data_7I62
# 
_entry.id   7I62 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   7I62         pdb_00007i62 10.2210/pdb7i62/pdb 
WWPDB D_1001408361 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_initial_refinement_model 
# 
_pdbx_database_status.entry_id                        7I62 
_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   2025-03-12 
_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-[(1-benzofuran-7-yl)acetyl]piperidine-3-carboxamide' 286.326   1  ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                   65.409    1  ?         ? ? ? 
4 water       nat water                                                        18.015    72 ?         ? ? ? 
# 
_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-[(1-benzofuran-7-yl)acetyl]piperidine-3-carboxamide' A1B4L 
3 'ZINC ION'                                                   ZN    
4 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 
A1B4L non-polymer         . '(3S)-1-[(1-benzofuran-7-yl)acetyl]piperidine-3-carboxamide' ? 'C16 H18 N2 O3'  286.326 
ALA   'L-peptide linking' y ALANINE                                                      ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                     ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                   ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                              ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                     ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                    ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                              ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                      ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                    ? 'C6 H10 N3 O2 1' 156.162 
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        A1B4L 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B4L 
_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 A1B4L 1  201 201 A1B4L LIG A . 
C 3 ZN    1  202 1   ZN    ZN  A . 
D 4 HOH   1  301 8   HOH   HOH A . 
D 4 HOH   2  302 7   HOH   HOH A . 
D 4 HOH   3  303 18  HOH   HOH A . 
D 4 HOH   4  304 9   HOH   HOH A . 
D 4 HOH   5  305 59  HOH   HOH A . 
D 4 HOH   6  306 27  HOH   HOH A . 
D 4 HOH   7  307 29  HOH   HOH A . 
D 4 HOH   8  308 36  HOH   HOH A . 
D 4 HOH   9  309 32  HOH   HOH A . 
D 4 HOH   10 310 47  HOH   HOH A . 
D 4 HOH   11 311 25  HOH   HOH A . 
D 4 HOH   12 312 12  HOH   HOH A . 
D 4 HOH   13 313 72  HOH   HOH A . 
D 4 HOH   14 314 10  HOH   HOH A . 
D 4 HOH   15 315 48  HOH   HOH A . 
D 4 HOH   16 316 40  HOH   HOH A . 
D 4 HOH   17 317 14  HOH   HOH A . 
D 4 HOH   18 318 16  HOH   HOH A . 
D 4 HOH   19 319 57  HOH   HOH A . 
D 4 HOH   20 320 23  HOH   HOH A . 
D 4 HOH   21 321 53  HOH   HOH A . 
D 4 HOH   22 322 73  HOH   HOH A . 
D 4 HOH   23 323 41  HOH   HOH A . 
D 4 HOH   24 324 2   HOH   HOH A . 
D 4 HOH   25 325 37  HOH   HOH A . 
D 4 HOH   26 326 17  HOH   HOH A . 
D 4 HOH   27 327 6   HOH   HOH A . 
D 4 HOH   28 328 13  HOH   HOH A . 
D 4 HOH   29 329 35  HOH   HOH A . 
D 4 HOH   30 330 4   HOH   HOH A . 
D 4 HOH   31 331 22  HOH   HOH A . 
D 4 HOH   32 332 67  HOH   HOH A . 
D 4 HOH   33 333 68  HOH   HOH A . 
D 4 HOH   34 334 21  HOH   HOH A . 
D 4 HOH   35 335 55  HOH   HOH A . 
D 4 HOH   36 336 30  HOH   HOH A . 
D 4 HOH   37 337 39  HOH   HOH A . 
D 4 HOH   38 338 5   HOH   HOH A . 
D 4 HOH   39 339 60  HOH   HOH A . 
D 4 HOH   40 340 20  HOH   HOH A . 
D 4 HOH   41 341 19  HOH   HOH A . 
D 4 HOH   42 342 34  HOH   HOH A . 
D 4 HOH   43 343 50  HOH   HOH A . 
D 4 HOH   44 344 56  HOH   HOH A . 
D 4 HOH   45 345 49  HOH   HOH A . 
D 4 HOH   46 346 51  HOH   HOH A . 
D 4 HOH   47 347 24  HOH   HOH A . 
D 4 HOH   48 348 3   HOH   HOH A . 
D 4 HOH   49 349 71  HOH   HOH A . 
D 4 HOH   50 350 45  HOH   HOH A . 
D 4 HOH   51 351 64  HOH   HOH A . 
D 4 HOH   52 352 28  HOH   HOH A . 
D 4 HOH   53 353 54  HOH   HOH A . 
D 4 HOH   54 354 15  HOH   HOH A . 
D 4 HOH   55 355 58  HOH   HOH A . 
D 4 HOH   56 356 61  HOH   HOH A . 
D 4 HOH   57 357 31  HOH   HOH A . 
D 4 HOH   58 358 74  HOH   HOH A . 
D 4 HOH   59 359 26  HOH   HOH A . 
D 4 HOH   60 360 11  HOH   HOH A . 
D 4 HOH   61 361 46  HOH   HOH A . 
D 4 HOH   62 362 63  HOH   HOH A . 
D 4 HOH   63 363 43  HOH   HOH A . 
D 4 HOH   64 364 66  HOH   HOH A . 
D 4 HOH   65 365 44  HOH   HOH A . 
D 4 HOH   66 366 38  HOH   HOH A . 
D 4 HOH   67 367 52  HOH   HOH A . 
D 4 HOH   68 368 70  HOH   HOH A . 
D 4 HOH   69 369 69  HOH   HOH A . 
D 4 HOH   70 370 62  HOH   HOH A . 
D 4 HOH   71 371 42  HOH   HOH A . 
D 4 HOH   72 372 65  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           7I62 
_cell.length_a           72.801 
_cell.length_b           62.004 
_cell.length_c           32.817 
_cell.angle_alpha        90.00 
_cell.angle_beta         93.02 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I62 
_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          7I62 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.33 
_exptl_crystal.density_percent_sol   47.14 
_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   2025-01-24 
_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   0.92204 
_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        0.92204 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I62 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.18 
_reflns.d_resolution_high            1.65 
_reflns.number_obs                   17515 
_reflns.percent_possible_obs         99.8 
_reflns.pdbx_Rmerge_I_obs            0.302 
_reflns.pdbx_netI_over_sigmaI        2.5 
_reflns.pdbx_redundancy              6.9 
_reflns.pdbx_Rrim_I_all              0.327 
_reflns.pdbx_Rpim_I_all              0.124 
_reflns.pdbx_CC_half                 0.980 
_reflns.pdbx_number_measured_all     120404 
_reflns.pdbx_chi_squared             0.28 
_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                  1.65 
_reflns_shell.d_res_low                   1.68 
_reflns_shell.number_measured_all         5810 
_reflns_shell.number_unique_obs           829 
_reflns_shell.Rmerge_I_obs                3.794 
_reflns_shell.pdbx_chi_squared            0.03 
_reflns_shell.pdbx_redundancy             7.0 
_reflns_shell.percent_possible_obs        97.2 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.1 
_reflns_shell.pdbx_Rrim_I_all             4.097 
_reflns_shell.pdbx_Rpim_I_all             1.531 
_reflns_shell.pdbx_CC_half                0.280 
_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                                 7I62 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     12698 
_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                             18.18 
_refine.ls_d_res_high                            1.654 
_refine.ls_percent_reflns_obs                    72.7 
_refine.ls_R_factor_obs                          0.2674 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2650 
_refine.ls_R_factor_R_free                       0.3129 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.920 
_refine.ls_number_reflns_R_free                  625 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.938 
_refine.correlation_coeff_Fo_to_Fc_free          0.896 
_refine.B_iso_mean                               43.09 
_refine.aniso_B[1][1]                            3.26660 
_refine.aniso_B[2][2]                            -2.09390 
_refine.aniso_B[3][3]                            -1.17280 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -8.32820 
_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             0.185 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.174 
_refine.pdbx_overall_SU_R_Blow_DPI               0.187 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.174 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I62 
_refine_analyze.Luzzati_coordinate_error_obs    0.37 
_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         22 
_refine_hist.number_atoms_solvent             72 
_refine_hist.number_atoms_total               1168 
_refine_hist.d_res_high                       1.654 
_refine_hist.d_res_low                        18.18 
# 
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  1123 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.02  ? 2.00  1528 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  373  '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  206  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1123 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.82  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           17.31 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  137  '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  861  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   32 
_refine_ls_shell.d_res_high                       1.65 
_refine_ls_shell.d_res_low                        1.82 
_refine_ls_shell.number_reflns_R_work             392 
_refine_ls_shell.R_factor_R_work                  0.5196 
_refine_ls_shell.percent_reflns_obs               9.28 
_refine_ls_shell.R_factor_R_free                  0.6100 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.39 
_refine_ls_shell.number_reflns_R_free             18 
_refine_ls_shell.number_reflns_all                410 
_refine_ls_shell.R_factor_all                     0.5239 
# 
_struct.entry_id                  7I62 
_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-0036702-001 (A71EV2A-x4908)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I62 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_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              7I62 
_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 
# 
_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 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P4 AA4 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 ? ? ? ? ? ? ? 2.389 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.489 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 1.920 ? ? 
# 
_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 97.0  ? 
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_555 109.1 ? 
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_555 108.7 ? 
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_555 117.5 ? 
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 88.9  ? 
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_555 127.6 ? 
# 
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 ? GLY A 122 ? GLY A 119 GLY A 128 
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 SER A 37  ? N SER A 43  O ARG A 10  ? O ARG A 16  
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 GLY A 116 ? O GLY A 122 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O ASP A 130 ? O ASP A 136 N HIS A 91  ? N HIS A 97  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7I62 
_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     368 
_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     369 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_556 
_pdbx_validate_symm_contact.dist              1.99 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASN 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     14 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -91.87 
_pdbx_validate_torsion.psi             34.56 
# 
_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         15.1281 
_pdbx_refine_tls.origin_y         6.6339 
_pdbx_refine_tls.origin_z         14.3412 
_pdbx_refine_tls.T[1][1]          0.0548 
_pdbx_refine_tls.T[2][2]          -0.0709 
_pdbx_refine_tls.T[3][3]          -0.0071 
_pdbx_refine_tls.T[1][2]          0.0414 
_pdbx_refine_tls.T[1][3]          -0.1673 
_pdbx_refine_tls.T[2][3]          -0.0222 
_pdbx_refine_tls.L[1][1]          1.2589 
_pdbx_refine_tls.L[2][2]          8.8668 
_pdbx_refine_tls.L[3][3]          2.0471 
_pdbx_refine_tls.L[1][2]          2.8749 
_pdbx_refine_tls.L[1][3]          -0.4095 
_pdbx_refine_tls.L[2][3]          -3.0778 
_pdbx_refine_tls.S[1][1]          -0.2156 
_pdbx_refine_tls.S[1][2]          0.0854 
_pdbx_refine_tls.S[1][3]          0.0032 
_pdbx_refine_tls.S[2][1]          0.3374 
_pdbx_refine_tls.S[2][2]          0.2862 
_pdbx_refine_tls.S[2][3]          -0.3246 
_pdbx_refine_tls.S[3][1]          -0.0717 
_pdbx_refine_tls.S[3][2]          -0.1907 
_pdbx_refine_tls.S[3][3]          -0.0706 
# 
_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 
A1B4L N1   N  N N 1   
A1B4L C4   C  N N 2   
A1B4L C5   C  N N 3   
A1B4L C6   C  N N 4   
A1B4L C7   C  Y N 5   
A1B4L C8   C  Y N 6   
A1B4L C10  C  Y N 7   
A1B4L C13  C  Y N 8   
A1B4L C15  C  N N 9   
A1B4L O1   O  N N 10  
A1B4L C3   C  N N 11  
A1B4L C2   C  N N 12  
A1B4L C1   C  N S 13  
A1B4L C    C  N N 14  
A1B4L O    O  N N 15  
A1B4L N    N  N N 16  
A1B4L C14  C  Y N 17  
A1B4L O2   O  Y N 18  
A1B4L C12  C  Y N 19  
A1B4L C11  C  Y N 20  
A1B4L C9   C  Y N 21  
A1B4L H7   H  N N 22  
A1B4L H8   H  N N 23  
A1B4L H10  H  N N 24  
A1B4L H9   H  N N 25  
A1B4L H11  H  N N 26  
A1B4L H13  H  N N 27  
A1B4L H15  H  N N 28  
A1B4L H17  H  N N 29  
A1B4L H16  H  N N 30  
A1B4L H6   H  N N 31  
A1B4L H5   H  N N 32  
A1B4L H4   H  N N 33  
A1B4L H3   H  N N 34  
A1B4L H    H  N N 35  
A1B4L H1   H  N N 36  
A1B4L H2   H  N N 37  
A1B4L H14  H  N N 38  
A1B4L H12  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 
GLN   N    N  N N 127 
GLN   CA   C  N S 128 
GLN   C    C  N N 129 
GLN   O    O  N N 130 
GLN   CB   C  N N 131 
GLN   CG   C  N N 132 
GLN   CD   C  N N 133 
GLN   OE1  O  N N 134 
GLN   NE2  N  N N 135 
GLN   OXT  O  N N 136 
GLN   H    H  N N 137 
GLN   H2   H  N N 138 
GLN   HA   H  N N 139 
GLN   HB2  H  N N 140 
GLN   HB3  H  N N 141 
GLN   HG2  H  N N 142 
GLN   HG3  H  N N 143 
GLN   HE21 H  N N 144 
GLN   HE22 H  N N 145 
GLN   HXT  H  N N 146 
GLU   N    N  N N 147 
GLU   CA   C  N S 148 
GLU   C    C  N N 149 
GLU   O    O  N N 150 
GLU   CB   C  N N 151 
GLU   CG   C  N N 152 
GLU   CD   C  N N 153 
GLU   OE1  O  N N 154 
GLU   OE2  O  N N 155 
GLU   OXT  O  N N 156 
GLU   H    H  N N 157 
GLU   H2   H  N N 158 
GLU   HA   H  N N 159 
GLU   HB2  H  N N 160 
GLU   HB3  H  N N 161 
GLU   HG2  H  N N 162 
GLU   HG3  H  N N 163 
GLU   HE2  H  N N 164 
GLU   HXT  H  N N 165 
GLY   N    N  N N 166 
GLY   CA   C  N N 167 
GLY   C    C  N N 168 
GLY   O    O  N N 169 
GLY   OXT  O  N N 170 
GLY   H    H  N N 171 
GLY   H2   H  N N 172 
GLY   HA2  H  N N 173 
GLY   HA3  H  N N 174 
GLY   HXT  H  N N 175 
HIS   N    N  N N 176 
HIS   CA   C  N S 177 
HIS   C    C  N N 178 
HIS   O    O  N N 179 
HIS   CB   C  N N 180 
HIS   CG   C  Y N 181 
HIS   ND1  N  Y N 182 
HIS   CD2  C  Y N 183 
HIS   CE1  C  Y N 184 
HIS   NE2  N  Y N 185 
HIS   OXT  O  N N 186 
HIS   H    H  N N 187 
HIS   H2   H  N N 188 
HIS   HA   H  N N 189 
HIS   HB2  H  N N 190 
HIS   HB3  H  N N 191 
HIS   HD1  H  N N 192 
HIS   HD2  H  N N 193 
HIS   HE1  H  N N 194 
HIS   HE2  H  N N 195 
HIS   HXT  H  N N 196 
HOH   O    O  N N 197 
HOH   H1   H  N N 198 
HOH   H2   H  N N 199 
ILE   N    N  N N 200 
ILE   CA   C  N S 201 
ILE   C    C  N N 202 
ILE   O    O  N N 203 
ILE   CB   C  N S 204 
ILE   CG1  C  N N 205 
ILE   CG2  C  N N 206 
ILE   CD1  C  N N 207 
ILE   OXT  O  N N 208 
ILE   H    H  N N 209 
ILE   H2   H  N N 210 
ILE   HA   H  N N 211 
ILE   HB   H  N N 212 
ILE   HG12 H  N N 213 
ILE   HG13 H  N N 214 
ILE   HG21 H  N N 215 
ILE   HG22 H  N N 216 
ILE   HG23 H  N N 217 
ILE   HD11 H  N N 218 
ILE   HD12 H  N N 219 
ILE   HD13 H  N N 220 
ILE   HXT  H  N N 221 
LEU   N    N  N N 222 
LEU   CA   C  N S 223 
LEU   C    C  N N 224 
LEU   O    O  N N 225 
LEU   CB   C  N N 226 
LEU   CG   C  N N 227 
LEU   CD1  C  N N 228 
LEU   CD2  C  N N 229 
LEU   OXT  O  N N 230 
LEU   H    H  N N 231 
LEU   H2   H  N N 232 
LEU   HA   H  N N 233 
LEU   HB2  H  N N 234 
LEU   HB3  H  N N 235 
LEU   HG   H  N N 236 
LEU   HD11 H  N N 237 
LEU   HD12 H  N N 238 
LEU   HD13 H  N N 239 
LEU   HD21 H  N N 240 
LEU   HD22 H  N N 241 
LEU   HD23 H  N N 242 
LEU   HXT  H  N N 243 
LYS   N    N  N N 244 
LYS   CA   C  N S 245 
LYS   C    C  N N 246 
LYS   O    O  N N 247 
LYS   CB   C  N N 248 
LYS   CG   C  N N 249 
LYS   CD   C  N N 250 
LYS   CE   C  N N 251 
LYS   NZ   N  N N 252 
LYS   OXT  O  N N 253 
LYS   H    H  N N 254 
LYS   H2   H  N N 255 
LYS   HA   H  N N 256 
LYS   HB2  H  N N 257 
LYS   HB3  H  N N 258 
LYS   HG2  H  N N 259 
LYS   HG3  H  N N 260 
LYS   HD2  H  N N 261 
LYS   HD3  H  N N 262 
LYS   HE2  H  N N 263 
LYS   HE3  H  N N 264 
LYS   HZ1  H  N N 265 
LYS   HZ2  H  N N 266 
LYS   HZ3  H  N N 267 
LYS   HXT  H  N N 268 
MET   N    N  N N 269 
MET   CA   C  N S 270 
MET   C    C  N N 271 
MET   O    O  N N 272 
MET   CB   C  N N 273 
MET   CG   C  N N 274 
MET   SD   S  N N 275 
MET   CE   C  N N 276 
MET   OXT  O  N N 277 
MET   H    H  N N 278 
MET   H2   H  N N 279 
MET   HA   H  N N 280 
MET   HB2  H  N N 281 
MET   HB3  H  N N 282 
MET   HG2  H  N N 283 
MET   HG3  H  N N 284 
MET   HE1  H  N N 285 
MET   HE2  H  N N 286 
MET   HE3  H  N N 287 
MET   HXT  H  N N 288 
PHE   N    N  N N 289 
PHE   CA   C  N S 290 
PHE   C    C  N N 291 
PHE   O    O  N N 292 
PHE   CB   C  N N 293 
PHE   CG   C  Y N 294 
PHE   CD1  C  Y N 295 
PHE   CD2  C  Y N 296 
PHE   CE1  C  Y N 297 
PHE   CE2  C  Y N 298 
PHE   CZ   C  Y N 299 
PHE   OXT  O  N N 300 
PHE   H    H  N N 301 
PHE   H2   H  N N 302 
PHE   HA   H  N N 303 
PHE   HB2  H  N N 304 
PHE   HB3  H  N N 305 
PHE   HD1  H  N N 306 
PHE   HD2  H  N N 307 
PHE   HE1  H  N N 308 
PHE   HE2  H  N N 309 
PHE   HZ   H  N N 310 
PHE   HXT  H  N N 311 
PRO   N    N  N N 312 
PRO   CA   C  N S 313 
PRO   C    C  N N 314 
PRO   O    O  N N 315 
PRO   CB   C  N N 316 
PRO   CG   C  N N 317 
PRO   CD   C  N N 318 
PRO   OXT  O  N N 319 
PRO   H    H  N N 320 
PRO   HA   H  N N 321 
PRO   HB2  H  N N 322 
PRO   HB3  H  N N 323 
PRO   HG2  H  N N 324 
PRO   HG3  H  N N 325 
PRO   HD2  H  N N 326 
PRO   HD3  H  N N 327 
PRO   HXT  H  N N 328 
SER   N    N  N N 329 
SER   CA   C  N S 330 
SER   C    C  N N 331 
SER   O    O  N N 332 
SER   CB   C  N N 333 
SER   OG   O  N N 334 
SER   OXT  O  N N 335 
SER   H    H  N N 336 
SER   H2   H  N N 337 
SER   HA   H  N N 338 
SER   HB2  H  N N 339 
SER   HB3  H  N N 340 
SER   HG   H  N N 341 
SER   HXT  H  N N 342 
THR   N    N  N N 343 
THR   CA   C  N S 344 
THR   C    C  N N 345 
THR   O    O  N N 346 
THR   CB   C  N R 347 
THR   OG1  O  N N 348 
THR   CG2  C  N N 349 
THR   OXT  O  N N 350 
THR   H    H  N N 351 
THR   H2   H  N N 352 
THR   HA   H  N N 353 
THR   HB   H  N N 354 
THR   HG1  H  N N 355 
THR   HG21 H  N N 356 
THR   HG22 H  N N 357 
THR   HG23 H  N N 358 
THR   HXT  H  N N 359 
TRP   N    N  N N 360 
TRP   CA   C  N S 361 
TRP   C    C  N N 362 
TRP   O    O  N N 363 
TRP   CB   C  N N 364 
TRP   CG   C  Y N 365 
TRP   CD1  C  Y N 366 
TRP   CD2  C  Y N 367 
TRP   NE1  N  Y N 368 
TRP   CE2  C  Y N 369 
TRP   CE3  C  Y N 370 
TRP   CZ2  C  Y N 371 
TRP   CZ3  C  Y N 372 
TRP   CH2  C  Y N 373 
TRP   OXT  O  N N 374 
TRP   H    H  N N 375 
TRP   H2   H  N N 376 
TRP   HA   H  N N 377 
TRP   HB2  H  N N 378 
TRP   HB3  H  N N 379 
TRP   HD1  H  N N 380 
TRP   HE1  H  N N 381 
TRP   HE3  H  N N 382 
TRP   HZ2  H  N N 383 
TRP   HZ3  H  N N 384 
TRP   HH2  H  N N 385 
TRP   HXT  H  N N 386 
TYR   N    N  N N 387 
TYR   CA   C  N S 388 
TYR   C    C  N N 389 
TYR   O    O  N N 390 
TYR   CB   C  N N 391 
TYR   CG   C  Y N 392 
TYR   CD1  C  Y N 393 
TYR   CD2  C  Y N 394 
TYR   CE1  C  Y N 395 
TYR   CE2  C  Y N 396 
TYR   CZ   C  Y N 397 
TYR   OH   O  N N 398 
TYR   OXT  O  N N 399 
TYR   H    H  N N 400 
TYR   H2   H  N N 401 
TYR   HA   H  N N 402 
TYR   HB2  H  N N 403 
TYR   HB3  H  N N 404 
TYR   HD1  H  N N 405 
TYR   HD2  H  N N 406 
TYR   HE1  H  N N 407 
TYR   HE2  H  N N 408 
TYR   HH   H  N N 409 
TYR   HXT  H  N N 410 
VAL   N    N  N N 411 
VAL   CA   C  N S 412 
VAL   C    C  N N 413 
VAL   O    O  N N 414 
VAL   CB   C  N N 415 
VAL   CG1  C  N N 416 
VAL   CG2  C  N N 417 
VAL   OXT  O  N N 418 
VAL   H    H  N N 419 
VAL   H2   H  N N 420 
VAL   HA   H  N N 421 
VAL   HB   H  N N 422 
VAL   HG11 H  N N 423 
VAL   HG12 H  N N 424 
VAL   HG13 H  N N 425 
VAL   HG21 H  N N 426 
VAL   HG22 H  N N 427 
VAL   HG23 H  N N 428 
VAL   HXT  H  N N 429 
ZN    ZN   ZN N N 430 
# 
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 
A1B4L N   C    sing N N 1   
A1B4L O   C    doub N N 2   
A1B4L C   C1   sing N N 3   
A1B4L C1  C2   sing N N 4   
A1B4L C2  C3   sing N N 5   
A1B4L C3  C4   sing N N 6   
A1B4L C4  N1   sing N N 7   
A1B4L N1  C5   sing N N 8   
A1B4L C5  O1   doub N N 9   
A1B4L C6  C5   sing N N 10  
A1B4L C7  C6   sing N N 11  
A1B4L C7  C8   doub Y N 12  
A1B4L C8  C9   sing Y N 13  
A1B4L C9  C10  doub Y N 14  
A1B4L C10 C11  sing Y N 15  
A1B4L C11 C12  sing Y N 16  
A1B4L C12 C13  doub Y N 17  
A1B4L C13 O2   sing Y N 18  
A1B4L O2  C14  sing Y N 19  
A1B4L C14 C7   sing Y N 20  
A1B4L C11 C14  doub Y N 21  
A1B4L C15 N1   sing N N 22  
A1B4L C1  C15  sing N N 23  
A1B4L C4  H7   sing N N 24  
A1B4L C4  H8   sing N N 25  
A1B4L C6  H10  sing N N 26  
A1B4L C6  H9   sing N N 27  
A1B4L C8  H11  sing N N 28  
A1B4L C10 H13  sing N N 29  
A1B4L C13 H15  sing N N 30  
A1B4L C15 H17  sing N N 31  
A1B4L C15 H16  sing N N 32  
A1B4L C3  H6   sing N N 33  
A1B4L C3  H5   sing N N 34  
A1B4L C2  H4   sing N N 35  
A1B4L C2  H3   sing N N 36  
A1B4L C1  H    sing N N 37  
A1B4L N   H1   sing N N 38  
A1B4L N   H2   sing N N 39  
A1B4L C12 H14  sing N N 40  
A1B4L C9  H12  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 
GLN   N   CA   sing N N 124 
GLN   N   H    sing N N 125 
GLN   N   H2   sing N N 126 
GLN   CA  C    sing N N 127 
GLN   CA  CB   sing N N 128 
GLN   CA  HA   sing N N 129 
GLN   C   O    doub N N 130 
GLN   C   OXT  sing N N 131 
GLN   CB  CG   sing N N 132 
GLN   CB  HB2  sing N N 133 
GLN   CB  HB3  sing N N 134 
GLN   CG  CD   sing N N 135 
GLN   CG  HG2  sing N N 136 
GLN   CG  HG3  sing N N 137 
GLN   CD  OE1  doub N N 138 
GLN   CD  NE2  sing N N 139 
GLN   NE2 HE21 sing N N 140 
GLN   NE2 HE22 sing N N 141 
GLN   OXT HXT  sing N N 142 
GLU   N   CA   sing N N 143 
GLU   N   H    sing N N 144 
GLU   N   H2   sing N N 145 
GLU   CA  C    sing N N 146 
GLU   CA  CB   sing N N 147 
GLU   CA  HA   sing N N 148 
GLU   C   O    doub N N 149 
GLU   C   OXT  sing N N 150 
GLU   CB  CG   sing N N 151 
GLU   CB  HB2  sing N N 152 
GLU   CB  HB3  sing N N 153 
GLU   CG  CD   sing N N 154 
GLU   CG  HG2  sing N N 155 
GLU   CG  HG3  sing N N 156 
GLU   CD  OE1  doub N N 157 
GLU   CD  OE2  sing N N 158 
GLU   OE2 HE2  sing N N 159 
GLU   OXT HXT  sing N N 160 
GLY   N   CA   sing N N 161 
GLY   N   H    sing N N 162 
GLY   N   H2   sing N N 163 
GLY   CA  C    sing N N 164 
GLY   CA  HA2  sing N N 165 
GLY   CA  HA3  sing N N 166 
GLY   C   O    doub N N 167 
GLY   C   OXT  sing N N 168 
GLY   OXT HXT  sing N N 169 
HIS   N   CA   sing N N 170 
HIS   N   H    sing N N 171 
HIS   N   H2   sing N N 172 
HIS   CA  C    sing N N 173 
HIS   CA  CB   sing N N 174 
HIS   CA  HA   sing N N 175 
HIS   C   O    doub N N 176 
HIS   C   OXT  sing N N 177 
HIS   CB  CG   sing N N 178 
HIS   CB  HB2  sing N N 179 
HIS   CB  HB3  sing N N 180 
HIS   CG  ND1  sing Y N 181 
HIS   CG  CD2  doub Y N 182 
HIS   ND1 CE1  doub Y N 183 
HIS   ND1 HD1  sing N N 184 
HIS   CD2 NE2  sing Y N 185 
HIS   CD2 HD2  sing N N 186 
HIS   CE1 NE2  sing Y N 187 
HIS   CE1 HE1  sing N N 188 
HIS   NE2 HE2  sing N N 189 
HIS   OXT HXT  sing N N 190 
HOH   O   H1   sing N N 191 
HOH   O   H2   sing N N 192 
ILE   N   CA   sing N N 193 
ILE   N   H    sing N N 194 
ILE   N   H2   sing N N 195 
ILE   CA  C    sing N N 196 
ILE   CA  CB   sing N N 197 
ILE   CA  HA   sing N N 198 
ILE   C   O    doub N N 199 
ILE   C   OXT  sing N N 200 
ILE   CB  CG1  sing N N 201 
ILE   CB  CG2  sing N N 202 
ILE   CB  HB   sing N N 203 
ILE   CG1 CD1  sing N N 204 
ILE   CG1 HG12 sing N N 205 
ILE   CG1 HG13 sing N N 206 
ILE   CG2 HG21 sing N N 207 
ILE   CG2 HG22 sing N N 208 
ILE   CG2 HG23 sing N N 209 
ILE   CD1 HD11 sing N N 210 
ILE   CD1 HD12 sing N N 211 
ILE   CD1 HD13 sing N N 212 
ILE   OXT HXT  sing N N 213 
LEU   N   CA   sing N N 214 
LEU   N   H    sing N N 215 
LEU   N   H2   sing N N 216 
LEU   CA  C    sing N N 217 
