data_7HUV
# 
_entry.id   7HUV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7HUV         pdb_00007huv 10.2210/pdb7huv/pdb 
WWPDB D_1001407960 ?            ?                   
# 
_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       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_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.entry_id                        7HUV 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
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 'Protease 2A'                                                                                    15892.732 1   
3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-[(4S)-4,5,6,7-tetrahydro-1H-pyrazolo[3,4-b]pyridine-4-carbonyl]piperidine-3-carboxamide' 277.322   1   ? 
? ? ? 
3 non-polymer syn 'ZINC ION'                                                                                       65.409    1   ? 
? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                             78.133    1   ? 
? ? ? 
5 water       nat water                                                                                            18.015    105 ? 
? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S)-1-[(4S)-4,5,6,7-tetrahydro-1H-pyrazolo[3,4-b]pyridine-4-carbonyl]piperidine-3-carboxamide' A1BSS 
3 'ZINC ION'                                                                                       ZN    
4 'DIMETHYL SULFOXIDE'                                                                             DMS   
5 water                                                                                            HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   144 
_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      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_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 
A1BSS non-polymer         . '(3S)-1-[(4S)-4,5,6,7-tetrahydro-1H-pyrazolo[3,4-b]pyridine-4-carbonyl]piperidine-3-carboxamide' ? 
'C13 H19 N5 O2'  277.322 
ALA   'L-peptide linking' y ALANINE                                                                                          ? 
'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                                         ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                       ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                  ? 
'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                         ? 
'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                                             ? 
'C2 H6 O S'      78.133  
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 
HOH   non-polymer         . WATER                                                                                            ? 
'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                       ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                          ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                           ? 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                                       ? 
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                    ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                          ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                           ? 
'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                                        ? 
'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                       ? 
'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                         ? 
'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                                           ? 
'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                                                       ? 
'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BSS 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BSS 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1BSS 1   201 201 A1BSS LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 6   DMS   DMS A . 
E 5 HOH   1   301 76  HOH   HOH A . 
E 5 HOH   2   302 9   HOH   HOH A . 
E 5 HOH   3   303 89  HOH   HOH A . 
E 5 HOH   4   304 90  HOH   HOH A . 
E 5 HOH   5   305 15  HOH   HOH A . 
E 5 HOH   6   306 24  HOH   HOH A . 
E 5 HOH   7   307 96  HOH   HOH A . 
E 5 HOH   8   308 101 HOH   HOH A . 
E 5 HOH   9   309 38  HOH   HOH A . 
E 5 HOH   10  310 92  HOH   HOH A . 
E 5 HOH   11  311 62  HOH   HOH A . 
E 5 HOH   12  312 106 HOH   HOH A . 
E 5 HOH   13  313 68  HOH   HOH A . 
E 5 HOH   14  314 27  HOH   HOH A . 
E 5 HOH   15  315 11  HOH   HOH A . 
E 5 HOH   16  316 105 HOH   HOH A . 
E 5 HOH   17  317 40  HOH   HOH A . 
E 5 HOH   18  318 1   HOH   HOH A . 
E 5 HOH   19  319 4   HOH   HOH A . 
E 5 HOH   20  320 94  HOH   HOH A . 
E 5 HOH   21  321 77  HOH   HOH A . 
E 5 HOH   22  322 86  HOH   HOH A . 
E 5 HOH   23  323 66  HOH   HOH A . 
E 5 HOH   24  324 72  HOH   HOH A . 
E 5 HOH   25  325 60  HOH   HOH A . 
E 5 HOH   26  326 69  HOH   HOH A . 
E 5 HOH   27  327 44  HOH   HOH A . 
E 5 HOH   28  328 103 HOH   HOH A . 
E 5 HOH   29  329 45  HOH   HOH A . 
E 5 HOH   30  330 75  HOH   HOH A . 
E 5 HOH   31  331 83  HOH   HOH A . 
E 5 HOH   32  332 16  HOH   HOH A . 
E 5 HOH   33  333 26  HOH   HOH A . 
E 5 HOH   34  334 37  HOH   HOH A . 
E 5 HOH   35  335 3   HOH   HOH A . 
E 5 HOH   36  336 100 HOH   HOH A . 
E 5 HOH   37  337 28  HOH   HOH A . 
E 5 HOH   38  338 57  HOH   HOH A . 
E 5 HOH   39  339 41  HOH   HOH A . 
E 5 HOH   40  340 18  HOH   HOH A . 
E 5 HOH   41  341 10  HOH   HOH A . 
E 5 HOH   42  342 108 HOH   HOH A . 
E 5 HOH   43  343 98  HOH   HOH A . 
E 5 HOH   44  344 43  HOH   HOH A . 
E 5 HOH   45  345 29  HOH   HOH A . 
E 5 HOH   46  346 84  HOH   HOH A . 
E 5 HOH   47  347 99  HOH   HOH A . 
E 5 HOH   48  348 64  HOH   HOH A . 
E 5 HOH   49  349 12  HOH   HOH A . 
E 5 HOH   50  350 79  HOH   HOH A . 
E 5 HOH   51  351 48  HOH   HOH A . 
E 5 HOH   52  352 50  HOH   HOH A . 
E 5 HOH   53  353 17  HOH   HOH A . 
E 5 HOH   54  354 87  HOH   HOH A . 
E 5 HOH   55  355 63  HOH   HOH A . 
E 5 HOH   56  356 55  HOH   HOH A . 
E 5 HOH   57  357 14  HOH   HOH A . 
E 5 HOH   58  358 5   HOH   HOH A . 
E 5 HOH   59  359 25  HOH   HOH A . 
E 5 HOH   60  360 61  HOH   HOH A . 
E 5 HOH   61  361 31  HOH   HOH A . 
E 5 HOH   62  362 58  HOH   HOH A . 
E 5 HOH   63  363 70  HOH   HOH A . 
E 5 HOH   64  364 85  HOH   HOH A . 
E 5 HOH   65  365 53  HOH   HOH A . 
E 5 HOH   66  366 34  HOH   HOH A . 
E 5 HOH   67  367 39  HOH   HOH A . 
E 5 HOH   68  368 91  HOH   HOH A . 
E 5 HOH   69  369 56  HOH   HOH A . 
E 5 HOH   70  370 13  HOH   HOH A . 
E 5 HOH   71  371 67  HOH   HOH A . 
E 5 HOH   72  372 8   HOH   HOH A . 
E 5 HOH   73  373 93  HOH   HOH A . 
E 5 HOH   74  374 6   HOH   HOH A . 
E 5 HOH   75  375 52  HOH   HOH A . 
E 5 HOH   76  376 65  HOH   HOH A . 
E 5 HOH   77  377 19  HOH   HOH A . 
E 5 HOH   78  378 33  HOH   HOH A . 
E 5 HOH   79  379 107 HOH   HOH A . 
E 5 HOH   80  380 22  HOH   HOH A . 
E 5 HOH   81  381 95  HOH   HOH A . 
E 5 HOH   82  382 59  HOH   HOH A . 
E 5 HOH   83  383 97  HOH   HOH A . 
E 5 HOH   84  384 78  HOH   HOH A . 
E 5 HOH   85  385 32  HOH   HOH A . 
E 5 HOH   86  386 54  HOH   HOH A . 
E 5 HOH   87  387 35  HOH   HOH A . 
E 5 HOH   88  388 73  HOH   HOH A . 
E 5 HOH   89  389 30  HOH   HOH A . 
E 5 HOH   90  390 102 HOH   HOH A . 
E 5 HOH   91  391 71  HOH   HOH A . 
E 5 HOH   92  392 80  HOH   HOH A . 
E 5 HOH   93  393 47  HOH   HOH A . 
E 5 HOH   94  394 82  HOH   HOH A . 
E 5 HOH   95  395 88  HOH   HOH A . 
E 5 HOH   96  396 7   HOH   HOH A . 
E 5 HOH   97  397 20  HOH   HOH A . 
E 5 HOH   98  398 23  HOH   HOH A . 
E 5 HOH   99  399 51  HOH   HOH A . 
E 5 HOH   100 400 74  HOH   HOH A . 
E 5 HOH   101 401 21  HOH   HOH A . 
E 5 HOH   102 402 109 HOH   HOH A . 
E 5 HOH   103 403 81  HOH   HOH A . 
E 5 HOH   104 404 2   HOH   HOH A . 
E 5 HOH   105 405 104 HOH   HOH A . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (23-JAN-2024)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
# 
_cell.entry_id           7HUV 
_cell.length_a           72.823 
_cell.length_b           61.506 
_cell.length_c           32.691 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.83 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HUV 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
# 
_exptl.entry_id          7HUV 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.30 
_exptl_crystal.density_percent_sol   46.53 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-10-10 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92208 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92208 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HUV 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             36.37 
_reflns.d_resolution_high            1.53 
_reflns.number_obs                   21871 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.125 
_reflns.pdbx_netI_over_sigmaI        7.3 
_reflns.pdbx_redundancy              6.8 
_reflns.pdbx_Rrim_I_all              0.135 
_reflns.pdbx_Rpim_I_all              0.051 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     148343 
_reflns.pdbx_chi_squared             0.87 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.53 
_reflns_shell.d_res_low                   1.61 
_reflns_shell.number_measured_all         18291 
_reflns_shell.number_unique_obs           3171 
_reflns_shell.Rmerge_I_obs                2.478 
_reflns_shell.pdbx_chi_squared            0.75 
_reflns_shell.pdbx_redundancy             5.8 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.6 
_reflns_shell.pdbx_Rrim_I_all             2.726 
_reflns_shell.pdbx_Rpim_I_all             1.123 
_reflns_shell.pdbx_CC_half                0.383 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HUV 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     21734 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             36.37 
_refine.ls_d_res_high                            1.528 
_refine.ls_percent_reflns_obs                    99.3 
_refine.ls_R_factor_obs                          0.2103 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2089 
_refine.ls_R_factor_R_free                       0.2401 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.510 
_refine.ls_number_reflns_R_free                  981 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.955 
_refine.correlation_coeff_Fo_to_Fc_free          0.934 
_refine.B_iso_mean                               30.27 
_refine.aniso_B[1][1]                            -2.80500 
_refine.aniso_B[2][2]                            3.97570 
_refine.aniso_B[3][3]                            -1.17070 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.22970 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             0.085 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.086 
_refine.pdbx_overall_SU_R_Blow_DPI               0.087 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.088 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HUV 
_refine_analyze.Luzzati_coordinate_error_obs    0.23 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         25 
_refine_hist.number_atoms_solvent             105 
_refine_hist.number_atoms_total               1204 
_refine_hist.d_res_high                       1.528 
_refine_hist.d_res_low                        36.37 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.010 ? 2.00  1129 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.99  ? 2.00  1537 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  380  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  202  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1129 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.11  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.83 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  139  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  940  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   50 
_refine_ls_shell.d_res_high                       1.53 
_refine_ls_shell.d_res_low                        1.54 
_refine_ls_shell.number_reflns_R_work             422 
_refine_ls_shell.R_factor_R_work                  0.3873 
_refine_ls_shell.percent_reflns_obs               90.23 
_refine_ls_shell.R_factor_R_free                  0.3400 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.95 
_refine_ls_shell.number_reflns_R_free             22 
_refine_ls_shell.number_reflns_all                444 
_refine_ls_shell.R_factor_all                     0.3849 
# 
_struct.entry_id                  7HUV 
_struct.title                     
;Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre -- Crystal structure of Coxsackievirus A16 (G-10) 2A protease in complex with ASAP-0031953-001 (A71EV2A-x3218)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HUV 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7HUV 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_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 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P4 AA4 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P5 AA5 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_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 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.417 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.303 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.329 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.209 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 110.3 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 107.4 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.7 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 109.2 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 99.4  ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 113.6 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? THR A 120 ? GLY A 119 THR A 126 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
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 TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HUV 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     307 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     307 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_656 
_pdbx_validate_symm_contact.dist              1.26 
# 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         15.1720 
_pdbx_refine_tls.origin_y         7.0741 
_pdbx_refine_tls.origin_z         14.2286 
_pdbx_refine_tls.T[1][1]          -0.0516 
_pdbx_refine_tls.T[2][2]          -0.0370 
_pdbx_refine_tls.T[3][3]          -0.0361 
_pdbx_refine_tls.T[1][2]          -0.0010 
_pdbx_refine_tls.T[1][3]          -0.0228 
_pdbx_refine_tls.T[2][3]          -0.0107 
_pdbx_refine_tls.L[1][1]          1.3458 
_pdbx_refine_tls.L[2][2]          4.7440 
_pdbx_refine_tls.L[3][3]          0.4233 
_pdbx_refine_tls.L[1][2]          1.7399 
_pdbx_refine_tls.L[1][3]          -0.6332 
_pdbx_refine_tls.L[2][3]          -1.2903 
_pdbx_refine_tls.S[1][1]          -0.1006 
_pdbx_refine_tls.S[1][2]          0.0518 
_pdbx_refine_tls.S[1][3]          0.0785 
_pdbx_refine_tls.S[2][1]          0.1659 
_pdbx_refine_tls.S[2][2]          0.1182 
_pdbx_refine_tls.S[2][3]          -0.1399 
_pdbx_refine_tls.S[3][1]          -0.0038 
_pdbx_refine_tls.S[3][2]          -0.0938 
_pdbx_refine_tls.S[3][3]          -0.0176 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLU 146 ? A GLU 140 
2 1 Y 1 A ALA 147 ? A ALA 141 
3 1 Y 1 A MET 148 ? A MET 142 
4 1 Y 1 A GLU 149 ? A GLU 143 
5 1 Y 1 A GLN 150 ? A GLN 144 
# 
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 
A1BSS N1   N  N N 1   
A1BSS N3   N  Y N 2   
A1BSS C4   C  N N 3   
A1BSS C5   C  N N 4   
A1BSS C6   C  N R 5   
A1BSS C7   C  N N 6   
A1BSS C8   C  N N 7   
A1BSS C10  C  Y N 8   
A1BSS O1   O  N N 9   
A1BSS C3   C  N N 10  
A1BSS C2   C  N N 11  
A1BSS C12  C  N N 12  
A1BSS C1   C  N S 13  
A1BSS C    C  N N 14  
A1BSS O    O  N N 15  
A1BSS N    N  N N 16  
A1BSS C11  C  Y N 17  
A1BSS N4   N  Y N 18  
A1BSS C9   C  Y N 19  
A1BSS N2   N  N N 20  
A1BSS H2   H  N N 21  
A1BSS H10  H  N N 22  
A1BSS H9   H  N N 23  
A1BSS H1   H  N N 24  
A1BSS H12  H  N N 25  
A1BSS H11  H  N N 26  
A1BSS H14  H  N N 27  
A1BSS H13  H  N N 28  
A1BSS H16  H  N N 29  
A1BSS H8   H  N N 30  
A1BSS H7   H  N N 31  
A1BSS H6   H  N N 32  
A1BSS H5   H  N N 33  
A1BSS H18  H  N N 34  
A1BSS H17  H  N N 35  
A1BSS H    H  N N 36  
A1BSS H3   H  N N 37  
A1BSS H4   H  N N 38  
A1BSS H15  H  N N 39  
ALA   N    N  N N 40  
ALA   CA   C  N S 41  
ALA   C    C  N N 42  
ALA   O    O  N N 43  
ALA   CB   C  N N 44  
ALA   OXT  O  N N 45  
ALA   H    H  N N 46  
ALA   H2   H  N N 47  
ALA   HA   H  N N 48  
ALA   HB1  H  N N 49  
ALA   HB2  H  N N 50  
ALA   HB3  H  N N 51  
ALA   HXT  H  N N 52  
ARG   N    N  N N 53  
ARG   CA   C  N S 54  
ARG   C    C  N N 55  
ARG   O    O  N N 56  
ARG   CB   C  N N 57  
ARG   CG   C  N N 58  
ARG   CD   C  N N 59  
ARG   NE   N  N N 60  
ARG   CZ   C  N N 61  
ARG   NH1  N  N N 62  
ARG   NH2  N  N N 63  
ARG   OXT  O  N N 64  
ARG   H    H  N N 65  
ARG   H2   H  N N 66  
ARG   HA   H  N N 67  
ARG   HB2  H  N N 68  
ARG   HB3  H  N N 69  
ARG   HG2  H  N N 70  
ARG   HG3  H  N N 71  
ARG   HD2  H  N N 72  
ARG   HD3  H  N N 73  
ARG   HE   H  N N 74  
ARG   HH11 H  N N 75  
ARG   HH12 H  N N 76  
ARG   HH21 H  N N 77  
ARG   HH22 H  N N 78  
ARG   HXT  H  N N 79  
ASN   N    N  N N 80  
ASN   CA   C  N S 81  
ASN   C    C  N N 82  
ASN   O    O  N N 83  
ASN   CB   C  N N 84  
ASN   CG   C  N N 85  
ASN   OD1  O  N N 86  
ASN   ND2  N  N N 87  
ASN   OXT  O  N N 88  
ASN   H    H  N N 89  
ASN   H2   H  N N 90  
ASN   HA   H  N N 91  
ASN   HB2  H  N N 92  
ASN   HB3  H  N N 93  
ASN   HD21 H  N N 94  
ASN   HD22 H  N N 95  
ASN   HXT  H  N N 96  
ASP   N    N  N N 97  
ASP   CA   C  N S 98  
ASP   C    C  N N 99  
ASP   O    O  N N 100 
ASP   CB   C  N N 101 
ASP   CG   C  N N 102 
ASP   OD1  O  N N 103 
ASP   OD2  O  N N 104 
ASP   OXT  O  N N 105 
ASP   H    H  N N 106 
ASP   H2   H  N N 107 
ASP   HA   H  N N 108 
ASP   HB2  H  N N 109 
ASP   HB3  H  N N 110 
ASP   HD2  H  N N 111 
ASP   HXT  H  N N 112 
CYS   N    N  N N 113 
CYS   CA   C  N R 114 
CYS   C    C  N N 115 
CYS   O    O  N N 116 
CYS   CB   C  N N 117 
CYS   SG   S  N N 118 
CYS   OXT  O  N N 119 
CYS   H    H  N N 120 
CYS   H2   H  N N 121 
CYS   HA   H  N N 122 
CYS   HB2  H  N N 123 
CYS   HB3  H  N N 124 
CYS   HG   H  N N 125 
CYS   HXT  H  N N 126 
DMS   S    S  N N 127 
DMS   O    O  N N 128 
DMS   C1   C  N N 129 
DMS   C2   C  N N 130 
DMS   H11  H  N N 131 
DMS   H12  H  N N 132 
DMS   H13  H  N N 133 
DMS   H21  H  N N 134 
DMS   H22  H  N N 135 
DMS   H23  H  N N 136 
GLN   N    N  N N 137 
GLN   CA   C  N S 138 
GLN   C    C  N N 139 
GLN   O    O  N N 140 
GLN   CB   C  N N 141 
GLN   CG   C  N N 142 
GLN   CD   C  N N 143 
GLN   OE1  O  N N 144 
GLN   NE2  N  N N 145 
GLN   OXT  O  N N 146 
GLN   H    H  N N 147 
GLN   H2   H  N N 148 
GLN   HA   H  N N 149 
GLN   HB2  H  N N 150 
GLN   HB3  H  N N 151 
GLN   HG2  H  N N 152 
GLN   HG3  H  N N 153 
GLN   HE21 H  N N 154 
GLN   HE22 H  N N 155 
GLN   HXT  H  N N 156 
GLU   N    N  N N 157 
GLU   CA   C  N S 158 
GLU   C    C  N N 159 
GLU   O    O  N N 160 
GLU   CB   C  N N 161 
GLU   CG   C  N N 162 
GLU   CD   C  N N 163 
GLU   OE1  O  N N 164 
GLU   OE2  O  N N 165 
GLU   OXT  O  N N 166 
GLU   H    H  N N 167 
GLU   H2   H  N N 168 
GLU   HA   H  N N 169 
GLU   HB2  H  N N 170 
GLU   HB3  H  N N 171 
GLU   HG2  H  N N 172 
GLU   HG3  H  N N 173 
GLU   HE2  H  N N 174 
GLU   HXT  H  N N 175 
GLY   N    N  N N 176 
GLY   CA   C  N N 177 
GLY   C    C  N N 178 
GLY   O    O  N N 179 
GLY   OXT  O  N N 180 
GLY   H    H  N N 181 
GLY   H2   H  N N 182 
GLY   HA2  H  N N 183 
GLY   HA3  H  N N 184 
GLY   HXT  H  N N 185 
HIS   N    N  N N 186 
HIS   CA   C  N S 187 
HIS   C    C  N N 188 
HIS   O    O  N N 189 
HIS   CB   C  N N 190 
HIS   CG   C  Y N 191 
HIS   ND1  N  Y N 192 
HIS   CD2  C  Y N 193 
HIS   CE1  C  Y N 194 
HIS   NE2  N  Y N 195 
HIS   OXT  O  N N 196 
HIS   H    H  N N 197 
HIS   H2   H  N N 198 
HIS   HA   H  N N 199 
HIS   HB2  H  N N 200 
HIS   HB3  H  N N 201 
HIS   HD1  H  N N 202 
HIS   HD2  H  N N 203 
HIS   HE1  H  N N 204 
HIS   HE2  H  N N 205 
HIS   HXT  H  N N 206 
HOH   O    O  N N 207 
HOH   H1   H  N N 208 
HOH   H2   H  N N 209 
ILE   N    N  N N 210 
ILE   CA   C  N S 211 
ILE   C    C  N N 212 
ILE   O    O  N N 213 
ILE   CB   C  N S 214 
ILE   CG1  C  N N 215 
ILE   CG2  C  N N 216 
ILE   CD1  C  N N 217 
ILE   OXT  O  N N 218 
ILE   H    H  N N 219 
ILE   H2   H  N N 220 
ILE   HA   H  N N 221 
ILE   HB   H  N N 222 
ILE   HG12 H  N N 223 
ILE   HG13 H  N N 224 
ILE   HG21 H  N N 225 
ILE   HG22 H  N N 226 
ILE   HG23 H  N N 227 
ILE   HD11 H  N N 228 
ILE   HD12 H  N N 229 
ILE   HD13 H  N N 230 
ILE   HXT  H  N N 231 
LEU   N    N  N N 232 
LEU   CA   C  N S 233 
LEU   C    C  N N 234 
LEU   O    O  N N 235 
LEU   CB   C  N N 236 
LEU   CG   C  N N 237 
LEU   CD1  C  N N 238 
LEU   CD2  C  N N 239 
LEU   OXT  O  N N 240 
LEU   H    H  N N 241 
LEU   H2   H  N N 242 
LEU   HA   H  N N 243 
LEU   HB2  H  N N 244 
LEU   HB3  H  N N 245 
LEU   HG   H  N N 246 
LEU   HD11 H  N N 247 
LEU   HD12 H  N N 248 
LEU   HD13 H  N N 249 
LEU   HD21 H  N N 250 
LEU   HD22 H  N N 251 
LEU   HD23 H  N N 252 
LEU   HXT  H  N N 253 
LYS   N    N  N N 254 
LYS   CA   C  N S 255 
LYS   C    C  N N 256 
LYS   O    O  N N 257 
LYS   CB   C  N N 258 
LYS   CG   C  N N 259 
LYS   CD   C  N N 260 
LYS   CE   C  N N 261 
LYS   NZ   N  N N 262 
LYS   OXT  O  N N 263 
LYS   H    H  N N 264 
LYS   H2   H  N N 265 
LYS   HA   H  N N 266 
LYS   HB2  H  N N 267 
LYS   HB3  H  N N 268 
LYS   HG2  H  N N 269 
LYS   HG3  H  N N 270 
LYS   HD2  H  N N 271 
LYS   HD3  H  N N 272 
LYS   HE2  H  N N 273 
LYS   HE3  H  N N 274 
LYS   HZ1  H  N N 275 
LYS   HZ2  H  N N 276 
LYS   HZ3  H  N N 277 
LYS   HXT  H  N N 278 
MET   N    N  N N 279 
MET   CA   C  N S 280 
MET   C    C  N N 281 
MET   O    O  N N 282 
MET   CB   C  N N 283 
MET   CG   C  N N 284 
MET   SD   S  N N 285 
MET   CE   C  N N 286 
MET   OXT  O  N N 287 
MET   H    H  N N 288 
MET   H2   H  N N 289 
MET   HA   H  N N 290 
MET   HB2  H  N N 291 
MET   HB3  H  N N 292 
MET   HG2  H  N N 293 
MET   HG3  H  N N 294 
MET   HE1  H  N N 295 
MET   HE2  H  N N 296 
MET   HE3  H  N N 297 
MET   HXT  H  N N 298 
PHE   N    N  N N 299 
PHE   CA   C  N S 300 
PHE   C    C  N N 301 
PHE   O    O  N N 302 
PHE   CB   C  N N 303 
PHE   CG   C  Y N 304 
PHE   CD1  C  Y N 305 
PHE   CD2  C  Y N 306 
PHE   CE1  C  Y N 307 
PHE   CE2  C  Y N 308 
PHE   CZ   C  Y N 309 
PHE   OXT  O  N N 310 
PHE   H    H  N N 311 
PHE   H2   H  N N 312 
PHE   HA   H  N N 313 
PHE   HB2  H  N N 314 
PHE   HB3  H  N N 315 
PHE   HD1  H  N N 316 
PHE   HD2  H  N N 317 
PHE   HE1  H  N N 318 
PHE   HE2  H  N N 319 
PHE   HZ   H  N N 320 
PHE   HXT  H  N N 321 
PRO   N    N  N N 322 
PRO   CA   C  N S 323 
PRO   C    C  N N 324 
PRO   O    O  N N 325 
PRO   CB   C  N N 326 
PRO   CG   C  N N 327 
PRO   CD   C  N N 328 
PRO   OXT  O  N N 329 
PRO   H    H  N N 330 
PRO   HA   H  N N 331 
PRO   HB2  H  N N 332 
PRO   HB3  H  N N 333 
PRO   HG2  H  N N 334 
PRO   HG3  H  N N 335 
PRO   HD2  H  N N 336 
PRO   HD3  H  N N 337 
PRO   HXT  H  N N 338 
SER   N    N  N N 339 
SER   CA   C  N S 340 
SER   C    C  N N 341 
SER   O    O  N N 342 
SER   CB   C  N N 343 
SER   OG   O  N N 344 
SER   OXT  O  N N 345 
SER   H    H  N N 346 
SER   H2   H  N N 347 
SER   HA   H  N N 348 
SER   HB2  H  N N 349 
SER   HB3  H  N N 350 
SER   HG   H  N N 351 
SER   HXT  H  N N 352 
THR   N    N  N N 353 
THR   CA   C  N S 354 
THR   C    C  N N 355 
THR   O    O  N N 356 
THR   CB   C  N R 357 
THR   OG1  O  N N 358 
THR   CG2  C  N N 359 
THR   OXT  O  N N 360 
THR   H    H  N N 361 
THR   H2   H  N N 362 
THR   HA   H  N N 363 
THR   HB   H  N N 364 
THR   HG1  H  N N 365 
THR   HG21 H  N N 366 
THR   HG22 H  N N 367 
THR   HG23 H  N N 368 
THR   HXT  H  N N 369 
TRP   N    N  N N 370 
TRP   CA   C  N S 371 
TRP   C    C  N N 372 
TRP   O    O  N N 373 
TRP   CB   C  N N 374 
TRP   CG   C  Y N 375 
TRP   CD1  C  Y N 376 
TRP   CD2  C  Y N 377 
TRP   NE1  N  Y N 378 
TRP   CE2  C  Y N 379 
TRP   CE3  C  Y N 380 
TRP   CZ2  C  Y N 381 
TRP   CZ3  C  Y N 382 
TRP   CH2  C  Y N 383 
TRP   OXT  O  N N 384 
TRP   H    H  N N 385 
TRP   H2   H  N N 386 
TRP   HA   H  N N 387 
TRP   HB2  H  N N 388 
TRP   HB3  H  N N 389 
TRP   HD1  H  N N 390 
TRP   HE1  H  N N 391 
TRP   HE3  H  N N 392 
TRP   HZ2  H  N N 393 
TRP   HZ3  H  N N 394 
TRP   HH2  H  N N 395 
TRP   HXT  H  N N 396 
TYR   N    N  N N 397 
TYR   CA   C  N S 398 
TYR   C    C  N N 399 
TYR   O    O  N N 400 
TYR   CB   C  N N 401 
TYR   CG   C  Y N 402 
TYR   CD1  C  Y N 403 
TYR   CD2  C  Y N 404 
TYR   CE1  C  Y N 405 
TYR   CE2  C  Y N 406 
TYR   CZ   C  Y N 407 
TYR   OH   O  N N 408 
TYR   OXT  O  N N 409 
TYR   H    H  N N 410 
TYR   H2   H  N N 411 
TYR   HA   H  N N 412 
TYR   HB2  H  N N 413 
TYR   HB3  H  N N 414 
TYR   HD1  H  N N 415 
TYR   HD2  H  N N 416 
TYR   HE1  H  N N 417 
TYR   HE2  H  N N 418 
TYR   HH   H  N N 419 
TYR   HXT  H  N N 420 
VAL   N    N  N N 421 
VAL   CA   C  N S 422 
VAL   C    C  N N 423 
VAL   O    O  N N 424 
VAL   CB   C  N N 425 
VAL   CG1  C  N N 426 
VAL   CG2  C  N N 427 
VAL   OXT  O  N N 428 
VAL   H    H  N N 429 
VAL   H2   H  N N 430 
VAL   HA   H  N N 431 
VAL   HB   H  N N 432 
VAL   HG11 H  N N 433 
VAL   HG12 H  N N 434 
VAL   HG13 H  N N 435 
VAL   HG21 H  N N 436 
VAL   HG22 H  N N 437 
VAL   HG23 H  N N 438 
VAL   HXT  H  N N 439 
ZN    ZN   ZN N N 440 
# 
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 
A1BSS N   C    sing N N 1   
A1BSS O   C    doub N N 2   
A1BSS C   C1   sing N N 3   
A1BSS C1  C2   sing N N 4   
A1BSS C2  C3   sing N N 5   
A1BSS C3  C4   sing N N 6   
A1BSS C4  N1   sing N N 7   
A1BSS N1  C5   sing N N 8   
A1BSS C5  O1   doub N N 9   
A1BSS C6  C5   sing N N 10  
A1BSS C6  C7   sing N N 11  
A1BSS C7  C8   sing N N 12  
A1BSS C8  N2   sing N N 13  
A1BSS N2  C9   sing N N 14  
A1BSS C9  N3   sing Y N 15  
A1BSS N3  N4   sing Y N 16  
A1BSS N4  C10  doub Y N 17  
A1BSS C10 C11  sing Y N 18  
A1BSS C9  C11  doub Y N 19  
A1BSS C11 C6   sing N N 20  
A1BSS C12 N1   sing N N 21  
A1BSS C1  C12  sing N N 22  
A1BSS N3  H2   sing N N 23  
A1BSS C4  H10  sing N N 24  
A1BSS C4  H9   sing N N 25  
A1BSS C6  H1   sing N N 26  
A1BSS C7  H12  sing N N 27  
A1BSS C7  H11  sing N N 28  
A1BSS C8  H14  sing N N 29  
A1BSS C8  H13  sing N N 30  
A1BSS C10 H16  sing N N 31  
A1BSS C3  H8   sing N N 32  
A1BSS C3  H7   sing N N 33  
A1BSS C2  H6   sing N N 34  
A1BSS C2  H5   sing N N 35  
A1BSS C12 H18  sing N N 36  
A1BSS C12 H17  sing N N 37  
A1BSS C1  H    sing N N 38  
A1BSS N   H3   sing N N 39  
A1BSS N   H4   sing N N 40  
A1BSS N2  H15  sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
DMS   S   O    doub N N 124 
DMS   S   C1   sing N N 125 
DMS   S   C2   sing N N 126 
DMS   C1  H11  sing N N 127 
DMS   C1  H12  sing N N 128 
DMS   C1  H13  sing N N 129 
DMS   C2  H21  sing N N 130 
DMS   C2  H22  sing N N 131 
DMS   C2  H23  sing N N 132 
GLN   N   CA   sing N N 133 
GLN   N   H    sing N N 134 
GLN   N   H2   sing N N 135 
GLN   CA  C    sing N N 136 
GLN   CA  CB   sing N N 137 
GLN   CA  HA   sing N N 138 
GLN   C   O    doub N N 139 
GLN   C   OXT  sing N N 140 
GLN   CB  CG   sing N N 141 
GLN   CB  HB2  sing N N 142 
GLN   CB  HB3  sing N N 143 
GLN   CG  CD   sing N N 144 
GLN   CG  HG2  sing N N 145 
GLN   CG  HG3  sing N N 146 
GLN   CD  OE1  doub N N 147 
GLN   CD  NE2  sing N N 148 
GLN   NE2 HE21 sing N N 149 
GLN   NE2 HE22 sing N N 150 
GLN   OXT HXT  sing N N 151 
GLU   N   CA   sing N N 152 
GLU   N   H    sing N N 153 
GLU   N   H2   sing N N 154 
GLU   CA  C    sing N N 155 
GLU   CA  CB   sing N N 156 
GLU   CA  HA   sing N N 157 
GLU   C   O    doub N N 158 
GLU   C   OXT  sing N N 159 
GLU   CB  CG   sing N N 160 
GLU   CB  HB2  sing N N 161 
GLU   CB  HB3  sing N N 162 
GLU   CG  CD   sing N N 163 
GLU   CG  HG2  sing N N 164 
GLU   CG  HG3  sing N N 165 
GLU   CD  OE1  doub N N 166 
GLU   CD  OE2  sing N N 167 
GLU   OE2 HE2  sing N N 168 
GLU   OXT HXT  sing N N 169 
GLY   N   CA   sing N N 170 
GLY   N   H    sing N N 171 
GLY   N   H2   sing N N 172 
GLY   CA  C    sing N N 173 
GLY   CA  HA2  sing N N 174 
GLY   CA  HA3  sing N N 175 
GLY   C   O    doub N N 176 
GLY   C   OXT  sing N N 177 
GLY   OXT HXT  sing N N 178 
HIS   N   CA   sing N N 179 
HIS   N   H    sing N N 180 
HIS   N   H2   sing N N 181 
HIS   CA  C    sing N N 182 
HIS   CA  CB   sing N N 183 
HIS   CA  HA   sing N N 184 
HIS   C   O    doub N N 185 
HIS   C   OXT  sing N N 186 
HIS   CB  CG   sing N N 187 
HIS   CB  HB2  sing N N 188 
HIS   CB  HB3  sing N N 189 
HIS   CG  ND1  sing Y N 190 
HIS   CG  CD2  doub Y N 191 
HIS   ND1 CE1  doub Y N 192 
HIS   ND1 HD1  sing N N 193 
HIS   CD2 NE2  sing Y N 194 
HIS   CD2 HD2  sing N N 195 
HIS   CE1 NE2  sing Y N 196 
HIS   CE1 HE1  sing N N 197 
HIS   NE2 HE2  sing N N 198 
HIS   OXT HXT  sing N N 199 
HOH   O   H1   sing N N 200 
HOH   O   H2   sing N N 201 
ILE   N   CA   sing N N 202 
ILE   N   H    sing N N 203 
ILE   N   H2   sing N N 204 
ILE   CA  C    sing N N 205 
ILE   CA  CB   sing N N 206 
ILE   CA  HA   sing N N 207 
ILE   C   O    doub N N 208 
ILE   C   OXT  sing N N 209 
ILE   CB  CG1  sing N N 210 
ILE   CB  CG2  sing N N 211 
ILE   CB  HB   sing N N 212 
ILE   CG1 CD1  sing N N 213 
ILE   CG1 HG12 sing N N 214 
ILE   CG1 HG13 sing N N 215 
ILE   CG2 HG21 sing N N 216 
ILE   CG2 HG22 sing N N 217 
ILE   CG2 HG23 sing N N 218 
ILE   CD1 HD11 sing N N 219 
ILE   CD1 HD12 sing N N 220 
ILE   CD1 HD13 sing N N 221 
ILE   OXT HXT  sing N N 222 
LEU   N   CA   sing N N 223 
LEU   N   H    sing N N 224 
LEU   N   H2   sing N N 225 
LEU   CA  C    sing N N 226 
LEU   CA  CB   sing N N 227 
LEU   CA  HA   sing N N 228 
LEU   C   O    doub N N 229 
LEU   C   OXT  sing N N 230 
LEU   CB  CG   sing N N 231 
LEU   CB  HB2  sing N N 232 
LEU   CB  HB3  sing N N 233 
LEU   CG  CD1  sing N N 234 
LEU   CG  CD2  sing N N 235 
LEU   CG  HG   sing N N 236 
LEU   CD1 HD11 sing N N 237 
LEU   CD1 HD12 sing N N 238 
LEU   CD1 HD13 sing N N 239 
LEU   CD2 HD21 sing N N 240 
LEU   CD2 HD22 sing N N 241 
LEU   CD2 HD23 sing N N 242 
LEU   OXT HXT  sing N N 243 
LYS   N   CA   sing N N 244 
