43  ? 12   SER C N   1 
ATOM   3091 C CA  . SER C 3 12  ? 279.636 237.924 187.371 1.00 24.93  ? 12   SER C CA  1 
ATOM   3092 C C   . SER C 3 12  ? 279.574 239.093 186.405 1.00 25.11  ? 12   SER C C   1 
ATOM   3093 O O   . SER C 3 12  ? 279.208 238.929 185.241 1.00 24.74  ? 12   SER C O   1 
ATOM   3094 C CB  . SER C 3 12  ? 280.951 237.193 187.206 1.00 25.61  ? 12   SER C CB  1 
ATOM   3095 O OG  . SER C 3 12  ? 281.100 236.725 185.893 1.00 25.95  ? 12   SER C OG  1 
ATOM   3096 N N   . ALA C 3 13  ? 279.951 240.272 186.885 1.00 26.09  ? 13   ALA C N   1 
ATOM   3097 C CA  . ALA C 3 13  ? 279.957 241.458 186.039 1.00 26.36  ? 13   ALA C CA  1 
ATOM   3098 C C   . ALA C 3 13  ? 280.963 242.482 186.549 1.00 25.78  ? 13   ALA C C   1 
ATOM   3099 O O   . ALA C 3 13  ? 281.313 242.485 187.729 1.00 26.09  ? 13   ALA C O   1 
ATOM   3100 C CB  . ALA C 3 13  ? 278.563 242.058 185.976 1.00 24.81  ? 13   ALA C CB  1 
ATOM   3101 N N   . SER C 3 14  ? 281.433 243.343 185.654 1.00 25.17  ? 14   SER C N   1 
ATOM   3102 C CA  . SER C 3 14  ? 282.407 244.367 186.013 1.00 24.87  ? 14   SER C CA  1 
ATOM   3103 C C   . SER C 3 14  ? 281.729 245.659 186.435 1.00 25.27  ? 14   SER C C   1 
ATOM   3104 O O   . SER C 3 14  ? 280.506 245.791 186.360 1.00 25.82  ? 14   SER C O   1 
ATOM   3105 C CB  . SER C 3 14  ? 283.361 244.624 184.861 1.00 26.51  ? 14   SER C CB  1 
ATOM   3106 O OG  . SER C 3 14  ? 282.701 245.198 183.771 1.00 26.01  ? 14   SER C OG  1 
ATOM   3107 N N   . VAL C 3 15  ? 282.524 246.608 186.906 1.00 26.38  ? 15   VAL C N   1 
ATOM   3108 C CA  . VAL C 3 15  ? 281.975 247.866 187.375 1.00 26.18  ? 15   VAL C CA  1 
ATOM   3109 C C   . VAL C 3 15  ? 281.383 248.654 186.219 1.00 25.45  ? 15   VAL C C   1 
ATOM   3110 O O   . VAL C 3 15  ? 282.027 248.838 185.186 1.00 24.75  ? 15   VAL C O   1 
ATOM   3111 C CB  . VAL C 3 15  ? 283.066 248.693 188.079 1.00 25.97  ? 15   VAL C CB  1 
ATOM   3112 C CG1 . VAL C 3 15  ? 282.526 250.063 188.484 1.00 26.01  ? 15   VAL C CG1 1 
ATOM   3113 C CG2 . VAL C 3 15  ? 283.553 247.928 189.295 1.00 25.44  ? 15   VAL C CG2 1 
ATOM   3114 N N   . GLY C 3 16  ? 280.149 249.107 186.398 1.00 25.23  ? 16   GLY C N   1 
ATOM   3115 C CA  . GLY C 3 16  ? 279.439 249.863 185.374 1.00 25.23  ? 16   GLY C CA  1 
ATOM   3116 C C   . GLY C 3 16  ? 278.435 248.999 184.615 1.00 24.97  ? 16   GLY C C   1 
ATOM   3117 O O   . GLY C 3 16  ? 277.571 249.519 183.911 1.00 25.06  ? 16   GLY C O   1 
ATOM   3118 N N   . ASP C 3 17  ? 278.543 247.682 184.765 1.00 25.25  ? 17   ASP C N   1 
ATOM   3119 C CA  . ASP C 3 17  ? 277.628 246.765 184.098 1.00 25.27  ? 17   ASP C CA  1 
ATOM   3120 C C   . ASP C 3 17  ? 276.247 246.787 184.734 1.00 24.31  ? 17   ASP C C   1 
ATOM   3121 O O   . ASP C 3 17  ? 276.103 247.070 185.923 1.00 24.07  ? 17   ASP C O   1 
ATOM   3122 C CB  . ASP C 3 17  ? 278.170 245.336 184.126 1.00 25.01  ? 17   ASP C CB  1 
ATOM   3123 C CG  . ASP C 3 17  ? 279.295 245.084 183.118 1.00 24.69  ? 17   ASP C CG  1 
ATOM   3124 O OD1 . ASP C 3 17  ? 279.445 245.869 182.213 1.00 27.88  ? 17   ASP C OD1 1 
ATOM   3125 O OD2 . ASP C 3 17  ? 279.990 244.100 183.265 1.00 26.60  ? 17   ASP C OD2 1 
ATOM   3126 N N   . ARG C 3 18  ? 275.235 246.465 183.938 1.00 24.51  ? 18   ARG C N   1 
ATOM   3127 C CA  . ARG C 3 18  ? 273.873 246.351 184.440 1.00 23.64  ? 18   ARG C CA  1 
ATOM   3128 C C   . ARG C 3 18  ? 273.571 244.912 184.834 1.00 22.73  ? 18   ARG C C   1 
ATOM   3129 O O   . ARG C 3 18  ? 273.758 243.988 184.042 1.00 23.70  ? 18   ARG C O   1 
ATOM   3130 C CB  . ARG C 3 18  ? 272.874 246.828 183.398 1.00 23.65  ? 18   ARG C CB  1 
ATOM   3131 C CG  . ARG C 3 18  ? 271.422 246.784 183.833 1.00 23.10  ? 18   ARG C CG  1 
ATOM   3132 C CD  . ARG C 3 18  ? 270.545 247.487 182.865 1.00 23.24  ? 18   ARG C CD  1 
ATOM   3133 N NE  . ARG C 3 18  ? 269.152 247.469 183.280 1.00 23.11  ? 18   ARG C NE  1 
ATOM   3134 C CZ  . ARG C 3 18  ? 268.251 246.528 182.926 1.00 24.22  ? 18   ARG C CZ  1 
ATOM   3135 N NH1 . ARG C 3 18  ? 267.013 246.612 183.360 1.00 24.42  ? 18   ARG C NH1 1 
ATOM   3136 N NH2 . ARG C 3 18  ? 268.609 245.522 182.144 1.00 23.88  ? 18   ARG C NH2 1 
ATOM   3137 N N   . VAL C 3 19  ? 273.126 244.725 186.070 1.00 22.02  ? 19   VAL C N   1 
ATOM   3138 C CA  . VAL C 3 19  ? 272.867 243.390 186.596 1.00 22.35  ? 19   VAL C CA  1 
ATOM   3139 C C   . VAL C 3 19  ? 271.402 243.174 186.935 1.00 21.13  ? 19   VAL C C   1 
ATOM   3140 O O   . VAL C 3 19  ? 270.810 243.937 187.697 1.00 21.17  ? 19   VAL C O   1 
ATOM   3141 C CB  . VAL C 3 19  ? 273.718 243.142 187.856 1.00 22.15  ? 19   VAL C CB  1 
ATOM   3142 C CG1 . VAL C 3 19  ? 273.376 241.791 188.468 1.00 22.61  ? 19   VAL C CG1 1 
ATOM   3143 C CG2 . VAL C 3 19  ? 275.195 243.198 187.489 1.00 23.19  ? 19   VAL C CG2 1 
ATOM   3144 N N   . THR C 3 20  ? 270.824 242.107 186.393 1.00 20.82  ? 20   THR C N   1 
ATOM   3145 C CA  . THR C 3 20  ? 269.438 241.771 186.692 1.00 19.86  ? 20   THR C CA  1 
ATOM   3146 C C   . THR C 3 20  ? 269.326 240.392 187.327 1.00 19.72  ? 20   THR C C   1 
ATOM   3147 O O   . THR C 3 20  ? 269.978 239.440 186.896 1.00 20.13  ? 20   THR C O   1 
ATOM   3148 C CB  . THR C 3 20  ? 268.568 241.820 185.425 1.00 19.98  ? 20   THR C CB  1 
ATOM   3149 O OG1 . THR C 3 20  ? 269.090 240.907 184.452 1.00 21.19  ? 20   THR C OG1 1 
ATOM   3150 C CG2 . THR C 3 20  ? 268.562 243.224 184.846 1.00 20.93  ? 20   THR C CG2 1 
ATOM   3151 N N   . ILE C 3 21  ? 268.469 240.292 188.338 1.00 18.52  ? 21   ILE C N   1 
ATOM   3152 C CA  . ILE C 3 21  ? 268.205 239.039 189.036 1.00 18.60  ? 21   ILE C CA  1 
ATOM   3153 C C   . ILE C 3 21  ? 266.717 238.710 189.006 1.00 16.89  ? 21   ILE C C   1 
ATOM   3154 O O   . ILE C 3 21  ? 265.878 239.556 189.321 1.00 18.21  ? 21   ILE C O   1 
ATOM   3155 C CB  . ILE C 3 21  ? 268.694 239.112 190.496 1.00 18.25  ? 21   ILE C CB  1 
ATOM   3156 C CG1 . ILE C 3 21  ? 270.207 239.394 190.522 1.00 19.05  ? 21   ILE C CG1 1 
ATOM   3157 C CG2 . ILE C 3 21  ? 268.358 237.811 191.230 1.00 19.10  ? 21   ILE C CG2 1 
ATOM   3158 C CD1 . ILE C 3 21  ? 270.758 239.697 191.900 1.00 19.09  ? 21   ILE C CD1 1 
ATOM   3159 N N   . THR C 3 22  ? 266.388 237.483 188.620 1.00 18.14  ? 22   THR C N   1 
ATOM   3160 C CA  . THR C 3 22  ? 264.994 237.065 188.528 1.00 17.96  ? 22   THR C CA  1 
ATOM   3161 C C   . THR C 3 22  ? 264.572 236.229 189.737 1.00 16.47  ? 22   THR C C   1 
ATOM   3162 O O   . THR C 3 22  ? 265.279 235.301 190.133 1.00 18.51  ? 22   THR C O   1 
ATOM   3163 C CB  . THR C 3 22  ? 264.754 236.260 187.233 1.00 18.38  ? 22   THR C CB  1 
ATOM   3164 O OG1 . THR C 3 22  ? 265.050 237.083 186.097 1.00 18.74  ? 22   THR C OG1 1 
ATOM   3165 C CG2 . THR C 3 22  ? 263.307 235.790 187.148 1.00 18.50  ? 22   THR C CG2 1 
ATOM   3166 N N   . CYS C 3 23  ? 263.398 236.545 190.297 1.00 16.77  ? 23   CYS C N   1 
ATOM   3167 C CA  . CYS C 3 23  ? 262.782 235.781 191.378 1.00 16.76  ? 23   CYS C CA  1 
ATOM   3168 C C   . CYS C 3 23  ? 261.367 235.359 190.993 1.00 16.03  ? 23   CYS C C   1 
ATOM   3169 O O   . CYS C 3 23  ? 260.593 236.153 190.459 1.00 16.05  ? 23   CYS C O   1 
ATOM   3170 C CB  . CYS C 3 23  ? 262.743 236.593 192.679 1.00 16.60  ? 23   CYS C CB  1 
ATOM   3171 S SG  . CYS C 3 23  ? 261.917 235.755 194.066 1.00 17.15  ? 23   CYS C SG  1 
ATOM   3172 N N   . GLN C 3 24  ? 261.047 234.100 191.250 1.00 17.13  ? 24   GLN C N   1 
ATOM   3173 C CA  . GLN C 3 24  ? 259.735 233.572 190.908 1.00 17.05  ? 24   GLN C CA  1 
ATOM   3174 C C   . GLN C 3 24  ? 259.086 232.864 192.087 1.00 16.06  ? 24   GLN C C   1 
ATOM   3175 O O   . GLN C 3 24  ? 259.768 232.334 192.966 1.00 16.44  ? 24   GLN C O   1 
ATOM   3176 C CB  . GLN C 3 24  ? 259.834 232.616 189.718 1.00 16.55  ? 24   GLN C CB  1 
ATOM   3177 C CG  . GLN C 3 24  ? 260.320 233.263 188.439 1.00 16.67  ? 24   GLN C CG  1 
ATOM   3178 C CD  . GLN C 3 24  ? 260.409 232.276 187.296 1.00 17.18  ? 24   GLN C CD  1 
ATOM   3179 O OE1 . GLN C 3 24  ? 261.102 231.259 187.393 1.00 17.46  ? 24   GLN C OE1 1 
ATOM   3180 N NE2 . GLN C 3 24  ? 259.708 232.566 186.206 1.00 17.21  ? 24   GLN C NE2 1 
ATOM   3181 N N   . ALA C 3 25  ? 257.757 232.850 192.093 1.00 16.04  ? 25   ALA C N   1 
ATOM   3182 C CA  . ALA C 3 25  ? 257.004 232.166 193.137 1.00 15.81  ? 25   ALA C CA  1 
ATOM   3183 C C   . ALA C 3 25  ? 256.041 231.154 192.532 1.00 15.84  ? 25   ALA C C   1 
ATOM   3184 O O   . ALA C 3 25  ? 255.477 231.382 191.462 1.00 15.59  ? 25   ALA C O   1 
ATOM   3185 C CB  . ALA C 3 25  ? 256.240 233.176 193.981 1.00 15.28  ? 25   ALA C CB  1 
ATOM   3186 N N   . SER C 3 26  ? 255.828 230.050 193.241 1.00 15.85  ? 26   SER C N   1 
ATOM   3187 C CA  . SER C 3 26  ? 254.892 229.017 192.805 1.00 15.24  ? 26   SER C CA  1 
ATOM   3188 C C   . SER C 3 26  ? 253.442 229.465 192.945 1.00 15.49  ? 26   SER C C   1 
ATOM   3189 O O   . SER C 3 26  ? 252.537 228.854 192.378 1.00 15.95  ? 26   SER C O   1 
ATOM   3190 C CB  . SER C 3 26  ? 255.113 227.749 193.603 1.00 15.93  ? 26   SER C CB  1 
ATOM   3191 O OG  . SER C 3 26  ? 254.723 227.921 194.938 1.00 15.22  ? 26   SER C OG  1 
ATOM   3192 N N   . GLN C 3 27  ? 253.224 230.520 193.718 1.00 15.03  ? 27   GLN C N   1 
ATOM   3193 C CA  . GLN C 3 27  ? 251.889 231.063 193.927 1.00 15.24  ? 27   GLN C CA  1 
ATOM   3194 C C   . GLN C 3 27  ? 251.882 232.566 193.716 1.00 14.33  ? 27   GLN C C   1 
ATOM   3195 O O   . GLN C 3 27  ? 252.907 233.228 193.869 1.00 14.89  ? 27   GLN C O   1 
ATOM   3196 C CB  . GLN C 3 27  ? 251.368 230.739 195.327 1.00 14.22  ? 27   GLN C CB  1 
ATOM   3197 C CG  . GLN C 3 27  ? 251.174 229.258 195.598 1.00 14.13  ? 27   GLN C CG  1 
ATOM   3198 C CD  . GLN C 3 27  ? 250.474 229.002 196.918 1.00 13.90  ? 27   GLN C CD  1 
ATOM   3199 O OE1 . GLN C 3 27  ? 249.996 229.936 197.568 1.00 12.12  ? 27   GLN C OE1 1 
ATOM   3200 N NE2 . GLN C 3 27  ? 250.410 227.740 197.323 1.00 13.77  ? 27   GLN C NE2 1 
ATOM   3201 N N   . ASP C 3 28  ? 250.718 233.104 193.383 1.00 14.19  ? 28   ASP C N   1 
ATOM   3202 C CA  . ASP C 3 28  ? 250.564 234.540 193.210 1.00 13.88  ? 28   ASP C CA  1 
ATOM   3203 C C   . ASP C 3 28  ? 250.623 235.248 194.557 1.00 13.49  ? 28   ASP C C   1 
ATOM   3204 O O   . ASP C 3 28  ? 249.779 235.021 195.424 1.00 13.62  ? 28   ASP C O   1 
ATOM   3205 C CB  . ASP C 3 28  ? 249.239 234.846 192.502 1.00 12.84  ? 28   ASP C CB  1 
ATOM   3206 C CG  . ASP C 3 28  ? 249.052 236.317 192.163 1.00 13.17  ? 28   ASP C CG  1 
ATOM   3207 O OD1 . ASP C 3 28  ? 249.572 237.149 192.869 1.00 13.23  ? 28   ASP C OD1 1 
ATOM   3208 O OD2 . ASP C 3 28  ? 248.399 236.599 191.186 1.00 12.39  ? 28   ASP C OD2 1 
ATOM   3209 N N   . ILE C 3 29  ? 251.648 236.076 194.737 1.00 13.39  ? 29   ILE C N   1 
ATOM   3210 C CA  . ILE C 3 29  ? 251.861 236.792 195.988 1.00 13.05  ? 29   ILE C CA  1 
ATOM   3211 C C   . ILE C 3 29  ? 251.760 238.294 195.766 1.00 11.94  ? 29   ILE C C   1 
ATOM   3212 O O   . ILE C 3 29  ? 252.329 239.088 196.519 1.00 13.58  ? 29   ILE C O   1 
ATOM   3213 C CB  . ILE C 3 29  ? 253.221 236.429 196.618 1.00 12.72  ? 29   ILE C CB  1 
ATOM   3214 C CG1 . ILE C 3 29  ? 254.362 236.744 195.643 1.00 13.26  ? 29   ILE C CG1 1 
ATOM   3215 C CG2 . ILE C 3 29  ? 253.229 234.960 197.013 1.00 13.42  ? 29   ILE C CG2 1 
ATOM   3216 C CD1 . ILE C 3 29  ? 255.743 236.682 196.265 1.00 13.04  ? 29   ILE C CD1 1 
ATOM   3217 N N   . ARG C 3 30  ? 251.036 238.675 194.719 1.00 12.99  ? 30   ARG C N   1 
ATOM   3218 C CA  . ARG C 3 30  ? 250.786 240.075 194.412 1.00 12.86  ? 30   ARG C CA  1 
ATOM   3219 C C   . ARG C 3 30  ? 252.060 240.905 194.483 1.00 12.39  ? 30   ARG C C   1 
ATOM   3220 O O   . ARG C 3 30  ? 252.953 240.741 193.655 1.00 14.59  ? 30   ARG C O   1 
ATOM   3221 C CB  . ARG C 3 30  ? 249.710 240.622 195.333 1.00 12.45  ? 30   ARG C CB  1 
ATOM   3222 C CG  . ARG C 3 30  ? 248.327 240.054 195.043 1.00 12.32  ? 30   ARG C CG  1 
ATOM   3223 C CD  . ARG C 3 30  ? 247.342 240.368 196.096 1.00 11.32  ? 30   ARG C CD  1 
ATOM   3224 N NE  . ARG C 3 30  ? 247.573 239.589 197.300 1.00 12.22  ? 30   ARG C NE  1 
ATOM   3225 C CZ  . ARG C 3 30  ? 246.688 239.450 198.305 1.00 12.52  ? 30   ARG C CZ  1 
ATOM   3226 N NH1 . ARG C 3 30  ? 246.999 238.725 199.355 1.00 12.51  ? 30   ARG C NH1 1 
ATOM   3227 N NH2 . ARG C 3 30  ? 245.505 240.038 198.236 1.00 12.11  ? 30   ARG C NH2 1 
ATOM   3228 N N   . PHE C 3 31  ? 252.128 241.832 195.427 1.00 12.23  ? 31   PHE C N   1 
ATOM   3229 C CA  . PHE C 3 31  ? 253.280 242.718 195.542 1.00 12.25  ? 31   PHE C CA  1 
ATOM   3230 C C   . PHE C 3 31  ? 253.897 242.668 196.929 1.00 11.73  ? 31   PHE C C   1 
ATOM   3231 O O   . PHE C 3 31  ? 254.417 243.665 197.425 1.00 11.70  ? 31   PHE C O   1 
ATOM   3232 C CB  . PHE C 3 31  ? 252.875 244.149 195.196 1.00 12.16  ? 31   PHE C CB  1 
ATOM   3233 C CG  . PHE C 3 31  ? 251.611 244.573 195.861 1.00 11.63  ? 31   PHE C CG  1 
ATOM   3234 C CD1 . PHE C 3 31  ? 251.611 245.085 197.145 1.00 11.18  ? 31   PHE C CD1 1 
ATOM   3235 C CD2 . PHE C 3 31  ? 250.406 244.451 195.196 1.00 11.87  ? 31   PHE C CD2 1 
ATOM   3236 C CE1 . PHE C 3 31  ? 250.431 245.462 197.745 1.00 10.86  ? 31   PHE C CE1 1 
ATOM   3237 C CE2 . PHE C 3 31  ? 249.229 244.827 195.795 1.00 11.12  ? 31   PHE C CE2 1 
ATOM   3238 C CZ  . PHE C 3 31  ? 249.243 245.332 197.071 1.00 10.85  ? 31   PHE C CZ  1 
ATOM   3239 N N   . TYR C 3 32  ? 253.847 241.501 197.556 1.00 11.61  ? 32   TYR C N   1 
ATOM   3240 C CA  . TYR C 3 32  ? 254.371 241.352 198.906 1.00 10.99  ? 32   TYR C CA  1 
ATOM   3241 C C   . TYR C 3 32  ? 255.670 240.559 198.926 1.00 10.83  ? 32   TYR C C   1 
ATOM   3242 O O   . TYR C 3 32  ? 255.707 239.407 199.362 1.00 10.88  ? 32   TYR C O   1 
ATOM   3243 C CB  . TYR C 3 32  ? 253.315 240.708 199.796 1.00 10.57  ? 32   TYR C CB  1 
ATOM   3244 C CG  . TYR C 3 32  ? 252.054 241.530 199.872 1.00 10.54  ? 32   TYR C CG  1 
ATOM   3245 C CD1 . TYR C 3 32  ? 252.040 242.705 200.604 1.00 10.53  ? 32   TYR C CD1 1 
ATOM   3246 C CD2 . TYR C 3 32  ? 250.913 241.119 199.205 1.00 11.58  ? 32   TYR C CD2 1 
ATOM   3247 C CE1 . TYR C 3 32  ? 250.893 243.463 200.674 1.00 10.62  ? 32   TYR C CE1 1 
ATOM   3248 C CE2 . TYR C 3 32  ? 249.763 241.879 199.274 1.00 10.85  ? 32   TYR C CE2 1 
ATOM   3249 C CZ  . TYR C 3 32  ? 249.752 243.047 200.006 1.00 10.71  ? 32   TYR C CZ  1 
ATOM   3250 O OH  . TYR C 3 32  ? 248.608 243.807 200.079 1.00 10.55  ? 32   TYR C OH  1 
ATOM   3251 N N   . LEU C 3 33  ? 256.734 241.188 198.432 1.00 11.43  ? 33   LEU C N   1 
ATOM   3252 C CA  . LEU C 3 33  ? 258.044 240.557 198.349 1.00 11.56  ? 33   LEU C CA  1 
ATOM   3253 C C   . LEU C 3 33  ? 259.166 241.510 198.766 1.00 11.32  ? 33   LEU C C   1 
ATOM   3254 O O   . LEU C 3 33  ? 259.193 242.674 198.361 1.00 11.52  ? 33   LEU C O   1 
ATOM   3255 C CB  . LEU C 3 33  ? 258.278 240.041 196.923 1.00 12.19  ? 33   LEU C CB  1 
ATOM   3256 C CG  . LEU C 3 33  ? 259.599 239.301 196.672 1.00 12.63  ? 33   LEU C CG  1 
ATOM   3257 C CD1 . LEU C 3 33  ? 259.346 238.147 195.729 1.00 14.15  ? 33   LEU C CD1 1 
ATOM   3258 C CD2 . LEU C 3 33  ? 260.611 240.259 196.064 1.00 13.42  ? 33   LEU C CD2 1 
ATOM   3259 N N   . ASN C 3 34  ? 260.096 241.000 199.573 1.00 11.27  ? 34   ASN C N   1 
ATOM   3260 C CA  . ASN C 3 34  ? 261.270 241.751 200.012 1.00 11.74  ? 34   ASN C CA  1 
ATOM   3261 C C   . ASN C 3 34  ? 262.524 241.325 199.256 1.00 11.69  ? 34   ASN C C   1 
ATOM   3262 O O   . ASN C 3 34  ? 262.687 240.151 198.924 1.00 13.06  ? 34   ASN C O   1 
ATOM   3263 C CB  . ASN C 3 34  ? 261.510 241.557 201.503 1.00 10.88  ? 34   ASN C CB  1 
ATOM   3264 C CG  . ASN C 3 34  ? 260.545 242.283 202.397 1.00 10.56  ? 34   ASN C CG  1 
ATOM   3265 O OD1 . ASN C 3 34  ? 260.137 243.411 202.109 1.00 10.81  ? 34   ASN C OD1 1 
ATOM   3266 N ND2 . ASN C 3 34  ? 260.185 241.657 203.496 1.00 9.91   ? 34   ASN C ND2 1 
ATOM   3267 N N   . TRP C 3 35  ? 263.448 242.265 199.061 1.00 12.41  ? 35   TRP C N   1 
ATOM   3268 C CA  . TRP C 3 35  ? 264.780 241.941 198.552 1.00 12.73  ? 35   TRP C CA  1 
ATOM   3269 C C   . TRP C 3 35  ? 265.852 242.279 199.582 1.00 12.45  ? 35   TRP C C   1 
ATOM   3270 O O   . TRP C 3 35  ? 265.905 243.403 200.088 1.00 12.45  ? 35   TRP C O   1 
ATOM   3271 C CB  . TRP C 3 35  ? 265.084 242.707 197.265 1.00 13.46  ? 35   TRP C CB  1 
ATOM   3272 C CG  . TRP C 3 35  ? 264.287 242.270 196.080 1.00 14.06  ? 35   TRP C CG  1 
ATOM   3273 C CD1 . TRP C 3 35  ? 263.116 242.802 195.644 1.00 14.21  ? 35   TRP C CD1 1 
ATOM   3274 C CD2 . TRP C 3 35  ? 264.615 241.209 195.157 1.00 14.45  ? 35   TRP C CD2 1 
ATOM   3275 N NE1 . TRP C 3 35  ? 262.694 242.150 194.516 1.00 14.51  ? 35   TRP C NE1 1 
ATOM   3276 C CE2 . TRP C 3 35  ? 263.598 241.172 194.204 1.00 14.58  ? 35   TRP C CE2 1 
ATOM   3277 C CE3 . TRP C 3 35  ? 265.678 240.304 195.061 1.00 14.51  ? 35   TRP C CE3 1 
ATOM   3278 C CZ2 . TRP C 3 35  ? 263.607 240.266 193.160 1.00 15.46  ? 35   TRP C CZ2 1 
ATOM   3279 C CZ3 . TRP C 3 35  ? 265.689 239.398 194.012 1.00 15.11  ? 35   TRP C CZ3 1 
ATOM   3280 C CH2 . TRP C 3 35  ? 264.680 239.382 193.086 1.00 15.80  ? 35   TRP C CH2 1 
ATOM   3281 N N   . TYR C 3 36  ? 266.734 241.315 199.848 1.00 12.59  ? 36   TYR C N   1 
ATOM   3282 C CA  . TYR C 3 36  ? 267.809 241.483 200.823 1.00 12.24  ? 36   TYR C CA  1 
ATOM   3283 C C   . TYR C 3 36  ? 269.182 241.343 200.186 1.00 13.12  ? 36   TYR C C   1 
ATOM   3284 O O   . TYR C 3 36  ? 269.363 240.590 199.230 1.00 13.71  ? 36   TYR C O   1 
ATOM   3285 C CB  . TYR C 3 36  ? 267.698 240.448 201.943 1.00 12.02  ? 36   TYR C CB  1 
ATOM   3286 C CG  . TYR C 3 36  ? 266.468 240.551 202.793 1.00 11.50  ? 36   TYR C CG  1 
ATOM   3287 C CD1 . TYR C 3 36  ? 266.482 241.312 203.948 1.00 11.00  ? 36   TYR C CD1 1 
ATOM   3288 C CD2 . TYR C 3 36  ? 265.330 239.868 202.429 1.00 11.38  ? 36   TYR C CD2 1 
ATOM   3289 C CE1 . TYR C 3 36  ? 265.355 241.383 204.734 1.00 9.95   ? 36   TYR C CE1 1 
ATOM   3290 C CE2 . TYR C 3 36  ? 264.210 239.941 203.214 1.00 10.80  ? 36   TYR C CE2 1 
ATOM   3291 C CZ  . TYR C 3 36  ? 264.216 240.689 204.359 1.00 9.86   ? 36   TYR C CZ  1 
ATOM   3292 O OH  . TYR C 3 36  ? 263.088 240.743 205.140 1.00 9.72   ? 36   TYR C OH  1 
ATOM   3293 N N   . GLN C 3 37  ? 270.158 242.032 200.760 1.00 12.75  ? 37   GLN C N   1 
ATOM   3294 C CA  . GLN C 3 37  ? 271.549 241.919 200.346 1.00 14.03  ? 37   GLN C CA  1 
ATOM   3295 C C   . GLN C 3 37  ? 272.423 241.440 201.496 1.00 13.56  ? 37   GLN C C   1 
ATOM   3296 O O   . GLN C 3 37  ? 272.518 242.105 202.527 1.00 13.41  ? 37   GLN C O   1 
ATOM   3297 C CB  . GLN C 3 37  ? 272.054 243.272 199.854 1.00 14.49  ? 37   GLN C CB  1 
ATOM   3298 C CG  . GLN C 3 37  ? 273.499 243.284 199.423 1.00 15.18  ? 37   GLN C CG  1 
ATOM   3299 C CD  . GLN C 3 37  ? 273.974 244.670 199.065 1.00 15.52  ? 37   GLN C CD  1 
ATOM   3300 O OE1 . GLN C 3 37  ? 273.409 245.668 199.517 1.00 15.70  ? 37   GLN C OE1 1 
ATOM   3301 N NE2 . GLN C 3 37  ? 275.015 244.747 198.255 1.00 17.59  ? 37   GLN C NE2 1 
ATOM   3302 N N   . GLN C 3 38  ? 273.069 240.290 201.323 1.00 14.04  ? 38   GLN C N   1 
ATOM   3303 C CA  . GLN C 3 38  ? 273.919 239.752 202.377 1.00 14.32  ? 38   GLN C CA  1 
ATOM   3304 C C   . GLN C 3 38  ? 275.376 239.654 201.962 1.00 15.37  ? 38   GLN C C   1 
ATOM   3305 O O   . GLN C 3 38  ? 275.710 239.028 200.954 1.00 15.63  ? 38   GLN C O   1 
ATOM   3306 C CB  . GLN C 3 38  ? 273.453 238.365 202.809 1.00 13.63  ? 38   GLN C CB  1 
ATOM   3307 C CG  . GLN C 3 38  ? 274.295 237.771 203.929 1.00 13.38  ? 38   GLN C CG  1 
ATOM   3308 C CD  . GLN C 3 38  ? 273.839 236.401 204.377 1.00 13.50  ? 38   GLN C CD  1 
ATOM   3309 O OE1 . GLN C 3 38  ? 273.494 235.526 203.567 1.00 14.14  ? 38   GLN C OE1 1 
ATOM   3310 N NE2 . GLN C 3 38  ? 273.845 236.199 205.688 1.00 12.55  ? 38   GLN C NE2 1 
ATOM   3311 N N   . LYS C 3 39  ? 276.246 240.215 202.786 1.00 15.24  ? 39   LYS C N   1 
ATOM   3312 C CA  . LYS C 3 39  ? 277.677 240.070 202.595 1.00 15.39  ? 39   LYS C CA  1 
ATOM   3313 C C   . LYS C 3 39  ? 278.177 239.053 203.617 1.00 14.60  ? 39   LYS C C   1 
ATOM   3314 O O   . LYS C 3 39  ? 277.610 238.962 204.705 1.00 14.44  ? 39   LYS C O   1 
ATOM   3315 C CB  . LYS C 3 39  ? 278.371 241.420 202.760 1.00 15.87  ? 39   LYS C CB  1 
ATOM   3316 C CG  . LYS C 3 39  ? 277.949 242.452 201.724 1.00 16.76  ? 39   LYS C CG  1 
ATOM   3317 C CD  . LYS C 3 39  ? 278.632 243.787 201.949 1.00 18.93  ? 39   LYS C CD  1 
ATOM   3318 C CE  . LYS C 3 39  ? 278.095 244.848 200.997 1.00 18.55  ? 39   LYS C CE  1 
ATOM   3319 N NZ  . LYS C 3 39  ? 278.723 246.177 201.236 1.00 19.44  ? 39   LYS C NZ  1 
ATOM   3320 N N   . PRO C 3 40  ? 279.217 238.278 203.304 1.00 15.10  ? 40   PRO C N   1 
ATOM   3321 C CA  . PRO C 3 40  ? 279.776 237.243 204.152 1.00 14.76  ? 40   PRO C CA  1 
ATOM   3322 C C   . PRO C 3 40  ? 280.080 237.757 205.551 1.00 14.61  ? 40   PRO C C   1 
ATOM   3323 O O   . PRO C 3 40  ? 280.743 238.781 205.716 1.00 14.80  ? 40   PRO C O   1 
ATOM   3324 C CB  . PRO C 3 40  ? 281.063 236.883 203.400 1.00 15.26  ? 40   PRO C CB  1 
ATOM   3325 C CG  . PRO C 3 40  ? 280.741 237.169 201.952 1.00 15.88  ? 40   PRO C CG  1 
ATOM   3326 C CD  . PRO C 3 40  ? 279.866 238.406 201.990 1.00 15.60  ? 40   PRO C CD  1 
ATOM   3327 N N   . GLY C 3 41  ? 279.608 237.025 206.557 1.00 14.44  ? 41   GLY C N   1 
ATOM   3328 C CA  . GLY C 3 41  ? 279.872 237.356 207.954 1.00 13.99  ? 41   GLY C CA  1 
ATOM   3329 C C   . GLY C 3 41  ? 278.877 238.354 208.545 1.00 13.65  ? 41   GLY C C   1 
ATOM   3330 O O   . GLY C 3 41  ? 278.961 238.684 209.728 1.00 13.79  ? 41   GLY C O   1 
ATOM   3331 N N   . LYS C 3 42  ? 277.942 238.839 207.733 1.00 13.76  ? 42   LYS C N   1 
ATOM   3332 C CA  . LYS C 3 42  ? 276.990 239.842 208.201 1.00 13.48  ? 42   LYS C CA  1 
ATOM   3333 C C   . LYS C 3 42  ? 275.541 239.383 208.062 1.00 13.00  ? 42   LYS C C   1 
ATOM   3334 O O   . LYS C 3 42  ? 275.224 238.533 207.229 1.00 13.04  ? 42   LYS C O   1 
ATOM   3335 C CB  . LYS C 3 42  ? 277.184 241.150 207.431 1.00 13.64  ? 42   LYS C CB  1 
ATOM   3336 C CG  . LYS C 3 42  ? 278.596 241.735 207.500 1.00 13.86  ? 42   LYS C CG  1 
ATOM   3337 C CD  . LYS C 3 42  ? 278.942 242.220 208.901 1.00 12.99  ? 42   LYS C CD  1 
ATOM   3338 C CE  . LYS C 3 42  ? 280.302 242.898 208.928 1.00 13.35  ? 42   LYS C CE  1 
ATOM   3339 N NZ  . LYS C 3 42  ? 280.683 243.328 210.302 1.00 14.14  ? 42   LYS C NZ  1 
ATOM   3340 N N   . ALA C 3 43  ? 274.658 239.979 208.861 1.00 12.27  ? 43   ALA C N   1 
ATOM   3341 C CA  . ALA C 3 43  ? 273.227 239.762 208.700 1.00 12.12  ? 43   ALA C CA  1 
ATOM   3342 C C   . ALA C 3 43  ? 272.770 240.430 207.400 1.00 12.45  ? 43   ALA C C   1 
ATOM   3343 O O   . ALA C 3 43  ? 273.370 241.421 206.987 1.00 12.79  ? 43   ALA C O   1 
ATOM   3344 C CB  . ALA C 3 43  ? 272.459 240.323 209.888 1.00 11.91  ? 43   ALA C CB  1 
ATOM   3345 N N   . PRO C 3 44  ? 271.729 239.908 206.741 1.00 12.10  ? 44   PRO C N   1 