LEU   CA  CB   sing N N 218 
LEU   CA  HA   sing N N 219 
LEU   C   O    doub N N 220 
LEU   C   OXT  sing N N 221 
LEU   CB  CG   sing N N 222 
LEU   CB  HB2  sing N N 223 
LEU   CB  HB3  sing N N 224 
LEU   CG  CD1  sing N N 225 
LEU   CG  CD2  sing N N 226 
LEU   CG  HG   sing N N 227 
LEU   CD1 HD11 sing N N 228 
LEU   CD1 HD12 sing N N 229 
LEU   CD1 HD13 sing N N 230 
LEU   CD2 HD21 sing N N 231 
LEU   CD2 HD22 sing N N 232 
LEU   CD2 HD23 sing N N 233 
LEU   OXT HXT  sing N N 234 
LYS   N   CA   sing N N 235 
LYS   N   H    sing N N 236 
LYS   N   H2   sing N N 237 
LYS   CA  C    sing N N 238 
LYS   CA  CB   sing N N 239 
LYS   CA  HA   sing N N 240 
LYS   C   O    doub N N 241 
LYS   C   OXT  sing N N 242 
LYS   CB  CG   sing N N 243 
LYS   CB  HB2  sing N N 244 
LYS   CB  HB3  sing N N 245 
LYS   CG  CD   sing N N 246 
LYS   CG  HG2  sing N N 247 
LYS   CG  HG3  sing N N 248 
LYS   CD  CE   sing N N 249 
LYS   CD  HD2  sing N N 250 
LYS   CD  HD3  sing N N 251 
LYS   CE  NZ   sing N N 252 
LYS   CE  HE2  sing N N 253 
LYS   CE  HE3  sing N N 254 
LYS   NZ  HZ1  sing N N 255 
LYS   NZ  HZ2  sing N N 256 
LYS   NZ  HZ3  sing N N 257 
LYS   OXT HXT  sing N N 258 
MET   N   CA   sing N N 259 
MET   N   H    sing N N 260 
MET   N   H2   sing N N 261 
MET   CA  C    sing N N 262 
MET   CA  CB   sing N N 263 
MET   CA  HA   sing N N 264 
MET   C   O    doub N N 265 
MET   C   OXT  sing N N 266 
MET   CB  CG   sing N N 267 
MET   CB  HB2  sing N N 268 
MET   CB  HB3  sing N N 269 
MET   CG  SD   sing N N 270 
MET   CG  HG2  sing N N 271 
MET   CG  HG3  sing N N 272 
MET   SD  CE   sing N N 273 
MET   CE  HE1  sing N N 274 
MET   CE  HE2  sing N N 275 
MET   CE  HE3  sing N N 276 
MET   OXT HXT  sing N N 277 
PHE   N   CA   sing N N 278 
PHE   N   H    sing N N 279 
PHE   N   H2   sing N N 280 
PHE   CA  C    sing N N 281 
PHE   CA  CB   sing N N 282 
PHE   CA  HA   sing N N 283 
PHE   C   O    doub N N 284 
PHE   C   OXT  sing N N 285 
PHE   CB  CG   sing N N 286 
PHE   CB  HB2  sing N N 287 
PHE   CB  HB3  sing N N 288 
PHE   CG  CD1  doub Y N 289 
PHE   CG  CD2  sing Y N 290 
PHE   CD1 CE1  sing Y N 291 
PHE   CD1 HD1  sing N N 292 
PHE   CD2 CE2  doub Y N 293 
PHE   CD2 HD2  sing N N 294 
PHE   CE1 CZ   doub Y N 295 
PHE   CE1 HE1  sing N N 296 
PHE   CE2 CZ   sing Y N 297 
PHE   CE2 HE2  sing N N 298 
PHE   CZ  HZ   sing N N 299 
PHE   OXT HXT  sing N N 300 
PRO   N   CA   sing N N 301 
PRO   N   CD   sing N N 302 
PRO   N   H    sing N N 303 
PRO   CA  C    sing N N 304 
PRO   CA  CB   sing N N 305 
PRO   CA  HA   sing N N 306 
PRO   C   O    doub N N 307 
PRO   C   OXT  sing N N 308 
PRO   CB  CG   sing N N 309 
PRO   CB  HB2  sing N N 310 
PRO   CB  HB3  sing N N 311 
PRO   CG  CD   sing N N 312 
PRO   CG  HG2  sing N N 313 
PRO   CG  HG3  sing N N 314 
PRO   CD  HD2  sing N N 315 
PRO   CD  HD3  sing N N 316 
PRO   OXT HXT  sing N N 317 
SER   N   CA   sing N N 318 
SER   N   H    sing N N 319 
SER   N   H2   sing N N 320 
SER   CA  C    sing N N 321 
SER   CA  CB   sing N N 322 
SER   CA  HA   sing N N 323 
SER   C   O    doub N N 324 
SER   C   OXT  sing N N 325 
SER   CB  OG   sing N N 326 
SER   CB  HB2  sing N N 327 
SER   CB  HB3  sing N N 328 
SER   OG  HG   sing N N 329 
SER   OXT HXT  sing N N 330 
THR   N   CA   sing N N 331 
THR   N   H    sing N N 332 
THR   N   H2   sing N N 333 
THR   CA  C    sing N N 334 
THR   CA  CB   sing N N 335 
THR   CA  HA   sing N N 336 
THR   C   O    doub N N 337 
THR   C   OXT  sing N N 338 
THR   CB  OG1  sing N N 339 
THR   CB  CG2  sing N N 340 
THR   CB  HB   sing N N 341 
THR   OG1 HG1  sing N N 342 
THR   CG2 HG21 sing N N 343 
THR   CG2 HG22 sing N N 344 
THR   CG2 HG23 sing N N 345 
THR   OXT HXT  sing N N 346 
TRP   N   CA   sing N N 347 
TRP   N   H    sing N N 348 
TRP   N   H2   sing N N 349 
TRP   CA  C    sing N N 350 
TRP   CA  CB   sing N N 351 
TRP   CA  HA   sing N N 352 
TRP   C   O    doub N N 353 
TRP   C   OXT  sing N N 354 
TRP   CB  CG   sing N N 355 
TRP   CB  HB2  sing N N 356 
TRP   CB  HB3  sing N N 357 
TRP   CG  CD1  doub Y N 358 
TRP   CG  CD2  sing Y N 359 
TRP   CD1 NE1  sing Y N 360 
TRP   CD1 HD1  sing N N 361 
TRP   CD2 CE2  doub Y N 362 
TRP   CD2 CE3  sing Y N 363 
TRP   NE1 CE2  sing Y N 364 
TRP   NE1 HE1  sing N N 365 
TRP   CE2 CZ2  sing Y N 366 
TRP   CE3 CZ3  doub Y N 367 
TRP   CE3 HE3  sing N N 368 
TRP   CZ2 CH2  doub Y N 369 
TRP   CZ2 HZ2  sing N N 370 
TRP   CZ3 CH2  sing Y N 371 
TRP   CZ3 HZ3  sing N N 372 
TRP   CH2 HH2  sing N N 373 
TRP   OXT HXT  sing N N 374 
TYR   N   CA   sing N N 375 
TYR   N   H    sing N N 376 
TYR   N   H2   sing N N 377 
TYR   CA  C    sing N N 378 
TYR   CA  CB   sing N N 379 
TYR   CA  HA   sing N N 380 
TYR   C   O    doub N N 381 
TYR   C   OXT  sing N N 382 
TYR   CB  CG   sing N N 383 
TYR   CB  HB2  sing N N 384 
TYR   CB  HB3  sing N N 385 
TYR   CG  CD1  doub Y N 386 
TYR   CG  CD2  sing Y N 387 
TYR   CD1 CE1  sing Y N 388 
TYR   CD1 HD1  sing N N 389 
TYR   CD2 CE2  doub Y N 390 
TYR   CD2 HD2  sing N N 391 
TYR   CE1 CZ   doub Y N 392 
TYR   CE1 HE1  sing N N 393 
TYR   CE2 CZ   sing Y N 394 
TYR   CE2 HE2  sing N N 395 
TYR   CZ  OH   sing N N 396 
TYR   OH  HH   sing N N 397 
TYR   OXT HXT  sing N N 398 
VAL   N   CA   sing N N 399 
VAL   N   H    sing N N 400 
VAL   N   H2   sing N N 401 
VAL   CA  C    sing N N 402 
VAL   CA  CB   sing N N 403 
VAL   CA  HA   sing N N 404 
VAL   C   O    doub N N 405 
VAL   C   OXT  sing N N 406 
VAL   CB  CG1  sing N N 407 
VAL   CB  CG2  sing N N 408 
VAL   CB  HB   sing N N 409 
VAL   CG1 HG11 sing N N 410 
VAL   CG1 HG12 sing N N 411 
VAL   CG1 HG13 sing N N 412 
VAL   CG2 HG21 sing N N 413 
VAL   CG2 HG22 sing N N 414 
VAL   CG2 HG23 sing N N 415 
VAL   OXT HXT  sing N N 416 
# 
_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_1002344 
_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                    7I62 
_atom_sites.fract_transf_matrix[1][1]   0.013736 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000725 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016128 
_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]   0.030514 
_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   ? 19.633 6.968   24.090 1.00 51.41 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.738 6.108   23.673 1.00 51.68 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.349 5.199   22.506 1.00 50.54 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.274 4.591   22.514 1.00 50.71 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.248 5.278   24.853 1.00 54.34 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.884 4.060   24.475 1.00 58.08 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.256 5.070   21.547 1.00 48.98 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.039 4.200   20.399 1.00 47.70 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.380 4.797   19.054 1.00 45.71 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.933 5.896   18.719 1.00 45.55 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.152 4.064   18.266 1.00 44.36 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.518 4.520   16.928 1.00 44.26 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.561 3.351   15.914 1.00 43.31 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.601 2.184   16.318 1.00 42.79 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.869 5.209   16.994 1.00 44.60 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.566 3.664   14.603 1.00 42.85 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.719 2.650   13.554 1.00 43.34 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.098 2.829   12.924 1.00 44.13 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.466 3.931   12.499 1.00 44.15 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.643 2.769   12.461 1.00 43.73 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.219 2.770   13.042 1.00 43.74 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.836 1.691   11.386 1.00 44.15 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.222 3.314   12.084 1.00 44.30 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.869 1.751   12.863 1.00 44.70 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.194 1.803   12.272 1.00 44.81 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.187 0.986   10.989 1.00 45.47 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.137 -0.246  11.047 1.00 45.20 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.228 1.291   13.272 1.00 44.23 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.220 2.068   14.565 1.00 43.50 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.932 3.253   14.694 1.00 44.50 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.462 1.647   15.643 1.00 43.96 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.913 3.984   15.877 1.00 45.10 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.426 2.371   16.827 1.00 44.98 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.163 3.532   16.946 1.00 46.03 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.125 4.214   18.134 1.00 47.52 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.128 1.675   9.830  1.00 45.42 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.138 1.019   8.519  1.00 45.88 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.268 1.609   7.716  1.00 47.06 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.308 2.823   7.523  1.00 47.50 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.788 1.103   7.769  1.00 46.35 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.237 2.533   7.739  1.00 46.41 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.905 0.523   6.365  1.00 46.55 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.241 0.767   7.337  1.00 47.68 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.434 1.184   6.613  1.00 48.96 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.166 2.283   7.358  1.00 50.25 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.284 2.209   8.587  1.00 51.51 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.537 3.370   6.658  1.00 49.35 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.218 4.465   7.318  1.00 49.11 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.248 5.536   7.825  1.00 47.39 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.607 6.720   7.877  1.00 47.05 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.313 5.030   6.431  1.00 52.02 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.486 4.077   6.324  1.00 58.81 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 33.770 3.306   7.248  1.00 60.32 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 34.189 4.098   5.193  1.00 61.27 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.045 5.114   8.272  1.00 46.16 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.057 6.078   8.808  1.00 44.71 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.495 5.683   10.160 1.00 43.33 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.145 4.514   10.392 1.00 42.74 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.859 6.278   7.851  1.00 44.50 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.207 6.880   6.507  1.00 45.29 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.789 8.131   6.416  1.00 45.94 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.946 6.195   5.328  1.00 46.49 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.146 8.670   5.189  1.00 47.28 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.283 6.732   4.092  1.00 47.73 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.869 7.979   4.026  1.00 48.96 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.219 8.520   2.811  1.00 51.89 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.323 6.695   11.024 1.00 42.10 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.648 6.576   12.316 1.00 41.17 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.314 7.374   12.155 1.00 40.62 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.336 8.507   11.693 1.00 40.64 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.526 7.146   13.456 1.00 41.29 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.772 7.311   14.768 1.00 43.53 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.669 7.653   15.933 1.00 45.67 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.145 8.711   16.807 1.00 47.60 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.652 8.501   18.027 1.00 49.47 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.534 7.262   18.503 1.00 49.09 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.243 9.524   18.768 1.00 48.16 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.169 6.757   12.447 1.00 40.10 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.844 7.385   12.310 1.00 39.46 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.270 7.577   13.698 1.00 38.04 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.105 6.598   14.409 1.00 39.02 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.880 6.500   11.480 1.00 40.37 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.519 7.174   11.332 1.00 41.22 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.464 6.167   10.113 1.00 40.66 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.959 8.796   14.085 1.00 35.91 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.442 9.084   15.428 1.00 35.22 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.195 9.971   15.407 1.00 33.58 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 19.943 10.630  14.396 1.00 32.86 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.516 9.769   16.330 1.00 36.26 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.306 8.753   17.128 1.00 37.21 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.408 10.749  15.560 1.00 36.68 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.470 10.100  16.563 1.00 32.33 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.413 11.110  16.658 1.00 32.37 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.195 12.444  16.691 1.00 32.70 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.149 12.557  17.458 1.00 33.40 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.626 11.010  17.972 1.00 33.23 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.006 9.667   18.246 1.00 36.17 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.661 8.744   18.744 1.00 37.78 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.733 9.538   17.959 1.00 35.78 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.855 13.403  15.830 1.00 31.94 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.522 14.684  15.754 1.00 32.58 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.495 15.390  17.118 1.00 34.82 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.530 15.925  17.520 1.00 36.08 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.878 15.566  14.656 1.00 32.03 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.625 16.851  14.293 1.00 31.86 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.626 17.790  13.647 1.00 34.70 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.152 19.033  13.066 1.00 36.72 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.232 20.192  13.719 1.00 39.32 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.954 20.254  15.020 1.00 36.00 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.633 21.291  13.086 1.00 40.47 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.376 15.286  17.891 1.00 35.27 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.321 15.932  19.224 1.00 36.43 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.279 15.297  20.268 1.00 37.33 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.528 15.896  21.310 1.00 37.31 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.883 16.045  19.770 1.00 37.03 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.354 14.786  20.369 1.00 40.26 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.680 13.842  19.597 1.00 41.70 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.413 14.344  21.649 1.00 41.47 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.374 12.853  20.423 1.00 42.28 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.791 13.107  21.668 1.00 42.72 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.835 14.124  19.977 1.00 37.67 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.794 13.485  20.892 1.00 38.68 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.223 13.464  20.340 1.00 40.15 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.066 12.752  20.895 1.00 40.66 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.373 12.034  21.193 1.00 38.34 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.092 11.816  21.978 1.00 39.00 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.861 10.315  22.187 1.00 39.23 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.147 12.535  23.337 1.00 38.45 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.477 14.141  19.210 1.00 41.10 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.790 14.150  18.582 1.00 42.87 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.830 14.839  19.457 1.00 44.27 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.503 15.781  20.174 1.00 43.90 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.718 14.814  17.208 1.00 42.90 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.072 14.322  19.434 1.00 45.92 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.206 14.842  20.199 1.00 48.16 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 27.983 15.924  19.402 1.00 50.12 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.663 16.157  18.230 1.00 50.18 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.137 13.665  20.546 1.00 49.91 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.783 13.217  19.347 1.00 50.73 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.421 12.544  21.267 1.00 50.50 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.031 16.553  20.010 1.00 51.34 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.867 17.487  19.268 1.00 53.30 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.616 16.723  18.159 1.00 53.60 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.798 17.277  17.084 1.00 53.88 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.898 18.164  20.161 1.00 56.28 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.358 18.838  21.381 1.00 62.62 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 30.275 20.219  21.465 1.00 65.88 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.020 18.307  22.583 1.00 65.09 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.858 20.480  22.696 1.00 66.87 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 29.699 19.362  23.411 1.00 66.75 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.016 15.449  18.395 1.00 53.33 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.703 14.668  17.364 1.00 53.30 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.817 14.347  16.183 1.00 51.32 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.311 14.292  15.063 1.00 51.45 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.383 13.389  17.908 1.00 56.54 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.739 13.157  17.272 1.00 62.38 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.359 14.090  16.730 1.00 65.41 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.253 11.933  17.320 1.00 63.74 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.508 14.160  16.412 1.00 49.72 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.545 13.945  15.317 1.00 47.86 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.449 15.235  14.465 1.00 47.00 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.384 15.174  13.245 1.00 47.88 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.165 13.574  15.880 1.00 47.52 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.067 12.176  16.462 1.00 49.41 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.732 11.269  15.933 1.00 49.60 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.306 11.990  17.438 1.00 49.70 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.495 16.399  15.102 1.00 45.40 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.444 17.689  14.400 1.00 44.56 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.774 18.089  13.708 1.00 45.00 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.756 18.741  12.673 1.00 44.49 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.955 18.789  15.365 1.00 43.01 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.461 18.827  15.489 1.00 40.75 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.701 18.268  16.473 1.00 41.02 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.547 19.391  14.549 1.00 39.45 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.364 18.493  16.222 1.00 40.73 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.247 19.222  15.070 1.00 39.86 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.701 20.096  13.355 1.00 39.33 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.117 19.702  14.420 1.00 39.53 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.577 20.551  12.704 1.00 39.46 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.302 20.344  13.234 1.00 39.36 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.911 17.699  14.277 1.00 46.08 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.224 17.982  13.677 1.00 47.80 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.576 17.030  12.503 1.00 49.25 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.574 17.243  11.805 1.00 50.58 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.313 17.922  14.741 1.00 47.50 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.781 15.977  12.315 1.00 48.54 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.912 14.987  11.253 1.00 48.14 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.573 14.791  10.514 1.00 46.66 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.334 13.719  9.966  1.00 47.24 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.365 13.663  11.862 1.00 49.72 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.808 13.708  12.257 1.00 52.14 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.645 14.232  11.516 1.00 54.93 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.132 13.195  13.428 1.00 51.04 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.696 15.818  10.531 1.00 44.60 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.369 15.823  9.939  1.00 42.22 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.420 15.477  8.474  1.00 40.83 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.279 15.991  7.772  1.00 40.61 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.785 17.226  10.119 1.00 41.73 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.453 17.557  9.428  1.00 41.88 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.321 16.781  10.055 1.00 41.01 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.189 19.072  9.450  1.00 41.53 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.522 14.564  8.022  1.00 39.66 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.329 14.181  6.623  1.00 38.31 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.010 14.879  6.133  1.00 36.85 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.989 15.589  5.123  1.00 37.34 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.198 12.638  6.464  1.00 39.00 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.896 12.279  5.021  1.00 39.54 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.426 11.885  6.977  1.00 39.41 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.931 14.700  6.906  1.00 34.79 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.576 15.122  6.624  1.00 33.23 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.789 15.218  7.940  1.00 31.75 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.953 14.372  8.817  1.00 31.33 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.908 14.026  5.754  1.00 32.96 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.445 14.244  5.526  1.00 33.75 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.874 15.254  4.810  1.00 34.71 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.361 13.517  6.128  1.00 34.12 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.507 15.178  4.890  1.00 35.33 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.162 14.112  5.685  1.00 35.06 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.287 12.434  7.012  1.00 34.58 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 17.906 13.615  6.040  1.00 35.52 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.041 11.962  7.385  1.00 35.25 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.871 12.531  6.883  1.00 35.42 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.904 16.213  8.056  1.00 30.78 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.040 16.337  9.220  1.00 30.64 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.668 16.926  8.800  1.00 31.89 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.609 17.714  7.846  1.00 32.16 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.724 17.121  10.380 1.00 30.39 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.271 18.506  10.025 1.00 30.72 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.301 19.676  9.881  1.00 31.38 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.640 20.629  9.142  1.00 32.31 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.207 19.641  10.484 1.00 30.29 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.576 16.559  9.498  1.00 31.65 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.244 17.066  9.152  1.00 32.71 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.347 17.155  10.402 1.00 33.06 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 15.760 16.151  10.798 1.00 33.40 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.601 16.182  8.069  1.00 34.85 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.345 16.714  7.385  1.00 40.39 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.684 17.611  7.955  1.00 39.50 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.006 16.208  6.283  1.00 44.49 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.225 18.353  11.003 1.00 32.42 ? 36  SER   A N   1 