LYS   N   H    sing N N 245 
LYS   N   H2   sing N N 246 
LYS   CA  C    sing N N 247 
LYS   CA  CB   sing N N 248 
LYS   CA  HA   sing N N 249 
LYS   C   O    doub N N 250 
LYS   C   OXT  sing N N 251 
LYS   CB  CG   sing N N 252 
LYS   CB  HB2  sing N N 253 
LYS   CB  HB3  sing N N 254 
LYS   CG  CD   sing N N 255 
LYS   CG  HG2  sing N N 256 
LYS   CG  HG3  sing N N 257 
LYS   CD  CE   sing N N 258 
LYS   CD  HD2  sing N N 259 
LYS   CD  HD3  sing N N 260 
LYS   CE  NZ   sing N N 261 
LYS   CE  HE2  sing N N 262 
LYS   CE  HE3  sing N N 263 
LYS   NZ  HZ1  sing N N 264 
LYS   NZ  HZ2  sing N N 265 
LYS   NZ  HZ3  sing N N 266 
LYS   OXT HXT  sing N N 267 
MET   N   CA   sing N N 268 
MET   N   H    sing N N 269 
MET   N   H2   sing N N 270 
MET   CA  C    sing N N 271 
MET   CA  CB   sing N N 272 
MET   CA  HA   sing N N 273 
MET   C   O    doub N N 274 
MET   C   OXT  sing N N 275 
MET   CB  CG   sing N N 276 
MET   CB  HB2  sing N N 277 
MET   CB  HB3  sing N N 278 
MET   CG  SD   sing N N 279 
MET   CG  HG2  sing N N 280 
MET   CG  HG3  sing N N 281 
MET   SD  CE   sing N N 282 
MET   CE  HE1  sing N N 283 
MET   CE  HE2  sing N N 284 
MET   CE  HE3  sing N N 285 
MET   OXT HXT  sing N N 286 
PHE   N   CA   sing N N 287 
PHE   N   H    sing N N 288 
PHE   N   H2   sing N N 289 
PHE   CA  C    sing N N 290 
PHE   CA  CB   sing N N 291 
PHE   CA  HA   sing N N 292 
PHE   C   O    doub N N 293 
PHE   C   OXT  sing N N 294 
PHE   CB  CG   sing N N 295 
PHE   CB  HB2  sing N N 296 
PHE   CB  HB3  sing N N 297 
PHE   CG  CD1  doub Y N 298 
PHE   CG  CD2  sing Y N 299 
PHE   CD1 CE1  sing Y N 300 
PHE   CD1 HD1  sing N N 301 
PHE   CD2 CE2  doub Y N 302 
PHE   CD2 HD2  sing N N 303 
PHE   CE1 CZ   doub Y N 304 
PHE   CE1 HE1  sing N N 305 
PHE   CE2 CZ   sing Y N 306 
PHE   CE2 HE2  sing N N 307 
PHE   CZ  HZ   sing N N 308 
PHE   OXT HXT  sing N N 309 
PRO   N   CA   sing N N 310 
PRO   N   CD   sing N N 311 
PRO   N   H    sing N N 312 
PRO   CA  C    sing N N 313 
PRO   CA  CB   sing N N 314 
PRO   CA  HA   sing N N 315 
PRO   C   O    doub N N 316 
PRO   C   OXT  sing N N 317 
PRO   CB  CG   sing N N 318 
PRO   CB  HB2  sing N N 319 
PRO   CB  HB3  sing N N 320 
PRO   CG  CD   sing N N 321 
PRO   CG  HG2  sing N N 322 
PRO   CG  HG3  sing N N 323 
PRO   CD  HD2  sing N N 324 
PRO   CD  HD3  sing N N 325 
PRO   OXT HXT  sing N N 326 
SER   N   CA   sing N N 327 
SER   N   H    sing N N 328 
SER   N   H2   sing N N 329 
SER   CA  C    sing N N 330 
SER   CA  CB   sing N N 331 
SER   CA  HA   sing N N 332 
SER   C   O    doub N N 333 
SER   C   OXT  sing N N 334 
SER   CB  OG   sing N N 335 
SER   CB  HB2  sing N N 336 
SER   CB  HB3  sing N N 337 
SER   OG  HG   sing N N 338 
SER   OXT HXT  sing N N 339 
THR   N   CA   sing N N 340 
THR   N   H    sing N N 341 
THR   N   H2   sing N N 342 
THR   CA  C    sing N N 343 
THR   CA  CB   sing N N 344 
THR   CA  HA   sing N N 345 
THR   C   O    doub N N 346 
THR   C   OXT  sing N N 347 
THR   CB  OG1  sing N N 348 
THR   CB  CG2  sing N N 349 
THR   CB  HB   sing N N 350 
THR   OG1 HG1  sing N N 351 
THR   CG2 HG21 sing N N 352 
THR   CG2 HG22 sing N N 353 
THR   CG2 HG23 sing N N 354 
THR   OXT HXT  sing N N 355 
TRP   N   CA   sing N N 356 
TRP   N   H    sing N N 357 
TRP   N   H2   sing N N 358 
TRP   CA  C    sing N N 359 
TRP   CA  CB   sing N N 360 
TRP   CA  HA   sing N N 361 
TRP   C   O    doub N N 362 
TRP   C   OXT  sing N N 363 
TRP   CB  CG   sing N N 364 
TRP   CB  HB2  sing N N 365 
TRP   CB  HB3  sing N N 366 
TRP   CG  CD1  doub Y N 367 
TRP   CG  CD2  sing Y N 368 
TRP   CD1 NE1  sing Y N 369 
TRP   CD1 HD1  sing N N 370 
TRP   CD2 CE2  doub Y N 371 
TRP   CD2 CE3  sing Y N 372 
TRP   NE1 CE2  sing Y N 373 
TRP   NE1 HE1  sing N N 374 
TRP   CE2 CZ2  sing Y N 375 
TRP   CE3 CZ3  doub Y N 376 
TRP   CE3 HE3  sing N N 377 
TRP   CZ2 CH2  doub Y N 378 
TRP   CZ2 HZ2  sing N N 379 
TRP   CZ3 CH2  sing Y N 380 
TRP   CZ3 HZ3  sing N N 381 
TRP   CH2 HH2  sing N N 382 
TRP   OXT HXT  sing N N 383 
TYR   N   CA   sing N N 384 
TYR   N   H    sing N N 385 
TYR   N   H2   sing N N 386 
TYR   CA  C    sing N N 387 
TYR   CA  CB   sing N N 388 
TYR   CA  HA   sing N N 389 
TYR   C   O    doub N N 390 
TYR   C   OXT  sing N N 391 
TYR   CB  CG   sing N N 392 
TYR   CB  HB2  sing N N 393 
TYR   CB  HB3  sing N N 394 
TYR   CG  CD1  doub Y N 395 
TYR   CG  CD2  sing Y N 396 
TYR   CD1 CE1  sing Y N 397 
TYR   CD1 HD1  sing N N 398 
TYR   CD2 CE2  doub Y N 399 
TYR   CD2 HD2  sing N N 400 
TYR   CE1 CZ   doub Y N 401 
TYR   CE1 HE1  sing N N 402 
TYR   CE2 CZ   sing Y N 403 
TYR   CE2 HE2  sing N N 404 
TYR   CZ  OH   sing N N 405 
TYR   OH  HH   sing N N 406 
TYR   OXT HXT  sing N N 407 
VAL   N   CA   sing N N 408 
VAL   N   H    sing N N 409 
VAL   N   H2   sing N N 410 
VAL   CA  C    sing N N 411 
VAL   CA  CB   sing N N 412 
VAL   CA  HA   sing N N 413 
VAL   C   O    doub N N 414 
VAL   C   OXT  sing N N 415 
VAL   CB  CG1  sing N N 416 
VAL   CB  CG2  sing N N 417 
VAL   CB  HB   sing N N 418 
VAL   CG1 HG11 sing N N 419 
VAL   CG1 HG12 sing N N 420 
VAL   CG1 HG13 sing N N 421 
VAL   CG2 HG21 sing N N 422 
VAL   CG2 HG22 sing N N 423 
VAL   CG2 HG23 sing N N 424 
VAL   OXT HXT  sing N N 425 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002329 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7HUV 
_atom_sites.fract_transf_matrix[1][1]   0.013732 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000679 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016259 
_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]   0.030627 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 18.990 6.516   24.257 1.00 36.17 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.161 6.614   23.378 1.00 35.90 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.235 5.451   22.384 1.00 33.80 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.521 4.451   22.547 1.00 34.08 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.440 6.698   24.213 1.00 38.74 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.474 5.607   25.116 1.00 42.03 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.060 5.603   21.347 1.00 30.92 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.259 4.567   20.344 1.00 29.03 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.546 5.123   18.958 1.00 28.07 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.139 6.245   18.634 1.00 27.16 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.248 4.347   18.128 1.00 27.06 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.608 4.784   16.777 1.00 26.42 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.621 3.608   15.775 1.00 25.30 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.641 2.461   16.198 1.00 25.55 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.995 5.429   16.817 1.00 26.75 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.623 3.901   14.460 1.00 23.98 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.748 2.935   13.372 1.00 23.29 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.120 3.157   12.738 1.00 24.89 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.505 4.287   12.477 1.00 24.41 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.657 3.161   12.299 1.00 22.86 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.260 3.121   12.893 1.00 21.42 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.818 2.193   11.126 1.00 24.56 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.243 3.781   11.924 1.00 21.36 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.898 2.084   12.566 1.00 26.79 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.231 2.172   12.005 1.00 28.68 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.225 1.403   10.719 1.00 31.13 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.077 0.183   10.748 1.00 32.91 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.214 1.541   12.983 1.00 28.68 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.347 2.335   14.252 1.00 29.18 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.169 3.453   14.311 1.00 30.01 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.593 2.025   15.371 1.00 29.70 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.290 4.199   15.474 1.00 30.63 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.690 2.777   16.536 1.00 30.95 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.535 3.869   16.578 1.00 31.41 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.631 4.620   17.714 1.00 31.49 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.315 2.099   9.597  1.00 31.38 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.273 1.499   8.266  1.00 32.19 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.374 2.136   7.421  1.00 33.20 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.430 3.361   7.275  1.00 33.40 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.873 1.656   7.610  1.00 33.76 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.362 3.092   7.705  1.00 33.45 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.895 1.183   6.162  1.00 36.03 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.289 1.310   6.904  1.00 33.06 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.424 1.809   6.141  1.00 34.40 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.256 2.795   6.945  1.00 36.41 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.467 2.587   8.146  1.00 37.64 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.566 3.945   6.357  1.00 36.26 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.308 4.997   7.048  1.00 36.55 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.367 6.062   7.678  1.00 34.39 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.776 7.194   7.920  1.00 34.43 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.309 5.626   6.106  1.00 40.81 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.521 4.757   5.926  1.00 49.03 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.011 4.143   6.883  1.00 51.86 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 34.045 4.692   4.704  1.00 51.51 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.130 5.668   8.011  1.00 32.43 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.152 6.586   8.601  1.00 30.85 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.638 6.124   9.956  1.00 29.24 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.505 4.923   10.207 1.00 29.64 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.923 6.716   7.667  1.00 29.96 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.260 7.281   6.309  1.00 30.78 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.882 8.518   6.185  1.00 31.91 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.984 6.570   5.150  1.00 31.35 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.227 9.030   4.940  1.00 33.40 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.298 7.084   3.896  1.00 32.97 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.903 8.326   3.795  1.00 34.89 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.230 8.858   2.561  1.00 37.78 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.246 7.110   10.788 1.00 27.13 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.604 6.905   12.076 1.00 25.28 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.312 7.734   12.028 1.00 23.69 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.338 8.928   11.764 1.00 22.99 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.523 7.328   13.239 1.00 26.23 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.817 7.583   14.579 1.00 27.90 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.815 7.838   15.699 1.00 30.95 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.362 8.886   16.614 1.00 32.82 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.817 8.663   17.805 1.00 34.32 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.665 7.418   18.252 1.00 32.72 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.416 9.682   18.561 1.00 32.48 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.155 7.075   12.227 1.00 22.77 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.850 7.747   12.189 1.00 22.10 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.323 7.882   13.602 1.00 22.30 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.167 6.861   14.275 1.00 22.15 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.846 6.945   11.366 1.00 21.26 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.524 7.744   11.198 1.00 21.06 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.434 6.541   10.001 1.00 20.67 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.983 9.109   14.041 1.00 21.44 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.523 9.308   15.427 1.00 21.45 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.328 10.263  15.448 1.00 20.86 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.110 10.991  14.472 1.00 20.71 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.656 9.895   16.345 1.00 23.90 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.702 8.860   16.693 1.00 27.20 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.282 11.153  15.725 1.00 23.33 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.578 10.325  16.576 1.00 19.77 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.532 11.362  16.708 1.00 19.73 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.264 12.725  16.720 1.00 20.87 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.269 12.878  17.447 1.00 22.35 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.768 11.258  18.042 1.00 20.37 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.951 9.991   18.134 1.00 22.71 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.447 8.945   18.593 1.00 23.91 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.698 10.070  17.692 1.00 21.34 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.786 13.679  15.919 1.00 20.87 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.467 14.988  15.856 1.00 20.19 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.515 15.677  17.213 1.00 21.45 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.543 16.281  17.555 1.00 22.99 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.829 15.864  14.778 1.00 19.93 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.626 17.133  14.393 1.00 20.23 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.654 18.021  13.601 1.00 21.49 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.239 19.277  13.096 1.00 22.32 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.251 20.417  13.782 1.00 24.86 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.797 20.455  15.030 1.00 22.71 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.725 21.531  13.226 1.00 25.87 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.462 15.503  18.043 1.00 21.07 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.435 16.150  19.361 1.00 23.13 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.389 15.530  20.395 1.00 26.19 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.655 16.152  21.447 1.00 28.06 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.009 16.250  19.908 1.00 24.35 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.431 14.973  20.422 1.00 24.50 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.815 14.060  19.577 1.00 25.65 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.336 14.522  21.700 1.00 25.11 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.390 13.073  20.368 1.00 26.57 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.674 13.315  21.654 1.00 25.87 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.003 14.388  20.051 1.00 25.84 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.963 13.720  20.908 1.00 26.86 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.396 13.740  20.310 1.00 27.18 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.307 13.142  20.896 1.00 27.71 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.487 12.272  21.164 1.00 26.85 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.141 12.160  21.918 1.00 27.39 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.735 10.697  22.136 1.00 27.04 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.188 12.894  23.265 1.00 26.67 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.593 14.356  19.110 1.00 26.50 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.905 14.392  18.479 1.00 27.15 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.941 15.060  19.395 1.00 27.77 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.591 15.973  20.139 1.00 27.76 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.839 15.127  17.155 1.00 26.71 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.179 14.555  19.382 1.00 28.80 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.284 15.031  20.217 1.00 29.77 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.150 16.110  19.473 1.00 30.17 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.969 16.332  18.280 1.00 29.55 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.171 13.819  20.617 1.00 31.43 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.893 13.403  19.453 1.00 32.54 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.365 12.654  21.179 1.00 32.48 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.174 16.698  20.153 1.00 30.48 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.085 17.636  19.484 1.00 32.21 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.800 16.953  18.312 1.00 32.48 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.945 17.554  17.246 1.00 32.57 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.147 18.171  20.471 1.00 35.48 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.561 18.958  21.590 1.00 43.02 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 29.753 20.049  21.351 1.00 46.68 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.713 18.806  22.929 1.00 46.14 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.419 20.517  22.545 1.00 48.10 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 29.973 19.802  23.525 1.00 47.92 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.257 15.697  18.523 1.00 32.22 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.947 14.924  17.493 1.00 32.38 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.032 14.700  16.305 1.00 30.29 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.462 14.859  15.169 1.00 30.53 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.429 13.587  18.033 1.00 36.27 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.171 12.785  16.975 1.00 45.50 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.240 13.193  16.496 1.00 47.93 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.568 11.682  16.527 1.00 47.66 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.759 14.346  16.546 1.00 28.74 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.789 14.204  15.445 1.00 27.35 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.707 15.499  14.606 1.00 26.52 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.822 15.442  13.382 1.00 27.03 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.399 13.870  15.976 1.00 26.47 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.238 12.440  16.465 1.00 29.37 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.820 11.538  15.846 1.00 29.41 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.528 12.238  17.470 1.00 29.78 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.563 16.667  15.266 1.00 25.57 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.476 17.940  14.522 1.00 26.39 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.805 18.321  13.814 1.00 28.91 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.758 18.902  12.731 1.00 29.74 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.975 19.073  15.440 1.00 26.14 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.488 19.087  15.622 1.00 25.01 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.791 18.669  16.717 1.00 26.09 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.521 19.621  14.706 1.00 24.11 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.438 18.863  16.517 1.00 25.93 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.243 19.406  15.269 1.00 25.24 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.605 20.166  13.421 1.00 24.62 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.065 19.837  14.645 1.00 25.27 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.429 20.534  12.773 1.00 24.95 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.177 20.362  13.385 1.00 25.08 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.967 17.947  14.384 1.00 29.97 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.274 18.231  13.764 1.00 31.86 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.573 17.326  12.561 1.00 33.15 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.483 17.627  11.778 1.00 34.01 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.398 18.106  14.792 1.00 32.73 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.855 16.179  12.451 1.00 31.81 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.969 15.237  11.330 1.00 30.91 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.609 15.109  10.632 1.00 29.32 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.252 14.030  10.174 1.00 28.01 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.463 13.890  11.821 1.00 32.35 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.875 13.992  12.367 1.00 37.58 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.836 14.190  11.610 1.00 40.61 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.020 13.861  13.681 1.00 37.56 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.855 16.224  10.575 1.00 28.46 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.537 16.260  9.966  1.00 26.86 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.560 15.889  8.480  1.00 28.25 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.329 16.472  7.714  1.00 29.08 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.931 17.672  10.136 1.00 26.71 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.542 17.882  9.491  1.00 26.33 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.473 17.004  10.157 1.00 26.91 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.116 19.343  9.559  1.00 25.91 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.628 14.986  8.054  1.00 26.90 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.391 14.612  6.656  1.00 27.07 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.032 15.246  6.179  1.00 27.40 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.955 15.897  5.123  1.00 28.84 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.357 13.061  6.516  1.00 28.09 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.920 12.642  5.112  1.00 28.43 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.713 12.450  6.876  1.00 28.87 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.984 15.090  6.995  1.00 25.71 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.634 15.560  6.679  1.00 24.90 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.795 15.618  7.948  1.00 23.05 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.971 14.802  8.832  1.00 23.06 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.000 14.577  5.663  1.00 24.84 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.524 14.753  5.394  1.00 25.27 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.942 15.612  4.505  1.00 26.79 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.452 14.021  6.006  1.00 24.96 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.571 15.455  4.525  1.00 27.00 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.246 14.488  5.438  1.00 26.14 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.396 13.001  6.967  1.00 24.81 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.007 13.947  5.774  1.00 25.78 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.163 12.463  7.291  1.00 25.74 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.986 12.960  6.729  1.00 25.82 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.942 16.617  8.063  1.00 21.56 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.021 16.702  9.191  1.00 21.59 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.704 17.283  8.714  1.00 21.33 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.679 18.066  7.761  1.00 21.40 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.619 17.442  10.394 1.00 23.16 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.202 18.819  10.061 1.00 24.59 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.186 19.943  9.923  1.00 25.26 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.464 20.919  9.187  1.00 28.75 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.112 19.863  10.560 1.00 24.68 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.606 16.860  9.343  1.00 20.16 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.295 17.376  8.994  1.00 20.40 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.488 17.532  10.288 1.00 20.70 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.048 16.543  10.873 1.00 21.65 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.629 16.506  7.918  1.00 21.39 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.342 17.062  7.347  1.00 27.28 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.630 17.773  8.077  1.00 27.75 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.023 16.737  6.185  1.00 28.50 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.311 18.805  10.747 1.00 20.31 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.569 19.095  11.961 0.50 21.36 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.574 19.052  11.982 0.50 21.41 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.117 18.582  11.853 1.00 21.87 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.528 18.151  12.842 1.00 22.67 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.590 20.600  12.231 0.50 22.88 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.628 20.530  12.371 0.50 23.09 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.849 20.911  13.392 0.50 25.13 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.818 21.289  11.492 0.50 25.39 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.515 18.678  10.647 1.00 21.84 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.125 18.245  10.470 1.00 23.05 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.961 16.726  10.626 1.00 22.72 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.864 16.275  10.916 1.00 24.13 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.550 18.715  9.137  1.00 26.82 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.027 17.952  8.038  1.00 29.51 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.043 15.962  10.480 1.00 20.51 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.995 14.489  10.642 1.00 19.90 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.602 14.030  11.975 1.00 19.83 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.536 12.830  12.280 1.00 20.49 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.756 13.791  9.505  1.00 20.07 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.139 14.075  8.146  1.00 20.37 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.932 13.409  7.016  1.00 22.15 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.926 11.940  7.122  1.00 19.03 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.079 11.117  6.086  1.00 21.76 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.167 11.603  4.846  1.00 22.59 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.047 9.793   6.269  1.00 21.87 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.253 14.937  12.722 1.00 19.25 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.999 14.585  13.954 1.00 17.70 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.142 13.627  13.646 1.00 17.69 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.442 12.782  14.475 1.00 18.61 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.096 14.057  15.105 1.00 19.34 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.827 13.772  16.412 1.00 21.70 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.644 14.611  16.824 1.00 22.81 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.579 12.679  17.028 1.00 22.53 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.776 13.725  12.439 1.00 17.18 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.919 12.881  12.083 1.00 16.88 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.191 13.691  11.851 1.00 18.38 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.148 14.813  11.353 1.00 20.55 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.684 12.100  10.784 1.00 16.57 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.617 10.973  10.883 1.00 17.91 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.495 10.259  9.504  1.00 18.38 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.020 9.940   11.972 1.00 19.21 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.335 13.054  12.158 1.00 17.75 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.668 13.594  11.883 1.00 19.02 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.543 12.391  11.512 1.00 20.56 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.482 11.354  12.189 1.00 21.84 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.304 14.312  13.095 1.00 19.83 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.649 14.979  12.768 1.00 21.36 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.792 16.309  13.529 1.00 20.79 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.849 14.092  13.216 1.00 22.72 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.357 12.516  10.461 1.00 20.56 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.313 11.485  10.040 1.00 21.59 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.722 12.113  10.116 1.00 23.97 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.961 13.224  9.599  1.00 23.87 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.010 10.965  8.609  1.00 22.64 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.054 9.924   8.144  1.00 23.74 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.600 10.359  8.564  1.00 22.12 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.607 11.424  10.814 1.00 24.38 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.002 