ATOM   3346 C CA  . PRO C 3 44  ? 271.083 240.466 205.566 1.00 12.09  ? 44   PRO C CA  1 
ATOM   3347 C C   . PRO C 3 44  ? 270.564 241.880 205.801 1.00 11.99  ? 44   PRO C C   1 
ATOM   3348 O O   . PRO C 3 44  ? 270.019 242.181 206.860 1.00 11.62  ? 44   PRO C O   1 
ATOM   3349 C CB  . PRO C 3 44  ? 269.916 239.498 205.347 1.00 11.52  ? 44   PRO C CB  1 
ATOM   3350 C CG  . PRO C 3 44  ? 270.368 238.206 205.968 1.00 11.91  ? 44   PRO C CG  1 
ATOM   3351 C CD  . PRO C 3 44  ? 271.201 238.606 207.156 1.00 11.87  ? 44   PRO C CD  1 
ATOM   3352 N N   . LYS C 3 45  ? 270.692 242.727 204.787 1.00 12.46  ? 45   LYS C N   1 
ATOM   3353 C CA  . LYS C 3 45  ? 270.153 244.082 204.828 1.00 12.32  ? 45   LYS C CA  1 
ATOM   3354 C C   . LYS C 3 45  ? 269.002 244.229 203.842 1.00 12.14  ? 45   LYS C C   1 
ATOM   3355 O O   . LYS C 3 45  ? 269.091 243.778 202.703 1.00 12.31  ? 45   LYS C O   1 
ATOM   3356 C CB  . LYS C 3 45  ? 271.248 245.101 204.509 1.00 12.05  ? 45   LYS C CB  1 
ATOM   3357 C CG  . LYS C 3 45  ? 270.784 246.550 204.512 1.00 12.00  ? 45   LYS C CG  1 
ATOM   3358 C CD  . LYS C 3 45  ? 271.936 247.495 204.222 1.00 11.66  ? 45   LYS C CD  1 
ATOM   3359 C CE  . LYS C 3 45  ? 271.463 248.938 204.148 1.00 11.31  ? 45   LYS C CE  1 
ATOM   3360 N NZ  . LYS C 3 45  ? 272.588 249.874 203.877 1.00 9.27   ? 45   LYS C NZ  1 
ATOM   3361 N N   . LEU C 3 46  ? 267.919 244.864 204.273 1.00 11.75  ? 46   LEU C N   1 
ATOM   3362 C CA  . LEU C 3 46  ? 266.778 245.066 203.388 1.00 11.95  ? 46   LEU C CA  1 
ATOM   3363 C C   . LEU C 3 46  ? 267.010 246.245 202.449 1.00 12.48  ? 46   LEU C C   1 
ATOM   3364 O O   . LEU C 3 46  ? 267.360 247.338 202.893 1.00 12.69  ? 46   LEU C O   1 
ATOM   3365 C CB  . LEU C 3 46  ? 265.510 245.315 204.214 1.00 11.06  ? 46   LEU C CB  1 
ATOM   3366 C CG  . LEU C 3 46  ? 264.203 245.498 203.422 1.00 11.04  ? 46   LEU C CG  1 
ATOM   3367 C CD1 . LEU C 3 46  ? 263.817 244.192 202.747 1.00 11.23  ? 46   LEU C CD1 1 
ATOM   3368 C CD2 . LEU C 3 46  ? 263.118 245.946 204.363 1.00 10.04  ? 46   LEU C CD2 1 
ATOM   3369 N N   . LEU C 3 47  ? 266.803 246.025 201.153 1.00 12.58  ? 47   LEU C N   1 
ATOM   3370 C CA  . LEU C 3 47  ? 266.937 247.099 200.174 1.00 13.21  ? 47   LEU C CA  1 
ATOM   3371 C C   . LEU C 3 47  ? 265.590 247.529 199.610 1.00 12.77  ? 47   LEU C C   1 
ATOM   3372 O O   . LEU C 3 47  ? 265.348 248.720 199.402 1.00 13.81  ? 47   LEU C O   1 
ATOM   3373 C CB  . LEU C 3 47  ? 267.839 246.671 199.010 1.00 13.96  ? 47   LEU C CB  1 
ATOM   3374 C CG  . LEU C 3 47  ? 269.296 246.310 199.345 1.00 13.75  ? 47   LEU C CG  1 
ATOM   3375 C CD1 . LEU C 3 47  ? 269.991 245.876 198.067 1.00 15.20  ? 47   LEU C CD1 1 
ATOM   3376 C CD2 . LEU C 3 47  ? 270.008 247.507 199.960 1.00 13.84  ? 47   LEU C CD2 1 
ATOM   3377 N N   . ILE C 3 48  ? 264.736 246.551 199.312 1.00 12.60  ? 48   ILE C N   1 
ATOM   3378 C CA  . ILE C 3 48  ? 263.438 246.830 198.699 1.00 12.20  ? 48   ILE C CA  1 
ATOM   3379 C C   . ILE C 3 48  ? 262.314 246.060 199.381 1.00 11.56  ? 48   ILE C C   1 
ATOM   3380 O O   . ILE C 3 48  ? 262.446 244.869 199.660 1.00 12.26  ? 48   ILE C O   1 
ATOM   3381 C CB  . ILE C 3 48  ? 263.449 246.493 197.193 1.00 12.91  ? 48   ILE C CB  1 
ATOM   3382 C CG1 . ILE C 3 48  ? 264.576 247.270 196.503 1.00 14.14  ? 48   ILE C CG1 1 
ATOM   3383 C CG2 . ILE C 3 48  ? 262.093 246.814 196.558 1.00 12.67  ? 48   ILE C CG2 1 
ATOM   3384 C CD1 . ILE C 3 48  ? 264.742 246.960 195.032 1.00 15.78  ? 48   ILE C CD1 1 
ATOM   3385 N N   . SER C 3 49  ? 261.191 246.732 199.608 1.00 11.42  ? 49   SER C N   1 
ATOM   3386 C CA  . SER C 3 49  ? 260.006 246.082 200.158 1.00 11.10  ? 49   SER C CA  1 
ATOM   3387 C C   . SER C 3 49  ? 258.805 246.307 199.255 1.00 10.48  ? 49   SER C C   1 
ATOM   3388 O O   . SER C 3 49  ? 258.860 247.106 198.321 1.00 15.10  ? 49   SER C O   1 
ATOM   3389 C CB  . SER C 3 49  ? 259.701 246.600 201.548 1.00 10.47  ? 49   SER C CB  1 
ATOM   3390 O OG  . SER C 3 49  ? 259.357 247.956 201.516 1.00 10.58  ? 49   SER C OG  1 
ATOM   3391 N N   . ASP C 3 50  ? 257.731 245.564 199.497 1.00 11.19  ? 50   ASP C N   1 
ATOM   3392 C CA  . ASP C 3 50  ? 256.507 245.718 198.721 1.00 11.42  ? 50   ASP C CA  1 
ATOM   3393 C C   . ASP C 3 50  ? 256.792 245.695 197.222 1.00 11.76  ? 50   ASP C C   1 
ATOM   3394 O O   . ASP C 3 50  ? 256.243 246.500 196.469 1.00 12.24  ? 50   ASP C O   1 
ATOM   3395 C CB  . ASP C 3 50  ? 255.792 247.018 199.089 1.00 11.17  ? 50   ASP C CB  1 
ATOM   3396 C CG  . ASP C 3 50  ? 255.368 247.089 200.559 1.00 10.53  ? 50   ASP C CG  1 
ATOM   3397 O OD1 . ASP C 3 50  ? 255.052 246.068 201.127 1.00 10.35  ? 50   ASP C OD1 1 
ATOM   3398 O OD2 . ASP C 3 50  ? 255.362 248.173 201.098 1.00 9.89   ? 50   ASP C OD2 1 
ATOM   3399 N N   . ALA C 3 51  ? 257.664 244.780 196.798 1.00 12.02  ? 51   ALA C N   1 
ATOM   3400 C CA  . ALA C 3 51  ? 258.035 244.584 195.394 1.00 12.84  ? 51   ALA C CA  1 
ATOM   3401 C C   . ALA C 3 51  ? 258.948 245.689 194.854 1.00 13.16  ? 51   ALA C C   1 
ATOM   3402 O O   . ALA C 3 51  ? 260.010 245.392 194.306 1.00 13.61  ? 51   ALA C O   1 
ATOM   3403 C CB  . ALA C 3 51  ? 256.793 244.473 194.516 1.00 13.89  ? 51   ALA C CB  1 
ATOM   3404 N N   . SER C 3 52  ? 258.522 246.948 194.951 1.00 12.98  ? 52   SER C N   1 
ATOM   3405 C CA  . SER C 3 52  ? 259.264 248.033 194.307 1.00 13.13  ? 52   SER C CA  1 
ATOM   3406 C C   . SER C 3 52  ? 259.523 249.263 195.181 1.00 13.03  ? 52   SER C C   1 
ATOM   3407 O O   . SER C 3 52  ? 260.011 250.277 194.682 1.00 13.27  ? 52   SER C O   1 
ATOM   3408 C CB  . SER C 3 52  ? 258.526 248.482 193.065 1.00 14.52  ? 52   SER C CB  1 
ATOM   3409 O OG  . SER C 3 52  ? 257.295 249.064 193.398 1.00 14.62  ? 52   SER C OG  1 
ATOM   3410 N N   . ASN C 3 53  ? 259.190 249.204 196.466 1.00 12.22  ? 53   ASN C N   1 
ATOM   3411 C CA  . ASN C 3 53  ? 259.406 250.361 197.333 1.00 12.22  ? 53   ASN C CA  1 
ATOM   3412 C C   . ASN C 3 53  ? 260.824 250.387 197.887 1.00 11.54  ? 53   ASN C C   1 
ATOM   3413 O O   . ASN C 3 53  ? 261.266 249.446 198.545 1.00 16.46  ? 53   ASN C O   1 
ATOM   3414 C CB  . ASN C 3 53  ? 258.387 250.412 198.459 1.00 11.45  ? 53   ASN C CB  1 
ATOM   3415 C CG  . ASN C 3 53  ? 257.016 250.818 197.986 1.00 11.80  ? 53   ASN C CG  1 
ATOM   3416 O OD1 . ASN C 3 53  ? 256.877 251.465 196.941 1.00 13.08  ? 53   ASN C OD1 1 
ATOM   3417 N ND2 . ASN C 3 53  ? 255.997 250.470 198.736 1.00 11.30  ? 53   ASN C ND2 1 
ATOM   3418 N N   . MET C 3 54  ? 261.545 251.465 197.607 1.00 12.84  ? 54   MET C N   1 
ATOM   3419 C CA  . MET C 3 54  ? 262.933 251.571 198.037 1.00 13.20  ? 54   MET C CA  1 
ATOM   3420 C C   . MET C 3 54  ? 263.014 251.996 199.493 1.00 13.14  ? 54   MET C C   1 
ATOM   3421 O O   . MET C 3 54  ? 262.270 252.875 199.929 1.00 12.62  ? 54   MET C O   1 
ATOM   3422 C CB  . MET C 3 54  ? 263.680 252.579 197.168 1.00 13.95  ? 54   MET C CB  1 
ATOM   3423 C CG  . MET C 3 54  ? 263.626 252.298 195.673 1.00 14.70  ? 54   MET C CG  1 
ATOM   3424 S SD  . MET C 3 54  ? 264.203 250.656 195.237 1.00 16.16  ? 54   MET C SD  1 
ATOM   3425 C CE  . MET C 3 54  ? 265.908 250.709 195.770 1.00 17.34  ? 54   MET C CE  1 
ATOM   3426 N N   . GLU C 3 55  ? 263.939 251.398 200.237 1.00 13.24  ? 55   GLU C N   1 
ATOM   3427 C CA  . GLU C 3 55  ? 264.137 251.779 201.628 1.00 13.54  ? 55   GLU C CA  1 
ATOM   3428 C C   . GLU C 3 55  ? 264.969 253.046 201.732 1.00 14.32  ? 55   GLU C C   1 
ATOM   3429 O O   . GLU C 3 55  ? 265.690 253.411 200.801 1.00 14.31  ? 55   GLU C O   1 
ATOM   3430 C CB  . GLU C 3 55  ? 264.804 250.653 202.417 1.00 13.66  ? 55   GLU C CB  1 
ATOM   3431 C CG  . GLU C 3 55  ? 264.019 249.364 202.441 1.00 12.66  ? 55   GLU C CG  1 
ATOM   3432 C CD  . GLU C 3 55  ? 262.636 249.541 202.962 1.00 12.02  ? 55   GLU C CD  1 
ATOM   3433 O OE1 . GLU C 3 55  ? 262.449 250.296 203.884 1.00 12.60  ? 55   GLU C OE1 1 
ATOM   3434 O OE2 . GLU C 3 55  ? 261.751 248.930 202.421 1.00 11.57  ? 55   GLU C OE2 1 
ATOM   3435 N N   . THR C 3 56  ? 264.842 253.735 202.856 1.00 14.23  ? 56   THR C N   1 
ATOM   3436 C CA  . THR C 3 56  ? 265.583 254.965 203.073 1.00 14.03  ? 56   THR C CA  1 
ATOM   3437 C C   . THR C 3 56  ? 267.070 254.677 203.203 1.00 15.38  ? 56   THR C C   1 
ATOM   3438 O O   . THR C 3 56  ? 267.478 253.792 203.955 1.00 15.85  ? 56   THR C O   1 
ATOM   3439 C CB  . THR C 3 56  ? 265.079 255.692 204.333 1.00 14.70  ? 56   THR C CB  1 
ATOM   3440 O OG1 . THR C 3 56  ? 263.680 255.971 204.192 1.00 15.73  ? 56   THR C OG1 1 
ATOM   3441 C CG2 . THR C 3 56  ? 265.832 256.997 204.546 1.00 15.90  ? 56   THR C CG2 1 
ATOM   3442 N N   . GLY C 3 57  ? 267.881 255.434 202.472 1.00 16.20  ? 57   GLY C N   1 
ATOM   3443 C CA  . GLY C 3 57  ? 269.329 255.285 202.535 1.00 16.52  ? 57   GLY C CA  1 
ATOM   3444 C C   . GLY C 3 57  ? 269.873 254.397 201.421 1.00 17.21  ? 57   GLY C C   1 
ATOM   3445 O O   . GLY C 3 57  ? 271.086 254.299 201.241 1.00 18.36  ? 57   GLY C O   1 
ATOM   3446 N N   . VAL C 3 58  ? 268.983 253.754 200.674 1.00 17.11  ? 58   VAL C N   1 
ATOM   3447 C CA  . VAL C 3 58  ? 269.407 252.890 199.579 1.00 18.01  ? 58   VAL C CA  1 
ATOM   3448 C C   . VAL C 3 58  ? 269.720 253.724 198.332 1.00 18.28  ? 58   VAL C C   1 
ATOM   3449 O O   . VAL C 3 58  ? 268.878 254.507 197.895 1.00 18.75  ? 58   VAL C O   1 
ATOM   3450 C CB  . VAL C 3 58  ? 268.315 251.852 199.264 1.00 16.81  ? 58   VAL C CB  1 
ATOM   3451 C CG1 . VAL C 3 58  ? 268.712 250.998 198.062 1.00 17.48  ? 58   VAL C CG1 1 
ATOM   3452 C CG2 . VAL C 3 58  ? 268.104 250.978 200.485 1.00 15.65  ? 58   VAL C CG2 1 
ATOM   3453 N N   . PRO C 3 59  ? 270.917 253.576 197.747 1.00 18.90  ? 59   PRO C N   1 
ATOM   3454 C CA  . PRO C 3 59  ? 271.387 254.266 196.559 1.00 19.49  ? 59   PRO C CA  1 
ATOM   3455 C C   . PRO C 3 59  ? 270.408 254.134 195.401 1.00 19.15  ? 59   PRO C C   1 
ATOM   3456 O O   . PRO C 3 59  ? 269.790 253.086 195.211 1.00 19.66  ? 59   PRO C O   1 
ATOM   3457 C CB  . PRO C 3 59  ? 272.705 253.544 196.267 1.00 20.16  ? 59   PRO C CB  1 
ATOM   3458 C CG  . PRO C 3 59  ? 273.181 253.072 197.617 1.00 20.53  ? 59   PRO C CG  1 
ATOM   3459 C CD  . PRO C 3 59  ? 271.922 252.699 198.366 1.00 19.10  ? 59   PRO C CD  1 
ATOM   3460 N N   . SER C 3 60  ? 270.287 255.206 194.623 1.00 19.53  ? 60   SER C N   1 
ATOM   3461 C CA  . SER C 3 60  ? 269.332 255.288 193.520 1.00 19.48  ? 60   SER C CA  1 
ATOM   3462 C C   . SER C 3 60  ? 269.641 254.320 192.384 1.00 20.00  ? 60   SER C C   1 
ATOM   3463 O O   . SER C 3 60  ? 268.812 254.111 191.500 1.00 19.47  ? 60   SER C O   1 
ATOM   3464 C CB  . SER C 3 60  ? 269.292 256.702 192.976 1.00 18.76  ? 60   SER C CB  1 
ATOM   3465 O OG  . SER C 3 60  ? 270.504 257.037 192.357 1.00 19.44  ? 60   SER C OG  1 
ATOM   3466 N N   . ARG C 3 61  ? 270.834 253.735 192.398 1.00 19.85  ? 61   ARG C N   1 
ATOM   3467 C CA  . ARG C 3 61  ? 271.213 252.784 191.360 1.00 20.74  ? 61   ARG C CA  1 
ATOM   3468 C C   . ARG C 3 61  ? 270.466 251.463 191.513 1.00 19.74  ? 61   ARG C C   1 
ATOM   3469 O O   . ARG C 3 61  ? 270.449 250.643 190.592 1.00 20.29  ? 61   ARG C O   1 
ATOM   3470 C CB  . ARG C 3 61  ? 272.715 252.537 191.356 1.00 21.14  ? 61   ARG C CB  1 
ATOM   3471 C CG  . ARG C 3 61  ? 273.280 251.820 192.569 1.00 21.36  ? 61   ARG C CG  1 
ATOM   3472 C CD  . ARG C 3 61  ? 274.749 251.638 192.432 1.00 22.57  ? 61   ARG C CD  1 
ATOM   3473 N NE  . ARG C 3 61  ? 275.340 250.966 193.577 1.00 22.53  ? 61   ARG C NE  1 
ATOM   3474 C CZ  . ARG C 3 61  ? 275.795 251.581 194.690 1.00 22.77  ? 61   ARG C CZ  1 
ATOM   3475 N NH1 . ARG C 3 61  ? 276.327 250.864 195.651 1.00 23.14  ? 61   ARG C NH1 1 
ATOM   3476 N NH2 . ARG C 3 61  ? 275.720 252.898 194.812 1.00 22.83  ? 61   ARG C NH2 1 
ATOM   3477 N N   . PHE C 3 62  ? 269.858 251.255 192.679 1.00 19.22  ? 62   PHE C N   1 
ATOM   3478 C CA  . PHE C 3 62  ? 269.085 250.047 192.932 1.00 19.06  ? 62   PHE C CA  1 
ATOM   3479 C C   . PHE C 3 62  ? 267.625 250.271 192.569 1.00 19.36  ? 62   PHE C C   1 
ATOM   3480 O O   . PHE C 3 62  ? 267.061 251.328 192.852 1.00 19.36  ? 62   PHE C O   1 
ATOM   3481 C CB  . PHE C 3 62  ? 269.177 249.640 194.402 1.00 19.68  ? 62   PHE C CB  1 
ATOM   3482 C CG  . PHE C 3 62  ? 270.520 249.149 194.821 1.00 19.40  ? 62   PHE C CG  1 
ATOM   3483 C CD1 . PHE C 3 62  ? 270.922 247.866 194.519 1.00 19.55  ? 62   PHE C CD1 1 
ATOM   3484 C CD2 . PHE C 3 62  ? 271.379 249.964 195.529 1.00 19.83  ? 62   PHE C CD2 1 
ATOM   3485 C CE1 . PHE C 3 62  ? 272.159 247.403 194.914 1.00 20.06  ? 62   PHE C CE1 1 
ATOM   3486 C CE2 . PHE C 3 62  ? 272.616 249.508 195.924 1.00 20.26  ? 62   PHE C CE2 1 
ATOM   3487 C CZ  . PHE C 3 62  ? 273.006 248.225 195.616 1.00 20.93  ? 62   PHE C CZ  1 
ATOM   3488 N N   . SER C 3 63  ? 267.003 249.262 191.980 1.00 19.41  ? 63   SER C N   1 
ATOM   3489 C CA  . SER C 3 63  ? 265.588 249.339 191.648 1.00 17.81  ? 63   SER C CA  1 
ATOM   3490 C C   . SER C 3 63  ? 264.976 247.952 191.568 1.00 17.40  ? 63   SER C C   1 
ATOM   3491 O O   . SER C 3 63  ? 265.690 246.948 191.594 1.00 17.22  ? 63   SER C O   1 
ATOM   3492 C CB  . SER C 3 63  ? 265.400 250.057 190.328 1.00 18.17  ? 63   SER C CB  1 
ATOM   3493 O OG  . SER C 3 63  ? 265.867 249.276 189.267 1.00 19.11  ? 63   SER C OG  1 
ATOM   3494 N N   . GLY C 3 64  ? 263.659 247.895 191.450 1.00 15.94  ? 64   GLY C N   1 
ATOM   3495 C CA  . GLY C 3 64  ? 262.978 246.620 191.298 1.00 15.41  ? 64   GLY C CA  1 
ATOM   3496 C C   . GLY C 3 64  ? 261.524 246.820 190.909 1.00 14.99  ? 64   GLY C C   1 
ATOM   3497 O O   . GLY C 3 64  ? 260.964 247.903 191.083 1.00 15.20  ? 64   GLY C O   1 
ATOM   3498 N N   . SER C 3 65  ? 260.926 245.768 190.368 1.00 14.74  ? 65   SER C N   1 
ATOM   3499 C CA  . SER C 3 65  ? 259.542 245.809 189.914 1.00 14.69  ? 65   SER C CA  1 
ATOM   3500 C C   . SER C 3 65  ? 258.988 244.408 189.729 1.00 14.79  ? 65   SER C C   1 
ATOM   3501 O O   . SER C 3 65  ? 259.724 243.424 189.823 1.00 15.22  ? 65   SER C O   1 
ATOM   3502 C CB  . SER C 3 65  ? 259.436 246.573 188.610 1.00 15.93  ? 65   SER C CB  1 
ATOM   3503 O OG  . SER C 3 65  ? 260.021 245.855 187.560 1.00 15.84  ? 65   SER C OG  1 
ATOM   3504 N N   . GLY C 3 66  ? 257.696 244.319 189.448 1.00 14.39  ? 66   GLY C N   1 
ATOM   3505 C CA  . GLY C 3 66  ? 257.071 243.037 189.154 1.00 14.80  ? 66   GLY C CA  1 
ATOM   3506 C C   . GLY C 3 66  ? 255.943 242.735 190.122 1.00 14.96  ? 66   GLY C C   1 
ATOM   3507 O O   . GLY C 3 66  ? 255.785 243.415 191.137 1.00 15.14  ? 66   GLY C O   1 
ATOM   3508 N N   . SER C 3 67  ? 255.147 241.729 189.786 1.00 14.72  ? 67   SER C N   1 
ATOM   3509 C CA  . SER C 3 67  ? 254.020 241.331 190.615 1.00 14.36  ? 67   SER C CA  1 
ATOM   3510 C C   . SER C 3 67  ? 253.583 239.907 190.305 1.00 14.36  ? 67   SER C C   1 
ATOM   3511 O O   . SER C 3 67  ? 253.916 239.350 189.255 1.00 14.46  ? 67   SER C O   1 
ATOM   3512 C CB  . SER C 3 67  ? 252.855 242.277 190.412 1.00 13.26  ? 67   SER C CB  1 
ATOM   3513 O OG  . SER C 3 67  ? 252.322 242.145 189.124 1.00 13.85  ? 67   SER C OG  1 
ATOM   3514 N N   . GLY C 3 68  ? 252.788 239.342 191.199 1.00 13.98  ? 68   GLY C N   1 
ATOM   3515 C CA  . GLY C 3 68  ? 252.216 238.023 190.988 1.00 14.03  ? 68   GLY C CA  1 
ATOM   3516 C C   . GLY C 3 68  ? 253.245 236.936 191.240 1.00 13.57  ? 68   GLY C C   1 
ATOM   3517 O O   . GLY C 3 68  ? 253.558 236.618 192.388 1.00 13.76  ? 68   GLY C O   1 
ATOM   3518 N N   . THR C 3 69  ? 253.744 236.341 190.166 1.00 14.28  ? 69   THR C N   1 
ATOM   3519 C CA  . THR C 3 69  ? 254.696 235.249 190.276 1.00 14.93  ? 69   THR C CA  1 
ATOM   3520 C C   . THR C 3 69  ? 256.077 235.596 189.738 1.00 14.36  ? 69   THR C C   1 
ATOM   3521 O O   . THR C 3 69  ? 256.992 234.778 189.824 1.00 17.40  ? 69   THR C O   1 
ATOM   3522 C CB  . THR C 3 69  ? 254.165 234.008 189.543 1.00 14.80  ? 69   THR C CB  1 
ATOM   3523 O OG1 . THR C 3 69  ? 253.909 234.339 188.165 1.00 14.75  ? 69   THR C OG1 1 
ATOM   3524 C CG2 . THR C 3 69  ? 252.881 233.526 190.199 1.00 14.70  ? 69   THR C CG2 1 
ATOM   3525 N N   . ASP C 3 70  ? 256.235 236.792 189.170 1.00 15.13  ? 70   ASP C N   1 
ATOM   3526 C CA  . ASP C 3 70  ? 257.500 237.149 188.528 1.00 15.72  ? 70   ASP C CA  1 
ATOM   3527 C C   . ASP C 3 70  ? 258.007 238.528 188.938 1.00 14.92  ? 70   ASP C C   1 
ATOM   3528 O O   . ASP C 3 70  ? 257.371 239.545 188.661 1.00 15.04  ? 70   ASP C O   1 
ATOM   3529 C CB  . ASP C 3 70  ? 257.348 237.083 187.008 1.00 15.26  ? 70   ASP C CB  1 
ATOM   3530 N N   . PHE C 3 71  ? 259.169 238.550 189.589 1.00 15.18  ? 71   PHE C N   1 
ATOM   3531 C CA  . PHE C 3 71  ? 259.763 239.782 190.099 1.00 15.85  ? 71   PHE C CA  1 
ATOM   3532 C C   . PHE C 3 71  ? 261.189 239.966 189.587 1.00 15.39  ? 71   PHE C C   1 
ATOM   3533 O O   . PHE C 3 71  ? 261.910 238.989 189.373 1.00 17.77  ? 71   PHE C O   1 
ATOM   3534 C CB  . PHE C 3 71  ? 259.770 239.756 191.626 1.00 15.45  ? 71   PHE C CB  1 
ATOM   3535 C CG  . PHE C 3 71  ? 258.403 239.658 192.230 1.00 15.06  ? 71   PHE C CG  1 
ATOM   3536 C CD1 . PHE C 3 71  ? 257.760 238.433 192.325 1.00 14.63  ? 71   PHE C CD1 1 
ATOM   3537 C CD2 . PHE C 3 71  ? 257.760 240.781 192.712 1.00 14.84  ? 71   PHE C CD2 1 
ATOM   3538 C CE1 . PHE C 3 71  ? 256.507 238.339 192.880 1.00 14.22  ? 71   PHE C CE1 1 
ATOM   3539 C CE2 . PHE C 3 71  ? 256.507 240.685 193.271 1.00 14.40  ? 71   PHE C CE2 1 
ATOM   3540 C CZ  . PHE C 3 71  ? 255.882 239.463 193.354 1.00 14.13  ? 71   PHE C CZ  1 
ATOM   3541 N N   . THR C 3 72  ? 261.605 241.219 189.418 1.00 16.09  ? 72   THR C N   1 
ATOM   3542 C CA  . THR C 3 72  ? 262.963 241.514 188.969 1.00 16.34  ? 72   THR C CA  1 
ATOM   3543 C C   . THR C 3 72  ? 263.674 242.526 189.862 1.00 16.45  ? 72   THR C C   1 
ATOM   3544 O O   . THR C 3 72  ? 263.117 243.564 190.222 1.00 15.80  ? 72   THR C O   1 
ATOM   3545 C CB  . THR C 3 72  ? 262.966 242.037 187.518 1.00 17.14  ? 72   THR C CB  1 
ATOM   3546 O OG1 . THR C 3 72  ? 262.382 241.055 186.653 1.00 17.19  ? 72   THR C OG1 1 
ATOM   3547 C CG2 . THR C 3 72  ? 264.393 242.335 187.051 1.00 17.71  ? 72   THR C CG2 1 
ATOM   3548 N N   . PHE C 3 73  ? 264.931 242.230 190.172 1.00 16.97  ? 73   PHE C N   1 
ATOM   3549 C CA  . PHE C 3 73  ? 265.810 243.139 190.901 1.00 16.29  ? 73   PHE C CA  1 
ATOM   3550 C C   . PHE C 3 73  ? 266.911 243.629 189.973 1.00 16.77  ? 73   PHE C C   1 
ATOM   3551 O O   . PHE C 3 73  ? 267.512 242.836 189.250 1.00 20.75  ? 73   PHE C O   1 
ATOM   3552 C CB  . PHE C 3 73  ? 266.414 242.423 192.103 1.00 16.38  ? 73   PHE C CB  1 
ATOM   3553 C CG  . PHE C 3 73  ? 267.386 243.222 192.896 1.00 16.93  ? 73   PHE C CG  1 
ATOM   3554 C CD1 . PHE C 3 73  ? 268.741 243.122 192.657 1.00 18.20  ? 73   PHE C CD1 1 
ATOM   3555 C CD2 . PHE C 3 73  ? 266.949 244.057 193.901 1.00 16.56  ? 73   PHE C CD2 1 
ATOM   3556 C CE1 . PHE C 3 73  ? 269.638 243.845 193.405 1.00 18.17  ? 73   PHE C CE1 1 
ATOM   3557 C CE2 . PHE C 3 73  ? 267.842 244.782 194.652 1.00 16.90  ? 73   PHE C CE2 1 
ATOM   3558 C CZ  . PHE C 3 73  ? 269.190 244.675 194.403 1.00 18.37  ? 73   PHE C CZ  1 
ATOM   3559 N N   . THR C 3 74  ? 267.159 244.935 189.961 1.00 18.64  ? 74   THR C N   1 
ATOM   3560 C CA  . THR C 3 74  ? 268.141 245.491 189.034 1.00 19.24  ? 74   THR C CA  1 
ATOM   3561 C C   . THR C 3 74  ? 269.140 246.439 189.688 1.00 19.16  ? 74   THR C C   1 
ATOM   3562 O O   . THR C 3 74  ? 268.774 247.301 190.489 1.00 20.85  ? 74   THR C O   1 
ATOM   3563 C CB  . THR C 3 74  ? 267.436 246.228 187.877 1.00 20.40  ? 74   THR C CB  1 
ATOM   3564 O OG1 . THR C 3 74  ? 266.600 245.307 187.169 1.00 20.19  ? 74   THR C OG1 1 
ATOM   3565 C CG2 . THR C 3 74  ? 268.455 246.830 186.907 1.00 21.23  ? 74   THR C CG2 1 
ATOM   3566 N N   . ILE C 3 75  ? 270.400 246.316 189.277 1.00 20.29  ? 75   ILE C N   1 
ATOM   3567 C CA  . ILE C 3 75  ? 271.425 247.300 189.599 1.00 21.37  ? 75   ILE C CA  1 
ATOM   3568 C C   . ILE C 3 75  ? 271.860 247.982 188.305 1.00 21.10  ? 75   ILE C C   1 
ATOM   3569 O O   . ILE C 3 75  ? 272.445 247.346 187.428 1.00 25.81  ? 75   ILE C O   1 
ATOM   3570 C CB  . ILE C 3 75  ? 272.644 246.649 190.277 1.00 22.43  ? 75   ILE C CB  1 
ATOM   3571 C CG1 . ILE C 3 75  ? 272.198 245.879 191.522 1.00 21.24  ? 75   ILE C CG1 1 
ATOM   3572 C CG2 . ILE C 3 75  ? 273.661 247.731 190.651 1.00 21.31  ? 75   ILE C CG2 1 
ATOM   3573 C CD1 . ILE C 3 75  ? 273.282 245.011 192.139 1.00 21.74  ? 75   ILE C CD1 1 
ATOM   3574 N N   . SER C 3 76  ? 271.540 249.265 188.164 1.00 21.39  ? 76   SER C N   1 
ATOM   3575 C CA  . SER C 3 76  ? 271.764 249.962 186.897 1.00 23.37  ? 76   SER C CA  1 
ATOM   3576 C C   . SER C 3 76  ? 273.242 250.116 186.549 1.00 23.79  ? 76   SER C C   1 
ATOM   3577 O O   . SER C 3 76  ? 273.606 250.170 185.374 1.00 23.83  ? 76   SER C O   1 
ATOM   3578 C CB  . SER C 3 76  ? 271.117 251.329 186.938 1.00 24.01  ? 76   SER C CB  1 
ATOM   3579 O OG  . SER C 3 76  ? 271.735 252.144 187.893 1.00 23.05  ? 76   SER C OG  1 
ATOM   3580 N N   . SER C 3 77  ? 274.088 250.193 187.567 1.00 24.04  ? 77   SER C N   1 
ATOM   3581 C CA  . SER C 3 77  ? 275.524 250.353 187.374 1.00 23.96  ? 77   SER C CA  1 
ATOM   3582 C C   . SER C 3 77  ? 276.286 249.721 188.524 1.00 23.61  ? 77   SER C C   1 
ATOM   3583 O O   . SER C 3 77  ? 276.458 250.337 189.579 1.00 23.41  ? 77   SER C O   1 
ATOM   3584 C CB  . SER C 3 77  ? 275.874 251.823 187.263 1.00 24.77  ? 77   SER C CB  1 
ATOM   3585 N N   . LEU C 3 78  ? 276.727 248.486 188.332 1.00 23.69  ? 78   LEU C N   1 
ATOM   3586 C CA  . LEU C 3 78  ? 277.343 247.726 189.410 1.00 24.05  ? 78   LEU C CA  1 
ATOM   3587 C C   . LEU C 3 78  ? 278.581 248.419 189.948 1.00 23.30  ? 78   LEU C C   1 
ATOM   3588 O O   . LEU C 3 78  ? 279.465 248.815 189.190 1.00 27.31  ? 78   LEU C O   1 
ATOM   3589 C CB  . LEU C 3 78  ? 277.726 246.324 188.908 1.00 24.54  ? 78   LEU C CB  1 
ATOM   3590 C CG  . LEU C 3 78  ? 278.222 245.326 189.978 1.00 24.97  ? 78   LEU C CG  1 
ATOM   3591 C CD1 . LEU C 3 78  ? 277.057 244.915 190.877 1.00 24.02  ? 78   LEU C CD1 1 
ATOM   3592 C CD2 . LEU C 3 78  ? 278.827 244.118 189.291 1.00 25.22  ? 78   LEU C CD2 1 
ATOM   3593 N N   . GLN C 3 79  ? 278.646 248.543 191.267 1.00 23.86  ? 79   GLN C N   1 
ATOM   3594 C CA  . GLN C 3 79  ? 279.790 249.118 191.956 1.00 24.14  ? 79   GLN C CA  1 
ATOM   3595 C C   . GLN C 3 79  ? 280.616 247.998 192.584 1.00 24.23  ? 79   GLN C C   1 
ATOM   3596 O O   . GLN C 3 79  ? 280.100 246.899 192.783 1.00 23.87  ? 79   GLN C O   1 
ATOM   3597 C CB  . GLN C 3 79  ? 279.300 250.118 193.010 1.00 23.72  ? 79   GLN C CB  1 
ATOM   3598 C CG  . GLN C 3 79  ? 278.536 251.273 192.419 1.00 23.53  ? 79   GLN C CG  1 
ATOM   3599 C CD  . GLN C 3 79  ? 279.359 252.040 191.421 1.00 25.45  ? 79   GLN C CD  1 
ATOM   3600 O OE1 . GLN C 3 79  ? 280.428 252.564 191.748 1.00 25.36  ? 79   GLN C OE1 1 