ATOM   241  C  CA  . SER   A 1 30  ? 15.403 18.555  12.201 1.00 32.65 ? 36  SER   A CA  1 
ATOM   242  C  C   . SER   A 1 30  ? 13.936 18.126  12.006 1.00 32.09 ? 36  SER   A C   1 
ATOM   243  O  O   . SER   A 1 30  ? 13.339 17.619  12.952 1.00 31.24 ? 36  SER   A O   1 
ATOM   244  C  CB  . SER   A 1 30  ? 15.508 19.989  12.728 1.00 33.67 ? 36  SER   A CB  1 
ATOM   245  O  OG  . SER   A 1 30  ? 15.005 20.876  11.752 1.00 37.48 ? 36  SER   A OG  1 
ATOM   246  N  N   . SER   A 1 31  ? 13.382 18.254  10.780 1.00 31.93 ? 37  SER   A N   1 
ATOM   247  C  CA  . SER   A 1 31  ? 12.020 17.771  10.529 1.00 31.98 ? 37  SER   A CA  1 
ATOM   248  C  C   . SER   A 1 31  ? 11.912 16.248  10.663 1.00 30.01 ? 37  SER   A C   1 
ATOM   249  O  O   . SER   A 1 31  ? 10.817 15.757  10.851 1.00 31.05 ? 37  SER   A O   1 
ATOM   250  C  CB  . SER   A 1 31  ? 11.477 18.249  9.184  1.00 34.65 ? 37  SER   A CB  1 
ATOM   251  O  OG  . SER   A 1 31  ? 12.025 17.516  8.100  1.00 37.74 ? 37  SER   A OG  1 
ATOM   252  N  N   . ARG   A 1 32  ? 13.015 15.505  10.564 1.00 28.00 ? 38  ARG   A N   1 
ATOM   253  C  CA  . ARG   A 1 32  ? 12.987 14.047  10.730 1.00 27.06 ? 38  ARG   A CA  1 
ATOM   254  C  C   . ARG   A 1 32  ? 13.625 13.568  12.035 1.00 27.73 ? 38  ARG   A C   1 
ATOM   255  O  O   . ARG   A 1 32  ? 13.525 12.386  12.356 1.00 29.02 ? 38  ARG   A O   1 
ATOM   256  C  CB  . ARG   A 1 32  ? 13.663 13.346  9.551  1.00 26.26 ? 38  ARG   A CB  1 
ATOM   257  C  CG  . ARG   A 1 32  ? 13.152 13.795  8.199  1.00 25.15 ? 38  ARG   A CG  1 
ATOM   258  C  CD  . ARG   A 1 32  ? 13.831 13.038  7.072  1.00 26.23 ? 38  ARG   A CD  1 
ATOM   259  N  NE  . ARG   A 1 32  ? 13.747 11.584  7.219  1.00 26.66 ? 38  ARG   A NE  1 
ATOM   260  C  CZ  . ARG   A 1 32  ? 13.883 10.717  6.212  1.00 27.74 ? 38  ARG   A CZ  1 
ATOM   261  N  NH1 . ARG   A 1 32  ? 14.100 11.151  4.976  1.00 24.18 ? 38  ARG   A NH1 1 
ATOM   262  N  NH2 . ARG   A 1 32  ? 13.786 9.408   6.436  1.00 28.02 ? 38  ARG   A NH2 1 
ATOM   263  N  N   . ASP   A 1 33  ? 14.313 14.482  12.772 1.00 27.28 ? 39  ASP   A N   1 
ATOM   264  C  CA  . ASP   A 1 33  ? 15.048 14.211  13.989 1.00 26.74 ? 39  ASP   A CA  1 
ATOM   265  C  C   . ASP   A 1 33  ? 16.192 13.261  13.623 1.00 26.34 ? 39  ASP   A C   1 
ATOM   266  O  O   . ASP   A 1 33  ? 16.447 12.320  14.367 1.00 26.29 ? 39  ASP   A O   1 
ATOM   267  C  CB  . ASP   A 1 33  ? 14.137 13.624  15.104 1.00 27.36 ? 39  ASP   A CB  1 
ATOM   268  C  CG  . ASP   A 1 33  ? 14.867 13.344  16.414 1.00 31.02 ? 39  ASP   A CG  1 
ATOM   269  O  OD1 . ASP   A 1 33  ? 15.682 14.200  16.839 1.00 30.69 ? 39  ASP   A OD1 1 
ATOM   270  O  OD2 . ASP   A 1 33  ? 14.651 12.256  16.997 1.00 32.56 ? 39  ASP   A OD2 1 
ATOM   271  N  N   . LEU   A 1 34  ? 16.876 13.477  12.473 1.00 25.91 ? 40  LEU   A N   1 
ATOM   272  C  CA  . LEU   A 1 34  ? 17.992 12.592  12.107 1.00 25.76 ? 40  LEU   A CA  1 
ATOM   273  C  C   . LEU   A 1 34  ? 19.274 13.358  11.910 1.00 27.73 ? 40  LEU   A C   1 
ATOM   274  O  O   . LEU   A 1 34  ? 19.273 14.532  11.549 1.00 29.19 ? 40  LEU   A O   1 
ATOM   275  C  CB  . LEU   A 1 34  ? 17.706 11.784  10.831 1.00 24.57 ? 40  LEU   A CB  1 
ATOM   276  C  CG  . LEU   A 1 34  ? 16.580 10.732  10.849 1.00 24.87 ? 40  LEU   A CG  1 
ATOM   277  C  CD1 . LEU   A 1 34  ? 16.526 9.995   9.489  1.00 24.90 ? 40  LEU   A CD1 1 
ATOM   278  C  CD2 . LEU   A 1 34  ? 16.710 9.771   12.043 1.00 24.43 ? 40  LEU   A CD2 1 
ATOM   279  N  N   . LEU   A 1 35  ? 20.373 12.688  12.126 1.00 28.48 ? 41  LEU   A N   1 
ATOM   280  C  CA  . LEU   A 1 35  ? 21.689 13.236  11.896 1.00 29.67 ? 41  LEU   A CA  1 
ATOM   281  C  C   . LEU   A 1 35  ? 22.530 12.045  11.570 1.00 31.76 ? 41  LEU   A C   1 
ATOM   282  O  O   . LEU   A 1 35  ? 22.441 11.002  12.213 1.00 32.50 ? 41  LEU   A O   1 
ATOM   283  C  CB  . LEU   A 1 35  ? 22.263 14.026  13.127 1.00 29.44 ? 41  LEU   A CB  1 
ATOM   284  C  CG  . LEU   A 1 35  ? 23.574 14.787  12.876 1.00 30.25 ? 41  LEU   A CG  1 
ATOM   285  C  CD1 . LEU   A 1 35  ? 23.638 16.055  13.686 1.00 31.90 ? 41  LEU   A CD1 1 
ATOM   286  C  CD2 . LEU   A 1 35  ? 24.779 13.940  13.154 1.00 31.02 ? 41  LEU   A CD2 1 
ATOM   287  N  N   . VAL   A 1 36  ? 23.281 12.165  10.516 1.00 33.16 ? 42  VAL   A N   1 
ATOM   288  C  CA  . VAL   A 1 36  ? 24.204 11.137  10.099 1.00 35.32 ? 42  VAL   A CA  1 
ATOM   289  C  C   . VAL   A 1 36  ? 25.614 11.771  10.136 1.00 38.07 ? 42  VAL   A C   1 
ATOM   290  O  O   . VAL   A 1 36  ? 25.832 12.854  9.576  1.00 37.49 ? 42  VAL   A O   1 
ATOM   291  C  CB  . VAL   A 1 36  ? 23.816 10.542  8.731  1.00 35.06 ? 42  VAL   A CB  1 
ATOM   292  C  CG1 . VAL   A 1 36  ? 24.918 9.641   8.205  1.00 35.52 ? 42  VAL   A CG1 1 
ATOM   293  C  CG2 . VAL   A 1 36  ? 22.490 9.797   8.826  1.00 35.12 ? 42  VAL   A CG2 1 
ATOM   294  N  N   . SER   A 1 37  ? 26.529 11.125  10.885 1.00 40.60 ? 43  SER   A N   1 
ATOM   295  C  CA  . SER   A 1 37  ? 27.917 11.537  11.050 1.00 43.26 ? 43  SER   A CA  1 
ATOM   296  C  C   . SER   A 1 37  ? 28.845 10.448  10.531 1.00 47.02 ? 43  SER   A C   1 
ATOM   297  O  O   . SER   A 1 37  ? 28.503 9.253   10.543 1.00 46.72 ? 43  SER   A O   1 
ATOM   298  C  CB  . SER   A 1 37  ? 28.224 11.842  12.515 1.00 43.56 ? 43  SER   A CB  1 
ATOM   299  O  OG  . SER   A 1 37  ? 27.981 10.729  13.364 1.00 44.03 ? 43  SER   A OG  1 
ATOM   300  N  N   . SER   A 1 38  ? 30.035 10.861  10.092 1.00 49.44 ? 44  SER   A N   1 
ATOM   301  C  CA  . SER   A 1 38  ? 31.029 9.943   9.564  1.00 52.55 ? 44  SER   A CA  1 
ATOM   302  C  C   . SER   A 1 38  ? 31.737 9.160   10.678 1.00 55.58 ? 44  SER   A C   1 
ATOM   303  O  O   . SER   A 1 38  ? 31.799 9.630   11.816 1.00 56.21 ? 44  SER   A O   1 
ATOM   304  C  CB  . SER   A 1 38  ? 32.047 10.696  8.714  1.00 54.01 ? 44  SER   A CB  1 
ATOM   305  O  OG  . SER   A 1 38  ? 32.569 11.814  9.411  1.00 55.97 ? 44  SER   A OG  1 
ATOM   306  N  N   . THR   A 1 39  ? 32.232 7.958   10.367 1.00 57.33 ? 45  THR   A N   1 
ATOM   307  C  CA  . THR   A 1 39  ? 32.941 7.132   11.355 1.00 60.44 ? 45  THR   A CA  1 
ATOM   308  C  C   . THR   A 1 39  ? 34.193 6.508   10.751 1.00 63.94 ? 45  THR   A C   1 
ATOM   309  O  O   . THR   A 1 39  ? 34.289 6.349   9.532  1.00 64.60 ? 45  THR   A O   1 
ATOM   310  C  CB  . THR   A 1 39  ? 32.042 6.054   12.024 1.00 61.47 ? 45  THR   A CB  1 
ATOM   311  O  OG1 . THR   A 1 39  ? 31.265 5.372   11.048 1.00 62.59 ? 45  THR   A OG1 1 
ATOM   312  C  CG2 . THR   A 1 39  ? 31.163 6.607   13.137 1.00 61.39 ? 45  THR   A CG2 1 
ATOM   313  N  N   . THR   A 1 40  ? 35.155 6.156   11.601 1.00 66.15 ? 46  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 40  ? 36.401 5.578   11.145 1.00 68.91 ? 46  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 40  ? 36.309 4.042   11.008 1.00 70.41 ? 46  THR   A C   1 
ATOM   316  O  O   . THR   A 1 40  ? 36.992 3.448   10.167 1.00 71.00 ? 46  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 40  ? 37.544 6.055   12.055 1.00 71.54 ? 46  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 40  ? 37.207 5.724   13.407 1.00 73.87 ? 46  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 40  ? 37.788 7.564   11.949 1.00 71.58 ? 46  THR   A CG2 1 
ATOM   320  N  N   . ALA   A 1 41  ? 35.478 3.398   11.833 1.00 70.42 ? 47  ALA   A N   1 
ATOM   321  C  CA  . ALA   A 1 41  ? 35.307 1.947   11.769 1.00 69.97 ? 47  ALA   A CA  1 
ATOM   322  C  C   . ALA   A 1 41  ? 34.198 1.573   10.766 1.00 70.25 ? 47  ALA   A C   1 
ATOM   323  O  O   . ALA   A 1 41  ? 33.369 2.428   10.413 1.00 70.02 ? 47  ALA   A O   1 
ATOM   324  C  CB  . ALA   A 1 41  ? 34.979 1.413   13.151 1.00 69.76 ? 47  ALA   A CB  1 
ATOM   325  N  N   . GLN   A 1 42  ? 34.173 0.294   10.305 1.00 70.21 ? 48  GLN   A N   1 
ATOM   326  C  CA  . GLN   A 1 42  ? 33.153 -0.170  9.353  1.00 70.05 ? 48  GLN   A CA  1 
ATOM   327  C  C   . GLN   A 1 42  ? 31.947 -0.847  10.007 1.00 69.91 ? 48  GLN   A C   1 
ATOM   328  O  O   . GLN   A 1 42  ? 31.996 -2.053  10.260 1.00 70.76 ? 48  GLN   A O   1 
ATOM   329  C  CB  . GLN   A 1 42  ? 33.756 -1.101  8.288  1.00 70.75 ? 48  GLN   A CB  1 
ATOM   330  C  CG  . GLN   A 1 42  ? 32.843 -1.344  7.087  1.00 73.25 ? 48  GLN   A CG  1 
ATOM   331  C  CD  . GLN   A 1 42  ? 33.329 -0.590  5.870  1.00 77.66 ? 48  GLN   A CD  1 
ATOM   332  O  OE1 . GLN   A 1 42  ? 34.279 -1.005  5.207  1.00 81.40 ? 48  GLN   A OE1 1 
ATOM   333  N  NE2 . GLN   A 1 42  ? 32.694 0.527   5.532  1.00 76.71 ? 48  GLN   A NE2 1 
ATOM   334  N  N   . GLY   A 1 43  ? 30.866 -0.085  10.198 1.00 68.59 ? 49  GLY   A N   1 
ATOM   335  C  CA  . GLY   A 1 43  ? 29.604 -0.551  10.763 1.00 67.69 ? 49  GLY   A CA  1 
ATOM   336  C  C   . GLY   A 1 43  ? 29.005 -1.692  9.970  1.00 66.49 ? 49  GLY   A C   1 
ATOM   337  O  O   . GLY   A 1 43  ? 29.165 -1.759  8.748  1.00 66.68 ? 49  GLY   A O   1 
ATOM   338  N  N   . CYS   A 1 44  ? 28.296 -2.580  10.644 1.00 65.38 ? 50  CYS   A N   1 
ATOM   339  C  CA  . CYS   A 1 44  ? 27.796 -3.781  9.986  1.00 64.85 ? 50  CYS   A CA  1 
ATOM   340  C  C   . CYS   A 1 44  ? 26.272 -3.987  10.057 1.00 61.91 ? 50  CYS   A C   1 
ATOM   341  O  O   . CYS   A 1 44  ? 25.804 -5.094  9.761  1.00 62.47 ? 50  CYS   A O   1 
ATOM   342  C  CB  . CYS   A 1 44  ? 28.553 -4.996  10.516 1.00 67.64 ? 50  CYS   A CB  1 
ATOM   343  S  SG  . CYS   A 1 44  ? 28.735 -5.026  12.325 1.00 76.56 ? 50  CYS   A SG  1 
ATOM   344  N  N   . ASP   A 1 45  ? 25.499 -2.942  10.382 1.00 58.64 ? 51  ASP   A N   1 
ATOM   345  C  CA  . ASP   A 1 45  ? 24.041 -3.063  10.416 1.00 56.19 ? 51  ASP   A CA  1 
ATOM   346  C  C   . ASP   A 1 45  ? 23.499 -3.094  8.979  1.00 53.42 ? 51  ASP   A C   1 
ATOM   347  O  O   . ASP   A 1 45  ? 23.969 -2.339  8.140  1.00 54.02 ? 51  ASP   A O   1 
ATOM   348  C  CB  . ASP   A 1 45  ? 23.402 -1.886  11.197 1.00 57.57 ? 51  ASP   A CB  1 
ATOM   349  C  CG  . ASP   A 1 45  ? 23.484 -2.017  12.704 1.00 60.83 ? 51  ASP   A CG  1 
ATOM   350  O  OD1 . ASP   A 1 45  ? 23.131 -3.100  13.223 1.00 62.45 ? 51  ASP   A OD1 1 
ATOM   351  O  OD2 . ASP   A 1 45  ? 23.903 -1.033  13.370 1.00 60.72 ? 51  ASP   A OD2 1 
ATOM   352  N  N   . THR   A 1 46  ? 22.528 -3.953  8.689  1.00 50.83 ? 52  THR   A N   1 
ATOM   353  C  CA  . THR   A 1 46  ? 21.921 -4.002  7.352  1.00 48.98 ? 52  THR   A CA  1 
ATOM   354  C  C   . THR   A 1 46  ? 20.659 -3.142  7.371  1.00 46.21 ? 52  THR   A C   1 
ATOM   355  O  O   . THR   A 1 46  ? 19.839 -3.313  8.269  1.00 46.19 ? 52  THR   A O   1 
ATOM   356  C  CB  . THR   A 1 46  ? 21.616 -5.468  6.930  1.00 50.12 ? 52  THR   A CB  1 
ATOM   357  O  OG1 . THR   A 1 46  ? 22.825 -6.056  6.428  1.00 51.51 ? 52  THR   A OG1 1 
ATOM   358  C  CG2 . THR   A 1 46  ? 20.520 -5.574  5.845  1.00 49.83 ? 52  THR   A CG2 1 
ATOM   359  N  N   . ILE   A 1 47  ? 20.481 -2.266  6.367  1.00 43.36 ? 53  ILE   A N   1 
ATOM   360  C  CA  . ILE   A 1 47  ? 19.280 -1.464  6.280  1.00 41.36 ? 53  ILE   A CA  1 
ATOM   361  C  C   . ILE   A 1 47  ? 18.252 -2.179  5.429  1.00 40.98 ? 53  ILE   A C   1 
ATOM   362  O  O   . ILE   A 1 47  ? 18.596 -2.740  4.382  1.00 41.75 ? 53  ILE   A O   1 
ATOM   363  C  CB  . ILE   A 1 47  ? 19.560 -0.042  5.744  1.00 40.51 ? 53  ILE   A CB  1 
ATOM   364  C  CG1 . ILE   A 1 47  ? 20.738 0.616   6.490  1.00 40.75 ? 53  ILE   A CG1 1 
ATOM   365  C  CG2 . ILE   A 1 47  ? 18.271 0.821   5.762  1.00 39.72 ? 53  ILE   A CG2 1 
ATOM   366  C  CD1 . ILE   A 1 47  ? 20.503 0.783   8.004  1.00 41.73 ? 53  ILE   A CD1 1 
ATOM   367  N  N   . ALA   A 1 48  ? 16.986 -2.177  5.888  1.00 39.66 ? 54  ALA   A N   1 
ATOM   368  C  CA  . ALA   A 1 48  ? 15.869 -2.756  5.157  1.00 38.58 ? 54  ALA   A CA  1 
ATOM   369  C  C   . ALA   A 1 48  ? 15.495 -1.802  3.999  1.00 39.11 ? 54  ALA   A C   1 
ATOM   370  O  O   . ALA   A 1 48  ? 15.542 -0.586  4.148  1.00 39.21 ? 54  ALA   A O   1 
ATOM   371  C  CB  . ALA   A 1 48  ? 14.679 -2.922  6.085  1.00 37.11 ? 54  ALA   A CB  1 
ATOM   372  N  N   . ARG   A 1 49  ? 15.155 -2.353  2.840  1.00 39.56 ? 55  ARG   A N   1 
ATOM   373  C  CA  . ARG   A 1 49  ? 14.695 -1.592  1.692  1.00 40.23 ? 55  ARG   A CA  1 
ATOM   374  C  C   . ARG   A 1 49  ? 13.363 -2.290  1.366  1.00 41.31 ? 55  ARG   A C   1 
ATOM   375  O  O   . ARG   A 1 49  ? 13.352 -3.322  0.691  1.00 42.04 ? 55  ARG   A O   1 
ATOM   376  C  CB  . ARG   A 1 49  ? 15.724 -1.693  0.566  1.00 42.37 ? 55  ARG   A CB  1 
ATOM   377  C  CG  . ARG   A 1 49  ? 17.111 -1.082  0.885  1.00 45.43 ? 55  ARG   A CG  1 
ATOM   378  C  CD  . ARG   A 1 49  ? 17.134 0.398   1.321  1.00 46.93 ? 55  ARG   A CD  1 
ATOM   379  N  NE  . ARG   A 1 49  ? 18.503 0.851   1.608  1.00 47.02 ? 55  ARG   A NE  1 
ATOM   380  C  CZ  . ARG   A 1 49  ? 18.809 1.956   2.290  1.00 46.53 ? 55  ARG   A CZ  1 
ATOM   381  N  NH1 . ARG   A 1 49  ? 17.852 2.736   2.765  1.00 44.01 ? 55  ARG   A NH1 1 
ATOM   382  N  NH2 . ARG   A 1 49  ? 20.077 2.293   2.488  1.00 46.13 ? 55  ARG   A NH2 1 
ATOM   383  N  N   . CYS   A 1 50  ? 12.253 -1.810  1.965  1.00 41.20 ? 56  CYS   A N   1 
ATOM   384  C  CA  . CYS   A 1 50  ? 10.987 -2.539  1.895  1.00 41.73 ? 56  CYS   A CA  1 
ATOM   385  C  C   . CYS   A 1 50  ? 9.788  -1.670  2.333  1.00 42.53 ? 56  CYS   A C   1 
ATOM   386  O  O   . CYS   A 1 50  ? 9.988  -0.576  2.835  1.00 42.69 ? 56  CYS   A O   1 
ATOM   387  C  CB  . CYS   A 1 50  ? 11.116 -3.758  2.808  1.00 43.02 ? 56  CYS   A CB  1 
ATOM   388  S  SG  . CYS   A 1 50  ? 11.090 -3.344  4.582  1.00 47.88 ? 56  CYS   A SG  1 
ATOM   389  N  N   . ASP   A 1 51  ? 8.551  -2.211  2.271  1.00 43.50 ? 57  ASP   A N   1 
ATOM   390  C  CA  . ASP   A 1 51  ? 7.372  -1.499  2.774  1.00 44.57 ? 57  ASP   A CA  1 
ATOM   391  C  C   . ASP   A 1 51  ? 6.699  -2.284  3.916  1.00 44.72 ? 57  ASP   A C   1 
ATOM   392  O  O   . ASP   A 1 51  ? 5.478  -2.328  3.995  1.00 44.70 ? 57  ASP   A O   1 
ATOM   393  C  CB  . ASP   A 1 51  ? 6.371  -1.192  1.656  1.00 47.44 ? 57  ASP   A CB  1 
ATOM   394  C  CG  . ASP   A 1 51  ? 5.600  -2.389  1.133  1.00 57.06 ? 57  ASP   A CG  1 
ATOM   395  O  OD1 . ASP   A 1 51  ? 6.046  -3.547  1.372  1.00 58.78 ? 57  ASP   A OD1 1 
ATOM   396  O  OD2 . ASP   A 1 51  ? 4.533  -2.180  0.520  1.00 61.76 ? 57  ASP   A OD2 1 
ATOM   397  N  N   . CYS   A 1 52  ? 7.494  -2.914  4.781  1.00 44.25 ? 58  CYS   A N   1 
ATOM   398  C  CA  . CYS   A 1 52  ? 6.987  -3.683  5.908  1.00 43.17 ? 58  CYS   A CA  1 
ATOM   399  C  C   . CYS   A 1 52  ? 6.190  -2.829  6.856  1.00 42.03 ? 58  CYS   A C   1 
ATOM   400  O  O   . CYS   A 1 52  ? 6.522  -1.671  7.052  1.00 43.33 ? 58  CYS   A O   1 
ATOM   401  C  CB  . CYS   A 1 52  ? 8.143  -4.343  6.650  1.00 43.54 ? 58  CYS   A CB  1 
ATOM   402  S  SG  . CYS   A 1 52  ? 8.757  -5.843  5.869  1.00 44.05 ? 58  CYS   A SG  1 
ATOM   403  N  N   . GLN   A 1 53  ? 5.180  -3.393  7.464  1.00 39.89 ? 59  GLN   A N   1 
ATOM   404  C  CA  . GLN   A 1 53  ? 4.414  -2.704  8.495  1.00 38.71 ? 59  GLN   A CA  1 
ATOM   405  C  C   . GLN   A 1 53  ? 4.288  -3.475  9.775  1.00 36.95 ? 59  GLN   A C   1 
ATOM   406  O  O   . GLN   A 1 53  ? 3.385  -3.214  10.565 1.00 37.19 ? 59  GLN   A O   1 
ATOM   407  C  CB  . GLN   A 1 53  ? 3.053  -2.259  8.008  1.00 40.40 ? 59  GLN   A CB  1 
ATOM   408  C  CG  . GLN   A 1 53  ? 3.147  -1.010  7.153  1.00 42.34 ? 59  GLN   A CG  1 
ATOM   409  C  CD  . GLN   A 1 53  ? 1.789  -0.652  6.668  1.00 46.58 ? 59  GLN   A CD  1 
ATOM   410  O  OE1 . GLN   A 1 53  ? 1.478  -0.775  5.476  1.00 49.04 ? 59  GLN   A OE1 1 
ATOM   411  N  NE2 . GLN   A 1 53  ? 0.939  -0.239  7.592  1.00 46.56 ? 59  GLN   A NE2 1 
ATOM   412  N  N   . THR   A 1 54  ? 5.170  -4.451  9.977  1.00 35.44 ? 60  THR   A N   1 
ATOM   413  C  CA  . THR   A 1 54  ? 5.313  -5.257  11.188 1.00 33.98 ? 60  THR   A CA  1 
ATOM   414  C  C   . THR   A 1 54  ? 6.828  -5.379  11.426 1.00 31.59 ? 60  THR   A C   1 
ATOM   415  O  O   . THR   A 1 54  ? 7.659  -5.296  10.495 1.00 29.69 ? 60  THR   A O   1 
ATOM   416  C  CB  . THR   A 1 54  ? 4.640  -6.651  11.107 1.00 35.58 ? 60  THR   A CB  1 
ATOM   417  O  OG1 . THR   A 1 54  ? 5.368  -7.491  10.204 1.00 37.01 ? 60  THR   A OG1 1 
ATOM   418  C  CG2 . THR   A 1 54  ? 3.159  -6.592  10.758 1.00 35.44 ? 60  THR   A CG2 1 
ATOM   419  N  N   . GLY   A 1 55  ? 7.164  -5.537  12.680 1.00 30.16 ? 61  GLY   A N   1 
ATOM   420  C  CA  . GLY   A 1 55  ? 8.552  -5.614  13.083 1.00 30.40 ? 61  GLY   A CA  1 
ATOM   421  C  C   . GLY   A 1 55  ? 8.703  -5.780  14.575 1.00 29.72 ? 61  GLY   A C   1 
ATOM   422  O  O   . GLY   A 1 55  ? 7.720  -6.092  15.260 1.00 29.85 ? 61  GLY   A O   1 
ATOM   423  N  N   . VAL   A 1 56  ? 9.951  -5.601  15.063 1.00 28.65 ? 62  VAL   A N   1 
ATOM   424  C  CA  . VAL   A 1 56  ? 10.406 -5.727  16.451 1.00 28.90 ? 62  VAL   A CA  1 
ATOM   425  C  C   . VAL   A 1 56  ? 11.301 -4.534  16.805 1.00 28.90 ? 62  VAL   A C   1 
ATOM   426  O  O   . VAL   A 1 56  ? 12.242 -4.220  16.075 1.00 29.74 ? 62  VAL   A O   1 
ATOM   427  C  CB  . VAL   A 1 56  ? 11.195 -7.053  16.657 1.00 29.23 ? 62  VAL   A CB  1 
ATOM   428  C  CG1 . VAL   A 1 56  ? 11.572 -7.262  18.115 1.00 29.29 ? 62  VAL   A CG1 1 
ATOM   429  C  CG2 . VAL   A 1 56  ? 10.424 -8.247  16.133 1.00 29.96 ? 62  VAL   A CG2 1 
ATOM   430  N  N   . TYR   A 1 57  ? 11.049 -3.913  17.926 1.00 28.01 ? 63  TYR   A N   1 
ATOM   431  C  CA  . TYR   A 1 57  ? 11.872 -2.793  18.394 1.00 28.35 ? 63  TYR   A CA  1 
ATOM   432  C  C   . TYR   A 1 57  ? 12.409 -3.070  19.796 1.00 29.64 ? 63  TYR   A C   1 
ATOM   433  O  O   . TYR   A 1 57  ? 11.774 -3.788  20.571 1.00 29.63 ? 63  TYR   A O   1 
ATOM   434  C  CB  . TYR   A 1 57  ? 11.111 -1.444  18.338 1.00 26.94 ? 63  TYR   A CB  1 
ATOM   435  C  CG  . TYR   A 1 57  ? 10.164 -1.177  19.492 1.00 26.70 ? 63  TYR   A CG  1 
ATOM   436  C  CD1 . TYR   A 1 57  ? 8.914  -1.780  19.544 1.00 26.80 ? 63  TYR   A CD1 1 
ATOM   437  C  CD2 . TYR   A 1 57  ? 10.488 -0.263  20.493 1.00 28.00 ? 63  TYR   A CD2 1 
ATOM   438  C  CE1 . TYR   A 1 57  ? 8.024  -1.516  20.578 1.00 27.63 ? 63  TYR   A CE1 1 
ATOM   439  C  CE2 . TYR   A 1 57  ? 9.599  0.013   21.542 1.00 28.86 ? 63  TYR   A CE2 1 
ATOM   440  C  CZ  . TYR   A 1 57  ? 8.357  -0.605  21.563 1.00 29.16 ? 63  TYR   A CZ  1 
ATOM   441  O  OH  . TYR   A 1 57  ? 7.452  -0.408  22.569 1.00 30.58 ? 63  TYR   A OH  1 
ATOM   442  N  N   . TYR   A 1 58  ? 13.564 -2.486  20.120 1.00 30.23 ? 64  TYR   A N   1 
ATOM   443  C  CA  . TYR   A 1 58  ? 14.142 -2.641  21.437 1.00 31.67 ? 64  TYR   A CA  1 
ATOM   444  C  C   . TYR   A 1 58  ? 13.683 -1.489  22.365 1.00 31.74 ? 64  TYR   A C   1 
ATOM   445  O  O   . TYR   A 1 58  ? 13.834 -0.329  21.987 1.00 30.75 ? 64  TYR   A O   1 
ATOM   446  C  CB  . TYR   A 1 58  ? 15.687 -2.736  21.374 1.00 32.18 ? 64  TYR   A CB  1 
ATOM   447  C  CG  . TYR   A 1 58  ? 16.272 -2.830  22.762 1.00 33.68 ? 64  TYR   A CG  1 
ATOM   448  C  CD1 . TYR   A 1 58  ? 16.036 -3.944  23.561 1.00 34.75 ? 64  TYR   A CD1 1 
ATOM   449  C  CD2 . TYR   A 1 58  ? 16.956 -1.759  23.323 1.00 35.33 ? 64  TYR   A CD2 1 
ATOM   450  C  CE1 . TYR   A 1 58  ? 16.512 -4.012  24.860 1.00 36.55 ? 64  TYR   A CE1 1 
ATOM   451  C  CE2 . TYR   A 1 58  ? 17.426 -1.806  24.628 1.00 36.81 ? 64  TYR   A CE2 1 
ATOM   452  C  CZ  . TYR   A 1 58  ? 17.192 -2.933  25.398 1.00 38.30 ? 64  TYR   A CZ  1 
ATOM   453  O  OH  . TYR   A 1 58  ? 17.624 -2.970  26.689 1.00 40.76 ? 64  TYR   A OH  1 
ATOM   454  N  N   . CYS   A 1 59  ? 13.162 -1.815  23.577 1.00 32.58 ? 65  CYS   A N   1 
ATOM   455  C  CA  . CYS   A 1 59  ? 12.668 -0.829  24.547 1.00 34.60 ? 65  CYS   A CA  1 
ATOM   456  C  C   . CYS   A 1 59  ? 13.537 -0.827  25.818 1.00 36.72 ? 65  CYS   A C   1 
ATOM   457  O  O   . CYS   A 1 59  ? 13.367 -1.680  26.704 1.00 36.25 ? 65  CYS   A O   1 
ATOM   458  C  CB  . CYS   A 1 59  ? 11.189 -1.072  24.861 1.00 35.19 ? 65  CYS   A CB  1 
ATOM   459  S  SG  . CYS   A 1 59  ? 10.531 -0.069  26.223 1.00 36.53 ? 65  CYS   A SG  1 
ATOM   460  N  N   . SER   A 1 60  ? 14.481 0.133   25.896 1.00 37.70 ? 66  SER   A N   1 
ATOM   461  C  CA  . SER   A 1 60  ? 15.439 0.190   26.990 1.00 39.13 ? 66  SER   A CA  1 
ATOM   462  C  C   . SER   A 1 60  ? 14.826 0.418   28.371 1.00 40.65 ? 66  SER   A C   1 
ATOM   463  O  O   . SER   A 1 60  ? 15.361 -0.110  29.362 1.00 41.22 ? 66  SER   A O   1 
ATOM   464  C  CB  . SER   A 1 60  ? 16.545 1.203   26.711 1.00 40.62 ? 66  SER   A CB  1 
ATOM   465  O  OG  . SER   A 1 60  ? 16.165 2.525   27.019 1.00 42.99 ? 66  SER   A OG  1 
ATOM   466  N  N   . SER   A 1 61  ? 13.676 1.120   28.443 1.00 40.91 ? 67  SER   A N   1 
ATOM   467  C  CA  . SER   A 1 61  ? 12.962 1.343   29.711 1.00 41.05 ? 67  SER   A CA  1 
ATOM   468  C  C   . SER   A 1 61  ? 12.360 0.034   30.314 1.00 40.87 ? 67  SER   A C   1 
ATOM   469  O  O   . SER   A 1 61  ? 11.970 0.023   31.484 1.00 40.58 ? 67  SER   A O   1 
ATOM   470  C  CB  . SER   A 1 61  ? 11.886 2.410   29.545 1.00 42.29 ? 67  SER   A CB  1 
ATOM   471  O  OG  . SER   A 1 61  ? 10.916 2.028   28.584 1.00 43.89 ? 67  SER   A OG  1 
ATOM   472  N  N   . ARG   A 1 62  ? 12.269 -1.045  29.511 1.00 39.83 ? 68  ARG   A N   1 
ATOM   473  C  CA  . ARG   A 1 62  ? 11.805 -2.351  29.968 1.00 40.58 ? 68  ARG   A CA  1 
ATOM   474  C  C   . ARG   A 1 62  ? 12.876 -3.460  29.772 1.00 42.56 ? 68  ARG   A C   1 
ATOM   475  O  O   . ARG   A 1 62  ? 12.643 -4.620  30.144 1.00 43.01 ? 68  ARG   A O   1 
ATOM   476  C  CB  . ARG   A 1 62  ? 10.563 -2.764  29.180 1.00 40.97 ? 68  ARG   A CB  1 
ATOM   477  C  CG  . ARG   A 1 62  ? 9.348  -1.920  29.420 1.00 41.91 ? 68  ARG   A CG  1 
ATOM   478  C  CD  . ARG   A 1 62  ? 8.671  -2.361  30.690 1.00 44.45 ? 68  ARG   A CD  1 
ATOM   479  N  NE  . ARG   A 1 62  ? 7.529  -1.513  30.992 1.00 46.11 ? 68  ARG   A NE  1 
ATOM   480  C  CZ  . ARG   A 1 62  ? 7.597  -0.357  31.642 1.00 46.53 ? 68  ARG   A CZ  1 
ATOM   481  N  NH1 . ARG   A 1 62  ? 8.768  0.108   32.068 1.00 45.53 ? 68  ARG   A NH1 1 
ATOM   482  N  NH2 . ARG   A 1 62  ? 6.502  0.361   31.842 1.00 46.29 ? 68  ARG   A NH2 1 
ATOM   483  N  N   . ARG   A 1 63  ? 14.019 -3.116  29.134 1.00 43.54 ? 69  ARG   A N   1 
ATOM   484  C  CA  . ARG   A 1 63  ? 15.082 -4.034  28.738 1.00 44.73 ? 69  ARG   A CA  1 
ATOM   485  C  C   . ARG   A 1 63  ? 14.485 -5.200  27.909 1.00 44.84 ? 69  ARG   A C   1 
ATOM   486  O  O   . ARG   A 1 63  ? 14.812 -6.374  28.138 1.00 45.93 ? 69  ARG   A O   1 