11.845  10.916 1.00 25.81 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.895 10.755  10.305 1.00 28.18 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.479 9.609   10.163 1.00 27.49 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.396 12.128  12.364 1.00 26.35 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.253 10.976  13.180 1.00 26.48 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.146 11.117  9.957  1.00 30.07 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.072 10.144  9.381  1.00 33.09 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.890 9.430   10.469 1.00 36.01 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.139 9.982   11.537 1.00 36.39 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 31.993 10.829  8.376  1.00 35.47 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.709 11.879  9.004  1.00 39.01 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.302 8.199   10.201 1.00 38.17 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.070 7.410   11.164 1.00 40.94 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.350 6.916   10.499 1.00 45.28 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.389 6.762   9.275  1.00 46.17 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.259 6.177   11.613 1.00 41.33 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.137 5.295   10.504 1.00 42.20 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.877 6.529   12.144 1.00 40.75 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.354 6.577   11.303 1.00 47.59 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.589 6.003   10.776 1.00 50.47 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.405 4.471   10.658 1.00 52.76 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.867 3.855   9.686  1.00 55.01 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.775 6.390   11.678 1.00 51.98 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.453 6.078   13.039 1.00 53.30 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.131 7.857   11.572 1.00 52.79 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.771 3.843   11.661 1.00 52.04 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.564 2.392   11.634 1.00 52.48 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.359 2.060   10.767 1.00 52.30 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.386 2.811   10.753 1.00 52.25 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.373 1.857   13.045 1.00 52.85 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.443 0.978   9.996  1.00 52.30 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.357 0.562   9.109  1.00 52.70 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.201 -0.070  9.899  1.00 51.46 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.439 -0.811  10.851 1.00 52.37 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.878 -0.393  8.020  1.00 55.76 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.069 -0.339  6.721  1.00 61.62 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.496 0.795   5.809  1.00 67.69 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 34.605 1.347   5.925  1.00 70.18 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.628 1.167   4.865  1.00 67.59 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.970 0.224   9.480  1.00 49.04 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.725 -0.246  10.085 1.00 47.89 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.075 -1.397  9.338  1.00 45.63 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.153 -1.476  8.107  1.00 45.94 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.397 -2.281  10.070 1.00 43.09 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.855 -3.486  9.469  1.00 41.68 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.373 -3.665  9.566  1.00 38.53 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.920 -4.777  9.277  1.00 38.34 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.573 -4.700  10.031 1.00 44.14 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.296 -4.784  9.547  1.00 54.16 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.610 -2.618  9.939  1.00 35.57 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.147 -2.741  9.992  1.00 34.81 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.608 -2.713  8.567  1.00 34.15 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.165 -2.044  7.691  1.00 35.13 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.490 -1.591  10.793 1.00 37.27 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.698 -1.661  12.290 1.00 42.02 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.763 -2.776  12.821 1.00 43.37 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.781 -0.588  12.935 1.00 43.05 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.532 -3.420  8.341  1.00 32.90 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.888 -3.481  7.034  1.00 33.47 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.654 -2.618  7.069  1.00 31.13 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.852 -2.794  7.987  1.00 30.98 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.461 -4.931  6.748  1.00 37.05 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.660 -5.685  6.556  1.00 38.80 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.596 -5.046  5.490  1.00 37.53 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.485 -1.699  6.103  1.00 29.04 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.267 -0.886  6.083  1.00 27.98 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.215 -1.609  5.240  1.00 27.23 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.544 -2.102  4.147  1.00 28.19 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.536 0.529   5.529  1.00 27.94 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.744 1.197   6.227  1.00 28.26 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.267 1.416   5.594  1.00 28.01 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.532 1.374   7.753  1.00 28.46 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.970 -1.684  5.732  1.00 25.35 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.883 -2.306  4.979  1.00 25.13 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.504 -1.386  3.808  1.00 25.49 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.487 -0.179  3.981  1.00 24.41 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.666 -2.489  5.887  1.00 24.36 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.143 -1.963  2.647  1.00 27.16 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.666 -1.244  1.466  1.00 28.66 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.322 -1.917  1.124  1.00 29.53 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.288 -2.916  0.396  1.00 30.51 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.690 -1.337  0.325  1.00 29.77 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.083 -0.791  0.680  1.00 30.48 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.121 0.699   1.144  1.00 31.65 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.494 1.122   1.443  1.00 32.38 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.816 2.233   2.101  1.00 32.21 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.872 3.074   2.501  1.00 30.23 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.087 2.519   2.350  1.00 30.02 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.228 -1.405  1.715  1.00 28.52 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.922 -2.066  1.670  1.00 28.48 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.777  -1.119  2.122  1.00 30.07 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.030 0.010   2.561  1.00 29.33 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.002 -3.250  2.632  1.00 27.20 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.102 -2.737  4.379  1.00 27.64 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.523  -1.661  2.156  1.00 31.37 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.399  -0.924  2.702  1.00 32.37 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.720  -1.736  3.794  1.00 32.15 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.510  -1.639  3.940  1.00 33.07 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.390  -0.428  1.633  1.00 36.19 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.584  -1.506  0.955  1.00 44.10 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.831  -2.704  1.235  1.00 45.55 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.694  -1.158  0.132  1.00 49.13 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.488  -2.537  4.582  1.00 30.09 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 6.975  -3.302  5.728  1.00 27.79 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.258  -2.350  6.676  1.00 26.36 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.709  -1.220  6.871  1.00 26.50 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.108  -3.999  6.493  1.00 27.31 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.752  -5.508  5.726  1.00 28.57 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.208  -2.813  7.289  1.00 23.65 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.522  -2.094  8.335  1.00 23.38 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.464  -2.901  9.608  1.00 21.87 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.583  -2.653  10.433 1.00 22.21 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.111  -1.632  7.922  1.00 25.65 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.077  -0.372  7.046  1.00 29.49 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.637  0.057   6.784  1.00 32.92 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.097  -0.076  5.675  1.00 35.01 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.962  0.524   7.828  1.00 33.39 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.334  -3.951  9.758  1.00 20.34 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.416  -4.739  10.997 1.00 20.42 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.914  -4.932  11.243 1.00 18.70 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.702  -5.050  10.316 1.00 17.91 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.736  -6.160  10.937 1.00 23.79 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.390  -6.923  9.920  1.00 25.23 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.244  -6.106  10.651 1.00 24.83 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.292  -4.961  12.495 1.00 17.14 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.683  -5.153  12.873 1.00 17.90 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.836  -5.260  14.370 1.00 17.56 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.869  -5.469  15.058 1.00 17.40 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.051 -5.184  14.869 1.00 17.03 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.357 -5.297  16.301 1.00 16.76 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.258 -4.109  16.694 1.00 17.27 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.238 -3.826  15.996 1.00 18.27 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.066 -6.657  16.551 1.00 18.25 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.547 -6.778  18.014 1.00 19.93 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.117 -7.804  16.212 1.00 18.61 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.983 -3.486  17.858 1.00 16.87 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.844 -2.391  18.324 1.00 16.11 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.384 -2.633  19.712 1.00 17.60 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.769 -3.350  20.488 1.00 16.99 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.144 -0.994  18.216 1.00 15.31 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.215 -0.670  19.366 1.00 16.65 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.945  -1.233  19.442 1.00 17.27 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.615 0.183   20.391 1.00 18.05 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 8.056  -0.858  20.456 1.00 18.53 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.757  0.510   21.444 1.00 19.23 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.491  -0.044  21.489 1.00 19.23 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.639  0.263   22.519 1.00 19.73 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.542 -2.047  20.007 1.00 17.45 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.139 -2.187  21.322 1.00 19.20 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.679 -1.019  22.192 1.00 19.74 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.840 0.151   21.815 1.00 18.71 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.673 -2.210  21.246 1.00 19.71 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.269 -2.372  22.627 1.00 21.21 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.041 -3.524  23.369 1.00 22.14 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.967 -1.336  23.232 1.00 23.55 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.547 -3.666  24.664 1.00 24.52 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.475 -1.465  24.524 1.00 25.46 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.266 -2.633  25.230 1.00 26.51 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.764 -2.731  26.517 1.00 29.11 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.136 -1.342  23.388 1.00 21.15 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.664 -0.343  24.344 1.00 22.76 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.572 -0.392  25.581 1.00 23.93 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.415 -1.257  26.466 1.00 24.50 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.199 -0.608  24.696 1.00 24.27 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.539 0.422   26.041 1.00 25.09 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.535 0.567   25.665 1.00 24.07 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.456 0.581   26.789 1.00 24.99 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.793 0.733   28.144 1.00 24.81 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.271 0.114   29.082 1.00 26.68 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.524 1.659   26.617 1.00 29.76 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 15.916 2.935   26.564 1.00 36.44 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.673 1.485   28.256 1.00 23.77 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.998 1.672   29.568 1.00 25.08 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.296 0.420   30.096 1.00 26.38 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.809 0.422   31.250 1.00 28.49 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 12.015 2.834   29.531 1.00 25.57 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.946 2.561   28.632 1.00 29.12 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.286 -0.660  29.290 1.00 26.27 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.751 -1.936  29.715 1.00 26.34 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.790 -3.085  29.521 1.00 28.37 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.488 -4.220  29.876 1.00 28.72 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.489 -2.270  28.901 1.00 27.29 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.297  -1.369  29.150 1.00 29.83 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.649  -1.635  30.484 1.00 32.34 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.460  -0.803  30.666 1.00 36.79 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.448  0.363   31.304 1.00 38.58 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.574  0.865   31.810 1.00 37.77 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.318  1.049   31.421 1.00 36.93 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 13.983 -2.802  28.913 1.00 28.97 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.017 -3.801  28.599 1.00 30.12 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.388 -4.983  27.819 1.00 29.67 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.638 -6.169  28.112 1.00 30.00 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.754 -4.265  29.870 1.00 32.28 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.747 -3.236  30.419 1.00 37.59 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.547 -3.839  31.566 1.00 43.57 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.196 -2.835  32.411 1.00 50.30 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.143 -2.833  33.743 1.00 54.89 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.455 -3.770  34.391 1.00 54.95 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.740 -1.868  34.438 1.00 56.46 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.500 -4.630  26.860 1.00 27.37 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.753 -5.615  26.073 1.00 26.36 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.575 -5.172  24.631 1.00 24.96 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.492 -3.968  24.342 1.00 25.45 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.319 -5.765  26.619 1.00 28.43 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.138 -6.664  27.841 1.00 35.24 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.689  -6.549  28.297 1.00 41.26 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.252  -7.641  29.236 1.00 48.03 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.412  -7.254  30.660 1.00 51.30 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.392 -6.160  23.767 1.00 22.76 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.032 -5.928  22.367 1.00 21.07 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.529 -6.207  22.277 1.00 22.20 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 9.988  -7.139  22.934 1.00 23.91 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.798 -6.880  21.428 1.00 21.63 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.288 -6.669  21.430 1.00 21.18 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 14.931 -5.988  20.403 1.00 24.29 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.215 -7.074  22.325 1.00 21.62 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.221 -6.029  20.697 1.00 22.96 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.437 -6.623  21.864 1.00 23.54 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.839  -5.398  21.470 1.00 20.58 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.399  -5.512  21.257 1.00 19.79 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.048  -5.590  19.795 1.00 19.55 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.531  -4.804  18.998 1.00 17.61 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.630  -4.304  21.848 1.00 20.96 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.666  -4.202  23.356 1.00 22.49 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.825  -4.976  24.148 1.00 24.58 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.504  -3.296  23.992 1.00 24.38 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.833  -4.863  25.542 1.00 26.10 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.538  -3.194  25.383 1.00 25.26 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.707  -3.983  26.154 1.00 27.03 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.703  -3.821  27.529 1.00 28.83 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.195  -6.544  19.413 1.00 19.10 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.689  -6.563  18.025 1.00 18.10 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.587  -5.481  17.865 1.00 19.49 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.726  -5.341  18.750 1.00 21.01 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.091  -7.970  17.889 1.00 18.96 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.679  -8.339  19.265 1.00 20.09 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.557  -7.584  20.255 1.00 18.89 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.596  -4.756  16.763 1.00 18.97 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.621  -3.691  16.504 1.00 19.52 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.153  -3.629  15.052 1.00 19.55 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.901  -3.938  14.131 1.00 20.61 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.221  -2.285  16.840 1.00 20.12 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.318  -2.059  18.352 1.00 21.35 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.572  -2.068  16.156 1.00 20.12 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 2.947  -3.093  14.859 1.00 19.67 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.444  -2.674  13.551 1.00 20.65 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.665  -1.151  13.553 1.00 21.21 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.421  -0.511  14.577 1.00 23.20 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 0.946  -2.945  13.408 1.00 25.16 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.719  -4.345  13.414 1.00 32.26 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.161  -0.585  12.456 1.00 20.06 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.449  0.859   12.441 1.00 20.45 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.930  1.510   11.191 1.00 22.64 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.757  0.839   10.163 1.00 23.42 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.953  1.155   12.696 1.00 20.22 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.929  0.407   11.807 1.00 20.04 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.403  -0.842  12.169 1.00 20.75 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.374  0.964   10.608 1.00 20.68 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.307  -1.522  11.367 1.00 20.91 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.279  0.283   9.801  1.00 21.34 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.719  -0.973  10.167 1.00 21.07 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.650  2.842   11.267 1.00 22.13 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.068  3.518   10.133 1.00 22.07 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.126  3.829   9.037  1.00 22.00 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.319  3.710   9.300  1.00 22.24 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.338  4.776   10.611 1.00 24.66 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.265  5.688   11.179 1.00 26.37 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.707  4.171   7.785  1.00 23.16 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.704  4.556   6.764  1.00 24.77 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.312  5.930   7.130  1.00 25.97 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.664  6.719   7.804  1.00 27.43 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.097  4.574   5.334  1.00 28.81 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.899  3.144   4.783  1.00 34.35 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.314  3.127   3.367  1.00 41.06 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.165  1.702   2.870  1.00 47.36 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.874  1.645   1.407  1.00 51.36 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.557  6.226   6.711  1.00 25.14 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.160  7.537   7.063  1.00 26.00 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.306  8.725   6.623  1.00 26.66 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.812  8.772   5.476  1.00 27.03 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.511  7.546   6.341  1.00 27.86 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.766  6.145   5.893  1.00 28.20 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.450  5.394   5.882  1.00 25.26 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.086  9.669   7.537  1.00 26.84 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.212  10.807  7.221  1.00 28.32 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.497  12.011  8.148  1.00 28.03 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.367  11.926  9.028  1.00 26.36 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.743  10.366  7.254  1.00 32.17 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.353  10.030  8.567  1.00 36.02 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.851  13.171  7.867  1.00 28.42 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 4.034  14.383  8.661  1.00 28.73 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.059  14.249  9.801  1.00 30.23 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.841  14.112  9.564  1.00 31.37 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.605  15.624  7.845  1.00 29.70 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.603  16.250  6.941  1.00 32.59 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.886  17.212  5.977  1.00 34.63 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.631  17.019  7.734  1.00 32.90 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.572  14.274  11.027 1.00 29.16 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.774  14.101  12.220 1.00 30.48 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.099  15.237  13.188 1.00 32.71 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.274  15.576  13.373 1.00 32.15 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.141  12.724  12.827 1.00 31.43 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.638  11.584  11.912 1.00 33.06 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.642  12.577  14.270 1.00 32.48 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 3.095  10.286  12.264 1.00 34.93 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.057  15.821  13.817 1.00 34.61 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.280  16.882  14.790 1.00 38.01 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 2.960  16.345  16.061 1.00 38.17 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.566  15.323  16.608 1.00 39.20 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 0.967  17.619  15.135 1.00 40.22 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.198  18.953  15.808 1.00 42.87 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.546  20.064  15.072 1.00 44.96 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 1.099  19.079  17.183 1.00 44.46 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 1.783  21.288  15.697 1.00 46.46 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 1.309  20.303  17.803 1.00 45.55 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.644  21.400  17.059 1.00 46.02 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 4.039  16.986  16.471 1.00 37.37 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.792  16.595  17.651 1.00 37.86 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 4.790  17.790  18.595 1.00 38.90 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.193  18.906  18.200 1.00 38.81 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.248  16.157  17.298 1.00 37.89 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 7.057  15.870  18.559 1.00 38.05 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.251  14.951  16.380 1.00 38.21 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 4.372  17.550  19.841 1.00 39.59 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 4.298  18.576  20.891 1.00 41.52 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 5.627  19.252  21.117 1.00 41.64 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 6.666  18.611  20.987 1.00 41.75 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 3.888  17.928  22.218 1.00 45.56 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.527  17.278  22.175 1.00 54.27 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.401  18.284  22.256 1.00 65.48 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 0.957  18.574  23.390 1.00 67.78 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 0.974  18.797  21.195 1.00 69.81 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 5.604  20.537  21.526 1.00 41.40 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 6.826  21.276  21.851 1.00 42.03 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 7.584  20.576  22.979 1.00 42.78 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 6.968  19.977  23.870 1.00 43.40 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 6.483  22.704  22.286 1.00 42.19 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 8.905  20.591  22.888 1.00 42.60 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 9.815  20.005  23.867 1.00 43.03 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 10.968 20.994  24.108 1.00 43.88 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 11.007 22.051  23.466 1.00 44.16 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 10.362 18.674  23.339 1.00 43.28 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.339 18.871  22.329 1.00 43.83 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 11.946 20.643  24.976 1.00 43.60 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 13.118 21.503  25.169 1.00 43.32 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 14.065 21.509  23.960 1.00 41.03 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 14.992 22.305  23.928 1.00 40.92 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 13.896 21.101  26.430 1.00 48.57 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 13.118 21.295  27.722 1.00 57.03 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 13.036 20.055  28.592 1.00 66.90 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 12.787 20.201  29.810 1.00 68.61 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 13.221 18.937  28.055 1.00 70.83 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 13.865 20.601  22.979 1.00 38.88 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 14.724 20.509  21.800 1.00 36.95 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.092 21.178  20.574 1.00 34.42 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 14.806 21.698  19.721 1.00 34.26 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.055 19.032  21.490 1.00 36.64 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.612 18.275  22.678 1.00 37.44 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 16.965 18.327  22.992 1.00 38.63 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 14.788 17.500  23.481 1.00 38.68 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.481 17.630  24.082 1.00 40.23 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 