ATOM   3601 N NE2 . GLN C 3 79  ? 278.873 252.103 190.188 1.00 25.33  ? 79   GLN C NE2 1 
ATOM   3602 N N   . PRO C 3 80  ? 281.892 248.235 192.895 1.00 24.70  ? 80   PRO C N   1 
ATOM   3603 C CA  . PRO C 3 80  ? 282.795 247.309 193.559 1.00 25.00  ? 80   PRO C CA  1 
ATOM   3604 C C   . PRO C 3 80  ? 282.308 246.930 194.957 1.00 23.38  ? 80   PRO C C   1 
ATOM   3605 O O   . PRO C 3 80  ? 282.742 245.927 195.519 1.00 23.82  ? 80   PRO C O   1 
ATOM   3606 C CB  . PRO C 3 80  ? 284.113 248.099 193.599 1.00 24.85  ? 80   PRO C CB  1 
ATOM   3607 C CG  . PRO C 3 80  ? 283.709 249.552 193.433 1.00 25.77  ? 80   PRO C CG  1 
ATOM   3608 C CD  . PRO C 3 80  ? 282.510 249.515 192.522 1.00 25.03  ? 80   PRO C CD  1 
ATOM   3609 N N   . GLU C 3 81  ? 281.415 247.741 195.518 1.00 23.32  ? 81   GLU C N   1 
ATOM   3610 C CA  . GLU C 3 81  ? 280.875 247.488 196.850 1.00 22.62  ? 81   GLU C CA  1 
ATOM   3611 C C   . GLU C 3 81  ? 279.580 246.676 196.805 1.00 22.60  ? 81   GLU C C   1 
ATOM   3612 O O   . GLU C 3 81  ? 278.991 246.383 197.847 1.00 21.84  ? 81   GLU C O   1 
ATOM   3613 C CB  . GLU C 3 81  ? 280.634 248.807 197.589 1.00 21.38  ? 81   GLU C CB  1 
ATOM   3614 C CG  . GLU C 3 81  ? 279.484 249.646 197.047 1.00 22.22  ? 81   GLU C CG  1 
ATOM   3615 C CD  . GLU C 3 81  ? 279.346 250.970 197.756 1.00 22.43  ? 81   GLU C CD  1 
ATOM   3616 O OE1 . GLU C 3 81  ? 280.235 251.320 198.491 1.00 20.52  ? 81   GLU C OE1 1 
ATOM   3617 O OE2 . GLU C 3 81  ? 278.345 251.626 197.571 1.00 22.41  ? 81   GLU C OE2 1 
ATOM   3618 N N   . ASP C 3 82  ? 279.126 246.331 195.602 1.00 23.09  ? 82   ASP C N   1 
ATOM   3619 C CA  . ASP C 3 82  ? 277.849 245.642 195.426 1.00 22.42  ? 82   ASP C CA  1 
ATOM   3620 C C   . ASP C 3 82  ? 278.012 244.137 195.285 1.00 21.81  ? 82   ASP C C   1 
ATOM   3621 O O   . ASP C 3 82  ? 277.101 243.451 194.822 1.00 21.70  ? 82   ASP C O   1 
ATOM   3622 C CB  . ASP C 3 82  ? 277.119 246.164 194.193 1.00 23.20  ? 82   ASP C CB  1 
ATOM   3623 C CG  . ASP C 3 82  ? 276.657 247.592 194.319 1.00 22.90  ? 82   ASP C CG  1 
ATOM   3624 O OD1 . ASP C 3 82  ? 276.389 248.026 195.412 1.00 22.05  ? 82   ASP C OD1 1 
ATOM   3625 O OD2 . ASP C 3 82  ? 276.574 248.249 193.307 1.00 23.36  ? 82   ASP C OD2 1 
ATOM   3626 N N   . ILE C 3 83  ? 279.168 243.619 195.666 1.00 21.97  ? 83   ILE C N   1 
ATOM   3627 C CA  . ILE C 3 83  ? 279.416 242.194 195.533 1.00 21.79  ? 83   ILE C CA  1 
ATOM   3628 C C   . ILE C 3 83  ? 278.852 241.464 196.745 1.00 21.17  ? 83   ILE C C   1 
ATOM   3629 O O   . ILE C 3 83  ? 279.408 241.531 197.842 1.00 21.73  ? 83   ILE C O   1 
ATOM   3630 C CB  . ILE C 3 83  ? 280.926 241.927 195.394 1.00 22.46  ? 83   ILE C CB  1 
ATOM   3631 C CG1 . ILE C 3 83  ? 281.519 242.830 194.280 1.00 23.10  ? 83   ILE C CG1 1 
ATOM   3632 C CG2 . ILE C 3 83  ? 281.188 240.462 195.098 1.00 22.64  ? 83   ILE C CG2 1 
ATOM   3633 C CD1 . ILE C 3 83  ? 280.850 242.693 192.920 1.00 23.16  ? 83   ILE C CD1 1 
ATOM   3634 N N   . ALA C 3 84  ? 277.711 240.812 196.546 1.00 20.27  ? 84   ALA C N   1 
ATOM   3635 C CA  . ALA C 3 84  ? 276.946 240.226 197.639 1.00 18.94  ? 84   ALA C CA  1 
ATOM   3636 C C   . ALA C 3 84  ? 275.968 239.179 197.125 1.00 18.18  ? 84   ALA C C   1 
ATOM   3637 O O   . ALA C 3 84  ? 275.710 239.094 195.922 1.00 19.55  ? 84   ALA C O   1 
ATOM   3638 C CB  . ALA C 3 84  ? 276.191 241.311 198.386 1.00 17.42  ? 84   ALA C CB  1 
ATOM   3639 N N   . THR C 3 85  ? 275.401 238.403 198.042 1.00 17.37  ? 85   THR C N   1 
ATOM   3640 C CA  . THR C 3 85  ? 274.348 237.460 197.691 1.00 17.63  ? 85   THR C CA  1 
ATOM   3641 C C   . THR C 3 85  ? 272.985 238.104 197.900 1.00 14.79  ? 85   THR C C   1 
ATOM   3642 O O   . THR C 3 85  ? 272.693 238.628 198.975 1.00 18.80  ? 85   THR C O   1 
ATOM   3643 C CB  . THR C 3 85  ? 274.441 236.174 198.531 1.00 16.91  ? 85   THR C CB  1 
ATOM   3644 O OG1 . THR C 3 85  ? 275.713 235.552 198.312 1.00 18.63  ? 85   THR C OG1 1 
ATOM   3645 C CG2 . THR C 3 85  ? 273.329 235.199 198.145 1.00 16.69  ? 85   THR C CG2 1 
ATOM   3646 N N   . TYR C 3 86  ? 272.154 238.081 196.871 1.00 16.86  ? 86   TYR C N   1 
ATOM   3647 C CA  . TYR C 3 86  ? 270.844 238.708 196.958 1.00 16.03  ? 86   TYR C CA  1 
ATOM   3648 C C   . TYR C 3 86  ? 269.738 237.674 197.117 1.00 15.06  ? 86   TYR C C   1 
ATOM   3649 O O   . TYR C 3 86  ? 269.703 236.671 196.404 1.00 15.87  ? 86   TYR C O   1 
ATOM   3650 C CB  . TYR C 3 86  ? 270.601 239.580 195.729 1.00 16.07  ? 86   TYR C CB  1 
ATOM   3651 C CG  . TYR C 3 86  ? 271.509 240.792 195.663 1.00 16.71  ? 86   TYR C CG  1 
ATOM   3652 C CD1 . TYR C 3 86  ? 272.769 240.690 195.092 1.00 17.56  ? 86   TYR C CD1 1 
ATOM   3653 C CD2 . TYR C 3 86  ? 271.083 242.004 196.176 1.00 16.32  ? 86   TYR C CD2 1 
ATOM   3654 C CE1 . TYR C 3 86  ? 273.592 241.796 195.037 1.00 17.81  ? 86   TYR C CE1 1 
ATOM   3655 C CE2 . TYR C 3 86  ? 271.908 243.107 196.117 1.00 16.66  ? 86   TYR C CE2 1 
ATOM   3656 C CZ  . TYR C 3 86  ? 273.154 243.006 195.552 1.00 16.80  ? 86   TYR C CZ  1 
ATOM   3657 O OH  . TYR C 3 86  ? 273.970 244.106 195.493 1.00 18.54  ? 86   TYR C OH  1 
ATOM   3658 N N   . TYR C 3 87  ? 268.827 237.926 198.052 1.00 14.44  ? 87   TYR C N   1 
ATOM   3659 C CA  . TYR C 3 87  ? 267.723 237.009 198.314 1.00 14.16  ? 87   TYR C CA  1 
ATOM   3660 C C   . TYR C 3 87  ? 266.382 237.690 198.091 1.00 13.62  ? 87   TYR C C   1 
ATOM   3661 O O   . TYR C 3 87  ? 266.222 238.865 198.427 1.00 13.21  ? 87   TYR C O   1 
ATOM   3662 C CB  . TYR C 3 87  ? 267.749 236.517 199.766 1.00 13.74  ? 87   TYR C CB  1 
ATOM   3663 C CG  . TYR C 3 87  ? 268.981 235.782 200.191 1.00 14.05  ? 87   TYR C CG  1 
ATOM   3664 C CD1 . TYR C 3 87  ? 269.052 234.406 200.070 1.00 14.25  ? 87   TYR C CD1 1 
ATOM   3665 C CD2 . TYR C 3 87  ? 270.034 236.483 200.739 1.00 14.34  ? 87   TYR C CD2 1 
ATOM   3666 C CE1 . TYR C 3 87  ? 270.180 233.738 200.497 1.00 14.08  ? 87   TYR C CE1 1 
ATOM   3667 C CE2 . TYR C 3 87  ? 271.152 235.817 201.165 1.00 14.19  ? 87   TYR C CE2 1 
ATOM   3668 C CZ  . TYR C 3 87  ? 271.232 234.455 201.048 1.00 13.99  ? 87   TYR C CZ  1 
ATOM   3669 O OH  . TYR C 3 87  ? 272.357 233.806 201.490 1.00 14.26  ? 87   TYR C OH  1 
ATOM   3670 N N   . CYS C 3 88  ? 265.393 236.926 197.621 1.00 13.44  ? 88   CYS C N   1 
ATOM   3671 C CA  . CYS C 3 88  ? 264.003 237.381 197.611 1.00 13.31  ? 88   CYS C CA  1 
ATOM   3672 C C   . CYS C 3 88  ? 263.209 236.624 198.673 1.00 12.58  ? 88   CYS C C   1 
ATOM   3673 O O   . CYS C 3 88  ? 263.458 235.445 198.935 1.00 12.26  ? 88   CYS C O   1 
ATOM   3674 C CB  . CYS C 3 88  ? 263.364 237.221 196.222 1.00 14.00  ? 88   CYS C CB  1 
ATOM   3675 S SG  . CYS C 3 88  ? 263.229 235.531 195.597 1.00 15.58  ? 88   CYS C SG  1 
ATOM   3676 N N   . GLN C 3 89  ? 262.255 237.308 199.292 1.00 11.85  ? 89   GLN C N   1 
ATOM   3677 C CA  . GLN C 3 89  ? 261.452 236.714 200.356 1.00 11.09  ? 89   GLN C CA  1 
ATOM   3678 C C   . GLN C 3 89  ? 259.986 237.104 200.240 1.00 10.97  ? 89   GLN C C   1 
ATOM   3679 O O   . GLN C 3 89  ? 259.661 238.261 199.992 1.00 10.94  ? 89   GLN C O   1 
ATOM   3680 C CB  . GLN C 3 89  ? 262.033 237.135 201.710 1.00 11.01  ? 89   GLN C CB  1 
ATOM   3681 C CG  . GLN C 3 89  ? 261.288 236.640 202.940 1.00 10.91  ? 89   GLN C CG  1 
ATOM   3682 C CD  . GLN C 3 89  ? 260.590 237.757 203.697 1.00 10.33  ? 89   GLN C CD  1 
ATOM   3683 O OE1 . GLN C 3 89  ? 261.188 238.801 203.994 1.00 10.27  ? 89   GLN C OE1 1 
ATOM   3684 N NE2 . GLN C 3 89  ? 259.327 237.547 204.021 1.00 10.24  ? 89   GLN C NE2 1 
ATOM   3685 N N   . GLN C 3 90  ? 259.097 236.140 200.441 1.00 10.86  ? 90   GLN C N   1 
ATOM   3686 C CA  . GLN C 3 90  ? 257.668 236.430 200.374 1.00 10.68  ? 90   GLN C CA  1 
ATOM   3687 C C   . GLN C 3 90  ? 257.073 236.550 201.764 1.00 10.28  ? 90   GLN C C   1 
ATOM   3688 O O   . GLN C 3 90  ? 257.450 235.810 202.674 1.00 10.24  ? 90   GLN C O   1 
ATOM   3689 C CB  . GLN C 3 90  ? 256.915 235.358 199.574 1.00 11.44  ? 90   GLN C CB  1 
ATOM   3690 C CG  . GLN C 3 90  ? 256.745 234.010 200.280 1.00 11.58  ? 90   GLN C CG  1 
ATOM   3691 C CD  . GLN C 3 90  ? 255.479 233.929 201.158 1.00 10.95  ? 90   GLN C CD  1 
ATOM   3692 O OE1 . GLN C 3 90  ? 254.569 234.767 201.083 1.00 10.70  ? 90   GLN C OE1 1 
ATOM   3693 N NE2 . GLN C 3 90  ? 255.420 232.902 201.996 1.00 10.74  ? 90   GLN C NE2 1 
ATOM   3694 N N   . TYR C 3 91  ? 256.129 237.472 201.919 1.00 10.23  ? 91   TYR C N   1 
ATOM   3695 C CA  . TYR C 3 91  ? 255.403 237.615 203.174 1.00 9.81   ? 91   TYR C CA  1 
ATOM   3696 C C   . TYR C 3 91  ? 253.911 237.761 202.935 1.00 9.59   ? 91   TYR C C   1 
ATOM   3697 O O   . TYR C 3 91  ? 253.223 238.483 203.654 1.00 9.31   ? 91   TYR C O   1 
ATOM   3698 C CB  . TYR C 3 91  ? 255.941 238.790 203.995 1.00 9.48   ? 91   TYR C CB  1 
ATOM   3699 C CG  . TYR C 3 91  ? 256.023 240.106 203.265 1.00 9.56   ? 91   TYR C CG  1 
ATOM   3700 C CD1 . TYR C 3 91  ? 257.144 240.398 202.521 1.00 10.15  ? 91   TYR C CD1 1 
ATOM   3701 C CD2 . TYR C 3 91  ? 255.000 241.038 203.368 1.00 9.10   ? 91   TYR C CD2 1 
ATOM   3702 C CE1 . TYR C 3 91  ? 257.247 241.601 201.875 1.00 10.28  ? 91   TYR C CE1 1 
ATOM   3703 C CE2 . TYR C 3 91  ? 255.110 242.253 202.717 1.00 9.28   ? 91   TYR C CE2 1 
ATOM   3704 C CZ  . TYR C 3 91  ? 256.236 242.531 201.971 1.00 10.10  ? 91   TYR C CZ  1 
ATOM   3705 O OH  . TYR C 3 91  ? 256.375 243.736 201.316 1.00 10.64  ? 91   TYR C OH  1 
ATOM   3706 N N   . ASP C 3 92  ? 253.413 237.065 201.920 1.00 9.91   ? 92   ASP C N   1 
ATOM   3707 C CA  . ASP C 3 92  ? 251.991 237.060 201.625 1.00 9.96   ? 92   ASP C CA  1 
ATOM   3708 C C   . ASP C 3 92  ? 251.271 236.116 202.575 1.00 9.45   ? 92   ASP C C   1 
ATOM   3709 O O   . ASP C 3 92  ? 250.222 236.451 203.129 1.00 9.56   ? 92   ASP C O   1 
ATOM   3710 C CB  . ASP C 3 92  ? 251.739 236.649 200.173 1.00 10.47  ? 92   ASP C CB  1 
ATOM   3711 C CG  . ASP C 3 92  ? 250.287 236.814 199.743 1.00 10.80  ? 92   ASP C CG  1 
ATOM   3712 O OD1 . ASP C 3 92  ? 249.794 237.915 199.786 1.00 10.93  ? 92   ASP C OD1 1 
ATOM   3713 O OD2 . ASP C 3 92  ? 249.689 235.838 199.363 1.00 11.34  ? 92   ASP C OD2 1 
ATOM   3714 N N   . ASN C 3 93  ? 251.859 234.941 202.783 1.00 10.15  ? 93   ASN C N   1 
ATOM   3715 C CA  . ASN C 3 93  ? 251.255 233.929 203.643 1.00 9.50   ? 93   ASN C CA  1 
ATOM   3716 C C   . ASN C 3 93  ? 252.283 233.226 204.512 1.00 8.63   ? 93   ASN C C   1 
ATOM   3717 O O   . ASN C 3 93  ? 253.360 232.858 204.044 1.00 9.40   ? 93   ASN C O   1 
ATOM   3718 C CB  . ASN C 3 93  ? 250.489 232.911 202.821 1.00 9.98   ? 93   ASN C CB  1 
ATOM   3719 C CG  . ASN C 3 93  ? 249.253 233.481 202.190 1.00 9.96   ? 93   ASN C CG  1 
ATOM   3720 O OD1 . ASN C 3 93  ? 248.234 233.676 202.864 1.00 10.49  ? 93   ASN C OD1 1 
ATOM   3721 N ND2 . ASN C 3 93  ? 249.318 233.751 200.915 1.00 10.54  ? 93   ASN C ND2 1 
ATOM   3722 N N   . LEU C 3 94  ? 251.931 233.011 205.774 1.00 8.78   ? 94   LEU C N   1 
ATOM   3723 C CA  . LEU C 3 94  ? 252.759 232.215 206.668 1.00 8.55   ? 94   LEU C CA  1 
ATOM   3724 C C   . LEU C 3 94  ? 252.616 230.737 206.320 1.00 8.51   ? 94   LEU C C   1 
ATOM   3725 O O   . LEU C 3 94  ? 251.532 230.295 205.941 1.00 9.14   ? 94   LEU C O   1 
ATOM   3726 C CB  . LEU C 3 94  ? 252.347 232.466 208.127 1.00 8.05   ? 94   LEU C CB  1 
ATOM   3727 C CG  . LEU C 3 94  ? 252.694 233.857 208.688 1.00 7.71   ? 94   LEU C CG  1 
ATOM   3728 C CD1 . LEU C 3 94  ? 251.889 234.117 209.940 1.00 6.97   ? 94   LEU C CD1 1 
ATOM   3729 C CD2 . LEU C 3 94  ? 254.184 233.902 209.022 1.00 7.90   ? 94   LEU C CD2 1 
ATOM   3730 N N   . PRO C 3 95  ? 253.698 229.967 206.441 1.00 8.44   ? 95   PRO C N   1 
ATOM   3731 C CA  . PRO C 3 95  ? 255.052 230.319 206.836 1.00 8.65   ? 95   PRO C CA  1 
ATOM   3732 C C   . PRO C 3 95  ? 255.766 231.127 205.761 1.00 8.96   ? 95   PRO C C   1 
ATOM   3733 O O   . PRO C 3 95  ? 255.502 230.960 204.571 1.00 9.40   ? 95   PRO C O   1 
ATOM   3734 C CB  . PRO C 3 95  ? 255.700 228.941 207.011 1.00 8.78   ? 95   PRO C CB  1 
ATOM   3735 C CG  . PRO C 3 95  ? 254.931 228.044 206.071 1.00 8.50   ? 95   PRO C CG  1 
ATOM   3736 C CD  . PRO C 3 95  ? 253.514 228.561 206.119 1.00 8.45   ? 95   PRO C CD  1 
ATOM   3737 N N   . PHE C 3 96  ? 256.691 231.979 206.185 1.00 9.17   ? 96   PHE C N   1 
ATOM   3738 C CA  . PHE C 3 96  ? 257.483 232.775 205.259 1.00 8.99   ? 96   PHE C CA  1 
ATOM   3739 C C   . PHE C 3 96  ? 258.651 231.967 204.724 1.00 9.51   ? 96   PHE C C   1 
ATOM   3740 O O   . PHE C 3 96  ? 259.135 231.046 205.381 1.00 9.48   ? 96   PHE C O   1 
ATOM   3741 C CB  . PHE C 3 96  ? 258.011 234.034 205.943 1.00 9.15   ? 96   PHE C CB  1 
ATOM   3742 C CG  . PHE C 3 96  ? 256.954 235.038 206.332 1.00 9.30   ? 96   PHE C CG  1 
ATOM   3743 C CD1 . PHE C 3 96  ? 255.636 234.939 205.884 1.00 9.35   ? 96   PHE C CD1 1 
ATOM   3744 C CD2 . PHE C 3 96  ? 257.288 236.100 207.151 1.00 8.65   ? 96   PHE C CD2 1 
ATOM   3745 C CE1 . PHE C 3 96  ? 254.697 235.877 206.257 1.00 8.80   ? 96   PHE C CE1 1 
ATOM   3746 C CE2 . PHE C 3 96  ? 256.348 237.032 207.516 1.00 8.12   ? 96   PHE C CE2 1 
ATOM   3747 C CZ  . PHE C 3 96  ? 255.056 236.920 207.073 1.00 8.65   ? 96   PHE C CZ  1 
ATOM   3748 N N   . THR C 3 97  ? 259.089 232.294 203.515 1.00 9.87   ? 97   THR C N   1 
ATOM   3749 C CA  . THR C 3 97  ? 260.223 231.605 202.915 1.00 9.96   ? 97   THR C CA  1 
ATOM   3750 C C   . THR C 3 97  ? 261.190 232.573 202.249 1.00 10.80  ? 97   THR C C   1 
ATOM   3751 O O   . THR C 3 97  ? 260.805 233.665 201.830 1.00 11.02  ? 97   THR C O   1 
ATOM   3752 C CB  . THR C 3 97  ? 259.756 230.577 201.869 1.00 11.04  ? 97   THR C CB  1 
ATOM   3753 O OG1 . THR C 3 97  ? 259.111 231.259 200.791 1.00 11.76  ? 97   THR C OG1 1 
ATOM   3754 C CG2 . THR C 3 97  ? 258.788 229.571 202.476 1.00 10.99  ? 97   THR C CG2 1 
ATOM   3755 N N   . PHE C 3 98  ? 262.436 232.134 202.105 1.00 11.23  ? 98   PHE C N   1 
ATOM   3756 C CA  . PHE C 3 98  ? 263.453 232.863 201.356 1.00 11.88  ? 98   PHE C CA  1 
ATOM   3757 C C   . PHE C 3 98  ? 263.859 232.045 200.137 1.00 12.84  ? 98   PHE C C   1 
ATOM   3758 O O   . PHE C 3 98  ? 263.894 230.815 200.200 1.00 13.31  ? 98   PHE C O   1 
ATOM   3759 C CB  . PHE C 3 98  ? 264.701 233.108 202.213 1.00 12.34  ? 98   PHE C CB  1 
ATOM   3760 C CG  . PHE C 3 98  ? 264.535 234.053 203.380 1.00 12.20  ? 98   PHE C CG  1 
ATOM   3761 C CD1 . PHE C 3 98  ? 264.038 233.607 204.595 1.00 11.83  ? 98   PHE C CD1 1 
ATOM   3762 C CD2 . PHE C 3 98  ? 264.915 235.380 203.271 1.00 12.01  ? 98   PHE C CD2 1 
ATOM   3763 C CE1 . PHE C 3 98  ? 263.919 234.471 205.668 1.00 11.68  ? 98   PHE C CE1 1 
ATOM   3764 C CE2 . PHE C 3 98  ? 264.798 236.242 204.343 1.00 11.93  ? 98   PHE C CE2 1 
ATOM   3765 C CZ  . PHE C 3 98  ? 264.300 235.786 205.541 1.00 11.70  ? 98   PHE C CZ  1 
ATOM   3766 N N   . GLY C 3 99  ? 264.211 232.718 199.048 1.00 13.31  ? 99   GLY C N   1 
ATOM   3767 C CA  . GLY C 3 99  ? 264.694 232.018 197.865 1.00 14.73  ? 99   GLY C CA  1 
ATOM   3768 C C   . GLY C 3 99  ? 266.131 231.539 198.080 1.00 14.87  ? 99   GLY C C   1 
ATOM   3769 O O   . GLY C 3 99  ? 266.775 231.930 199.052 1.00 14.72  ? 99   GLY C O   1 
ATOM   3770 N N   . PRO C 3 100 ? 266.652 230.709 197.169 1.00 15.25  ? 100  PRO C N   1 
ATOM   3771 C CA  . PRO C 3 100 ? 267.975 230.102 197.180 1.00 15.44  ? 100  PRO C CA  1 
ATOM   3772 C C   . PRO C 3 100 ? 269.111 231.103 197.371 1.00 16.00  ? 100  PRO C C   1 
ATOM   3773 O O   . PRO C 3 100 ? 270.104 230.799 198.030 1.00 16.16  ? 100  PRO C O   1 
ATOM   3774 C CB  . PRO C 3 100 ? 268.042 229.475 195.784 1.00 15.69  ? 100  PRO C CB  1 
ATOM   3775 C CG  . PRO C 3 100 ? 266.610 229.166 195.445 1.00 16.05  ? 100  PRO C CG  1 
ATOM   3776 C CD  . PRO C 3 100 ? 265.825 230.321 196.023 1.00 15.47  ? 100  PRO C CD  1 
ATOM   3777 N N   . GLY C 3 101 ? 268.965 232.286 196.785 1.00 15.89  ? 101  GLY C N   1 
ATOM   3778 C CA  . GLY C 3 101 ? 269.999 233.309 196.871 1.00 16.00  ? 101  GLY C CA  1 
ATOM   3779 C C   . GLY C 3 101 ? 270.837 233.351 195.599 1.00 17.23  ? 101  GLY C C   1 
ATOM   3780 O O   . GLY C 3 101 ? 271.324 232.323 195.128 1.00 18.12  ? 101  GLY C O   1 
ATOM   3781 N N   . THR C 3 102 ? 271.015 234.547 195.050 1.00 17.74  ? 102  THR C N   1 
ATOM   3782 C CA  . THR C 3 102 ? 271.804 234.731 193.837 1.00 18.74  ? 102  THR C CA  1 
ATOM   3783 C C   . THR C 3 102 ? 273.137 235.381 194.153 1.00 18.43  ? 102  THR C C   1 
ATOM   3784 O O   . THR C 3 102 ? 273.188 236.461 194.740 1.00 20.80  ? 102  THR C O   1 
ATOM   3785 C CB  . THR C 3 102 ? 271.052 235.594 192.811 1.00 18.56  ? 102  THR C CB  1 
ATOM   3786 O OG1 . THR C 3 102 ? 269.848 234.924 192.425 1.00 17.91  ? 102  THR C OG1 1 
ATOM   3787 C CG2 . THR C 3 102 ? 271.923 235.848 191.580 1.00 19.68  ? 102  THR C CG2 1 
ATOM   3788 N N   . LYS C 3 103 ? 274.220 234.723 193.766 1.00 20.21  ? 103  LYS C N   1 
ATOM   3789 C CA  . LYS C 3 103 ? 275.546 235.252 194.049 1.00 20.34  ? 103  LYS C CA  1 
ATOM   3790 C C   . LYS C 3 103 ? 276.061 236.120 192.912 1.00 20.81  ? 103  LYS C C   1 
ATOM   3791 O O   . LYS C 3 103 ? 276.209 235.654 191.783 1.00 22.30  ? 103  LYS C O   1 
ATOM   3792 C CB  . LYS C 3 103 ? 276.533 234.117 194.317 1.00 21.20  ? 103  LYS C CB  1 
ATOM   3793 N N   . VAL C 3 104 ? 276.370 237.374 193.224 1.00 21.68  ? 104  VAL C N   1 
ATOM   3794 C CA  . VAL C 3 104 ? 276.934 238.281 192.237 1.00 22.24  ? 104  VAL C CA  1 
ATOM   3795 C C   . VAL C 3 104 ? 278.418 238.482 192.493 1.00 22.50  ? 104  VAL C C   1 
ATOM   3796 O O   . VAL C 3 104 ? 278.811 238.939 193.565 1.00 22.60  ? 104  VAL C O   1 
ATOM   3797 C CB  . VAL C 3 104 ? 276.210 239.641 192.278 1.00 21.76  ? 104  VAL C CB  1 
ATOM   3798 C CG1 . VAL C 3 104 ? 276.846 240.617 191.283 1.00 23.92  ? 104  VAL C CG1 1 
ATOM   3799 C CG2 . VAL C 3 104 ? 274.736 239.433 191.956 1.00 21.77  ? 104  VAL C CG2 1 
ATOM   3800 N N   . ASP C 3 105 ? 279.241 238.122 191.514 1.00 23.59  ? 105  ASP C N   1 
ATOM   3801 C CA  . ASP C 3 105 ? 280.684 238.258 191.644 1.00 24.32  ? 105  ASP C CA  1 
ATOM   3802 C C   . ASP C 3 105 ? 281.159 239.520 190.920 1.00 25.05  ? 105  ASP C C   1 
ATOM   3803 O O   . ASP C 3 105 ? 280.358 240.219 190.294 1.00 24.92  ? 105  ASP C O   1 
ATOM   3804 C CB  . ASP C 3 105 ? 281.373 237.004 191.084 1.00 24.94  ? 105  ASP C CB  1 
ATOM   3805 N N   . PHE C 3 106 ? 282.466 239.791 190.981 1.00 25.56  ? 106  PHE C N   1 
ATOM   3806 C CA  . PHE C 3 106 ? 283.065 240.971 190.356 1.00 25.89  ? 106  PHE C CA  1 
ATOM   3807 C C   . PHE C 3 106 ? 283.250 240.767 188.854 1.00 25.00  ? 106  PHE C C   1 
ATOM   3808 O O   . PHE C 3 106 ? 283.665 239.692 188.400 1.00 24.76  ? 106  PHE C O   1 
ATOM   3809 C CB  . PHE C 3 106 ? 284.414 241.306 191.020 1.00 26.06  ? 106  PHE C CB  1 
ATOM   3810 N N   . LYS D 4 5   ? 226.274 291.555 194.946 1.00 134.04 ? 5    LYS H N   1 
ATOM   3811 C CA  . LYS D 4 5   ? 225.427 292.489 194.216 1.00 132.99 ? 5    LYS H CA  1 
ATOM   3812 C C   . LYS D 4 5   ? 224.351 293.077 195.139 1.00 134.11 ? 5    LYS H C   1 
ATOM   3813 O O   . LYS D 4 5   ? 223.431 292.375 195.569 1.00 134.16 ? 5    LYS H O   1 
ATOM   3814 C CB  . LYS D 4 5   ? 224.790 291.804 192.990 1.00 134.09 ? 5    LYS H CB  1 
ATOM   3815 N N   . GLU D 4 6   ? 224.496 294.367 195.455 1.00 133.50 ? 6    GLU H N   1 
ATOM   3816 C CA  . GLU D 4 6   ? 223.597 295.098 196.345 1.00 133.70 ? 6    GLU H CA  1 
ATOM   3817 C C   . GLU D 4 6   ? 222.300 295.500 195.645 1.00 132.72 ? 6    GLU H C   1 
ATOM   3818 O O   . GLU D 4 6   ? 222.321 295.979 194.510 1.00 136.68 ? 6    GLU H O   1 
ATOM   3819 C CB  . GLU D 4 6   ? 224.299 296.353 196.869 1.00 135.45 ? 6    GLU H CB  1 
ATOM   3820 N N   . SER D 4 7   ? 221.182 295.366 196.353 1.00 135.69 ? 7    SER H N   1 
ATOM   3821 C CA  . SER D 4 7   ? 219.895 295.824 195.843 1.00 138.68 ? 7    SER H CA  1 
ATOM   3822 C C   . SER D 4 7   ? 218.972 296.266 196.974 1.00 139.40 ? 7    SER H C   1 
ATOM   3823 O O   . SER D 4 7   ? 219.180 295.922 198.139 1.00 135.82 ? 7    SER H O   1 
ATOM   3824 C CB  . SER D 4 7   ? 219.227 294.727 195.037 1.00 140.21 ? 7    SER H CB  1 
ATOM   3825 N N   . GLY D 4 8   ? 217.946 297.036 196.627 1.00 140.10 ? 8    GLY H N   1 
ATOM   3826 C CA  . GLY D 4 8   ? 216.979 297.514 197.608 1.00 141.38 ? 8    GLY H CA  1 
ATOM   3827 C C   . GLY D 4 8   ? 216.549 298.937 197.273 1.00 143.94 ? 8    GLY H C   1 
ATOM   3828 O O   . GLY D 4 8   ? 216.869 299.442 196.198 1.00 143.12 ? 8    GLY H O   1 
ATOM   3829 N N   . PRO D 4 9   ? 215.808 299.583 198.176 1.00 143.54 ? 9    PRO H N   1 
ATOM   3830 C CA  . PRO D 4 9   ? 215.286 300.935 198.076 1.00 145.02 ? 9    PRO H CA  1 
ATOM   3831 C C   . PRO D 4 9   ? 216.422 301.929 197.887 1.00 143.76 ? 9    PRO H C   1 
ATOM   3832 O O   . PRO D 4 9   ? 217.510 301.743 198.431 1.00 145.91 ? 9    PRO H O   1 
ATOM   3833 C CB  . PRO D 4 9   ? 214.588 301.122 199.431 1.00 144.15 ? 9    PRO H CB  1 
ATOM   3834 C CG  . PRO D 4 9   ? 214.277 299.713 199.900 1.00 144.24 ? 9    PRO H CG  1 
ATOM   3835 C CD  . PRO D 4 9   ? 215.437 298.880 199.403 1.00 143.76 ? 9    PRO H CD  1 
ATOM   3836 N N   . THR D 4 10  ? 216.168 302.975 197.106 1.00 145.51 ? 10   THR H N   1 
ATOM   3837 C CA  . THR D 4 10  ? 217.188 303.982 196.825 1.00 144.73 ? 10   THR H CA  1 
ATOM   3838 C C   . THR D 4 10  ? 216.874 305.327 197.471 1.00 144.05 ? 10   THR H C   1 
ATOM   3839 O O   . THR D 4 10  ? 217.765 306.161 197.640 1.00 142.91 ? 10   THR H O   1 
ATOM   3840 C CB  . THR D 4 10  ? 217.349 304.171 195.307 1.00 144.67 ? 10   THR H CB  1 
ATOM   3841 N N   . LEU D 4 11  ? 215.611 305.546 197.821 1.00 146.76 ? 11   LEU H N   1 
ATOM   3842 C CA  . LEU D 4 11  ? 215.201 306.814 198.411 1.00 146.73 ? 11   LEU H CA  1 
ATOM   3843 C C   . LEU D 4 11  ? 214.302 306.606 199.620 1.00 144.11 ? 11   LEU H C   1 
ATOM   3844 O O   . LEU D 4 11  ? 213.241 305.988 199.519 1.00 144.65 ? 11   LEU H O   1 
ATOM   3845 C CB  . LEU D 4 11  ? 214.471 307.671 197.367 1.00 144.16 ? 11   LEU H CB  1 
ATOM   3846 N N   . VAL D 4 12  ? 214.727 307.136 200.761 1.00 145.70 ? 12   VAL H N   1 
ATOM   3847 C CA  . VAL D 4 12  ? 213.936 307.048 201.980 1.00 144.65 ? 12   VAL H CA  1 
ATOM   3848 C C   . VAL D 4 12  ? 213.836 308.409 202.660 1.00 146.15 ? 12   VAL H C   1 
ATOM   3849 O O   . VAL D 4 12  ? 214.691 309.273 202.472 1.00 144.75 ? 12   VAL H O   1 
ATOM   3850 C CB  . VAL D 4 12  ? 214.544 306.014 202.955 1.00 146.63 ? 12   VAL H CB  1 
ATOM   3851 N N   . LYS D 4 13  ? 212.813 308.582 203.481 1.00 146.88 ? 13   LYS H N   1 
ATOM   3852 C CA  . LYS D 4 13  ? 212.666 309.802 204.263 1.00 145.48 ? 13   LYS H CA  1 
ATOM   3853 C C   . LYS D 4 13  ? 213.531 309.728 205.524 1.00 148.23 ? 13   LYS H C   1 
ATOM   3854 O O   . LYS D 4 13  ? 214.014 308.652 205.873 1.00 139.68 ? 13   LYS H O   1 
ATOM   3855 C CB  . LYS D 4 13  ? 211.192 310.034 204.613 1.00 146.05 ? 13   LYS H CB  1 
ATOM   3856 N N   . PRO D 4 14  ? 213.797 310.867 206.172 1.00 146.77 ? 14   PRO H N   1 