ATOM   487  C  CB  . ARG   A 1 63  ? 15.901 -4.500  29.940 1.00 46.72 ? 69  ARG   A CB  1 
ATOM   488  C  CG  . ARG   A 1 63  ? 16.888 -3.446  30.429 1.00 51.71 ? 69  ARG   A CG  1 
ATOM   489  C  CD  . ARG   A 1 63  ? 17.914 -4.061  31.338 1.00 58.15 ? 69  ARG   A CD  1 
ATOM   490  N  NE  . ARG   A 1 63  ? 18.280 -3.161  32.432 1.00 65.24 ? 69  ARG   A NE  1 
ATOM   491  C  CZ  . ARG   A 1 63  ? 18.185 -3.470  33.723 1.00 70.57 ? 69  ARG   A CZ  1 
ATOM   492  N  NH1 . ARG   A 1 63  ? 17.740 -4.668  34.098 1.00 70.83 ? 69  ARG   A NH1 1 
ATOM   493  N  NH2 . ARG   A 1 63  ? 18.542 -2.585  34.652 1.00 72.32 ? 69  ARG   A NH2 1 
ATOM   494  N  N   . LYS   A 1 64  ? 13.538 -4.863  27.005 1.00 42.98 ? 70  LYS   A N   1 
ATOM   495  C  CA  . LYS   A 1 64  ? 12.778 -5.846  26.231 1.00 41.65 ? 70  LYS   A CA  1 
ATOM   496  C  C   . LYS   A 1 64  ? 12.576 -5.448  24.782 1.00 39.51 ? 70  LYS   A C   1 
ATOM   497  O  O   . LYS   A 1 64  ? 12.233 -4.299  24.526 1.00 39.86 ? 70  LYS   A O   1 
ATOM   498  C  CB  . LYS   A 1 64  ? 11.363 -5.945  26.823 1.00 42.80 ? 70  LYS   A CB  1 
ATOM   499  C  CG  . LYS   A 1 64  ? 11.045 -7.269  27.438 1.00 47.33 ? 70  LYS   A CG  1 
ATOM   500  C  CD  . LYS   A 1 64  ? 9.682  -7.234  28.057 1.00 53.23 ? 70  LYS   A CD  1 
ATOM   501  C  CE  . LYS   A 1 64  ? 9.573  -8.200  29.207 1.00 58.31 ? 70  LYS   A CE  1 
ATOM   502  N  NZ  . LYS   A 1 64  ? 10.269 -7.686  30.421 1.00 62.04 ? 70  LYS   A NZ  1 
ATOM   503  N  N   . HIS   A 1 65  ? 12.637 -6.432  23.862 1.00 37.14 ? 71  HIS   A N   1 
ATOM   504  C  CA  . HIS   A 1 65  ? 12.308 -6.288  22.446 1.00 35.35 ? 71  HIS   A CA  1 
ATOM   505  C  C   . HIS   A 1 65  ? 10.811 -6.640  22.328 1.00 34.67 ? 71  HIS   A C   1 
ATOM   506  O  O   . HIS   A 1 65  ? 10.370 -7.634  22.900 1.00 34.76 ? 71  HIS   A O   1 
ATOM   507  C  CB  . HIS   A 1 65  ? 13.097 -7.280  21.599 1.00 35.24 ? 71  HIS   A CB  1 
ATOM   508  C  CG  . HIS   A 1 65  ? 14.573 -7.066  21.608 1.00 37.36 ? 71  HIS   A CG  1 
ATOM   509  N  ND1 . HIS   A 1 65  ? 15.201 -6.292  20.636 1.00 39.23 ? 71  HIS   A ND1 1 
ATOM   510  C  CD2 . HIS   A 1 65  ? 15.506 -7.531  22.463 1.00 38.50 ? 71  HIS   A CD2 1 
ATOM   511  C  CE1 . HIS   A 1 65  ? 16.487 -6.332  20.926 1.00 39.49 ? 71  HIS   A CE1 1 
ATOM   512  N  NE2 . HIS   A 1 65  ? 16.718 -7.039  22.035 1.00 39.45 ? 71  HIS   A NE2 1 
ATOM   513  N  N   . TYR   A 1 66  ? 10.035 -5.818  21.613 1.00 33.92 ? 72  TYR   A N   1 
ATOM   514  C  CA  . TYR   A 1 66  ? 8.597  -5.985  21.447 1.00 32.97 ? 72  TYR   A CA  1 
ATOM   515  C  C   . TYR   A 1 66  ? 8.170  -6.054  19.982 1.00 32.34 ? 72  TYR   A C   1 
ATOM   516  O  O   . TYR   A 1 66  ? 8.484  -5.157  19.188 1.00 30.48 ? 72  TYR   A O   1 
ATOM   517  C  CB  . TYR   A 1 66  ? 7.841  -4.793  22.048 1.00 32.23 ? 72  TYR   A CB  1 
ATOM   518  C  CG  . TYR   A 1 66  ? 7.805  -4.738  23.545 1.00 33.20 ? 72  TYR   A CG  1 
ATOM   519  C  CD1 . TYR   A 1 66  ? 7.090  -5.674  24.276 1.00 34.29 ? 72  TYR   A CD1 1 
ATOM   520  C  CD2 . TYR   A 1 66  ? 8.386  -3.684  24.233 1.00 34.75 ? 72  TYR   A CD2 1 
ATOM   521  C  CE1 . TYR   A 1 66  ? 7.017  -5.604  25.662 1.00 35.69 ? 72  TYR   A CE1 1 
ATOM   522  C  CE2 . TYR   A 1 66  ? 8.288  -3.582  25.614 1.00 35.83 ? 72  TYR   A CE2 1 
ATOM   523  C  CZ  . TYR   A 1 66  ? 7.618  -4.554  26.328 1.00 37.10 ? 72  TYR   A CZ  1 
ATOM   524  O  OH  . TYR   A 1 66  ? 7.546  -4.476  27.700 1.00 39.58 ? 72  TYR   A OH  1 
ATOM   525  N  N   . PRO   A 1 67  ? 7.317  -7.051  19.648 1.00 32.65 ? 73  PRO   A N   1 
ATOM   526  C  CA  . PRO   A 1 67  ? 6.748  -7.085  18.286 1.00 32.33 ? 73  PRO   A CA  1 
ATOM   527  C  C   . PRO   A 1 67  ? 5.672  -5.977  18.182 1.00 31.86 ? 73  PRO   A C   1 
ATOM   528  O  O   . PRO   A 1 67  ? 4.945  -5.745  19.173 1.00 32.21 ? 73  PRO   A O   1 
ATOM   529  C  CB  . PRO   A 1 67  ? 6.160  -8.500  18.174 1.00 33.31 ? 73  PRO   A CB  1 
ATOM   530  C  CG  . PRO   A 1 67  ? 5.905  -8.946  19.594 1.00 33.91 ? 73  PRO   A CG  1 
ATOM   531  C  CD  . PRO   A 1 67  ? 6.829  -8.159  20.501 1.00 32.47 ? 73  PRO   A CD  1 
ATOM   532  N  N   . VAL   A 1 68  ? 5.605  -5.264  17.009 1.00 29.79 ? 74  VAL   A N   1 
ATOM   533  C  CA  . VAL   A 1 68  ? 4.726  -4.124  16.755 1.00 29.33 ? 74  VAL   A CA  1 
ATOM   534  C  C   . VAL   A 1 68  ? 4.253  -4.053  15.321 1.00 29.87 ? 74  VAL   A C   1 
ATOM   535  O  O   . VAL   A 1 68  ? 4.980  -4.383  14.375 1.00 29.97 ? 74  VAL   A O   1 
ATOM   536  C  CB  . VAL   A 1 68  ? 5.396  -2.728  17.095 1.00 29.95 ? 74  VAL   A CB  1 
ATOM   537  C  CG1 . VAL   A 1 68  ? 5.427  -2.438  18.590 1.00 31.27 ? 74  VAL   A CG1 1 
ATOM   538  C  CG2 . VAL   A 1 68  ? 6.775  -2.577  16.466 1.00 29.22 ? 74  VAL   A CG2 1 
ATOM   539  N  N   . SER   A 1 69  ? 3.064  -3.495  15.146 1.00 30.49 ? 75  SER   A N   1 
ATOM   540  C  CA  . SER   A 1 69  ? 2.551  -3.170  13.815 1.00 31.36 ? 75  SER   A CA  1 
ATOM   541  C  C   . SER   A 1 69  ? 2.722  -1.699  13.746 1.00 30.93 ? 75  SER   A C   1 
ATOM   542  O  O   . SER   A 1 69  ? 2.381  -1.018  14.713 1.00 30.55 ? 75  SER   A O   1 
ATOM   543  C  CB  . SER   A 1 69  ? 1.066  -3.489  13.685 1.00 33.34 ? 75  SER   A CB  1 
ATOM   544  O  OG  . SER   A 1 69  ? 0.933  -4.849  13.328 1.00 37.15 ? 75  SER   A OG  1 
ATOM   545  N  N   . PHE   A 1 70  ? 3.236  -1.196  12.634 1.00 30.98 ? 76  PHE   A N   1 
ATOM   546  C  CA  . PHE   A 1 70  ? 3.464  0.235   12.551 1.00 32.59 ? 76  PHE   A CA  1 
ATOM   547  C  C   . PHE   A 1 70  ? 2.900  0.861   11.285 1.00 35.06 ? 76  PHE   A C   1 
ATOM   548  O  O   . PHE   A 1 70  ? 2.578  0.153   10.322 1.00 36.62 ? 76  PHE   A O   1 
ATOM   549  C  CB  . PHE   A 1 70  ? 4.943  0.548   12.768 1.00 31.86 ? 76  PHE   A CB  1 
ATOM   550  C  CG  . PHE   A 1 70  ? 5.922  -0.158  11.868 1.00 30.87 ? 76  PHE   A CG  1 
ATOM   551  C  CD1 . PHE   A 1 70  ? 6.503  -1.346  12.255 1.00 30.68 ? 76  PHE   A CD1 1 
ATOM   552  C  CD2 . PHE   A 1 70  ? 6.274  0.381   10.642 1.00 30.96 ? 76  PHE   A CD2 1 
ATOM   553  C  CE1 . PHE   A 1 70  ? 7.429  -1.978  11.440 1.00 31.16 ? 76  PHE   A CE1 1 
ATOM   554  C  CE2 . PHE   A 1 70  ? 7.211  -0.246  9.833  1.00 31.32 ? 76  PHE   A CE2 1 
ATOM   555  C  CZ  . PHE   A 1 70  ? 7.784  -1.421  10.233 1.00 30.65 ? 76  PHE   A CZ  1 
ATOM   556  N  N   . SER   A 1 71  ? 2.677  2.175   11.324 1.00 35.32 ? 77  SER   A N   1 
ATOM   557  C  CA  . SER   A 1 71  ? 2.100  2.856   10.176 1.00 36.38 ? 77  SER   A CA  1 
ATOM   558  C  C   . SER   A 1 71  ? 3.148  3.170   9.100  1.00 36.66 ? 77  SER   A C   1 
ATOM   559  O  O   . SER   A 1 71  ? 4.328  2.880   9.275  1.00 36.00 ? 77  SER   A O   1 
ATOM   560  C  CB  . SER   A 1 71  ? 1.355  4.113   10.620 1.00 37.93 ? 77  SER   A CB  1 
ATOM   561  O  OG  . SER   A 1 71  ? 2.246  5.163   10.955 1.00 39.32 ? 77  SER   A OG  1 
ATOM   562  N  N   . LYS   A 1 72  ? 2.691  3.700   7.966  1.00 37.95 ? 78  LYS   A N   1 
ATOM   563  C  CA  . LYS   A 1 72  ? 3.539  4.106   6.840  1.00 39.99 ? 78  LYS   A CA  1 
ATOM   564  C  C   . LYS   A 1 72  ? 4.189  5.472   7.149  1.00 41.44 ? 78  LYS   A C   1 
ATOM   565  O  O   . LYS   A 1 72  ? 3.623  6.265   7.905  1.00 41.87 ? 78  LYS   A O   1 
ATOM   566  C  CB  . LYS   A 1 72  ? 2.711  4.143   5.532  1.00 42.29 ? 78  LYS   A CB  1 
ATOM   567  C  CG  . LYS   A 1 72  ? 1.879  2.859   5.347  1.00 47.33 ? 78  LYS   A CG  1 
ATOM   568  C  CD  . LYS   A 1 72  ? 1.626  2.508   3.880  1.00 53.04 ? 78  LYS   A CD  1 
ATOM   569  C  CE  . LYS   A 1 72  ? 2.905  2.172   3.154  1.00 57.76 ? 78  LYS   A CE  1 
ATOM   570  N  NZ  . LYS   A 1 72  ? 2.792  2.429   1.693  1.00 59.55 ? 78  LYS   A NZ  1 
ATOM   571  N  N   . PRO   A 1 73  ? 5.415  5.711   6.650  1.00 41.88 ? 79  PRO   A N   1 
ATOM   572  C  CA  . PRO   A 1 73  ? 6.113  6.980   6.957  1.00 43.33 ? 79  PRO   A CA  1 
ATOM   573  C  C   . PRO   A 1 73  ? 5.296  8.224   6.601  1.00 44.62 ? 79  PRO   A C   1 
ATOM   574  O  O   . PRO   A 1 73  ? 4.887  8.381   5.452  1.00 44.70 ? 79  PRO   A O   1 
ATOM   575  C  CB  . PRO   A 1 73  ? 7.394  6.896   6.122  1.00 43.81 ? 79  PRO   A CB  1 
ATOM   576  C  CG  . PRO   A 1 73  ? 7.596  5.449   5.875  1.00 43.96 ? 79  PRO   A CG  1 
ATOM   577  C  CD  . PRO   A 1 73  ? 6.226  4.838   5.787  1.00 41.58 ? 79  PRO   A CD  1 
ATOM   578  N  N   . SER   A 1 74  ? 5.055  9.106   7.593  1.00 45.12 ? 80  SER   A N   1 
ATOM   579  C  CA  . SER   A 1 74  ? 4.212  10.274  7.373  1.00 46.15 ? 80  SER   A CA  1 
ATOM   580  C  C   . SER   A 1 74  ? 4.534  11.493  8.285  1.00 46.32 ? 80  SER   A C   1 
ATOM   581  O  O   . SER   A 1 74  ? 5.401  11.419  9.149  1.00 45.11 ? 80  SER   A O   1 
ATOM   582  C  CB  . SER   A 1 74  ? 2.753  9.857   7.544  1.00 48.70 ? 80  SER   A CB  1 
ATOM   583  O  OG  . SER   A 1 74  ? 2.504  9.514   8.898  1.00 52.16 ? 80  SER   A OG  1 
ATOM   584  N  N   . LEU   A 1 75  ? 3.845  12.636  8.033  1.00 47.26 ? 81  LEU   A N   1 
ATOM   585  C  CA  . LEU   A 1 75  ? 3.939  13.894  8.783  1.00 48.28 ? 81  LEU   A CA  1 
ATOM   586  C  C   . LEU   A 1 75  ? 3.016  13.764  9.989  1.00 49.57 ? 81  LEU   A C   1 
ATOM   587  O  O   . LEU   A 1 75  ? 1.822  13.533  9.803  1.00 50.83 ? 81  LEU   A O   1 
ATOM   588  C  CB  . LEU   A 1 75  ? 3.397  15.045  7.920  1.00 48.17 ? 81  LEU   A CB  1 
ATOM   589  C  CG  . LEU   A 1 75  ? 4.378  15.733  7.015  1.00 49.02 ? 81  LEU   A CG  1 
ATOM   590  C  CD1 . LEU   A 1 75  ? 3.653  16.584  6.041  1.00 50.10 ? 81  LEU   A CD1 1 
ATOM   591  C  CD2 . LEU   A 1 75  ? 5.361  16.565  7.813  1.00 49.23 ? 81  LEU   A CD2 1 
ATOM   592  N  N   . ILE   A 1 76  ? 3.537  13.915  11.204 1.00 49.04 ? 82  ILE   A N   1 
ATOM   593  C  CA  . ILE   A 1 76  ? 2.722  13.791  12.403 1.00 49.71 ? 82  ILE   A CA  1 
ATOM   594  C  C   . ILE   A 1 76  ? 3.051  14.941  13.344 1.00 51.38 ? 82  ILE   A C   1 
ATOM   595  O  O   . ILE   A 1 76  ? 4.227  15.250  13.546 1.00 51.41 ? 82  ILE   A O   1 
ATOM   596  C  CB  . ILE   A 1 76  ? 2.950  12.396  13.081 1.00 49.55 ? 82  ILE   A CB  1 
ATOM   597  C  CG1 . ILE   A 1 76  ? 2.308  11.248  12.267 1.00 50.56 ? 82  ILE   A CG1 1 
ATOM   598  C  CG2 . ILE   A 1 76  ? 2.474  12.372  14.535 1.00 49.29 ? 82  ILE   A CG2 1 
ATOM   599  C  CD1 . ILE   A 1 76  ? 2.918  9.948   12.423 1.00 51.54 ? 82  ILE   A CD1 1 
ATOM   600  N  N   . PHE   A 1 77  ? 2.023  15.566  13.934 1.00 52.36 ? 83  PHE   A N   1 
ATOM   601  C  CA  . PHE   A 1 77  ? 2.241  16.629  14.897 1.00 54.11 ? 83  PHE   A CA  1 
ATOM   602  C  C   . PHE   A 1 77  ? 2.948  16.093  16.147 1.00 55.04 ? 83  PHE   A C   1 
ATOM   603  O  O   . PHE   A 1 77  ? 2.547  15.068  16.710 1.00 55.17 ? 83  PHE   A O   1 
ATOM   604  C  CB  . PHE   A 1 77  ? 0.906  17.265  15.315 1.00 54.72 ? 83  PHE   A CB  1 
ATOM   605  C  CG  . PHE   A 1 77  ? 1.088  18.497  16.172 1.00 55.44 ? 83  PHE   A CG  1 
ATOM   606  C  CD1 . PHE   A 1 77  ? 1.612  19.659  15.639 1.00 55.88 ? 83  PHE   A CD1 1 
ATOM   607  C  CD2 . PHE   A 1 77  ? 0.755  18.481  17.516 1.00 56.28 ? 83  PHE   A CD2 1 
ATOM   608  C  CE1 . PHE   A 1 77  ? 1.798  20.782  16.432 1.00 56.56 ? 83  PHE   A CE1 1 
ATOM   609  C  CE2 . PHE   A 1 77  ? 0.912  19.615  18.302 1.00 56.63 ? 83  PHE   A CE2 1 
ATOM   610  C  CZ  . PHE   A 1 77  ? 1.455  20.750  17.761 1.00 56.30 ? 83  PHE   A CZ  1 
ATOM   611  N  N   . VAL   A 1 78  ? 4.016  16.785  16.561 1.00 55.32 ? 84  VAL   A N   1 
ATOM   612  C  CA  . VAL   A 1 78  ? 4.785  16.451  17.744 1.00 56.08 ? 84  VAL   A CA  1 
ATOM   613  C  C   . VAL   A 1 78  ? 4.800  17.712  18.607 1.00 57.16 ? 84  VAL   A C   1 
ATOM   614  O  O   . VAL   A 1 78  ? 5.185  18.792  18.127 1.00 57.21 ? 84  VAL   A O   1 
ATOM   615  C  CB  . VAL   A 1 78  ? 6.215  15.954  17.391 1.00 56.46 ? 84  VAL   A CB  1 
ATOM   616  C  CG1 . VAL   A 1 78  ? 7.069  15.781  18.643 1.00 56.73 ? 84  VAL   A CG1 1 
ATOM   617  C  CG2 . VAL   A 1 78  ? 6.165  14.653  16.594 1.00 56.88 ? 84  VAL   A CG2 1 
ATOM   618  N  N   . GLU   A 1 79  ? 4.316  17.585  19.857 1.00 57.62 ? 85  GLU   A N   1 
ATOM   619  C  CA  . GLU   A 1 79  ? 4.235  18.684  20.814 1.00 58.63 ? 85  GLU   A CA  1 
ATOM   620  C  C   . GLU   A 1 79  ? 5.618  19.233  21.156 1.00 59.31 ? 85  GLU   A C   1 
ATOM   621  O  O   . GLU   A 1 79  ? 6.616  18.508  21.078 1.00 59.22 ? 85  GLU   A O   1 
ATOM   622  C  CB  . GLU   A 1 79  ? 3.492  18.243  22.083 1.00 61.92 ? 85  GLU   A CB  1 
ATOM   623  C  CG  . GLU   A 1 79  ? 2.665  19.353  22.718 1.00 69.29 ? 85  GLU   A CG  1 
ATOM   624  C  CD  . GLU   A 1 79  ? 1.959  18.978  24.008 1.00 79.06 ? 85  GLU   A CD  1 
ATOM   625  O  OE1 . GLU   A 1 79  ? 1.220  19.831  24.554 1.00 81.23 ? 85  GLU   A OE1 1 
ATOM   626  O  OE2 . GLU   A 1 79  ? 2.144  17.830  24.477 1.00 82.52 ? 85  GLU   A OE2 1 
ATOM   627  N  N   . ALA   A 1 80  ? 5.679  20.529  21.481 1.00 59.56 ? 86  ALA   A N   1 
ATOM   628  C  CA  . ALA   A 1 80  ? 6.916  21.243  21.811 1.00 60.52 ? 86  ALA   A CA  1 
ATOM   629  C  C   . ALA   A 1 80  ? 7.763  20.557  22.896 1.00 60.96 ? 86  ALA   A C   1 
ATOM   630  O  O   . ALA   A 1 80  ? 7.230  20.174  23.930 1.00 61.82 ? 86  ALA   A O   1 
ATOM   631  C  CB  . ALA   A 1 80  ? 6.584  22.666  22.253 1.00 60.60 ? 86  ALA   A CB  1 
ATOM   632  N  N   . SER   A 1 81  ? 9.082  20.463  22.681 1.00 60.18 ? 87  SER   A N   1 
ATOM   633  C  CA  . SER   A 1 81  ? 10.032 19.904  23.644 1.00 59.98 ? 87  SER   A CA  1 
ATOM   634  C  C   . SER   A 1 81  ? 11.178 20.926  23.928 1.00 60.11 ? 87  SER   A C   1 
ATOM   635  O  O   . SER   A 1 81  ? 11.176 22.041  23.391 1.00 60.02 ? 87  SER   A O   1 
ATOM   636  C  CB  . SER   A 1 81  ? 10.610 18.599  23.094 1.00 60.77 ? 87  SER   A CB  1 
ATOM   637  O  OG  . SER   A 1 81  ? 11.533 18.833  22.044 1.00 62.20 ? 87  SER   A OG  1 
ATOM   638  N  N   . GLU   A 1 82  ? 12.159 20.551  24.769 1.00 60.00 ? 88  GLU   A N   1 
ATOM   639  C  CA  . GLU   A 1 82  ? 13.328 21.412  25.020 1.00 59.88 ? 88  GLU   A CA  1 
ATOM   640  C  C   . GLU   A 1 82  ? 14.290 21.456  23.794 1.00 58.19 ? 88  GLU   A C   1 
ATOM   641  O  O   . GLU   A 1 82  ? 15.162 22.325  23.724 1.00 58.60 ? 88  GLU   A O   1 
ATOM   642  C  CB  . GLU   A 1 82  ? 14.086 20.966  26.299 1.00 63.15 ? 88  GLU   A CB  1 
ATOM   643  C  CG  . GLU   A 1 82  ? 14.255 19.454  26.455 1.00 69.91 ? 88  GLU   A CG  1 
ATOM   644  C  CD  . GLU   A 1 82  ? 14.722 18.996  27.829 1.00 78.81 ? 88  GLU   A CD  1 
ATOM   645  O  OE1 . GLU   A 1 82  ? 15.206 19.847  28.613 1.00 81.66 ? 88  GLU   A OE1 1 
ATOM   646  O  OE2 . GLU   A 1 82  ? 14.604 17.784  28.123 1.00 80.83 ? 88  GLU   A OE2 1 
ATOM   647  N  N   . TYR   A 1 83  ? 14.120 20.520  22.836 1.00 56.14 ? 89  TYR   A N   1 
ATOM   648  C  CA  . TYR   A 1 83  ? 14.947 20.390  21.644 1.00 54.26 ? 89  TYR   A CA  1 
ATOM   649  C  C   . TYR   A 1 83  ? 14.285 21.033  20.411 1.00 51.64 ? 89  TYR   A C   1 
ATOM   650  O  O   . TYR   A 1 83  ? 14.989 21.478  19.502 1.00 51.01 ? 89  TYR   A O   1 
ATOM   651  C  CB  . TYR   A 1 83  ? 15.219 18.902  21.355 1.00 54.34 ? 89  TYR   A CB  1 
ATOM   652  C  CG  . TYR   A 1 83  ? 15.679 18.098  22.555 1.00 55.56 ? 89  TYR   A CG  1 
ATOM   653  C  CD1 . TYR   A 1 83  ? 17.006 18.118  22.966 1.00 56.36 ? 89  TYR   A CD1 1 
ATOM   654  C  CD2 . TYR   A 1 83  ? 14.787 17.314  23.276 1.00 56.62 ? 89  TYR   A CD2 1 
ATOM   655  C  CE1 . TYR   A 1 83  ? 17.433 17.385  24.072 1.00 57.12 ? 89  TYR   A CE1 1 
ATOM   656  C  CE2 . TYR   A 1 83  ? 15.202 16.575  24.381 1.00 57.42 ? 89  TYR   A CE2 1 
ATOM   657  C  CZ  . TYR   A 1 83  ? 16.527 16.613  24.777 1.00 58.27 ? 89  TYR   A CZ  1 
ATOM   658  O  OH  . TYR   A 1 83  ? 16.947 15.864  25.857 1.00 60.24 ? 89  TYR   A OH  1 
ATOM   659  N  N   . TYR   A 1 84  ? 12.946 21.030  20.355 1.00 49.55 ? 90  TYR   A N   1 
ATOM   660  C  CA  . TYR   A 1 84  ? 12.247 21.547  19.192 1.00 48.74 ? 90  TYR   A CA  1 
ATOM   661  C  C   . TYR   A 1 84  ? 10.995 22.297  19.556 1.00 48.98 ? 90  TYR   A C   1 
ATOM   662  O  O   . TYR   A 1 84  ? 10.263 21.866  20.454 1.00 49.37 ? 90  TYR   A O   1 
ATOM   663  C  CB  . TYR   A 1 84  ? 11.777 20.377  18.292 1.00 47.85 ? 90  TYR   A CB  1 
ATOM   664  C  CG  . TYR   A 1 84  ? 12.847 19.487  17.710 1.00 46.89 ? 90  TYR   A CG  1 
ATOM   665  C  CD1 . TYR   A 1 84  ? 12.989 18.170  18.132 1.00 46.87 ? 90  TYR   A CD1 1 
ATOM   666  C  CD2 . TYR   A 1 84  ? 13.654 19.927  16.671 1.00 46.52 ? 90  TYR   A CD2 1 
ATOM   667  C  CE1 . TYR   A 1 84  ? 13.939 17.328  17.565 1.00 47.18 ? 90  TYR   A CE1 1 
ATOM   668  C  CE2 . TYR   A 1 84  ? 14.615 19.096  16.104 1.00 46.72 ? 90  TYR   A CE2 1 
ATOM   669  C  CZ  . TYR   A 1 84  ? 14.744 17.792  16.543 1.00 47.26 ? 90  TYR   A CZ  1 
ATOM   670  O  OH  . TYR   A 1 84  ? 15.682 16.964  15.977 1.00 47.22 ? 90  TYR   A OH  1 
ATOM   671  N  N   . PRO   A 1 85  ? 10.623 23.314  18.763 1.00 48.39 ? 91  PRO   A N   1 
ATOM   672  C  CA  . PRO   A 1 85  ? 9.292  23.936  18.971 1.00 48.72 ? 91  PRO   A CA  1 
ATOM   673  C  C   . PRO   A 1 85  ? 8.180  22.970  18.480 1.00 49.07 ? 91  PRO   A C   1 
ATOM   674  O  O   . PRO   A 1 85  ? 8.489  21.947  17.845 1.00 48.78 ? 91  PRO   A O   1 
ATOM   675  C  CB  . PRO   A 1 85  ? 9.361  25.200  18.121 1.00 49.22 ? 91  PRO   A CB  1 
ATOM   676  C  CG  . PRO   A 1 85  ? 10.355 24.854  17.018 1.00 49.24 ? 91  PRO   A CG  1 
ATOM   677  C  CD  . PRO   A 1 85  ? 11.349 23.896  17.614 1.00 47.50 ? 91  PRO   A CD  1 
ATOM   678  N  N   . ALA   A 1 86  ? 6.898  23.269  18.758 1.00 48.97 ? 92  ALA   A N   1 
ATOM   679  C  CA  . ALA   A 1 86  ? 5.804  22.381  18.301 1.00 49.34 ? 92  ALA   A CA  1 
ATOM   680  C  C   . ALA   A 1 86  ? 5.758  22.412  16.756 1.00 48.46 ? 92  ALA   A C   1 
ATOM   681  O  O   . ALA   A 1 86  ? 5.756  23.496  16.172 1.00 48.54 ? 92  ALA   A O   1 
ATOM   682  C  CB  . ALA   A 1 86  ? 4.470  22.834  18.879 1.00 49.78 ? 92  ALA   A CB  1 
ATOM   683  N  N   . ARG   A 1 87  ? 5.806  21.229  16.104 1.00 46.93 ? 93  ARG   A N   1 
ATOM   684  C  CA  . ARG   A 1 87  ? 5.877  21.165  14.646 1.00 45.31 ? 93  ARG   A CA  1 
ATOM   685  C  C   . ARG   A 1 87  ? 5.334  19.822  14.103 1.00 44.75 ? 93  ARG   A C   1 
ATOM   686  O  O   . ARG   A 1 87  ? 4.959  18.957  14.882 1.00 45.54 ? 93  ARG   A O   1 
ATOM   687  C  CB  . ARG   A 1 87  ? 7.373  21.319  14.267 1.00 44.70 ? 93  ARG   A CB  1 
ATOM   688  C  CG  . ARG   A 1 87  ? 8.184  19.998  14.384 1.00 43.69 ? 93  ARG   A CG  1 
ATOM   689  C  CD  . ARG   A 1 87  ? 9.554  20.121  14.985 1.00 43.63 ? 93  ARG   A CD  1 
ATOM   690  N  NE  . ARG   A 1 87  ? 10.443 19.041  14.521 1.00 43.22 ? 93  ARG   A NE  1 
ATOM   691  C  CZ  . ARG   A 1 87  ? 10.542 17.846  15.103 1.00 40.77 ? 93  ARG   A CZ  1 
ATOM   692  N  NH1 . ARG   A 1 87  ? 11.359 16.927  14.610 1.00 38.89 ? 93  ARG   A NH1 1 
ATOM   693  N  NH2 . ARG   A 1 87  ? 9.813  17.561  16.176 1.00 38.00 ? 93  ARG   A NH2 1 
ATOM   694  N  N   . TYR   A 1 88  ? 5.368  19.617  12.774 1.00 43.86 ? 94  TYR   A N   1 
ATOM   695  C  CA  . TYR   A 1 88  ? 5.072  18.308  12.187 1.00 43.38 ? 94  TYR   A CA  1 
ATOM   696  C  C   . TYR   A 1 88  ? 6.430  17.621  11.884 1.00 40.41 ? 94  TYR   A C   1 
ATOM   697  O  O   . TYR   A 1 88  ? 7.292  18.214  11.224 1.00 39.83 ? 94  TYR   A O   1 
ATOM   698  C  CB  . TYR   A 1 88  ? 4.347  18.441  10.852 1.00 44.70 ? 94  TYR   A CB  1 
ATOM   699  C  CG  . TYR   A 1 88  ? 2.932  18.956  10.929 1.00 47.51 ? 94  TYR   A CG  1 
ATOM   700  C  CD1 . TYR   A 1 88  ? 1.856  18.083  10.981 1.00 49.19 ? 94  TYR   A CD1 1 
ATOM   701  C  CD2 . TYR   A 1 88  ? 2.664  20.309  10.827 1.00 49.36 ? 94  TYR   A CD2 1 
ATOM   702  C  CE1 . TYR   A 1 88  ? 0.546  18.549  10.963 1.00 51.02 ? 94  TYR   A CE1 1 
ATOM   703  C  CE2 . TYR   A 1 88  ? 1.364  20.790  10.843 1.00 51.36 ? 94  TYR   A CE2 1 
ATOM   704  C  CZ  . TYR   A 1 88  ? 0.304  19.906  10.915 1.00 52.97 ? 94  TYR   A CZ  1 
ATOM   705  O  OH  . TYR   A 1 88  ? -0.983 20.407  10.876 1.00 56.61 ? 94  TYR   A OH  1 
ATOM   706  N  N   . GLN   A 1 89  ? 6.620  16.383  12.360 1.00 37.77 ? 95  GLN   A N   1 
ATOM   707  C  CA  . GLN   A 1 89  ? 7.843  15.638  12.056 1.00 35.35 ? 95  GLN   A CA  1 
ATOM   708  C  C   . GLN   A 1 89  ? 7.493  14.715  10.894 1.00 33.39 ? 95  GLN   A C   1 
ATOM   709  O  O   . GLN   A 1 89  ? 6.460  14.055  10.927 1.00 33.23 ? 95  GLN   A O   1 
ATOM   710  C  CB  . GLN   A 1 89  ? 8.339  14.840  13.288 1.00 36.18 ? 95  GLN   A CB  1 
ATOM   711  C  CG  . GLN   A 1 89  ? 9.617  13.986  13.056 1.00 34.84 ? 95  GLN   A CG  1 
ATOM   712  C  CD  . GLN   A 1 89  ? 10.167 13.442  14.353 1.00 37.06 ? 95  GLN   A CD  1 
ATOM   713  O  OE1 . GLN   A 1 89  ? 10.301 14.169  15.343 1.00 38.63 ? 95  GLN   A OE1 1 
ATOM   714  N  NE2 . GLN   A 1 89  ? 10.525 12.156  14.381 1.00 35.35 ? 95  GLN   A NE2 1 
ATOM   715  N  N   . SER   A 1 90  ? 8.314  14.714  9.837  1.00 31.82 ? 96  SER   A N   1 
ATOM   716  C  CA  . SER   A 1 90  ? 8.059  13.898  8.647  1.00 31.00 ? 96  SER   A CA  1 
ATOM   717  C  C   . SER   A 1 90  ? 8.778  12.552  8.720  1.00 31.70 ? 96  SER   A C   1 
ATOM   718  O  O   . SER   A 1 90  ? 9.716  12.397  9.513  1.00 32.73 ? 96  SER   A O   1 
ATOM   719  C  CB  . SER   A 1 90  ? 8.501  14.634  7.393  1.00 30.51 ? 96  SER   A CB  1 
ATOM   720  O  OG  . SER   A 1 90  ? 9.901  14.826  7.449  1.00 32.61 ? 96  SER   A OG  1 
ATOM   721  N  N   . HIS   A 1 91  ? 8.314  11.572  7.915  1.00 30.62 ? 97  HIS   A N   1 
ATOM   722  C  CA  . HIS   A 1 91  ? 8.873  10.230  7.856  1.00 29.52 ? 97  HIS   A CA  1 
ATOM   723  C  C   . HIS   A 1 91  ? 8.715  9.491   9.193  1.00 29.34 ? 97  HIS   A C   1 
ATOM   724  O  O   . HIS   A 1 91  ? 9.556  8.680   9.547  1.00 28.43 ? 97  HIS   A O   1 
ATOM   725  C  CB  . HIS   A 1 91  ? 10.334 10.311  7.424  1.00 29.46 ? 97  HIS   A CB  1 
ATOM   726  C  CG  . HIS   A 1 91  ? 10.508 10.921  6.076  1.00 31.47 ? 97  HIS   A CG  1 
ATOM   727  N  ND1 . HIS   A 1 91  ? 10.534 10.142  4.933  1.00 33.32 ? 97  HIS   A ND1 1 
ATOM   728  C  CD2 . HIS   A 1 91  ? 10.588 12.222  5.716  1.00 32.64 ? 97  HIS   A CD2 1 
ATOM   729  C  CE1 . HIS   A 1 91  ? 10.669 10.991  3.919  1.00 33.21 ? 97  HIS   A CE1 1 
ATOM   730  N  NE2 . HIS   A 1 91  ? 10.688 12.249  4.338  1.00 33.32 ? 97  HIS   A NE2 1 
ATOM   731  N  N   . LEU   A 1 92  ? 7.656  9.812   9.960  1.00 30.35 ? 98  LEU   A N   1 
ATOM   732  C  CA  . LEU   A 1 92  ? 7.441  9.212   11.287 1.00 30.99 ? 98  LEU   A CA  1 
ATOM   733  C  C   . LEU   A 1 92  ? 6.418  8.086   11.227 1.00 30.94 ? 98  LEU   A C   1 
ATOM   734  O  O   . LEU   A 1 92  ? 5.361  8.260   10.608 1.00 30.66 ? 98  LEU   A O   1 
ATOM   735  C  CB  . LEU   A 1 92  ? 6.998  10.318  12.269 1.00 30.82 ? 98  LEU   A CB  1 
ATOM   736  C  CG  . LEU   A 1 92  ? 6.762  9.934   13.735 1.00 32.32 ? 98  LEU   A CG  1 
ATOM   737  C  CD1 . LEU   A 1 92  ? 8.031  9.431   14.377 1.00 32.63 ? 98  LEU   A CD1 1 
ATOM   738  C  CD2 . LEU   A 1 92  ? 6.196  11.129  14.529 1.00 32.75 ? 98  LEU   A CD2 1 
ATOM   739  N  N   . MET   A 1 93  ? 6.718  6.929   11.881 1.00 30.14 ? 99  MET   A N   1 
ATOM   740  C  CA  . MET   A 1 93  ? 5.780  5.799   11.867 1.00 30.51 ? 99  MET   A CA  1 
ATOM   741  C  C   . MET   A 1 93  ? 5.313  5.450   13.267 1.00 30.62 ? 99  MET   A C   1 
ATOM   742  O  O   . MET   A 1 93  ? 6.157  5.199   14.121 1.00 31.74 ? 99  MET   A O   1 
ATOM   743  C  CB  . MET   A 1 93  ? 6.420  4.580   11.208 1.00 30.90 ? 99  MET   A CB  1 
ATOM   744  C  CG  . MET   A 1 93  ? 6.940  4.868   9.818  1.00 31.95 ? 99  MET   A CG  1 
ATOM   745  S  SD  . MET   A 1 93  ? 8.004  3.559   9.183  1.00 37.09 ? 99  MET   A SD  1 
ATOM   746  C  CE  . MET   A 1 93  ? 9.235  3.525   10.394 1.00 34.42 ? 99  MET   A CE  1 
ATOM   747  N  N   . LEU   A 1 94  ? 3.997  5.441   13.525 1.00 30.41 ? 100 LEU   A N   1 
ATOM   748  C  CA  . LEU   A 1 94  ? 3.517  5.108   14.872 1.00 30.67 ? 100 LEU   A CA  1 
ATOM   749  C  C   . LEU   A 1 94  ? 3.069  3.636   15.053 1.00 30.20 ? 100 LEU   A C   1 
ATOM   750  O  O   . LEU   A 1 94  ? 2.579  2.990   14.132 1.00 29.57 ? 100 LEU   A O   1 
ATOM   751  C  CB  . LEU   A 1 94  ? 2.409  6.072   15.361 1.00 31.00 ? 100 LEU   A CB  1 
ATOM   752  C  CG  . LEU   A 1 94  ? 2.815  7.550   15.443 1.00 32.71 ? 100 LEU   A CG  1 
ATOM   753  C  CD1 . LEU   A 1 94  ? 1.675  8.412   15.936 1.00 33.42 ? 100 LEU   A CD1 1 
ATOM   754  C  CD2 . LEU   A 1 94  ? 3.940  7.754   16.383 1.00 33.06 ? 100 LEU   A CD2 1 