15.294 16.787  24.562 1.00 40.10 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.642 16.849  24.858 1.00 41.98 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 17.129 16.128  25.933 1.00 45.18 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 12.757 21.141  20.466 1.00 33.17 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.079 21.760  19.328 1.00 32.16 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 10.815 22.490  19.752 1.00 33.80 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.157 22.075  20.702 1.00 33.81 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.658 20.692  18.289 1.00 30.13 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.747 19.782  17.777 1.00 27.14 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 13.554 20.163  16.713 1.00 26.23 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 12.869 18.475  18.249 1.00 26.24 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.522 19.308  16.198 1.00 25.71 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 13.820 17.601  17.723 1.00 24.35 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.628 18.010  16.682 1.00 24.83 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.637 17.180  16.213 1.00 22.36 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.399 23.523  18.991 1.00 34.62 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.056  24.086  19.231 1.00 35.74 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 7.997  23.073  18.697 1.00 36.92 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.347  22.082  18.008 1.00 37.34 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.066  25.374  18.396 1.00 36.46 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.011 25.076  17.249 1.00 36.09 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.047 24.099  17.787 1.00 34.24 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.699  23.316  18.959 1.00 37.39 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.642  22.443  18.441 1.00 37.92 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.679  22.511  16.892 1.00 37.58 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 5.824  23.601  16.332 1.00 37.91 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.291  22.895  18.981 1.00 38.65 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.724  21.348  16.224 1.00 36.30 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 5.910  21.327  14.774 1.00 35.08 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.428  20.011  14.142 1.00 34.02 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.142  19.045  14.859 1.00 34.03 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.421  21.499  14.493 1.00 34.75 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.224  20.207  14.794 1.00 33.53 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.665  20.438  15.139 1.00 31.71 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.550 19.350  14.689 1.00 31.23 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.657 18.169  15.290 1.00 31.82 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.521 17.264  14.841 1.00 26.33 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 9.915  17.889  16.355 1.00 33.24 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.401  19.961  12.794 1.00 33.28 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.144  18.701  12.121 1.00 33.36 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.518  18.064  11.911 1.00 30.73 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.418  18.711  11.364 1.00 30.04 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.534  18.901  10.740 1.00 35.20 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.095  19.355  10.732 1.00 38.72 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.058  18.439  10.642 1.00 40.41 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.775  20.704  10.715 1.00 40.92 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 0.728  18.856  10.580 1.00 42.62 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.455  21.133  10.641 1.00 42.39 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.434  20.208  10.575 1.00 44.17 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.870 20.650  10.489 1.00 47.11 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.680  16.810  12.340 1.00 27.89 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.904  16.039  12.086 1.00 24.50 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.581  15.158  10.867 1.00 23.78 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.530  14.513  10.830 1.00 23.90 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.282  15.179  13.299 1.00 24.20 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.501  14.250  13.030 1.00 23.55 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.209 13.772  14.278 1.00 24.54 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.406 14.524  15.242 1.00 24.61 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.688 12.526  14.254 1.00 22.85 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.430  15.184  9.852  1.00 22.04 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.201  14.430  8.623  1.00 21.70 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.893  13.043  8.712  1.00 20.94 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.764  12.822  9.595  1.00 20.41 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.778  15.208  7.447  1.00 23.03 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.182 15.374  7.575  1.00 24.83 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.437  12.097  7.850  1.00 21.04 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.026  10.766  7.774  1.00 20.23 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.911  10.013  9.100  1.00 19.92 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.767  9.204   9.410  1.00 19.98 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.491 10.872  7.322  1.00 20.20 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.649 11.483  5.952  1.00 24.66 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.696 10.692  4.813  1.00 27.42 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.715 12.788  5.579  1.00 26.54 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.802 11.528  3.787  1.00 27.72 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.801 12.799  4.194  1.00 28.05 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.832  10.256  9.849  1.00 20.39 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.606  9.647   11.162 1.00 20.16 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.537  8.543   11.045 1.00 20.02 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.547  8.720   10.329 1.00 21.26 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.118  10.742  12.139 1.00 20.07 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.959  10.345  13.625 1.00 20.63 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.255  9.864   14.195 1.00 20.31 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.383  11.542  14.456 1.00 22.93 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.747  7.440   11.778 1.00 18.87 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.850  6.258   11.759 1.00 18.69 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.411  5.989   13.174 1.00 19.70 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.278  5.907   14.044 1.00 20.47 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.661  5.038   11.258 1.00 19.21 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.147  5.224   9.800  1.00 21.93 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.259  3.935   9.233  1.00 25.23 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.647  4.120   10.379 1.00 22.95 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.100  5.850   13.438 1.00 19.81 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.644  5.584   14.793 1.00 20.74 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.197  4.140   14.959 1.00 21.29 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.660  3.527   14.028 1.00 21.31 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.428  6.470   15.155 1.00 21.74 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.651  7.982   15.218 1.00 25.24 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.376  8.692   15.736 1.00 27.65 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.799  8.322   16.102 1.00 24.62 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.300  3.670   16.194 1.00 20.68 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.845  2.361   16.625 1.00 20.92 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.286  2.536   18.047 1.00 20.91 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.625  3.499   18.735 1.00 21.77 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.024  1.374   16.665 1.00 22.01 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.470  1.591   18.487 1.00 21.02 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.999  1.563   19.859 1.00 22.30 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 2.089  0.826   20.653 1.00 24.05 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.402  -0.339  20.360 1.00 24.04 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.342 0.819   19.947 1.00 23.24 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.773 0.698   21.388 1.00 24.49 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.412 1.551   19.131 1.00 24.02 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.675  1.500   21.630 1.00 24.25 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.755  0.917   22.410 1.00 25.28 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.373  1.891   23.389 1.00 25.38 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 4.054  3.087   23.379 1.00 26.24 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 5.266  1.379   24.244 1.00 24.25 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.891  2.189   25.268 1.00 24.88 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 7.123  2.908   24.782 1.00 24.14 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.977  2.321   24.115 1.00 23.85 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 6.236  1.323   26.484 1.00 25.65 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.668  2.138   27.651 1.00 29.26 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.789  3.017   28.282 1.00 32.46 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.896  2.278   28.208 1.00 30.65 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.491  3.601   29.250 1.00 33.32 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.758  3.177   29.256 1.00 32.93 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 7.219  4.177   25.105 1.00 24.23 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.367  4.989   24.744 1.00 25.24 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.449  6.159   25.705 1.00 27.94 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 7.499  6.949   25.778 1.00 28.76 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.231  5.495   23.313 1.00 26.03 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 9.173  6.517   22.984 1.00 28.37 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.528  6.235   26.510 1.00 28.78 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 9.801  7.371   27.376 1.00 31.07 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 11.129 8.067   26.944 1.00 32.79 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.833 7.540   26.084 1.00 33.40 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 9.705  7.041   28.875 1.00 33.58 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 10.160 5.682   29.312 1.00 38.46 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 9.762  5.409   30.751 1.00 42.32 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 10.307 6.084   31.652 1.00 40.78 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 8.905  4.531   30.986 1.00 42.95 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 11.417 9.321   27.378 1.00 34.46 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.527 10.094  26.757 1.00 34.85 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 13.840 9.360   26.378 1.00 33.33 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 14.332 9.475   25.229 1.00 34.19 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 12.795 11.196  27.785 1.00 36.00 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 11.492 11.372  28.527 1.00 36.34 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 10.594 10.179  28.246 1.00 34.38 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.411 8.631   27.329 1.00 30.64 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.641 7.872   27.122 1.00 29.31 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.532 6.712   26.140 1.00 26.97 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.528 6.058   25.841 1.00 26.62 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.324 6.442   25.619 1.00 25.21 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 14.132 5.388   24.624 1.00 23.82 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.526 5.800   23.217 1.00 22.03 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.644 4.917   22.338 1.00 20.51 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.692 4.856   24.613 1.00 24.57 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.428 4.026   25.853 1.00 24.41 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.359 3.336   26.311 1.00 23.30 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.299 4.085   26.377 1.00 25.13 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.713 7.109   22.961 1.00 21.78 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 15.114 7.547   21.596 1.00 21.34 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.412 6.888   21.192 1.00 21.11 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.316 6.740   22.038 1.00 21.20 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.231 9.069   21.512 1.00 22.56 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.642 9.936   21.592 1.00 26.31 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.498 6.474   19.949 1.00 19.36 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.696 5.800   19.468 1.00 19.29 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.538 4.282   19.372 1.00 20.23 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.323 3.603   18.689 1.00 20.60 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.547 3.720   20.063 1.00 20.13 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.265 2.289   19.975 1.00 19.66 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.878 1.918   18.544 1.00 19.23 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.108 2.641   17.894 1.00 19.50 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.473 0.837   18.027 1.00 18.90 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.238 0.455   16.637 1.00 18.75 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 14.944 -0.302  16.442 1.00 18.85 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.575 -1.151  17.268 1.00 19.73 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.486 -0.329  16.119 1.00 20.98 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.675 0.635   15.846 1.00 23.26 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.190 -1.214  14.895 1.00 21.71 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 20.015 -0.113  15.480 1.00 26.06 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.288 -0.022  15.293 1.00 18.06 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.117 -0.744  14.790 1.00 16.79 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.621 -1.563  13.590 1.00 16.50 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.301 -1.021  12.696 1.00 16.05 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.043 0.245   14.294 1.00 16.17 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.859 -0.383  13.519 1.00 16.34 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 10.012 -1.336  14.405 1.00 16.84 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.934  0.742   12.966 1.00 17.75 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.337 -2.887  13.586 1.00 17.29 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.846 -3.751  12.510 1.00 18.50 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.744 -4.618  11.967 1.00 19.83 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.929 -5.102  12.720 1.00 19.34 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.890 -4.748  13.073 1.00 21.95 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.133 -4.212  13.720 1.00 29.21 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.027 -5.388  14.157 1.00 32.53 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 17.581 -6.013  12.963 1.00 38.12 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 18.738 -5.667  12.404 1.00 40.00 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.558 -4.822  13.022 1.00 38.99 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 19.112 -6.212  11.260 1.00 40.53 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.780 -4.892  10.670 1.00 21.88 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.869 -5.857  10.034 1.00 24.99 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.765 -7.019  9.488  1.00 28.65 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 13.988 -7.013  9.699  1.00 28.90 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.091 -5.174  8.909  1.00 24.71 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.138 -4.624  7.542  1.00 23.99 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.173 -7.993  8.755  1.00 30.99 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 12.960 -9.095  8.187  1.00 33.47 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.068 -8.611  7.228  1.00 33.69 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.057 -9.325  7.036  1.00 35.39 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.036 -10.085 7.441  1.00 37.91 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.170 -9.414  6.366  1.00 43.96 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.235 -10.374 5.656  1.00 51.29 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.035  -10.091 5.488  1.00 53.94 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.765 -11.518 5.204  1.00 50.57 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 13.921 -7.414  6.634  1.00 32.11 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.891 -6.888  5.665  1.00 31.05 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.063 -6.080  6.266  1.00 29.47 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.035 -5.771  5.563  1.00 30.61 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.174 -6.055  4.592  1.00 32.45 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 13.021 -6.765  3.927  1.00 36.60 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.709 -6.458  4.244  1.00 38.59 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 13.022 -7.686  2.930  1.00 38.28 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 10.952 -7.224  3.471  1.00 39.68 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.693 -7.988  2.664  1.00 39.61 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 15.974 -5.745  7.545  1.00 26.98 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.016 -4.960  8.196  1.00 24.23 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.488 -3.802  9.038  1.00 21.53 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.350 -3.826  9.469  1.00 21.79 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.315 -2.798  9.267  1.00 21.06 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 16.974 -1.613  10.049 1.00 20.85 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 15.969 -0.749  9.334  1.00 20.28 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.212 -0.342  8.184  1.00 21.41 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.231 -0.780  10.423 1.00 22.76 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.825 0.500   11.179 1.00 23.21 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.203 -1.611  11.257 1.00 23.80 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.877 -0.409  10.018 1.00 19.66 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.829 0.438   9.433  1.00 18.87 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 13.985 1.922   9.871  1.00 18.36 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.810 2.860   9.088  1.00 17.90 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.431 -0.107  9.862  1.00 20.07 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.324 0.855   9.448  1.00 20.31 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.174 -1.496  9.277  1.00 21.17 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.276 2.109   11.156 1.00 17.38 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.389 3.449   11.718 1.00 18.12 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.743 3.439   13.189 1.00 17.45 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.115 2.400   13.710 1.00 17.33 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.637 4.590   13.850 1.00 16.78 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 14.964 4.661   15.277 1.00 16.72 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.868 5.382   16.043 1.00 16.83 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.210 6.274   15.517 1.00 15.93 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.342 5.366   15.483 1.00 18.36 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.397 6.708   14.721 1.00 20.27 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.538 4.467   15.187 1.00 19.50 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.731 7.540   15.121 1.00 21.89 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.669 5.014   17.331 1.00 16.14 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.698 5.688   18.159 1.00 15.58 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 13.033 7.214   18.207 1.00 17.05 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.182 7.604   18.423 1.00 17.11 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.679 5.127   19.588 1.00 17.07 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.774 5.980   20.443 1.00 17.89 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.192 3.660   19.598 1.00 17.21 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 12.012 8.037   18.039 1.00 17.12 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.171 9.483   18.014 1.00 17.54 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.116 10.216  18.869 1.00 21.08 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.402 11.309  19.384 1.00 23.41 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.179 9.988   16.567 1.00 19.41 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.207 11.409  16.460 1.00 20.80 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.915  9.632   19.040 1.00 21.95 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.872  10.276  19.874 1.00 22.51 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 8.160  9.242   20.799 1.00 24.39 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.266  8.031   20.589 1.00 22.49 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.821  11.015  18.986 1.00 24.16 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 6.970  10.044  18.380 1.00 25.32 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 8.456  11.877  17.900 1.00 24.92 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.406  9.733   21.781 1.00 26.36 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.626  8.853   22.639 1.00 28.98 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.524  9.569   23.378 1.00 32.00 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 5.183  10.678  23.015 1.00 33.36 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.956  8.916   24.385 1.00 33.90 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.880  9.486   25.184 1.00 36.33 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.494  9.059   24.722 1.00 37.09 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 2.299  8.751   23.545 1.00 37.12 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.529  9.059   25.634 1.00 36.89 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 0.135  8.685   25.344 1.00 37.41 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.014 7.238   24.839 1.00 36.22 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -0.957 6.945   24.102 1.00 36.80 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.520 9.651   24.342 1.00 39.28 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.764 11.041  24.867 1.00 44.41 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -0.957 11.257  26.077 1.00 45.94 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -0.823 12.000  23.954 1.00 45.65 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.921  6.363   25.202 1.00 34.31 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.881  4.978   24.776 1.00 32.75 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.234  4.758   23.317 1.00 30.20 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.898  3.708   22.762 1.00 30.90 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.936  5.716   22.703 1.00 28.12 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.354  5.617   21.313 1.00 26.99 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.884  5.740   21.268 1.00 26.51 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.489  6.313   22.182 1.00 28.66 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.750  6.768   20.490 1.00 27.53 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.197  6.844   20.428 1.00 29.43 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.250 8.209   19.941 1.00 30.98 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.350 5.756   19.511 1.00 30.75 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.486  5.175   20.228 1.00 22.32 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.909  5.293   19.968 1.00 20.15 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 6.069  5.713   18.510 1.00 19.44 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.408  5.152   17.641 1.00 20.54 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.714  3.999   20.299 1.00 19.69 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.089  2.741   19.705 1.00 20.68 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.161  4.129   19.874 1.00 19.70 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.908  6.718   18.253 1.00 17.59 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.129  7.162   16.877 1.00 17.38 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.560  6.892   16.476 1.00 19.11 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.464  7.035   17.296 1.00 20.27 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.753  6.437   15.233 1.00 18.27 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 10.068 6.062   14.710 1.00 17.98 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.375 6.951   13.520 1.00 17.49 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.553  7.101   12.606 1.00 17.12 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 10.046 4.611   14.163 1.00 16.71 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.536  3.603   15.190 1.00 16.39 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.377 3.094   16.166 1.00 16.86 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.221  3.159   15.162 1.00 17.32 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.894  2.220   17.137 1.00 17.60 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.761  2.228   16.092 1.00 18.08 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.606  1.749   17.072 1.00 17.79 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.603 7.503   13.510 1.00 17.63 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.118 8.249   12.375 1.00 16.20 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.552 7.221   11.312 1.00 16.23 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.430 6.376   11.562 1.00 16.25 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.337 9.064   12.821 1.00 14.65 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.917 7.247   10.128 1.00 17.12 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.276 6.300   9.058  1.00 18.61 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.631 6.584   8.464  1.00 19.50 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 13.991 7.771   8.339  1.00 20.00 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.220 6.364   7.927  1.00 21.55 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.419 5.330   6.823  1.00 25.06 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.563 4.153   7.140  1.00 24.23 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.479 5.725   5.636  1.00 27.53 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.402 5.514   8.078  1.00 17.47 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.680 5.743   7.378  1.00 18.23 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.707 5.007   6.018  1.00 19.87 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.707 5.116   5.317  1.00 22.11 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 16.936 5.391   8.217  1.00 18.58 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 16.976 6.211   9.525  1.00 19.05 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 16.980 3.887   8.522  1.00 17.54 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.642 4.251   5.647  1.00 19.37 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.609 3.433   4.431  1.00 20.21 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.711 4.197   3.133  1.00 23.94 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.153 3.623   2.130  1.00 25.50 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.360 2.539   4.406  1.00 20.28 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.306 1.610   5.600  1.00 21.23 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 11.986 0.851   5.548  1.00 21.81 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 10.865 1.676   5.989  1.00 22.12 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.620  1.252   6.137  1.00 23.26 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.291  0.005   5.809  1.00 23.11 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.685  2.074   6.597  1.00 21.90 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.322 5.479   3.137  1.00 24.47 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.425 6.290   1.929  1.00 25.34 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 15.848 6.838   1.680  1.00 25.75 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.137 7.324   0.570  1.00 26.78 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.402 