ATOM   3857 C CA  . PRO D 4 14  ? 214.413 310.989 207.482 1.00 146.87 ? 14   PRO H CA  1 
ATOM   3858 C C   . PRO D 4 14  ? 213.654 310.202 208.546 1.00 144.71 ? 14   PRO H C   1 
ATOM   3859 O O   . PRO D 4 14  ? 212.424 310.142 208.534 1.00 145.89 ? 14   PRO H O   1 
ATOM   3860 C CB  . PRO D 4 14  ? 214.340 312.501 207.736 1.00 143.90 ? 14   PRO H CB  1 
ATOM   3861 C CG  . PRO D 4 14  ? 214.348 313.117 206.353 1.00 143.88 ? 14   PRO H CG  1 
ATOM   3862 C CD  . PRO D 4 14  ? 213.561 312.152 205.493 1.00 145.34 ? 14   PRO H CD  1 
ATOM   3863 N N   . THR D 4 15  ? 214.412 309.620 209.469 1.00 145.72 ? 15   THR H N   1 
ATOM   3864 C CA  . THR D 4 15  ? 213.897 308.807 210.568 1.00 144.27 ? 15   THR H CA  1 
ATOM   3865 C C   . THR D 4 15  ? 213.121 307.596 210.060 1.00 145.47 ? 15   THR H C   1 
ATOM   3866 O O   . THR D 4 15  ? 212.104 307.207 210.635 1.00 142.02 ? 15   THR H O   1 
ATOM   3867 C CB  . THR D 4 15  ? 213.005 309.640 211.511 1.00 144.72 ? 15   THR H CB  1 
ATOM   3868 N N   . GLN D 4 16  ? 213.630 306.979 208.999 1.00 141.99 ? 16   GLN H N   1 
ATOM   3869 C CA  . GLN D 4 16  ? 213.042 305.765 208.447 1.00 144.57 ? 16   GLN H CA  1 
ATOM   3870 C C   . GLN D 4 16  ? 214.009 304.596 208.527 1.00 143.85 ? 16   GLN H C   1 
ATOM   3871 O O   . GLN D 4 16  ? 215.221 304.786 208.651 1.00 144.03 ? 16   GLN H O   1 
ATOM   3872 C CB  . GLN D 4 16  ? 212.605 305.977 207.000 1.00 142.69 ? 16   GLN H CB  1 
ATOM   3873 N N   . THR D 4 17  ? 213.468 303.384 208.452 1.00 141.19 ? 17   THR H N   1 
ATOM   3874 C CA  . THR D 4 17  ? 214.289 302.180 208.455 1.00 141.38 ? 17   THR H CA  1 
ATOM   3875 C C   . THR D 4 17  ? 214.504 301.654 207.041 1.00 139.46 ? 17   THR H C   1 
ATOM   3876 O O   . THR D 4 17  ? 213.553 301.455 206.284 1.00 140.31 ? 17   THR H O   1 
ATOM   3877 C CB  . THR D 4 17  ? 213.661 301.078 209.329 1.00 140.40 ? 17   THR H CB  1 
ATOM   3878 N N   . LEU D 4 18  ? 215.765 301.436 206.694 1.00 142.09 ? 18   LEU H N   1 
ATOM   3879 C CA  . LEU D 4 18  ? 216.148 300.946 205.377 1.00 138.30 ? 18   LEU H CA  1 
ATOM   3880 C C   . LEU D 4 18  ? 216.702 299.533 205.435 1.00 136.85 ? 18   LEU H C   1 
ATOM   3881 O O   . LEU D 4 18  ? 217.561 299.228 206.263 1.00 146.67 ? 18   LEU H O   1 
ATOM   3882 C CB  . LEU D 4 18  ? 217.215 301.862 204.777 1.00 135.41 ? 18   LEU H CB  1 
ATOM   3883 N N   . THR D 4 19  ? 216.250 298.682 204.520 1.00 136.53 ? 19   THR H N   1 
ATOM   3884 C CA  . THR D 4 19  ? 216.808 297.340 204.410 1.00 136.01 ? 19   THR H CA  1 
ATOM   3885 C C   . THR D 4 19  ? 217.449 297.115 203.044 1.00 135.98 ? 19   THR H C   1 
ATOM   3886 O O   . THR D 4 19  ? 216.809 297.296 202.007 1.00 137.10 ? 19   THR H O   1 
ATOM   3887 C CB  . THR D 4 19  ? 215.731 296.268 204.660 1.00 134.11 ? 19   THR H CB  1 
ATOM   3888 N N   . LEU D 4 20  ? 218.715 296.702 203.052 1.00 136.60 ? 20   LEU H N   1 
ATOM   3889 C CA  . LEU D 4 20  ? 219.450 296.403 201.825 1.00 135.58 ? 20   LEU H CA  1 
ATOM   3890 C C   . LEU D 4 20  ? 219.866 294.937 201.792 1.00 140.14 ? 20   LEU H C   1 
ATOM   3891 O O   . LEU D 4 20  ? 220.218 294.358 202.819 1.00 126.77 ? 20   LEU H O   1 
ATOM   3892 C CB  . LEU D 4 20  ? 220.701 297.287 201.717 1.00 134.44 ? 20   LEU H CB  1 
ATOM   3893 N N   . THR D 4 21  ? 219.842 294.339 200.606 1.00 132.26 ? 21   THR H N   1 
ATOM   3894 C CA  . THR D 4 21  ? 220.214 292.934 200.469 1.00 134.33 ? 21   THR H CA  1 
ATOM   3895 C C   . THR D 4 21  ? 221.391 292.740 199.511 1.00 134.35 ? 21   THR H C   1 
ATOM   3896 O O   . THR D 4 21  ? 221.412 293.307 198.418 1.00 132.00 ? 21   THR H O   1 
ATOM   3897 C CB  . THR D 4 21  ? 219.012 292.093 199.986 1.00 133.72 ? 21   THR H CB  1 
ATOM   3898 N N   . CYS D 4 22  ? 222.365 291.923 199.933 1.00 133.02 ? 22   CYS H N   1 
ATOM   3899 C CA  . CYS D 4 22  ? 223.515 291.546 199.115 1.00 133.97 ? 22   CYS H CA  1 
ATOM   3900 C C   . CYS D 4 22  ? 223.375 290.114 198.614 1.00 131.21 ? 22   CYS H C   1 
ATOM   3901 O O   . CYS D 4 22  ? 223.269 289.170 199.402 1.00 128.39 ? 22   CYS H O   1 
ATOM   3902 C CB  . CYS D 4 22  ? 224.816 291.682 199.917 1.00 135.90 ? 22   CYS H CB  1 
ATOM   3903 S SG  . CYS D 4 22  ? 226.319 291.228 199.002 1.00 133.91 ? 22   CYS H SG  1 
ATOM   3904 N N   . LYS D 4 23  ? 223.398 289.949 197.299 1.00 130.34 ? 23   LYS H N   1 
ATOM   3905 C CA  . LYS D 4 23  ? 223.348 288.625 196.696 1.00 128.25 ? 23   LYS H CA  1 
ATOM   3906 C C   . LYS D 4 23  ? 224.758 288.145 196.376 1.00 126.60 ? 23   LYS H C   1 
ATOM   3907 O O   . LYS D 4 23  ? 225.515 288.830 195.684 1.00 128.29 ? 23   LYS H O   1 
ATOM   3908 C CB  . LYS D 4 23  ? 222.490 288.648 195.432 1.00 127.09 ? 23   LYS H CB  1 
ATOM   3909 N N   . LEU D 4 24  ? 225.126 286.976 196.888 1.00 124.62 ? 24   LEU H N   1 
ATOM   3910 C CA  . LEU D 4 24  ? 226.476 286.465 196.669 1.00 123.34 ? 24   LEU H CA  1 
ATOM   3911 C C   . LEU D 4 24  ? 226.481 285.234 195.778 1.00 122.84 ? 24   LEU H C   1 
ATOM   3912 O O   . LEU D 4 24  ? 225.494 284.505 195.697 1.00 122.07 ? 24   LEU H O   1 
ATOM   3913 C CB  . LEU D 4 24  ? 227.158 286.170 198.015 1.00 124.44 ? 24   LEU H CB  1 
ATOM   3914 N N   . SER D 4 25  ? 227.603 285.015 195.100 1.00 121.88 ? 25   SER H N   1 
ATOM   3915 C CA  . SER D 4 25  ? 227.771 283.851 194.242 1.00 120.54 ? 25   SER H CA  1 
ATOM   3916 C C   . SER D 4 25  ? 229.231 283.424 194.187 1.00 119.14 ? 25   SER H C   1 
ATOM   3917 O O   . SER D 4 25  ? 230.132 284.204 194.502 1.00 118.71 ? 25   SER H O   1 
ATOM   3918 C CB  . SER D 4 25  ? 227.270 284.150 192.843 1.00 120.25 ? 25   SER H CB  1 
ATOM   3919 N N   . GLY D 4 26  ? 229.459 282.174 193.793 1.00 119.25 ? 26   GLY H N   1 
ATOM   3920 C CA  . GLY D 4 26  ? 230.806 281.619 193.704 1.00 118.27 ? 26   GLY H CA  1 
ATOM   3921 C C   . GLY D 4 26  ? 231.147 280.847 194.972 1.00 117.17 ? 26   GLY H C   1 
ATOM   3922 O O   . GLY D 4 26  ? 232.114 280.086 195.016 1.00 117.90 ? 26   GLY H O   1 
ATOM   3923 N N   . PHE D 4 27  ? 230.336 281.052 196.002 1.00 116.37 ? 27   PHE H N   1 
ATOM   3924 C CA  . PHE D 4 27  ? 230.494 280.387 197.285 1.00 115.89 ? 27   PHE H CA  1 
ATOM   3925 C C   . PHE D 4 27  ? 229.162 280.383 198.015 1.00 114.95 ? 27   PHE H C   1 
ATOM   3926 O O   . PHE D 4 27  ? 228.283 281.188 197.713 1.00 116.51 ? 27   PHE H O   1 
ATOM   3927 C CB  . PHE D 4 27  ? 231.555 281.098 198.129 1.00 115.24 ? 27   PHE H CB  1 
ATOM   3928 N N   . SER D 4 28  ? 229.014 279.500 198.992 1.00 113.32 ? 28   SER H N   1 
ATOM   3929 C CA  . SER D 4 28  ? 227.812 279.516 199.812 1.00 114.06 ? 28   SER H CA  1 
ATOM   3930 C C   . SER D 4 28  ? 228.035 280.277 201.104 1.00 108.65 ? 28   SER H C   1 
ATOM   3931 O O   . SER D 4 28  ? 229.120 280.240 201.684 1.00 109.26 ? 28   SER H O   1 
ATOM   3932 C CB  . SER D 4 28  ? 227.333 278.116 200.120 1.00 111.13 ? 28   SER H CB  1 
ATOM   3933 N N   . VAL D 4 29  ? 226.989 280.944 201.569 1.00 114.38 ? 29   VAL H N   1 
ATOM   3934 C CA  . VAL D 4 29  ? 227.047 281.715 202.802 1.00 112.49 ? 29   VAL H CA  1 
ATOM   3935 C C   . VAL D 4 29  ? 227.182 280.799 204.016 1.00 110.80 ? 29   VAL H C   1 
ATOM   3936 O O   . VAL D 4 29  ? 227.466 281.256 205.123 1.00 110.73 ? 29   VAL H O   1 
ATOM   3937 C CB  . VAL D 4 29  ? 225.788 282.598 202.935 1.00 115.17 ? 29   VAL H CB  1 
ATOM   3938 N N   . ASN D 4 30  ? 226.945 279.506 203.810 1.00 109.86 ? 30   ASN H N   1 
ATOM   3939 C CA  . ASN D 4 30  ? 226.999 278.528 204.886 1.00 109.37 ? 30   ASN H CA  1 
ATOM   3940 C C   . ASN D 4 30  ? 228.343 277.808 204.944 1.00 105.88 ? 30   ASN H C   1 
ATOM   3941 O O   . ASN D 4 30  ? 228.527 276.891 205.746 1.00 104.84 ? 30   ASN H O   1 
ATOM   3942 C CB  . ASN D 4 30  ? 225.890 277.513 204.714 1.00 110.96 ? 30   ASN H CB  1 
ATOM   3943 N N   . THR D 4 31  ? 229.276 278.203 204.083 1.00 104.07 ? 31   THR H N   1 
ATOM   3944 C CA  . THR D 4 31  ? 230.581 277.552 204.031 1.00 98.33  ? 31   THR H CA  1 
ATOM   3945 C C   . THR D 4 31  ? 231.522 278.114 205.089 1.00 96.60  ? 31   THR H C   1 
ATOM   3946 O O   . THR D 4 31  ? 231.601 279.326 205.292 1.00 99.08  ? 31   THR H O   1 
ATOM   3947 C CB  . THR D 4 31  ? 231.207 277.678 202.627 1.00 97.44  ? 31   THR H CB  1 
ATOM   3948 N N   . GLY D 4 32  ? 232.233 277.227 205.773 1.00 93.56  ? 32   GLY H N   1 
ATOM   3949 C CA  . GLY D 4 32  ? 233.146 277.653 206.822 1.00 86.94  ? 32   GLY H CA  1 
ATOM   3950 C C   . GLY D 4 32  ? 234.246 278.543 206.260 1.00 87.06  ? 32   GLY H C   1 
ATOM   3951 O O   . GLY D 4 32  ? 234.746 278.314 205.159 1.00 84.45  ? 32   GLY H O   1 
ATOM   3952 N N   . GLY D 4 33  ? 234.614 279.569 207.020 1.00 92.24  ? 33   GLY H N   1 
ATOM   3953 C CA  . GLY D 4 33  ? 235.647 280.509 206.604 1.00 94.08  ? 33   GLY H CA  1 
ATOM   3954 C C   . GLY D 4 33  ? 235.055 281.724 205.892 1.00 97.18  ? 33   GLY H C   1 
ATOM   3955 O O   . GLY D 4 33  ? 235.754 282.706 205.647 1.00 99.80  ? 33   GLY H O   1 
ATOM   3956 N N   . VAL D 4 34  ? 233.766 281.653 205.565 1.00 99.33  ? 34   VAL H N   1 
ATOM   3957 C CA  . VAL D 4 34  ? 233.078 282.737 204.872 1.00 102.62 ? 34   VAL H CA  1 
ATOM   3958 C C   . VAL D 4 34  ? 232.544 283.803 205.819 1.00 104.97 ? 34   VAL H C   1 
ATOM   3959 O O   . VAL D 4 34  ? 231.980 283.496 206.870 1.00 105.00 ? 34   VAL H O   1 
ATOM   3960 C CB  . VAL D 4 34  ? 231.912 282.179 204.028 1.00 102.62 ? 34   VAL H CB  1 
ATOM   3961 N N   . GLY D 4 35  ? 232.688 285.058 205.413 1.00 110.87 ? 35   GLY H N   1 
ATOM   3962 C CA  . GLY D 4 35  ? 232.101 286.179 206.132 1.00 111.21 ? 35   GLY H CA  1 
ATOM   3963 C C   . GLY D 4 35  ? 231.650 287.242 205.139 1.00 114.92 ? 35   GLY H C   1 
ATOM   3964 O O   . GLY D 4 35  ? 232.146 287.295 204.014 1.00 115.16 ? 35   GLY H O   1 
ATOM   3965 N N   . VAL D 4 36  ? 230.701 288.075 205.550 1.00 117.11 ? 36   VAL H N   1 
ATOM   3966 C CA  . VAL D 4 36  ? 230.233 289.181 204.719 1.00 118.49 ? 36   VAL H CA  1 
ATOM   3967 C C   . VAL D 4 36  ? 230.129 290.464 205.537 1.00 119.55 ? 36   VAL H C   1 
ATOM   3968 O O   . VAL D 4 36  ? 229.546 290.471 206.621 1.00 120.53 ? 36   VAL H O   1 
ATOM   3969 C CB  . VAL D 4 36  ? 228.871 288.845 204.075 1.00 118.74 ? 36   VAL H CB  1 
ATOM   3970 N N   . GLY D 4 37  ? 230.694 291.548 205.019 1.00 121.73 ? 37   GLY H N   1 
ATOM   3971 C CA  . GLY D 4 37  ? 230.655 292.823 205.719 1.00 123.72 ? 37   GLY H CA  1 
ATOM   3972 C C   . GLY D 4 37  ? 229.926 293.894 204.925 1.00 127.91 ? 37   GLY H C   1 
ATOM   3973 O O   . GLY D 4 37  ? 229.807 293.808 203.703 1.00 127.31 ? 37   GLY H O   1 
ATOM   3974 N N   . TRP D 4 38  ? 229.480 294.929 205.633 1.00 128.65 ? 38   TRP H N   1 
ATOM   3975 C CA  . TRP D 4 38  ? 228.843 296.081 205.016 1.00 133.37 ? 38   TRP H CA  1 
ATOM   3976 C C   . TRP D 4 38  ? 229.593 297.366 205.329 1.00 135.40 ? 38   TRP H C   1 
ATOM   3977 O O   . TRP D 4 38  ? 229.944 297.637 206.481 1.00 123.16 ? 38   TRP H O   1 
ATOM   3978 C CB  . TRP D 4 38  ? 227.400 296.205 205.485 1.00 132.97 ? 38   TRP H CB  1 
ATOM   3979 N N   . ILE D 4 39  ? 229.825 298.146 204.283 1.00 133.96 ? 39   ILE H N   1 
ATOM   3980 C CA  . ILE D 4 39  ? 230.554 299.406 204.346 1.00 131.43 ? 39   ILE H CA  1 
ATOM   3981 C C   . ILE D 4 39  ? 229.792 300.494 203.590 1.00 138.25 ? 39   ILE H C   1 
ATOM   3982 O O   . ILE D 4 39  ? 229.224 300.230 202.533 1.00 131.84 ? 39   ILE H O   1 
ATOM   3983 C CB  . ILE D 4 39  ? 231.968 299.216 203.751 1.00 132.84 ? 39   ILE H CB  1 
ATOM   3984 N N   . ARG D 4 40  ? 229.784 301.715 204.114 1.00 135.85 ? 40   ARG H N   1 
ATOM   3985 C CA  . ARG D 4 40  ? 229.128 302.811 203.406 1.00 134.51 ? 40   ARG H CA  1 
ATOM   3986 C C   . ARG D 4 40  ? 230.131 303.885 203.027 1.00 138.25 ? 40   ARG H C   1 
ATOM   3987 O O   . ARG D 4 40  ? 231.141 304.074 203.704 1.00 133.53 ? 40   ARG H O   1 
ATOM   3988 C CB  . ARG D 4 40  ? 228.028 303.449 204.239 1.00 136.20 ? 40   ARG H CB  1 
ATOM   3989 N N   . GLN D 4 41  ? 229.842 304.606 201.954 1.00 127.60 ? 41   GLN H N   1 
ATOM   3990 C CA  . GLN D 4 41  ? 230.723 305.674 201.515 1.00 134.59 ? 41   GLN H CA  1 
ATOM   3991 C C   . GLN D 4 41  ? 229.948 306.899 201.041 1.00 147.61 ? 41   GLN H C   1 
ATOM   3992 O O   . GLN D 4 41  ? 229.466 306.920 199.908 1.00 134.91 ? 41   GLN H O   1 
ATOM   3993 C CB  . GLN D 4 41  ? 231.612 305.173 200.389 1.00 137.12 ? 41   GLN H CB  1 
ATOM   3994 N N   . PRO D 4 42  ? 229.795 307.914 201.897 1.00 136.72 ? 42   PRO H N   1 
ATOM   3995 C CA  . PRO D 4 42  ? 229.158 309.183 201.610 1.00 136.77 ? 42   PRO H CA  1 
ATOM   3996 C C   . PRO D 4 42  ? 229.895 309.833 200.443 1.00 141.76 ? 42   PRO H C   1 
ATOM   3997 O O   . PRO D 4 42  ? 231.082 309.567 200.254 1.00 136.63 ? 42   PRO H O   1 
ATOM   3998 C CB  . PRO D 4 42  ? 229.336 309.955 202.922 1.00 138.20 ? 42   PRO H CB  1 
ATOM   3999 C CG  . PRO D 4 42  ? 229.519 308.878 203.982 1.00 137.43 ? 42   PRO H CG  1 
ATOM   4000 C CD  . PRO D 4 42  ? 230.259 307.760 203.277 1.00 136.96 ? 42   PRO H CD  1 
ATOM   4001 N N   . PRO D 4 43  ? 229.221 310.651 199.632 1.00 138.83 ? 43   PRO H N   1 
ATOM   4002 C CA  . PRO D 4 43  ? 229.773 311.333 198.478 1.00 140.81 ? 43   PRO H CA  1 
ATOM   4003 C C   . PRO D 4 43  ? 231.036 312.106 198.832 1.00 140.05 ? 43   PRO H C   1 
ATOM   4004 O O   . PRO D 4 43  ? 231.006 313.012 199.664 1.00 140.24 ? 43   PRO H O   1 
ATOM   4005 C CB  . PRO D 4 43  ? 228.631 312.285 198.097 1.00 141.94 ? 43   PRO H CB  1 
ATOM   4006 C CG  . PRO D 4 43  ? 227.377 311.580 198.573 1.00 139.37 ? 43   PRO H CG  1 
ATOM   4007 C CD  . PRO D 4 43  ? 227.788 310.889 199.858 1.00 141.45 ? 43   PRO H CD  1 
ATOM   4008 N N   . GLY D 4 44  ? 232.139 311.765 198.171 1.00 141.17 ? 44   GLY H N   1 
ATOM   4009 C CA  . GLY D 4 44  ? 233.404 312.471 198.351 1.00 141.34 ? 44   GLY H CA  1 
ATOM   4010 C C   . GLY D 4 44  ? 234.137 312.085 199.636 1.00 140.24 ? 44   GLY H C   1 
ATOM   4011 O O   . GLY D 4 44  ? 235.152 312.692 199.978 1.00 141.13 ? 44   GLY H O   1 
ATOM   4012 N N   . LYS D 4 45  ? 233.619 311.093 200.356 1.00 139.47 ? 45   LYS H N   1 
ATOM   4013 C CA  . LYS D 4 45  ? 234.203 310.708 201.638 1.00 138.78 ? 45   LYS H CA  1 
ATOM   4014 C C   . LYS D 4 45  ? 234.840 309.322 201.605 1.00 138.93 ? 45   LYS H C   1 
ATOM   4015 O O   . LYS D 4 45  ? 234.636 308.548 200.668 1.00 137.75 ? 45   LYS H O   1 
ATOM   4016 C CB  . LYS D 4 45  ? 233.149 310.776 202.743 1.00 138.71 ? 45   LYS H CB  1 
ATOM   4017 N N   . ALA D 4 46  ? 235.626 309.028 202.639 1.00 136.68 ? 46   ALA H N   1 
ATOM   4018 C CA  . ALA D 4 46  ? 236.295 307.741 202.792 1.00 135.08 ? 46   ALA H CA  1 
ATOM   4019 C C   . ALA D 4 46  ? 235.317 306.662 203.247 1.00 135.21 ? 46   ALA H C   1 
ATOM   4020 O O   . ALA D 4 46  ? 234.219 306.960 203.717 1.00 136.83 ? 46   ALA H O   1 
ATOM   4021 C CB  . ALA D 4 46  ? 237.444 307.857 203.783 1.00 132.90 ? 46   ALA H CB  1 
ATOM   4022 N N   . LEU D 4 47  ? 235.730 305.408 203.101 1.00 135.34 ? 47   LEU H N   1 
ATOM   4023 C CA  . LEU D 4 47  ? 234.917 304.258 203.483 1.00 132.06 ? 47   LEU H CA  1 
ATOM   4024 C C   . LEU D 4 47  ? 234.669 304.213 204.990 1.00 134.77 ? 47   LEU H C   1 
ATOM   4025 O O   . LEU D 4 47  ? 235.588 304.415 205.784 1.00 133.17 ? 47   LEU H O   1 
ATOM   4026 C CB  . LEU D 4 47  ? 235.644 302.970 203.069 1.00 133.30 ? 47   LEU H CB  1 
ATOM   4027 N N   . GLU D 4 48  ? 233.432 303.904 205.378 1.00 134.68 ? 48   GLU H N   1 
ATOM   4028 C CA  . GLU D 4 48  ? 233.083 303.726 206.786 1.00 131.28 ? 48   GLU H CA  1 
ATOM   4029 C C   . GLU D 4 48  ? 232.524 302.332 207.054 1.00 133.29 ? 48   GLU H C   1 
ATOM   4030 O O   . GLU D 4 48  ? 231.542 301.916 206.437 1.00 130.14 ? 48   GLU H O   1 
ATOM   4031 C CB  . GLU D 4 48  ? 232.045 304.760 207.228 1.00 132.86 ? 48   GLU H CB  1 
ATOM   4032 N N   . TRP D 4 49  ? 233.137 301.616 207.988 1.00 131.01 ? 49   TRP H N   1 
ATOM   4033 C CA  . TRP D 4 49  ? 232.676 300.279 208.342 1.00 132.42 ? 49   TRP H CA  1 
ATOM   4034 C C   . TRP D 4 49  ? 231.381 300.332 209.137 1.00 132.86 ? 49   TRP H C   1 
ATOM   4035 O O   . TRP D 4 49  ? 231.261 301.102 210.088 1.00 131.14 ? 49   TRP H O   1 
ATOM   4036 C CB  . TRP D 4 49  ? 233.737 299.548 209.163 1.00 130.16 ? 49   TRP H CB  1 
ATOM   4037 N N   . LEU D 4 50  ? 230.419 299.495 208.759 1.00 135.09 ? 50   LEU H N   1 
ATOM   4038 C CA  . LEU D 4 50  ? 229.166 299.408 209.491 1.00 131.75 ? 50   LEU H CA  1 
ATOM   4039 C C   . LEU D 4 50  ? 229.139 298.180 210.388 1.00 134.40 ? 50   LEU H C   1 
ATOM   4040 O O   . LEU D 4 50  ? 229.032 298.293 211.611 1.00 123.26 ? 50   LEU H O   1 
ATOM   4041 C CB  . LEU D 4 50  ? 227.991 299.331 208.506 1.00 133.40 ? 50   LEU H CB  1 
ATOM   4042 N N   . ALA D 4 51  ? 229.192 297.004 209.767 1.00 128.57 ? 51   ALA H N   1 
ATOM   4043 C CA  . ALA D 4 51  ? 229.059 295.749 210.500 1.00 130.68 ? 51   ALA H CA  1 
ATOM   4044 C C   . ALA D 4 51  ? 229.521 294.561 209.663 1.00 131.45 ? 51   ALA H C   1 
ATOM   4045 O O   . ALA D 4 51  ? 229.593 294.645 208.438 1.00 128.52 ? 51   ALA H O   1 
ATOM   4046 C CB  . ALA D 4 51  ? 227.616 295.556 210.925 1.00 130.24 ? 51   ALA H CB  1 
ATOM   4047 N N   . LEU D 4 52  ? 229.801 293.441 210.326 1.00 125.66 ? 52   LEU H N   1 
ATOM   4048 C CA  . LEU D 4 52  ? 230.100 292.198 209.618 1.00 123.65 ? 52   LEU H CA  1 
ATOM   4049 C C   . LEU D 4 52  ? 229.467 290.983 210.282 1.00 121.53 ? 52   LEU H C   1 
ATOM   4050 O O   . LEU D 4 52  ? 229.317 290.930 211.505 1.00 123.14 ? 52   LEU H O   1 
ATOM   4051 C CB  . LEU D 4 52  ? 231.619 292.002 209.489 1.00 122.30 ? 52   LEU H CB  1 
ATOM   4052 N N   . ILE D 4 53  ? 229.132 289.989 209.464 1.00 118.81 ? 53   ILE H N   1 
ATOM   4053 C CA  . ILE D 4 53  ? 228.586 288.724 209.944 1.00 114.62 ? 53   ILE H CA  1 
ATOM   4054 C C   . ILE D 4 53  ? 229.445 287.546 209.489 1.00 118.84 ? 53   ILE H C   1 
ATOM   4055 O O   . ILE D 4 53  ? 229.864 287.477 208.333 1.00 113.96 ? 53   ILE H O   1 
ATOM   4056 C CB  . ILE D 4 53  ? 227.129 288.546 209.461 1.00 118.26 ? 53   ILE H CB  1 
ATOM   4057 N N   . TYR D 4 54  ? 229.703 286.619 210.406 1.00 110.65 ? 54   TYR H N   1 
ATOM   4058 C CA  . TYR D 4 54  ? 230.500 285.436 210.102 1.00 111.82 ? 54   TYR H CA  1 
ATOM   4059 C C   . TYR D 4 54  ? 229.624 284.216 209.831 1.00 112.71 ? 54   TYR H C   1 
ATOM   4060 O O   . TYR D 4 54  ? 228.479 284.143 210.275 1.00 112.43 ? 54   TYR H O   1 
ATOM   4061 C CB  . TYR D 4 54  ? 231.472 285.126 211.245 1.00 109.03 ? 54   TYR H CB  1 
ATOM   4062 N N   . TRP D 4 55  ? 230.189 283.240 209.128 1.00 103.93 ? 55   TRP H N   1 
ATOM   4063 C CA  . TRP D 4 55  ? 229.528 281.966 208.841 1.00 104.86 ? 55   TRP H CA  1 
ATOM   4064 C C   . TRP D 4 55  ? 228.985 281.271 210.091 1.00 109.14 ? 55   TRP H C   1 
ATOM   4065 O O   . TRP D 4 55  ? 228.071 280.451 210.000 1.00 106.33 ? 55   TRP H O   1 
ATOM   4066 C CB  . TRP D 4 55  ? 230.512 281.028 208.140 1.00 100.02 ? 55   TRP H CB  1 
ATOM   4067 C CG  . TRP D 4 55  ? 231.712 280.687 208.984 1.00 108.52 ? 55   TRP H CG  1 
ATOM   4068 C CD1 . TRP D 4 55  ? 232.876 281.392 209.066 1.00 98.21  ? 55   TRP H CD1 1 
ATOM   4069 C CD2 . TRP D 4 55  ? 231.875 279.547 209.858 1.00 96.04  ? 55   TRP H CD2 1 
ATOM   4070 N NE1 . TRP D 4 55  ? 233.740 280.778 209.930 1.00 95.79  ? 55   TRP H NE1 1 
ATOM   4071 C CE2 . TRP D 4 55  ? 233.147 279.648 210.424 1.00 95.87  ? 55   TRP H CE2 1 
ATOM   4072 C CE3 . TRP D 4 55  ? 231.058 278.467 210.199 1.00 97.04  ? 55   TRP H CE3 1 
ATOM   4073 C CZ2 . TRP D 4 55  ? 233.626 278.711 211.317 1.00 90.30  ? 55   TRP H CZ2 1 
ATOM   4074 C CZ3 . TRP D 4 55  ? 231.540 277.525 211.095 1.00 91.92  ? 55   TRP H CZ3 1 
ATOM   4075 C CH2 . TRP D 4 55  ? 232.791 277.645 211.639 1.00 86.52  ? 55   TRP H CH2 1 
ATOM   4076 N N   . ASN D 4 56  ? 229.564 281.578 211.248 1.00 102.90 ? 56   ASN H N   1 
ATOM   4077 C CA  . ASN D 4 56  ? 229.169 280.950 212.506 1.00 104.45 ? 56   ASN H CA  1 
ATOM   4078 C C   . ASN D 4 56  ? 228.156 281.798 213.272 1.00 111.32 ? 56   ASN H C   1 
ATOM   4079 O O   . ASN D 4 56  ? 227.899 281.560 214.452 1.00 109.61 ? 56   ASN H O   1 
ATOM   4080 C CB  . ASN D 4 56  ? 230.391 280.656 213.354 1.00 104.42 ? 56   ASN H CB  1 
ATOM   4081 N N   . ASP D 4 57  ? 227.577 282.775 212.578 1.00 108.27 ? 57   ASP H N   1 
ATOM   4082 C CA  . ASP D 4 57  ? 226.529 283.657 213.090 1.00 109.45 ? 57   ASP H CA  1 
ATOM   4083 C C   . ASP D 4 57  ? 227.030 284.683 214.104 1.00 113.83 ? 57   ASP H C   1 
ATOM   4084 O O   . ASP D 4 57  ? 226.238 285.459 214.648 1.00 113.75 ? 57   ASP H O   1 
ATOM   4085 C CB  . ASP D 4 57  ? 225.386 282.847 213.722 1.00 111.95 ? 57   ASP H CB  1 
ATOM   4086 N N   . ASP D 4 58  ? 228.343 284.741 214.320 1.00 110.20 ? 58   ASP H N   1 
ATOM   4087 C CA  . ASP D 4 58  ? 228.894 285.788 215.172 1.00 113.02 ? 58   ASP H CA  1 
ATOM   4088 C C   . ASP D 4 58  ? 228.913 287.103 214.402 1.00 119.58 ? 58   ASP H C   1 
ATOM   4089 O O   . ASP D 4 58  ? 228.957 287.108 213.170 1.00 112.57 ? 58   ASP H O   1 
ATOM   4090 C CB  . ASP D 4 58  ? 230.294 285.420 215.668 1.00 113.58 ? 58   ASP H CB  1 
ATOM   4091 N N   . LYS D 4 59  ? 228.829 288.218 215.119 1.00 114.35 ? 59   LYS H N   1 
ATOM   4092 C CA  . LYS D 4 59  ? 228.719 289.519 214.464 1.00 120.27 ? 59   LYS H CA  1 
ATOM   4093 C C   . LYS D 4 59  ? 229.484 290.621 215.186 1.00 120.57 ? 59   LYS H C   1 
ATOM   4094 O O   . LYS D 4 59  ? 229.527 290.664 216.415 1.00 119.62 ? 59   LYS H O   1 
ATOM   4095 C CB  . LYS D 4 59  ? 227.245 289.918 214.342 1.00 120.82 ? 59   LYS H CB  1 
ATOM   4096 N N   . LEU D 4 60  ? 230.034 291.550 214.408 1.00 123.31 ? 60   LEU H N   1 
ATOM   4097 C CA  . LEU D 4 60  ? 230.678 292.737 214.958 1.00 127.19 ? 60   LEU H CA  1 
ATOM   4098 C C   . LEU D 4 60  ? 230.080 293.997 214.347 1.00 128.76 ? 60   LEU H C   1 
ATOM   4099 O O   . LEU D 4 60  ? 229.722 294.018 213.169 1.00 114.76 ? 60   LEU H O   1 
ATOM   4100 C CB  . LEU D 4 60  ? 232.191 292.706 214.702 1.00 124.58 ? 60   LEU H CB  1 
ATOM   4101 N N   . TYR D 4 61  ? 229.979 295.050 215.150 1.00 129.73 ? 61   TYR H N   1 
ATOM   4102 C CA  . TYR D 4 61  ? 229.436 296.323 214.686 1.00 133.01 ? 61   TYR H CA  1 
ATOM   4103 C C   . TYR D 4 61  ? 230.348 297.482 215.064 1.00 134.58 ? 61   TYR H C   1 
ATOM   4104 O O   . TYR D 4 61  ? 231.001 297.448 216.106 1.00 130.63 ? 61   TYR H O   1 
ATOM   4105 C CB  . TYR D 4 61  ? 228.054 296.565 215.295 1.00 132.09 ? 61   TYR H CB  1 
ATOM   4106 N N   . SER D 4 62  ? 230.343 298.532 214.246 1.00 132.00 ? 62   SER H N   1 
ATOM   4107 C CA  . SER D 4 62  ? 231.033 299.769 214.590 1.00 131.61 ? 62   SER H CA  1 
ATOM   4108 C C   . SER D 4 62  ? 230.284 300.471 215.728 1.00 130.07 ? 62   SER H C   1 
ATOM   4109 O O   . SER D 4 62  ? 229.131 300.860 215.538 1.00 135.10 ? 62   SER H O   1 
ATOM   4110 C CB  . SER D 4 62  ? 231.105 300.680 213.379 1.00 130.25 ? 62   SER H CB  1 
ATOM   4111 N N   . PRO D 4 63  ? 230.919 300.674 216.894 1.00 133.99 ? 63   PRO H N   1 