ATOM   755  N  N   . ALA   A 1 95  ? 3.267  3.137   16.276 1.00 30.00 ? 101 ALA   A N   1 
ATOM   756  C  CA  . ALA   A 1 95  ? 2.905  1.803   16.721 1.00 29.60 ? 101 ALA   A CA  1 
ATOM   757  C  C   . ALA   A 1 95  ? 2.347  1.852   18.133 1.00 29.46 ? 101 ALA   A C   1 
ATOM   758  O  O   . ALA   A 1 95  ? 2.639  2.743   18.915 1.00 28.89 ? 101 ALA   A O   1 
ATOM   759  C  CB  . ALA   A 1 95  ? 4.128  0.903   16.675 1.00 29.27 ? 101 ALA   A CB  1 
ATOM   760  N  N   . VAL   A 1 96  ? 1.511  0.905   18.450 1.00 30.58 ? 102 VAL   A N   1 
ATOM   761  C  CA  . VAL   A 1 96  ? 0.975  0.739   19.790 1.00 32.36 ? 102 VAL   A CA  1 
ATOM   762  C  C   . VAL   A 1 96  ? 2.091  -0.051  20.547 1.00 34.50 ? 102 VAL   A C   1 
ATOM   763  O  O   . VAL   A 1 96  ? 2.558  -1.108  20.083 1.00 34.31 ? 102 VAL   A O   1 
ATOM   764  C  CB  . VAL   A 1 96  ? -0.396 0.032   19.729 1.00 32.76 ? 102 VAL   A CB  1 
ATOM   765  C  CG1 . VAL   A 1 96  ? -0.890 -0.347  21.120 1.00 32.67 ? 102 VAL   A CG1 1 
ATOM   766  C  CG2 . VAL   A 1 96  ? -1.429 0.916   18.991 1.00 32.31 ? 102 VAL   A CG2 1 
ATOM   767  N  N   . GLY   A 1 97  ? 2.633  0.591   21.583 1.00 35.69 ? 103 GLY   A N   1 
ATOM   768  C  CA  . GLY   A 1 97  ? 3.740  0.060   22.355 1.00 37.11 ? 103 GLY   A CA  1 
ATOM   769  C  C   . GLY   A 1 97  ? 4.272  1.019   23.403 1.00 38.45 ? 103 GLY   A C   1 
ATOM   770  O  O   . GLY   A 1 97  ? 4.193  2.241   23.242 1.00 38.72 ? 103 GLY   A O   1 
ATOM   771  N  N   . HIS   A 1 98  ? 4.803  0.458   24.511 1.00 38.90 ? 104 HIS   A N   1 
ATOM   772  C  CA  . HIS   A 1 98  ? 5.400  1.259   25.564 1.00 39.31 ? 104 HIS   A CA  1 
ATOM   773  C  C   . HIS   A 1 98  ? 6.716  1.926   25.089 1.00 38.90 ? 104 HIS   A C   1 
ATOM   774  O  O   . HIS   A 1 98  ? 7.531  1.323   24.378 1.00 38.05 ? 104 HIS   A O   1 
ATOM   775  C  CB  . HIS   A 1 98  ? 5.660  0.408   26.812 1.00 40.57 ? 104 HIS   A CB  1 
ATOM   776  C  CG  . HIS   A 1 98  ? 6.429  1.134   27.871 1.00 43.75 ? 104 HIS   A CG  1 
ATOM   777  N  ND1 . HIS   A 1 98  ? 5.813  2.028   28.722 1.00 46.12 ? 104 HIS   A ND1 1 
ATOM   778  C  CD2 . HIS   A 1 98  ? 7.757  1.111   28.145 1.00 45.21 ? 104 HIS   A CD2 1 
ATOM   779  C  CE1 . HIS   A 1 98  ? 6.777  2.521   29.485 1.00 46.60 ? 104 HIS   A CE1 1 
ATOM   780  N  NE2 . HIS   A 1 98  ? 7.965  2.001   29.172 1.00 46.36 ? 104 HIS   A NE2 1 
ATOM   781  N  N   . SER   A 1 99  ? 6.918  3.163   25.544 1.00 38.73 ? 105 SER   A N   1 
ATOM   782  C  CA  . SER   A 1 99  ? 8.120  3.939   25.330 1.00 39.46 ? 105 SER   A CA  1 
ATOM   783  C  C   . SER   A 1 99  ? 8.191  5.073   26.352 1.00 41.17 ? 105 SER   A C   1 
ATOM   784  O  O   . SER   A 1 99  ? 7.176  5.532   26.863 1.00 40.83 ? 105 SER   A O   1 
ATOM   785  C  CB  . SER   A 1 99  ? 8.190  4.478   23.908 1.00 39.30 ? 105 SER   A CB  1 
ATOM   786  O  OG  . SER   A 1 99  ? 7.013  5.173   23.548 1.00 40.79 ? 105 SER   A OG  1 
ATOM   787  N  N   . GLU   A 1 100 ? 9.400  5.521   26.633 1.00 42.78 ? 106 GLU   A N   1 
ATOM   788  C  CA  . GLU   A 1 100 ? 9.708  6.604   27.566 1.00 44.79 ? 106 GLU   A CA  1 
ATOM   789  C  C   . GLU   A 1 100 ? 10.769 7.513   26.887 1.00 45.93 ? 106 GLU   A C   1 
ATOM   790  O  O   . GLU   A 1 100 ? 11.374 7.065   25.905 1.00 46.59 ? 106 GLU   A O   1 
ATOM   791  C  CB  . GLU   A 1 100 ? 10.207 6.002   28.888 1.00 48.63 ? 106 GLU   A CB  1 
ATOM   792  C  CG  . GLU   A 1 100 ? 9.198  6.119   30.029 1.00 55.99 ? 106 GLU   A CG  1 
ATOM   793  C  CD  . GLU   A 1 100 ? 9.381  5.130   31.172 1.00 60.88 ? 106 GLU   A CD  1 
ATOM   794  O  OE1 . GLU   A 1 100 ? 10.286 5.344   32.009 1.00 63.68 ? 106 GLU   A OE1 1 
ATOM   795  O  OE2 . GLU   A 1 100 ? 8.616  4.143   31.234 1.00 60.41 ? 106 GLU   A OE2 1 
ATOM   796  N  N   . PRO   A 1 101 ? 11.012 8.783   27.323 1.00 45.90 ? 107 PRO   A N   1 
ATOM   797  C  CA  . PRO   A 1 101 ? 11.975 9.643   26.588 1.00 45.05 ? 107 PRO   A CA  1 
ATOM   798  C  C   . PRO   A 1 101 ? 13.405 9.093   26.432 1.00 44.15 ? 107 PRO   A C   1 
ATOM   799  O  O   . PRO   A 1 101 ? 14.033 9.331   25.404 1.00 44.49 ? 107 PRO   A O   1 
ATOM   800  C  CB  . PRO   A 1 101 ? 11.944 10.962  27.352 1.00 45.91 ? 107 PRO   A CB  1 
ATOM   801  C  CG  . PRO   A 1 101 ? 10.633 10.966  28.086 1.00 46.68 ? 107 PRO   A CG  1 
ATOM   802  C  CD  . PRO   A 1 101 ? 10.371 9.522   28.435 1.00 45.51 ? 107 PRO   A CD  1 
ATOM   803  N  N   . GLY   A 1 102 ? 13.876 8.289   27.383 1.00 42.77 ? 108 GLY   A N   1 
ATOM   804  C  CA  . GLY   A 1 102 ? 15.182 7.638   27.257 1.00 41.35 ? 108 GLY   A CA  1 
ATOM   805  C  C   . GLY   A 1 102 ? 15.216 6.488   26.255 1.00 39.81 ? 108 GLY   A C   1 
ATOM   806  O  O   . GLY   A 1 102 ? 16.271 5.870   26.020 1.00 39.31 ? 108 GLY   A O   1 
ATOM   807  N  N   . ASP   A 1 103 ? 14.060 6.196   25.622 1.00 38.38 ? 109 ASP   A N   1 
ATOM   808  C  CA  . ASP   A 1 103 ? 13.975 5.103   24.665 1.00 36.54 ? 109 ASP   A CA  1 
ATOM   809  C  C   . ASP   A 1 103 ? 14.409 5.477   23.267 1.00 35.18 ? 109 ASP   A C   1 
ATOM   810  O  O   . ASP   A 1 103 ? 14.727 4.575   22.509 1.00 35.31 ? 109 ASP   A O   1 
ATOM   811  C  CB  . ASP   A 1 103 ? 12.593 4.461   24.672 1.00 36.86 ? 109 ASP   A CB  1 
ATOM   812  C  CG  . ASP   A 1 103 ? 12.447 3.529   25.856 1.00 38.71 ? 109 ASP   A CG  1 
ATOM   813  O  OD1 . ASP   A 1 103 ? 13.416 2.825   26.178 1.00 37.97 ? 109 ASP   A OD1 1 
ATOM   814  O  OD2 . ASP   A 1 103 ? 11.375 3.523   26.471 1.00 41.09 ? 109 ASP   A OD2 1 
ATOM   815  N  N   . CYS   A 1 104 ? 14.496 6.783   22.938 1.00 34.22 ? 110 CYS   A N   1 
ATOM   816  C  CA  . CYS   A 1 104 ? 15.007 7.292   21.657 1.00 33.91 ? 110 CYS   A CA  1 
ATOM   817  C  C   . CYS   A 1 104 ? 16.301 6.615   21.215 1.00 33.60 ? 110 CYS   A C   1 
ATOM   818  O  O   . CYS   A 1 104 ? 17.214 6.505   22.013 1.00 34.31 ? 110 CYS   A O   1 
ATOM   819  C  CB  . CYS   A 1 104 ? 15.180 8.805   21.725 1.00 34.20 ? 110 CYS   A CB  1 
ATOM   820  S  SG  . CYS   A 1 104 ? 13.618 9.708   21.730 1.00 37.48 ? 110 CYS   A SG  1 
ATOM   821  N  N   . GLY   A 1 105 ? 16.361 6.139   19.971 1.00 32.67 ? 111 GLY   A N   1 
ATOM   822  C  CA  . GLY   A 1 105 ? 17.558 5.468   19.477 1.00 32.23 ? 111 GLY   A CA  1 
ATOM   823  C  C   . GLY   A 1 105 ? 17.434 3.957   19.412 1.00 31.83 ? 111 GLY   A C   1 
ATOM   824  O  O   . GLY   A 1 105 ? 18.204 3.293   18.718 1.00 32.91 ? 111 GLY   A O   1 
ATOM   825  N  N   . GLY   A 1 106 ? 16.457 3.394   20.107 1.00 30.11 ? 112 GLY   A N   1 
ATOM   826  C  CA  . GLY   A 1 106 ? 16.171 1.963   20.043 1.00 28.41 ? 112 GLY   A CA  1 
ATOM   827  C  C   . GLY   A 1 106 ? 15.796 1.577   18.630 1.00 25.45 ? 112 GLY   A C   1 
ATOM   828  O  O   . GLY   A 1 106 ? 15.016 2.260   17.996 1.00 24.23 ? 112 GLY   A O   1 
ATOM   829  N  N   . ILE   A 1 107 ? 16.443 0.568   18.102 1.00 24.64 ? 113 ILE   A N   1 
ATOM   830  C  CA  . ILE   A 1 107 ? 16.246 0.122   16.744 1.00 24.95 ? 113 ILE   A CA  1 
ATOM   831  C  C   . ILE   A 1 107 ? 14.941 -0.653  16.526 1.00 25.30 ? 113 ILE   A C   1 
ATOM   832  O  O   . ILE   A 1 107 ? 14.554 -1.479  17.352 1.00 25.41 ? 113 ILE   A O   1 
ATOM   833  C  CB  . ILE   A 1 107 ? 17.517 -0.685  16.391 1.00 25.58 ? 113 ILE   A CB  1 
ATOM   834  C  CG1 . ILE   A 1 107 ? 18.648 0.270   15.979 1.00 25.82 ? 113 ILE   A CG1 1 
ATOM   835  C  CG2 . ILE   A 1 107 ? 17.284 -1.832  15.375 1.00 26.30 ? 113 ILE   A CG2 1 
ATOM   836  C  CD1 . ILE   A 1 107 ? 20.056 -0.312  16.095 1.00 25.90 ? 113 ILE   A CD1 1 
ATOM   837  N  N   . LEU   A 1 108 ? 14.239 -0.321  15.432 1.00 25.81 ? 114 LEU   A N   1 
ATOM   838  C  CA  . LEU   A 1 108 ? 13.090 -1.023  14.878 1.00 27.24 ? 114 LEU   A CA  1 
ATOM   839  C  C   . LEU   A 1 108 ? 13.656 -1.904  13.713 1.00 28.09 ? 114 LEU   A C   1 
ATOM   840  O  O   . LEU   A 1 108 ? 14.435 -1.425  12.902 1.00 27.74 ? 114 LEU   A O   1 
ATOM   841  C  CB  . LEU   A 1 108 ? 12.038 -0.036  14.352 1.00 27.82 ? 114 LEU   A CB  1 
ATOM   842  C  CG  . LEU   A 1 108 ? 10.805 -0.647  13.600 1.00 27.89 ? 114 LEU   A CG  1 
ATOM   843  C  CD1 . LEU   A 1 108 ? 9.915  -1.409  14.545 1.00 27.87 ? 114 LEU   A CD1 1 
ATOM   844  C  CD2 . LEU   A 1 108 ? 9.983  0.447   12.932 1.00 27.90 ? 114 LEU   A CD2 1 
ATOM   845  N  N   . ARG   A 1 109 ? 13.300 -3.189  13.674 1.00 28.83 ? 115 ARG   A N   1 
ATOM   846  C  CA  . ARG   A 1 109 ? 13.818 -4.132  12.691 1.00 29.83 ? 115 ARG   A CA  1 
ATOM   847  C  C   . ARG   A 1 109 ? 12.684 -5.039  12.203 1.00 31.70 ? 115 ARG   A C   1 
ATOM   848  O  O   . ARG   A 1 109 ? 11.759 -5.362  12.951 1.00 30.39 ? 115 ARG   A O   1 
ATOM   849  C  CB  . ARG   A 1 109 ? 14.880 -5.032  13.368 1.00 31.73 ? 115 ARG   A CB  1 
ATOM   850  C  CG  . ARG   A 1 109 ? 16.319 -4.919  12.874 1.00 37.17 ? 115 ARG   A CG  1 
ATOM   851  C  CD  . ARG   A 1 109 ? 17.224 -6.043  13.411 1.00 41.65 ? 115 ARG   A CD  1 
ATOM   852  N  NE  . ARG   A 1 109 ? 18.552 -6.053  12.773 1.00 45.32 ? 115 ARG   A NE  1 
ATOM   853  C  CZ  . ARG   A 1 109 ? 19.577 -5.293  13.170 1.00 50.30 ? 115 ARG   A CZ  1 
ATOM   854  N  NH1 . ARG   A 1 109 ? 20.744 -5.354  12.535 1.00 51.49 ? 115 ARG   A NH1 1 
ATOM   855  N  NH2 . ARG   A 1 109 ? 19.431 -4.440  14.182 1.00 50.73 ? 115 ARG   A NH2 1 
ATOM   856  N  N   . CYS   A 1 110 ? 12.773 -5.466  10.941 1.00 33.54 ? 116 CYS   A N   1 
ATOM   857  C  CA  . CYS   A 1 110 ? 11.891 -6.452  10.316 1.00 35.25 ? 116 CYS   A CA  1 
ATOM   858  C  C   . CYS   A 1 110 ? 12.822 -7.547  9.723  1.00 38.27 ? 116 CYS   A C   1 
ATOM   859  O  O   . CYS   A 1 110 ? 14.046 -7.474  9.915  1.00 38.99 ? 116 CYS   A O   1 
ATOM   860  C  CB  . CYS   A 1 110 ? 11.041 -5.792  9.238  1.00 35.73 ? 116 CYS   A CB  1 
ATOM   861  S  SG  . CYS   A 1 110 ? 12.006 -5.045  7.902  1.00 39.13 ? 116 CYS   A SG  1 
ATOM   862  N  N   . GLN   A 1 111 ? 12.275 -8.559  9.029  1.00 39.77 ? 117 GLN   A N   1 
ATOM   863  C  CA  . GLN   A 1 111 ? 13.102 -9.626  8.462  1.00 42.07 ? 117 GLN   A CA  1 
ATOM   864  C  C   . GLN   A 1 111 ? 14.166 -9.107  7.488  1.00 43.11 ? 117 GLN   A C   1 
ATOM   865  O  O   . GLN   A 1 111 ? 15.216 -9.745  7.340  1.00 43.61 ? 117 GLN   A O   1 
ATOM   866  C  CB  . GLN   A 1 111 ? 12.221 -10.679 7.754  1.00 45.38 ? 117 GLN   A CB  1 
ATOM   867  C  CG  . GLN   A 1 111 ? 11.220 -10.070 6.774  1.00 51.67 ? 117 GLN   A CG  1 
ATOM   868  C  CD  . GLN   A 1 111 ? 10.446 -11.078 5.949  1.00 59.28 ? 117 GLN   A CD  1 
ATOM   869  O  OE1 . GLN   A 1 111 ? 9.303  -10.816 5.532  1.00 61.87 ? 117 GLN   A OE1 1 
ATOM   870  N  NE2 . GLN   A 1 111 ? 11.051 -12.235 5.658  1.00 59.80 ? 117 GLN   A NE2 1 
ATOM   871  N  N   . HIS   A 1 112 ? 13.878 -7.954  6.826  1.00 42.57 ? 118 HIS   A N   1 
ATOM   872  C  CA  . HIS   A 1 112 ? 14.687 -7.293  5.792  1.00 42.17 ? 118 HIS   A CA  1 
ATOM   873  C  C   . HIS   A 1 112 ? 15.860 -6.487  6.315  1.00 40.84 ? 118 HIS   A C   1 
ATOM   874  O  O   . HIS   A 1 112 ? 16.768 -6.163  5.539  1.00 42.16 ? 118 HIS   A O   1 
ATOM   875  C  CB  . HIS   A 1 112 ? 13.796 -6.376  4.948  1.00 43.88 ? 118 HIS   A CB  1 
ATOM   876  C  CG  . HIS   A 1 112 ? 12.689 -7.094  4.248  1.00 48.70 ? 118 HIS   A CG  1 
ATOM   877  N  ND1 . HIS   A 1 112 ? 11.391 -7.021  4.697  1.00 51.56 ? 118 HIS   A ND1 1 
ATOM   878  C  CD2 . HIS   A 1 112 ? 12.727 -7.898  3.157  1.00 50.27 ? 118 HIS   A CD2 1 
ATOM   879  C  CE1 . HIS   A 1 112 ? 10.676 -7.778  3.874  1.00 51.67 ? 118 HIS   A CE1 1 
ATOM   880  N  NE2 . HIS   A 1 112 ? 11.437 -8.322  2.930  1.00 51.75 ? 118 HIS   A NE2 1 
ATOM   881  N  N   . GLY   A 1 113 ? 15.811 -6.090  7.582  1.00 38.15 ? 119 GLY   A N   1 
ATOM   882  C  CA  . GLY   A 1 113 ? 16.883 -5.293  8.158  1.00 36.07 ? 119 GLY   A CA  1 
ATOM   883  C  C   . GLY   A 1 113 ? 16.421 -4.216  9.104  1.00 33.59 ? 119 GLY   A C   1 
ATOM   884  O  O   . GLY   A 1 113 ? 15.388 -4.356  9.756  1.00 33.05 ? 119 GLY   A O   1 
ATOM   885  N  N   . VAL   A 1 114 ? 17.223 -3.152  9.223  1.00 32.08 ? 120 VAL   A N   1 
ATOM   886  C  CA  . VAL   A 1 114 ? 16.923 -2.023  10.081 1.00 31.58 ? 120 VAL   A CA  1 
ATOM   887  C  C   . VAL   A 1 114 ? 15.901 -1.089  9.403  1.00 30.84 ? 120 VAL   A C   1 
ATOM   888  O  O   . VAL   A 1 114 ? 16.125 -0.625  8.286  1.00 30.23 ? 120 VAL   A O   1 
ATOM   889  C  CB  . VAL   A 1 114 ? 18.207 -1.271  10.503 1.00 32.26 ? 120 VAL   A CB  1 
ATOM   890  C  CG1 . VAL   A 1 114 ? 17.860 0.071   11.163 1.00 33.05 ? 120 VAL   A CG1 1 
ATOM   891  C  CG2 . VAL   A 1 114 ? 19.057 -2.132  11.434 1.00 31.99 ? 120 VAL   A CG2 1 
ATOM   892  N  N   . VAL   A 1 115 ? 14.785 -0.832  10.083 1.00 30.05 ? 121 VAL   A N   1 
ATOM   893  C  CA  . VAL   A 1 115 ? 13.727 0.010   9.564  1.00 30.48 ? 121 VAL   A CA  1 
ATOM   894  C  C   . VAL   A 1 115 ? 13.909 1.486   9.992  1.00 31.60 ? 121 VAL   A C   1 
ATOM   895  O  O   . VAL   A 1 115 ? 13.736 2.415   9.202  1.00 32.14 ? 121 VAL   A O   1 
ATOM   896  C  CB  . VAL   A 1 115 ? 12.368 -0.544  10.052 1.00 30.54 ? 121 VAL   A CB  1 
ATOM   897  C  CG1 . VAL   A 1 115 ? 11.217 0.342   9.578  1.00 30.69 ? 121 VAL   A CG1 1 
ATOM   898  C  CG2 . VAL   A 1 115 ? 12.180 -2.002  9.625  1.00 30.43 ? 121 VAL   A CG2 1 
ATOM   899  N  N   . GLY   A 1 116 ? 14.203 1.678   11.260 1.00 31.18 ? 122 GLY   A N   1 
ATOM   900  C  CA  . GLY   A 1 116 ? 14.358 3.006   11.818 1.00 30.54 ? 122 GLY   A CA  1 
ATOM   901  C  C   . GLY   A 1 116 ? 14.634 2.938   13.295 1.00 29.54 ? 122 GLY   A C   1 
ATOM   902  O  O   . GLY   A 1 116 ? 14.970 1.861   13.827 1.00 28.98 ? 122 GLY   A O   1 
ATOM   903  N  N   . ILE   A 1 117 ? 14.576 4.121   13.952 1.00 28.01 ? 123 ILE   A N   1 
ATOM   904  C  CA  . ILE   A 1 117 ? 14.854 4.237   15.383 1.00 27.39 ? 123 ILE   A CA  1 
ATOM   905  C  C   . ILE   A 1 117 ? 13.785 5.045   16.115 1.00 26.51 ? 123 ILE   A C   1 
ATOM   906  O  O   . ILE   A 1 117 ? 13.288 6.023   15.546 1.00 26.70 ? 123 ILE   A O   1 
ATOM   907  C  CB  . ILE   A 1 117 ? 16.245 4.879   15.591 1.00 27.75 ? 123 ILE   A CB  1 
ATOM   908  C  CG1 . ILE   A 1 117 ? 16.384 6.213   14.870 1.00 28.81 ? 123 ILE   A CG1 1 
ATOM   909  C  CG2 . ILE   A 1 117 ? 17.389 3.929   15.233 1.00 27.42 ? 123 ILE   A CG2 1 
ATOM   910  C  CD1 . ILE   A 1 117 ? 17.363 7.139   15.621 1.00 30.75 ? 123 ILE   A CD1 1 
ATOM   911  N  N   . VAL   A 1 118 ? 13.464 4.680   17.397 1.00 25.50 ? 124 VAL   A N   1 
ATOM   912  C  CA  . VAL   A 1 118 ? 12.524 5.401   18.290 1.00 25.87 ? 124 VAL   A CA  1 
ATOM   913  C  C   . VAL   A 1 118 ? 12.914 6.886   18.324 1.00 27.10 ? 124 VAL   A C   1 
ATOM   914  O  O   . VAL   A 1 118 ? 14.085 7.228   18.468 1.00 25.55 ? 124 VAL   A O   1 
ATOM   915  C  CB  . VAL   A 1 118 ? 12.465 4.836   19.764 1.00 26.98 ? 124 VAL   A CB  1 
ATOM   916  C  CG1 . VAL   A 1 118 ? 11.419 5.569   20.611 1.00 27.29 ? 124 VAL   A CG1 1 
ATOM   917  C  CG2 . VAL   A 1 118 ? 12.201 3.339   19.784 1.00 28.04 ? 124 VAL   A CG2 1 
ATOM   918  N  N   . SER   A 1 119 ? 11.932 7.768   18.112 1.00 29.42 ? 125 SER   A N   1 
ATOM   919  C  CA  . SER   A 1 119 ? 12.165 9.189   18.068 1.00 31.28 ? 125 SER   A CA  1 
ATOM   920  C  C   . SER   A 1 119 ? 11.090 9.937   18.836 1.00 33.02 ? 125 SER   A C   1 
ATOM   921  O  O   . SER   A 1 119 ? 11.373 11.044  19.282 1.00 32.81 ? 125 SER   A O   1 
ATOM   922  C  CB  . SER   A 1 119 ? 12.299 9.666   16.621 1.00 33.89 ? 125 SER   A CB  1 
ATOM   923  O  OG  . SER   A 1 119 ? 11.746 10.955  16.398 1.00 38.17 ? 125 SER   A OG  1 
ATOM   924  N  N   . THR   A 1 120 ? 9.842  9.402   18.906 1.00 34.21 ? 126 THR   A N   1 
ATOM   925  C  CA  . THR   A 1 120 ? 8.738  9.996   19.692 1.00 36.45 ? 126 THR   A CA  1 
ATOM   926  C  C   . THR   A 1 120 ? 7.966  8.863   20.410 1.00 38.15 ? 126 THR   A C   1 
ATOM   927  O  O   . THR   A 1 120 ? 8.252  7.707   20.162 1.00 38.40 ? 126 THR   A O   1 
ATOM   928  C  CB  . THR   A 1 120 ? 7.814  11.024  18.910 1.00 37.93 ? 126 THR   A CB  1 
ATOM   929  O  OG1 . THR   A 1 120 ? 6.503  10.491  18.724 1.00 39.13 ? 126 THR   A OG1 1 
ATOM   930  C  CG2 . THR   A 1 120 ? 8.367  11.485  17.582 1.00 38.97 ? 126 THR   A CG2 1 
ATOM   931  N  N   . GLY   A 1 121 ? 6.992  9.199   21.254 1.00 39.83 ? 127 GLY   A N   1 
ATOM   932  C  CA  . GLY   A 1 121 ? 6.145  8.252   21.964 1.00 42.58 ? 127 GLY   A CA  1 
ATOM   933  C  C   . GLY   A 1 121 ? 5.266  8.926   23.005 1.00 45.58 ? 127 GLY   A C   1 
ATOM   934  O  O   . GLY   A 1 121 ? 5.320  10.148  23.170 1.00 46.49 ? 127 GLY   A O   1 
ATOM   935  N  N   . GLY   A 1 122 ? 4.473  8.139   23.731 1.00 47.19 ? 128 GLY   A N   1 
ATOM   936  C  CA  . GLY   A 1 122 ? 3.588  8.670   24.780 1.00 49.84 ? 128 GLY   A CA  1 
ATOM   937  C  C   . GLY   A 1 122 ? 2.153  8.178   24.660 1.00 52.25 ? 128 GLY   A C   1 
ATOM   938  O  O   . GLY   A 1 122 ? 1.721  7.831   23.562 1.00 53.28 ? 128 GLY   A O   1 
ATOM   939  N  N   . ASN   A 1 123 ? 1.401  8.116   25.764 1.00 53.20 ? 129 ASN   A N   1 
ATOM   940  C  CA  . ASN   A 1 123 ? -0.004 7.665   25.741 1.00 53.44 ? 129 ASN   A CA  1 
ATOM   941  C  C   . ASN   A 1 123 ? -0.235 6.230   25.220 1.00 52.09 ? 129 ASN   A C   1 
ATOM   942  O  O   . ASN   A 1 123 ? -1.325 5.939   24.725 1.00 53.36 ? 129 ASN   A O   1 
ATOM   943  C  CB  . ASN   A 1 123 ? -0.849 8.635   24.925 1.00 55.92 ? 129 ASN   A CB  1 
ATOM   944  C  CG  . ASN   A 1 123 ? -1.008 9.947   25.615 1.00 61.42 ? 129 ASN   A CG  1 
ATOM   945  O  OD1 . ASN   A 1 123 ? -1.264 9.986   26.827 1.00 63.44 ? 129 ASN   A OD1 1 
ATOM   946  N  ND2 . ASN   A 1 123 ? -0.866 11.047  24.856 1.00 61.86 ? 129 ASN   A ND2 1 
ATOM   947  N  N   . GLY   A 1 124 ? 0.761  5.360   25.330 1.00 49.03 ? 130 GLY   A N   1 
ATOM   948  C  CA  . GLY   A 1 124 ? 0.634  4.004   24.817 1.00 46.79 ? 130 GLY   A CA  1 
ATOM   949  C  C   . GLY   A 1 124 ? 0.977  3.894   23.341 1.00 44.97 ? 130 GLY   A C   1 
ATOM   950  O  O   . GLY   A 1 124 ? 0.592  2.913   22.705 1.00 46.11 ? 130 GLY   A O   1 
ATOM   951  N  N   . LEU   A 1 125 ? 1.703  4.889   22.772 1.00 42.17 ? 131 LEU   A N   1 
ATOM   952  C  CA  . LEU   A 1 125 ? 2.165  4.859   21.383 1.00 41.25 ? 131 LEU   A CA  1 
ATOM   953  C  C   . LEU   A 1 125 ? 3.702  4.976   21.319 1.00 39.55 ? 131 LEU   A C   1 
ATOM   954  O  O   . LEU   A 1 125 ? 4.313  5.461   22.255 1.00 40.65 ? 131 LEU   A O   1 
ATOM   955  C  CB  . LEU   A 1 125 ? 1.599  6.021   20.526 1.00 41.47 ? 131 LEU   A CB  1 
ATOM   956  C  CG  . LEU   A 1 125 ? 0.141  6.408   20.643 1.00 43.18 ? 131 LEU   A CG  1 
ATOM   957  C  CD1 . LEU   A 1 125 ? -0.119 7.609   19.792 1.00 43.35 ? 131 LEU   A CD1 1 
ATOM   958  C  CD2 . LEU   A 1 125 ? -0.760 5.271   20.215 1.00 44.35 ? 131 LEU   A CD2 1 
ATOM   959  N  N   . VAL   A 1 126 ? 4.313  4.621   20.184 1.00 36.95 ? 132 VAL   A N   1 
ATOM   960  C  CA  . VAL   A 1 126 ? 5.745  4.787   19.973 1.00 34.74 ? 132 VAL   A CA  1 
ATOM   961  C  C   . VAL   A 1 126 ? 5.954  5.210   18.527 1.00 33.46 ? 132 VAL   A C   1 
ATOM   962  O  O   . VAL   A 1 126 ? 5.389  4.591   17.621 1.00 34.00 ? 132 VAL   A O   1 
ATOM   963  C  CB  . VAL   A 1 126 ? 6.620  3.540   20.412 1.00 34.12 ? 132 VAL   A CB  1 
ATOM   964  C  CG1 . VAL   A 1 126 ? 6.024  2.212   19.950 1.00 33.93 ? 132 VAL   A CG1 1 
ATOM   965  C  CG2 . VAL   A 1 126 ? 8.083  3.678   19.988 1.00 33.30 ? 132 VAL   A CG2 1 
ATOM   966  N  N   . GLY   A 1 127 ? 6.725  6.278   18.318 1.00 31.59 ? 133 GLY   A N   1 
ATOM   967  C  CA  . GLY   A 1 127 ? 7.037  6.793   16.990 1.00 31.07 ? 133 GLY   A CA  1 
ATOM   968  C  C   . GLY   A 1 127 ? 8.467  6.542   16.564 1.00 30.15 ? 133 GLY   A C   1 
ATOM   969  O  O   . GLY   A 1 127 ? 9.383  6.818   17.324 1.00 30.09 ? 133 GLY   A O   1 
ATOM   970  N  N   . PHE   A 1 128 ? 8.664  6.009   15.349 1.00 29.49 ? 134 PHE   A N   1 
ATOM   971  C  CA  . PHE   A 1 128 ? 9.975  5.681   14.779 1.00 28.76 ? 134 PHE   A CA  1 
ATOM   972  C  C   . PHE   A 1 128 ? 10.330 6.541   13.516 1.00 28.56 ? 134 PHE   A C   1 
ATOM   973  O  O   . PHE   A 1 128 ? 9.569  6.605   12.566 1.00 28.33 ? 134 PHE   A O   1 
ATOM   974  C  CB  . PHE   A 1 128 ? 10.043 4.176   14.397 1.00 27.46 ? 134 PHE   A CB  1 
ATOM   975  C  CG  . PHE   A 1 128 ? 9.596  3.163   15.431 1.00 26.85 ? 134 PHE   A CG  1 
ATOM   976  C  CD1 . PHE   A 1 128 ? 10.490 2.658   16.368 1.00 26.24 ? 134 PHE   A CD1 1 
ATOM   977  C  CD2 . PHE   A 1 128 ? 8.309  2.640   15.406 1.00 27.48 ? 134 PHE   A CD2 1 
ATOM   978  C  CE1 . PHE   A 1 128 ? 10.083 1.701   17.302 1.00 26.02 ? 134 PHE   A CE1 1 
ATOM   979  C  CE2 . PHE   A 1 128 ? 7.917  1.653   16.323 1.00 27.16 ? 134 PHE   A CE2 1 
ATOM   980  C  CZ  . PHE   A 1 128 ? 8.813  1.185   17.264 1.00 25.50 ? 134 PHE   A CZ  1 
ATOM   981  N  N   . ALA   A 1 129 ? 11.519 7.139   13.506 1.00 28.45 ? 135 ALA   A N   1 
ATOM   982  C  CA  . ALA   A 1 129 ? 12.014 7.887   12.376 1.00 29.06 ? 135 ALA   A CA  1 
ATOM   983  C  C   . ALA   A 1 129 ? 12.514 6.874   11.354 1.00 30.78 ? 135 ALA   A C   1 
ATOM   984  O  O   . ALA   A 1 129 ? 13.445 6.135   11.635 1.00 31.32 ? 135 ALA   A O   1 
ATOM   985  C  CB  . ALA   A 1 129 ? 13.166 8.774   12.827 1.00 29.16 ? 135 ALA   A CB  1 
ATOM   986  N  N   . ASP   A 1 130 ? 11.871 6.789   10.201 1.00 31.66 ? 136 ASP   A N   1 
ATOM   987  C  CA  . ASP   A 1 130 ? 12.240 5.845   9.144  1.00 32.46 ? 136 ASP   A CA  1 
ATOM   988  C  C   . ASP   A 1 130 ? 13.542 6.219   8.453  1.00 32.31 ? 136 ASP   A C   1 
ATOM   989  O  O   . ASP   A 1 130 ? 13.853 7.407   8.350  1.00 33.30 ? 136 ASP   A O   1 
ATOM   990  C  CB  . ASP   A 1 130 ? 11.138 5.836   8.110  1.00 34.99 ? 136 ASP   A CB  1 
ATOM   991  C  CG  . ASP   A 1 130 ? 11.225 4.696   7.150  1.00 42.23 ? 136 ASP   A CG  1 
ATOM   992  O  OD1 . ASP   A 1 130 ? 11.379 3.557   7.605  1.00 43.71 ? 136 ASP   A OD1 1 
ATOM   993  O  OD2 . ASP   A 1 130 ? 11.112 4.942   5.931  1.00 46.80 ? 136 ASP   A OD2 1 
ATOM   994  N  N   . VAL   A 1 131 ? 14.324 5.206   8.002  1.00 31.22 ? 137 VAL   A N   1 
ATOM   995  C  CA  . VAL   A 1 131 ? 15.605 5.387   7.280  1.00 30.48 ? 137 VAL   A CA  1 
ATOM   996  C  C   . VAL   A 1 131 ? 15.682 4.489   5.971  1.00 30.96 ? 137 VAL   A C   1 
ATOM   997  O  O   . VAL   A 1 131 ? 16.733 4.433   5.290  1.00 31.05 ? 137 VAL   A O   1 
ATOM   998  C  CB  . VAL   A 1 131 ? 16.811 5.099   8.208  1.00 29.97 ? 137 VAL   A CB  1 
ATOM   999  C  CG1 . VAL   A 1 131 ? 16.731 5.893   9.513  1.00 30.06 ? 137 VAL   A CG1 1 
ATOM   1000 C  CG2 . VAL   A 1 131 ? 16.969 3.594   8.493  1.00 29.53 ? 137 VAL   A CG2 1 
ATOM   1001 N  N   . ARG   A 1 132 ? 14.588 3.810   5.618  1.00 31.01 ? 138 ARG   A N   1 
ATOM   1002 C  CA  . ARG   A 1 132 ? 14.603 2.925   4.436  1.00 33.20 ? 138 ARG   A CA  1 
ATOM   1003 C  C   . ARG   A 1 132 ? 14.709 3.664   3.104  1.00 35.52 ? 138 ARG   A C   1 
ATOM   1004 O  O   . ARG   A 1 132 ? 15.208 3.086   2.158  1.00 36.76 ? 138 ARG   A O   1 
ATOM   1005 C  CB  . ARG   A 1 132 ? 13.430 1.961   4.426  1.00 33.23 ? 138 ARG   A CB  1 
ATOM   1006 C  CG  . ARG   A 1 132 ? 13.475 1.077   5.645  1.00 33.25 ? 138 ARG   A CG  1 
ATOM   1007 C  CD  . ARG   A 1 132 ? 12.221 0.286   5.742  1.00 33.43 ? 138 ARG   A CD  1 
ATOM   1008 N  NE  . ARG   A 1 132 ? 11.096 1.104   6.195  1.00 33.80 ? 138 ARG   A NE  1 
ATOM   1009 C  CZ  . ARG   A 1 132 ? 9.835  0.683   6.198  1.00 34.28 ? 138 ARG   A CZ  1 
ATOM   1010 N  NH1 . ARG   A 1 132 ? 9.535  -0.532  5.764  1.00 35.89 ? 138 ARG   A NH1 1 
ATOM   1011 N  NH2 . ARG   A 1 132 ? 8.860  1.483   6.619  1.00 31.88 ? 138 ARG   A NH2 1 
ATOM   1012 N  N   . ASP   A 1 133 ? 14.328 4.938   3.055  1.00 36.14 ? 139 ASP   A N   1 
ATOM   1013 C  CA  . ASP   A 1 133 ? 14.416 5.781   1.866  1.00 36.87 ? 139 ASP   A CA  1 
ATOM   1014 C  C   . ASP   A 1 133 ? 15.822 6.327   1.626  1.00 37.84 ? 139 ASP   A C   1 
ATOM   1015 O  O   . ASP   A 1 133 ? 16.111 6.754   0.498  1.00 37.47 ? 139 ASP   A O   1 
ATOM   1016 C  CB  . ASP   A 1 133 ? 13.450 6.966   1.988  1.00 38.36 ? 139 ASP   A CB  1 
ATOM   1017 C  CG  . ASP   A 1 133 ? 13.762 7.921   3.136  1.00 43.38 ? 139 ASP   A CG  1 
ATOM   1018 O  OD1 . ASP   A 1 133 ? 13.963 7.438   4.289  1.00 42.91 ? 139 ASP   A OD1 1 
ATOM   1019 O  OD2 . ASP   A 1 133 ? 13.769 9.145   2.898  1.00 46.09 ? 139 ASP   A OD2 1 
ATOM   1020 N  N   . LEU   A 1 134 ? 16.684 6.364   2.672  1.00 38.92 ? 140 LEU   A N   1 
ATOM   1021 C  CA  . LEU   A 1 134 ? 18.055 6.923   2.567  1.00 40.31 ? 140 LEU   A CA  1 
ATOM   1022 C  C   . LEU   A 1 134 ? 18.985 5.939   1.885  1.00 42.04 ? 140 LEU   A C   1 