7.442   1.955  1.00 27.46 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.672 8.450   3.050  1.00 30.86 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 13.960 8.019   4.199  1.00 29.20 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.597 9.665   2.765  1.00 31.14 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.745 6.759   2.688  1.00 25.51 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.116 7.300   2.589  1.00 25.17 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 19.023 6.337   1.874  1.00 26.07 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.896 5.707   2.487  1.00 26.57 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.650 7.670   3.985  1.00 24.36 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.742 8.624   4.791  1.00 24.07 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.295 8.873   6.186  1.00 24.21 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.516 9.959   4.062  1.00 25.42 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.825 6.222   0.540  1.00 25.85 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.528 5.224   -0.257 1.00 27.60 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 21.035 5.425   -0.286 1.00 29.48 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.776 4.435   -0.384 1.00 29.85 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 18.975 5.108   -1.707 1.00 28.82 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.476 5.022   -1.906 1.00 31.30 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.145 4.785   -3.389 1.00 33.33 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 16.837 3.936   -1.021 1.00 31.52 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.492 6.690   -0.104 1.00 29.81 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 22.915 7.020   -0.102 1.00 30.39 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.669 6.413   1.096  1.00 31.99 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 24.891 6.350   1.061  1.00 33.16 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.121 8.538   -0.185 1.00 29.18 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.360 9.312   0.844  1.00 27.60 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.127 9.875   0.705  1.00 27.64 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 22.789 9.599   2.185  1.00 26.78 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 20.781 10.539  1.865  1.00 27.30 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 21.796 10.402  2.779  1.00 26.72 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 23.977 9.358   2.896  1.00 27.49 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 21.926 10.913  4.065  1.00 27.66 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.110 9.887   4.166  1.00 28.51 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.083 10.634  4.744  1.00 28.35 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 22.962 5.966   2.158  1.00 31.67 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.632 5.352   3.309  1.00 32.92 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.469 4.116   2.929  1.00 37.85 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.360 3.751   3.693  1.00 38.32 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.613 4.963   4.383  1.00 30.95 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 21.977 6.115   5.130  1.00 29.86 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 20.857 5.604   6.038  1.00 29.77 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.029 6.882   5.968  1.00 29.86 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.167 3.468   1.774  1.00 41.21 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.869 2.271   1.277  1.00 45.70 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 25.883 2.506   0.187  1.00 50.84 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.414 1.518   -0.324 1.00 52.85 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.865 1.294   0.688  1.00 47.08 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.952 0.740   1.724  1.00 51.58 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.454 0.332   2.792  1.00 53.37 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.736 0.717   1.479  1.00 52.94 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 26.087 3.750   -0.257 1.00 52.90 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 27.034 4.014   -1.342 1.00 55.49 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 27.992 5.148   -0.996 1.00 57.13 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.906 5.453   -1.772 1.00 58.17 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 26.289 4.301   -2.658 1.00 59.08 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.322 5.471   -2.582 1.00 65.57 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 24.124 5.352   -3.506 1.00 73.73 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 23.955 6.224   -4.390 1.00 76.07 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 23.353 4.379   -3.349 1.00 76.50 ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1BSS B 2 .   ? 10.105 14.070  22.410 1.00 32.74 ? 201 A1BSS A N1  1 
HETATM 1079 N  N3  . A1BSS B 2 .   ? 7.678  9.999   25.783 1.00 39.75 ? 201 A1BSS A N3  1 
HETATM 1080 C  C4  . A1BSS B 2 .   ? 11.140 14.780  23.180 1.00 32.39 ? 201 A1BSS A C4  1 
HETATM 1081 C  C5  . A1BSS B 2 .   ? 9.382  13.026  22.858 1.00 34.42 ? 201 A1BSS A C5  1 
HETATM 1082 C  C6  . A1BSS B 2 .   ? 9.967  12.199  23.993 1.00 37.89 ? 201 A1BSS A C6  1 
HETATM 1083 C  C7  . A1BSS B 2 .   ? 10.910 11.127  23.356 1.00 39.48 ? 201 A1BSS A C7  1 
HETATM 1084 C  C8  . A1BSS B 2 .   ? 10.790 9.749   23.972 1.00 40.18 ? 201 A1BSS A C8  1 
HETATM 1085 C  C10 . A1BSS B 2 .   ? 7.852  12.123  25.700 1.00 39.81 ? 201 A1BSS A C10 1 
HETATM 1086 O  O1  . A1BSS B 2 .   ? 8.374  12.655  22.283 1.00 32.53 ? 201 A1BSS A O1  1 
HETATM 1087 C  C3  . A1BSS B 2 .   ? 12.474 14.763  22.446 1.00 31.27 ? 201 A1BSS A C3  1 
HETATM 1088 C  C2  . A1BSS B 2 .   ? 12.304 15.229  20.996 1.00 30.61 ? 201 A1BSS A C2  1 
HETATM 1089 C  C12 . A1BSS B 2 .   ? 9.922  14.561  21.042 1.00 31.33 ? 201 A1BSS A C12 1 
HETATM 1090 C  C1  . A1BSS B 2 .   ? 11.232 14.403  20.273 1.00 30.29 ? 201 A1BSS A C1  1 
HETATM 1091 C  C   . A1BSS B 2 .   ? 11.031 14.873  18.844 1.00 29.57 ? 201 A1BSS A C   1 
HETATM 1092 O  O   . A1BSS B 2 .   ? 10.643 16.022  18.599 1.00 29.98 ? 201 A1BSS A O   1 
HETATM 1093 N  N   . A1BSS B 2 .   ? 11.281 13.976  17.904 1.00 27.91 ? 201 A1BSS A N   1 
HETATM 1094 C  C11 . A1BSS B 2 .   ? 8.859  11.615  24.851 1.00 39.22 ? 201 A1BSS A C11 1 
HETATM 1095 N  N4  . A1BSS B 2 .   ? 7.138  11.155  26.270 1.00 39.87 ? 201 A1BSS A N4  1 
HETATM 1096 C  C9  . A1BSS B 2 .   ? 8.687  10.260  24.947 1.00 39.64 ? 201 A1BSS A C9  1 
HETATM 1097 N  N2  . A1BSS B 2 .   ? 9.399  9.413   24.237 1.00 40.38 ? 201 A1BSS A N2  1 
HETATM 1098 ZN ZN  . ZN    C 3 .   ? 10.951 -4.846  5.550  1.00 29.04 2 202 ZN    A ZN  1 
HETATM 1099 S  S   . DMS   D 4 .   ? 19.753 -0.397  19.883 1.00 57.44 ? 203 DMS   A S   1 
HETATM 1100 O  O   . DMS   D 4 .   ? 18.322 -0.657  19.536 1.00 56.20 ? 203 DMS   A O   1 
HETATM 1101 C  C1  . DMS   D 4 .   ? 19.931 0.138   21.614 1.00 56.96 ? 203 DMS   A C1  1 
HETATM 1102 C  C2  . DMS   D 4 .   ? 20.403 1.120   19.102 1.00 57.27 ? 203 DMS   A C2  1 
HETATM 1103 O  O   . HOH   E 5 .   ? 23.512 21.700  8.042  1.00 32.95 ? 301 HOH   A O   1 
HETATM 1104 O  O   . HOH   E 5 .   ? 23.626 -0.146  15.377 1.00 43.21 ? 302 HOH   A O   1 
HETATM 1105 O  O   . HOH   E 5 .   ? 22.684 -1.587  4.205  1.00 41.24 ? 303 HOH   A O   1 
HETATM 1106 O  O   . HOH   E 5 .   ? 29.482 3.069   10.431 1.00 32.88 ? 304 HOH   A O   1 
HETATM 1107 O  O   . HOH   E 5 .   ? 2.738  7.851   9.885  1.00 53.22 ? 305 HOH   A O   1 
HETATM 1108 O  O   . HOH   E 5 .   ? 8.962  2.317   2.842  1.00 32.06 ? 306 HOH   A O   1 
HETATM 1109 O  O   . HOH   E 5 .   ? 35.446 15.405  16.937 1.00 47.82 ? 307 HOH   A O   1 
HETATM 1110 O  O   . HOH   E 5 .   ? 27.413 15.878  3.003  1.00 48.92 ? 308 HOH   A O   1 
HETATM 1111 O  O   . HOH   E 5 .   ? 3.784  -4.960  21.117 1.00 30.06 ? 309 HOH   A O   1 
HETATM 1112 O  O   . HOH   E 5 .   ? 12.792 6.560   31.143 1.00 37.99 ? 310 HOH   A O   1 
HETATM 1113 O  O   . HOH   E 5 .   ? 7.965  -4.041  0.643  1.00 33.73 ? 311 HOH   A O   1 
HETATM 1114 O  O   . HOH   E 5 .   ? 6.120  13.916  22.062 1.00 49.70 ? 312 HOH   A O   1 
HETATM 1115 O  O   . HOH   E 5 .   ? 7.113  16.439  22.362 1.00 40.56 ? 313 HOH   A O   1 
HETATM 1116 O  O   . HOH   E 5 .   ? 11.538 1.943   33.388 1.00 27.85 ? 314 HOH   A O   1 
HETATM 1117 O  O   . HOH   E 5 .   ? 10.553 8.002   4.655  1.00 31.98 ? 315 HOH   A O   1 
HETATM 1118 O  O   . HOH   E 5 .   ? 6.523  17.486  24.655 1.00 55.05 ? 316 HOH   A O   1 
HETATM 1119 O  O   . HOH   E 5 .   ? 4.454  5.590   24.741 1.00 30.74 ? 317 HOH   A O   1 
HETATM 1120 O  O   . HOH   E 5 .   ? 20.111 8.679   18.993 1.00 21.62 ? 318 HOH   A O   1 
HETATM 1121 O  O   . HOH   E 5 .   ? 0.521  -0.407  16.458 1.00 22.21 ? 319 HOH   A O   1 
HETATM 1122 O  O   . HOH   E 5 .   ? 8.176  19.422  18.282 1.00 36.61 ? 320 HOH   A O   1 
HETATM 1123 O  O   . HOH   E 5 .   ? -0.012 15.421  8.138  1.00 43.48 ? 321 HOH   A O   1 
HETATM 1124 O  O   . HOH   E 5 .   ? 18.411 18.855  5.531  1.00 40.38 ? 322 HOH   A O   1 
HETATM 1125 O  O   . HOH   E 5 .   ? 36.807 15.962  12.091 1.00 40.46 ? 323 HOH   A O   1 
HETATM 1126 O  O   . HOH   E 5 .   ? 6.409  -5.596  29.090 1.00 37.21 ? 324 HOH   A O   1 
HETATM 1127 O  O   . HOH   E 5 .   ? 9.796  18.079  20.125 1.00 31.62 ? 325 HOH   A O   1 
HETATM 1128 O  O   . HOH   E 5 .   ? 30.773 20.446  10.759 1.00 38.78 ? 326 HOH   A O   1 
HETATM 1129 O  O   . HOH   E 5 .   ? -0.644 -4.857  15.694 0.50 24.90 ? 327 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? 26.210 4.040   19.947 1.00 53.88 ? 328 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? 0.163  1.665   24.388 1.00 36.73 ? 329 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? 19.130 -4.872  27.492 1.00 50.78 ? 330 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 12.259 -5.067  -0.919 1.00 43.21 ? 331 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? 17.808 20.977  9.617  1.00 24.27 ? 332 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? 10.214 4.646   3.471  1.00 27.90 ? 333 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 1.069  -2.710  20.073 1.00 37.97 ? 334 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? 14.827 2.317   23.191 1.00 21.34 ? 335 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 14.599 11.196  0.722  1.00 52.78 ? 336 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 10.046 4.289   33.719 1.00 36.20 ? 337 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? 10.970 16.856  5.386  1.00 61.64 ? 338 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 15.238 12.089  24.107 1.00 31.88 ? 339 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? 17.888 18.624  16.961 1.00 23.00 ? 340 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 17.894 2.268   23.137 1.00 28.44 ? 341 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 21.684 -5.746  10.247 1.00 45.42 ? 342 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? 21.453 18.930  17.783 1.00 43.78 ? 343 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? 22.965 18.180  19.509 1.00 44.48 ? 344 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 5.989  1.419   6.108  1.00 37.06 ? 345 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? 11.130 17.714  26.612 1.00 40.53 ? 346 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? 7.875  -8.324  24.380 1.00 44.63 ? 347 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 31.017 20.358  16.920 1.00 32.07 ? 348 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 11.248 11.351  11.505 1.00 21.39 ? 349 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? 30.076 4.408   3.586  1.00 52.89 ? 350 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 4.486  10.101  19.780 1.00 42.71 ? 351 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 18.674 12.470  1.873  1.00 43.68 ? 352 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 4.151  -5.337  6.463  1.00 37.46 ? 353 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 16.774 -7.740  10.644 1.00 42.20 ? 354 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? 19.170 8.995   25.697 1.00 43.03 ? 355 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? 28.604 -2.278  12.948 1.00 43.41 ? 356 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? 3.077  3.294   27.325 1.00 38.48 ? 357 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 13.066 10.286  9.425  1.00 18.92 ? 358 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? 6.972  3.437   32.922 1.00 37.38 ? 359 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 14.765 -4.631  17.168 1.00 26.47 ? 360 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? 30.095 10.760  19.376 1.00 32.11 ? 361 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? 14.397 20.975  8.628  1.00 41.83 ? 362 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 0.192  3.314   6.593  1.00 40.79 ? 363 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? 18.012 0.397   30.050 1.00 39.20 ? 364 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? 12.014 21.076  12.699 1.00 38.38 ? 365 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? 6.700  12.641  5.555  1.00 32.83 ? 366 HOH   A O   1 
HETATM 1169 O  O   . HOH   E 5 .   ? 4.078  -2.367  21.659 1.00 33.98 ? 367 HOH   A O   1 
HETATM 1170 O  O   . HOH   E 5 .   ? 31.229 2.471   12.741 1.00 42.99 ? 368 HOH   A O   1 
HETATM 1171 O  O   . HOH   E 5 .   ? 1.832  13.122  5.707  1.00 37.88 ? 369 HOH   A O   1 
HETATM 1172 O  O   . HOH   E 5 .   ? 5.504  -1.568  24.103 1.00 26.58 ? 370 HOH   A O   1 
HETATM 1173 O  O   . HOH   E 5 .   ? 14.472 14.272  3.602  1.00 33.65 ? 371 HOH   A O   1 
HETATM 1174 O  O   . HOH   E 5 .   ? 8.416  -7.527  8.849  1.00 42.68 ? 372 HOH   A O   1 
HETATM 1175 O  O   . HOH   E 5 .   ? -0.507 -5.967  11.242 1.00 49.42 ? 373 HOH   A O   1 
HETATM 1176 O  O   . HOH   E 5 .   ? 19.658 23.477  15.519 1.00 28.39 ? 374 HOH   A O   1 
HETATM 1177 O  O   . HOH   E 5 .   ? 15.809 -4.773  1.759  1.00 34.24 ? 375 HOH   A O   1 
HETATM 1178 O  O   . HOH   E 5 .   ? 12.136 -8.134  13.010 1.00 38.57 ? 376 HOH   A O   1 
HETATM 1179 O  O   . HOH   E 5 .   ? 1.289  -2.988  17.451 1.00 30.72 ? 377 HOH   A O   1 
HETATM 1180 O  O   . HOH   E 5 .   ? 23.801 2.123   19.616 1.00 39.46 ? 378 HOH   A O   1 
HETATM 1181 O  O   . HOH   E 5 .   ? 20.835 19.019  21.330 1.00 46.23 ? 379 HOH   A O   1 
HETATM 1182 O  O   . HOH   E 5 .   ? 22.410 18.813  5.918  1.00 31.69 ? 380 HOH   A O   1 
HETATM 1183 O  O   . HOH   E 5 .   ? 4.773  -1.386  29.165 1.00 57.94 ? 381 HOH   A O   1 
HETATM 1184 O  O   . HOH   E 5 .   ? 2.448  -6.619  14.704 1.00 40.24 ? 382 HOH   A O   1 
HETATM 1185 O  O   . HOH   E 5 .   ? 13.466 -11.398 3.584  1.00 50.35 ? 383 HOH   A O   1 
HETATM 1186 O  O   . HOH   E 5 .   ? -0.111 12.208  20.848 1.00 51.71 ? 384 HOH   A O   1 
HETATM 1187 O  O   . HOH   E 5 .   ? 22.029 8.662   21.057 1.00 30.36 ? 385 HOH   A O   1 
HETATM 1188 O  O   . HOH   E 5 .   ? 26.467 -1.940  14.361 1.00 38.81 ? 386 HOH   A O   1 
HETATM 1189 O  O   . HOH   E 5 .   ? 0.488  -3.413  9.833  1.00 44.32 ? 387 HOH   A O   1 
HETATM 1190 O  O   . HOH   E 5 .   ? 6.265  -4.252  -1.601 1.00 66.58 ? 388 HOH   A O   1 
HETATM 1191 O  O   . HOH   E 5 .   ? 28.456 16.478  23.348 1.00 44.84 ? 389 HOH   A O   1 
HETATM 1192 O  O   . HOH   E 5 .   ? 16.841 -10.786 4.616  1.00 69.96 ? 390 HOH   A O   1 
HETATM 1193 O  O   . HOH   E 5 .   ? 24.284 7.122   20.593 1.00 43.90 ? 391 HOH   A O   1 
HETATM 1194 O  O   . HOH   E 5 .   ? 7.057  -5.543  2.792  1.00 33.91 ? 392 HOH   A O   1 
HETATM 1195 O  O   . HOH   E 5 .   ? 3.679  12.682  18.640 1.00 57.01 ? 393 HOH   A O   1 
HETATM 1196 O  O   . HOH   E 5 .   ? 28.264 21.988  18.679 1.00 46.30 ? 394 HOH   A O   1 
HETATM 1197 O  O   . HOH   E 5 .   ? 8.598  17.445  25.979 1.00 47.10 ? 395 HOH   A O   1 
HETATM 1198 O  O   . HOH   E 5 .   ? 20.877 21.697  17.848 1.00 32.78 ? 396 HOH   A O   1 
HETATM 1199 O  O   . HOH   E 5 .   ? 2.113  1.289   26.399 1.00 38.99 ? 397 HOH   A O   1 
HETATM 1200 O  O   . HOH   E 5 .   ? 8.660  22.158  26.573 1.00 48.12 ? 398 HOH   A O   1 
HETATM 1201 O  O   . HOH   E 5 .   ? 8.705  19.481  6.722  1.00 58.85 ? 399 HOH   A O   1 
HETATM 1202 O  O   . HOH   E 5 .   ? 32.700 21.566  15.137 1.00 41.27 ? 400 HOH   A O   1 
HETATM 1203 O  O   . HOH   E 5 .   ? 0.871  -2.104  23.802 1.00 45.24 ? 401 HOH   A O   1 
HETATM 1204 O  O   . HOH   E 5 .   ? 13.463 14.095  26.121 1.00 53.51 ? 402 HOH   A O   1 
HETATM 1205 O  O   . HOH   E 5 .   ? 9.389  -8.624  12.485 1.00 36.06 ? 403 HOH   A O   1 
HETATM 1206 O  O   . HOH   E 5 .   ? 19.978 -3.813  22.524 1.00 62.27 ? 404 HOH   A O   1 
HETATM 1207 O  O   . HOH   E 5 .   ? 5.406  -8.473  23.373 1.00 44.69 ? 405 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER   A 1   ? 0.5581 0.4010 0.4152 -0.0308 -0.1149 -0.0052 7   SER   A N   
2    C CA  . SER   A 1   ? 0.5305 0.3967 0.4369 -0.0283 -0.1262 0.0007  7   SER   A CA  
3    C C   . SER   A 1   ? 0.4793 0.3760 0.4288 -0.0207 -0.1179 0.0036  7   SER   A C   
4    O O   . SER   A 1   ? 0.4854 0.3839 0.4256 -0.0190 -0.1098 0.0030  7   SER   A O   
5    C CB  . SER   A 1   ? 0.5732 0.4203 0.4786 -0.0403 -0.1562 0.0110  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.6254 0.4579 0.5137 -0.0477 -0.1690 0.0184  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.4211 0.3386 0.4152 -0.0168 -0.1175 0.0061  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.3766 0.3168 0.4095 -0.0117 -0.1065 0.0078  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.3486 0.3071 0.4107 -0.0069 -0.0929 0.0041  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.3413 0.3004 0.3901 -0.0052 -0.0875 -0.0012 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.3184 0.2893 0.4203 -0.0054 -0.0854 0.0072  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2984 0.2812 0.4242 -0.0031 -0.0701 0.0036  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2750 0.2657 0.4206 -0.0027 -0.0502 0.0015  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2762 0.2652 0.4294 -0.0032 -0.0510 0.0049  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2911 0.2723 0.4529 -0.0042 -0.0814 0.0107  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2547 0.2507 0.4057 -0.0033 -0.0320 -0.0039 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2417 0.2377 0.4056 -0.0060 -0.0098 -0.0075 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2484 0.2418 0.4554 -0.0062 -0.0003 -0.0046 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2404 0.2351 0.4518 -0.0056 -0.0036 -0.0043 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2474 0.2448 0.3762 -0.0104 0.0038  -0.0152 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2394 0.2408 0.3337 -0.0096 -0.0050 -0.0162 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2703 0.2602 0.4027 -0.0170 0.0277  -0.0201 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2463 0.2512 0.3141 -0.0143 0.0008  -0.0191 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2614 0.2508 0.5057 -0.0066 0.0119  -0.0014 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2698 0.2552 0.5647 -0.0063 0.0250  0.0028  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.3050 0.2791 0.5987 -0.0115 0.0594  -0.0058 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.3272 0.2966 0.6266 -0.0127 0.0703  -0.0067 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2514 0.2387 0.5996 -0.0033 0.0108  0.0166  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2577 0.2493 0.6019 -0.0021 -0.0247 0.0258  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2602 0.2529 0.6272 -0.0018 -0.0361 0.0313  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2755 0.2664 0.5865 -0.0029 -0.0457 0.0278  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2721 0.2633 0.6285 -0.0035 -0.0688 0.0390  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2974 0.2846 0.5941 -0.0050 -0.0762 0.0348  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2964 0.2829 0.6141 -0.0059 -0.0881 0.0401  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3071 0.2849 0.6045 -0.0104 -0.1180 0.0463  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.3152 0.2818 0.5952 -0.0160 0.0769  -0.0125 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.3369 0.2846 0.6015 -0.0249 0.1113  -0.0222 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.3436 0.2802 0.6377 -0.0265 0.1319  -0.0224 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.3473 0.2894 0.6322 -0.0257 0.1216  -0.0215 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.3810 0.3249 0.5766 -0.0339 0.1113  -0.0311 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.3813 0.3371 0.5526 -0.0323 0.0901  -0.0293 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.4272 0.3447 0.5972 -0.0475 0.1450  -0.0408 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.3338 0.2540 0.6682 -0.0284 0.1628  -0.0230 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.3430 0.2500 0.7141 -0.0294 0.1873  -0.0224 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.3452 0.2715 0.7667 -0.0194 0.1617  -0.0094 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.3439 0.2872 0.7992 -0.0120 0.1340  0.0020  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.3462 0.2697 0.7617 -0.0209 0.1654  -0.0111 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.3306 0.2704 0.7879 -0.0132 0.1403  0.0004  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.3140 0.2704 0.7221 -0.0116 0.1042  -0.0003 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.3074 0.2717 0.7291 -0.0084 0.0882  0.0047  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3783 0.3051 0.8674 -0.0148 0.1670  0.0002  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.4608 0.3761 1.0261 -0.0126 0.1959  0.0070  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4737 0.4013 1.0954 -0.0063 0.1797  0.0201  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.4992 0.3885 1.0695 -0.0187 0.2401  -0.0007 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.3050 0.2658 0.6613 -0.0135 0.0921  -0.0057 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2953 0.2688 0.6079 -0.0119 0.0636  -0.0065 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2735 0.2572 0.5801 -0.0077 0.0368  -0.0017 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2774 0.2588 0.5899 -0.0080 0.0420  -0.0012 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.3068 0.2745 0.5568 -0.0198 0.0740  -0.0166 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.3253 0.2788 0.5655 -0.0273 0.0977  -0.0214 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.3324 0.2896 0.5905 -0.0244 0.0927  -0.0179 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.3496 0.2823 0.5594 -0.0389 0.1256  -0.0294 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.3598 0.3016 0.6079 -0.0320 0.1155  -0.0219 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.3821 0.2957 0.5750 -0.0486 0.1483  -0.0338 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.3981 0.3172 0.6103 -0.0446 0.1430  -0.0298 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.4477 0.3462 0.6415 -0.0547 0.1659  -0.0337 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.2504 0.2422 0.5382 -0.0048 0.0104  0.0007  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.2325 0.2283 0.4999 -0.0029 -0.0139 0.0036  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2288 0.2275 0.4440 -0.0034 -0.0189 -0.0032 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.2213 0.2216 0.4307 -0.0030 -0.0219 -0.0041 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2341 0.2299 0.5324 -0.0012 -0.0402 0.0147  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2689 0.2614 0.5300 -0.0021 -0.0662 0.0160  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.3006 0.2871 0.5883 -0.0049 -0.0941 0.0284  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.3411 0.3181 0.5877 -0.0078 -0.1144 0.0266  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.3764 0.3410 0.5864 -0.0121 -0.1316 0.0278  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.3561 0.3194 0.5676 -0.0134 -0.1341 0.0320  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.3713 0.3217 0.5409 -0.0160 -0.1444 0.0243  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.2279 0.2276 0.4097 -0.0043 -0.0180 -0.0070 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2317 0.2348 0.3732 -0.0046 -0.0211 -0.0110 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2409 0.2415 0.3649 -0.0016 -0.0391 -0.0092 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2409 0.2387 0.3621 -0.0016 -0.0428 -0.0078 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2287 0.2328 0.3462 -0.0094 -0.0069 -0.0153 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2346 0.2441 0.3216 -0.0104 -0.0109 -0.0158 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2203 0.2180 0.3472 -0.0158 0.0144  -0.0183 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.2356 0.2343 0.3446 -0.0001 -0.0480 -0.0097 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.2470 0.2353 0.3329 0.0007  -0.0616 -0.0093 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.2480 0.2360 0.3086 0.0024  -0.0569 -0.0126 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.2411 0.2380 0.3078 0.0028  -0.0493 -0.0130 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.2782 0.2548 0.3750 -0.0013 -0.0803 -0.0048 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.3110 0.2861 0.4364 -0.0035 -0.0895 0.0024  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2642 0.2442 0.3779 -0.0005 -0.0800 -0.0048 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.2473 0.2227 0.2811 0.0027  -0.0605 -0.0141 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.2533 0.2251 0.2711 0.0048  -0.0534 -0.0164 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.2675 0.2336 0.2920 0.0045  -0.0592 -0.0169 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.2912 0.2438 0.3142 0.0011  -0.0728 -0.0163 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.2786 0.2300 0.2652 0.0042  -0.0525 -0.0190 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.3090 0.2651 0.2888 0.0049  -0.0462 -0.0183 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.3268 0.2785 0.3031 0.0025  -0.0538 -0.0172 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.2880 0.2532 0.2696 0.0078  -0.0332 -0.0174 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.2613 0.2370 0.2948 0.0069  -0.0509 -0.0164 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.2513 0.2226 0.2934 0.0069  -0.0553 -0.0168 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.2841 0.2292 0.3015 0.0046  -0.0607 -0.0207 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.3064 0.2411 0.3260 0.0013  -0.0725 -0.0209 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.2385 0.2243 0.2945 0.0092  -0.0456 -0.0140 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.2372 0.2232 0.3081 0.0094  -0.0490 -0.0135 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.2465 0.2433 0.3268 0.0114  -0.0396 -0.0091 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.2511 0.2500 0.3470 0.0118  -0.0410 -0.0075 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.2884 0.2743 0.3821 0.0136  -0.0405 -0.0101 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.2751 0.2407 0.3472 0.0139  -0.0377 -0.0153 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.2943 0.2841 0.4045 0.0141  -0.0412 -0.0080 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.2928 0.2234 0.2843 0.0047  -0.0522 -0.0237 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.3412 0.2383 0.2991 -0.0001 -0.0533 -0.0289 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.3950 0.2706 0.3296 -0.0089 -0.0725 -0.0289 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.4405 0.2834 0.3421 -0.0171 -0.0787 -0.0326 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.3677 0.2512 0.3063 0.0022  -0.0332 -0.0322 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.3766 0.2559 0.2984 0.0014  -0.0303 -0.0322 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.3743 0.2813 0.3191 0.0065  -0.0254 -0.0274 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.4083 0.2561 0.2896 -0.0052 -0.0310 -0.0363 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.3977 0.2920 0.3198 0.0045  -0.0231 -0.0288 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.4137 0.2723 0.2968 -0.0025 -0.0260 -0.0339 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.3789 0.2708 0.3322 -0.0089 -0.0833 -0.0236 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.4003 0.2768 0.3436 -0.0173 -0.1045 -0.0194 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.3855 0.2771 0.3701 -0.0182 -0.1206 -0.0122 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.3930 0.2764 0.3832 -0.0252 -0.1408 -0.0049 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.4013 0.2815 0.3376 -0.0168 -0.1025 -0.0175 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.4278 0.2889 0.3240 -0.0170 -0.0868 -0.0235 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.4231 0.2890 0.3152 -0.0165 -0.0859 -0.0209 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.4495 0.2674 0.2963 -0.0279 -0.0922 -0.0278 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.3585 0.2725 0.3760 -0.0116 -0.1113 -0.0125 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.3484 0.2753 0.4081 -0.0118 -0.1211 -0.0060 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.3643 0.2701 0.4207 -0.0208 -0.1448 -0.0013 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.3838 0.2667 0.4042 -0.0258 -0.1477 -0.0063 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.3281 0.2748 0.4120 -0.0053 -0.1059 -0.0080 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.3631 0.2741 0.4571 -0.0242 -0.1612 0.0090  24  THR   A N   
135  C CA  . THR   A 18  ? 0.3797 0.2724 0.4791 -0.0350 -0.1893 0.0177  24  THR   A CA  
136  C C   . THR   A 18  ? 0.3687 0.2715 0.5060 -0.0326 -0.1899 0.0198  24  THR   A C   
137  O O   . THR   A 18  ? 0.3459 0.2702 0.5067 -0.0228 -0.1683 0.0155  24  THR   A O   