ATOM   4112 C CA  . PRO D 4 63  ? 230.343 301.198 218.127 1.00 134.04 ? 63   PRO H CA  1 
ATOM   4113 C C   . PRO D 4 63  ? 229.496 302.458 217.942 1.00 134.30 ? 63   PRO H C   1 
ATOM   4114 O O   . PRO D 4 63  ? 228.474 302.618 218.611 1.00 134.38 ? 63   PRO H O   1 
ATOM   4115 C CB  . PRO D 4 63  ? 231.600 301.511 218.948 1.00 134.95 ? 63   PRO H CB  1 
ATOM   4116 C CG  . PRO D 4 63  ? 232.609 300.488 218.491 1.00 135.94 ? 63   PRO H CG  1 
ATOM   4117 C CD  . PRO D 4 63  ? 232.349 300.322 217.006 1.00 131.62 ? 63   PRO H CD  1 
ATOM   4118 N N   . SER D 4 64  ? 229.907 303.341 217.038 1.00 133.95 ? 64   SER H N   1 
ATOM   4119 C CA  . SER D 4 64  ? 229.186 304.598 216.829 1.00 133.88 ? 64   SER H CA  1 
ATOM   4120 C C   . SER D 4 64  ? 227.859 304.417 216.093 1.00 134.30 ? 64   SER H C   1 
ATOM   4121 O O   . SER D 4 64  ? 226.997 305.295 216.137 1.00 134.04 ? 64   SER H O   1 
ATOM   4122 C CB  . SER D 4 64  ? 230.058 305.578 216.069 1.00 133.43 ? 64   SER H CB  1 
ATOM   4123 N N   . LEU D 4 65  ? 227.704 303.292 215.400 1.00 134.78 ? 65   LEU H N   1 
ATOM   4124 C CA  . LEU D 4 65  ? 226.498 303.036 214.620 1.00 137.17 ? 65   LEU H CA  1 
ATOM   4125 C C   . LEU D 4 65  ? 225.755 301.790 215.087 1.00 127.75 ? 65   LEU H C   1 
ATOM   4126 O O   . LEU D 4 65  ? 224.612 301.564 214.693 1.00 133.00 ? 65   LEU H O   1 
ATOM   4127 C CB  . LEU D 4 65  ? 226.850 302.899 213.135 1.00 134.87 ? 65   LEU H CB  1 
ATOM   4128 N N   . LYS D 4 66  ? 226.405 300.983 215.922 1.00 136.14 ? 66   LYS H N   1 
ATOM   4129 C CA  . LYS D 4 66  ? 225.858 299.699 216.358 1.00 137.83 ? 66   LYS H CA  1 
ATOM   4130 C C   . LYS D 4 66  ? 224.407 299.789 216.812 1.00 137.51 ? 66   LYS H C   1 
ATOM   4131 O O   . LYS D 4 66  ? 223.607 298.900 216.527 1.00 139.53 ? 66   LYS H O   1 
ATOM   4132 C CB  . LYS D 4 66  ? 226.703 299.123 217.496 1.00 134.19 ? 66   LYS H CB  1 
ATOM   4133 N N   . SER D 4 67  ? 224.067 300.851 217.533 1.00 138.01 ? 67   SER H N   1 
ATOM   4134 C CA  . SER D 4 67  ? 222.735 300.979 218.114 1.00 139.38 ? 67   SER H CA  1 
ATOM   4135 C C   . SER D 4 67  ? 221.630 301.055 217.063 1.00 139.12 ? 67   SER H C   1 
ATOM   4136 O O   . SER D 4 67  ? 220.455 300.867 217.381 1.00 139.91 ? 67   SER H O   1 
ATOM   4137 C CB  . SER D 4 67  ? 222.674 302.207 219.003 1.00 137.53 ? 67   SER H CB  1 
ATOM   4138 N N   . ARG D 4 68  ? 221.998 301.354 215.819 1.00 138.06 ? 68   ARG H N   1 
ATOM   4139 C CA  . ARG D 4 68  ? 221.019 301.485 214.748 1.00 139.18 ? 68   ARG H CA  1 
ATOM   4140 C C   . ARG D 4 68  ? 221.249 300.479 213.621 1.00 147.18 ? 68   ARG H C   1 
ATOM   4141 O O   . ARG D 4 68  ? 220.666 300.605 212.546 1.00 135.54 ? 68   ARG H O   1 
ATOM   4142 C CB  . ARG D 4 68  ? 221.034 302.906 214.198 1.00 139.71 ? 68   ARG H CB  1 
ATOM   4143 N N   . LEU D 4 69  ? 222.103 299.481 213.860 1.00 138.13 ? 69   LEU H N   1 
ATOM   4144 C CA  . LEU D 4 69  ? 222.421 298.498 212.823 1.00 136.06 ? 69   LEU H CA  1 
ATOM   4145 C C   . LEU D 4 69  ? 222.078 297.067 213.229 1.00 134.82 ? 69   LEU H C   1 
ATOM   4146 O O   . LEU D 4 69  ? 222.417 296.619 214.324 1.00 133.95 ? 69   LEU H O   1 
ATOM   4147 C CB  . LEU D 4 69  ? 223.915 298.554 212.476 1.00 138.09 ? 69   LEU H CB  1 
ATOM   4148 N N   . THR D 4 70  ? 221.453 296.339 212.307 1.00 133.00 ? 70   THR H N   1 
ATOM   4149 C CA  . THR D 4 70  ? 221.191 294.912 212.477 1.00 134.77 ? 70   THR H CA  1 
ATOM   4150 C C   . THR D 4 70  ? 221.618 294.130 211.236 1.00 136.68 ? 70   THR H C   1 
ATOM   4151 O O   . THR D 4 70  ? 221.289 294.508 210.110 1.00 129.76 ? 70   THR H O   1 
ATOM   4152 C CB  . THR D 4 70  ? 219.699 294.647 212.768 1.00 135.20 ? 70   THR H CB  1 
ATOM   4153 N N   . VAL D 4 71  ? 222.341 293.029 211.437 1.00 131.38 ? 71   VAL H N   1 
ATOM   4154 C CA  . VAL D 4 71  ? 222.748 292.187 210.314 1.00 129.66 ? 71   VAL H CA  1 
ATOM   4155 C C   . VAL D 4 71  ? 222.305 290.739 210.493 1.00 131.93 ? 71   VAL H C   1 
ATOM   4156 O O   . VAL D 4 71  ? 222.562 290.120 211.526 1.00 129.70 ? 71   VAL H O   1 
ATOM   4157 C CB  . VAL D 4 71  ? 224.278 292.232 210.123 1.00 133.34 ? 71   VAL H CB  1 
ATOM   4158 N N   . THR D 4 72  ? 221.648 290.204 209.469 1.00 129.52 ? 72   THR H N   1 
ATOM   4159 C CA  . THR D 4 72  ? 221.224 288.808 209.453 1.00 129.34 ? 72   THR H CA  1 
ATOM   4160 C C   . THR D 4 72  ? 221.570 288.182 208.109 1.00 129.08 ? 72   THR H C   1 
ATOM   4161 O O   . THR D 4 72  ? 221.884 288.893 207.154 1.00 125.48 ? 72   THR H O   1 
ATOM   4162 C CB  . THR D 4 72  ? 219.711 288.675 209.716 1.00 129.76 ? 72   THR H CB  1 
ATOM   4163 N N   . LYS D 4 73  ? 221.490 286.858 208.017 1.00 125.93 ? 73   LYS H N   1 
ATOM   4164 C CA  . LYS D 4 73  ? 221.745 286.195 206.741 1.00 124.91 ? 73   LYS H CA  1 
ATOM   4165 C C   . LYS D 4 73  ? 220.714 285.118 206.428 1.00 123.66 ? 73   LYS H C   1 
ATOM   4166 O O   . LYS D 4 73  ? 220.231 284.418 207.318 1.00 124.55 ? 73   LYS H O   1 
ATOM   4167 C CB  . LYS D 4 73  ? 223.158 285.605 206.706 1.00 123.46 ? 73   LYS H CB  1 
ATOM   4168 N N   . ASP D 4 74  ? 220.399 284.992 205.142 1.00 125.20 ? 74   ASP H N   1 
ATOM   4169 C CA  . ASP D 4 74  ? 219.495 283.967 204.639 1.00 122.82 ? 74   ASP H CA  1 
ATOM   4170 C C   . ASP D 4 74  ? 220.291 282.759 204.165 1.00 124.66 ? 74   ASP H C   1 
ATOM   4171 O O   . ASP D 4 74  ? 221.052 282.838 203.198 1.00 124.03 ? 74   ASP H O   1 
ATOM   4172 C CB  . ASP D 4 74  ? 218.621 284.517 203.508 1.00 125.02 ? 74   ASP H CB  1 
ATOM   4173 N N   . THR D 4 75  ? 220.141 281.648 204.876 1.00 122.11 ? 75   THR H N   1 
ATOM   4174 C CA  . THR D 4 75  ? 220.949 280.459 204.644 1.00 122.47 ? 75   THR H CA  1 
ATOM   4175 C C   . THR D 4 75  ? 220.418 279.603 203.500 1.00 122.83 ? 75   THR H C   1 
ATOM   4176 O O   . THR D 4 75  ? 221.038 278.606 203.127 1.00 122.65 ? 75   THR H O   1 
ATOM   4177 C CB  . THR D 4 75  ? 221.028 279.608 205.921 1.00 122.76 ? 75   THR H CB  1 
ATOM   4178 N N   . SER D 4 76  ? 219.259 279.971 202.962 1.00 123.20 ? 76   SER H N   1 
ATOM   4179 C CA  . SER D 4 76  ? 218.663 279.212 201.869 1.00 124.10 ? 76   SER H CA  1 
ATOM   4180 C C   . SER D 4 76  ? 218.916 279.888 200.527 1.00 122.84 ? 76   SER H C   1 
ATOM   4181 O O   . SER D 4 76  ? 219.156 279.224 199.519 1.00 122.86 ? 76   SER H O   1 
ATOM   4182 C CB  . SER D 4 76  ? 217.169 279.063 202.086 1.00 123.57 ? 76   SER H CB  1 
ATOM   4183 N N   . LYS D 4 77  ? 218.863 281.216 200.522 1.00 122.99 ? 77   LYS H N   1 
ATOM   4184 C CA  . LYS D 4 77  ? 219.003 281.990 199.293 1.00 122.85 ? 77   LYS H CA  1 
ATOM   4185 C C   . LYS D 4 77  ? 220.433 282.450 199.042 1.00 126.64 ? 77   LYS H C   1 
ATOM   4186 O O   . LYS D 4 77  ? 220.724 283.027 197.994 1.00 122.94 ? 77   LYS H O   1 
ATOM   4187 C CB  . LYS D 4 77  ? 218.089 283.212 199.328 1.00 125.94 ? 77   LYS H CB  1 
ATOM   4188 N N   . ASN D 4 78  ? 221.320 282.224 200.008 1.00 117.27 ? 78   ASN H N   1 
ATOM   4189 C CA  . ASN D 4 78  ? 222.682 282.742 199.922 1.00 123.61 ? 78   ASN H CA  1 
ATOM   4190 C C   . ASN D 4 78  ? 222.668 284.261 199.772 1.00 127.63 ? 78   ASN H C   1 
ATOM   4191 O O   . ASN D 4 78  ? 223.184 284.813 198.798 1.00 124.11 ? 78   ASN H O   1 
ATOM   4192 C CB  . ASN D 4 78  ? 223.451 282.077 198.792 1.00 121.36 ? 78   ASN H CB  1 
ATOM   4193 N N   . GLN D 4 79  ? 222.006 284.923 200.718 1.00 123.42 ? 79   GLN H N   1 
ATOM   4194 C CA  . GLN D 4 79  ? 221.890 286.377 200.717 1.00 124.88 ? 79   GLN H CA  1 
ATOM   4195 C C   . GLN D 4 79  ? 222.140 286.939 202.112 1.00 126.92 ? 79   GLN H C   1 
ATOM   4196 O O   . GLN D 4 79  ? 221.812 286.301 203.111 1.00 126.49 ? 79   GLN H O   1 
ATOM   4197 C CB  . GLN D 4 79  ? 220.502 286.806 200.230 1.00 127.84 ? 79   GLN H CB  1 
ATOM   4198 N N   . VAL D 4 80  ? 222.690 288.145 202.177 1.00 128.47 ? 80   VAL H N   1 
ATOM   4199 C CA  . VAL D 4 80  ? 222.908 288.811 203.459 1.00 127.64 ? 80   VAL H CA  1 
ATOM   4200 C C   . VAL D 4 80  ? 222.129 290.116 203.529 1.00 133.42 ? 80   VAL H C   1 
ATOM   4201 O O   . VAL D 4 80  ? 222.092 290.884 202.568 1.00 124.67 ? 80   VAL H O   1 
ATOM   4202 C CB  . VAL D 4 80  ? 224.407 289.056 203.700 1.00 128.22 ? 80   VAL H CB  1 
ATOM   4203 N N   . VAL D 4 81  ? 221.460 290.342 204.654 1.00 130.06 ? 81   VAL H N   1 
ATOM   4204 C CA  . VAL D 4 81  ? 220.586 291.498 204.785 1.00 132.48 ? 81   VAL H CA  1 
ATOM   4205 C C   . VAL D 4 81  ? 221.034 292.477 205.867 1.00 139.60 ? 81   VAL H C   1 
ATOM   4206 O O   . VAL D 4 81  ? 221.239 292.106 207.024 1.00 130.99 ? 81   VAL H O   1 
ATOM   4207 C CB  . VAL D 4 81  ? 219.150 291.029 205.079 1.00 132.67 ? 81   VAL H CB  1 
ATOM   4208 N N   . LEU D 4 82  ? 221.158 293.740 205.474 1.00 133.96 ? 82   LEU H N   1 
ATOM   4209 C CA  . LEU D 4 82  ? 221.508 294.822 206.388 1.00 141.28 ? 82   LEU H CA  1 
ATOM   4210 C C   . LEU D 4 82  ? 220.317 295.728 206.657 1.00 143.03 ? 82   LEU H C   1 
ATOM   4211 O O   . LEU D 4 82  ? 219.689 296.234 205.726 1.00 119.00 ? 82   LEU H O   1 
ATOM   4212 C CB  . LEU D 4 82  ? 222.638 295.674 205.800 1.00 136.02 ? 82   LEU H CB  1 
ATOM   4213 N N   . THR D 4 83  ? 220.042 295.981 207.930 1.00 139.88 ? 83   THR H N   1 
ATOM   4214 C CA  . THR D 4 83  ? 218.994 296.922 208.299 1.00 139.03 ? 83   THR H CA  1 
ATOM   4215 C C   . THR D 4 83  ? 219.566 298.080 209.106 1.00 145.47 ? 83   THR H C   1 
ATOM   4216 O O   . THR D 4 83  ? 220.281 297.875 210.089 1.00 133.11 ? 83   THR H O   1 
ATOM   4217 C CB  . THR D 4 83  ? 217.875 296.232 209.105 1.00 135.25 ? 83   THR H CB  1 
ATOM   4218 N N   . MET D 4 84  ? 219.241 299.302 208.696 1.00 142.63 ? 84   MET H N   1 
ATOM   4219 C CA  . MET D 4 84  ? 219.678 300.487 209.424 1.00 143.23 ? 84   MET H CA  1 
ATOM   4220 C C   . MET D 4 84  ? 218.472 301.342 209.797 1.00 136.68 ? 84   MET H C   1 
ATOM   4221 O O   . MET D 4 84  ? 217.621 301.631 208.955 1.00 128.74 ? 84   MET H O   1 
ATOM   4222 C CB  . MET D 4 84  ? 220.694 301.273 208.597 1.00 139.37 ? 84   MET H CB  1 
ATOM   4223 N N   . THR D 4 85  ? 218.384 301.719 211.070 1.00 140.78 ? 85   THR H N   1 
ATOM   4224 C CA  . THR D 4 85  ? 217.201 302.416 211.566 1.00 146.36 ? 85   THR H CA  1 
ATOM   4225 C C   . THR D 4 85  ? 217.427 303.907 211.769 1.00 136.98 ? 85   THR H C   1 
ATOM   4226 O O   . THR D 4 85  ? 218.564 304.368 211.891 1.00 139.86 ? 85   THR H O   1 
ATOM   4227 C CB  . THR D 4 85  ? 216.736 301.804 212.900 1.00 143.61 ? 85   THR H CB  1 
ATOM   4228 N N   . ASN D 4 86  ? 216.322 304.649 211.841 1.00 142.36 ? 86   ASN H N   1 
ATOM   4229 C CA  . ASN D 4 86  ? 216.340 306.069 212.168 1.00 144.81 ? 86   ASN H CA  1 
ATOM   4230 C C   . ASN D 4 86  ? 217.389 306.839 211.377 1.00 142.16 ? 86   ASN H C   1 
ATOM   4231 O O   . ASN D 4 86  ? 218.192 307.568 211.959 1.00 140.52 ? 86   ASN H O   1 
ATOM   4232 C CB  . ASN D 4 86  ? 216.538 306.270 213.658 1.00 143.92 ? 86   ASN H CB  1 
ATOM   4233 N N   . MET D 4 87  ? 217.406 306.663 210.059 1.00 142.66 ? 87   MET H N   1 
ATOM   4234 C CA  . MET D 4 87  ? 218.442 307.298 209.251 1.00 146.90 ? 87   MET H CA  1 
ATOM   4235 C C   . MET D 4 87  ? 218.267 308.808 209.165 1.00 141.00 ? 87   MET H C   1 
ATOM   4236 O O   . MET D 4 87  ? 217.157 309.314 208.994 1.00 145.37 ? 87   MET H O   1 
ATOM   4237 C CB  . MET D 4 87  ? 218.476 306.694 207.851 1.00 146.28 ? 87   MET H CB  1 
ATOM   4238 N N   . ASP D 4 88  ? 219.386 309.516 209.248 1.00 144.37 ? 88   ASP H N   1 
ATOM   4239 C CA  . ASP D 4 88  ? 219.428 310.966 209.103 1.00 146.34 ? 88   ASP H CA  1 
ATOM   4240 C C   . ASP D 4 88  ? 219.915 311.329 207.703 1.00 149.46 ? 88   ASP H C   1 
ATOM   4241 O O   . ASP D 4 88  ? 220.560 310.513 207.051 1.00 138.56 ? 88   ASP H O   1 
ATOM   4242 C CB  . ASP D 4 88  ? 220.359 311.576 210.158 1.00 149.38 ? 88   ASP H CB  1 
ATOM   4243 N N   . PRO D 4 89  ? 219.644 312.544 207.222 1.00 145.13 ? 89   PRO H N   1 
ATOM   4244 C CA  . PRO D 4 89  ? 220.123 313.091 205.961 1.00 145.59 ? 89   PRO H CA  1 
ATOM   4245 C C   . PRO D 4 89  ? 221.631 312.896 205.783 1.00 146.31 ? 89   PRO H C   1 
ATOM   4246 O O   . PRO D 4 89  ? 222.113 312.704 204.665 1.00 143.80 ? 89   PRO H O   1 
ATOM   4247 C CB  . PRO D 4 89  ? 219.752 314.572 206.103 1.00 142.42 ? 89   PRO H CB  1 
ATOM   4248 C CG  . PRO D 4 89  ? 218.510 314.560 206.974 1.00 141.94 ? 89   PRO H CG  1 
ATOM   4249 C CD  . PRO D 4 89  ? 218.741 313.436 207.968 1.00 145.46 ? 89   PRO H CD  1 
ATOM   4250 N N   . VAL D 4 90  ? 222.368 312.908 206.891 1.00 147.06 ? 90   VAL H N   1 
ATOM   4251 C CA  . VAL D 4 90  ? 223.820 312.753 206.855 1.00 145.63 ? 90   VAL H CA  1 
ATOM   4252 C C   . VAL D 4 90  ? 224.244 311.317 206.556 1.00 146.23 ? 90   VAL H C   1 
ATOM   4253 O O   . VAL D 4 90  ? 225.427 311.043 206.354 1.00 141.69 ? 90   VAL H O   1 
ATOM   4254 C CB  . VAL D 4 90  ? 224.443 313.203 208.191 1.00 151.30 ? 90   VAL H CB  1 
ATOM   4255 N N   . ASP D 4 91  ? 223.281 310.401 206.540 1.00 136.53 ? 91   ASP H N   1 
ATOM   4256 C CA  . ASP D 4 91  ? 223.560 308.993 206.290 1.00 142.24 ? 91   ASP H CA  1 
ATOM   4257 C C   . ASP D 4 91  ? 223.481 308.667 204.802 1.00 145.67 ? 91   ASP H C   1 
ATOM   4258 O O   . ASP D 4 91  ? 223.594 307.505 204.410 1.00 140.87 ? 91   ASP H O   1 
ATOM   4259 C CB  . ASP D 4 91  ? 222.591 308.091 207.069 1.00 141.14 ? 91   ASP H CB  1 
ATOM   4260 N N   . THR D 4 92  ? 223.307 309.693 203.972 1.00 143.75 ? 92   THR H N   1 
ATOM   4261 C CA  . THR D 4 92  ? 223.318 309.494 202.527 1.00 141.81 ? 92   THR H CA  1 
ATOM   4262 C C   . THR D 4 92  ? 224.683 308.980 202.092 1.00 140.57 ? 92   THR H C   1 
ATOM   4263 O O   . THR D 4 92  ? 225.710 309.597 202.380 1.00 139.64 ? 92   THR H O   1 
ATOM   4264 C CB  . THR D 4 92  ? 222.976 310.806 201.790 1.00 142.11 ? 92   THR H CB  1 
ATOM   4265 N N   . ALA D 4 93  ? 224.692 307.831 201.425 1.00 141.64 ? 93   ALA H N   1 
ATOM   4266 C CA  . ALA D 4 93  ? 225.944 307.175 201.071 1.00 137.99 ? 93   ALA H CA  1 
ATOM   4267 C C   . ALA D 4 93  ? 225.733 306.041 200.086 1.00 135.74 ? 93   ALA H C   1 
ATOM   4268 O O   . ALA D 4 93  ? 224.624 305.524 199.948 1.00 143.35 ? 93   ALA H O   1 
ATOM   4269 C CB  . ALA D 4 93  ? 226.618 306.642 202.327 1.00 136.43 ? 93   ALA H CB  1 
ATOM   4270 N N   . THR D 4 94  ? 226.818 305.607 199.453 1.00 139.55 ? 94   THR H N   1 
ATOM   4271 C CA  . THR D 4 94  ? 226.784 304.383 198.668 1.00 131.60 ? 94   THR H CA  1 
ATOM   4272 C C   . THR D 4 94  ? 227.103 303.199 199.567 1.00 175.47 ? 94   THR H C   1 
ATOM   4273 O O   . THR D 4 94  ? 228.099 303.210 200.290 1.00 128.17 ? 94   THR H O   1 
ATOM   4274 C CB  . THR D 4 94  ? 227.787 304.421 197.500 1.00 140.21 ? 94   THR H CB  1 
ATOM   4275 N N   . TYR D 4 95  ? 226.248 302.189 199.541 1.00 132.42 ? 95   TYR H N   1 
ATOM   4276 C CA  . TYR D 4 95  ? 226.438 301.014 200.376 1.00 131.39 ? 95   TYR H CA  1 
ATOM   4277 C C   . TYR D 4 95  ? 227.054 299.872 199.594 1.00 133.61 ? 95   TYR H C   1 
ATOM   4278 O O   . TYR D 4 95  ? 226.627 299.562 198.482 1.00 126.91 ? 95   TYR H O   1 
ATOM   4279 C CB  . TYR D 4 95  ? 225.110 300.592 200.999 1.00 141.01 ? 95   TYR H CB  1 
ATOM   4280 N N   . TYR D 4 96  ? 228.061 299.244 200.187 1.00 130.80 ? 96   TYR H N   1 
ATOM   4281 C CA  . TYR D 4 96  ? 228.750 298.121 199.576 1.00 134.81 ? 96   TYR H CA  1 
ATOM   4282 C C   . TYR D 4 96  ? 228.721 296.904 200.493 1.00 139.49 ? 96   TYR H C   1 
ATOM   4283 O O   . TYR D 4 96  ? 228.836 297.038 201.715 1.00 131.99 ? 96   TYR H O   1 
ATOM   4284 C CB  . TYR D 4 96  ? 230.219 298.471 199.309 1.00 134.86 ? 96   TYR H CB  1 
ATOM   4285 N N   . CYS D 4 97  ? 228.667 295.716 199.893 1.00 132.15 ? 97   CYS H N   1 
ATOM   4286 C CA  . CYS D 4 97  ? 228.893 294.459 200.600 1.00 129.42 ? 97   CYS H CA  1 
ATOM   4287 C C   . CYS D 4 97  ? 230.170 293.811 200.073 1.00 131.43 ? 97   CYS H C   1 
ATOM   4288 O O   . CYS D 4 97  ? 230.523 293.967 198.899 1.00 125.98 ? 97   CYS H O   1 
ATOM   4289 C CB  . CYS D 4 97  ? 227.692 293.508 200.450 1.00 133.20 ? 97   CYS H CB  1 
ATOM   4290 S SG  . CYS D 4 97  ? 227.310 292.979 198.744 1.00 131.39 ? 97   CYS H SG  1 
ATOM   4291 N N   . ALA D 4 98  ? 230.864 293.082 200.941 1.00 127.06 ? 98   ALA H N   1 
ATOM   4292 C CA  . ALA D 4 98  ? 232.081 292.398 200.526 1.00 123.99 ? 98   ALA H CA  1 
ATOM   4293 C C   . ALA D 4 98  ? 232.357 291.166 201.378 1.00 122.16 ? 98   ALA H C   1 
ATOM   4294 O O   . ALA D 4 98  ? 231.961 291.095 202.540 1.00 119.39 ? 98   ALA H O   1 
ATOM   4295 C CB  . ALA D 4 98  ? 233.267 293.352 200.597 1.00 124.47 ? 98   ALA H CB  1 
ATOM   4296 N N   . HIS D 4 99  ? 233.076 290.211 200.799 1.00 120.13 ? 99   HIS H N   1 
ATOM   4297 C CA  . HIS D 4 99  ? 233.516 289.023 201.522 1.00 117.16 ? 99   HIS H CA  1 
ATOM   4298 C C   . HIS D 4 99  ? 234.588 289.380 202.543 1.00 117.23 ? 99   HIS H C   1 
ATOM   4299 O O   . HIS D 4 99  ? 235.484 290.178 202.268 1.00 121.44 ? 99   HIS H O   1 
ATOM   4300 C CB  . HIS D 4 99  ? 234.047 287.962 200.554 1.00 118.06 ? 99   HIS H CB  1 
ATOM   4301 N N   . VAL D 4 100 ? 234.487 288.786 203.726 1.00 111.82 ? 100  VAL H N   1 
ATOM   4302 C CA  . VAL D 4 100 ? 235.409 289.068 204.816 1.00 112.13 ? 100  VAL H CA  1 
ATOM   4303 C C   . VAL D 4 100 ? 236.295 287.874 205.142 1.00 108.68 ? 100  VAL H C   1 
ATOM   4304 O O   . VAL D 4 100 ? 235.807 286.811 205.528 1.00 108.46 ? 100  VAL H O   1 
ATOM   4305 C CB  . VAL D 4 100 ? 234.616 289.459 206.081 1.00 112.79 ? 100  VAL H CB  1 
ATOM   4306 N N   . LEU D 4 101 ? 237.603 288.076 205.038 1.00 107.71 ? 101  LEU H N   1 
ATOM   4307 C CA  . LEU D 4 101 ? 238.569 287.061 205.429 1.00 104.88 ? 101  LEU H CA  1 
ATOM   4308 C C   . LEU D 4 101 ? 238.744 287.102 206.940 1.00 101.65 ? 101  LEU H C   1 
ATOM   4309 O O   . LEU D 4 101 ? 238.783 288.182 207.533 1.00 102.12 ? 101  LEU H O   1 
ATOM   4310 C CB  . LEU D 4 101 ? 239.913 287.314 204.732 1.00 106.95 ? 101  LEU H CB  1 
ATOM   4311 N N   . VAL D 4 102 ? 238.827 285.930 207.563 1.00 95.09  ? 102  VAL H N   1 
ATOM   4312 C CA  . VAL D 4 102 ? 238.931 285.851 209.016 1.00 92.30  ? 102  VAL H CA  1 
ATOM   4313 C C   . VAL D 4 102 ? 240.003 284.856 209.454 1.00 85.52  ? 102  VAL H C   1 
ATOM   4314 O O   . VAL D 4 102 ? 240.200 283.824 208.813 1.00 80.88  ? 102  VAL H O   1 
ATOM   4315 C CB  . VAL D 4 102 ? 237.560 285.444 209.607 1.00 93.52  ? 102  VAL H CB  1 
ATOM   4316 N N   . TRP D 4 103 ? 240.661 285.158 210.568 1.00 85.39  ? 103  TRP H N   1 
ATOM   4317 C CA  . TRP D 4 103 ? 241.624 284.256 211.193 1.00 76.30  ? 103  TRP H CA  1 
ATOM   4318 C C   . TRP D 4 103 ? 240.873 283.180 211.971 1.00 77.36  ? 103  TRP H C   1 
ATOM   4319 O O   . TRP D 4 103 ? 239.736 283.398 212.389 1.00 77.75  ? 103  TRP H O   1 
ATOM   4320 C CB  . TRP D 4 103 ? 242.553 285.039 212.124 1.00 81.05  ? 103  TRP H CB  1 
ATOM   4321 C CG  . TRP D 4 103 ? 243.480 285.993 211.401 1.00 80.30  ? 103  TRP H CG  1 
ATOM   4322 C CD1 . TRP D 4 103 ? 243.200 287.273 211.031 1.00 87.22  ? 103  TRP H CD1 1 
ATOM   4323 C CD2 . TRP D 4 103 ? 244.845 285.747 210.979 1.00 77.62  ? 103  TRP H CD2 1 
ATOM   4324 N NE1 . TRP D 4 103 ? 244.284 287.830 210.401 1.00 85.83  ? 103  TRP H NE1 1 
ATOM   4325 C CE2 . TRP D 4 103 ? 245.294 286.911 210.356 1.00 83.61  ? 103  TRP H CE2 1 
ATOM   4326 C CE3 . TRP D 4 103 ? 245.703 284.654 211.079 1.00 79.60  ? 103  TRP H CE3 1 
ATOM   4327 C CZ2 . TRP D 4 103 ? 246.566 287.012 209.825 1.00 82.86  ? 103  TRP H CZ2 1 
ATOM   4328 C CZ3 . TRP D 4 103 ? 246.981 284.755 210.548 1.00 74.16  ? 103  TRP H CZ3 1 
ATOM   4329 C CH2 . TRP D 4 103 ? 247.399 285.905 209.935 1.00 76.55  ? 103  TRP H CH2 1 
ATOM   4330 N N   . PHE D 4 104 ? 241.470 281.999 212.115 1.00 71.83  ? 104  PHE H N   1 
ATOM   4331 C CA  . PHE D 4 104 ? 240.758 280.888 212.744 1.00 67.91  ? 104  PHE H CA  1 
ATOM   4332 C C   . PHE D 4 104 ? 241.150 280.645 214.194 1.00 67.78  ? 104  PHE H C   1 
ATOM   4333 O O   . PHE D 4 104 ? 240.309 280.250 215.000 1.00 69.76  ? 104  PHE H O   1 
ATOM   4334 C CB  . PHE D 4 104 ? 240.963 279.611 211.938 1.00 63.64  ? 104  PHE H CB  1 
ATOM   4335 C CG  . PHE D 4 104 ? 240.300 279.652 210.602 1.00 63.69  ? 104  PHE H CG  1 
ATOM   4336 C CD1 . PHE D 4 104 ? 238.925 279.504 210.491 1.00 61.96  ? 104  PHE H CD1 1 
ATOM   4337 C CD2 . PHE D 4 104 ? 241.041 279.840 209.451 1.00 63.16  ? 104  PHE H CD2 1 
ATOM   4338 C CE1 . PHE D 4 104 ? 238.309 279.540 209.258 1.00 67.34  ? 104  PHE H CE1 1 
ATOM   4339 C CE2 . PHE D 4 104 ? 240.429 279.880 208.217 1.00 65.61  ? 104  PHE H CE2 1 
ATOM   4340 C CZ  . PHE D 4 104 ? 239.061 279.728 208.121 1.00 67.62  ? 104  PHE H CZ  1 
ATOM   4341 N N   . GLY D 4 105 ? 242.416 280.869 214.533 1.00 69.08  ? 105  GLY H N   1 
ATOM   4342 C CA  . GLY D 4 105 ? 242.858 280.652 215.909 1.00 68.94  ? 105  GLY H CA  1 
ATOM   4343 C C   . GLY D 4 105 ? 242.040 281.516 216.859 1.00 73.34  ? 105  GLY H C   1 
ATOM   4344 O O   . GLY D 4 105 ? 241.123 281.037 217.526 1.00 75.10  ? 105  GLY H O   1 
ATOM   4345 N N   . GLU D 4 106 ? 242.332 282.808 216.855 1.00 75.46  ? 106  GLU H N   1 
ATOM   4346 C CA  . GLU D 4 106 ? 241.467 283.798 217.472 1.00 78.66  ? 106  GLU H CA  1 
ATOM   4347 C C   . GLU D 4 106 ? 240.649 284.425 216.361 1.00 79.97  ? 106  GLU H C   1 
ATOM   4348 O O   . GLU D 4 106 ? 241.189 284.730 215.296 1.00 83.10  ? 106  GLU H O   1 
ATOM   4349 C CB  . GLU D 4 106 ? 242.276 284.863 218.213 1.00 80.58  ? 106  GLU H CB  1 
ATOM   4350 N N   . VAL D 4 107 ? 239.352 284.592 216.582 1.00 81.99  ? 107  VAL H N   1 
ATOM   4351 C CA  . VAL D 4 107 ? 238.494 285.061 215.505 1.00 85.14  ? 107  VAL H CA  1 
ATOM   4352 C C   . VAL D 4 107 ? 238.663 286.555 215.282 1.00 87.35  ? 107  VAL H C   1 
ATOM   4353 O O   . VAL D 4 107 ? 237.836 287.365 215.701 1.00 91.53  ? 107  VAL H O   1 
ATOM   4354 C CB  . VAL D 4 107 ? 237.019 284.732 215.804 1.00 86.71  ? 107  VAL H CB  1 
ATOM   4355 N N   . LEU D 4 108 ? 239.736 286.901 214.588 1.00 86.66  ? 108  LEU H N   1 
ATOM   4356 C CA  . LEU D 4 108 ? 240.023 288.276 214.226 1.00 91.75  ? 108  LEU H CA  1 
ATOM   4357 C C   . LEU D 4 108 ? 239.752 288.465 212.739 1.00 92.59  ? 108  LEU H C   1 
ATOM   4358 O O   . LEU D 4 108 ? 239.997 287.553 211.952 1.00 91.10  ? 108  LEU H O   1 
ATOM   4359 C CB  . LEU D 4 108 ? 241.496 288.596 214.520 1.00 87.40  ? 108  LEU H CB  1 
ATOM   4360 C CG  . LEU D 4 108 ? 241.972 288.340 215.955 1.00 85.26  ? 108  LEU H CG  1 
ATOM   4361 C CD1 . LEU D 4 108 ? 243.476 288.564 216.026 1.00 82.41  ? 108  LEU H CD1 1 
ATOM   4362 C CD2 . LEU D 4 108 ? 241.240 289.267 216.915 1.00 85.87  ? 108  LEU H CD2 1 
ATOM   4363 N N   . PRO D 4 109 ? 239.250 289.627 212.334 1.00 96.69  ? 109  PRO H N   1 
ATOM   4364 C CA  . PRO D 4 109 ? 239.012 290.026 210.961 1.00 102.29 ? 109  PRO H CA  1 
ATOM   4365 C C   . PRO D 4 109 ? 240.329 290.308 210.251 1.00 103.57 ? 109  PRO H C   1 
ATOM   4366 O O   . PRO D 4 109 ? 241.327 290.637 210.894 1.00 103.96 ? 109  PRO H O   1 