ATOM   1023 O  O   . LEU   A 1 134 ? 19.800 5.295   2.544  1.00 42.02 ? 140 LEU   A O   1 
ATOM   1024 C  CB  . LEU   A 1 134 ? 18.605 7.312   3.958  1.00 40.31 ? 140 LEU   A CB  1 
ATOM   1025 C  CG  . LEU   A 1 134 ? 17.682 8.141   4.837  1.00 40.87 ? 140 LEU   A CG  1 
ATOM   1026 C  CD1 . LEU   A 1 134 ? 18.274 8.333   6.205  1.00 40.60 ? 140 LEU   A CD1 1 
ATOM   1027 C  CD2 . LEU   A 1 134 ? 17.329 9.457   4.163  1.00 41.39 ? 140 LEU   A CD2 1 
ATOM   1028 N  N   . LEU   A 1 135 ? 18.859 5.817   0.558  1.00 43.39 ? 141 LEU   A N   1 
ATOM   1029 C  CA  . LEU   A 1 135 ? 19.607 4.832   -0.221 1.00 45.67 ? 141 LEU   A CA  1 
ATOM   1030 C  C   . LEU   A 1 135 ? 21.139 5.072   -0.250 1.00 47.82 ? 141 LEU   A C   1 
ATOM   1031 O  O   . LEU   A 1 135 ? 21.887 4.107   -0.422 1.00 47.79 ? 141 LEU   A O   1 
ATOM   1032 C  CB  . LEU   A 1 135 ? 19.030 4.711   -1.653 1.00 45.99 ? 141 LEU   A CB  1 
ATOM   1033 C  CG  . LEU   A 1 135 ? 17.482 4.657   -1.784 1.00 47.59 ? 141 LEU   A CG  1 
ATOM   1034 C  CD1 . LEU   A 1 135 ? 17.073 4.388   -3.199 1.00 48.18 ? 141 LEU   A CD1 1 
ATOM   1035 C  CD2 . LEU   A 1 135 ? 16.859 3.583   -0.887 1.00 47.97 ? 141 LEU   A CD2 1 
ATOM   1036 N  N   . TRP   A 1 136 ? 21.599 6.323   0.009  1.00 48.85 ? 142 TRP   A N   1 
ATOM   1037 C  CA  . TRP   A 1 136 ? 23.027 6.674   0.023  1.00 50.88 ? 142 TRP   A CA  1 
ATOM   1038 C  C   . TRP   A 1 136 ? 23.825 6.068   1.187  1.00 52.94 ? 142 TRP   A C   1 
ATOM   1039 O  O   . TRP   A 1 136 ? 25.059 6.107   1.160  1.00 53.28 ? 142 TRP   A O   1 
ATOM   1040 C  CB  . TRP   A 1 136 ? 23.233 8.193   -0.020 1.00 50.97 ? 142 TRP   A CB  1 
ATOM   1041 C  CG  . TRP   A 1 136 ? 22.490 8.943   1.053  1.00 51.69 ? 142 TRP   A CG  1 
ATOM   1042 C  CD1 . TRP   A 1 136 ? 21.219 9.430   0.982  1.00 52.44 ? 142 TRP   A CD1 1 
ATOM   1043 C  CD2 . TRP   A 1 136 ? 22.979 9.284   2.357  1.00 52.05 ? 142 TRP   A CD2 1 
ATOM   1044 N  NE1 . TRP   A 1 136 ? 20.887 10.056  2.162  1.00 52.86 ? 142 TRP   A NE1 1 
ATOM   1045 C  CE2 . TRP   A 1 136 ? 21.951 9.986   3.020  1.00 52.67 ? 142 TRP   A CE2 1 
ATOM   1046 C  CE3 . TRP   A 1 136 ? 24.199 9.101   3.014  1.00 53.03 ? 142 TRP   A CE3 1 
ATOM   1047 C  CZ2 . TRP   A 1 136 ? 22.093 10.466  4.318  1.00 53.63 ? 142 TRP   A CZ2 1 
ATOM   1048 C  CZ3 . TRP   A 1 136 ? 24.345 9.594   4.296  1.00 54.09 ? 142 TRP   A CZ3 1 
ATOM   1049 C  CH2 . TRP   A 1 136 ? 23.305 10.279  4.930  1.00 54.11 ? 142 TRP   A CH2 1 
ATOM   1050 N  N   . LEU   A 1 137 ? 23.134 5.524   2.202  1.00 54.03 ? 143 LEU   A N   1 
ATOM   1051 C  CA  . LEU   A 1 137 ? 23.768 4.859   3.343  1.00 56.14 ? 143 LEU   A CA  1 
ATOM   1052 C  C   . LEU   A 1 137 ? 24.513 3.579   2.918  1.00 59.94 ? 143 LEU   A C   1 
ATOM   1053 O  O   . LEU   A 1 137 ? 25.424 3.149   3.625  1.00 60.34 ? 143 LEU   A O   1 
ATOM   1054 C  CB  . LEU   A 1 137 ? 22.708 4.490   4.400  1.00 55.45 ? 143 LEU   A CB  1 
ATOM   1055 C  CG  . LEU   A 1 137 ? 21.939 5.634   5.074  1.00 55.45 ? 143 LEU   A CG  1 
ATOM   1056 C  CD1 . LEU   A 1 137 ? 20.928 5.086   6.081  1.00 55.48 ? 143 LEU   A CD1 1 
ATOM   1057 C  CD2 . LEU   A 1 137 ? 22.873 6.590   5.774  1.00 55.26 ? 143 LEU   A CD2 1 
ATOM   1058 N  N   . ASP   A 1 138 ? 24.104 2.948   1.791  1.00 62.45 ? 144 ASP   A N   1 
ATOM   1059 C  CA  . ASP   A 1 138 ? 24.727 1.728   1.269  1.00 65.52 ? 144 ASP   A CA  1 
ATOM   1060 C  C   . ASP   A 1 138 ? 25.686 1.974   0.119  1.00 68.33 ? 144 ASP   A C   1 
ATOM   1061 O  O   . ASP   A 1 138 ? 26.072 1.004   -0.530 1.00 69.02 ? 144 ASP   A O   1 
ATOM   1062 C  CB  . ASP   A 1 138 ? 23.653 0.764   0.748  1.00 68.38 ? 144 ASP   A CB  1 
ATOM   1063 C  CG  . ASP   A 1 138 ? 22.719 0.249   1.808  1.00 74.10 ? 144 ASP   A CG  1 
ATOM   1064 O  OD1 . ASP   A 1 138 ? 23.174 0.068   2.957  1.00 75.40 ? 144 ASP   A OD1 1 
ATOM   1065 O  OD2 . ASP   A 1 138 ? 21.528 0.019   1.489  1.00 76.20 ? 144 ASP   A OD2 1 
ATOM   1066 N  N   . GLU   A 1 139 ? 26.050 3.236   -0.177 1.00 69.94 ? 145 GLU   A N   1 
ATOM   1067 C  CA  . GLU   A 1 139 ? 26.926 3.511   -1.316 1.00 72.02 ? 145 GLU   A CA  1 
ATOM   1068 C  C   . GLU   A 1 139 ? 27.917 4.651   -1.101 1.00 73.01 ? 145 GLU   A C   1 
ATOM   1069 O  O   . GLU   A 1 139 ? 28.596 5.077   -2.045 1.00 73.54 ? 145 GLU   A O   1 
ATOM   1070 C  CB  . GLU   A 1 139 ? 26.079 3.761   -2.572 1.00 76.00 ? 145 GLU   A CB  1 
ATOM   1071 C  CG  . GLU   A 1 139 ? 25.005 4.828   -2.407 1.00 82.31 ? 145 GLU   A CG  1 
ATOM   1072 C  CD  . GLU   A 1 139 ? 23.956 4.814   -3.505 1.00 89.90 ? 145 GLU   A CD  1 
ATOM   1073 O  OE1 . GLU   A 1 139 ? 23.338 5.877   -3.753 1.00 90.52 ? 145 GLU   A OE1 1 
ATOM   1074 O  OE2 . GLU   A 1 139 ? 23.755 3.738   -4.121 1.00 92.81 ? 145 GLU   A OE2 1 
HETATM 1075 N  N1  . A1B4L B 2 .   ? 10.024 13.843  22.461 1.00 54.56 ? 201 A1B4L A N1  1 
HETATM 1076 C  C4  . A1B4L B 2 .   ? 11.034 14.582  23.233 1.00 54.53 ? 201 A1B4L A C4  1 
HETATM 1077 C  C5  . A1B4L B 2 .   ? 9.313  12.787  22.910 1.00 54.12 ? 201 A1B4L A C5  1 
HETATM 1078 C  C6  . A1B4L B 2 .   ? 9.440  12.448  24.382 1.00 53.76 ? 201 A1B4L A C6  1 
HETATM 1079 C  C7  . A1B4L B 2 .   ? 8.854  11.090  24.692 1.00 53.33 ? 201 A1B4L A C7  1 
HETATM 1080 C  C8  . A1B4L B 2 .   ? 7.802  10.948  25.594 1.00 53.26 ? 201 A1B4L A C8  1 
HETATM 1081 C  C10 . A1B4L B 2 .   ? 7.784  8.561   25.243 1.00 52.95 ? 201 A1B4L A C10 1 
HETATM 1082 C  C13 . A1B4L B 2 .   ? 10.516 8.551   22.865 1.00 52.34 ? 201 A1B4L A C13 1 
HETATM 1083 C  C15 . A1B4L B 2 .   ? 9.848  14.345  21.096 1.00 54.36 ? 201 A1B4L A C15 1 
HETATM 1084 O  O1  . A1B4L B 2 .   ? 8.591  12.134  22.175 1.00 54.01 ? 201 A1B4L A O1  1 
HETATM 1085 C  C3  . A1B4L B 2 .   ? 12.375 14.573  22.509 1.00 54.49 ? 201 A1B4L A C3  1 
HETATM 1086 C  C2  . A1B4L B 2 .   ? 12.219 15.006  21.047 1.00 54.43 ? 201 A1B4L A C2  1 
HETATM 1087 C  C1  . A1B4L B 2 .   ? 11.157 14.171  20.322 1.00 54.13 ? 201 A1B4L A C1  1 
HETATM 1088 C  C   . A1B4L B 2 .   ? 11.012 14.588  18.869 1.00 53.69 ? 201 A1B4L A C   1 
HETATM 1089 O  O   . A1B4L B 2 .   ? 10.740 15.751  18.562 1.00 53.39 ? 201 A1B4L A O   1 
HETATM 1090 N  N   . A1B4L B 2 .   ? 11.171 13.627  17.974 1.00 53.58 ? 201 A1B4L A N   1 
HETATM 1091 C  C14 . A1B4L B 2 .   ? 9.340  9.933   24.087 1.00 52.80 ? 201 A1B4L A C14 1 
HETATM 1092 O  O2  . A1B4L B 2 .   ? 10.378 9.884   23.192 1.00 52.27 ? 201 A1B4L A O2  1 
HETATM 1093 C  C12 . A1B4L B 2 .   ? 9.626  7.782   23.493 1.00 52.60 ? 201 A1B4L A C12 1 
HETATM 1094 C  C11 . A1B4L B 2 .   ? 8.834  8.654   24.320 1.00 52.78 ? 201 A1B4L A C11 1 
HETATM 1095 C  C9  . A1B4L B 2 .   ? 7.278  9.694   25.871 1.00 53.16 ? 201 A1B4L A C9  1 
HETATM 1096 ZN ZN  . ZN    C 3 .   ? 11.208 -5.425  5.749  1.00 42.18 2 202 ZN    A ZN  1 
HETATM 1097 O  O   . HOH   D 4 .   ? 0.906  -1.157  16.573 1.00 34.09 ? 301 HOH   A O   1 
HETATM 1098 O  O   . HOH   D 4 .   ? 11.686 1.498   33.412 1.00 53.66 ? 302 HOH   A O   1 
HETATM 1099 O  O   . HOH   D 4 .   ? 10.749 7.129   4.843  1.00 41.07 ? 303 HOH   A O   1 
HETATM 1100 O  O   . HOH   D 4 .   ? 20.220 8.344   18.998 1.00 26.09 ? 304 HOH   A O   1 
HETATM 1101 O  O   . HOH   D 4 .   ? 22.556 -1.997  4.351  1.00 35.27 ? 305 HOH   A O   1 
HETATM 1102 O  O   . HOH   D 4 .   ? 9.813  17.795  19.824 1.00 40.47 ? 306 HOH   A O   1 
HETATM 1103 O  O   . HOH   D 4 .   ? 23.864 21.305  8.014  1.00 57.50 ? 307 HOH   A O   1 
HETATM 1104 O  O   . HOH   D 4 .   ? 8.236  -4.941  1.348  1.00 59.90 ? 308 HOH   A O   1 
HETATM 1105 O  O   . HOH   D 4 .   ? 2.695  -5.689  20.521 1.00 43.65 ? 309 HOH   A O   1 
HETATM 1106 O  O   . HOH   D 4 .   ? 8.398  19.326  18.132 1.00 51.44 ? 310 HOH   A O   1 
HETATM 1107 O  O   . HOH   D 4 .   ? 10.498 4.005   3.494  1.00 34.88 ? 311 HOH   A O   1 
HETATM 1108 O  O   . HOH   D 4 .   ? 14.556 1.866   23.349 1.00 42.78 ? 312 HOH   A O   1 
HETATM 1109 O  O   . HOH   D 4 .   ? 4.121  5.148   24.912 1.00 52.84 ? 313 HOH   A O   1 
HETATM 1110 O  O   . HOH   D 4 .   ? 6.194  0.711   5.809  1.00 36.19 ? 314 HOH   A O   1 
HETATM 1111 O  O   . HOH   D 4 .   ? 6.615  -6.329  29.459 1.00 35.96 ? 315 HOH   A O   1 
HETATM 1112 O  O   . HOH   D 4 .   ? 6.967  2.662   33.343 1.00 45.86 ? 316 HOH   A O   1 
HETATM 1113 O  O   . HOH   D 4 .   ? 17.637 20.471  9.769  1.00 49.65 ? 317 HOH   A O   1 
HETATM 1114 O  O   . HOH   D 4 .   ? 11.141 10.925  11.414 1.00 24.07 ? 318 HOH   A O   1 
HETATM 1115 O  O   . HOH   D 4 .   ? 2.121  9.802   21.585 1.00 54.25 ? 319 HOH   A O   1 
HETATM 1116 O  O   . HOH   D 4 .   ? 18.150 18.333  16.922 1.00 36.48 ? 320 HOH   A O   1 
HETATM 1117 O  O   . HOH   D 4 .   ? 29.981 3.984   3.951  1.00 47.40 ? 321 HOH   A O   1 
HETATM 1118 O  O   . HOH   D 4 .   ? 13.947 20.345  8.215  1.00 42.12 ? 322 HOH   A O   1 
HETATM 1119 O  O   . HOH   D 4 .   ? 35.208 7.687   7.167  1.00 50.47 ? 323 HOH   A O   1 
HETATM 1120 O  O   . HOH   D 4 .   ? 12.999 9.897   9.502  1.00 31.69 ? 324 HOH   A O   1 
HETATM 1121 O  O   . HOH   D 4 .   ? 19.925 22.379  7.640  1.00 38.08 ? 325 HOH   A O   1 
HETATM 1122 O  O   . HOH   D 4 .   ? 14.739 11.989  24.103 1.00 36.24 ? 326 HOH   A O   1 
HETATM 1123 O  O   . HOH   D 4 .   ? 11.710 20.526  12.388 1.00 29.28 ? 327 HOH   A O   1 
HETATM 1124 O  O   . HOH   D 4 .   ? 11.052 16.348  5.270  1.00 56.21 ? 328 HOH   A O   1 
HETATM 1125 O  O   . HOH   D 4 .   ? 29.675 10.516  19.903 1.00 46.35 ? 329 HOH   A O   1 
HETATM 1126 O  O   . HOH   D 4 .   ? 5.093  -2.437  24.691 1.00 39.70 ? 330 HOH   A O   1 
HETATM 1127 O  O   . HOH   D 4 .   ? 8.410  1.904   3.221  1.00 40.24 ? 331 HOH   A O   1 
HETATM 1128 O  O   . HOH   D 4 .   ? 19.806 23.214  15.351 1.00 29.91 ? 332 HOH   A O   1 
HETATM 1129 O  O   . HOH   D 4 .   ? 3.703  11.486  19.037 1.00 41.36 ? 333 HOH   A O   1 
HETATM 1130 O  O   . HOH   D 4 .   ? 4.268  -6.038  6.373  1.00 41.09 ? 334 HOH   A O   1 
HETATM 1131 O  O   . HOH   D 4 .   ? 9.035  20.551  10.303 1.00 44.20 ? 335 HOH   A O   1 
HETATM 1132 O  O   . HOH   D 4 .   ? 14.030 13.960  3.671  1.00 42.23 ? 336 HOH   A O   1 
HETATM 1133 O  O   . HOH   D 4 .   ? 9.120  -8.710  9.306  1.00 50.60 ? 337 HOH   A O   1 
HETATM 1134 O  O   . HOH   D 4 .   ? 22.014 18.625  5.988  1.00 35.02 ? 338 HOH   A O   1 
HETATM 1135 O  O   . HOH   D 4 .   ? 13.222 -6.733  32.440 1.00 42.25 ? 339 HOH   A O   1 
HETATM 1136 O  O   . HOH   D 4 .   ? 1.495  -3.381  18.132 1.00 35.78 ? 340 HOH   A O   1 
HETATM 1137 O  O   . HOH   D 4 .   ? 15.066 -5.213  17.183 1.00 38.44 ? 341 HOH   A O   1 
HETATM 1138 O  O   . HOH   D 4 .   ? 17.082 2.379   23.410 1.00 38.38 ? 342 HOH   A O   1 
HETATM 1139 O  O   . HOH   D 4 .   ? 18.207 18.879  27.734 1.00 47.53 ? 343 HOH   A O   1 
HETATM 1140 O  O   . HOH   D 4 .   ? 1.697  12.762  5.545  1.00 56.81 ? 344 HOH   A O   1 
HETATM 1141 O  O   . HOH   D 4 .   ? 18.170 11.947  1.911  1.00 39.80 ? 345 HOH   A O   1 
HETATM 1142 O  O   . HOH   D 4 .   ? 22.206 18.098  19.424 1.00 38.91 ? 346 HOH   A O   1 
HETATM 1143 O  O   . HOH   D 4 .   ? 9.670  2.420   34.419 1.00 74.33 ? 347 HOH   A O   1 
HETATM 1144 O  O   . HOH   D 4 .   ? 14.438 -5.469  34.527 1.00 41.05 ? 348 HOH   A O   1 
HETATM 1145 O  O   . HOH   D 4 .   ? 14.991 13.108  26.514 1.00 51.07 ? 349 HOH   A O   1 
HETATM 1146 O  O   . HOH   D 4 .   ? 28.980 21.599  18.562 1.00 43.05 ? 350 HOH   A O   1 
HETATM 1147 O  O   . HOH   D 4 .   ? 24.236 6.851   21.351 1.00 44.64 ? 351 HOH   A O   1 
HETATM 1148 O  O   . HOH   D 4 .   ? 4.767  -2.546  29.118 1.00 53.86 ? 352 HOH   A O   1 
HETATM 1149 O  O   . HOH   D 4 .   ? 0.891  0.174   24.878 1.00 45.09 ? 353 HOH   A O   1 
HETATM 1150 O  O   . HOH   D 4 .   ? 21.787 8.514   21.004 1.00 34.73 ? 354 HOH   A O   1 
HETATM 1151 O  O   . HOH   D 4 .   ? -1.331 1.379   5.355  1.00 66.68 ? 355 HOH   A O   1 
HETATM 1152 O  O   . HOH   D 4 .   ? 2.379  2.358   27.856 1.00 39.98 ? 356 HOH   A O   1 
HETATM 1153 O  O   . HOH   D 4 .   ? 21.218 20.677  17.734 1.00 64.83 ? 357 HOH   A O   1 
HETATM 1154 O  O   . HOH   D 4 .   ? 6.146  22.662  10.958 1.00 42.69 ? 358 HOH   A O   1 
HETATM 1155 O  O   . HOH   D 4 .   ? 12.260 -8.957  12.859 1.00 42.20 ? 359 HOH   A O   1 
HETATM 1156 O  O   . HOH   D 4 .   ? 4.416  7.505   28.173 1.00 45.81 ? 360 HOH   A O   1 
HETATM 1157 O  O   . HOH   D 4 .   ? 7.091  25.841  13.728 1.00 44.84 ? 361 HOH   A O   1 
HETATM 1158 O  O   . HOH   D 4 .   ? -1.298 13.152  12.257 1.00 47.92 ? 362 HOH   A O   1 
HETATM 1159 O  O   . HOH   D 4 .   ? 1.969  -7.211  16.426 1.00 32.98 ? 363 HOH   A O   1 
HETATM 1160 O  O   . HOH   D 4 .   ? 7.570  -7.162  2.552  1.00 75.98 ? 364 HOH   A O   1 
HETATM 1161 O  O   . HOH   D 4 .   ? 7.308  5.965   34.707 1.00 56.10 ? 365 HOH   A O   1 
HETATM 1162 O  O   . HOH   D 4 .   ? 8.769  16.833  25.737 1.00 56.73 ? 366 HOH   A O   1 
HETATM 1163 O  O   . HOH   D 4 .   ? 11.407 23.023  14.169 1.00 41.21 ? 367 HOH   A O   1 
HETATM 1164 O  O   . HOH   D 4 .   ? 26.741 20.752  19.381 1.00 39.41 ? 368 HOH   A O   1 
HETATM 1165 O  O   . HOH   D 4 .   ? 9.544  -9.277  12.762 1.00 31.40 ? 369 HOH   A O   1 
HETATM 1166 O  O   . HOH   D 4 .   ? 9.225  24.536  13.114 1.00 43.46 ? 370 HOH   A O   1 
HETATM 1167 O  O   . HOH   D 4 .   ? 30.017 22.034  9.214  1.00 47.11 ? 371 HOH   A O   1 
HETATM 1168 O  O   . HOH   D 4 .   ? 12.662 14.392  32.312 1.00 49.96 ? 372 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   ? 0.9314 0.4283 0.5937 -0.0033 -0.3665 0.0056  7   SER   A N   
2    C CA  . SER   A 1   ? 0.8890 0.4292 0.6454 -0.0085 -0.3945 0.0191  7   SER   A CA  
3    C C   . SER   A 1   ? 0.8238 0.4402 0.6563 0.0094  -0.3587 0.0110  7   SER   A C   
4    O O   . SER   A 1   ? 0.8324 0.4568 0.6374 0.0181  -0.3304 0.0017  7   SER   A O   
5    C CB  . SER   A 1   ? 0.9482 0.4387 0.6778 -0.0287 -0.4373 0.0349  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.9483 0.4866 0.7718 -0.0266 -0.4477 0.0459  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.7573 0.4218 0.6819 0.0121  -0.3602 0.0163  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.7015 0.4228 0.6880 0.0240  -0.3258 0.0087  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.6452 0.4073 0.6841 0.0299  -0.3021 0.0031  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.6541 0.4157 0.6608 0.0325  -0.2917 -0.0041 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.5915 0.3845 0.7097 0.0317  -0.2897 0.0065  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.5655 0.3886 0.7275 0.0345  -0.2610 0.0004  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.5325 0.3770 0.7361 0.0377  -0.2232 -0.0065 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.5220 0.3621 0.7416 0.0391  -0.2249 -0.0028 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.5487 0.3724 0.7735 0.0294  -0.2837 0.0159  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.5184 0.3776 0.7321 0.0365  -0.1888 -0.0164 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.5146 0.3771 0.7549 0.0353  -0.1479 -0.0240 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.4951 0.3632 0.8183 0.0358  -0.1290 -0.0173 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.4911 0.3653 0.8213 0.0327  -0.1281 -0.0169 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.5419 0.4024 0.7173 0.0271  -0.1198 -0.0391 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.5645 0.4255 0.6718 0.0271  -0.1373 -0.0406 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.5495 0.3950 0.7331 0.0205  -0.0768 -0.0478 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.5870 0.4511 0.6452 0.0173  -0.1248 -0.0460 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.4802 0.3458 0.8725 0.0404  -0.1111 -0.0105 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.4480 0.3187 0.9360 0.0432  -0.0848 -0.0006 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.4651 0.3149 0.9479 0.0409  -0.0197 -0.0165 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.4617 0.2980 0.9577 0.0449  -0.0014 -0.0179 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.4042 0.2839 0.9926 0.0499  -0.1147 0.0263  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.3995 0.2820 0.9712 0.0450  -0.1819 0.0424  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.3984 0.2888 1.0034 0.0400  -0.2073 0.0566  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.4305 0.2991 0.9409 0.0428  -0.2180 0.0426  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.4214 0.2991 0.9931 0.0312  -0.2685 0.0704  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.4602 0.3141 0.9349 0.0345  -0.2746 0.0552  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.4639 0.3190 0.9662 0.0278  -0.3005 0.0691  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.5093 0.3351 0.9611 0.0156  -0.3562 0.0812  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.4802 0.3186 0.9270 0.0315  0.0142  -0.0297 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.5077 0.3083 0.9274 0.0228  0.0791  -0.0462 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.5031 0.2986 0.9864 0.0223  0.1184  -0.0424 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.5081 0.3181 0.9787 0.0168  0.1012  -0.0409 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.5649 0.3402 0.8561 0.0037  0.0848  -0.0657 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.5741 0.3699 0.8193 -0.0032 0.0497  -0.0652 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.6004 0.3202 0.8481 -0.0126 0.1503  -0.0817 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.4905 0.2670 1.0543 0.0300  0.1711  -0.0378 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.4815 0.2519 1.1269 0.0323  0.2188  -0.0305 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.4520 0.2727 1.1844 0.0396  0.1691  -0.0055 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.4402 0.2941 1.2228 0.0486  0.1105  0.0145  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.4409 0.2618 1.1723 0.0315  0.1846  -0.0070 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.3989 0.2623 1.2049 0.0352  0.1357  0.0170  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.4051 0.2830 1.1124 0.0265  0.0715  0.0099  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.3896 0.2850 1.1131 0.0224  0.0458  0.0194  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.4114 0.2716 1.2935 0.0335  0.1853  0.0252  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.4504 0.3087 1.4756 0.0480  0.2379  0.0450  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4361 0.3145 1.5412 0.0605  0.2106  0.0656  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.4786 0.3087 1.5408 0.0462  0.3167  0.0408  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.4234 0.2937 1.0366 0.0247  0.0457  -0.0042 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.4306 0.3112 0.9570 0.0193  -0.0078 -0.0095 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.4162 0.3060 0.9242 0.0261  -0.0596 -0.0024 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.4140 0.2953 0.9145 0.0303  -0.0503 -0.0063 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.4747 0.3323 0.8836 0.0055  0.0128  -0.0334 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.4968 0.3343 0.8897 -0.0081 0.0564  -0.0423 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.4898 0.3431 0.9125 -0.0101 0.0424  -0.0338 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.5447 0.3390 0.8828 -0.0223 0.1112  -0.0591 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.5192 0.3509 0.9264 -0.0241 0.0839  -0.0413 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.5796 0.3434 0.8907 -0.0390 0.1533  -0.0675 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.5761 0.3610 0.9230 -0.0393 0.1396  -0.0587 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.6339 0.3859 0.9516 -0.0573 0.1822  -0.0666 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.4049 0.3042 0.8905 0.0251  -0.1120 0.0060  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.4098 0.3046 0.8500 0.0277  -0.1597 0.0100  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.4406 0.3282 0.7744 0.0241  -0.1649 -0.0071 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.4459 0.3356 0.7628 0.0196  -0.1662 -0.0093 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.3946 0.2900 0.8843 0.0255  -0.2131 0.0352  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.4556 0.3288 0.8696 0.0231  -0.2604 0.0366  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.4754 0.3336 0.9263 0.0140  -0.3170 0.0638  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.5418 0.3655 0.9013 0.0056  -0.3557 0.0622  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.6010 0.3863 0.8924 -0.0005 -0.3892 0.0651  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.5928 0.3758 0.8966 0.0012  -0.3922 0.0692  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.6280 0.3704 0.8316 -0.0090 -0.4160 0.0627  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.4572 0.3377 0.7288 0.0261  -0.1646 -0.0168 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.4775 0.3547 0.6669 0.0240  -0.1669 -0.0272 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.4771 0.3415 0.6269 0.0298  -0.2019 -0.0222 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.4925 0.3502 0.6399 0.0329  -0.2088 -0.0199 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.5026 0.3783 0.6528 0.0188  -0.1366 -0.0386 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.5346 0.4120 0.6196 0.0156  -0.1432 -0.0416 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.5016 0.3709 0.6725 0.0088  -0.0960 -0.0455 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.4656 0.3195 0.5791 0.0302  -0.2203 -0.0209 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.4835 0.3088 0.5457 0.0337  -0.2466 -0.0175 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.4852 0.3030 0.4877 0.0385  -0.2374 -0.0235 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.4685 0.3042 0.4758 0.0369  -0.2225 -0.0267 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.5018 0.3006 0.5752 0.0276  -0.2845 -0.0049 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.5051 0.2939 0.6148 0.0230  -0.3086 0.0081  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.4881 0.3011 0.6046 0.0228  -0.2859 -0.0007 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.4988 0.2837 0.4458 0.0433  -0.2460 -0.0229 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.5188 0.2902 0.4210 0.0502  -0.2338 -0.0251 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.5312 0.2826 0.4286 0.0460  -0.2510 -0.0233 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.5525 0.2731 0.4433 0.0381  -0.2791 -0.0182 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.5647 0.2920 0.4058 0.0558  -0.2320 -0.0251 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.5988 0.3364 0.4390 0.0582  -0.2216 -0.0251 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.6200 0.3488 0.4667 0.0520  -0.2387 -0.0235 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.5890 0.3447 0.4258 0.0661  -0.1958 -0.0238 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.5137 0.2820 0.4180 0.0482  -0.2389 -0.0245 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.5287 0.2803 0.4289 0.0440  -0.2533 -0.0228 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.6009 0.2873 0.4349 0.0444  -0.2685 -0.0221 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.6283 0.2868 0.4559 0.0335  -0.2973 -0.0173 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.5102 0.2865 0.4204 0.0468  -0.2358 -0.0233 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.5090 0.2772 0.4245 0.0410  -0.2491 -0.0217 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.5450 0.3211 0.4522 0.0466  -0.2334 -0.0198 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.5691 0.3432 0.4828 0.0407  -0.2427 -0.0181 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.6278 0.3601 0.5059 0.0444  -0.2520 -0.0176 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.6206 0.3009 0.4466 0.0513  -0.2529 -0.0198 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.6390 0.3732 0.5256 0.0386  -0.2598 -0.0154 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.6341 0.2893 0.4167 0.0541  -0.2494 -0.0250 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.7032 0.2774 0.4034 0.0516  -0.2563 -0.0264 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.7397 0.2699 0.4087 0.0345  -0.2926 -0.0220 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.7914 0.2432 0.3832 0.0232  -0.3094 -0.0211 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.7355 0.2805 0.3908 0.0669  -0.2172 -0.0298 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.7817 0.3240 0.4240 0.0689  -0.2068 -0.0302 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.7580 0.3671 0.4595 0.0767  -0.1904 -0.0273 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.8430 0.3185 0.4140 0.0611  -0.2128 -0.0322 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.7825 0.3696 0.4543 0.0757  -0.1863 -0.0281 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.8410 0.3482 0.4341 0.0664  -0.1988 -0.0311 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.7100 0.2841 0.4371 0.0300  -0.3064 -0.0173 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.7380 0.2774 0.4542 0.0124  -0.3463 -0.0071 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.7182 0.2921 0.5152 0.0011  -0.3789 0.0061  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.7203 0.2837 0.5410 -0.0124 -0.4128 0.0203  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.7251 0.2803 0.4513 0.0159  -0.3380 -0.0077 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.7727 0.2867 0.4225 0.0233  -0.3103 -0.0160 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.7616 0.2970 0.4318 0.0238  -0.3092 -0.0141 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.8368 0.2476 0.3767 0.0086  -0.3262 -0.0153 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.6981 0.3165 0.5469 0.0066  -0.3665 0.0040  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.6801 0.3342 0.6147 -0.0021 -0.3868 0.0171  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.7204 0.3237 0.6378 -0.0230 -0.4379 0.0351  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.7662 0.3065 0.5953 -0.0301 -0.4498 0.0320  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.6508 0.3524 0.6268 0.0059  -0.3585 0.0094  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.7058 0.3309 0.7080 -0.0345 -0.4680 0.0565  24  THR   A N   