138  C CB  . THR   A 18  ? 0.3895 0.2841 0.5206 -0.0403 -0.2087 0.0318  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.3732 0.2950 0.5682 -0.0318 -0.1969 0.0371  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.4149 0.3035 0.5158 -0.0412 -0.2058 0.0303  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.3751 0.2618 0.5210 -0.0431 -0.2166 0.0285  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.3798 0.2766 0.5676 -0.0410 -0.2184 0.0322  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.3511 0.2768 0.6061 -0.0318 -0.2050 0.0392  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.3390 0.2797 0.6188 -0.0243 -0.1868 0.0355  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.4275 0.3017 0.6188 -0.0561 -0.2538 0.0436  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.5589 0.3968 0.6791 -0.0681 -0.2646 0.0356  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.6182 0.4498 0.7057 -0.0634 -0.2443 0.0211  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.6244 0.4275 0.7010 -0.0860 -0.2925 0.0408  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.6700 0.4621 0.6954 -0.0777 -0.2564 0.0162  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.6790 0.4508 0.6908 -0.0926 -0.2858 0.0273  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.3367 0.2671 0.6206 -0.0335 -0.2127 0.0495  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.3100 0.2622 0.6581 -0.0258 -0.1961 0.0560  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.2834 0.2500 0.6174 -0.0155 -0.1604 0.0423  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.2707 0.2495 0.6398 -0.0100 -0.1399 0.0414  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.3495 0.3016 0.7269 -0.0297 -0.2093 0.0691  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.4369 0.4075 0.8844 -0.0220 -0.1872 0.0754  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.4463 0.4230 0.9517 -0.0210 -0.1862 0.0842  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.4640 0.4414 0.9053 -0.0167 -0.1652 0.0695  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.2825 0.2457 0.5639 -0.0142 -0.1527 0.0324  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.2666 0.2419 0.5307 -0.0070 -0.1232 0.0213  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.2549 0.2350 0.5175 -0.0040 -0.1120 0.0158  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.2517 0.2423 0.5331 -0.0006 -0.0909 0.0137  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.2753 0.2448 0.4855 -0.0070 -0.1207 0.0133  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.3130 0.2812 0.5217 -0.0084 -0.1236 0.0167  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.2975 0.2754 0.5447 -0.0064 -0.1140 0.0211  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.3357 0.2911 0.5047 -0.0117 -0.1334 0.0147  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.2542 0.2235 0.4937 -0.0067 -0.1256 0.0139  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.2628 0.2367 0.5031 -0.0038 -0.1158 0.0097  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.2750 0.2558 0.5677 -0.0031 -0.1145 0.0165  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2799 0.2692 0.5808 0.0003  -0.0972 0.0136  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.2775 0.2350 0.4808 -0.0070 -0.1276 0.0053  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.2788 0.2330 0.4384 -0.0047 -0.1159 -0.0029 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.3106 0.2483 0.4324 -0.0083 -0.1218 -0.0060 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.2659 0.2318 0.4182 0.0007  -0.0968 -0.0073 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.3162 0.2562 0.4130 -0.0040 -0.1048 -0.0122 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.2942 0.2530 0.4116 0.0014  -0.0910 -0.0119 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.2603 0.2414 0.4336 0.0041  -0.0841 -0.0061 28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.2943 0.2621 0.4038 0.0056  -0.0753 -0.0138 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2665 0.2558 0.4258 0.0068  -0.0705 -0.0079 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.2791 0.2631 0.4105 0.0077  -0.0672 -0.0108 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.2771 0.2539 0.6076 -0.0071 -0.1320 0.0271  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2791 0.2623 0.6692 -0.0062 -0.1296 0.0356  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2805 0.2743 0.7048 -0.0015 -0.1009 0.0359  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2752 0.2727 0.7445 0.0003  -0.0884 0.0402  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2809 0.2560 0.7068 -0.0133 -0.1600 0.0500  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2698 0.2653 0.6736 -0.0004 -0.0894 0.0315  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2506 0.2501 0.6739 0.0018  -0.0594 0.0293  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2485 0.2492 0.6164 0.0020  -0.0418 0.0171  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2347 0.2345 0.5950 0.0012  -0.0251 0.0138  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2579 0.2567 0.7144 0.0011  -0.0627 0.0373  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.3021 0.3008 0.8249 -0.0003 -0.0805 0.0532  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.3227 0.3229 0.8975 0.0015  -0.0643 0.0581  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.3034 0.2981 0.8254 -0.0051 -0.1143 0.0626  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2492 0.2510 0.5811 0.0022  -0.0466 0.0119  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2436 0.2477 0.5293 0.0014  -0.0348 0.0042  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2619 0.2643 0.5470 -0.0021 -0.0073 0.0011  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2661 0.2657 0.5732 -0.0030 0.0041  0.0026  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2488 0.2545 0.5114 0.0025  -0.0441 0.0023  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2555 0.2654 0.4795 0.0012  -0.0349 -0.0018 31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2722 0.2822 0.4681 0.0013  -0.0391 -0.0042 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2528 0.2642 0.4674 0.0028  -0.0412 -0.0015 31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2559 0.2568 0.5093 -0.0057 0.0033  -0.0033 32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2670 0.2599 0.5018 -0.0133 0.0276  -0.0071 32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2849 0.2816 0.4746 -0.0178 0.0230  -0.0081 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.3093 0.3010 0.4856 -0.0242 0.0323  -0.0075 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2830 0.2685 0.5159 -0.0166 0.0417  -0.0101 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.3035 0.2746 0.5023 -0.0281 0.0655  -0.0153 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2759 0.2579 0.5630 -0.0125 0.0481  -0.0064 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2674 0.2720 0.4374 -0.0149 0.0081  -0.0079 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2660 0.2758 0.4043 -0.0185 0.0028  -0.0060 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2422 0.2594 0.3742 -0.0116 -0.0127 -0.0055 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.2413 0.2569 0.3779 -0.0081 -0.0169 -0.0077 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2773 0.2797 0.3869 -0.0296 0.0151  -0.0071 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2901 0.2985 0.3715 -0.0351 0.0065  -0.0021 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.3138 0.3229 0.3811 -0.0429 0.0036  0.0046  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2882 0.3027 0.3575 -0.0338 -0.0008 -0.0013 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.3194 0.3357 0.3709 -0.0468 -0.0064 0.0110  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.3069 0.3265 0.3596 -0.0409 -0.0080 0.0069  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2848 0.3003 0.3575 -0.0281 -0.0022 -0.0054 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.3036 0.3297 0.3465 -0.0420 -0.0151 0.0109  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2999 0.3206 0.3573 -0.0291 -0.0079 -0.0030 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.3031 0.3296 0.3482 -0.0353 -0.0139 0.0051  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.2241 0.2472 0.3480 -0.0101 -0.0199 -0.0021 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.2264 0.2518 0.3420 -0.0046 -0.0288 -0.0020 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.2237 0.2564 0.3302 -0.0070 -0.0291 0.0044  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2224 0.2583 0.3323 -0.0114 -0.0278 0.0096  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2450 0.2642 0.3706 0.0019  -0.0381 -0.0047 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2580 0.2775 0.3987 0.0030  -0.0395 -0.0029 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2663 0.2900 0.4033 0.0043  -0.0388 0.0009  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.3056 0.3328 0.4541 0.0032  -0.0372 0.0044  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2631 0.2857 0.3890 0.0065  -0.0387 0.0013  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.2113 0.2460 0.3088 -0.0050 -0.0309 0.0056  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.2111 0.2538 0.3101 -0.0068 -0.0318 0.0146  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.2155 0.2548 0.3162 0.0010  -0.0309 0.0132  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.2319 0.2686 0.3220 0.0019  -0.0295 0.0106  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2263 0.2736 0.3128 -0.0175 -0.0318 0.0208  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2952 0.3519 0.3894 -0.0225 -0.0372 0.0346  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2938 0.3547 0.4060 -0.0148 -0.0371 0.0387  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.3144 0.3720 0.3965 -0.0355 -0.0411 0.0423  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.2075 0.2438 0.3203 0.0061  -0.0293 0.0146  36  SER   A N   
241  C CA  A SER   A 30  ? 0.2245 0.2506 0.3362 0.0123  -0.0230 0.0122  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.2256 0.2515 0.3366 0.0123  -0.0231 0.0120  36  SER   A CA  
243  C C   . SER   A 30  ? 0.2258 0.2601 0.3450 0.0117  -0.0185 0.0208  36  SER   A C   
244  O O   . SER   A 30  ? 0.2418 0.2664 0.3532 0.0153  -0.0114 0.0172  36  SER   A O   
245  C CB  A SER   A 30  ? 0.2413 0.2611 0.3668 0.0162  -0.0188 0.0129  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2455 0.2634 0.3685 0.0165  -0.0187 0.0117  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2764 0.2804 0.3981 0.0208  -0.0078 0.0096  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2613 0.2932 0.4101 0.0156  -0.0168 0.0243  36  SER   A OG  
249  N N   . SER   A 31  ? 0.2149 0.2653 0.3497 0.0058  -0.0232 0.0336  37  SER   A N   
250  C CA  . SER   A 31  ? 0.2225 0.2821 0.3713 0.0037  -0.0224 0.0453  37  SER   A CA  
251  C C   . SER   A 31  ? 0.2253 0.2842 0.3537 0.0006  -0.0237 0.0410  37  SER   A C   
252  O O   . SER   A 31  ? 0.2387 0.3009 0.3771 0.0013  -0.0205 0.0474  37  SER   A O   
253  C CB  . SER   A 31  ? 0.2586 0.3333 0.4272 -0.0052 -0.0322 0.0628  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2994 0.3767 0.4452 -0.0172 -0.0419 0.0635  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.2069 0.2609 0.3116 -0.0023 -0.0269 0.0309  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.2057 0.2579 0.2925 -0.0051 -0.0270 0.0261  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.2141 0.2526 0.2869 0.0022  -0.0227 0.0138  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.2273 0.2635 0.2876 0.0012  -0.0222 0.0103  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.2126 0.2657 0.2844 -0.0150 -0.0310 0.0244  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.2131 0.2738 0.2870 -0.0270 -0.0376 0.0372  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.2460 0.2992 0.2963 -0.0393 -0.0371 0.0335  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.2142 0.2617 0.2470 -0.0429 -0.0331 0.0271  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2599 0.2981 0.2688 -0.0571 -0.0311 0.0263  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2772 0.3092 0.2722 -0.0709 -0.0340 0.0324  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2675 0.3000 0.2633 -0.0594 -0.0259 0.0201  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.2104 0.2381 0.2830 0.0077  -0.0214 0.0080  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.2024 0.2130 0.2571 0.0108  -0.0223 -0.0019 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.2034 0.2154 0.2534 0.0074  -0.0292 -0.0058 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.2221 0.2249 0.2599 0.0078  -0.0317 -0.0100 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.2318 0.2303 0.2727 0.0136  -0.0150 -0.0041 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.2778 0.2536 0.2933 0.0136  -0.0185 -0.0127 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.2979 0.2611 0.3078 0.0129  -0.0233 -0.0165 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.2954 0.2648 0.2956 0.0128  -0.0180 -0.0146 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1902 0.2118 0.2508 0.0033  -0.0306 -0.0037 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1858 0.2064 0.2490 0.0004  -0.0318 -0.0071 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.2008 0.2188 0.2787 0.0009  -0.0348 -0.0083 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.2250 0.2463 0.3094 0.0009  -0.0344 -0.0058 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1806 0.2080 0.2408 -0.0073 -0.0257 -0.0048 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.2011 0.2310 0.2486 -0.0097 -0.0237 -0.0035 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.2098 0.2408 0.2479 -0.0210 -0.0184 -0.0017 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.2208 0.2438 0.2653 -0.0055 -0.0247 -0.0086 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1913 0.2039 0.2790 0.0009  -0.0378 -0.0107 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.2007 0.2114 0.3106 0.0009  -0.0399 -0.0103 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.2149 0.2247 0.3416 -0.0015 -0.0339 -0.0105 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.2328 0.2398 0.3571 -0.0010 -0.0371 -0.0107 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.2129 0.2136 0.3269 0.0035  -0.0541 -0.0103 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.2229 0.2232 0.3654 0.0031  -0.0578 -0.0081 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.2205 0.2118 0.3576 0.0040  -0.0690 -0.0085 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.2330 0.2292 0.4013 0.0019  -0.0653 -0.0044 41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.2087 0.2188 0.3538 -0.0042 -0.0233 -0.0102 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.2153 0.2210 0.3839 -0.0063 -0.0120 -0.0102 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.2332 0.2370 0.4407 -0.0039 -0.0149 -0.0065 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.2304 0.2351 0.4414 -0.0041 -0.0134 -0.0062 42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.2351 0.2364 0.3887 -0.0141 0.0093  -0.0137 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.2433 0.2351 0.4235 -0.0165 0.0275  -0.0150 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.2394 0.2432 0.3577 -0.0178 0.0082  -0.0152 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.2287 0.2302 0.4675 -0.0020 -0.0213 -0.0019 43  SER   A N   
298  C CA  . SER   A 37  ? 0.2316 0.2317 0.5174 -0.0006 -0.0255 0.0047  43  SER   A CA  
299  C C   . SER   A 37  ? 0.2493 0.2455 0.5758 -0.0016 -0.0054 0.0072  43  SER   A C   
300  O O   . SER   A 37  ? 0.2447 0.2384 0.5615 -0.0031 0.0056  0.0043  43  SER   A O   
301  C CB  . SER   A 37  ? 0.2357 0.2341 0.5313 0.0003  -0.0546 0.0118  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.2384 0.2345 0.5331 -0.0005 -0.0633 0.0151  43  SER   A OG  
303  N N   . SER   A 38  ? 0.2575 0.2518 0.6331 -0.0007 0.0010  0.0130  44  SER   A N   
304  C CA  . SER   A 38  ? 0.2820 0.2700 0.7052 -0.0011 0.0247  0.0163  44  SER   A CA  
305  C C   . SER   A 38  ? 0.3005 0.2920 0.7759 0.0012  0.0062  0.0296  44  SER   A C   
306  O O   . SER   A 38  ? 0.3011 0.2972 0.7844 0.0016  -0.0255 0.0381  44  SER   A O   
307  C CB  . SER   A 38  ? 0.3036 0.2856 0.7586 -0.0017 0.0459  0.0167  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.3358 0.3249 0.8216 0.0013  0.0227  0.0256  44  SER   A OG  
309  N N   . THR   A 39  ? 0.3180 0.3048 0.8276 0.0013  0.0257  0.0322  45  THR   A N   
310  C CA  . THR   A 39  ? 0.3332 0.3237 0.8986 0.0027  0.0086  0.0476  45  THR   A CA  
311  C C   . THR   A 39  ? 0.3636 0.3488 1.0082 0.0043  0.0357  0.0559  45  THR   A C   
312  O O   . THR   A 39  ? 0.3800 0.3536 1.0206 0.0032  0.0747  0.0456  45  THR   A O   
313  C CB  . THR   A 39  ? 0.3474 0.3374 0.8858 0.0019  0.0074  0.0447  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3614 0.3417 0.9003 0.0008  0.0471  0.0354  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.3647 0.3576 0.8260 0.0006  -0.0110 0.0352  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3674 0.3579 1.0828 0.0054  0.0165  0.0752  46  THR   A N   
317  C CA  . THR   A 40  ? 0.3757 0.3618 1.1802 0.0076  0.0430  0.0864  46  THR   A CA  
318  C C   . THR   A 40  ? 0.4019 0.3820 1.2209 0.0081  0.0656  0.0854  46  THR   A C   
319  O O   . THR   A 40  ? 0.4233 0.3902 1.2768 0.0089  0.1098  0.0811  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3655 0.3611 1.2483 0.0075  0.0091  0.1112  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3855 0.3876 1.2519 0.0036  -0.0354 0.1221  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3760 0.3743 1.2556 0.0069  -0.0040 0.1116  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3990 0.3857 1.1925 0.0068  0.0373  0.0894  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.4016 0.3837 1.2088 0.0073  0.0558  0.0893  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.4298 0.4011 1.1564 0.0051  0.0852  0.0651  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.4533 0.4271 1.1049 0.0032  0.0724  0.0529  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.4022 0.3939 1.2120 0.0057  0.0136  0.1040  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.4287 0.3860 1.1726 0.0043  0.1256  0.0588  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.4638 0.4065 1.1322 -0.0009 0.1535  0.0372  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.4626 0.4139 1.0787 -0.0016 0.1295  0.0341  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.4587 0.4186 1.1127 0.0013  0.1107  0.0475  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.5000 0.4181 1.2006 -0.0039 0.2073  0.0306  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.6088 0.5030 1.2295 -0.0137 0.2410  0.0079  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6926 0.5755 1.3039 -0.0170 0.2578  0.0024  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6998 0.5879 1.3788 -0.0114 0.2582  0.0142  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.7243 0.5909 1.2527 -0.0273 0.2712  -0.0143 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.4609 0.4089 0.9936 -0.0062 0.1304  0.0180  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.4626 0.4174 0.9394 -0.0073 0.1113  0.0133  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.4491 0.3886 0.8959 -0.0132 0.1415  0.0011  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.4650 0.3843 0.8962 -0.0202 0.1765  -0.0101 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.4196 0.3654 0.8522 -0.0122 0.1281  0.0027  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.4140 0.3448 0.8250 -0.0180 0.1553  -0.0073 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.3967 0.3308 0.7364 -0.0223 0.1432  -0.0162 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.4025 0.3259 0.7284 -0.0270 0.1604  -0.0223 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.4234 0.3542 0.8995 -0.0136 0.1617  0.0037  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.5225 0.4424 1.0928 -0.0107 0.1913  0.0134  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.3688 0.3160 0.6666 -0.0211 0.1160  -0.0167 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.3784 0.3292 0.6149 -0.0251 0.1059  -0.0235 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.3910 0.3240 0.5824 -0.0374 0.1300  -0.0359 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.4068 0.3288 0.5990 -0.0419 0.1451  -0.0392 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.4128 0.3801 0.6233 -0.0203 0.0738  -0.0197 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.4619 0.4404 0.6941 -0.0124 0.0467  -0.0089 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.4735 0.4513 0.7232 -0.0111 0.0468  -0.0048 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.4740 0.4595 0.7023 -0.0090 0.0250  -0.0043 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.3905 0.3187 0.5411 -0.0445 0.1324  -0.0416 52  THR   A N   
356  C CA  . THR   A 46  ? 0.4213 0.3295 0.5209 -0.0601 0.1500  -0.0516 52  THR   A CA  
357  C C   . THR   A 46  ? 0.4019 0.3232 0.4578 -0.0629 0.1253  -0.0498 52  THR   A C   
358  O O   . THR   A 46  ? 0.3956 0.3339 0.4476 -0.0564 0.1050  -0.0454 52  THR   A O   
359  C CB  . THR   A 46  ? 0.4770 0.3692 0.5615 -0.0684 0.1677  -0.0578 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.4896 0.3658 0.6189 -0.0669 0.1967  -0.0596 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.5120 0.3811 0.5329 -0.0884 0.1791  -0.0668 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.3882 0.3010 0.4143 -0.0725 0.1277  -0.0521 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.3820 0.3076 0.3737 -0.0758 0.1043  -0.0478 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.3934 0.3034 0.3377 -0.0934 0.1087  -0.0512 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.4235 0.3044 0.3432 -0.1091 0.1319  -0.0587 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.3831 0.3095 0.3689 -0.0778 0.0998  -0.0455 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.3678 0.3048 0.4012 -0.0629 0.0980  -0.0426 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.3871 0.3290 0.3481 -0.0797 0.0751  -0.0384 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.3544 0.3151 0.4119 -0.0472 0.0736  -0.0360 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.3689 0.2947 0.2996 -0.0925 0.0879  -0.0455 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.3843 0.2975 0.2731 -0.1104 0.0864  -0.0457 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.4049 0.3064 0.2573 -0.1275 0.0806  -0.0422 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.3819 0.2991 0.2465 -0.1205 0.0669  -0.0356 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.3652 0.3012 0.2592 -0.1031 0.0648  -0.0380 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.4515 0.3238 0.2568 -0.1515 0.0893  -0.0457 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.4905 0.3463 0.2521 -0.1733 0.0805  -0.0403 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.5145 0.3649 0.2425 -0.1912 0.0640  -0.0338 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.5509 0.3691 0.2393 -0.2108 0.0783  -0.0414 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.5284 0.3442 0.2585 -0.1896 0.1095  -0.0513 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.5215 0.3426 0.2939 -0.1715 0.1278  -0.0568 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.5167 0.3678 0.3180 -0.1568 0.1065  -0.0469 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.5120 0.3651 0.3531 -0.1419 0.1237  -0.0520 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.4894 0.3682 0.3661 -0.1251 0.1097  -0.0459 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.4562 0.3591 0.3333 -0.1206 0.0817  -0.0357 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.4491 0.3279 0.3636 -0.1135 0.1244  -0.0495 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.4849 0.3659 0.2329 -0.1837 0.0356  -0.0196 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.4882 0.3720 0.2220 -0.1954 0.0179  -0.0108 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.4882 0.4041 0.2503 -0.1885 -0.0120 0.0082  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.4624 0.3978 0.2541 -0.1731 -0.0169 0.0125  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.4618 0.3534 0.2182 -0.1809 0.0297  -0.0192 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.4326 0.3655 0.2522 -0.1454 0.0233  -0.0159 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.5031 0.4254 0.2635 -0.1976 -0.0297 0.0192  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.4929 0.4458 0.2913 -0.1890 -0.0533 0.0378  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.4741 0.4451 0.3023 -0.1744 -0.0531 0.0384  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.4739 0.4601 0.3227 -0.1772 -0.0717 0.0548  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.5493 0.4963 0.3293 -0.2151 -0.0806 0.0581  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.6675 0.5951 0.4130 -0.2410 -0.0919 0.0635  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.6941 0.6105 0.4261 -0.2394 -0.0754 0.0493  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.7371 0.6598 0.4697 -0.2644 -0.1189 0.0832  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.4465 0.4160 0.2810 -0.1589 -0.0323 0.0223  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.4033 0.3882 0.2644 -0.1436 -0.0299 0.0218  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.3619 0.3741 0.2654 -0.1259 -0.0404 0.0338  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.3565 0.3763 0.2739 -0.1161 -0.0403 0.0346  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.3968 0.3772 0.2636 -0.1280 -0.0081 0.0050  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.4353 0.3843 0.2658 -0.1445 0.0114  -0.0095 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.3166 0.3410 0.2409 -0.1217 -0.0461 0.0420  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2928 0.3378 0.2578 -0.1039 -0.0485 0.0512  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2683 0.3171 0.2456 -0.0877 -0.0359 0.0438  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2588 0.3196 0.2657 -0.0773 -0.0360 0.0524  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.3092 0.3664 0.2992 -0.1136 -0.0674 0.0734  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3557 0.4153 0.3494 -0.1232 -0.0814 0.0853  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3819 0.4560 0.4129 -0.1314 -0.1011 0.1110  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.4147 0.4829 0.4324 -0.1554 -0.1221 0.1251  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3662 0.4571 0.4453 -0.1129 -0.0942 0.1183  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.2601 0.2967 0.2161 -0.0868 -0.0241 0.0290  60  THR   A N   
416  C CA  . THR   A 54  ? 0.2574 0.2957 0.2227 -0.0722 -0.0133 0.0224  60  THR   A CA  
417  C C   . THR   A 54  ? 0.2427 0.2709 0.1968 -0.0656 -0.0020 0.0082  60  THR   A C   
418  O O   . THR   A 54  ? 0.2423 0.2591 0.1789 -0.0757 0.0016  0.0019  60  THR   A O   
419  C CB  . THR   A 54  ? 0.3032 0.3380 0.2627 -0.0800 -0.0125 0.0231  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.3368 0.3548 0.2670 -0.0954 -0.0087 0.0146  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.3077 0.3524 0.2835 -0.0884 -0.0254 0.0395  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.2187 0.2489 0.1835 -0.0500 0.0036  0.0043  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.2316 0.2540 0.1945 -0.0436 0.0107  -0.0054 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.2247 0.2471 0.1955 -0.0296 0.0120  -0.0061 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.2207 0.2463 0.1944 -0.0257 0.0120  -0.0015 61  GLY   A O   
426  N N   . VAL   A 56  ? 0.2188 0.2354 0.1928 -0.0238 0.0131  -0.0108 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.2168 0.2282 0.1919 -0.0141 0.0109  -0.0104 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.2240 0.2316 0.2007 -0.0094 0.0049  -0.0111 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.2337 0.2416 0.2188 -0.0119 0.0048  -0.0136 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.2355 0.2414 0.2166 -0.0146 0.0144  -0.0128 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2599 0.2574 0.2398 -0.0075 0.0078  -0.0101 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2405 0.2485 0.2180 -0.0196 0.0205  -0.0126 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.2243 0.2250 0.1918 -0.0035 0.0015  -0.0093 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.2179 0.2113 0.1828 -0.0008 -0.0054 -0.0100 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.2464 0.2235 0.1987 0.0011  -0.0127 -0.0088 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.2454 0.2149 0.1852 0.0017  -0.0099 -0.0074 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.2085 0.2034 0.1698 0.0012  -0.0033 -0.0091 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.2347 0.2171 0.1809 0.0050  0.0024  -0.0079 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.2405 0.2265 0.1891 0.0058  0.0114  -0.0048 63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.2647 0.2281 0.1929 0.0066  0.0002  -0.0099 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.2648 0.2365 0.2027 0.0094  0.0219  -0.0037 63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.2922 0.2371 0.2012 0.0085  0.0104  -0.0103 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.2889 0.2377 0.2040 0.0105  0.0229  -0.0074 63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.3078 0.2355 0.2065 0.0124  0.0377  -0.0079 63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.2460 0.2161 0.2010 0.0005  -0.0231 -0.0082 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.2796 0.2307 0.2193 -0.0014 -0.0352 -0.0047 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.3030 0.2353 0.2119 -0.0018 -0.0353 -0.0067 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.2885 0.2226 0.1999 -0.0009 -0.0351 -0.0091 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.2783 0.2297 0.2410 -0.0037 -0.0491 -0.0003 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.3100 0.2400 0.2559 -0.0088 -0.0669 0.0066  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.3274 0.2494 0.2644 -0.0110 -0.0699 0.0112  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.3491 0.2636 0.2822 -0.0133 -0.0817 0.0089  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.3726 0.2710 0.2879 -0.0187 -0.0888 0.0192  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.3892 0.2790 0.2990 -0.0218 -0.1013 0.0165  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.4085 0.2899 0.3087 -0.0250 -0.1054 0.0222  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.4605 0.3136 0.3319 -0.0363 -0.1274 0.0313  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.3384 0.2491 0.2161 -0.0041 -0.0341 -0.0060 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.3798 0.2638 0.2212 -0.0065 -0.0294 -0.0091 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.4152 0.2691 0.2248 -0.0161 -0.0478 -0.0053 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.4359 0.2726 0.2224 -0.0209 -0.0509 -0.0020 65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.4058 0.2831 0.2332 -0.0035 -0.0089 -0.0113 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.4471 0.2812 0.2251 -0.0077 0.0052  -0.0162 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.4208 0.2663 0.2276 -0.0206 -0.0619 -0.0047 66  SER   A N   