ATOM   4367 C CB  . PRO D 4 109 ? 238.162 291.283 211.135 1.00 107.53 ? 109  PRO H CB  1 
ATOM   4368 C CG  . PRO D 4 109 ? 238.577 291.838 212.485 1.00 109.02 ? 109  PRO H CG  1 
ATOM   4369 C CD  . PRO D 4 109 ? 238.884 290.627 213.334 1.00 101.84 ? 109  PRO H CD  1 
ATOM   4370 N N   . ASP D 4 110 ? 240.324 290.196 208.927 1.00 104.87 ? 110  ASP H N   1 
ATOM   4371 C CA  . ASP D 4 110 ? 241.516 290.472 208.134 1.00 106.69 ? 110  ASP H CA  1 
ATOM   4372 C C   . ASP D 4 110 ? 241.272 291.538 207.064 1.00 110.93 ? 110  ASP H C   1 
ATOM   4373 O O   . ASP D 4 110 ? 241.605 292.707 207.257 1.00 113.46 ? 110  ASP H O   1 
ATOM   4374 C CB  . ASP D 4 110 ? 242.037 289.178 207.497 1.00 103.01 ? 110  ASP H CB  1 
ATOM   4375 N N   . ALA D 4 111 ? 240.711 291.138 205.927 1.00 110.85 ? 111  ALA H N   1 
ATOM   4376 C CA  . ALA D 4 111 ? 240.553 292.064 204.810 1.00 114.50 ? 111  ALA H CA  1 
ATOM   4377 C C   . ALA D 4 111 ? 239.307 291.763 203.990 1.00 115.73 ? 111  ALA H C   1 
ATOM   4378 O O   . ALA D 4 111 ? 238.775 290.653 204.023 1.00 118.48 ? 111  ALA H O   1 
ATOM   4379 C CB  . ALA D 4 111 ? 241.781 292.016 203.911 1.00 115.27 ? 111  ALA H CB  1 
ATOM   4380 N N   . PHE D 4 112 ? 238.855 292.766 203.247 1.00 121.22 ? 112  PHE H N   1 
ATOM   4381 C CA  . PHE D 4 112 ? 237.702 292.629 202.363 1.00 122.41 ? 112  PHE H CA  1 
ATOM   4382 C C   . PHE D 4 112 ? 238.192 292.445 200.931 1.00 119.79 ? 112  PHE H C   1 
ATOM   4383 O O   . PHE D 4 112 ? 238.780 293.363 200.362 1.00 126.50 ? 112  PHE H O   1 
ATOM   4384 C CB  . PHE D 4 112 ? 236.831 293.888 202.429 1.00 123.67 ? 112  PHE H CB  1 
ATOM   4385 N N   . ASP D 4 113 ? 238.013 291.251 200.369 1.00 121.45 ? 113  ASP H N   1 
ATOM   4386 C CA  . ASP D 4 113 ? 238.588 290.958 199.056 1.00 121.76 ? 113  ASP H CA  1 
ATOM   4387 C C   . ASP D 4 113 ? 237.578 291.029 197.911 1.00 122.99 ? 113  ASP H C   1 
ATOM   4388 O O   . ASP D 4 113 ? 237.805 291.729 196.922 1.00 124.51 ? 113  ASP H O   1 
ATOM   4389 C CB  . ASP D 4 113 ? 239.308 289.601 199.064 1.00 121.92 ? 113  ASP H CB  1 
ATOM   4390 N N   . VAL D 4 114 ? 236.472 290.307 198.031 1.00 122.17 ? 114  VAL H N   1 
ATOM   4391 C CA  . VAL D 4 114 ? 235.467 290.289 196.972 1.00 123.72 ? 114  VAL H CA  1 
ATOM   4392 C C   . VAL D 4 114 ? 234.366 291.303 197.244 1.00 128.44 ? 114  VAL H C   1 
ATOM   4393 O O   . VAL D 4 114 ? 233.630 291.186 198.221 1.00 120.91 ? 114  VAL H O   1 
ATOM   4394 C CB  . VAL D 4 114 ? 234.851 288.884 196.834 1.00 123.06 ? 114  VAL H CB  1 
ATOM   4395 N N   . TRP D 4 115 ? 234.259 292.301 196.374 1.00 125.76 ? 115  TRP H N   1 
ATOM   4396 C CA  . TRP D 4 115 ? 233.313 293.398 196.555 1.00 127.16 ? 115  TRP H CA  1 
ATOM   4397 C C   . TRP D 4 115 ? 232.168 293.354 195.553 1.00 127.32 ? 115  TRP H C   1 
ATOM   4398 O O   . TRP D 4 115 ? 232.314 292.834 194.446 1.00 128.44 ? 115  TRP H O   1 
ATOM   4399 C CB  . TRP D 4 115 ? 234.030 294.742 196.427 1.00 128.24 ? 115  TRP H CB  1 
ATOM   4400 N N   . GLY D 4 116 ? 231.042 293.950 195.937 1.00 129.38 ? 116  GLY H N   1 
ATOM   4401 C CA  . GLY D 4 116 ? 229.903 294.126 195.043 1.00 130.79 ? 116  GLY H CA  1 
ATOM   4402 C C   . GLY D 4 116 ? 230.089 295.369 194.174 1.00 129.08 ? 116  GLY H C   1 
ATOM   4403 O O   . GLY D 4 116 ? 231.214 295.737 193.836 1.00 131.37 ? 116  GLY H O   1 
ATOM   4404 N N   . GLN D 4 117 ? 228.983 295.989 193.768 1.00 132.40 ? 117  GLN H N   1 
ATOM   4405 C CA  . GLN D 4 117 ? 229.054 297.127 192.855 1.00 133.17 ? 117  GLN H CA  1 
ATOM   4406 C C   . GLN D 4 117 ? 228.767 298.450 193.554 1.00 131.77 ? 117  GLN H C   1 
ATOM   4407 O O   . GLN D 4 117 ? 229.286 299.494 193.155 1.00 134.56 ? 117  GLN H O   1 
ATOM   4408 C CB  . GLN D 4 117 ? 228.086 296.928 191.688 1.00 133.77 ? 117  GLN H CB  1 
ATOM   4409 N N   . GLY D 4 118 ? 227.930 298.401 194.584 1.00 136.52 ? 118  GLY H N   1 
ATOM   4410 C CA  . GLY D 4 118 ? 227.560 299.593 195.338 1.00 134.26 ? 118  GLY H CA  1 
ATOM   4411 C C   . GLY D 4 118 ? 226.173 300.106 194.965 1.00 137.59 ? 118  GLY H C   1 
ATOM   4412 O O   . GLY D 4 118 ? 225.857 300.278 193.787 1.00 137.48 ? 118  GLY H O   1 
ATOM   4413 N N   . THR D 4 119 ? 225.356 300.377 195.979 1.00 136.30 ? 119  THR H N   1 
ATOM   4414 C CA  . THR D 4 119 ? 224.014 300.914 195.764 1.00 139.78 ? 119  THR H CA  1 
ATOM   4415 C C   . THR D 4 119 ? 223.878 302.277 196.433 1.00 138.64 ? 119  THR H C   1 
ATOM   4416 O O   . THR D 4 119 ? 224.237 302.446 197.597 1.00 126.17 ? 119  THR H O   1 
ATOM   4417 C CB  . THR D 4 119 ? 222.926 299.947 196.280 1.00 137.99 ? 119  THR H CB  1 
ATOM   4418 N N   . MET D 4 120 ? 223.395 303.265 195.687 1.00 143.25 ? 120  MET H N   1 
ATOM   4419 C CA  . MET D 4 120 ? 223.316 304.619 196.225 1.00 143.07 ? 120  MET H CA  1 
ATOM   4420 C C   . MET D 4 120 ? 222.027 304.852 196.994 1.00 140.21 ? 120  MET H C   1 
ATOM   4421 O O   . MET D 4 120 ? 220.932 304.679 196.460 1.00 144.88 ? 120  MET H O   1 
ATOM   4422 C CB  . MET D 4 120 ? 223.447 305.648 195.105 1.00 139.64 ? 120  MET H CB  1 
ATOM   4423 N N   . VAL D 4 121 ? 222.169 305.281 198.245 1.00 142.06 ? 121  VAL H N   1 
ATOM   4424 C CA  . VAL D 4 121 ? 221.029 305.552 199.108 1.00 139.14 ? 121  VAL H CA  1 
ATOM   4425 C C   . VAL D 4 121 ? 220.918 307.019 199.490 1.00 150.79 ? 121  VAL H C   1 
ATOM   4426 O O   . VAL D 4 121 ? 221.811 307.576 200.130 1.00 137.08 ? 121  VAL H O   1 
ATOM   4427 C CB  . VAL D 4 121 ? 221.147 304.727 200.397 1.00 143.98 ? 121  VAL H CB  1 
ATOM   4428 N N   . THR D 4 122 ? 219.781 307.619 199.156 1.00 143.75 ? 122  THR H N   1 
ATOM   4429 C CA  . THR D 4 122 ? 219.493 308.998 199.531 1.00 142.30 ? 122  THR H CA  1 
ATOM   4430 C C   . THR D 4 122 ? 218.411 309.029 200.606 1.00 146.23 ? 122  THR H C   1 
ATOM   4431 O O   . THR D 4 122 ? 217.363 308.401 200.445 1.00 140.25 ? 122  THR H O   1 
ATOM   4432 C CB  . THR D 4 122 ? 219.042 309.822 198.307 1.00 143.79 ? 122  THR H CB  1 
ATOM   4433 N N   . VAL D 4 123 ? 218.672 309.747 201.705 1.00 142.43 ? 123  VAL H N   1 
ATOM   4434 C CA  . VAL D 4 123 ? 217.722 309.855 202.816 1.00 144.78 ? 123  VAL H CA  1 
ATOM   4435 C C   . VAL D 4 123 ? 216.889 311.128 202.669 1.00 144.45 ? 123  VAL H C   1 
ATOM   4436 O O   . VAL D 4 123 ? 217.390 312.173 202.249 1.00 142.37 ? 123  VAL H O   1 
ATOM   4437 C CB  . VAL D 4 123 ? 218.464 309.835 204.193 1.00 144.26 ? 123  VAL H CB  1 
ATOM   4438 N N   . SER E 5 1   ? 236.518 304.194 215.503 1.00 124.34 ? 1    SER L N   1 
ATOM   4439 C CA  . SER E 5 1   ? 237.272 303.528 214.451 1.00 126.24 ? 1    SER L CA  1 
ATOM   4440 C C   . SER E 5 1   ? 238.776 303.696 214.684 1.00 126.18 ? 1    SER L C   1 
ATOM   4441 O O   . SER E 5 1   ? 239.195 304.524 215.501 1.00 127.62 ? 1    SER L O   1 
ATOM   4442 C CB  . SER E 5 1   ? 236.866 304.077 213.089 1.00 126.01 ? 1    SER L CB  1 
ATOM   4443 N N   . TYR E 5 2   ? 239.585 302.903 213.966 1.00 128.07 ? 2    TYR L N   1 
ATOM   4444 C CA  . TYR E 5 2   ? 241.046 302.969 214.069 1.00 129.37 ? 2    TYR L CA  1 
ATOM   4445 C C   . TYR E 5 2   ? 241.608 304.108 213.225 1.00 127.48 ? 2    TYR L C   1 
ATOM   4446 O O   . TYR E 5 2   ? 241.288 304.235 212.041 1.00 132.04 ? 2    TYR L O   1 
ATOM   4447 C CB  . TYR E 5 2   ? 241.682 301.637 213.666 1.00 127.77 ? 2    TYR L CB  1 
ATOM   4448 N N   . GLU E 5 3   ? 242.434 304.947 213.845 1.00 130.64 ? 3    GLU L N   1 
ATOM   4449 C CA  . GLU E 5 3   ? 242.995 306.115 213.175 1.00 130.52 ? 3    GLU L CA  1 
ATOM   4450 C C   . GLU E 5 3   ? 244.031 305.743 212.120 1.00 133.70 ? 3    GLU L C   1 
ATOM   4451 O O   . GLU E 5 3   ? 245.002 305.043 212.411 1.00 131.69 ? 3    GLU L O   1 
ATOM   4452 C CB  . GLU E 5 3   ? 243.635 307.048 214.208 1.00 128.32 ? 3    GLU L CB  1 
ATOM   4453 N N   . LEU E 5 4   ? 243.841 306.267 210.913 1.00 133.31 ? 4    LEU L N   1 
ATOM   4454 C CA  . LEU E 5 4   ? 244.771 306.085 209.803 1.00 127.29 ? 4    LEU L CA  1 
ATOM   4455 C C   . LEU E 5 4   ? 244.945 307.392 209.034 1.00 129.27 ? 4    LEU L C   1 
ATOM   4456 O O   . LEU E 5 4   ? 243.966 308.027 208.639 1.00 131.79 ? 4    LEU L O   1 
ATOM   4457 C CB  . LEU E 5 4   ? 244.266 304.992 208.857 1.00 131.22 ? 4    LEU L CB  1 
ATOM   4458 N N   . THR E 5 5   ? 246.195 307.799 208.833 1.00 129.31 ? 5    THR L N   1 
ATOM   4459 C CA  . THR E 5 5   ? 246.489 309.071 208.181 1.00 130.57 ? 5    THR L CA  1 
ATOM   4460 C C   . THR E 5 5   ? 247.174 308.890 206.833 1.00 135.75 ? 5    THR L C   1 
ATOM   4461 O O   . THR E 5 5   ? 248.169 308.173 206.719 1.00 125.11 ? 5    THR L O   1 
ATOM   4462 C CB  . THR E 5 5   ? 247.370 309.955 209.085 1.00 128.31 ? 5    THR L CB  1 
ATOM   4463 N N   . GLN E 5 6   ? 246.649 309.569 205.817 1.00 131.68 ? 6    GLN L N   1 
ATOM   4464 C CA  . GLN E 5 6   ? 247.231 309.531 204.479 1.00 134.63 ? 6    GLN L CA  1 
ATOM   4465 C C   . GLN E 5 6   ? 247.431 310.951 203.940 1.00 132.98 ? 6    GLN L C   1 
ATOM   4466 O O   . GLN E 5 6   ? 246.662 311.848 204.284 1.00 132.70 ? 6    GLN L O   1 
ATOM   4467 C CB  . GLN E 5 6   ? 246.323 308.751 203.520 1.00 135.00 ? 6    GLN L CB  1 
ATOM   4468 N N   . PRO E 5 7   ? 248.459 311.174 203.109 1.00 136.68 ? 7    PRO L N   1 
ATOM   4469 C CA  . PRO E 5 7   ? 248.641 312.336 202.257 1.00 135.28 ? 7    PRO L CA  1 
ATOM   4470 C C   . PRO E 5 7   ? 247.459 312.447 201.304 1.00 135.86 ? 7    PRO L C   1 
ATOM   4471 O O   . PRO E 5 7   ? 246.926 311.427 200.873 1.00 134.53 ? 7    PRO L O   1 
ATOM   4472 C CB  . PRO E 5 7   ? 249.944 312.008 201.512 1.00 137.15 ? 7    PRO L CB  1 
ATOM   4473 C CG  . PRO E 5 7   ? 250.670 311.040 202.423 1.00 138.27 ? 7    PRO L CG  1 
ATOM   4474 C CD  . PRO E 5 7   ? 249.573 310.227 203.086 1.00 135.86 ? 7    PRO L CD  1 
ATOM   4475 N N   . PRO E 5 8   ? 247.039 313.664 200.959 1.00 138.06 ? 8    PRO L N   1 
ATOM   4476 C CA  . PRO E 5 8   ? 245.919 313.958 200.088 1.00 136.41 ? 8    PRO L CA  1 
ATOM   4477 C C   . PRO E 5 8   ? 246.157 313.537 198.640 1.00 139.17 ? 8    PRO L C   1 
ATOM   4478 O O   . PRO E 5 8   ? 245.203 313.240 197.919 1.00 135.17 ? 8    PRO L O   1 
ATOM   4479 C CB  . PRO E 5 8   ? 245.797 315.485 200.218 1.00 138.16 ? 8    PRO L CB  1 
ATOM   4480 C CG  . PRO E 5 8   ? 247.181 315.955 200.644 1.00 138.72 ? 8    PRO L CG  1 
ATOM   4481 C CD  . PRO E 5 8   ? 247.738 314.831 201.491 1.00 137.40 ? 8    PRO L CD  1 
ATOM   4482 N N   . SER E 5 9   ? 247.420 313.490 198.213 1.00 137.78 ? 9    SER L N   1 
ATOM   4483 C CA  . SER E 5 9   ? 247.709 313.125 196.830 1.00 136.60 ? 9    SER L CA  1 
ATOM   4484 C C   . SER E 5 9   ? 249.169 312.764 196.583 1.00 138.20 ? 9    SER L C   1 
ATOM   4485 O O   . SER E 5 9   ? 250.067 313.182 197.316 1.00 138.70 ? 9    SER L O   1 
ATOM   4486 C CB  . SER E 5 9   ? 247.318 314.259 195.901 1.00 138.48 ? 9    SER L CB  1 
ATOM   4487 N N   . VAL E 5 10  ? 249.385 312.030 195.495 1.00 139.22 ? 10   VAL L N   1 
ATOM   4488 C CA  . VAL E 5 10  ? 250.702 311.728 194.942 1.00 138.60 ? 10   VAL L CA  1 
ATOM   4489 C C   . VAL E 5 10  ? 250.704 312.017 193.443 1.00 139.73 ? 10   VAL L C   1 
ATOM   4490 O O   . VAL E 5 10  ? 249.777 311.625 192.734 1.00 137.34 ? 10   VAL L O   1 
ATOM   4491 C CB  . VAL E 5 10  ? 251.075 310.253 195.212 1.00 139.03 ? 10   VAL L CB  1 
ATOM   4492 N N   . SER E 5 11  ? 251.728 312.711 192.959 1.00 140.57 ? 11   SER L N   1 
ATOM   4493 C CA  . SER E 5 11  ? 251.784 313.066 191.542 1.00 142.40 ? 11   SER L CA  1 
ATOM   4494 C C   . SER E 5 11  ? 252.992 312.460 190.842 1.00 142.31 ? 11   SER L C   1 
ATOM   4495 O O   . SER E 5 11  ? 254.138 312.730 191.206 1.00 142.63 ? 11   SER L O   1 
ATOM   4496 C CB  . SER E 5 11  ? 251.803 314.573 191.384 1.00 142.14 ? 11   SER L CB  1 
ATOM   4497 N N   . VAL E 5 12  ? 252.721 311.621 189.845 1.00 143.10 ? 12   VAL L N   1 
ATOM   4498 C CA  . VAL E 5 12  ? 253.768 310.956 189.077 1.00 143.21 ? 12   VAL L CA  1 
ATOM   4499 C C   . VAL E 5 12  ? 253.505 311.047 187.581 1.00 141.09 ? 12   VAL L C   1 
ATOM   4500 O O   . VAL E 5 12  ? 252.373 311.267 187.150 1.00 140.84 ? 12   VAL L O   1 
ATOM   4501 C CB  . VAL E 5 12  ? 253.869 309.468 189.470 1.00 142.16 ? 12   VAL L CB  1 
ATOM   4502 N N   . SER E 5 13  ? 254.538 310.804 186.790 1.00 142.07 ? 13   SER L N   1 
ATOM   4503 C CA  . SER E 5 13  ? 254.375 310.631 185.356 1.00 142.65 ? 13   SER L CA  1 
ATOM   4504 C C   . SER E 5 13  ? 254.243 309.139 185.074 1.00 142.57 ? 13   SER L C   1 
ATOM   4505 O O   . SER E 5 13  ? 254.753 308.324 185.842 1.00 143.56 ? 13   SER L O   1 
ATOM   4506 C CB  . SER E 5 13  ? 255.569 311.217 184.622 1.00 142.27 ? 13   SER L CB  1 
ATOM   4507 N N   . PRO E 5 14  ? 253.554 308.747 184.005 1.00 142.57 ? 14   PRO L N   1 
ATOM   4508 C CA  . PRO E 5 14  ? 253.401 307.371 183.594 1.00 143.58 ? 14   PRO L CA  1 
ATOM   4509 C C   . PRO E 5 14  ? 254.772 306.762 183.352 1.00 143.36 ? 14   PRO L C   1 
ATOM   4510 O O   . PRO E 5 14  ? 255.621 307.364 182.693 1.00 143.02 ? 14   PRO L O   1 
ATOM   4511 C CB  . PRO E 5 14  ? 252.559 307.488 182.313 1.00 142.56 ? 14   PRO L CB  1 
ATOM   4512 C CG  . PRO E 5 14  ? 252.705 308.942 181.868 1.00 141.24 ? 14   PRO L CG  1 
ATOM   4513 C CD  . PRO E 5 14  ? 252.901 309.731 183.146 1.00 141.57 ? 14   PRO L CD  1 
ATOM   4514 N N   . GLY E 5 15  ? 254.985 305.575 183.906 1.00 140.71 ? 15   GLY L N   1 
ATOM   4515 C CA  . GLY E 5 15  ? 256.263 304.883 183.802 1.00 142.19 ? 15   GLY L CA  1 
ATOM   4516 C C   . GLY E 5 15  ? 257.114 305.060 185.058 1.00 142.41 ? 15   GLY L C   1 
ATOM   4517 O O   . GLY E 5 15  ? 258.086 304.333 185.262 1.00 141.69 ? 15   GLY L O   1 
ATOM   4518 N N   . GLN E 5 16  ? 256.743 306.015 185.910 1.00 142.02 ? 16   GLN L N   1 
ATOM   4519 C CA  . GLN E 5 16  ? 257.485 306.266 187.143 1.00 140.92 ? 16   GLN L CA  1 
ATOM   4520 C C   . GLN E 5 16  ? 256.965 305.421 188.295 1.00 143.56 ? 16   GLN L C   1 
ATOM   4521 O O   . GLN E 5 16  ? 255.888 304.824 188.210 1.00 137.82 ? 16   GLN L O   1 
ATOM   4522 C CB  . GLN E 5 16  ? 257.439 307.747 187.530 1.00 143.29 ? 16   GLN L CB  1 
ATOM   4523 N N   . THR E 5 17  ? 257.742 305.362 189.372 1.00 141.06 ? 17   THR L N   1 
ATOM   4524 C CA  . THR E 5 17  ? 257.335 304.626 190.559 1.00 142.30 ? 17   THR L CA  1 
ATOM   4525 C C   . THR E 5 17  ? 256.524 305.513 191.499 1.00 140.40 ? 17   THR L C   1 
ATOM   4526 O O   . THR E 5 17  ? 256.976 306.589 191.895 1.00 141.90 ? 17   THR L O   1 
ATOM   4527 C CB  . THR E 5 17  ? 258.559 304.072 191.312 1.00 141.00 ? 17   THR L CB  1 
ATOM   4528 N N   . ALA E 5 18  ? 255.332 305.052 191.862 1.00 140.26 ? 18   ALA L N   1 
ATOM   4529 C CA  . ALA E 5 18  ? 254.477 305.788 192.786 1.00 141.64 ? 18   ALA L CA  1 
ATOM   4530 C C   . ALA E 5 18  ? 254.735 305.337 194.212 1.00 139.00 ? 18   ALA L C   1 
ATOM   4531 O O   . ALA E 5 18  ? 254.956 304.152 194.464 1.00 137.01 ? 18   ALA L O   1 
ATOM   4532 C CB  . ALA E 5 18  ? 253.009 305.603 192.434 1.00 139.25 ? 18   ALA L CB  1 
ATOM   4533 N N   . SER E 5 19  ? 254.660 306.274 195.152 1.00 138.74 ? 19   SER L N   1 
ATOM   4534 C CA  . SER E 5 19  ? 254.815 305.954 196.566 1.00 137.69 ? 19   SER L CA  1 
ATOM   4535 C C   . SER E 5 19  ? 253.679 306.534 197.396 1.00 136.34 ? 19   SER L C   1 
ATOM   4536 O O   . SER E 5 19  ? 253.606 307.744 197.615 1.00 136.51 ? 19   SER L O   1 
ATOM   4537 C CB  . SER E 5 19  ? 256.140 306.482 197.077 1.00 138.66 ? 19   SER L CB  1 
ATOM   4538 N N   . ILE E 5 20  ? 252.792 305.660 197.855 1.00 137.84 ? 20   ILE L N   1 
ATOM   4539 C CA  . ILE E 5 20  ? 251.627 306.061 198.633 1.00 135.73 ? 20   ILE L CA  1 
ATOM   4540 C C   . ILE E 5 20  ? 251.721 305.508 200.049 1.00 133.41 ? 20   ILE L C   1 
ATOM   4541 O O   . ILE E 5 20  ? 251.825 304.299 200.247 1.00 136.30 ? 20   ILE L O   1 
ATOM   4542 C CB  . ILE E 5 20  ? 250.337 305.581 197.942 1.00 135.93 ? 20   ILE L CB  1 
ATOM   4543 N N   . THR E 5 21  ? 251.715 306.393 201.038 1.00 136.10 ? 21   THR L N   1 
ATOM   4544 C CA  . THR E 5 21  ? 251.945 305.963 202.412 1.00 134.92 ? 21   THR L CA  1 
ATOM   4545 C C   . THR E 5 21  ? 250.728 306.161 203.314 1.00 133.40 ? 21   THR L C   1 
ATOM   4546 O O   . THR E 5 21  ? 249.824 306.936 202.996 1.00 131.06 ? 21   THR L O   1 
ATOM   4547 C CB  . THR E 5 21  ? 253.156 306.707 203.008 1.00 133.80 ? 21   THR L CB  1 
ATOM   4548 N N   . CYS E 5 22  ? 250.732 305.451 204.448 1.00 132.26 ? 22   CYS L N   1 
ATOM   4549 C CA  . CYS E 5 22  ? 249.706 305.544 205.485 1.00 130.21 ? 22   CYS L CA  1 
ATOM   4550 C C   . CYS E 5 22  ? 250.307 305.271 206.857 1.00 133.54 ? 22   CYS L C   1 
ATOM   4551 O O   . CYS E 5 22  ? 251.076 304.322 207.031 1.00 125.42 ? 22   CYS L O   1 
ATOM   4552 C CB  . CYS E 5 22  ? 248.571 304.551 205.212 1.00 134.76 ? 22   CYS L CB  1 
ATOM   4553 S SG  . CYS E 5 22  ? 247.236 304.595 206.427 1.00 136.46 ? 22   CYS L SG  1 
ATOM   4554 N N   . SER E 5 23  ? 249.969 306.096 207.838 1.00 130.97 ? 23   SER L N   1 
ATOM   4555 C CA  . SER E 5 23  ? 250.529 305.931 209.174 1.00 130.26 ? 23   SER L CA  1 
ATOM   4556 C C   . SER E 5 23  ? 249.461 305.815 210.251 1.00 130.28 ? 23   SER L C   1 
ATOM   4557 O O   . SER E 5 23  ? 248.339 306.300 210.092 1.00 129.55 ? 23   SER L O   1 
ATOM   4558 C CB  . SER E 5 23  ? 251.453 307.090 209.496 1.00 129.87 ? 23   SER L CB  1 
ATOM   4559 N N   . GLY E 5 24  ? 249.837 305.202 211.369 1.00 126.61 ? 24   GLY L N   1 
ATOM   4560 C CA  . GLY E 5 24  ? 248.948 305.069 212.519 1.00 128.29 ? 24   GLY L CA  1 
ATOM   4561 C C   . GLY E 5 24  ? 249.756 304.850 213.791 1.00 126.55 ? 24   GLY L C   1 
ATOM   4562 O O   . GLY E 5 24  ? 250.979 304.985 213.785 1.00 127.81 ? 24   GLY L O   1 
ATOM   4563 N N   . ASP E 5 25  ? 249.075 304.531 214.888 1.00 127.61 ? 25   ASP L N   1 
ATOM   4564 C CA  . ASP E 5 25  ? 249.755 304.330 216.164 1.00 127.13 ? 25   ASP L CA  1 
ATOM   4565 C C   . ASP E 5 25  ? 250.122 302.869 216.395 1.00 126.65 ? 25   ASP L C   1 
ATOM   4566 O O   . ASP E 5 25  ? 251.122 302.567 217.045 1.00 125.65 ? 25   ASP L O   1 
ATOM   4567 C CB  . ASP E 5 25  ? 248.873 304.814 217.316 1.00 127.08 ? 25   ASP L CB  1 
ATOM   4568 N N   . LYS E 5 26  ? 249.291 301.966 215.885 1.00 127.71 ? 26   LYS L N   1 
ATOM   4569 C CA  . LYS E 5 26  ? 249.463 300.533 216.096 1.00 128.33 ? 26   LYS L CA  1 
ATOM   4570 C C   . LYS E 5 26  ? 249.597 299.807 214.768 1.00 124.73 ? 26   LYS L C   1 
ATOM   4571 O O   . LYS E 5 26  ? 249.414 298.594 214.690 1.00 124.87 ? 26   LYS L O   1 
ATOM   4572 C CB  . LYS E 5 26  ? 248.267 299.965 216.856 1.00 126.20 ? 26   LYS L CB  1 
ATOM   4573 N N   . LEU E 5 27  ? 249.865 300.560 213.713 1.00 112.14 ? 27   LEU L N   1 
ATOM   4574 C CA  . LEU E 5 27  ? 249.849 300.010 212.366 1.00 128.59 ? 27   LEU L CA  1 
ATOM   4575 C C   . LEU E 5 27  ? 250.892 298.911 212.190 1.00 128.42 ? 27   LEU L C   1 
ATOM   4576 O O   . LEU E 5 27  ? 250.641 297.913 211.517 1.00 123.30 ? 27   LEU L O   1 
ATOM   4577 C CB  . LEU E 5 27  ? 250.066 301.141 211.350 1.00 129.28 ? 27   LEU L CB  1 
ATOM   4578 N N   . GLY E 5 28  ? 252.051 299.077 212.816 1.00 120.49 ? 28   GLY L N   1 
ATOM   4579 C CA  . GLY E 5 28  ? 253.139 298.115 212.670 1.00 126.29 ? 28   GLY L CA  1 
ATOM   4580 C C   . GLY E 5 28  ? 252.942 296.888 213.555 1.00 120.96 ? 28   GLY L C   1 
ATOM   4581 O O   . GLY E 5 28  ? 253.712 295.930 213.480 1.00 120.42 ? 28   GLY L O   1 
ATOM   4582 N N   . GLU E 5 29  ? 251.917 296.922 214.403 1.00 122.21 ? 29   GLU L N   1 
ATOM   4583 C CA  . GLU E 5 29  ? 251.637 295.822 215.315 1.00 119.14 ? 29   GLU L CA  1 
ATOM   4584 C C   . GLU E 5 29  ? 250.575 294.895 214.742 1.00 115.32 ? 29   GLU L C   1 
ATOM   4585 O O   . GLU E 5 29  ? 250.235 293.874 215.341 1.00 113.07 ? 29   GLU L O   1 
ATOM   4586 C CB  . GLU E 5 29  ? 251.177 296.359 216.672 1.00 120.13 ? 29   GLU L CB  1 
ATOM   4587 N N   . THR E 5 30  ? 250.034 295.271 213.589 1.00 115.75 ? 30   THR L N   1 
ATOM   4588 C CA  . THR E 5 30  ? 248.956 294.523 212.964 1.00 113.08 ? 30   THR L CA  1 
ATOM   4589 C C   . THR E 5 30  ? 249.219 294.345 211.479 1.00 115.78 ? 30   THR L C   1 
ATOM   4590 O O   . THR E 5 30  ? 250.336 294.558 211.008 1.00 109.60 ? 30   THR L O   1 
ATOM   4591 C CB  . THR E 5 30  ? 247.597 295.217 213.186 1.00 115.70 ? 30   THR L CB  1 
ATOM   4592 N N   . TYR E 5 31  ? 248.205 293.909 210.748 1.00 111.30 ? 31   TYR L N   1 
ATOM   4593 C CA  . TYR E 5 31  ? 248.337 293.743 209.311 1.00 114.07 ? 31   TYR L CA  1 
ATOM   4594 C C   . TYR E 5 31  ? 247.664 294.882 208.562 1.00 114.90 ? 31   TYR L C   1 
ATOM   4595 O O   . TYR E 5 31  ? 246.517 295.230 208.840 1.00 116.28 ? 31   TYR L O   1 
ATOM   4596 C CB  . TYR E 5 31  ? 247.755 292.405 208.865 1.00 109.40 ? 31   TYR L CB  1 
ATOM   4597 N N   . ALA E 5 32  ? 248.377 295.445 207.596 1.00 117.86 ? 32   ALA L N   1 
ATOM   4598 C CA  . ALA E 5 32  ? 247.839 296.518 206.772 1.00 120.53 ? 32   ALA L CA  1 
ATOM   4599 C C   . ALA E 5 32  ? 247.323 295.978 205.445 1.00 120.83 ? 32   ALA L C   1 
ATOM   4600 O O   . ALA E 5 32  ? 247.805 294.959 204.946 1.00 117.08 ? 32   ALA L O   1 
ATOM   4601 C CB  . ALA E 5 32  ? 248.907 297.575 206.527 1.00 123.16 ? 32   ALA L CB  1 
ATOM   4602 N N   . SER E 5 33  ? 246.377 296.691 204.845 1.00 122.97 ? 33   SER L N   1 
ATOM   4603 C CA  . SER E 5 33  ? 245.917 296.357 203.501 1.00 122.56 ? 33   SER L CA  1 
ATOM   4604 C C   . SER E 5 33  ? 245.621 297.618 202.701 1.00 144.34 ? 33   SER L C   1 
ATOM   4605 O O   . SER E 5 33  ? 245.403 298.690 203.268 1.00 127.53 ? 33   SER L O   1 
ATOM   4606 C CB  . SER E 5 33  ? 244.686 295.476 203.567 1.00 122.92 ? 33   SER L CB  1 
ATOM   4607 N N   . TRP E 5 34  ? 245.638 297.489 201.375 1.00 128.82 ? 34   TRP L N   1 
ATOM   4608 C CA  . TRP E 5 34  ? 245.409 298.625 200.489 1.00 128.53 ? 34   TRP L CA  1 
ATOM   4609 C C   . TRP E 5 34  ? 244.341 298.363 199.441 1.00 135.58 ? 34   TRP L C   1 
ATOM   4610 O O   . TRP E 5 34  ? 244.272 297.275 198.862 1.00 115.49 ? 34   TRP L O   1 
ATOM   4611 C CB  . TRP E 5 34  ? 246.697 299.003 199.775 1.00 130.26 ? 34   TRP L CB  1 
ATOM   4612 N N   . TYR E 5 35  ? 243.566 299.407 199.147 1.00 128.27 ? 35   TYR L N   1 
ATOM   4613 C CA  . TYR E 5 35  ? 242.521 299.358 198.133 1.00 135.31 ? 35   TYR L CA  1 
ATOM   4614 C C   . TYR E 5 35  ? 242.701 300.413 197.051 1.00 136.64 ? 35   TYR L C   1 
ATOM   4615 O O   . TYR E 5 35  ? 243.137 301.531 197.322 1.00 133.85 ? 35   TYR L O   1 
ATOM   4616 C CB  . TYR E 5 35  ? 241.156 299.544 198.785 1.00 131.23 ? 35   TYR L CB  1 
ATOM   4617 N N   . GLN E 5 36  ? 242.299 300.064 195.834 1.00 131.90 ? 36   GLN L N   1 
ATOM   4618 C CA  . GLN E 5 36  ? 242.299 300.984 194.703 1.00 135.72 ? 36   GLN L CA  1 
ATOM   4619 C C   . GLN E 5 36  ? 240.876 301.307 194.267 1.00 137.34 ? 36   GLN L C   1 
ATOM   4620 O O   . GLN E 5 36  ? 240.125 300.409 193.888 1.00 131.26 ? 36   GLN L O   1 
ATOM   4621 C CB  . GLN E 5 36  ? 243.055 300.366 193.529 1.00 132.92 ? 36   GLN L CB  1 