135  C CA  . THR   A 18  ? 0.7458 0.3299 0.7542 -0.0593 -0.5260 0.0826  24  THR   A CA  
136  C C   . THR   A 18  ? 0.7446 0.3536 0.8061 -0.0632 -0.5309 0.0904  24  THR   A C   
137  O O   . THR   A 18  ? 0.7172 0.3764 0.8130 -0.0465 -0.4870 0.0748  24  THR   A O   
138  C CB  . THR   A 18  ? 0.7322 0.3353 0.8287 -0.0690 -0.5563 0.1084  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.6738 0.3540 0.8996 -0.0561 -0.5272 0.1133  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.7622 0.3444 0.8124 -0.0659 -0.5520 0.1016  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.7695 0.3418 0.8395 -0.0884 -0.5870 0.1172  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.7639 0.3638 0.8976 -0.0936 -0.5941 0.1288  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.6899 0.3743 0.9724 -0.0814 -0.5654 0.1386  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.6658 0.3895 0.9920 -0.0733 -0.5347 0.1317  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.8224 0.3681 0.9480 -0.1265 -0.6654 0.1618  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.9892 0.4306 0.9594 -0.1462 -0.6984 0.1565  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 1.0738 0.4641 0.9654 -0.1565 -0.7091 0.1510  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 1.0735 0.4445 0.9551 -0.1614 -0.7250 0.1594  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 1.1673 0.4534 0.9201 -0.1767 -0.7366 0.1487  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 1.1760 0.4451 0.9151 -0.1816 -0.7477 0.1539  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.6547 0.3612 1.0104 -0.0803 -0.5705 0.1537  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.5850 0.3611 1.0791 -0.0672 -0.5333 0.1620  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.5529 0.3654 1.0318 -0.0438 -0.4614 0.1272  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.5133 0.3683 1.0733 -0.0365 -0.4218 0.1269  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.5915 0.3795 1.1772 -0.0712 -0.5551 0.1898  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.5929 0.4315 1.3458 -0.0713 -0.5486 0.2214  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.6128 0.4652 1.4073 -0.0773 -0.5503 0.2317  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.5656 0.4320 1.4242 -0.0643 -0.5384 0.2395  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.5748 0.3659 0.9484 -0.0346 -0.4440 0.1000  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.5510 0.3698 0.8978 -0.0177 -0.3849 0.0705  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.5450 0.3700 0.8708 -0.0187 -0.3701 0.0609  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.5366 0.3925 0.8903 -0.0132 -0.3269 0.0496  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.5887 0.3818 0.8351 -0.0100 -0.3778 0.0508  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.6076 0.4005 0.8693 -0.0069 -0.3800 0.0546  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.5692 0.3952 0.9200 -0.0033 -0.3621 0.0624  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.6498 0.4057 0.8328 -0.0078 -0.3954 0.0494  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.5545 0.3432 0.8273 -0.0286 -0.4066 0.0665  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.5501 0.3404 0.8024 -0.0306 -0.3985 0.0598  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.5133 0.3328 0.8636 -0.0397 -0.4013 0.0786  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.4983 0.3368 0.8555 -0.0387 -0.3742 0.0698  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.5837 0.3149 0.7355 -0.0372 -0.4318 0.0576  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.5909 0.3035 0.6540 -0.0234 -0.4053 0.0346  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.6269 0.3043 0.6273 -0.0193 -0.4086 0.0289  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.5760 0.3076 0.6155 -0.0126 -0.3699 0.0180  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.6421 0.3174 0.5880 -0.0046 -0.3748 0.0109  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.6124 0.3200 0.5821 -0.0011 -0.3547 0.0057  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.5548 0.3163 0.6235 -0.0138 -0.3523 0.0151  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.6135 0.3322 0.5565 0.0098  -0.3253 -0.0055 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.5667 0.3350 0.5977 -0.0054 -0.3261 0.0023  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.5902 0.3400 0.5654 0.0066  -0.3143 -0.0060 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.4997 0.3219 0.9293 -0.0500 -0.4346 0.1073  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.4730 0.3268 1.0165 -0.0579 -0.4350 0.1311  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.4441 0.3455 1.0816 -0.0456 -0.3731 0.1269  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.4198 0.3478 1.1540 -0.0491 -0.3558 0.1432  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.4536 0.2920 1.0593 -0.0760 -0.4978 0.1705  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.4438 0.3495 1.0511 -0.0327 -0.3383 0.1064  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.4105 0.3430 1.0755 -0.0228 -0.2756 0.0971  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.4280 0.3524 0.9924 -0.0163 -0.2354 0.0622  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.4307 0.3602 1.0040 -0.0099 -0.1938 0.0510  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.4028 0.3434 1.1428 -0.0173 -0.2804 0.1140  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.3838 0.3410 1.2562 -0.0246 -0.3090 0.1545  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.3873 0.3639 1.3358 -0.0275 -0.2869 0.1664  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.3622 0.3103 1.2666 -0.0301 -0.3608 0.1797  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.4385 0.3469 0.9093 -0.0194 -0.2504 0.0481  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.4404 0.3416 0.8220 -0.0163 -0.2250 0.0230  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.4160 0.3257 0.8097 -0.0210 -0.1698 0.0112  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.3955 0.3115 0.8361 -0.0282 -0.1531 0.0175  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.4628 0.3477 0.7749 -0.0196 -0.2510 0.0187  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.4921 0.3726 0.7265 -0.0189 -0.2312 0.0004  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.4993 0.3727 0.6863 -0.0094 -0.2318 -0.0076 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.5064 0.3729 0.6986 -0.0221 -0.2530 0.0011  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.4185 0.3221 0.7664 -0.0197 -0.1409 -0.0048 32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.4126 0.3055 0.7374 -0.0304 -0.0901 -0.0185 32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.4294 0.3116 0.6591 -0.0395 -0.0991 -0.0297 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.4482 0.3200 0.6506 -0.0541 -0.0843 -0.0336 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.4216 0.3062 0.7541 -0.0273 -0.0566 -0.0255 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.4552 0.3108 0.7364 -0.0444 -0.0060 -0.0409 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.3875 0.2840 0.8257 -0.0168 -0.0476 -0.0106 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.4173 0.3012 0.6034 -0.0311 -0.1248 -0.0314 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.4226 0.3013 0.5389 -0.0361 -0.1341 -0.0357 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.4086 0.2913 0.5066 -0.0198 -0.1659 -0.0318 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.3967 0.2805 0.5132 -0.0096 -0.1717 -0.0306 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.4358 0.3015 0.5149 -0.0489 -0.1053 -0.0437 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.4659 0.3297 0.4867 -0.0558 -0.1200 -0.0413 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.4906 0.3497 0.4786 -0.0694 -0.1301 -0.0362 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.4753 0.3451 0.4762 -0.0483 -0.1303 -0.0388 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.5071 0.3708 0.4646 -0.0711 -0.1461 -0.0281 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.4990 0.3697 0.4635 -0.0582 -0.1446 -0.0299 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.4748 0.3497 0.4896 -0.0349 -0.1298 -0.0408 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.5076 0.3860 0.4559 -0.0551 -0.1549 -0.0217 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.4904 0.3703 0.4787 -0.0319 -0.1394 -0.0360 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.5014 0.3842 0.4601 -0.0418 -0.1503 -0.0260 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.4095 0.2896 0.4703 -0.0179 -0.1829 -0.0290 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.4179 0.2920 0.4540 -0.0027 -0.2014 -0.0261 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.4442 0.3205 0.4470 -0.0040 -0.2013 -0.0215 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.4486 0.3270 0.4464 -0.0160 -0.2004 -0.0185 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.4195 0.2757 0.4597 0.0061  -0.2272 -0.0222 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.4248 0.2747 0.4677 0.0003  -0.2385 -0.0188 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.4487 0.2889 0.4546 0.0035  -0.2422 -0.0170 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.4581 0.3004 0.4690 -0.0053 -0.2449 -0.0149 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.4478 0.2781 0.4251 0.0149  -0.2400 -0.0162 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.4471 0.3225 0.4330 0.0075  -0.2022 -0.0179 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.4623 0.3441 0.4366 0.0078  -0.2017 -0.0070 35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.4740 0.3443 0.4379 0.0285  -0.2004 -0.0025 35  ASP   A C   
235  O O   . ASP   A 29  ? 0.4770 0.3527 0.4393 0.0328  -0.1929 -0.0013 35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.4856 0.3819 0.4568 -0.0108 -0.1940 -0.0017 35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.5526 0.4585 0.5237 -0.0197 -0.2013 0.0172  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.5369 0.4436 0.5204 -0.0040 -0.2057 0.0275  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.6083 0.5158 0.5664 -0.0443 -0.2027 0.0239  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.4769 0.3253 0.4295 0.0404  -0.2038 -0.0001 36  SER   A N   
241  C CA  . SER   A 30  ? 0.4949 0.3173 0.4284 0.0597  -0.1931 0.0029  36  SER   A CA  
242  C C   . SER   A 30  ? 0.4729 0.3175 0.4290 0.0652  -0.1778 0.0182  36  SER   A C   
243  O O   . SER   A 30  ? 0.4703 0.3011 0.4156 0.0781  -0.1634 0.0188  36  SER   A O   
244  C CB  . SER   A 30  ? 0.5277 0.3126 0.4389 0.0691  -0.1939 0.0026  36  SER   A CB  
245  O OG  . SER   A 30  ? 0.5602 0.3651 0.4987 0.0659  -0.1941 0.0146  36  SER   A OG  
246  N N   . SER   A 31  ? 0.4499 0.3265 0.4368 0.0520  -0.1834 0.0328  37  SER   A N   
247  C CA  . SER   A 31  ? 0.4320 0.3327 0.4502 0.0520  -0.1769 0.0539  37  SER   A CA  
248  C C   . SER   A 31  ? 0.4055 0.3179 0.4169 0.0461  -0.1742 0.0497  37  SER   A C   
249  O O   . SER   A 31  ? 0.4064 0.3327 0.4406 0.0504  -0.1665 0.0661  37  SER   A O   
250  C CB  . SER   A 31  ? 0.4481 0.3731 0.4955 0.0322  -0.1929 0.0751  37  SER   A CB  
251  O OG  . SER   A 31  ? 0.4906 0.4242 0.5191 0.0040  -0.2065 0.0695  37  SER   A OG  
252  N N   . ARG   A 32  ? 0.3897 0.2969 0.3773 0.0364  -0.1794 0.0307  38  ARG   A N   
253  C CA  . ARG   A 32  ? 0.3780 0.2916 0.3585 0.0318  -0.1756 0.0257  38  ARG   A CA  
254  C C   . ARG   A 32  ? 0.4010 0.2917 0.3609 0.0469  -0.1705 0.0102  38  ARG   A C   
255  O O   . ARG   A 32  ? 0.4179 0.3115 0.3732 0.0461  -0.1670 0.0072  38  ARG   A O   
256  C CB  . ARG   A 32  ? 0.3685 0.2884 0.3408 0.0072  -0.1808 0.0189  38  ARG   A CB  
257  C CG  . ARG   A 32  ? 0.3507 0.2794 0.3253 -0.0160 -0.1906 0.0341  38  ARG   A CG  
258  C CD  . ARG   A 32  ? 0.3774 0.2942 0.3249 -0.0434 -0.1881 0.0247  38  ARG   A CD  
259  N NE  . ARG   A 32  ? 0.3884 0.3015 0.3232 -0.0477 -0.1793 0.0190  38  ARG   A NE  
260  C CZ  . ARG   A 32  ? 0.4189 0.3133 0.3216 -0.0747 -0.1738 0.0158  38  ARG   A CZ  
261  N NH1 . ARG   A 32  ? 0.3900 0.2645 0.2644 -0.1020 -0.1759 0.0179  38  ARG   A NH1 
262  N NH2 . ARG   A 32  ? 0.4284 0.3165 0.3196 -0.0765 -0.1650 0.0105  38  ARG   A NH2 
263  N N   . ASP   A 33  ? 0.4103 0.2729 0.3533 0.0571  -0.1740 0.0020  39  ASP   A N   
264  C CA  . ASP   A 33  ? 0.4238 0.2535 0.3387 0.0643  -0.1786 -0.0092 39  ASP   A CA  
265  C C   . ASP   A 33  ? 0.4095 0.2514 0.3398 0.0524  -0.1895 -0.0175 39  ASP   A C   
266  O O   . ASP   A 33  ? 0.4151 0.2464 0.3375 0.0543  -0.1925 -0.0212 39  ASP   A O   
267  C CB  . ASP   A 33  ? 0.4456 0.2560 0.3380 0.0766  -0.1641 -0.0065 39  ASP   A CB  
268  C CG  . ASP   A 33  ? 0.5217 0.2859 0.3709 0.0784  -0.1735 -0.0162 39  ASP   A CG  
269  O OD1 . ASP   A 33  ? 0.5373 0.2671 0.3617 0.0759  -0.1880 -0.0208 39  ASP   A OD1 
270  O OD2 . ASP   A 33  ? 0.5463 0.3060 0.3847 0.0789  -0.1706 -0.0172 39  ASP   A OD2 
271  N N   . LEU   A 34  ? 0.3898 0.2506 0.3438 0.0398  -0.1920 -0.0193 40  LEU   A N   
272  C CA  . LEU   A 34  ? 0.3778 0.2458 0.3554 0.0308  -0.1925 -0.0259 40  LEU   A CA  
273  C C   . LEU   A 34  ? 0.3973 0.2600 0.3962 0.0263  -0.2025 -0.0277 40  LEU   A C   
274  O O   . LEU   A 34  ? 0.4185 0.2788 0.4118 0.0245  -0.2068 -0.0257 40  LEU   A O   
275  C CB  . LEU   A 34  ? 0.3540 0.2407 0.3390 0.0163  -0.1761 -0.0267 40  LEU   A CB  
276  C CG  . LEU   A 34  ? 0.3600 0.2540 0.3309 0.0148  -0.1687 -0.0226 40  LEU   A CG  
277  C CD1 . LEU   A 34  ? 0.3617 0.2583 0.3260 -0.0068 -0.1554 -0.0241 40  LEU   A CD1 
278  C CD2 . LEU   A 34  ? 0.3574 0.2430 0.3278 0.0264  -0.1715 -0.0259 40  LEU   A CD2 
279  N N   . LEU   A 35  ? 0.3964 0.2585 0.4271 0.0241  -0.2064 -0.0289 41  LEU   A N   
280  C CA  . LEU   A 35  ? 0.3986 0.2608 0.4679 0.0186  -0.2147 -0.0260 41  LEU   A CA  
281  C C   . LEU   A 35  ? 0.4045 0.2780 0.5242 0.0153  -0.2003 -0.0259 41  LEU   A C   
282  O O   . LEU   A 35  ? 0.4131 0.2838 0.5378 0.0200  -0.2026 -0.0251 41  LEU   A O   
283  C CB  . LEU   A 35  ? 0.4077 0.2429 0.4681 0.0215  -0.2481 -0.0185 41  LEU   A CB  
284  C CG  . LEU   A 35  ? 0.4027 0.2394 0.5073 0.0134  -0.2627 -0.0104 41  LEU   A CG  
285  C CD1 . LEU   A 35  ? 0.4482 0.2511 0.5127 0.0120  -0.2920 -0.0056 41  LEU   A CD1 
286  C CD2 . LEU   A 35  ? 0.3877 0.2317 0.5594 0.0099  -0.2723 0.0006  41  LEU   A CD2 
287  N N   . VAL   A 36  ? 0.4071 0.2900 0.5626 0.0071  -0.1804 -0.0270 42  VAL   A N   
288  C CA  . VAL   A 36  ? 0.4135 0.3019 0.6267 0.0051  -0.1565 -0.0260 42  VAL   A CA  
289  C C   . VAL   A 36  ? 0.4230 0.3173 0.7060 0.0035  -0.1652 -0.0136 42  VAL   A C   
290  O O   . VAL   A 36  ? 0.4170 0.3123 0.6952 -0.0030 -0.1646 -0.0135 42  VAL   A O   
291  C CB  . VAL   A 36  ? 0.4197 0.3027 0.6097 -0.0060 -0.1140 -0.0379 42  VAL   A CB  
292  C CG1 . VAL   A 36  ? 0.4065 0.2850 0.6583 -0.0074 -0.0781 -0.0377 42  VAL   A CG1 
293  C CG2 . VAL   A 36  ? 0.4412 0.3196 0.5735 -0.0067 -0.1135 -0.0440 42  VAL   A CG2 
294  N N   . SER   A 37  ? 0.4313 0.3295 0.7818 0.0083  -0.1789 0.0007  43  SER   A N   
295  C CA  . SER   A 37  ? 0.4332 0.3403 0.8703 0.0058  -0.1928 0.0206  43  SER   A CA  
296  C C   . SER   A 37  ? 0.4459 0.3644 0.9762 0.0091  -0.1552 0.0280  43  SER   A C   
297  O O   . SER   A 37  ? 0.4444 0.3589 0.9720 0.0145  -0.1352 0.0214  43  SER   A O   
298  C CB  . SER   A 37  ? 0.4395 0.3346 0.8809 0.0045  -0.2517 0.0392  43  SER   A CB  
299  O OG  . SER   A 37  ? 0.4488 0.3362 0.8881 0.0090  -0.2648 0.0427  43  SER   A OG  
300  N N   . SER   A 38  ? 0.4436 0.3742 1.0610 0.0062  -0.1434 0.0435  44  SER   A N   
301  C CA  . SER   A 38  ? 0.4449 0.3841 1.1676 0.0111  -0.0992 0.0541  44  SER   A CA  
302  C C   . SER   A 38  ? 0.4489 0.3995 1.2635 0.0172  -0.1335 0.0822  44  SER   A C   
303  O O   . SER   A 38  ? 0.4595 0.4092 1.2670 0.0120  -0.1978 0.0991  44  SER   A O   
304  C CB  . SER   A 38  ? 0.4371 0.3856 1.2295 0.0060  -0.0709 0.0641  44  SER   A CB  
305  O OG  . SER   A 38  ? 0.4483 0.4093 1.2691 -0.0001 -0.1272 0.0858  44  SER   A OG  
306  N N   . THR   A 39  ? 0.4440 0.3974 1.3367 0.0260  -0.0914 0.0876  45  THR   A N   
307  C CA  . THR   A 39  ? 0.4458 0.4108 1.4396 0.0313  -0.1230 0.1183  45  THR   A CA  
308  C C   . THR   A 39  ? 0.4342 0.4138 1.5813 0.0400  -0.0720 0.1403  45  THR   A C   
309  O O   . THR   A 39  ? 0.4456 0.4140 1.5949 0.0436  0.0023  0.1224  45  THR   A O   
310  C CB  . THR   A 39  ? 0.4847 0.4354 1.4153 0.0360  -0.1363 0.1063  45  THR   A CB  
311  O OG1 . THR   A 39  ? 0.5270 0.4608 1.3905 0.0406  -0.0742 0.0741  45  THR   A OG1 
312  C CG2 . THR   A 39  ? 0.5235 0.4609 1.3483 0.0278  -0.2024 0.1022  45  THR   A CG2 
313  N N   . THR   A 40  ? 0.4130 0.4119 1.6884 0.0415  -0.1106 0.1813  46  THR   A N   
314  C CA  . THR   A 40  ? 0.3848 0.4018 1.8315 0.0517  -0.0646 0.2104  46  THR   A CA  
315  C C   . THR   A 40  ? 0.3954 0.4004 1.8796 0.0667  -0.0162 0.2048  46  THR   A C   
316  O O   . THR   A 40  ? 0.3708 0.3731 1.9536 0.0790  0.0600  0.2095  46  THR   A O   
317  C CB  . THR   A 40  ? 0.3630 0.4089 1.9464 0.0428  -0.1340 0.2651  46  THR   A CB  
318  O OG1 . THR   A 40  ? 0.4074 0.4450 1.9542 0.0334  -0.2155 0.2800  46  THR   A OG1 
319  C CG2 . THR   A 40  ? 0.3682 0.4219 1.9295 0.0282  -0.1648 0.2710  46  THR   A CG2 
320  N N   . ALA   A 41  ? 0.4254 0.4185 1.8315 0.0657  -0.0565 0.1953  47  ALA   A N   
321  C CA  . ALA   A 41  ? 0.4168 0.3957 1.8462 0.0785  -0.0169 0.1890  47  ALA   A CA  
322  C C   . ALA   A 41  ? 0.4800 0.4230 1.7661 0.0801  0.0476  0.1382  47  ALA   A C   
323  O O   . ALA   A 41  ? 0.5230 0.4563 1.6813 0.0697  0.0405  0.1109  47  ALA   A O   
324  C CB  . ALA   A 41  ? 0.4183 0.3989 1.8333 0.0738  -0.0936 0.2060  47  ALA   A CB  
325  N N   . GLN   A 42  ? 0.4807 0.3997 1.7872 0.0911  0.1083  0.1280  48  GLN   A N   
326  C CA  . GLN   A 42  ? 0.5399 0.4147 1.7071 0.0872  0.1656  0.0837  48  GLN   A CA  
327  C C   . GLN   A 42  ? 0.5786 0.4426 1.6352 0.0837  0.1272  0.0668  48  GLN   A C   
328  O O   . GLN   A 42  ? 0.5807 0.4334 1.6747 0.0925  0.1410  0.0716  48  GLN   A O   
329  C CB  . GLN   A 42  ? 0.5417 0.3785 1.7680 0.0969  0.2653  0.0770  48  GLN   A CB  
330  C CG  . GLN   A 42  ? 0.6451 0.4217 1.7164 0.0843  0.3281  0.0329  48  GLN   A CG  
331  C CD  . GLN   A 42  ? 0.7114 0.4622 1.7770 0.0764  0.3919  0.0228  48  GLN   A CD  
332  O OE1 . GLN   A 42  ? 0.7354 0.4617 1.8958 0.0857  0.4684  0.0306  48  GLN   A OE1 
333  N NE2 . GLN   A 42  ? 0.7356 0.4872 1.6917 0.0590  0.3662  0.0060  48  GLN   A NE2 
334  N N   . GLY   A 43  ? 0.6054 0.4706 1.5303 0.0715  0.0863  0.0474  49  GLY   A N   
335  C CA  . GLY   A 43  ? 0.6340 0.4902 1.4476 0.0670  0.0524  0.0312  49  GLY   A CA  
336  C C   . GLY   A 43  ? 0.6528 0.4692 1.4043 0.0656  0.1093  0.0070  49  GLY   A C   
337  O O   . GLY   A 43  ? 0.6740 0.4570 1.4027 0.0604  0.1747  -0.0096 49  GLY   A O   
338  N N   . CYS   A 44  ? 0.6530 0.4649 1.3660 0.0670  0.0847  0.0045  50  CYS   A N   
339  C CA  . CYS   A 44  ? 0.6778 0.4481 1.3382 0.0646  0.1344  -0.0149 50  CYS   A CA  
340  C C   . CYS   A 44  ? 0.6911 0.4487 1.2123 0.0515  0.1116  -0.0351 50  CYS   A C   
341  O O   . CYS   A 44  ? 0.7241 0.4482 1.2015 0.0477  0.1387  -0.0468 50  CYS   A O   
342  C CB  . CYS   A 44  ? 0.6778 0.4467 1.4456 0.0796  0.1443  0.0038  50  CYS   A CB  
343  S SG  . CYS   A 44  ? 0.7539 0.5674 1.5877 0.0860  0.0524  0.0364  50  CYS   A SG  
344  N N   . ASP   A 45  ? 0.6645 0.4447 1.1191 0.0439  0.0665  -0.0379 51  ASP   A N   
345  C CA  . ASP   A 45  ? 0.6744 0.4469 1.0136 0.0321  0.0473  -0.0518 51  ASP   A CA  
346  C C   . ASP   A 45  ? 0.6814 0.4130 0.9353 0.0129  0.0932  -0.0718 51  ASP   A C   
347  O O   . ASP   A 45  ? 0.6916 0.4131 0.9480 0.0066  0.1192  -0.0762 51  ASP   A O   
348  C CB  . ASP   A 45  ? 0.6928 0.4978 0.9966 0.0316  -0.0081 -0.0461 51  ASP   A CB  
349  C CG  . ASP   A 45  ? 0.7167 0.5418 1.0529 0.0417  -0.0590 -0.0299 51  ASP   A CG  
350  O OD1 . ASP   A 45  ? 0.7421 0.5588 1.0720 0.0439  -0.0640 -0.0286 51  ASP   A OD1 
351  O OD2 . ASP   A 45  ? 0.7014 0.5438 1.0618 0.0446  -0.0950 -0.0180 51  ASP   A OD2 
352  N N   . THR   A 46  ? 0.6848 0.3876 0.8589 0.0001  0.1007  -0.0821 52  THR   A N   
353  C CA  . THR   A 46  ? 0.7105 0.3635 0.7868 -0.0261 0.1344  -0.0977 52  THR   A CA  
354  C C   . THR   A 46  ? 0.6931 0.3676 0.6950 -0.0402 0.0908  -0.0952 52  THR   A C   
355  O O   . THR   A 46  ? 0.6863 0.3900 0.6788 -0.0345 0.0511  -0.0876 52  THR   A O   
356  C CB  . THR   A 46  ? 0.7589 0.3579 0.7875 -0.0369 0.1672  -0.1073 52  THR   A CB  
357  O OG1 . THR   A 46  ? 0.7706 0.3308 0.8557 -0.0289 0.2283  -0.1125 52  THR   A OG1 
358  C CG2 . THR   A 46  ? 0.8160 0.3631 0.7141 -0.0722 0.1745  -0.1177 52  THR   A CG2 
359  N N   . ILE   A 47  ? 0.6802 0.3363 0.6309 -0.0597 0.1007  -0.1001 53  ILE   A N   
360  C CA  . ILE   A 47  ? 0.6688 0.3432 0.5596 -0.0742 0.0615  -0.0936 53  ILE   A CA  
361  C C   . ILE   A 47  ? 0.7124 0.3388 0.5057 -0.1060 0.0665  -0.0961 53  ILE   A C   
362  O O   . ILE   A 47  ? 0.7611 0.3218 0.5034 -0.1272 0.1089  -0.1079 53  ILE   A O   
363  C CB  . ILE   A 47  ? 0.6546 0.3390 0.5457 -0.0797 0.0581  -0.0924 53  ILE   A CB  
364  C CG1 . ILE   A 47  ? 0.6130 0.3353 0.6001 -0.0524 0.0556  -0.0886 53  ILE   A CG1 
365  C CG2 . ILE   A 47  ? 0.6515 0.3604 0.4972 -0.0913 0.0147  -0.0809 53  ILE   A CG2 
366  C CD1 . ILE   A 47  ? 0.5932 0.3654 0.6270 -0.0287 0.0098  -0.0770 53  ILE   A CD1 
367  N N   . ALA   A 48  ? 0.6958 0.3491 0.4621 -0.1112 0.0245  -0.0834 54  ALA   A N   
368  C CA  . ALA   A 48  ? 0.7236 0.3386 0.4037 -0.1451 0.0154  -0.0778 54  ALA   A CA  
369  C C   . ALA   A 48  ? 0.7589 0.3478 0.3794 -0.1767 0.0089  -0.0727 54  ALA   A C   
370  O O   . ALA   A 48  ? 0.7358 0.3636 0.3906 -0.1666 -0.0085 -0.0664 54  ALA   A O   
371  C CB  . ALA   A 48  ? 0.6854 0.3469 0.3776 -0.1378 -0.0275 -0.0604 54  ALA   A CB  
372  N N   . ARG   A 49  ? 0.8207 0.3363 0.3462 -0.2174 0.0222  -0.0750 55  ARG   A N   
373  C CA  . ARG   A 49  ? 0.8661 0.3438 0.3188 -0.2565 0.0094  -0.0665 55  ARG   A CA  
374  C C   . ARG   A 49  ? 0.9124 0.3628 0.2945 -0.2928 -0.0259 -0.0473 55  ARG   A C   
375  O O   . ARG   A 49  ? 0.9757 0.3476 0.2741 -0.3227 -0.0047 -0.0555 55  ARG   A O   
376  C CB  . ARG   A 49  ? 0.9409 0.3354 0.3337 -0.2771 0.0646  -0.0879 55  ARG   A CB  
377  C CG  . ARG   A 49  ? 0.9415 0.3653 0.4192 -0.2412 0.1016  -0.1029 55  ARG   A CG  
378  C CD  . ARG   A 49  ? 0.9153 0.4103 0.4574 -0.2223 0.0688  -0.0919 55  ARG   A CD  