464  C CA  . SER   A 60  ? 0.4521 0.2679 0.2294 -0.0327 -0.0845 0.0013  66  SER   A CA  
465  C C   . SER   A 60  ? 0.4850 0.2576 0.2001 -0.0421 -0.0789 -0.0016 66  SER   A C   
466  O O   . SER   A 60  ? 0.5252 0.2747 0.2139 -0.0531 -0.0966 0.0058  66  SER   A O   
467  C CB  . SER   A 60  ? 0.5104 0.3239 0.2963 -0.0367 -0.1004 0.0028  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.6053 0.4082 0.3713 -0.0347 -0.0849 -0.0065 66  SER   A OG  
469  N N   . SER   A 61  ? 0.4836 0.2433 0.1764 -0.0385 -0.0531 -0.0111 67  SER   A N   
470  C CA  . SER   A 61  ? 0.5373 0.2486 0.1669 -0.0483 -0.0410 -0.0155 67  SER   A CA  
471  C C   . SER   A 61  ? 0.5608 0.2652 0.1763 -0.0487 -0.0327 -0.0129 67  SER   A C   
472  O O   . SER   A 61  ? 0.6214 0.2812 0.1799 -0.0588 -0.0227 -0.0158 67  SER   A O   
473  C CB  . SER   A 61  ? 0.5517 0.2498 0.1700 -0.0436 -0.0113 -0.0256 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.5706 0.3027 0.2330 -0.0291 0.0107  -0.0267 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.5304 0.2744 0.1935 -0.0395 -0.0362 -0.0078 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.5346 0.2759 0.1904 -0.0398 -0.0316 -0.0041 68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.5442 0.3051 0.2288 -0.0419 -0.0579 0.0068  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.5499 0.3097 0.2316 -0.0426 -0.0572 0.0112  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.5258 0.2954 0.2155 -0.0263 -0.0053 -0.0082 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.5696 0.3211 0.2426 -0.0231 0.0241  -0.0156 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.6346 0.3408 0.2535 -0.0311 0.0395  -0.0178 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.6988 0.3877 0.3113 -0.0268 0.0734  -0.0245 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.7472 0.3974 0.3212 -0.0335 0.0858  -0.0313 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.7584 0.3835 0.2931 -0.0460 0.0635  -0.0323 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.7297 0.3656 0.3080 -0.0283 0.1207  -0.0364 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.5342 0.3141 0.2526 -0.0420 -0.0784 0.0116  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.5284 0.3287 0.2875 -0.0426 -0.0992 0.0227  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.5006 0.3310 0.2959 -0.0321 -0.0834 0.0216  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.5005 0.3327 0.3066 -0.0343 -0.0917 0.0298  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.5768 0.3453 0.3045 -0.0581 -0.1261 0.0352  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.6594 0.4036 0.3654 -0.0708 -0.1506 0.0402  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.7529 0.4682 0.4346 -0.0885 -0.1829 0.0567  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.8663 0.5432 0.5018 -0.1062 -0.2059 0.0607  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.9649 0.5913 0.5292 -0.1264 -0.2205 0.0657  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.9818 0.5914 0.5147 -0.1301 -0.2129 0.0673  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 1.0123 0.6013 0.5315 -0.1445 -0.2416 0.0686  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.4592 0.3104 0.2703 -0.0221 -0.0610 0.0121  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.4290 0.3050 0.2676 -0.0144 -0.0456 0.0102  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.3903 0.2952 0.2629 -0.0074 -0.0350 0.0046  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.3980 0.3026 0.2663 -0.0061 -0.0319 0.0004  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.4690 0.3322 0.2791 -0.0127 -0.0262 0.0061  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.5742 0.4122 0.3524 -0.0189 -0.0296 0.0111  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.6639 0.4872 0.4166 -0.0165 -0.0052 0.0058  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.7639 0.5686 0.4925 -0.0205 -0.0021 0.0099  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.8412 0.5986 0.5092 -0.0325 -0.0065 0.0110  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.3458 0.2719 0.2471 -0.0043 -0.0282 0.0045  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.3088 0.2578 0.2339 -0.0009 -0.0174 -0.0003 71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.3243 0.2773 0.2417 0.0013  -0.0027 -0.0021 71  HIS   A C   
509  O O   . HIS   A 65  ? 0.3515 0.2975 0.2593 0.0013  0.0012  0.0000  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.3001 0.2639 0.2577 -0.0018 -0.0173 0.0004  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2883 0.2503 0.2662 -0.0034 -0.0295 0.0043  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.3179 0.2895 0.3155 -0.0033 -0.0272 0.0013  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.2954 0.2467 0.2795 -0.0060 -0.0446 0.0126  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2951 0.2627 0.3147 -0.0045 -0.0389 0.0076  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.3085 0.2643 0.3216 -0.0066 -0.0517 0.0154  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.2978 0.2619 0.2223 0.0028  0.0048  -0.0043 72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.2846 0.2552 0.2122 0.0043  0.0168  -0.0030 72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.2675 0.2587 0.2164 0.0011  0.0180  -0.0024 72  TYR   A C   
519  O O   . TYR   A 66  ? 0.2384 0.2363 0.1943 -0.0006 0.0139  -0.0037 72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.3068 0.2662 0.2235 0.0074  0.0252  -0.0026 72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.3466 0.2770 0.2311 0.0076  0.0287  -0.0039 72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.3810 0.2996 0.2535 0.0082  0.0393  -0.0023 72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.3843 0.2955 0.2466 0.0054  0.0216  -0.0065 72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.4240 0.3093 0.2583 0.0057  0.0441  -0.0037 72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.4197 0.2974 0.2427 0.0017  0.0238  -0.0076 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.4523 0.3156 0.2590 0.0013  0.0356  -0.0065 72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.5040 0.3278 0.2636 -0.0048 0.0398  -0.0081 72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.2566 0.2558 0.2133 -0.0014 0.0228  -0.0001 73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.2345 0.2485 0.2046 -0.0082 0.0217  0.0020  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2464 0.2667 0.2276 -0.0071 0.0235  0.0088  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2664 0.2814 0.2505 -0.0015 0.0316  0.0125  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2438 0.2603 0.2164 -0.0121 0.0251  0.0032  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2634 0.2702 0.2295 -0.0049 0.0310  0.0047  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.2580 0.2506 0.2090 0.0005  0.0287  0.0017  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.2340 0.2636 0.2233 -0.0127 0.0175  0.0115  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.2323 0.2696 0.2399 -0.0125 0.0172  0.0206  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.2252 0.2747 0.2428 -0.0250 0.0068  0.0284  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.2441 0.2920 0.2471 -0.0339 0.0012  0.0236  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2422 0.2744 0.2479 -0.0064 0.0181  0.0181  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2678 0.2826 0.2608 0.0031  0.0283  0.0135  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2462 0.2779 0.2403 -0.0102 0.0104  0.0111  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.2150 0.2738 0.2584 -0.0264 0.0046  0.0415  75  SER   A N   
543  C CA  . SER   A 69  ? 0.2201 0.2891 0.2754 -0.0396 -0.0096 0.0532  75  SER   A CA  
544  C C   . SER   A 69  ? 0.2221 0.2938 0.2900 -0.0341 -0.0097 0.0563  75  SER   A C   
545  O O   . SER   A 69  ? 0.2437 0.3122 0.3256 -0.0215 0.0023  0.0561  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2633 0.3425 0.3501 -0.0445 -0.0143 0.0700  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3582 0.4344 0.4333 -0.0499 -0.0142 0.0670  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.2096 0.2834 0.2690 -0.0440 -0.0211 0.0580  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.2099 0.2861 0.2812 -0.0387 -0.0211 0.0605  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.2298 0.3152 0.3151 -0.0524 -0.0375 0.0760  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.2452 0.3295 0.3152 -0.0694 -0.0503 0.0807  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.2191 0.2850 0.2643 -0.0328 -0.0158 0.0442  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.2285 0.2878 0.2450 -0.0435 -0.0199 0.0355  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.2455 0.2971 0.2457 -0.0427 -0.0136 0.0255  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.2403 0.2986 0.2470 -0.0549 -0.0279 0.0375  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.2577 0.3003 0.2363 -0.0521 -0.0124 0.0172  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.2617 0.3083 0.2408 -0.0653 -0.0261 0.0283  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.2650 0.3037 0.2320 -0.0639 -0.0172 0.0182  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.2119 0.3038 0.3253 -0.0468 -0.0375 0.0851  77  SER   A N   
560  C CA  . SER   A 71  ? 0.2014 0.3029 0.3340 -0.0604 -0.0554 0.1037  77  SER   A CA  
561  C C   . SER   A 71  ? 0.2147 0.3090 0.3121 -0.0725 -0.0653 0.0978  77  SER   A C   
562  O O   . SER   A 71  ? 0.2307 0.3149 0.2996 -0.0664 -0.0552 0.0796  77  SER   A O   
563  C CB  . SER   A 71  ? 0.2148 0.3257 0.3967 -0.0499 -0.0500 0.1172  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2421 0.3458 0.4142 -0.0375 -0.0373 0.1040  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.2282 0.3253 0.3265 -0.0914 -0.0856 0.1141  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2644 0.3503 0.3265 -0.1034 -0.0916 0.1082  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2724 0.3629 0.3515 -0.0894 -0.0841 0.1052  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2729 0.3752 0.3941 -0.0773 -0.0805 0.1146  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.3207 0.4029 0.3709 -0.1306 -0.1166 0.1271  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.4082 0.4759 0.4211 -0.1489 -0.1224 0.1239  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.5040 0.5613 0.4950 -0.1803 -0.1495 0.1429  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.6046 0.6424 0.5525 -0.1995 -0.1527 0.1371  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.6764 0.6927 0.5824 -0.2348 -0.1774 0.1510  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.2757 0.3553 0.3241 -0.0911 -0.0795 0.0921  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.2800 0.3633 0.3445 -0.0784 -0.0733 0.0892  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2722 0.3678 0.3728 -0.0823 -0.0862 0.1109  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2785 0.3742 0.3741 -0.1021 -0.1054 0.1271  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.3210 0.3900 0.3477 -0.0854 -0.0699 0.0760  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.3418 0.3969 0.3327 -0.0973 -0.0673 0.0672  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.2994 0.3606 0.2998 -0.1052 -0.0778 0.0798  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.2596 0.3633 0.3969 -0.0652 -0.0762 0.1126  80  SER   A N   
582  C CA  . SER   A 74  ? 0.2590 0.3753 0.4417 -0.0668 -0.0855 0.1348  80  SER   A CA  
583  C C   . SER   A 74  ? 0.2464 0.3634 0.4554 -0.0480 -0.0685 0.1291  80  SER   A C   
584  O O   . SER   A 74  ? 0.2360 0.3425 0.4231 -0.0356 -0.0526 0.1084  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2912 0.4187 0.5124 -0.0716 -0.0938 0.1553  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3337 0.4609 0.5739 -0.0543 -0.0733 0.1473  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.2329 0.3603 0.4867 -0.0479 -0.0737 0.1482  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2287 0.3541 0.5088 -0.0320 -0.0565 0.1439  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.2361 0.3607 0.5520 -0.0195 -0.0376 0.1465  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.2316 0.3682 0.5919 -0.0240 -0.0439 0.1680  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.2235 0.3604 0.5445 -0.0380 -0.0688 0.1664  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2701 0.4044 0.5640 -0.0461 -0.0801 0.1635  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2773 0.4246 0.6140 -0.0568 -0.0986 0.1923  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2813 0.4052 0.5635 -0.0309 -0.0611 0.1432  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.2341 0.3426 0.5311 -0.0055 -0.0150 0.1259  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.2467 0.3463 0.5652 0.0056  0.0080  0.1241  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.2794 0.3611 0.6023 0.0180  0.0317  0.1133  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.2889 0.3592 0.5733 0.0196  0.0314  0.0966  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2773 0.3665 0.5504 0.0063  0.0114  0.1071  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2930 0.3972 0.5658 -0.0066 -0.0088 0.1187  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.2958 0.3663 0.5721 0.0180  0.0390  0.0984  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.3334 0.4298 0.5641 -0.0076 -0.0082 0.1036  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.2891 0.3658 0.6601 0.0259  0.0535  0.1230  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.3399 0.3928 0.7114 0.0360  0.0805  0.1117  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.3724 0.3945 0.6834 0.0403  0.0970  0.0858  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.3923 0.4078 0.6894 0.0409  0.1037  0.0820  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.3452 0.3965 0.7867 0.0428  0.1048  0.1288  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.3841 0.4121 0.8327 0.0505  0.1308  0.1204  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.3990 0.4385 0.8709 0.0493  0.1203  0.1288  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.4241 0.4148 0.8503 0.0575  0.1663  0.1033  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.4241 0.4403 0.9009 0.0559  0.1450  0.1201  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.4466 0.4104 0.8737 0.0625  0.1919  0.0945  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.4388 0.4165 0.8933 0.0621  0.1812  0.1028  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.3810 0.3848 0.6541 0.0416  0.0997  0.0693  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.4177 0.3898 0.6310 0.0426  0.1100  0.0471  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.4433 0.3824 0.6524 0.0469  0.1372  0.0383  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.4365 0.3782 0.6598 0.0476  0.1348  0.0399  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.4322 0.4089 0.5987 0.0370  0.0844  0.0355  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.4646 0.4073 0.5739 0.0362  0.0913  0.0160  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.4272 0.4304 0.5942 0.0316  0.0626  0.0424  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.4715 0.3762 0.6567 0.0487  0.1639  0.0282  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.5151 0.3772 0.6852 0.0503  0.1956  0.0172  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.5383 0.3826 0.6613 0.0454  0.1840  0.0026  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.5504 0.4016 0.6342 0.0403  0.1571  -0.0043 85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.5935 0.4152 0.7224 0.0487  0.2216  0.0053  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.6840 0.5176 0.8606 0.0539  0.2386  0.0189  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.8075 0.6328 1.0476 0.0608  0.2736  0.0299  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.8583 0.6373 1.0796 0.0612  0.3131  0.0196  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.8273 0.6896 1.1357 0.0646  0.2624  0.0495  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.5425 0.3605 0.6699 0.0464  0.2061  -0.0022 86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.5733 0.3687 0.6550 0.0406  0.1969  -0.0163 86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.6218 0.3792 0.6245 0.0310  0.1922  -0.0336 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.6474 0.3767 0.6250 0.0290  0.2126  -0.0388 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.5807 0.3455 0.6769 0.0423  0.2285  -0.0198 86  ALA   A CB  
635  N N   . SER   A 81  ? 0.6308 0.3893 0.5984 0.0246  0.1635  -0.0404 87  SER   A N   
636  C CA  . SER   A 81  ? 0.6708 0.3961 0.5678 0.0133  0.1506  -0.0533 87  SER   A CA  
637  C C   . SER   A 81  ? 0.6989 0.4024 0.5658 0.0054  0.1384  -0.0618 87  SER   A C   
638  O O   . SER   A 81  ? 0.6859 0.4033 0.5888 0.0104  0.1417  -0.0581 87  SER   A O   
639  C CB  . SER   A 81  ? 0.6627 0.4220 0.5596 0.0131  0.1192  -0.0479 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.6511 0.4441 0.5701 0.0143  0.0915  -0.0432 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.7267 0.3985 0.5313 -0.0076 0.1207  -0.0711 88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.7380 0.3914 0.5168 -0.0167 0.1034  -0.0770 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.6781 0.3812 0.4996 -0.0111 0.0721  -0.0680 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.6815 0.3771 0.4961 -0.0163 0.0586  -0.0706 88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.8463 0.4507 0.5485 -0.0348 0.0889  -0.0860 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.9938 0.5351 0.6381 -0.0449 0.1217  -0.0975 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 1.1433 0.6609 0.7377 -0.0544 0.1160  -0.0991 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 1.2088 0.6631 0.7348 -0.0693 0.1346  -0.1098 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 1.1702 0.7296 0.7914 -0.0480 0.0939  -0.0898 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.6214 0.3719 0.4841 -0.0020 0.0615  -0.0578 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.5706 0.3635 0.4697 0.0021  0.0365  -0.0501 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.5082 0.3361 0.4637 0.0125  0.0460  -0.0410 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.4910 0.3404 0.4702 0.0140  0.0324  -0.0370 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.5581 0.3747 0.4594 0.0022  0.0178  -0.0453 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.5958 0.3803 0.4465 -0.0086 0.0060  -0.0508 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.6203 0.3941 0.4535 -0.0177 -0.0197 -0.0515 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.6275 0.3918 0.4502 -0.0106 0.0194  -0.0536 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.6655 0.4091 0.4539 -0.0298 -0.0347 -0.0533 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.6722 0.4055 0.4459 -0.0222 0.0066  -0.0570 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.7052 0.4283 0.4616 -0.0324 -0.0220 -0.0561 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.7718 0.4636 0.4813 -0.0459 -0.0384 -0.0563 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.4826 0.3161 0.4617 0.0188  0.0683  -0.0359 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.4403 0.3059 0.4756 0.0266  0.0743  -0.0236 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.4595 0.3084 0.5164 0.0312  0.1061  -0.0212 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.4758 0.2977 0.5110 0.0301  0.1255  -0.0267 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.3919 0.2970 0.4557 0.0294  0.0622  -0.0117 90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.3533 0.2754 0.4025 0.0255  0.0367  -0.0131 90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.3285 0.2725 0.3957 0.0248  0.0212  -0.0087 90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.3520 0.2696 0.3753 0.0228  0.0306  -0.0169 90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.3200 0.2775 0.3794 0.0214  0.0031  -0.0096 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.3243 0.2580 0.3428 0.0198  0.0106  -0.0168 90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.3176 0.2707 0.3553 0.0192  -0.0016 -0.0133 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.2834 0.2475 0.3187 0.0162  -0.0166 -0.0139 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.4479 0.3141 0.5533 0.0364  0.1129  -0.0110 91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.4522 0.3096 0.5960 0.0421  0.1440  -0.0039 91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.4456 0.3321 0.6249 0.0458  0.1425  0.0108  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.4437 0.3577 0.6172 0.0433  0.1169  0.0151  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.4400 0.3146 0.6308 0.0458  0.1437  0.0062  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.4232 0.3329 0.6151 0.0431  0.1089  0.0116  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.4232 0.3206 0.5570 0.0372  0.0925  -0.0027 91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.4401 0.3206 0.6601 0.0510  0.1702  0.0196  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.4239 0.3321 0.6848 0.0537  0.1676  0.0362  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.3896 0.3446 0.6936 0.0522  0.1376  0.0556  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.3810 0.3446 0.7146 0.0533  0.1353  0.0630  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.4225 0.3151 0.7307 0.0598  0.2046  0.0444  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.3677 0.3477 0.6639 0.0478  0.1135  0.0614  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.3329 0.3484 0.6517 0.0424  0.0844  0.0768  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.3114 0.3488 0.6323 0.0366  0.0668  0.0868  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.3219 0.3488 0.6225 0.0380  0.0752  0.0794  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.3443 0.3575 0.6187 0.0386  0.0671  0.0629  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.3485 0.3560 0.5696 0.0349  0.0557  0.0482  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.3443 0.3368 0.5238 0.0334  0.0486  0.0317  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.3444 0.3469 0.4953 0.0281  0.0290  0.0267  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.3641 0.3584 0.4866 0.0270  0.0281  0.0189  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.2982 0.3010 0.4014 0.0225  0.0126  0.0150  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.3910 0.3666 0.5052 0.0301  0.0447  0.0151  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.2869 0.3514 0.6263 0.0285  0.0417  0.1030  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2861 0.3664 0.6150 0.0197  0.0228  0.1098  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2738 0.3492 0.5444 0.0152  0.0101  0.0918  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2684 0.3452 0.5279 0.0126  0.0015  0.0886  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.2889 0.3941 0.6546 0.0089  0.0002  0.1354  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.3066 0.4226 0.7419 0.0109  0.0064  0.1598  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.3172 0.4429 0.7754 0.0066  0.0014  0.1736  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.3176 0.4354 0.8018 0.0160  0.0156  0.1717  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.3165 0.4540 0.8488 0.0077  0.0054  0.1996  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.3074 0.4367 0.8664 0.0175  0.0210  0.1976  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.3179 0.4574 0.9029 0.0134  0.0155  0.2122  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.3232 0.4752 0.9918 0.0148  0.0202  0.2407  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.2506 0.3201 0.4888 0.0143  0.0101  0.0812  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.2241 0.2904 0.4164 0.0095  -0.0011 0.0671  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.2102 0.2926 0.4009 -0.0030 -0.0189 0.0784  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.2038 0.2933 0.4110 -0.0057 -0.0202 0.0889  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.2373 0.2856 0.3967 0.0149  0.0090  0.0502  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.2420 0.2888 0.3642 0.0100  -0.0024 0.0385  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.2714 0.2980 0.3630 0.0148  0.0039  0.0229  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.2807 0.2892 0.3652 0.0199  0.0133  0.0161  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.2567 0.2837 0.3277 0.0115  -0.0023 0.0174  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1935 0.2792 0.3649 -0.0118 -0.0317 0.0772  96  SER   A N   
719  C CA  . SER   A 90  ? 0.1904 0.2838 0.3504 -0.0273 -0.0474 0.0868  96  SER   A CA  
720  C C   . SER   A 90  ? 0.1967 0.2813 0.3177 -0.0304 -0.0458 0.0718  96  SER   A C   
721  O O   . SER   A 90  ? 0.1985 0.2732 0.3039 -0.0210 -0.0359 0.0554  96  SER   A O   
722  C CB  . SER   A 90  ? 0.2084 0.3036 0.3629 -0.0372 -0.0583 0.0929  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2427 0.3279 0.3728 -0.0330 -0.0519 0.0758  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.2017 0.2884 0.3092 -0.0446 -0.0560 0.0788  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.2059 0.2833 0.2794 -0.0493 -0.0530 0.0661  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.2025 0.2771 0.2772 -0.0366 -0.0419 0.0560  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.2135 0.2794 0.2663 -0.0346 -0.0362 0.0424  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.2174 0.2840 0.2662 -0.0515 -0.0488 0.0532  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2781 0.3422 0.3168 -0.0665 -0.0578 0.0620  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.3277 0.3802 0.3338 -0.0856 -0.0622 0.0634  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.2951 0.3639 0.3494 -0.0664 -0.0627 0.0703  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.3351 0.3840 0.3342 -0.0975 -0.0703 0.0725  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.3251 0.3856 0.3553 -0.0860 -0.0717 0.0777  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1974 0.2780 0.2994 -0.0291 -0.0382 0.0641  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1969 0.2712 0.2978 -0.0181 -0.0260 0.0556  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1914 0.2714 0.2979 -0.0238 -0.0290 0.0637  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1956 0.2865 0.3255 -0.0321 -0.0387 0.0810  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1884 0.2594 0.3148 -0.0061 -0.0139 0.0579  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.2035 0.2596 0.3209 0.0043  0.0021  0.0477  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.2160 0.2585 0.2971 0.0063  0.0019  0.0310  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2279 0.2747 0.3688 0.0134  0.0183  0.0503  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1858 0.2581 0.2732 -0.0199 -0.0221 0.0528  99  MET   A N   
743  C CA  . MET   A 93  ? 0.1815 0.2576 0.2710 -0.0248 -0.0237 0.0581  99  MET   A CA  
744  C C   . MET   A 93  ? 0.1947 0.2635 0.2901 -0.0124 -0.0086 0.0533  99  MET   A C   
745  O O   . MET   A 93  ? 0.2162 0.2720 0.2898 -0.0051 -0.0010 0.0395  99  MET   A O   
746  C CB  . MET   A 93  ? 0.2013 0.2713 0.2571 -0.0331 -0.0273 0.0478  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.2410 0.3106 0.2816 -0.0483 -0.0383 0.0507  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.3000 0.3557 0.3030 -0.0574 -0.0343 0.0362  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2736 0.3227 0.2756 -0.0407 -0.0226 0.0205  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1846 0.2592 0.3090 -0.0110 -0.0042 0.0653  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1995 0.2624 0.3261 -0.0002 0.0140  0.0603  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.2089 0.2727 0.3273 -0.0032 0.0137  0.0598  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.2016 0.2781 0.3300 -0.0136 0.0008  0.0700  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1963 0.2615 0.3684 0.0057  0.0265  0.0740  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2365 0.2981 0.4243 0.0108  0.0327  0.0754  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2510 0.3109 0.4888 0.0178  0.0519  0.0884  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2491 0.2893 0.3970 0.0168  0.0416  0.0562  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.2123 0.2602 0.3134 0.0049  0.0282  0.0497  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.2184 0.2640 0.3124 0.0045  0.0320  0.0485  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.2242 0.2509 0.3192 0.0144  0.0546  0.0455  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.2438 0.2541 0.3294 0.0200  0.0657  0.0395  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.2470 0.2865 0.3029 0.0017  0.0249  0.0351  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.2239 0.2491 0.3258 0.0153  0.0626  0.0489  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.2506 0.2523 0.3444 0.0229  0.0865  0.0445  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.2965 0.2793 0.3381 0.0225  0.0840  0.0293  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.2972 0.2885 0.3276 0.0185  0.0723  0.0274  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.2491 0.2579 0.3762 0.0236  0.0958  0.0561  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.2795 0.2590 0.3920 0.0304  0.1238  0.0501  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.2322 0.2612 0.4194 0.0224  0.0942  0.0753  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.3182 0.2743 0.3291 0.0253  0.0938  0.0196  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.3534 0.2902 0.3170 0.0228  0.0871  0.0084  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.3767 0.2817 0.3058 0.0226  0.0945  -0.0003 103 GLY   A C   
773  O O   . GLY   A 97  ? 0.3856 0.2842 0.3272 0.0251  0.1061  0.0006  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.3844 0.2672 0.2696 0.0181  0.0868  -0.0076 104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.4186 0.2651 0.2615 0.0140  0.0904  -0.0153 104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.4074 0.2614 0.2483 0.0115  0.0703  -0.0178 104 HIS   A C   