ATOM   4622 N N   . GLN E 5 37  ? 240.497 302.581 194.318 1.00 134.38 ? 37   GLN L N   1 
ATOM   4623 C CA  . GLN E 5 37  ? 239.128 302.955 193.978 1.00 137.44 ? 37   GLN L CA  1 
ATOM   4624 C C   . GLN E 5 37  ? 239.034 304.072 192.945 1.00 136.91 ? 37   GLN L C   1 
ATOM   4625 O O   . GLN E 5 37  ? 239.757 305.066 193.010 1.00 133.98 ? 37   GLN L O   1 
ATOM   4626 C CB  . GLN E 5 37  ? 238.362 303.379 195.229 1.00 135.51 ? 37   GLN L CB  1 
ATOM   4627 N N   . LYS E 5 38  ? 238.089 303.926 192.025 1.00 137.78 ? 38   LYS L N   1 
ATOM   4628 C CA  . LYS E 5 38  ? 237.763 304.982 191.079 1.00 138.24 ? 38   LYS L CA  1 
ATOM   4629 C C   . LYS E 5 38  ? 236.322 305.435 191.322 1.00 143.84 ? 38   LYS L C   1 
ATOM   4630 O O   . LYS E 5 38  ? 235.503 304.636 191.774 1.00 133.26 ? 38   LYS L O   1 
ATOM   4631 C CB  . LYS E 5 38  ? 237.953 304.486 189.647 1.00 138.64 ? 38   LYS L CB  1 
ATOM   4632 N N   . PRO E 5 39  ? 235.984 306.695 191.033 1.00 137.93 ? 39   PRO L N   1 
ATOM   4633 C CA  . PRO E 5 39  ? 234.654 307.258 191.159 1.00 137.92 ? 39   PRO L CA  1 
ATOM   4634 C C   . PRO E 5 39  ? 233.626 306.404 190.433 1.00 138.84 ? 39   PRO L C   1 
ATOM   4635 O O   . PRO E 5 39  ? 233.825 306.029 189.276 1.00 138.00 ? 39   PRO L O   1 
ATOM   4636 C CB  . PRO E 5 39  ? 234.823 308.626 190.485 1.00 138.88 ? 39   PRO L CB  1 
ATOM   4637 C CG  . PRO E 5 39  ? 236.278 308.975 190.709 1.00 137.83 ? 39   PRO L CG  1 
ATOM   4638 C CD  . PRO E 5 39  ? 237.014 307.652 190.598 1.00 137.80 ? 39   PRO L CD  1 
ATOM   4639 N N   . GLY E 5 40  ? 232.528 306.101 191.119 1.00 138.31 ? 40   GLY L N   1 
ATOM   4640 C CA  . GLY E 5 40  ? 231.448 305.305 190.548 1.00 139.66 ? 40   GLY L CA  1 
ATOM   4641 C C   . GLY E 5 40  ? 231.720 303.803 190.625 1.00 139.29 ? 40   GLY L C   1 
ATOM   4642 O O   . GLY E 5 40  ? 230.933 303.002 190.122 1.00 138.68 ? 40   GLY L O   1 
ATOM   4643 N N   . GLN E 5 41  ? 232.836 303.421 191.243 1.00 138.50 ? 41   GLN L N   1 
ATOM   4644 C CA  . GLN E 5 41  ? 233.218 302.014 191.314 1.00 138.21 ? 41   GLN L CA  1 
ATOM   4645 C C   . GLN E 5 41  ? 233.554 301.574 192.737 1.00 136.71 ? 41   GLN L C   1 
ATOM   4646 O O   . GLN E 5 41  ? 233.943 302.389 193.575 1.00 136.48 ? 41   GLN L O   1 
ATOM   4647 C CB  . GLN E 5 41  ? 234.413 301.754 190.393 1.00 139.27 ? 41   GLN L CB  1 
ATOM   4648 N N   . SER E 5 42  ? 233.423 300.274 192.995 1.00 136.41 ? 42   SER L N   1 
ATOM   4649 C CA  . SER E 5 42  ? 233.841 299.703 194.270 1.00 134.46 ? 42   SER L CA  1 
ATOM   4650 C C   . SER E 5 42  ? 235.365 299.708 194.351 1.00 132.60 ? 42   SER L C   1 
ATOM   4651 O O   . SER E 5 42  ? 236.033 299.711 193.317 1.00 134.63 ? 42   SER L O   1 
ATOM   4652 C CB  . SER E 5 42  ? 233.322 298.278 194.390 1.00 132.59 ? 42   SER L CB  1 
ATOM   4653 N N   . PRO E 5 43  ? 235.933 299.723 195.560 1.00 132.97 ? 43   PRO L N   1 
ATOM   4654 C CA  . PRO E 5 43  ? 237.347 299.576 195.843 1.00 134.48 ? 43   PRO L CA  1 
ATOM   4655 C C   . PRO E 5 43  ? 237.822 298.156 195.562 1.00 132.52 ? 43   PRO L C   1 
ATOM   4656 O O   . PRO E 5 43  ? 237.126 297.188 195.865 1.00 131.15 ? 43   PRO L O   1 
ATOM   4657 C CB  . PRO E 5 43  ? 237.422 299.928 197.335 1.00 130.86 ? 43   PRO L CB  1 
ATOM   4658 C CG  . PRO E 5 43  ? 236.044 299.626 197.871 1.00 133.07 ? 43   PRO L CG  1 
ATOM   4659 C CD  . PRO E 5 43  ? 235.094 299.941 196.741 1.00 133.38 ? 43   PRO L CD  1 
ATOM   4660 N N   . ILE E 5 44  ? 239.029 298.039 195.028 1.00 129.75 ? 44   ILE L N   1 
ATOM   4661 C CA  . ILE E 5 44  ? 239.629 296.743 194.749 1.00 130.49 ? 44   ILE L CA  1 
ATOM   4662 C C   . ILE E 5 44  ? 240.805 296.475 195.670 1.00 133.68 ? 44   ILE L C   1 
ATOM   4663 O O   . ILE E 5 44  ? 241.701 297.304 195.804 1.00 128.00 ? 44   ILE L O   1 
ATOM   4664 C CB  . ILE E 5 44  ? 240.095 296.660 193.283 1.00 131.15 ? 44   ILE L CB  1 
ATOM   4665 N N   . LEU E 5 45  ? 240.805 295.311 196.304 1.00 128.39 ? 45   LEU L N   1 
ATOM   4666 C CA  . LEU E 5 45  ? 241.915 294.940 197.166 1.00 128.60 ? 45   LEU L CA  1 
ATOM   4667 C C   . LEU E 5 45  ? 243.134 294.633 196.313 1.00 129.80 ? 45   LEU L C   1 
ATOM   4668 O O   . LEU E 5 45  ? 243.079 293.775 195.433 1.00 125.97 ? 45   LEU L O   1 
ATOM   4669 C CB  . LEU E 5 45  ? 241.540 293.707 198.006 1.00 127.55 ? 45   LEU L CB  1 
ATOM   4670 N N   . VAL E 5 46  ? 244.230 295.338 196.567 1.00 128.48 ? 46   VAL L N   1 
ATOM   4671 C CA  . VAL E 5 46  ? 245.454 295.119 195.806 1.00 128.89 ? 46   VAL L CA  1 
ATOM   4672 C C   . VAL E 5 46  ? 246.545 294.505 196.672 1.00 127.97 ? 46   VAL L C   1 
ATOM   4673 O O   . VAL E 5 46  ? 247.351 293.708 196.193 1.00 127.88 ? 46   VAL L O   1 
ATOM   4674 C CB  . VAL E 5 46  ? 245.941 296.430 195.139 1.00 129.49 ? 46   VAL L CB  1 
ATOM   4675 N N   . ILE E 5 47  ? 246.579 294.888 197.945 1.00 128.58 ? 47   ILE L N   1 
ATOM   4676 C CA  . ILE E 5 47  ? 247.553 294.336 198.883 1.00 126.73 ? 47   ILE L CA  1 
ATOM   4677 C C   . ILE E 5 47  ? 246.893 293.978 200.212 1.00 128.93 ? 47   ILE L C   1 
ATOM   4678 O O   . ILE E 5 47  ? 246.152 294.778 200.781 1.00 122.52 ? 47   ILE L O   1 
ATOM   4679 C CB  . ILE E 5 47  ? 248.730 295.308 199.118 1.00 128.93 ? 47   ILE L CB  1 
ATOM   4680 N N   . TYR E 5 48  ? 247.195 292.789 200.725 1.00 122.11 ? 48   TYR L N   1 
ATOM   4681 C CA  . TYR E 5 48  ? 246.696 292.374 202.033 1.00 119.71 ? 48   TYR L CA  1 
ATOM   4682 C C   . TYR E 5 48  ? 247.819 291.770 202.863 1.00 120.45 ? 48   TYR L C   1 
ATOM   4683 O O   . TYR E 5 48  ? 248.844 291.351 202.328 1.00 124.48 ? 48   TYR L O   1 
ATOM   4684 C CB  . TYR E 5 48  ? 245.536 291.388 201.886 1.00 119.87 ? 48   TYR L CB  1 
ATOM   4685 N N   . GLN E 5 49  ? 247.644 291.763 204.180 1.00 117.02 ? 49   GLN L N   1 
ATOM   4686 C CA  . GLN E 5 49  ? 248.673 291.247 205.073 1.00 111.64 ? 49   GLN L CA  1 
ATOM   4687 C C   . GLN E 5 49  ? 250.036 291.855 204.763 1.00 118.70 ? 49   GLN L C   1 
ATOM   4688 O O   . GLN E 5 49  ? 251.031 291.143 204.621 1.00 115.08 ? 49   GLN L O   1 
ATOM   4689 C CB  . GLN E 5 49  ? 248.729 289.720 205.038 1.00 109.43 ? 49   GLN L CB  1 
ATOM   4690 N N   . ASP E 5 50  ? 250.062 293.182 204.671 1.00 118.52 ? 50   ASP L N   1 
ATOM   4691 C CA  . ASP E 5 50  ? 251.267 293.982 204.457 1.00 119.06 ? 50   ASP L CA  1 
ATOM   4692 C C   . ASP E 5 50  ? 251.824 293.913 203.035 1.00 121.47 ? 50   ASP L C   1 
ATOM   4693 O O   . ASP E 5 50  ? 251.993 294.949 202.391 1.00 122.98 ? 50   ASP L O   1 
ATOM   4694 C CB  . ASP E 5 50  ? 252.370 293.604 205.453 1.00 119.44 ? 50   ASP L CB  1 
ATOM   4695 N N   . ASN E 5 51  ? 252.164 292.717 202.560 1.00 120.80 ? 51   ASN L N   1 
ATOM   4696 C CA  . ASN E 5 51  ? 252.841 292.618 201.269 1.00 122.40 ? 51   ASN L CA  1 
ATOM   4697 C C   . ASN E 5 51  ? 252.369 291.482 200.355 1.00 122.61 ? 51   ASN L C   1 
ATOM   4698 O O   . ASN E 5 51  ? 253.119 291.050 199.480 1.00 122.57 ? 51   ASN L O   1 
ATOM   4699 C CB  . ASN E 5 51  ? 254.338 292.518 201.488 1.00 125.59 ? 51   ASN L CB  1 
ATOM   4700 N N   . LYS E 5 52  ? 251.141 291.002 200.529 1.00 120.90 ? 52   LYS L N   1 
ATOM   4701 C CA  . LYS E 5 52  ? 250.655 289.923 199.673 1.00 121.87 ? 52   LYS L CA  1 
ATOM   4702 C C   . LYS E 5 52  ? 249.654 290.422 198.639 1.00 120.28 ? 52   LYS L C   1 
ATOM   4703 O O   . LYS E 5 52  ? 248.726 291.161 198.964 1.00 124.32 ? 52   LYS L O   1 
ATOM   4704 C CB  . LYS E 5 52  ? 250.019 288.817 200.514 1.00 119.23 ? 52   LYS L CB  1 
ATOM   4705 N N   . ARG E 5 53  ? 249.823 289.991 197.392 1.00 124.50 ? 53   ARG L N   1 
ATOM   4706 C CA  . ARG E 5 53  ? 248.865 290.337 196.347 1.00 125.44 ? 53   ARG L CA  1 
ATOM   4707 C C   . ARG E 5 53  ? 247.801 289.250 196.206 1.00 125.81 ? 53   ARG L C   1 
ATOM   4708 O O   . ARG E 5 53  ? 248.127 288.065 196.252 1.00 124.43 ? 53   ARG L O   1 
ATOM   4709 C CB  . ARG E 5 53  ? 249.551 290.505 194.998 1.00 126.61 ? 53   ARG L CB  1 
ATOM   4710 N N   . PRO E 5 54  ? 246.530 289.629 196.041 1.00 127.06 ? 54   PRO L N   1 
ATOM   4711 C CA  . PRO E 5 54  ? 245.432 288.793 195.597 1.00 127.02 ? 54   PRO L CA  1 
ATOM   4712 C C   . PRO E 5 54  ? 245.678 288.338 194.168 1.00 126.75 ? 54   PRO L C   1 
ATOM   4713 O O   . PRO E 5 54  ? 246.311 289.050 193.385 1.00 127.50 ? 54   PRO L O   1 
ATOM   4714 C CB  . PRO E 5 54  ? 244.222 289.733 195.677 1.00 126.83 ? 54   PRO L CB  1 
ATOM   4715 C CG  . PRO E 5 54  ? 244.643 290.840 196.616 1.00 125.57 ? 54   PRO L CG  1 
ATOM   4716 C CD  . PRO E 5 54  ? 246.140 290.974 196.431 1.00 122.38 ? 54   PRO L CD  1 
ATOM   4717 N N   . SER E 5 55  ? 245.159 287.173 193.814 1.00 128.33 ? 55   SER L N   1 
ATOM   4718 C CA  . SER E 5 55  ? 245.291 286.712 192.442 1.00 128.63 ? 55   SER L CA  1 
ATOM   4719 C C   . SER E 5 55  ? 244.598 287.686 191.499 1.00 128.70 ? 55   SER L C   1 
ATOM   4720 O O   . SER E 5 55  ? 243.506 288.175 191.792 1.00 129.29 ? 55   SER L O   1 
ATOM   4721 C CB  . SER E 5 55  ? 244.697 285.325 192.293 1.00 129.18 ? 55   SER L CB  1 
ATOM   4722 N N   . GLY E 5 56  ? 245.233 287.961 190.366 1.00 127.94 ? 56   GLY L N   1 
ATOM   4723 C CA  . GLY E 5 56  ? 244.665 288.859 189.364 1.00 128.46 ? 56   GLY L CA  1 
ATOM   4724 C C   . GLY E 5 56  ? 245.222 290.278 189.469 1.00 128.82 ? 56   GLY L C   1 
ATOM   4725 O O   . GLY E 5 56  ? 245.031 291.090 188.565 1.00 130.33 ? 56   GLY L O   1 
ATOM   4726 N N   . ILE E 5 57  ? 245.917 290.572 190.565 1.00 128.96 ? 57   ILE L N   1 
ATOM   4727 C CA  . ILE E 5 57  ? 246.498 291.895 190.762 1.00 130.92 ? 57   ILE L CA  1 
ATOM   4728 C C   . ILE E 5 57  ? 247.879 291.984 190.101 1.00 131.43 ? 57   ILE L C   1 
ATOM   4729 O O   . ILE E 5 57  ? 248.746 291.155 190.381 1.00 132.93 ? 57   ILE L O   1 
ATOM   4730 C CB  . ILE E 5 57  ? 246.604 292.226 192.262 1.00 129.14 ? 57   ILE L CB  1 
ATOM   4731 N N   . PRO E 5 58  ? 248.106 292.980 189.231 1.00 132.61 ? 58   PRO L N   1 
ATOM   4732 C CA  . PRO E 5 58  ? 249.327 293.215 188.481 1.00 133.83 ? 58   PRO L CA  1 
ATOM   4733 C C   . PRO E 5 58  ? 250.564 293.229 189.366 1.00 140.47 ? 58   PRO L C   1 
ATOM   4734 O O   . PRO E 5 58  ? 250.536 293.732 190.490 1.00 118.21 ? 58   PRO L O   1 
ATOM   4735 C CB  . PRO E 5 58  ? 249.073 294.602 187.877 1.00 135.50 ? 58   PRO L CB  1 
ATOM   4736 C CG  . PRO E 5 58  ? 247.577 294.675 187.719 1.00 133.93 ? 58   PRO L CG  1 
ATOM   4737 C CD  . PRO E 5 58  ? 247.019 293.928 188.911 1.00 132.00 ? 58   PRO L CD  1 
ATOM   4738 N N   . GLU E 5 59  ? 251.658 292.703 188.822 1.00 133.29 ? 59   GLU L N   1 
ATOM   4739 C CA  . GLU E 5 59  ? 252.940 292.597 189.514 1.00 136.38 ? 59   GLU L CA  1 
ATOM   4740 C C   . GLU E 5 59  ? 253.548 293.962 189.800 1.00 134.32 ? 59   GLU L C   1 
ATOM   4741 O O   . GLU E 5 59  ? 254.566 294.069 190.485 1.00 133.94 ? 59   GLU L O   1 
ATOM   4742 C CB  . GLU E 5 59  ? 253.920 291.751 188.695 1.00 134.88 ? 59   GLU L CB  1 
ATOM   4743 N N   . ARG E 5 60  ? 252.922 295.006 189.269 1.00 135.16 ? 60   ARG L N   1 
ATOM   4744 C CA  . ARG E 5 60  ? 253.358 296.373 189.504 1.00 137.39 ? 60   ARG L CA  1 
ATOM   4745 C C   . ARG E 5 60  ? 253.229 296.728 190.981 1.00 143.29 ? 60   ARG L C   1 
ATOM   4746 O O   . ARG E 5 60  ? 253.898 297.639 191.467 1.00 132.19 ? 60   ARG L O   1 
ATOM   4747 C CB  . ARG E 5 60  ? 252.540 297.360 188.675 1.00 137.30 ? 60   ARG L CB  1 
ATOM   4748 N N   . PHE E 5 61  ? 252.334 296.033 191.683 1.00 135.11 ? 61   PHE L N   1 
ATOM   4749 C CA  . PHE E 5 61  ? 252.058 296.338 193.081 1.00 135.21 ? 61   PHE L CA  1 
ATOM   4750 C C   . PHE E 5 61  ? 252.955 295.593 194.063 1.00 134.63 ? 61   PHE L C   1 
ATOM   4751 O O   . PHE E 5 61  ? 253.136 294.377 193.976 1.00 133.29 ? 61   PHE L O   1 
ATOM   4752 C CB  . PHE E 5 61  ? 250.597 296.032 193.408 1.00 136.55 ? 61   PHE L CB  1 
ATOM   4753 N N   . SER E 5 62  ? 253.454 296.337 195.041 1.00 132.24 ? 62   SER L N   1 
ATOM   4754 C CA  . SER E 5 62  ? 254.229 295.797 196.150 1.00 133.49 ? 62   SER L CA  1 
ATOM   4755 C C   . SER E 5 62  ? 254.063 296.713 197.353 1.00 131.70 ? 62   SER L C   1 
ATOM   4756 O O   . SER E 5 62  ? 253.477 297.789 197.233 1.00 133.47 ? 62   SER L O   1 
ATOM   4757 C CB  . SER E 5 62  ? 255.694 295.675 195.774 1.00 130.95 ? 62   SER L CB  1 
ATOM   4758 N N   . GLY E 5 63  ? 254.563 296.300 198.510 1.00 130.98 ? 63   GLY L N   1 
ATOM   4759 C CA  . GLY E 5 63  ? 254.436 297.145 199.691 1.00 131.86 ? 63   GLY L CA  1 
ATOM   4760 C C   . GLY E 5 63  ? 255.143 296.571 200.907 1.00 129.10 ? 63   GLY L C   1 
ATOM   4761 O O   . GLY E 5 63  ? 255.761 295.507 200.841 1.00 127.91 ? 63   GLY L O   1 
ATOM   4762 N N   . SER E 5 64  ? 255.063 297.309 202.010 1.00 128.11 ? 64   SER L N   1 
ATOM   4763 C CA  . SER E 5 64  ? 255.696 296.922 203.266 1.00 128.59 ? 64   SER L CA  1 
ATOM   4764 C C   . SER E 5 64  ? 255.042 297.627 204.450 1.00 129.14 ? 64   SER L C   1 
ATOM   4765 O O   . SER E 5 64  ? 254.212 298.521 204.271 1.00 128.50 ? 64   SER L O   1 
ATOM   4766 C CB  . SER E 5 64  ? 257.180 297.237 203.232 1.00 130.15 ? 64   SER L CB  1 
ATOM   4767 N N   . ASN E 5 65  ? 255.416 297.216 205.659 1.00 128.70 ? 65   ASN L N   1 
ATOM   4768 C CA  . ASN E 5 65  ? 254.885 297.812 206.882 1.00 127.15 ? 65   ASN L CA  1 
ATOM   4769 C C   . ASN E 5 65  ? 255.936 297.833 207.989 1.00 129.96 ? 65   ASN L C   1 
ATOM   4770 O O   . ASN E 5 65  ? 256.293 296.790 208.535 1.00 131.65 ? 65   ASN L O   1 
ATOM   4771 C CB  . ASN E 5 65  ? 253.640 297.064 207.332 1.00 126.21 ? 65   ASN L CB  1 
ATOM   4772 N N   . SER E 5 66  ? 256.451 299.023 208.294 1.00 130.63 ? 66   SER L N   1 
ATOM   4773 C CA  . SER E 5 66  ? 257.484 299.171 209.316 1.00 131.21 ? 66   SER L CA  1 
ATOM   4774 C C   . SER E 5 66  ? 257.395 300.536 209.984 1.00 131.40 ? 66   SER L C   1 
ATOM   4775 O O   . SER E 5 66  ? 256.915 301.499 209.388 1.00 131.85 ? 66   SER L O   1 
ATOM   4776 C CB  . SER E 5 66  ? 258.861 298.983 208.708 1.00 131.41 ? 66   SER L CB  1 
ATOM   4777 N N   . GLU E 5 67  ? 257.852 300.619 211.230 1.00 131.48 ? 67   GLU L N   1 
ATOM   4778 C CA  . GLU E 5 67  ? 257.844 301.880 211.972 1.00 130.94 ? 67   GLU L CA  1 
ATOM   4779 C C   . GLU E 5 67  ? 256.454 302.516 211.969 1.00 129.37 ? 67   GLU L C   1 
ATOM   4780 O O   . GLU E 5 67  ? 256.316 303.735 211.855 1.00 129.64 ? 67   GLU L O   1 
ATOM   4781 C CB  . GLU E 5 67  ? 258.871 302.856 211.388 1.00 131.90 ? 67   GLU L CB  1 
ATOM   4782 N N   . ASN E 5 68  ? 255.430 301.674 212.086 1.00 128.90 ? 68   ASN L N   1 
ATOM   4783 C CA  . ASN E 5 68  ? 254.032 302.100 212.111 1.00 130.61 ? 68   ASN L CA  1 
ATOM   4784 C C   . ASN E 5 68  ? 253.607 302.858 210.855 1.00 131.76 ? 68   ASN L C   1 
ATOM   4785 O O   . ASN E 5 68  ? 252.627 303.607 210.881 1.00 129.70 ? 68   ASN L O   1 
ATOM   4786 C CB  . ASN E 5 68  ? 253.742 302.917 213.356 1.00 127.66 ? 68   ASN L CB  1 
ATOM   4787 N N   . THR E 5 69  ? 254.303 302.625 209.747 1.00 126.01 ? 69   THR L N   1 
ATOM   4788 C CA  . THR E 5 69  ? 253.922 303.203 208.469 1.00 128.36 ? 69   THR L CA  1 
ATOM   4789 C C   . THR E 5 69  ? 253.829 302.135 207.388 1.00 133.36 ? 69   THR L C   1 
ATOM   4790 O O   . THR E 5 69  ? 254.769 301.368 207.167 1.00 130.05 ? 69   THR L O   1 
ATOM   4791 C CB  . THR E 5 69  ? 254.911 304.302 208.028 1.00 131.01 ? 69   THR L CB  1 
ATOM   4792 N N   . ALA E 5 70  ? 252.703 302.107 206.690 1.00 130.95 ? 70   ALA L N   1 
ATOM   4793 C CA  . ALA E 5 70  ? 252.510 301.190 205.581 1.00 131.12 ? 70   ALA L CA  1 
ATOM   4794 C C   . ALA E 5 70  ? 252.758 301.919 204.272 1.00 131.96 ? 70   ALA L C   1 
ATOM   4795 O O   . ALA E 5 70  ? 252.425 303.101 204.136 1.00 130.90 ? 70   ALA L O   1 
ATOM   4796 C CB  . ALA E 5 70  ? 251.107 300.602 205.607 1.00 128.35 ? 70   ALA L CB  1 
ATOM   4797 N N   . THR E 5 71  ? 253.340 301.224 203.306 1.00 132.45 ? 71   THR L N   1 
ATOM   4798 C CA  . THR E 5 71  ? 253.572 301.822 202.001 1.00 132.69 ? 71   THR L CA  1 
ATOM   4799 C C   . THR E 5 71  ? 253.090 300.934 200.866 1.00 134.12 ? 71   THR L C   1 
ATOM   4800 O O   . THR E 5 71  ? 253.385 299.738 200.821 1.00 136.41 ? 71   THR L O   1 
ATOM   4801 C CB  . THR E 5 71  ? 255.066 302.151 201.793 1.00 134.31 ? 71   THR L CB  1 
ATOM   4802 N N   . LEU E 5 72  ? 252.398 301.551 199.916 1.00 127.23 ? 72   LEU L N   1 
ATOM   4803 C CA  . LEU E 5 72  ? 252.041 300.918 198.658 1.00 130.66 ? 72   LEU L CA  1 
ATOM   4804 C C   . LEU E 5 72  ? 252.913 301.483 197.552 1.00 142.28 ? 72   LEU L C   1 
ATOM   4805 O O   . LEU E 5 72  ? 253.069 302.701 197.427 1.00 135.34 ? 72   LEU L O   1 
ATOM   4806 C CB  . LEU E 5 72  ? 250.551 301.146 198.348 1.00 134.79 ? 72   LEU L CB  1 
ATOM   4807 N N   . THR E 5 73  ? 253.494 300.601 196.753 1.00 134.09 ? 73   THR L N   1 
ATOM   4808 C CA  . THR E 5 73  ? 254.374 301.019 195.674 1.00 136.55 ? 73   THR L CA  1 
ATOM   4809 C C   . THR E 5 73  ? 253.882 300.491 194.338 1.00 139.15 ? 73   THR L C   1 
ATOM   4810 O O   . THR E 5 73  ? 253.518 299.320 194.217 1.00 133.56 ? 73   THR L O   1 
ATOM   4811 C CB  . THR E 5 73  ? 255.819 300.539 195.913 1.00 135.56 ? 73   THR L CB  1 
ATOM   4812 N N   . ILE E 5 74  ? 253.877 301.358 193.333 1.00 135.53 ? 74   ILE L N   1 
ATOM   4813 C CA  . ILE E 5 74  ? 253.515 300.939 191.988 1.00 140.36 ? 74   ILE L CA  1 
ATOM   4814 C C   . ILE E 5 74  ? 254.687 301.145 191.041 1.00 135.11 ? 74   ILE L C   1 
ATOM   4815 O O   . ILE E 5 74  ? 255.110 302.277 190.805 1.00 135.07 ? 74   ILE L O   1 
ATOM   4816 C CB  . ILE E 5 74  ? 252.291 301.713 191.465 1.00 138.97 ? 74   ILE L CB  1 
ATOM   4817 N N   . SER E 5 75  ? 255.217 300.050 190.509 1.00 140.80 ? 75   SER L N   1 
ATOM   4818 C CA  . SER E 5 75  ? 256.361 300.108 189.607 1.00 141.16 ? 75   SER L CA  1 
ATOM   4819 C C   . SER E 5 75  ? 255.910 300.201 188.159 1.00 140.66 ? 75   SER L C   1 
ATOM   4820 O O   . SER E 5 75  ? 255.188 299.331 187.672 1.00 140.73 ? 75   SER L O   1 
ATOM   4821 C CB  . SER E 5 75  ? 257.237 298.887 189.798 1.00 140.83 ? 75   SER L CB  1 
ATOM   4822 N N   . GLY E 5 76  ? 256.321 301.262 187.470 1.00 140.17 ? 76   GLY L N   1 
ATOM   4823 C CA  . GLY E 5 76  ? 255.892 301.470 186.094 1.00 141.50 ? 76   GLY L CA  1 
ATOM   4824 C C   . GLY E 5 76  ? 254.432 301.896 186.057 1.00 142.36 ? 76   GLY L C   1 
ATOM   4825 O O   . GLY E 5 76  ? 253.627 301.321 185.323 1.00 141.43 ? 76   GLY L O   1 
ATOM   4826 N N   . THR E 5 77  ? 254.084 302.879 186.883 1.00 143.37 ? 77   THR L N   1 
ATOM   4827 C CA  . THR E 5 77  ? 252.698 303.305 187.032 1.00 144.42 ? 77   THR L CA  1 
ATOM   4828 C C   . THR E 5 77  ? 252.066 303.607 185.685 1.00 144.28 ? 77   THR L C   1 
ATOM   4829 O O   . THR E 5 77  ? 252.627 304.339 184.869 1.00 140.24 ? 77   THR L O   1 
ATOM   4830 C CB  . THR E 5 77  ? 252.595 304.553 187.935 1.00 141.03 ? 77   THR L CB  1 
ATOM   4831 N N   . GLN E 5 78  ? 250.893 303.032 185.455 1.00 140.59 ? 78   GLN L N   1 
ATOM   4832 C CA  . GLN E 5 78  ? 250.163 303.232 184.212 1.00 142.55 ? 78   GLN L CA  1 
ATOM   4833 C C   . GLN E 5 78  ? 249.086 304.282 184.400 1.00 141.19 ? 78   GLN L C   1 
ATOM   4834 O O   . GLN E 5 78  ? 248.679 304.563 185.524 1.00 136.48 ? 78   GLN L O   1 
ATOM   4835 C CB  . GLN E 5 78  ? 249.544 301.915 183.741 1.00 144.27 ? 78   GLN L CB  1 
ATOM   4836 N N   . THR E 5 79  ? 248.596 304.845 183.303 1.00 141.05 ? 79   THR L N   1 
ATOM   4837 C CA  . THR E 5 79  ? 247.515 305.819 183.395 1.00 142.21 ? 79   THR L CA  1 
ATOM   4838 C C   . THR E 5 79  ? 246.239 305.139 183.876 1.00 142.58 ? 79   THR L C   1 
ATOM   4839 O O   . THR E 5 79  ? 245.359 305.772 184.459 1.00 139.85 ? 79   THR L O   1 
ATOM   4840 C CB  . THR E 5 79  ? 247.280 306.513 182.044 1.00 139.52 ? 79   THR L CB  1 
ATOM   4841 N N   . MET E 5 80  ? 246.177 303.826 183.692 1.00 144.97 ? 80   MET L N   1 
ATOM   4842 C CA  . MET E 5 80  ? 245.049 303.028 184.149 1.00 141.67 ? 80   MET L CA  1 
ATOM   4843 C C   . MET E 5 80  ? 245.046 302.897 185.670 1.00 142.44 ? 80   MET L C   1 
ATOM   4844 O O   . MET E 5 80  ? 244.047 302.487 186.265 1.00 137.78 ? 80   MET L O   1 
ATOM   4845 C CB  . MET E 5 80  ? 245.083 301.648 183.497 1.00 142.19 ? 80   MET L CB  1 
ATOM   4846 N N   . ASP E 5 81  ? 246.169 303.254 186.296 1.00 137.92 ? 81   ASP L N   1 
ATOM   4847 C CA  . ASP E 5 81  ? 246.322 303.160 187.742 1.00 138.34 ? 81   ASP L CA  1 
ATOM   4848 C C   . ASP E 5 81  ? 245.937 304.476 188.411 1.00 143.22 ? 81   ASP L C   1 
ATOM   4849 O O   . ASP E 5 81  ? 246.085 304.635 189.624 1.00 136.59 ? 81   ASP L O   1 
ATOM   4850 C CB  . ASP E 5 81  ? 247.770 302.810 188.116 1.00 141.91 ? 81   ASP L CB  1 
ATOM   4851 N N   . GLU E 5 82  ? 245.435 305.424 187.625 1.00 138.19 ? 82   GLU L N   1 
ATOM   4852 C CA  . GLU E 5 82  ? 245.054 306.712 188.184 1.00 140.48 ? 82   GLU L CA  1 
ATOM   4853 C C   . GLU E 5 82  ? 243.781 306.553 189.004 1.00 139.07 ? 82   GLU L C   1 
ATOM   4854 O O   . GLU E 5 82  ? 242.672 306.516 188.470 1.00 137.31 ? 82   GLU L O   1 
ATOM   4855 C CB  . GLU E 5 82  ? 244.863 307.749 187.072 1.00 139.70 ? 82   GLU L CB  1 
ATOM   4856 N N   . ALA E 5 83  ? 243.966 306.404 190.310 1.00 136.92 ? 83   ALA L N   1 
ATOM   4857 C CA  . ALA E 5 83  ? 242.887 306.062 191.228 1.00 136.61 ? 83   ALA L CA  1 
ATOM   4858 C C   . ALA E 5 83  ? 243.183 306.571 192.634 1.00 140.40 ? 83   ALA L C   1 
ATOM   4859 O O   . ALA E 5 83  ? 244.320 306.924 192.950 1.00 128.99 ? 83   ALA L O   1 
ATOM   4860 C CB  . ALA E 5 83  ? 242.688 304.556 191.253 1.00 134.43 ? 83   ALA L CB  1 
ATOM   4861 N N   . ASP E 5 84  ? 242.154 306.593 193.475 1.00 137.53 ? 84   ASP L N   1 
ATOM   4862 C CA  . ASP E 5 84  ? 242.309 306.959 194.877 1.00 143.47 ? 84   ASP L CA  1 
ATOM   4863 C C   . ASP E 5 84  ? 242.640 305.726 195.708 1.00 122.74 ? 84   ASP L C   1 
ATOM   4864 O O   . ASP E 5 84  ? 241.893 304.746 195.707 1.00 134.88 ? 84   ASP L O   1 
ATOM   4865 C CB  . ASP E 5 84  ? 241.036 307.623 195.408 1.00 135.08 ? 84   ASP L CB  1 
ATOM   4866 N N   . TYR E 5 85  ? 243.781 305.751 196.384 1.00 135.70 ? 85   TYR L N   1 
ATOM   4867 C CA  . TYR E 5 85  ? 244.211 304.595 197.156 1.00 132.80 ? 85   TYR L CA  1 
ATOM   4868 C C   . TYR E 5 85  ? 243.940 304.775 198.637 1.00 128.44 ? 85   TYR L C   1 
ATOM   4869 O O   . TYR E 5 85  ? 244.193 305.836 199.207 1.00 132.53 ? 85   TYR L O   1 
ATOM   4870 C CB  . TYR E 5 85  ? 245.689 304.310 196.907 1.00 137.84 ? 85   TYR L CB  1 
ATOM   4871 N N   . TYR E 5 86  ? 243.418 303.728 199.259 1.00 135.49 ? 86   TYR L N   1 
ATOM   4872 C CA  . TYR E 5 86  ? 243.074 303.771 200.671 1.00 130.12 ? 86   TYR L CA  1 
ATOM   4873 C C   . TYR E 5 86  ? 243.810 302.695 201.455 1.00 140.89 ? 86   TYR L C   1 
ATOM   4874 O O   . TYR E 5 86  ? 243.985 301.577 200.968 1.00 128.12 ? 86   TYR L O   1 
ATOM   4875 C CB  . TYR E 5 86  ? 241.564 303.586 200.850 1.00 131.03 ? 86   TYR L CB  1 
ATOM   4876 N N   . CYS E 5 87  ? 244.181 303.020 202.695 1.00 134.12 ? 87   CYS L N   1 
ATOM   4877 C CA  . CYS E 5 87  ? 244.755 302.054 203.629 1.00 122.19 ? 87   CYS L CA  1 
ATOM   4878 C C   . CYS E 5 87  ? 243.691 301.583 204.617 1.00 127.46 ? 87   CYS L C   1 
ATOM   4879 O O   . CYS E 5 87  ? 242.804 302.345 205.015 1.00 134.66 ? 87   CYS L O   1 
ATOM   4880 C CB  . CYS E 5 87  ? 245.951 302.659 204.384 1.00 133.83 ? 87   CYS L CB  1 
ATOM   4881 S SG  . CYS E 5 87  ? 245.562 304.124 205.391 1.00 130.65 ? 87   CYS L SG  1 
ATOM   4882 N N   . GLN E 5 88  ? 243.800 300.327 205.032 1.00 128.07 ? 88   GLN L N   1 
ATOM   4883 C CA  . GLN E 5 88  ? 242.874 299.755 206.000 1.00 128.96 ? 88   GLN L CA  1 
ATOM   4884 C C   . GLN E 5 88  ? 243.620 298.946 207.053 1.00 126.40 ? 88   GLN L C   1 
ATOM   4885 O O   . GLN E 5 88  ? 244.610 298.274 206.752 1.00 126.52 ? 88   GLN L O   1 
ATOM   4886 C CB  . GLN E 5 88  ? 241.844 298.874 205.282 1.00 127.77 ? 88   GLN L CB  1 
ATOM   4887 N N   . ALA E 5 89  ? 243.145 299.013 208.292 1.00 126.73 ? 89   ALA L N   1 
ATOM   4888 C CA  . ALA E 5 89  ? 243.736 298.235 209.377 1.00 124.71 ? 89   ALA L CA  1 
ATOM   4889 C C   . ALA E 5 89  ? 242.735 298.049 210.510 1.00 124.92 ? 89   ALA L C   1 
ATOM   4890 O O   . ALA E 5 89  ? 241.796 298.831 210.655 1.00 127.25 ? 89   ALA L O   1 
ATOM   4891 C CB  . ALA E 5 89  ? 244.998 298.912 209.886 1.00 125.13 ? 89   ALA L CB  1 
ATOM   4892 N N   . TRP E 5 90  ? 242.942 297.015 211.318 1.00 122.22 ? 90   TRP L N   1 
ATOM   4893 C CA  . TRP E 5 90  ? 242.066 296.738 212.451 1.00 121.39 ? 90   TRP L CA  1 
ATOM   4894 C C   . TRP E 5 90  ? 242.769 296.974 213.782 1.00 124.11 ? 90   TRP L C   1 
ATOM   4895 O O   . TRP E 5 90  ? 243.972 296.751 213.907 1.00 122.08 ? 90   TRP L O   1 
ATOM   4896 C CB  . TRP E 5 90  ? 241.586 295.288 212.411 1.00 120.73 ? 90   TRP L CB  1 
ATOM   4897 N N   . ASP E 5 91  ? 241.997 297.370 214.788 1.00 121.64 ? 91   ASP L N   1 
ATOM   4898 C CA  . ASP E 5 91  ? 242.497 297.499 216.153 1.00 124.12 ? 91   ASP L CA  1 
ATOM   4899 C C   . ASP E 5 91  ? 241.535 296.828 217.124 1.00 123.00 ? 91   ASP L C   1 
ATOM   4900 O O   . ASP E 5 91  ? 240.431 297.319 217.352 1.00 122.66 ? 91   ASP L O   1 
ATOM   4901 C CB  . ASP E 5 91  ? 242.673 298.970 216.538 1.00 125.90 ? 91   ASP L CB  1 
ATOM   4902 N N   . LYS E 5 92  ? 241.921 295.669 217.643 1.00 122.10 ? 92   LYS L N   1 
ATOM   4903 C CA  . LYS E 5 92  ? 241.043 294.902 218.522 1.00 121.35 ? 92   LYS L CA  1 
ATOM   4904 C C   . LYS E 5 92  ? 239.687 294.657 217.873 1.00 121.69 ? 92   LYS L C   1 
ATOM   4905 O O   . LYS E 5 92  ? 238.650 294.826 218.510 1.00 121.32 ? 92   LYS L O   1 
ATOM   4906 C CB  . LYS E 5 92  ? 240.864 295.609 219.868 1.00 122.33 ? 92   LYS L CB  1 
ATOM   4907 N N   . THR E 5 93  ? 239.725 294.256 216.600 1.00 119.51 ? 93   THR L N   1 
ATOM   4908 C CA  . THR E 5 93  ? 238.569 293.914 215.755 1.00 120.09 ? 93   THR L CA  1 
ATOM   4909 C C   . THR E 5 93  ? 237.756 295.132 215.311 1.00 122.41 ? 93   THR L C   1 
ATOM   4910 O O   . THR E 5 93  ? 236.765 294.987 214.595 1.00 122.28 ? 93   THR L O   1 
ATOM   4911 C CB  . THR E 5 93  ? 237.616 292.871 216.401 1.00 119.01 ? 93   THR L CB  1 
ATOM   4912 N N   . ILE E 5 94  ? 238.191 296.331 215.692 1.00 120.45 ? 94   ILE L N   1 
ATOM   4913 C CA  . ILE E 5 94  ? 237.542 297.551 215.223 1.00 122.44 ? 94   ILE L CA  1 
ATOM   4914 C C   . ILE E 5 94  ? 238.174 298.023 213.917 1.00 127.09 ? 94   ILE L C   1 
ATOM   4915 O O   . ILE E 5 94  ? 239.394 298.138 213.809 1.00 128.32 ? 94   ILE L O   1 
ATOM   4916 C CB  . ILE E 5 94  ? 237.624 298.670 216.281 1.00 123.16 ? 94   ILE L CB  1 
ATOM   4917 N N   . ALA E 5 95  ? 237.334 298.266 212.918 1.00 125.05 ? 95   ALA L N   1 
ATOM   4918 C CA  . ALA E 5 95  ? 237.792 298.670 211.593 1.00 124.80 ? 95   ALA L CA  1 
ATOM   4919 C C   . ALA E 5 95  ? 238.218 300.128 211.562 1.00 126.36 ? 95   ALA L C   1 
ATOM   4920 O O   . ALA E 5 95  ? 237.886 300.907 212.456 1.00 126.98 ? 95   ALA L O   1 
ATOM   4921 C CB  . ALA E 5 95  ? 236.697 298.457 210.564 1.00 125.48 ? 95   ALA L CB  1 
ATOM   4922 N N   . GLY E 5 96  ? 238.913 300.498 210.494 1.00 127.15 ? 96   GLY L N   1 
ATOM   4923 C CA  . GLY E 5 96  ? 239.268 301.884 210.237 1.00 130.30 ? 96   GLY L CA  1 
ATOM   4924 C C   . GLY E 5 96  ? 239.891 302.026 208.857 1.00 129.61 ? 96   GLY L C   1 
ATOM   4925 O O   . GLY E 5 96  ? 240.599 301.134 208.384 1.00 130.43 ? 96   GLY L O   1 
ATOM   4926 N N   . PHE E 5 97  ? 239.630 303.163 208.221 1.00 131.01 ? 97   PHE L N   1 
ATOM   4927 C CA  . PHE E 5 97  ? 240.161 303.467 206.897 1.00 129.96 ? 97   PHE L CA  1 
ATOM   4928 C C   . PHE E 5 97  ? 240.853 304.822 206.901 1.00 130.42 ? 97   PHE L C   1 
ATOM   4929 O O   . PHE E 5 97  ? 240.466 305.721 207.649 1.00 132.13 ? 97   PHE L O   1 
ATOM   4930 C CB  . PHE E 5 97  ? 239.043 303.486 205.849 1.00 130.13 ? 97   PHE L CB  1 
ATOM   4931 N N   . GLY E 5 98  ? 241.849 304.981 206.038 1.00 136.26 ? 98   GLY L N   1 
ATOM   4932 C CA  . GLY E 5 98  ? 242.527 306.263 205.900 1.00 133.20 ? 98   GLY L CA  1 
ATOM   4933 C C   . GLY E 5 98  ? 241.703 307.231 205.060 1.00 129.93 ? 98   GLY L C   1 
ATOM   4934 O O   . GLY E 5 98  ? 240.669 306.861 204.500 1.00 128.44 ? 98   GLY L O   1 
ATOM   4935 N N   . GLY E 5 99  ? 242.167 308.476 204.975 1.00 131.28 ? 99   GLY L N   1 
ATOM   4936 C CA  . GLY E 5 99  ? 241.462 309.519 204.232 1.00 129.87 ? 99   GLY L CA  1 
ATOM   4937 C C   . GLY E 5 99  ? 241.402 309.237 202.734 1.00 129.77 ? 99   GLY L C   1 
ATOM   4938 O O   . GLY E 5 99  ? 240.436 309.602 202.065 1.00 131.24 ? 99   GLY L O   1 
ATOM   4939 N N   . GLY E 5 100 ? 242.448 308.610 202.209 1.00 131.54 ? 100  GLY L N   1 
ATOM   4940 C CA  . GLY E 5 100 ? 242.531 308.309 200.786 1.00 131.94 ? 100  GLY L CA  1 
ATOM   4941 C C   . GLY E 5 100 ? 243.508 309.237 200.078 1.00 133.52 ? 100  GLY L C   1 
ATOM   4942 O O   . GLY E 5 100 ? 243.476 310.453 200.272 1.00 134.56 ? 100  GLY L O   1 
ATOM   4943 N N   . THR E 5 101 ? 244.370 308.658 199.251 1.00 136.07 ? 101  THR L N   1 
ATOM   4944 C CA  . THR E 5 101 ? 245.378 309.416 198.526 1.00 137.43 ? 101  THR L CA  1 
ATOM   4945 C C   . THR E 5 101 ? 245.076 309.421 197.037 1.00 131.03 ? 101  THR L C   1 
ATOM   4946 O O   . THR E 5 101 ? 245.008 308.363 196.409 1.00 131.23 ? 101  THR L O   1 
ATOM   4947 C CB  . THR E 5 101 ? 246.778 308.809 198.743 1.00 137.86 ? 101  THR L CB  1 
ATOM   4948 N N   . LYS E 5 102 ? 244.929 310.604 196.456 1.00 139.23 ? 102  LYS L N   1 
ATOM   4949 C CA  . LYS E 5 102 ? 244.664 310.691 195.027 1.00 133.90 ? 102  LYS L CA  1 
ATOM   4950 C C   . LYS E 5 102 ? 245.953 310.566 194.233 1.00 142.06 ? 102  LYS L C   1 
ATOM   4951 O O   . LYS E 5 102 ? 246.836 311.417 194.341 1.00 135.61 ? 102  LYS L O   1 
ATOM   4952 C CB  . LYS E 5 102 ? 243.976 312.014 194.686 1.00 137.50 ? 102  LYS L CB  1 
ATOM   4953 N N   . LEU E 5 103 ? 246.056 309.521 193.420 1.00 137.03 ? 103  LEU L N   1 
ATOM   4954 C CA  . LEU E 5 103 ? 247.239 309.337 192.593 1.00 145.63 ? 103  LEU L CA  1 
ATOM   4955 C C   . LEU E 5 103 ? 246.985 309.880 191.198 1.00 140.71 ? 103  LEU L C   1 
ATOM   4956 O O   . LEU E 5 103 ? 246.114 309.386 190.485 1.00 135.36 ? 103  LEU L O   1 
ATOM   4957 C CB  . LEU E 5 103 ? 247.620 307.852 192.501 1.00 138.05 ? 103  LEU L CB  1 
ATOM   4958 N N   . THR E 5 104 ? 247.752 310.887 190.815 1.00 139.16 ? 104  THR L N   1 
ATOM   4959 C CA  . THR E 5 104 ? 247.623 311.504 189.503 1.00 139.77 ? 104  THR L CA  1 
ATOM   4960 C C   . THR E 5 104 ? 248.761 311.018 188.616 1.00 144.81 ? 104  THR L C   1 
ATOM   4961 O O   . THR E 5 104 ? 249.922 311.072 189.028 1.00 136.92 ? 104  THR L O   1 
ATOM   4962 C CB  . THR E 5 104 ? 247.653 313.043 189.611 1.00 142.07 ? 104  THR L CB  1 
ATOM   4963 N N   . VAL E 5 105 ? 248.431 310.514 187.417 1.00 139.93 ? 105  VAL L N   1 
ATOM   4964 C CA  . VAL E 5 105 ? 249.428 309.928 186.516 1.00 141.99 ? 105  VAL L CA  1 
ATOM   4965 C C   . VAL E 5 105 ? 249.515 310.748 185.227 1.00 140.85 ? 105  VAL L C   1 
ATOM   4966 O O   . VAL E 5 105 ? 248.702 310.594 184.312 1.00 138.46 ? 105  VAL L O   1 
ATOM   4967 C CB  . VAL E 5 105 ? 249.087 308.433 186.200 1.00 140.89 ? 105  VAL L CB  1 
HETATM 4968 C C1  . NAG F 6 .   ? 237.633 272.318 205.811 1.00 32.25  ? 1    NAG D C1  1 
HETATM 4969 C C2  . NAG F 6 .   ? 237.884 273.261 204.581 1.00 34.34  ? 1    NAG D C2  1 
HETATM 4970 C C3  . NAG F 6 .   ? 236.533 273.628 203.931 1.00 35.17  ? 1    NAG D C3  1 
HETATM 4971 C C4  . NAG F 6 .   ? 235.845 272.321 203.492 1.00 35.33  ? 1    NAG D C4  1 
HETATM 4972 C C5  . NAG F 6 .   ? 235.641 271.428 204.740 1.00 32.56  ? 1    NAG D C5  1 
HETATM 4973 C C6  . NAG F 6 .   ? 234.958 270.112 204.396 1.00 31.56  ? 1    NAG D C6  1 
HETATM 4974 C C7  . NAG F 6 .   ? 238.181 275.326 205.887 1.00 37.35  ? 1    NAG D C7  1 
HETATM 4975 C C8  . NAG F 6 .   ? 238.987 276.528 206.273 1.00 43.64  ? 1    NAG D C8  1 
HETATM 4976 N N2  . NAG F 6 .   ? 238.640 274.459 204.984 1.00 34.86  ? 1    NAG D N2  1 
HETATM 4977 O O3  . NAG F 6 .   ? 236.759 274.481 202.795 1.00 38.20  ? 1    NAG D O3  1 
HETATM 4978 O O4  . NAG F 6 .   ? 234.567 272.618 202.909 1.00 37.48  ? 1    NAG D O4  1 
HETATM 4979 O O5  . NAG F 6 .   ? 236.936 271.129 205.364 1.00 29.61  ? 1    NAG D O5  1 
HETATM 4980 O O6  . NAG F 6 .   ? 235.637 269.419 203.361 1.00 29.51  ? 1    NAG D O6  1 
HETATM 4981 O O7  . NAG F 6 .   ? 237.083 275.147 206.417 1.00 38.19  ? 1    NAG D O7  1 
HETATM 4982 C C1  . NAG F 6 .   ? 234.433 272.078 201.512 1.00 37.50  ? 2    NAG D C1  1 
HETATM 4983 C C2  . NAG F 6 .   ? 232.930 272.087 201.100 1.00 38.82  ? 2    NAG D C2  1 
HETATM 4984 C C3  . NAG F 6 .   ? 232.832 271.485 199.677 1.00 40.24  ? 2    NAG D C3  1 
HETATM 4985 C C4  . NAG F 6 .   ? 233.701 272.313 198.702 1.00 40.80  ? 2    NAG D C4  1 
HETATM 4986 C C5  . NAG F 6 .   ? 235.161 272.297 199.218 1.00 39.90  ? 2    NAG D C5  1 
HETATM 4987 C C6  . NAG F 6 .   ? 236.072 273.155 198.350 1.00 40.55  ? 2    NAG D C6  1 
HETATM 4988 C C7  . NAG F 6 .   ? 231.482 271.790 203.027 1.00 37.60  ? 2    NAG D C7  1 
HETATM 4989 C C8  . NAG F 6 .   ? 230.712 270.925 203.975 1.00 36.45  ? 2    NAG D C8  1 
HETATM 4990 N N2  . NAG F 6 .   ? 232.168 271.243 202.028 1.00 38.08  ? 2    NAG D N2  1 
HETATM 4991 O O3  . NAG F 6 .   ? 231.460 271.501 199.253 1.00 40.79  ? 2    NAG D O3  1 
HETATM 4992 O O4  . NAG F 6 .   ? 233.669 271.697 197.403 1.00 42.01  ? 2    NAG D O4  1 
HETATM 4993 O O5  . NAG F 6 .   ? 235.227 272.834 200.581 1.00 38.20  ? 2    NAG D O5  1 
HETATM 4994 O O6  . NAG F 6 .   ? 237.444 272.911 198.645 1.00 39.70  ? 2    NAG D O6  1 
HETATM 4995 O O7  . NAG F 6 .   ? 231.483 273.016 203.183 1.00 44.61  ? 2    NAG D O7  1 
HETATM 4996 C C1  . BMA F 6 .   ? 233.051 272.572 196.356 1.00 43.04  ? 3    BMA D C1  1 
HETATM 4997 C C2  . BMA F 6 .   ? 233.368 271.971 194.949 1.00 43.92  ? 3    BMA D C2  1 
HETATM 4998 C C3  . BMA F 6 .   ? 232.740 272.902 193.887 1.00 44.84  ? 3    BMA D C3  1 
HETATM 4999 C C4  . BMA F 6 .   ? 231.221 273.008 194.139 1.00 45.57  ? 3    BMA D C4  1 
HETATM 5000 C C5  . BMA F 6 .   ? 231.004 273.592 195.561 1.00 44.69  ? 3    BMA D C5  1 
HETATM 5001 C C6  . BMA F 6 .   ? 229.531 273.735 195.900 1.00 45.16  ? 3    BMA D C6  1 
HETATM 5002 O O2  . BMA F 6 .   ? 232.853 270.646 194.837 1.00 44.31  ? 3    BMA D O2  1 
HETATM 5003 O O3  . BMA F 6 .   ? 232.998 272.403 192.573 1.00 44.13  ? 3    BMA D O3  1 
HETATM 5004 O O4  . BMA F 6 .   ? 230.646 273.859 193.147 1.00 46.90  ? 3    BMA D O4  1 
HETATM 5005 O O5  . BMA F 6 .   ? 231.632 272.715 196.553 1.00 43.60  ? 3    BMA D O5  1 
HETATM 5006 O O6  . BMA F 6 .   ? 229.018 274.980 195.436 1.00 45.73  ? 3    BMA D O6  1 
HETATM 5007 C C1  . NAG G 7 .   ? 242.572 241.604 204.372 1.00 13.69  ? 1    NAG E C1  1 
HETATM 5008 C C2  . NAG G 7 .   ? 242.754 241.068 202.910 1.00 14.50  ? 1    NAG E C2  1 
HETATM 5009 C C3  . NAG G 7 .   ? 242.123 239.663 202.834 1.00 14.77  ? 1    NAG E C3  1 
HETATM 5010 C C4  . NAG G 7 .   ? 242.821 238.738 203.854 1.00 15.83  ? 1    NAG E C4  1 
HETATM 5011 C C5  . NAG G 7 .   ? 242.642 239.351 205.267 1.00 15.66  ? 1    NAG E C5  1 
HETATM 5012 C C6  . NAG G 7 .   ? 243.328 238.525 206.346 1.00 15.79  ? 1    NAG E C6  1 
HETATM 5013 C C7  . NAG G 7 .   ? 242.699 242.511 200.954 1.00 14.73  ? 1    NAG E C7  1 
HETATM 5014 C C8  . NAG G 7 .   ? 241.979 243.425 200.012 1.00 14.13  ? 1    NAG E C8  1 
HETATM 5015 N N2  . NAG G 7 .   ? 242.055 241.961 201.982 1.00 14.79  ? 1    NAG E N2  1 
HETATM 5016 O O3  . NAG G 7 .   ? 242.276 239.146 201.503 1.00 14.88  ? 1    NAG E O3  1 
HETATM 5017 O O4  . NAG G 7 .   ? 242.198 237.444 203.820 1.00 15.60  ? 1    NAG E O4  1 
HETATM 5018 O O5  . NAG G 7 .   ? 243.212 240.702 205.300 1.00 14.18  ? 1    NAG E O5  1 
HETATM 5019 O O6  . NAG G 7 .   ? 242.828 238.854 207.635 1.00 17.22  ? 1    NAG E O6  1 
HETATM 5020 O O7  . NAG G 7 .   ? 243.898 242.273 200.774 1.00 14.16  ? 1    NAG E O7  1 
HETATM 5021 C C1  . NAG G 7 .   ? 243.097 236.354 203.308 1.00 16.31  ? 2    NAG E C1  1 
HETATM 5022 C C2  . NAG G 7 .   ? 242.518 234.977 203.763 1.00 17.45  ? 2    NAG E C2  1 
HETATM 5023 C C3  . NAG G 7 .   ? 243.465 233.864 203.251 1.00 16.73  ? 2    NAG E C3  1 
HETATM 5024 C C4  . NAG G 7 .   ? 243.557 233.961 201.714 1.00 16.95  ? 2    NAG E C4  1 
HETATM 5025 C C5  . NAG G 7 .   ? 244.100 235.357 201.331 1.00 15.97  ? 2    NAG E C5  1 
HETATM 5026 C C6  . NAG G 7 .   ? 244.168 235.527 199.821 1.00 16.11  ? 2    NAG E C6  1 
HETATM 5027 C C7  . NAG G 7 .   ? 241.313 235.031 205.870 1.00 17.96  ? 2    NAG E C7  1 
HETATM 5028 C C8  . NAG G 7 .   ? 241.273 234.973 207.365 1.00 17.66  ? 2    NAG E C8  1 
HETATM 5029 N N2  . NAG G 7 .   ? 242.473 234.924 205.227 1.00 17.31  ? 2    NAG E N2  1 
HETATM 5030 O O3  . NAG G 7 .   ? 242.939 232.586 203.627 1.00 17.35  ? 2    NAG E O3  1 
HETATM 5031 O O4  . NAG G 7 .   ? 244.429 232.943 201.233 1.00 16.76  ? 2    NAG E O4  1 
HETATM 5032 O O5  . NAG G 7 .   ? 243.219 236.400 201.870 1.00 16.00  ? 2    NAG E O5  1 
HETATM 5033 O O6  . NAG G 7 .   ? 242.905 235.307 199.201 1.00 17.31  ? 2    NAG E O6  1 
HETATM 5034 O O7  . NAG G 7 .   ? 240.260 235.172 205.236 1.00 18.30  ? 2    NAG E O7  1 
HETATM 5035 C C1  . NAG H 7 .   ? 256.868 248.429 232.569 1.00 9.64   ? 1    NAG F C1  1 
HETATM 5036 C C2  . NAG H 7 .   ? 256.674 246.975 233.126 1.00 10.20  ? 1    NAG F C2  1 
HETATM 5037 C C3  . NAG H 7 .   ? 257.379 246.883 234.498 1.00 10.77  ? 1    NAG F C3  1 
HETATM 5038 C C4  . NAG H 7 .   ? 258.879 247.207 234.322 1.00 11.58  ? 1    NAG F C4  1 
HETATM 5039 C C5  . NAG H 7 .   ? 259.004 248.626 233.709 1.00 11.41  ? 1    NAG F C5  1 
HETATM 5040 C C6  . NAG H 7 .   ? 260.453 248.988 233.438 1.00 12.05  ? 1    NAG F C6  1 
HETATM 5041 C C7  . NAG H 7 .   ? 254.577 246.018 232.373 1.00 8.92   ? 1    NAG F C7  1 
HETATM 5042 C C8  . NAG H 7 .   ? 253.117 245.738 232.549 1.00 7.67   ? 1    NAG F C8  1 
HETATM 5043 N N2  . NAG H 7 .   ? 255.246 246.700 233.296 1.00 9.33   ? 1    NAG F N2  1 
HETATM 5044 O O3  . NAG H 7 .   ? 257.222 245.558 235.024 1.00 11.01  ? 1    NAG F O3  1 
HETATM 5045 O O4  . NAG H 7 .   ? 259.518 247.201 235.613 1.00 12.03  ? 1    NAG F O4  1 
HETATM 5046 O O5  . NAG H 7 .   ? 258.282 248.701 232.435 1.00 10.43  ? 1    NAG F O5  1 
HETATM 5047 O O6  . NAG H 7 .   ? 260.571 250.337 233.012 1.00 12.03  ? 1    NAG F O6  1 
HETATM 5048 O O7  . NAG H 7 .   ? 255.159 245.606 231.362 1.00 9.12   ? 1    NAG F O7  1 
HETATM 5049 C C1  . NAG H 7 .   ? 260.620 246.184 235.724 1.00 12.82  ? 2    NAG F C1  1 
HETATM 5050 C C2  . NAG H 7 .   ? 261.431 246.427 237.040 1.00 13.60  ? 2    NAG F C2  1 
HETATM 5051 C C3  . NAG H 7 .   ? 262.570 245.377 237.096 1.00 13.72  ? 2    NAG F C3  1 
HETATM 5052 C C4  . NAG H 7 .   ? 261.952 243.966 237.054 1.00 13.87  ? 2    NAG F C4  1 
HETATM 5053 C C5  . NAG H 7 .   ? 261.142 243.818 235.749 1.00 13.04  ? 2    NAG F C5  1 
HETATM 5054 C C6  . NAG H 7 .   ? 260.478 242.458 235.660 1.00 11.96  ? 2    NAG F C6  1 
HETATM 5055 C C7  . NAG H 7 .   ? 261.516 248.752 237.755 1.00 13.78  ? 2    NAG F C7  1 
HETATM 5056 C C8  . NAG H 7 .   ? 262.139 250.115 237.727 1.00 15.18  ? 2    NAG F C8  1 
HETATM 5057 N N2  . NAG H 7 .   ? 262.030 247.767 237.018 1.00 13.45  ? 2    NAG F N2  1 
HETATM 5058 O O3  . NAG H 7 .   ? 263.321 245.538 238.305 1.00 14.15  ? 2    NAG F O3  1 
HETATM 5059 O O4  . NAG H 7 .   ? 262.998 242.998 237.102 1.00 15.44  ? 2    NAG F O4  1 
HETATM 5060 O O5  . NAG H 7 .   ? 260.094 244.840 235.692 1.00 13.04  ? 2    NAG F O5  1 
HETATM 5061 O O6  . NAG H 7 .   ? 259.569 242.236 236.733 1.00 12.00  ? 2    NAG F O6  1 
HETATM 5062 O O7  . NAG H 7 .   ? 260.530 248.543 238.471 1.00 12.99  ? 2    NAG F O7  1 
HETATM 5063 C C1  . NAG I 8 .   ? 222.523 261.517 238.530 1.00 21.87  ? 1301 NAG A C1  1 
HETATM 5064 C C2  . NAG I 8 .   ? 223.589 261.690 239.665 1.00 22.63  ? 1301 NAG A C2  1 
HETATM 5065 C C3  . NAG I 8 .   ? 223.008 262.623 240.746 1.00 22.95  ? 1301 NAG A C3  1 
HETATM 5066 C C4  . NAG I 8 .   ? 222.654 263.977 240.098 1.00 24.00  ? 1301 NAG A C4  1 
HETATM 5067 C C5  . NAG I 8 .   ? 221.633 263.738 238.959 1.00 23.55  ? 1301 NAG A C5  1 
HETATM 5068 C C6  . NAG I 8 .   ? 221.284 265.033 238.246 1.00 25.22  ? 1301 NAG A C6  1 
HETATM 5069 C C7  . NAG I 8 .   ? 225.049 259.795 240.098 1.00 20.03  ? 1301 NAG A C7  1 
HETATM 5070 C C8  . NAG I 8 .   ? 225.314 258.448 240.697 1.00 18.83  ? 1301 NAG A C8  1 
HETATM 5071 N N2  . NAG I 8 .   ? 223.863 260.371 240.252 1.00 22.63  ? 1301 NAG A N2  1 
HETATM 5072 O O3  . NAG I 8 .   ? 223.977 262.819 241.784 1.00 23.97  ? 1301 NAG A O3  1 
HETATM 5073 O O4  . NAG I 8 .   ? 222.095 264.836 241.088 1.00 24.52  ? 1301 NAG A O4  1 
HETATM 5074 O O5  . NAG I 8 .   ? 222.198 262.812 237.970 1.00 22.78  ? 1301 NAG A O5  1 
HETATM 5075 O O6  . NAG I 8 .   ? 220.107 264.888 237.465 1.00 26.37  ? 1301 NAG A O6  1 
HETATM 5076 O O7  . NAG I 8 .   ? 225.944 260.370 239.462 1.00 21.63  ? 1301 NAG A O7  1 
HETATM 5077 C C1  . NAG J 8 .   ? 241.706 252.729 189.625 1.00 16.21  ? 1302 NAG A C1  1 
HETATM 5078 C C2  . NAG J 8 .   ? 241.038 251.595 188.770 1.00 17.16  ? 1302 NAG A C2  1 
HETATM 5079 C C3  . NAG J 8 .   ? 241.909 251.368 187.514 1.00 17.51  ? 1302 NAG A C3  1 
HETATM 5080 C C4  . NAG J 8 .   ? 242.001 252.688 186.724 1.00 17.71  ? 1302 NAG A C4  1 
HETATM 5081 C C5  . NAG J 8 .   ? 242.611 253.780 187.633 1.00 17.19  ? 1302 NAG A C5  1 
HETATM 5082 C C6  . NAG J 8 .   ? 242.665 255.122 186.923 1.00 17.34  ? 1302 NAG A C6  1 
HETATM 5083 C C7  . NAG J 8 .   ? 239.897 250.023 190.225 1.00 17.63  ? 1302 NAG A C7  1 
HETATM 5084 C C8  . NAG J 8 .   ? 239.853 248.756 191.022 1.00 18.36  ? 1302 NAG A C8  1 
HETATM 5085 N N2  . NAG J 8 .   ? 240.992 250.354 189.551 1.00 17.38  ? 1302 NAG A N2  1 
HETATM 5086 O O3  . NAG J 8 .   ? 241.320 250.349 186.702 1.00 17.55  ? 1302 NAG A O3  1 
HETATM 5087 O O4  . NAG J 8 .   ? 242.823 252.490 185.580 1.00 18.37  ? 1302 NAG A O4  1 
HETATM 5088 O O5  . NAG J 8 .   ? 241.797 253.942 188.838 1.00 16.42  ? 1302 NAG A O5  1 
HETATM 5089 O O6  . NAG J 8 .   ? 243.530 256.029 187.596 1.00 16.50  ? 1302 NAG A O6  1 
HETATM 5090 O O7  . NAG J 8 .   ? 238.901 250.760 190.196 1.00 16.91  ? 1302 NAG A O7  1 
HETATM 5091 C C1  . NAG K 8 .   ? 255.249 285.915 219.986 1.00 86.14  ? 1303 NAG A C1  1 
HETATM 5092 C C2  . NAG K 8 .   ? 255.384 287.199 220.876 1.00 86.06  ? 1303 NAG A C2  1 
HETATM 5093 C C3  . NAG K 8 .   ? 256.722 287.893 220.543 1.00 87.87  ? 1303 NAG A C3  1 
HETATM 5094 C C4  . NAG K 8 .   ? 257.873 286.906 220.813 1.00 88.04  ? 1303 NAG A C4  1 
HETATM 5095 C C5  . NAG K 8 .   ? 257.668 285.645 219.942 1.00 87.64  ? 1303 NAG A C5  1 
HETATM 5096 C C6  . NAG K 8 .   ? 258.748 284.608 220.203 1.00 87.70  ? 1303 NAG A C6  1 
HETATM 5097 C C7  . NAG K 8 .   ? 253.199 288.153 221.349 1.00 85.46  ? 1303 NAG A C7  1 
HETATM 5098 C C8  . NAG K 8 .   ? 252.070 289.090 221.044 1.00 85.20  ? 1303 NAG A C8  1 
HETATM 5099 N N2  . NAG K 8 .   ? 254.279 288.118 220.575 1.00 85.45  ? 1303 NAG A N2  1 
HETATM 5100 O O3  . NAG K 8 .   ? 256.875 289.056 221.363 1.00 88.25  ? 1303 NAG A O3  1 
HETATM 5101 O O4  . NAG K 8 .   ? 259.110 287.533 220.493 1.00 89.50  ? 1303 NAG A O4  1 
HETATM 5102 O O5  . NAG K 8 .   ? 256.369 285.033 220.244 1.00 86.20  ? 1303 NAG A O5  1 
HETATM 5103 O O6  . NAG K 8 .   ? 258.790 283.632 219.170 1.00 86.17  ? 1303 NAG A O6  1 
HETATM 5104 O O7  . NAG K 8 .   ? 253.118 287.409 222.336 1.00 85.57  ? 1303 NAG A O7  1 
HETATM 5105 C C1  . NAG L 8 .   ? 262.504 263.865 197.962 1.00 30.37  ? 1304 NAG A C1  1 
HETATM 5106 C C2  . NAG L 8 .   ? 261.838 264.418 196.646 1.00 30.49  ? 1304 NAG A C2  1 
HETATM 5107 C C3  . NAG L 8 .   ? 261.648 263.240 195.669 1.00 30.53  ? 1304 NAG A C3  1 
HETATM 5108 C C4  . NAG L 8 .   ? 263.022 262.600 195.383 1.00 30.83  ? 1304 NAG A C4  1 
HETATM 5109 C C5  . NAG L 8 .   ? 263.642 262.115 196.716 1.00 31.30  ? 1304 NAG A C5  1 
HETATM 5110 C C6  . NAG L 8 .   ? 265.025 261.525 196.496 1.00 30.97  ? 1304 NAG A C6  1 
HETATM 5111 C C7  . NAG L 8 .   ? 260.380 266.294 197.145 1.00 29.40  ? 1304 NAG A C7  1 
HETATM 5112 C C8  . NAG L 8 .   ? 259.043 266.871 197.490 1.00 27.52  ? 1304 NAG A C8  1 
HETATM 5113 N N2  . NAG L 8 .   ? 260.526 264.984 196.981 1.00 30.32  ? 1304 NAG A N2  1 
HETATM 5114 O O3  . NAG L 8 .   ? 261.073 263.723 194.448 1.00 30.32  ? 1304 NAG A O3  1 
HETATM 5115 O O4  . NAG L 8 .   ? 262.850 261.502 194.492 1.00 30.13  ? 1304 NAG A O4  1 
HETATM 5116 O O5  . NAG L 8 .   ? 263.772 263.247 197.641 1.00 31.06  ? 1304 NAG A O5  1 
HETATM 5117 O O6  . NAG L 8 .   ? 265.466 260.805 197.638 1.00 32.03  ? 1304 NAG A O6  1 
HETATM 5118 O O7  . NAG L 8 .   ? 261.358 267.047 197.035 1.00 30.09  ? 1304 NAG A O7  1 
HETATM 5119 C C1  . NAG M 8 .   ? 260.088 278.199 204.001 1.00 31.24  ? 1305 NAG A C1  1 
HETATM 5120 C C2  . NAG M 8 .   ? 259.766 278.428 202.484 1.00 31.79  ? 1305 NAG A C2  1 
HETATM 5121 C C3  . NAG M 8 .   ? 261.085 278.333 201.688 1.00 31.30  ? 1305 NAG A C3  1 
HETATM 5122 C C4  . NAG M 8 .   ? 262.070 279.396 202.219 1.00 31.94  ? 1305 NAG A C4  1 
HETATM 5123 C C5  . NAG M 8 .   ? 262.310 279.146 203.726 1.00 31.80  ? 1305 NAG A C5  1 
HETATM 5124 C C6  . NAG M 8 .   ? 263.223 280.197 204.333 1.00 31.69  ? 1305 NAG A C6  1 
HETATM 5125 C C7  . NAG M 8 .   ? 257.572 277.656 201.781 1.00 30.57  ? 1305 NAG A C7  1 
HETATM 5126 C C8  . NAG M 8 .   ? 256.638 276.583 201.315 1.00 31.47  ? 1305 NAG A C8  1 
HETATM 5127 N N2  . NAG M 8 .   ? 258.848 277.378 202.029 1.00 31.12  ? 1305 NAG A N2  1 
HETATM 5128 O O3  . NAG M 8 .   ? 260.822 278.560 200.299 1.00 31.39  ? 1305 NAG A O3  1 
HETATM 5129 O O4  . NAG M 8 .   ? 263.297 279.297 201.505 1.00 31.97  ? 1305 NAG A O4  1 
HETATM 5130 O O5  . NAG M 8 .   ? 261.037 279.193 204.450 1.00 30.91  ? 1305 NAG A O5  1 
HETATM 5131 O O6  . NAG M 8 .   ? 262.711 281.511 204.145 1.00 31.81  ? 1305 NAG A O6  1 
HETATM 5132 O O7  . NAG M 8 .   ? 257.144 278.807 201.934 1.00 31.22  ? 1305 NAG A O7  1 
# 