777  O O   . HIS   A 98  ? 0.3930 0.2688 0.2444 0.0103  0.0495  -0.0161 104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.4550 0.2702 0.2495 0.0074  0.0885  -0.0192 104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.5336 0.3024 0.2756 -0.0005 0.0942  -0.0264 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.5889 0.3267 0.3176 -0.0001 0.1244  -0.0306 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.5713 0.3191 0.2741 -0.0101 0.0732  -0.0293 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.6330 0.3277 0.3054 -0.0109 0.1219  -0.0377 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.6322 0.3318 0.2872 -0.0178 0.0891  -0.0362 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.4189 0.2534 0.2483 0.0107  0.0786  -0.0218 105 SER   A N   
785  C CA  . SER   A 99  ? 0.4315 0.2694 0.2580 0.0081  0.0612  -0.0243 105 SER   A CA  
786  C C   . SER   A 99  ? 0.4911 0.2886 0.2820 0.0035  0.0736  -0.0313 105 SER   A C   
787  O O   . SER   A 99  ? 0.5004 0.2888 0.3037 0.0077  0.0982  -0.0318 105 SER   A O   
788  C CB  . SER   A 99  ? 0.4125 0.2884 0.2881 0.0140  0.0570  -0.0188 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.4419 0.3185 0.3176 0.0125  0.0460  -0.0213 105 SER   A OG  
790  N N   . GLU   A 100 ? 0.5261 0.2953 0.2721 -0.0064 0.0577  -0.0358 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.5831 0.3098 0.2876 -0.0143 0.0649  -0.0431 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.6002 0.3362 0.3096 -0.0179 0.0391  -0.0428 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.5851 0.3567 0.3272 -0.0145 0.0180  -0.0371 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.6553 0.3278 0.2927 -0.0269 0.0727  -0.0483 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.7242 0.3956 0.3415 -0.0331 0.0526  -0.0436 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.8144 0.4293 0.3642 -0.0457 0.0665  -0.0483 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.8297 0.3975 0.3223 -0.0606 0.0618  -0.0534 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.8223 0.4369 0.3729 -0.0421 0.0822  -0.0469 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.6395 0.3460 0.3240 -0.0237 0.0440  -0.0489 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.6331 0.3554 0.3355 -0.0245 0.0227  -0.0476 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.6016 0.3466 0.3184 -0.0276 -0.0116 -0.0408 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.5842 0.3674 0.3474 -0.0203 -0.0215 -0.0366 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.6824 0.3531 0.3323 -0.0366 0.0283  -0.0558 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.7068 0.3434 0.3307 -0.0365 0.0652  -0.0623 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.6648 0.3265 0.3148 -0.0275 0.0750  -0.0571 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.5886 0.3082 0.2674 -0.0392 -0.0287 -0.0386 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.5599 0.2969 0.2569 -0.0430 -0.0602 -0.0297 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.4991 0.2803 0.2452 -0.0322 -0.0609 -0.0240 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.4808 0.2787 0.2519 -0.0336 -0.0819 -0.0165 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.4656 0.2642 0.2282 -0.0221 -0.0373 -0.0268 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.4214 0.2582 0.2254 -0.0139 -0.0366 -0.0224 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.3720 0.2436 0.2215 -0.0071 -0.0388 -0.0210 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.3338 0.2323 0.2134 -0.0035 -0.0406 -0.0177 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.4295 0.2704 0.2338 -0.0081 -0.0140 -0.0239 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.4507 0.2619 0.2148 -0.0147 -0.0130 -0.0239 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.4429 0.2467 0.1959 -0.0218 -0.0339 -0.0194 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.4718 0.2656 0.2175 -0.0135 0.0090  -0.0272 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.3686 0.2377 0.2213 -0.0065 -0.0370 -0.0237 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.3395 0.2391 0.2323 -0.0014 -0.0388 -0.0218 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.3253 0.2373 0.2395 -0.0036 -0.0562 -0.0175 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.3366 0.2309 0.2379 -0.0102 -0.0729 -0.0148 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.3577 0.2498 0.2495 -0.0010 -0.0359 -0.0247 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.4086 0.2941 0.2969 0.0041  -0.0098 -0.0274 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.2836 0.2224 0.2298 0.0002  -0.0522 -0.0159 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.2703 0.2195 0.2431 -0.0013 -0.0622 -0.0121 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.2773 0.2338 0.2577 -0.0013 -0.0593 -0.0100 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.2687 0.2363 0.2775 -0.0015 -0.0597 -0.0076 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.2866 0.2349 0.2433 -0.0011 -0.0542 -0.0110 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.2764 0.2315 0.2392 -0.0010 -0.0503 -0.0094 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.2571 0.2333 0.2403 0.0007  -0.0376 -0.0113 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.2587 0.2425 0.2397 0.0018  -0.0298 -0.0131 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.2438 0.2270 0.2473 -0.0008 -0.0358 -0.0100 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.2338 0.2295 0.2489 -0.0028 -0.0231 -0.0128 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.2382 0.2382 0.2399 -0.0041 -0.0150 -0.0137 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.2534 0.2486 0.2476 -0.0028 -0.0161 -0.0124 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.2524 0.2486 0.2961 -0.0048 -0.0198 -0.0120 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.2747 0.2703 0.3389 -0.0043 -0.0244 -0.0106 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.2594 0.2595 0.3059 -0.0097 -0.0033 -0.0161 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2975 0.2919 0.4008 -0.0053 -0.0194 -0.0075 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.2261 0.2345 0.2256 -0.0081 -0.0080 -0.0148 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.2112 0.2246 0.2023 -0.0125 -0.0021 -0.0139 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.2068 0.2188 0.2013 -0.0209 0.0064  -0.0173 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.2005 0.2107 0.1985 -0.0251 0.0097  -0.0193 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.2022 0.2229 0.1892 -0.0143 -0.0034 -0.0097 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.2038 0.2306 0.1864 -0.0223 -0.0013 -0.0057 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.2108 0.2372 0.1917 -0.0187 0.0010  -0.0041 114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.2171 0.2523 0.2051 -0.0251 -0.0060 0.0024  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.2185 0.2279 0.2106 -0.0239 0.0121  -0.0187 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.2364 0.2382 0.2285 -0.0331 0.0244  -0.0235 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.2593 0.2597 0.2343 -0.0422 0.0280  -0.0235 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.2518 0.2574 0.2258 -0.0382 0.0236  -0.0204 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2750 0.2709 0.2883 -0.0286 0.0303  -0.0251 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.3590 0.3545 0.3965 -0.0212 0.0246  -0.0226 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3936 0.3839 0.4584 -0.0189 0.0297  -0.0209 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.4642 0.4450 0.5393 -0.0262 0.0509  -0.0265 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.4819 0.4568 0.5812 -0.0269 0.0606  -0.0274 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.4595 0.4399 0.5819 -0.0201 0.0477  -0.0212 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.4927 0.4533 0.5938 -0.0353 0.0847  -0.0341 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.2938 0.2839 0.2535 -0.0560 0.0368  -0.0272 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.3423 0.3256 0.2817 -0.0687 0.0399  -0.0276 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.3956 0.3598 0.3333 -0.0757 0.0600  -0.0368 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.3928 0.3528 0.3523 -0.0687 0.0699  -0.0404 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.3475 0.3282 0.2631 -0.0837 0.0322  -0.0231 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.3513 0.3118 0.2483 -0.0968 0.0438  -0.0294 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.4377 0.3881 0.3518 -0.0904 0.0671  -0.0400 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.4779 0.4053 0.3886 -0.0984 0.0906  -0.0497 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.4890 0.3969 0.3942 -0.1058 0.1079  -0.0564 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.5112 0.4023 0.4311 -0.1061 0.1313  -0.0637 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.5509 0.4619 0.4275 -0.1170 0.0944  -0.0525 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.6436 0.5464 0.4805 -0.1364 0.0817  -0.0483 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.7542 0.6389 0.5555 -0.1575 0.0808  -0.0490 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.7889 0.6828 0.5776 -0.1661 0.0587  -0.0383 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.7592 0.6163 0.5458 -0.1673 0.1050  -0.0606 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.4744 0.3833 0.3622 -0.1115 0.0983  -0.0534 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.4710 0.3594 0.3492 -0.1199 0.1151  -0.0594 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.4329 0.3339 0.3528 -0.1025 0.1168  -0.0579 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.4524 0.3362 0.3745 -0.1071 0.1351  -0.0630 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.5065 0.3854 0.3411 -0.1383 0.1039  -0.0559 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.5780 0.4424 0.3702 -0.1591 0.0974  -0.0546 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.5969 0.4824 0.3869 -0.1596 0.0697  -0.0424 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.6252 0.4533 0.3758 -0.1816 0.1152  -0.0632 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.6305 0.4954 0.3816 -0.1818 0.0680  -0.0425 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.6516 0.4800 0.3733 -0.1967 0.0946  -0.0556 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.3822 0.3099 0.3330 -0.0843 0.0986  -0.0507 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.3314 0.2702 0.3190 -0.0699 0.0952  -0.0477 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.2885 0.2497 0.2797 -0.0594 0.0700  -0.0398 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.2929 0.2646 0.2703 -0.0585 0.0565  -0.0358 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.2741 0.2406 0.2854 -0.0519 0.0658  -0.0377 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.2649 0.2477 0.2795 -0.0426 0.0456  -0.0316 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.2657 0.2518 0.2531 -0.0503 0.0383  -0.0292 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.2881 0.2638 0.2616 -0.0608 0.0461  -0.0313 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.2786 0.2635 0.3226 -0.0344 0.0430  -0.0299 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.2815 0.2783 0.3221 -0.0270 0.0240  -0.0251 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.2808 0.2643 0.3593 -0.0273 0.0446  -0.0278 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.2554 0.2541 0.2375 -0.0455 0.0240  -0.0236 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.2486 0.2531 0.2153 -0.0521 0.0149  -0.0176 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.2348 0.2486 0.2143 -0.0432 0.0058  -0.0136 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.2304 0.2454 0.2045 -0.0491 0.0023  -0.0097 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.2631 0.2754 0.2241 -0.0526 0.0077  -0.0120 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.2639 0.2852 0.2226 -0.0573 -0.0038 -0.0018 121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.2859 0.2878 0.2307 -0.0641 0.0154  -0.0155 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.2163 0.2340 0.2100 -0.0304 0.0016  -0.0142 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.2213 0.2435 0.2235 -0.0227 -0.0058 -0.0116 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.2121 0.2309 0.2199 -0.0126 -0.0105 -0.0131 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.2115 0.2259 0.2212 -0.0113 -0.0093 -0.0151 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.2037 0.2217 0.2122 -0.0070 -0.0159 -0.0115 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.2080 0.2156 0.2117 -0.0010 -0.0214 -0.0129 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.2144 0.2177 0.2073 0.0027  -0.0196 -0.0113 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1989 0.2087 0.1978 0.0029  -0.0165 -0.0082 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.2272 0.2291 0.2411 0.0002  -0.0287 -0.0141 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.2476 0.2548 0.2678 -0.0001 -0.0278 -0.0135 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.2358 0.2375 0.2678 -0.0019 -0.0291 -0.0143 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.2670 0.2668 0.2978 0.0015  -0.0367 -0.0141 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.2157 0.2049 0.1928 0.0051  -0.0201 -0.0128 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.2163 0.1944 0.1811 0.0081  -0.0131 -0.0126 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.2366 0.2085 0.2027 0.0094  -0.0139 -0.0138 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.2409 0.2054 0.2036 0.0079  -0.0236 -0.0162 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.2513 0.2072 0.1902 0.0079  -0.0133 -0.0152 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.2732 0.2105 0.1960 0.0098  -0.0009 -0.0167 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.2510 0.2130 0.1900 0.0073  -0.0107 -0.0135 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.2338 0.2083 0.2084 0.0121  -0.0037 -0.0109 125 SER   A N   
922  C CA  . SER   A 119 ? 0.2391 0.2085 0.2188 0.0136  -0.0017 -0.0114 125 SER   A CA  
923  C C   . SER   A 119 ? 0.2914 0.2435 0.2660 0.0170  0.0148  -0.0116 125 SER   A C   
924  O O   . SER   A 119 ? 0.3298 0.2644 0.2951 0.0173  0.0187  -0.0155 125 SER   A O   
925  C CB  . SER   A 119 ? 0.2462 0.2388 0.2525 0.0126  -0.0054 -0.0055 125 SER   A CB  
926  O OG  . SER   A 119 ? 0.2613 0.2514 0.2775 0.0146  -0.0026 -0.0043 125 SER   A OG  
927  N N   . THR   A 120 ? 0.2994 0.2536 0.2809 0.0189  0.0265  -0.0075 126 THR   A N   
928  C CA  . THR   A 120 ? 0.3130 0.2478 0.2947 0.0224  0.0478  -0.0074 126 THR   A CA  
929  C C   . THR   A 120 ? 0.3479 0.2673 0.3117 0.0225  0.0593  -0.0091 126 THR   A C   
930  O O   . THR   A 120 ? 0.3210 0.2522 0.2814 0.0208  0.0497  -0.0079 126 THR   A O   
931  C CB  . THR   A 120 ? 0.3115 0.2668 0.3395 0.0260  0.0560  0.0044  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.3119 0.2883 0.3620 0.0253  0.0535  0.0138  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.3090 0.2826 0.3554 0.0246  0.0428  0.0082  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.3854 0.2771 0.3389 0.0243  0.0822  -0.0119 127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.4293 0.3041 0.3676 0.0244  0.0971  -0.0129 127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.4740 0.3230 0.4188 0.0277  0.1294  -0.0130 127 GLY   A C   
937  O O   . GLY   A 121 ? 0.4801 0.3327 0.4549 0.0312  0.1396  -0.0091 127 GLY   A O   
938  N N   . GLY   A 122 ? 0.5154 0.3376 0.4350 0.0264  0.1472  -0.0167 128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.5553 0.3462 0.4790 0.0290  0.1842  -0.0178 128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.5374 0.3519 0.5198 0.0363  0.1993  -0.0042 128 GLY   A C   
941  O O   . GLY   A 122 ? 0.5080 0.3662 0.5364 0.0391  0.1800  0.0079  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.5458 0.3290 0.5267 0.0380  0.2343  -0.0056 129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.5258 0.3273 0.5682 0.0450  0.2523  0.0088  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.4968 0.3302 0.5490 0.0444  0.2297  0.0159  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.4735 0.3382 0.5865 0.0484  0.2284  0.0319  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.5137 0.3458 0.6329 0.0512  0.2544  0.0248  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.5862 0.3867 0.7145 0.0539  0.2868  0.0210  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.6353 0.3855 0.7249 0.0520  0.3211  0.0088  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.5758 0.4027 0.7560 0.0572  0.2784  0.0322  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.4943 0.3195 0.4897 0.0385  0.2106  0.0056  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.4643 0.3156 0.4646 0.0375  0.1910  0.0105  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.4052 0.3032 0.4391 0.0367  0.1589  0.0194  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.4002 0.3221 0.4518 0.0356  0.1466  0.0264  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.3742 0.2818 0.4124 0.0359  0.1460  0.0185  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.3395 0.2845 0.4014 0.0332  0.1178  0.0258  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.3489 0.2888 0.3695 0.0293  0.0988  0.0141  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.3978 0.3083 0.3830 0.0288  0.1062  0.0038  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.3232 0.2860 0.4369 0.0354  0.1199  0.0385  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.3252 0.2961 0.4969 0.0392  0.1377  0.0549  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.3260 0.3050 0.5461 0.0420  0.1441  0.0665  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.3232 0.3244 0.5209 0.0342  0.1182  0.0678  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.2858 0.2513 0.3109 0.0252  0.0755  0.0164  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.2666 0.2322 0.2668 0.0219  0.0581  0.0084  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.2392 0.2323 0.2672 0.0189  0.0437  0.0157  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.2390 0.2520 0.2893 0.0153  0.0379  0.0249  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.2720 0.2333 0.2430 0.0186  0.0472  0.0018  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.2731 0.2531 0.2594 0.0166  0.0438  0.0076  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.2747 0.2398 0.2342 0.0154  0.0299  -0.0033 132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.2175 0.2090 0.2418 0.0187  0.0379  0.0123  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.2007 0.2141 0.2457 0.0145  0.0250  0.0190  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.2291 0.2433 0.2538 0.0108  0.0119  0.0110  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.2564 0.2542 0.2595 0.0129  0.0114  0.0022  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.2110 0.2413 0.2420 0.0038  0.0017  0.0148  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.2118 0.2420 0.2294 -0.0002 -0.0063 0.0080  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1991 0.2385 0.2268 -0.0053 -0.0121 0.0123  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1869 0.2372 0.2265 -0.0117 -0.0158 0.0222  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1965 0.2313 0.2071 -0.0067 -0.0085 0.0074  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1970 0.2254 0.2003 -0.0029 -0.0031 0.0054  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.2121 0.2277 0.2007 0.0009  -0.0030 -0.0020 134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.2036 0.2381 0.2165 -0.0041 0.0004  0.0128  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.2275 0.2349 0.2063 0.0035  0.0016  -0.0029 134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.2178 0.2454 0.2237 -0.0006 0.0067  0.0110  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.2253 0.2388 0.2119 0.0030  0.0076  0.0027  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.2043 0.2383 0.2273 -0.0038 -0.0146 0.0059  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1823 0.2222 0.2111 -0.0091 -0.0188 0.0084  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1858 0.2265 0.2042 -0.0191 -0.0195 0.0067  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1905 0.2245 0.2026 -0.0183 -0.0164 -0.0009 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1652 0.1973 0.1943 -0.0041 -0.0200 0.0020  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1961 0.2422 0.2121 -0.0301 -0.0231 0.0145  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.2234 0.2628 0.2208 -0.0429 -0.0210 0.0117  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.2392 0.2699 0.2318 -0.0455 -0.0152 0.0048  136 ASP   A C   
992  O O   . ASP   A 130 ? 0.2416 0.2749 0.2434 -0.0425 -0.0179 0.0069  136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.2622 0.3047 0.2519 -0.0580 -0.0296 0.0236  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.3211 0.3497 0.2815 -0.0752 -0.0267 0.0205  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.3151 0.3380 0.2676 -0.0747 -0.0193 0.0131  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.3609 0.3813 0.3038 -0.0902 -0.0305 0.0251  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.2212 0.2401 0.2026 -0.0509 -0.0051 -0.0033 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.2346 0.2425 0.2155 -0.0545 0.0048  -0.0090 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.2709 0.2611 0.2232 -0.0729 0.0152  -0.0115 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.3051 0.2812 0.2537 -0.0781 0.0283  -0.0168 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.2325 0.2379 0.2354 -0.0434 0.0116  -0.0161 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.2292 0.2447 0.2499 -0.0295 -0.0002 -0.0139 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.2218 0.2214 0.2232 -0.0441 0.0193  -0.0205 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.2725 0.2599 0.2034 -0.0840 0.0109  -0.0079 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.3027 0.2672 0.1980 -0.1045 0.0207  -0.0112 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.3641 0.3133 0.2323 -0.1216 0.0204  -0.0075 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.4040 0.3253 0.2394 -0.1386 0.0358  -0.0142 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.3086 0.2741 0.1877 -0.1136 0.0116  -0.0062 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.3103 0.2859 0.2103 -0.0990 0.0150  -0.0108 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.3211 0.2995 0.2083 -0.1080 0.0049  -0.0042 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.3120 0.3111 0.2174 -0.1025 -0.0137 0.0093  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.3227 0.3299 0.2310 -0.1067 -0.0247 0.0187  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.3315 0.3272 0.2193 -0.1182 -0.0217 0.0158  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.2908 0.3163 0.2251 -0.0997 -0.0374 0.0315  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.3618 0.3259 0.2419 -0.1184 0.0047  0.0029  139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.3859 0.3359 0.2411 -0.1350 0.0022  0.0083  139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.3925 0.3317 0.2543 -0.1301 0.0201  -0.0008 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.4212 0.3409 0.2553 -0.1459 0.0245  0.0008  139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.4011 0.3711 0.2711 -0.1346 -0.0218 0.0254  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.4216 0.4152 0.3356 -0.1110 -0.0244 0.0259  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.3904 0.3931 0.3262 -0.0938 -0.0182 0.0179  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.4196 0.4199 0.3438 -0.1110 -0.0330 0.0346  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.3739 0.3236 0.2718 -0.1098 0.0296  -0.0089 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.3658 0.3089 0.2818 -0.1032 0.0446  -0.0153 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.3918 0.3062 0.2927 -0.1132 0.0721  -0.0261 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.3882 0.3026 0.3189 -0.1019 0.0857  -0.0330 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.3329 0.2978 0.2948 -0.0801 0.0387  -0.0164 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.3170 0.3052 0.2925 -0.0701 0.0167  -0.0074 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.3034 0.3042 0.3123 -0.0513 0.0122  -0.0100 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.3352 0.3254 0.3053 -0.0759 0.0089  0.0006  140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.4143 0.3003 0.2676 -0.1364 0.0810  -0.0268 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.4567 0.3068 0.2852 -0.1502 0.1117  -0.0382 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.4729 0.3132 0.3342 -0.1411 0.1380  -0.0457 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.4813 0.3018 0.3513 -0.1420 0.1656  -0.0551 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.5071 0.3211 0.2666 -0.1812 0.1157  -0.0374 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.5475 0.3679 0.2741 -0.1952 0.0867  -0.0261 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.6126 0.3884 0.2654 -0.2302 0.0921  -0.0258 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.5396 0.3761 0.2820 -0.1863 0.0800  -0.0275 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.4630 0.3191 0.3505 -0.1308 0.1292  -0.0404 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.4597 0.3096 0.3856 -0.1216 0.1507  -0.0449 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.4541 0.3216 0.4398 -0.1013 0.1537  -0.0466 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.4594 0.3180 0.4827 -0.0957 0.1751  -0.0496 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.4360 0.2991 0.3736 -0.1167 0.1374  -0.0379 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.3971 0.2966 0.3548 -0.1023 0.1036  -0.0288 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.4027 0.3132 0.3342 -0.1086 0.0801  -0.0201 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.3610 0.2870 0.3697 -0.0808 0.0910  -0.0270 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.3772 0.3182 0.3418 -0.0909 0.0583  -0.0144 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.3533 0.3021 0.3599 -0.0749 0.0640  -0.0192 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.3526 0.2824 0.4096 -0.0676 0.0996  -0.0296 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.3464 0.3169 0.3878 -0.0575 0.0480  -0.0167 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.3460 0.2995 0.4378 -0.0515 0.0784  -0.0250 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.3423 0.3135 0.4214 -0.0472 0.0541  -0.0199 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.4385 0.3295 0.4352 -0.0911 0.1323  -0.0434 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.4325 0.3376 0.4807 -0.0747 0.1316  -0.0430 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.4974 0.3789 0.5618 -0.0789 0.1641  -0.0500 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.4825 0.3724 0.6012 -0.0664 0.1673  -0.0473 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.4013 0.3283 0.4463 -0.0671 0.1067  -0.0393 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.3790 0.3299 0.4256 -0.0582 0.0780  -0.0321 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.3764 0.3418 0.4130 -0.0536 0.0602  -0.0295 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.3599 0.3226 0.4522 -0.0441 0.0701  -0.0286 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.5661 0.4160 0.5836 -0.0978 0.1877  -0.0579 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.6302 0.4502 0.6559 -0.1045 0.2249  -0.0664 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.7066 0.4930 0.7319 -0.1143 0.2617  -0.0724 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.7416 0.4970 0.7694 -0.1220 0.2980  -0.0806 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.6745 0.4731 0.6413 -0.1223 0.2312  -0.0730 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.7205 0.5465 0.6927 -0.1132 0.2040  -0.0684 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.7187 0.5644 0.7448 -0.0960 0.1994  -0.0648 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.7534 0.5804 0.6776 -0.1240 0.1865  -0.0671 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.7353 0.5226 0.7521 -0.1161 0.2562  -0.0694 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.7815 0.5332 0.7938 -0.1267 0.2936  -0.0753 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.7773 0.5482 0.8452 -0.1118 0.2881  -0.0680 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.7958 0.5409 0.8733 -0.1172 0.3195  -0.0714 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.8675 0.5849 0.7925 -0.1531 0.3000  -0.0805 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.9510 0.6938 0.8466 -0.1543 0.2589  -0.0710 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 1.0900 0.8095 0.9020 -0.1803 0.2493  -0.0713 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 1.1390 0.8419 0.9094 -0.1956 0.2464  -0.0682 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 1.1337 0.8507 0.9224 -0.1866 0.2432  -0.0734 145 GLU   A OE2 
1078 N N1  . A1BSS B .   ? 0.5003 0.3351 0.4087 0.0164  0.0753  -0.0320 201 A1BSS A N1  
1079 N N3  . A1BSS B .   ? 0.6482 0.4071 0.4551 0.0080  0.1197  -0.0395 201 A1BSS A N3  
1080 C C4  . A1BSS B .   ? 0.5205 0.3226 0.3877 0.0085  0.0682  -0.0414 201 A1BSS A C4  
1081 C C5  . A1BSS B .   ? 0.5259 0.3561 0.4257 0.0168  0.0840  -0.0311 201 A1BSS A C5  
1082 C C6  . A1BSS B .   ? 0.5987 0.3979 0.4433 0.0083  0.0765  -0.0387 201 A1BSS A C6  
1083 C C7  . A1BSS B .   ? 0.6063 0.4350 0.4586 0.0070  0.0471  -0.0347 201 A1BSS A C7  
1084 C C8  . A1BSS B .   ? 0.6255 0.4464 0.4548 0.0039  0.0437  -0.0347 201 A1BSS A C8  
1085 C C10 . A1BSS B .   ? 0.6526 0.3928 0.4671 0.0084  0.1345  -0.0445 201 A1BSS A C10 
1086 O O1  . A1BSS B .   ? 0.4819 0.3352 0.4189 0.0227  0.0930  -0.0225 201 A1BSS A O1  
1087 C C3  . A1BSS B .   ? 0.4954 0.3206 0.3721 0.0066  0.0388  -0.0394 201 A1BSS A C3  
1088 C C2  . A1BSS B .   ? 0.4560 0.3216 0.3854 0.0141  0.0364  -0.0309 201 A1BSS A C2  
1089 C C12 . A1BSS B .   ? 0.4524 0.3258 0.4124 0.0223  0.0699  -0.0222 201 A1BSS A C12 
1090 C C1  . A1BSS B .   ? 0.4320 0.3258 0.3929 0.0195  0.0428  -0.0221 201 A1BSS A C1  
1091 C C   . A1BSS B .   ? 0.3963 0.3250 0.4022 0.0231  0.0377  -0.0120 201 A1BSS A C   
1092 O O   . A1BSS B .   ? 0.3939 0.3231 0.4221 0.0260  0.0473  -0.0085 201 A1BSS A O   
1093 N N   . A1BSS B .   ? 0.3626 0.3175 0.3802 0.0216  0.0233  -0.0071 201 A1BSS A N   
1094 C C11 . A1BSS B .   ? 0.6289 0.4047 0.4567 0.0084  0.1006  -0.0403 201 A1BSS A C11 
1095 N N4  . A1BSS B .   ? 0.6615 0.3904 0.4631 0.0081  0.1471  -0.0442 201 A1BSS A N4  
1096 C C9  . A1BSS B .   ? 0.6327 0.4182 0.4555 0.0081  0.0938  -0.0374 201 A1BSS A C9  
1097 N N2  . A1BSS B .   ? 0.6272 0.4435 0.4635 0.0083  0.0683  -0.0331 201 A1BSS A N2  
# 