379  N NE  . ARG   A 49  ? 0.8832 0.3990 0.5041 -0.1923 0.1026  -0.1038 55  ARG   A NE  
380  C CZ  . ARG   A 49  ? 0.8301 0.4110 0.5267 -0.1661 0.0791  -0.0970 55  ARG   A CZ  
381  N NH1 . ARG   A 49  ? 0.7800 0.4089 0.4831 -0.1631 0.0286  -0.0809 55  ARG   A NH1 
382  N NH2 . ARG   A 49  ? 0.7969 0.3910 0.5647 -0.1439 0.1076  -0.1042 55  ARG   A NH2 
383  N N   . CYS   A 50  ? 0.8753 0.3907 0.2994 -0.2873 -0.0772 -0.0204 56  CYS   A N   
384  C CA  . CYS   A 50  ? 0.8975 0.4037 0.2841 -0.3149 -0.1134 0.0032  56  CYS   A CA  
385  C C   . CYS   A 50  ? 0.8648 0.4417 0.3095 -0.3114 -0.1655 0.0384  56  CYS   A C   
386  O O   . CYS   A 50  ? 0.8255 0.4580 0.3386 -0.2819 -0.1689 0.0398  56  CYS   A O   
387  C CB  . CYS   A 50  ? 0.9006 0.4192 0.3148 -0.2897 -0.0975 -0.0077 56  CYS   A CB  
388  S SG  . CYS   A 50  ? 0.8843 0.5096 0.4254 -0.2299 -0.1101 -0.0035 56  CYS   A SG  
389  N N   . ASP   A 51  ? 0.8820 0.4600 0.3108 -0.3373 -0.2034 0.0681  57  ASP   A N   
390  C CA  . ASP   A 51  ? 0.8471 0.4957 0.3507 -0.3298 -0.2462 0.1056  57  ASP   A CA  
391  C C   . ASP   A 51  ? 0.8141 0.5110 0.3740 -0.3050 -0.2525 0.1161  57  ASP   A C   
392  O O   . ASP   A 51  ? 0.7944 0.5193 0.3847 -0.3196 -0.2888 0.1536  57  ASP   A O   
393  C CB  . ASP   A 51  ? 0.9092 0.5262 0.3670 -0.3852 -0.2937 0.1438  57  ASP   A CB  
394  C CG  . ASP   A 51  ? 1.0722 0.6365 0.4594 -0.4317 -0.3194 0.1632  57  ASP   A CG  
395  O OD1 . ASP   A 51  ? 1.1195 0.6490 0.4648 -0.4269 -0.2907 0.1380  57  ASP   A OD1 
396  O OD2 . ASP   A 51  ? 1.1366 0.6947 0.5155 -0.4736 -0.3710 0.2066  57  ASP   A OD2 
397  N N   . CYS   A 52  ? 0.7996 0.5048 0.3770 -0.2696 -0.2182 0.0862  58  CYS   A N   
398  C CA  . CYS   A 52  ? 0.7583 0.5019 0.3801 -0.2462 -0.2204 0.0923  58  CYS   A CA  
399  C C   . CYS   A 52  ? 0.6900 0.5066 0.4005 -0.2177 -0.2354 0.1159  58  CYS   A C   
400  O O   . CYS   A 52  ? 0.6851 0.5278 0.4334 -0.1971 -0.2299 0.1126  58  CYS   A O   
401  C CB  . CYS   A 52  ? 0.7638 0.4996 0.3908 -0.2141 -0.1832 0.0566  58  CYS   A CB  
402  S SG  . CYS   A 52  ? 0.8286 0.4794 0.3656 -0.2426 -0.1591 0.0348  58  CYS   A SG  
403  N N   . GLN   A 53  ? 0.6427 0.4875 0.3852 -0.2156 -0.2496 0.1390  59  GLN   A N   
404  C CA  . GLN   A 53  ? 0.5787 0.4857 0.4064 -0.1850 -0.2517 0.1602  59  GLN   A CA  
405  C C   . GLN   A 53  ? 0.5419 0.4684 0.3936 -0.1574 -0.2354 0.1530  59  GLN   A C   
406  O O   . GLN   A 53  ? 0.5114 0.4783 0.4233 -0.1406 -0.2355 0.1763  59  GLN   A O   
407  C CB  . GLN   A 53  ? 0.5775 0.5101 0.4476 -0.2093 -0.2859 0.2090  59  GLN   A CB  
408  C CG  . GLN   A 53  ? 0.5992 0.5318 0.4776 -0.2207 -0.2993 0.2191  59  GLN   A CG  
409  C CD  . GLN   A 53  ? 0.6271 0.5850 0.5576 -0.2474 -0.3383 0.2735  59  GLN   A CD  
410  O OE1 . GLN   A 53  ? 0.6855 0.6079 0.5701 -0.2963 -0.3746 0.2950  59  GLN   A OE1 
411  N NE2 . GLN   A 53  ? 0.5762 0.5902 0.6029 -0.2183 -0.3313 0.2993  59  GLN   A NE2 
412  N N   . THR   A 54  ? 0.5485 0.4429 0.3551 -0.1534 -0.2192 0.1226  60  THR   A N   
413  C CA  . THR   A 54  ? 0.5237 0.4262 0.3412 -0.1286 -0.2042 0.1102  60  THR   A CA  
414  C C   . THR   A 54  ? 0.5095 0.3859 0.3049 -0.1104 -0.1817 0.0718  60  THR   A C   
415  O O   . THR   A 54  ? 0.5076 0.3511 0.2693 -0.1239 -0.1746 0.0557  60  THR   A O   
416  C CB  . THR   A 54  ? 0.5577 0.4452 0.3490 -0.1514 -0.2164 0.1229  60  THR   A CB  
417  O OG1 . THR   A 54  ? 0.6174 0.4491 0.3398 -0.1758 -0.2131 0.1032  60  THR   A OG1 
418  C CG2 . THR   A 54  ? 0.5379 0.4502 0.3584 -0.1754 -0.2443 0.1672  60  THR   A CG2 
419  N N   . GLY   A 55  ? 0.4802 0.3685 0.2972 -0.0815 -0.1706 0.0606  61  GLY   A N   
420  C CA  . GLY   A 55  ? 0.4903 0.3603 0.3043 -0.0636 -0.1561 0.0324  61  GLY   A CA  
421  C C   . GLY   A 55  ? 0.4726 0.3518 0.3048 -0.0379 -0.1534 0.0279  61  GLY   A C   
422  O O   . GLY   A 55  ? 0.4676 0.3611 0.3054 -0.0353 -0.1567 0.0433  61  GLY   A O   
423  N N   . VAL   A 56  ? 0.4605 0.3269 0.3013 -0.0219 -0.1483 0.0091  62  VAL   A N   
424  C CA  . VAL   A 56  ? 0.4635 0.3236 0.3110 -0.0030 -0.1518 0.0035  62  VAL   A CA  
425  C C   . VAL   A 56  ? 0.4593 0.3171 0.3217 0.0109  -0.1536 -0.0045 62  VAL   A C   
426  O O   . VAL   A 56  ? 0.4662 0.3199 0.3437 0.0090  -0.1503 -0.0138 62  VAL   A O   
427  C CB  . VAL   A 56  ? 0.4754 0.3134 0.3220 -0.0046 -0.1529 -0.0063 62  VAL   A CB  
428  C CG1 . VAL   A 56  ? 0.4797 0.3061 0.3272 0.0085  -0.1645 -0.0068 62  VAL   A CG1 
429  C CG2 . VAL   A 56  ? 0.4937 0.3260 0.3185 -0.0218 -0.1505 -0.0005 62  VAL   A CG2 
430  N N   . TYR   A 57  ? 0.4523 0.3056 0.3063 0.0232  -0.1570 -0.0008 63  TYR   A N   
431  C CA  . TYR   A 57  ? 0.4598 0.3009 0.3166 0.0332  -0.1628 -0.0070 63  TYR   A CA  
432  C C   . TYR   A 57  ? 0.4938 0.3024 0.3300 0.0383  -0.1769 -0.0090 63  TYR   A C   
433  O O   . TYR   A 57  ? 0.5059 0.3025 0.3175 0.0374  -0.1761 -0.0044 63  TYR   A O   
434  C CB  . TYR   A 57  ? 0.4397 0.2908 0.2930 0.0394  -0.1530 0.0000  63  TYR   A CB  
435  C CG  . TYR   A 57  ? 0.4504 0.2862 0.2780 0.0483  -0.1424 0.0081  63  TYR   A CG  
436  C CD1 . TYR   A 57  ? 0.4454 0.2965 0.2765 0.0462  -0.1301 0.0219  63  TYR   A CD1 
437  C CD2 . TYR   A 57  ? 0.4887 0.2888 0.2863 0.0571  -0.1415 0.0036  63  TYR   A CD2 
438  C CE1 . TYR   A 57  ? 0.4677 0.3017 0.2804 0.0555  -0.1111 0.0303  63  TYR   A CE1 
439  C CE2 . TYR   A 57  ? 0.5201 0.2925 0.2838 0.0644  -0.1218 0.0095  63  TYR   A CE2 
440  C CZ  . TYR   A 57  ? 0.5133 0.3051 0.2895 0.0652  -0.1031 0.0229  63  TYR   A CZ  
441  O OH  . TYR   A 57  ? 0.5497 0.3131 0.2991 0.0731  -0.0756 0.0301  63  TYR   A OH  
442  N N   . TYR   A 58  ? 0.5045 0.2955 0.3487 0.0405  -0.1925 -0.0135 64  TYR   A N   
443  C CA  . TYR   A 58  ? 0.5444 0.2957 0.3633 0.0389  -0.2148 -0.0114 64  TYR   A CA  
444  C C   . TYR   A 58  ? 0.5752 0.2913 0.3394 0.0418  -0.2122 -0.0104 64  TYR   A C   
445  O O   . TYR   A 58  ? 0.5596 0.2799 0.3288 0.0459  -0.2076 -0.0127 64  TYR   A O   
446  C CB  . TYR   A 58  ? 0.5380 0.2836 0.4009 0.0356  -0.2392 -0.0103 64  TYR   A CB  
447  C CG  . TYR   A 58  ? 0.5827 0.2812 0.4160 0.0278  -0.2723 -0.0023 64  TYR   A CG  
448  C CD1 . TYR   A 58  ? 0.6109 0.2882 0.4213 0.0217  -0.2832 0.0026  64  TYR   A CD1 
449  C CD2 . TYR   A 58  ? 0.6200 0.2871 0.4354 0.0228  -0.2949 0.0018  64  TYR   A CD2 
450  C CE1 . TYR   A 58  ? 0.6647 0.2889 0.4349 0.0090  -0.3176 0.0121  64  TYR   A CE1 
451  C CE2 . TYR   A 58  ? 0.6724 0.2829 0.4435 0.0086  -0.3305 0.0117  64  TYR   A CE2 
452  C CZ  . TYR   A 58  ? 0.7072 0.2947 0.4534 0.0009  -0.3422 0.0171  64  TYR   A CZ  
453  O OH  . TYR   A 58  ? 0.7785 0.3008 0.4693 -0.0182 -0.3807 0.0286  64  TYR   A OH  
454  N N   . CYS   A 59  ? 0.6187 0.2929 0.3261 0.0383  -0.2126 -0.0075 65  CYS   A N   
455  C CA  . CYS   A 59  ? 0.6839 0.3067 0.3240 0.0394  -0.2009 -0.0079 65  CYS   A CA  
456  C C   . CYS   A 59  ? 0.7544 0.3061 0.3346 0.0241  -0.2339 -0.0063 65  CYS   A C   
457  O O   . CYS   A 59  ? 0.7741 0.2905 0.3127 0.0145  -0.2423 -0.0028 65  CYS   A O   
458  C CB  . CYS   A 59  ? 0.6998 0.3220 0.3152 0.0459  -0.1643 -0.0041 65  CYS   A CB  
459  S SG  . CYS   A 59  ? 0.7753 0.3152 0.2976 0.0472  -0.1361 -0.0055 65  CYS   A SG  
460  N N   . SER   A 60  ? 0.7770 0.3047 0.3508 0.0186  -0.2566 -0.0064 66  SER   A N   
461  C CA  . SER   A 60  ? 0.8352 0.2940 0.3576 -0.0020 -0.2993 0.0006  66  SER   A CA  
462  C C   . SER   A 60  ? 0.9246 0.2916 0.3283 -0.0147 -0.2910 -0.0008 66  SER   A C   
463  O O   . SER   A 60  ? 0.9688 0.2763 0.3211 -0.0370 -0.3276 0.0076  66  SER   A O   
464  C CB  . SER   A 60  ? 0.8475 0.3022 0.3937 -0.0073 -0.3272 0.0042  66  SER   A CB  
465  O OG  . SER   A 60  ? 0.9154 0.3233 0.3946 -0.0069 -0.3107 -0.0022 66  SER   A OG  
466  N N   . SER   A 61  ? 0.9470 0.2988 0.3088 -0.0018 -0.2410 -0.0093 67  SER   A N   
467  C CA  . SER   A 61  ? 1.0190 0.2762 0.2644 -0.0115 -0.2166 -0.0124 67  SER   A CA  
468  C C   . SER   A 61  ? 1.0285 0.2748 0.2495 -0.0175 -0.2094 -0.0090 67  SER   A C   
469  O O   . SER   A 61  ? 1.0907 0.2459 0.2051 -0.0322 -0.1968 -0.0105 67  SER   A O   
470  C CB  . SER   A 61  ? 1.0428 0.2927 0.2713 0.0079  -0.1572 -0.0195 67  SER   A CB  
471  O OG  . SER   A 61  ? 1.0034 0.3430 0.3212 0.0308  -0.1225 -0.0167 67  SER   A OG  
472  N N   . ARG   A 62  ? 0.9568 0.2881 0.2685 -0.0076 -0.2148 -0.0051 68  ARG   A N   
473  C CA  . ARG   A 62  ? 0.9710 0.3001 0.2705 -0.0137 -0.2139 -0.0008 68  ARG   A CA  
474  C C   . ARG   A 62  ? 0.9686 0.3266 0.3218 -0.0249 -0.2669 0.0071  68  ARG   A C   
475  O O   . ARG   A 62  ? 0.9767 0.3330 0.3243 -0.0315 -0.2735 0.0117  68  ARG   A O   
476  C CB  . ARG   A 62  ? 0.9316 0.3329 0.2922 0.0072  -0.1688 -0.0002 68  ARG   A CB  
477  C CG  . ARG   A 62  ? 0.9613 0.3409 0.2901 0.0201  -0.1116 -0.0015 68  ARG   A CG  
478  C CD  . ARG   A 62  ? 1.0489 0.3525 0.2876 0.0097  -0.0871 -0.0005 68  ARG   A CD  
479  N NE  . ARG   A 62  ? 1.0888 0.3626 0.3006 0.0237  -0.0231 -0.0003 68  ARG   A NE  
480  C CZ  . ARG   A 62  ? 1.1477 0.3395 0.2807 0.0213  -0.0005 -0.0078 68  ARG   A CZ  
481  N NH1 . ARG   A 62  ? 1.1775 0.3079 0.2447 0.0019  -0.0441 -0.0149 68  ARG   A NH1 
482  N NH2 . ARG   A 62  ? 1.1550 0.3244 0.2796 0.0379  0.0660  -0.0059 68  ARG   A NH2 
483  N N   . ARG   A 63  ? 0.9504 0.3385 0.3655 -0.0251 -0.3001 0.0101  69  ARG   A N   
484  C CA  . ARG   A 63  ? 0.9272 0.3521 0.4201 -0.0301 -0.3406 0.0197  69  ARG   A CA  
485  C C   . ARG   A 63  ? 0.8846 0.3773 0.4416 -0.0162 -0.3174 0.0169  69  ARG   A C   
486  O O   . ARG   A 63  ? 0.8914 0.3849 0.4687 -0.0236 -0.3391 0.0243  69  ARG   A O   
487  C CB  . ARG   A 63  ? 0.9923 0.3463 0.4364 -0.0575 -0.3931 0.0343  69  ARG   A CB  
488  C CG  . ARG   A 63  ? 1.0838 0.3842 0.4969 -0.0754 -0.4327 0.0431  69  ARG   A CG  
489  C CD  . ARG   A 63  ? 1.1867 0.4350 0.5879 -0.1050 -0.4979 0.0658  69  ARG   A CD  
490  N NE  . ARG   A 63  ? 1.3478 0.4929 0.6380 -0.1354 -0.5318 0.0737  69  ARG   A NE  
491  C CZ  . ARG   A 63  ? 1.4862 0.5329 0.6621 -0.1672 -0.5594 0.0823  69  ARG   A CZ  
492  N NH1 . ARG   A 63  ? 1.4934 0.5385 0.6592 -0.1704 -0.5574 0.0846  69  ARG   A NH1 
493  N NH2 . ARG   A 63  ? 1.5813 0.5228 0.6439 -0.1990 -0.5903 0.0891  69  ARG   A NH2 
494  N N   . LYS   A 64  ? 0.8365 0.3786 0.4181 0.0012  -0.2747 0.0082  70  LYS   A N   
495  C CA  . LYS   A 64  ? 0.7875 0.3831 0.4117 0.0095  -0.2521 0.0072  70  LYS   A CA  
496  C C   . LYS   A 64  ? 0.7192 0.3769 0.4052 0.0219  -0.2302 0.0024  70  LYS   A C   
497  O O   . LYS   A 64  ? 0.7244 0.3867 0.4033 0.0288  -0.2132 -0.0002 70  LYS   A O   
498  C CB  . LYS   A 64  ? 0.8262 0.4043 0.3956 0.0112  -0.2196 0.0083  70  LYS   A CB  
499  C CG  . LYS   A 64  ? 0.8945 0.4595 0.4445 0.0024  -0.2264 0.0133  70  LYS   A CG  
500  C CD  . LYS   A 64  ? 0.9943 0.5365 0.4916 0.0038  -0.1904 0.0162  70  LYS   A CD  
501  C CE  . LYS   A 64  ? 1.0974 0.5854 0.5328 -0.0116 -0.2033 0.0202  70  LYS   A CE  
502  N NZ  . LYS   A 64  ? 1.2002 0.6030 0.5540 -0.0279 -0.2276 0.0191  70  LYS   A NZ  
503  N N   . HIS   A 65  ? 0.6588 0.3568 0.3954 0.0225  -0.2276 0.0020  71  HIS   A N   
504  C CA  . HIS   A 65  ? 0.6065 0.3517 0.3848 0.0272  -0.2072 -0.0013 71  HIS   A CA  
505  C C   . HIS   A 65  ? 0.5978 0.3605 0.3591 0.0265  -0.1850 0.0053  71  HIS   A C   
506  O O   . HIS   A 65  ? 0.6089 0.3607 0.3512 0.0218  -0.1869 0.0096  71  HIS   A O   
507  C CB  . HIS   A 65  ? 0.5842 0.3453 0.4095 0.0239  -0.2121 -0.0045 71  HIS   A CB  
508  C CG  . HIS   A 65  ? 0.6009 0.3522 0.4664 0.0253  -0.2306 -0.0055 71  HIS   A CG  
509  N ND1 . HIS   A 65  ? 0.6059 0.3756 0.5093 0.0290  -0.2217 -0.0104 71  HIS   A ND1 
510  C CD2 . HIS   A 65  ? 0.6194 0.3450 0.4984 0.0219  -0.2589 0.0016  71  HIS   A CD2 
511  C CE1 . HIS   A 65  ? 0.5987 0.3570 0.5446 0.0294  -0.2416 -0.0056 71  HIS   A CE1 
512  N NE2 . HIS   A 65  ? 0.6106 0.3426 0.5458 0.0245  -0.2676 0.0034  71  HIS   A NE2 
513  N N   . TYR   A 66  ? 0.5753 0.3650 0.3487 0.0302  -0.1663 0.0093  72  TYR   A N   
514  C CA  . TYR   A 66  ? 0.5554 0.3669 0.3305 0.0289  -0.1477 0.0228  72  TYR   A CA  
515  C C   . TYR   A 66  ? 0.5234 0.3731 0.3324 0.0200  -0.1455 0.0295  72  TYR   A C   
516  O O   . TYR   A 66  ? 0.4899 0.3520 0.3162 0.0207  -0.1450 0.0267  72  TYR   A O   
517  C CB  . TYR   A 66  ? 0.5528 0.3557 0.3159 0.0397  -0.1263 0.0298  72  TYR   A CB  
518  C CG  . TYR   A 66  ? 0.6002 0.3517 0.3095 0.0434  -0.1191 0.0270  72  TYR   A CG  
519  C CD1 . TYR   A 66  ? 0.6260 0.3642 0.3128 0.0395  -0.1105 0.0341  72  TYR   A CD1 
520  C CD2 . TYR   A 66  ? 0.6464 0.3552 0.3187 0.0482  -0.1191 0.0185  72  TYR   A CD2 
521  C CE1 . TYR   A 66  ? 0.6846 0.3636 0.3079 0.0391  -0.1010 0.0313  72  TYR   A CE1 
522  C CE2 . TYR   A 66  ? 0.7041 0.3493 0.3079 0.0463  -0.1108 0.0162  72  TYR   A CE2 
523  C CZ  . TYR   A 66  ? 0.7348 0.3631 0.3117 0.0412  -0.1010 0.0221  72  TYR   A CZ  
524  O OH  . TYR   A 66  ? 0.8182 0.3717 0.3138 0.0352  -0.0916 0.0191  72  TYR   A OH  
525  N N   . PRO   A 67  ? 0.5211 0.3854 0.3338 0.0087  -0.1452 0.0414  73  PRO   A N   
526  C CA  . PRO   A 67  ? 0.5021 0.3921 0.3343 -0.0068 -0.1479 0.0529  73  PRO   A CA  
527  C C   . PRO   A 67  ? 0.4775 0.3940 0.3391 -0.0023 -0.1377 0.0737  73  PRO   A C   
528  O O   . PRO   A 67  ? 0.4800 0.3967 0.3472 0.0098  -0.1218 0.0841  73  PRO   A O   
529  C CB  . PRO   A 67  ? 0.5184 0.4074 0.3397 -0.0223 -0.1545 0.0618  73  PRO   A CB  
530  C CG  . PRO   A 67  ? 0.5348 0.4111 0.3425 -0.0112 -0.1487 0.0626  73  PRO   A CG  
531  C CD  . PRO   A 67  ? 0.5291 0.3817 0.3230 0.0060  -0.1453 0.0468  73  PRO   A CD  
532  N N   . VAL   A 68  ? 0.4394 0.3728 0.3198 -0.0120 -0.1439 0.0804  74  VAL   A N   
533  C CA  . VAL   A 68  ? 0.4119 0.3712 0.3313 -0.0083 -0.1378 0.1022  74  VAL   A CA  
534  C C   . VAL   A 68  ? 0.4080 0.3843 0.3426 -0.0339 -0.1568 0.1208  74  VAL   A C   
535  O O   . VAL   A 68  ? 0.4259 0.3840 0.3290 -0.0514 -0.1688 0.1070  74  VAL   A O   
536  C CB  . VAL   A 68  ? 0.4222 0.3727 0.3433 0.0115  -0.1265 0.0884  74  VAL   A CB  
537  C CG1 . VAL   A 68  ? 0.4527 0.3790 0.3563 0.0334  -0.1059 0.0804  74  VAL   A CG1 
538  C CG2 . VAL   A 68  ? 0.4258 0.3600 0.3243 0.0069  -0.1376 0.0640  74  VAL   A CG2 
539  N N   . SER   A 69  ? 0.3892 0.3955 0.3736 -0.0368 -0.1579 0.1538  75  SER   A N   
540  C CA  . SER   A 69  ? 0.3896 0.4097 0.3923 -0.0641 -0.1825 0.1782  75  SER   A CA  
541  C C   . SER   A 69  ? 0.3709 0.4016 0.4028 -0.0484 -0.1737 0.1785  75  SER   A C   
542  O O   . SER   A 69  ? 0.3509 0.3924 0.4175 -0.0211 -0.1489 0.1830  75  SER   A O   
543  C CB  . SER   A 69  ? 0.3865 0.4373 0.4430 -0.0796 -0.1955 0.2234  75  SER   A CB  
544  O OG  . SER   A 69  ? 0.4530 0.4876 0.4709 -0.1054 -0.2139 0.2252  75  SER   A OG  
545  N N   . PHE   A 70  ? 0.3809 0.4021 0.3940 -0.0659 -0.1905 0.1737  76  PHE   A N   
546  C CA  . PHE   A 70  ? 0.3899 0.4197 0.4288 -0.0512 -0.1834 0.1730  76  PHE   A CA  
547  C C   . PHE   A 70  ? 0.4091 0.4512 0.4720 -0.0786 -0.2108 0.2026  76  PHE   A C   
548  O O   . PHE   A 70  ? 0.4403 0.4718 0.4791 -0.1149 -0.2385 0.2180  76  PHE   A O   
549  C CB  . PHE   A 70  ? 0.4049 0.4072 0.3986 -0.0368 -0.1714 0.1320  76  PHE   A CB  
550  C CG  . PHE   A 70  ? 0.4202 0.3933 0.3596 -0.0592 -0.1816 0.1103  76  PHE   A CG  
551  C CD1 . PHE   A 70  ? 0.4358 0.3880 0.3419 -0.0583 -0.1751 0.0902  76  PHE   A CD1 
552  C CD2 . PHE   A 70  ? 0.4314 0.3924 0.3527 -0.0810 -0.1938 0.1105  76  PHE   A CD2 
553  C CE1 . PHE   A 70  ? 0.4673 0.3871 0.3294 -0.0758 -0.1751 0.0704  76  PHE   A CE1 
554  C CE2 . PHE   A 70  ? 0.4663 0.3902 0.3336 -0.1005 -0.1924 0.0888  76  PHE   A CE2 
555  C CZ  . PHE   A 70  ? 0.4733 0.3767 0.3145 -0.0965 -0.1804 0.0689  76  PHE   A CZ  
556  N N   . SER   A 71  ? 0.3908 0.4508 0.5005 -0.0638 -0.2048 0.2149  77  SER   A N   
557  C CA  . SER   A 71  ? 0.3898 0.4622 0.5302 -0.0901 -0.2346 0.2478  77  SER   A CA  
558  C C   . SER   A 71  ? 0.4259 0.4656 0.5015 -0.1120 -0.2493 0.2246  77  SER   A C   
559  O O   . SER   A 71  ? 0.4451 0.4577 0.4649 -0.1030 -0.2326 0.1843  77  SER   A O   
560  C CB  . SER   A 71  ? 0.3701 0.4745 0.5965 -0.0655 -0.2209 0.2747  77  SER   A CB  
561  O OG  . SER   A 71  ? 0.3980 0.4886 0.6073 -0.0401 -0.1991 0.2452  77  SER   A OG  
562  N N   . LYS   A 72  ? 0.4391 0.4787 0.5243 -0.1437 -0.2814 0.2536  78  LYS   A N   
563  C CA  . LYS   A 72  ? 0.4977 0.5012 0.5205 -0.1697 -0.2950 0.2375  78  LYS   A CA  
564  C C   . LYS   A 72  ? 0.5049 0.5185 0.5511 -0.1399 -0.2761 0.2207  78  LYS   A C   
565  O O   . LYS   A 72  ? 0.4754 0.5224 0.5930 -0.1108 -0.2643 0.2368  78  LYS   A O   
566  C CB  . LYS   A 72  ? 0.5328 0.5243 0.5496 -0.2211 -0.3424 0.2799  78  LYS   A CB  
567  C CG  . LYS   A 72  ? 0.6037 0.5873 0.6072 -0.2514 -0.3660 0.3047  78  LYS   A CG  
568  C CD  . LYS   A 72  ? 0.7176 0.6494 0.6483 -0.3154 -0.4114 0.3266  78  LYS   A CD  
569  C CE  . LYS   A 72  ? 0.8396 0.7025 0.6525 -0.3334 -0.3939 0.2807  78  LYS   A CE  
570  N NZ  . LYS   A 72  ? 0.9056 0.7111 0.6460 -0.3925 -0.4324 0.3001  78  LYS   A NZ  
571  N N   . PRO   A 73  ? 0.5413 0.5223 0.5275 -0.1451 -0.2679 0.1871  79  PRO   A N   
572  C CA  . PRO   A 73  ? 0.5512 0.5393 0.5559 -0.1185 -0.2522 0.1706  79  PRO   A CA  
573  C C   . PRO   A 73  ? 0.5401 0.5520 0.6033 -0.1213 -0.2709 0.2058  79  PRO   A C   
574  O O   . PRO   A 73  ? 0.5482 0.5498 0.6006 -0.1593 -0.3035 0.2312  79  PRO   A O   
575  C CB  . PRO   A 73  ? 0.5945 0.5418 0.5284 -0.1363 -0.2470 0.1392  79  PRO   A CB  
576  C CG  . PRO   A 73  ? 0.6243 0.5419 0.5042 -0.1567 -0.2436 0.1274  79  PRO   A CG  
577  C CD  . PRO   A 73  ? 0.5823 0.5144 0.4831 -0.1754 -0.2683 0.1637  79  PRO   A CD  
578  N N   . SER   A 74  ? 0.5185 0.5553 0.6405 -0.0829 -0.2502 0.2088  80  SER   A N   
579  C CA  . SER   A 74  ? 0.5001 0.5607 0.6925 -0.0799 -0.2617 0.2448  80  SER   A CA  
580  C C   . SER   A 74  ? 0.4916 0.5550 0.7131 -0.0389 -0.2309 0.2306  80  SER   A C   
581  O O   . SER   A 74  ? 0.4953 0.5404 0.6782 -0.0150 -0.2046 0.1942  80  SER   A O   
582  C CB  . SER   A 74  ? 0.4967 0.5895 0.7641 -0.0837 -0.2718 0.2907  80  SER   A CB  
583  O OG  . SER   A 74  ? 0.5278 0.6315 0.8225 -0.0462 -0.2334 0.2813  80  SER   A OG  
584  N N   . LEU   A 75  ? 0.4757 0.5566 0.7632 -0.0345 -0.2379 0.2621  81  LEU   A N   
585  C CA  . LEU   A 75  ? 0.4792 0.5566 0.7985 0.0010  -0.2092 0.2562  81  LEU   A CA  
586  C C   . LEU   A 75  ? 0.4726 0.5611 0.8497 0.0337  -0.1718 0.2704  81  LEU   A C   
587  O O   . LEU   A 75  ? 0.4525 0.5717 0.9070 0.0277  -0.1793 0.3134  81  LEU   A O   
588  C CB  . LEU   A 75  ? 0.4531 0.5455 0.8315 -0.0109 -0.2329 0.2921  81  LEU   A CB  
589  C CG  . LEU   A 75  ? 0.4886 0.5605 0.8135 -0.0304 -0.2545 0.2740  81  LEU   A CG  
590  C CD1 . LEU   A 75  ? 0.4773 0.5650 0.8612 -0.0510 -0.2874 0.3174  81  LEU   A CD1 
591  C CD2 . LEU   A 75  ? 0.5109 0.5582 0.8015 0.0013  -0.2233 0.2358  81  LEU   A CD2 
592  N N   . ILE   A 76  ? 0.4881 0.5473 0.8280 0.0652  -0.1325 0.2379  82  ILE   A N   
593  C CA  . ILE   A 76  ? 0.4855 0.5403 0.8627 0.0948  -0.0892 0.2473  82  ILE   A CA  
594  C C   . ILE   A 76  ? 0.5272 0.5397 0.8852 0.1267  -0.0489 0.2280  82  ILE   A C   
595  O O   . ILE   A 76  ? 0.5648 0.5429 0.8457 0.1274  -0.0526 0.1914  82  ILE   A O   
596  C CB  . ILE   A 76  ? 0.5038 0.5493 0.8297 0.0931  -0.0817 0.2265  82  ILE   A CB  
597  C CG1 . ILE   A 76  ? 0.4941 0.5772 0.8499 0.0633  -0.1148 0.2538  82  ILE   A CG1 
598  C CG2 . ILE   A 76  ? 0.5088 0.5272 0.8367 0.1248  -0.0296 0.2217  82  ILE   A CG2 
599  C CD1 . ILE   A 76  ? 0.5313 0.6038 0.8231 0.0522  -0.1216 0.2290  82  ILE   A CD1 
600  N N   . PHE   A 77  ? 0.5170 0.5272 0.9453 0.1520  -0.0089 0.2542  83  PHE   A N   
601  C CA  . PHE   A 77  ? 0.5670 0.5221 0.9668 0.1815  0.0371  0.2360  83  PHE   A CA  
602  C C   . PHE   A 77  ? 0.6328 0.5296 0.9287 0.1912  0.0633  0.1951  83  PHE   A C   
603  O O   . PHE   A 77  ? 0.6356 0.5343 0.9261 0.1923  0.0775  0.1962  83  PHE   A O   
604  C CB  . PHE   A 77  ? 0.5399 0.4982 1.0409 0.2081  0.0860  0.2742  83  PHE   A CB  
605  C CG  . PHE   A 77  ? 0.5825 0.4733 1.0507 0.2367  0.1368  0.2570  83  PHE   A CG  
606  C CD1 . PHE   A 77  ? 0.5936 0.4737 1.0557 0.2356  0.1203  0.2523  83  PHE   A CD1 
607  C CD2 . PHE   A 77  ? 0.6254 0.4546 1.0583 0.2619  0.2023  0.2448  83  PHE   A CD2 
608  C CE1 . PHE   A 77  ? 0.6390 0.4485 1.0614 0.2597  0.1666  0.2358  83  PHE   A CE1 
609  C CE2 . PHE   A 77  ? 0.6708 0.4224 1.0585 0.2846  0.2520  0.2285  83  PHE   A CE2 
610  C CZ  . PHE   A 77  ? 0.6721 0.4141 1.0530 0.2833  0.2325  0.2233  83  PHE   A CZ  
611  N N   . VAL   A 78  ? 0.6821 0.5250 0.8947 0.1949  0.0649  0.1616  84  VAL   A N   
612  C CA  . VAL   A 78  ? 0.7490 0.5255 0.8562 0.1989  0.0812  0.1260  84  VAL   A CA  
613  C C   . VAL   A 78  ? 0.8018 0.5022 0.8677 0.2195  0.1245  0.1161  84  VAL   A C   
614  O O   . VAL   A 78  ? 0.8029 0.4974 0.8733 0.2200  0.1131  0.1149  84  VAL   A O   
615  C CB  . VAL   A 78  ? 0.7756 0.5542 0.8153 0.1760  0.0316  0.0972  84  VAL   A CB  
616  C CG1 . VAL   A 78  ? 0.8388 0.5430 0.7738 0.1771  0.0406  0.0661  84  VAL   A CG1 
617  C CG2 . VAL   A 78  ? 0.7502 0.5900 0.8211 0.1562  -0.0018 0.1052  84  VAL   A CG2 
618  N N   . GLU   A 79  ? 0.8430 0.4798 0.8664 0.2353  0.1774  0.1102  85  GLU   A N   
619  C CA  . GLU   A 79  ? 0.9062 0.4498 0.8719 0.2534  0.2296  0.0992  85  GLU   A CA  
620  C C   . GLU   A 79  ? 0.9753 0.4534 0.8247 0.2389  0.2004  0.0654  85  GLU   A C   
621  O O   . GLU   A 79  ? 0.9863 0.4767 0.7872 0.2176  0.1515  0.0479  85  GLU   A O   
622  C CB  . GLU   A 79  ? 0.9824 0.4613 0.9091 0.2673  0.2934  0.0976  85  GLU   A CB  
623  C CG  . GLU   A 79  ? 1.0942 0.5051 1.0333 0.2948  0.3705  0.1076  85  GLU   A CG  
624  C CD  . GLU   A 79  ? 1.2622 0.5924 1.1493 0.3077  0.4440  0.1036  85  GLU   A CD  
625  O OE1 . GLU   A 79  ? 1.3083 0.5736 1.2046 0.3316  0.5186  0.1117  85  GLU   A OE1 
626  O OE2 . GLU   A 79  ? 1.3241 0.6511 1.1599 0.2938  0.4305  0.0926  85  GLU   A OE2 
627  N N   . ALA   A 80  ? 1.0129 0.4236 0.8267 0.2500  0.2290  0.0597  86  ALA   A N   
628  C CA  . ALA   A 80  ? 1.0836 0.4252 0.7905 0.2353  0.2017  0.0327  86  ALA   A CA  
629  C C   . ALA   A 80  ? 1.1573 0.4234 0.7354 0.2157  0.1866  0.0065  86  ALA   A C   
630  O O   . ALA   A 80  ? 1.2092 0.4088 0.7307 0.2209  0.2314  0.0020  86  ALA   A O   
631  C CB  . ALA   A 80  ? 1.1218 0.3815 0.7991 0.2525  0.2508  0.0319  86  ALA   A CB  
632  N N   . SER   A 81  ? 1.1613 0.4313 0.6940 0.1919  0.1250  -0.0082 87  SER   A N   
633  C CA  . SER   A 81  ? 1.2197 0.4199 0.6394 0.1685  0.0971  -0.0274 87  SER   A CA  
634  C C   . SER   A 81  ? 1.2748 0.4014 0.6078 0.1507  0.0653  -0.0409 87  SER   A C   
635  O O   . SER   A 81  ? 1.2627 0.3947 0.6230 0.1588  0.0694  -0.0376 87  SER   A O   
636  C CB  . SER   A 81  ? 1.1855 0.4707 0.6527 0.1538  0.0454  -0.0257 87  SER   A CB  
637  O OG  . SER   A 81  ? 1.1659 0.5146 0.6828 0.1434  -0.0047 -0.0248 87  SER   A OG  
638  N N   . GLU   A 82  ? 1.3305 0.3876 0.5616 0.1240  0.0294  -0.0530 88  GLU   A N   
639  C CA  . GLU   A 82  ? 1.3762 0.3681 0.5310 0.1012  -0.0127 -0.0606 88  GLU   A CA  
640  C C   . GLU   A 82  ? 1.2892 0.3842 0.5375 0.0936  -0.0711 -0.0539 88  GLU   A C   
641  O O   . GLU   A 82  ? 1.3159 0.3789 0.5317 0.0787  -0.1041 -0.0557 88  GLU   A O   
642  C CB  . GLU   A 82  ? 1.4975 0.3821 0.5198 0.0693  -0.0419 -0.0688 88  GLU   A CB  
643  C CG  . GLU   A 82  ? 1.5585 0.4907 0.6069 0.0601  -0.0676 -0.0651 88  GLU   A CG  
644  C CD  . GLU   A 82  ? 1.7559 0.5706 0.6681 0.0292  -0.0879 -0.0700 88  GLU   A CD  
645  O OE1 . GLU   A 82  ? 1.8724 0.5670 0.6631 0.0065  -0.0992 -0.0753 88  GLU   A OE1 
646  O OE2 . GLU   A 82  ? 1.7709 0.6081 0.6923 0.0246  -0.0952 -0.0674 88  GLU   A OE2 
647  N N   . TYR   A 83  ? 1.1879 0.3988 0.5464 0.1022  -0.0809 -0.0457 89  TYR   A N   
648  C CA  . TYR   A 83  ? 1.1049 0.4081 0.5488 0.0950  -0.1248 -0.0403 89  TYR   A CA  
649  C C   . TYR   A 83  ? 1.0181 0.3932 0.5509 0.1128  -0.1054 -0.0316 89  TYR   A C   
650  O O   . TYR   A 83  ? 0.9811 0.4002 0.5567 0.1054  -0.1346 -0.0292 89  TYR   A O   
651  C CB  . TYR   A 83  ? 1.0664 0.4369 0.5614 0.0884  -0.1473 -0.0374 89  TYR   A CB  
652  C CG  . TYR   A 83  ? 1.1281 0.4353 0.5477 0.0718  -0.1653 -0.0416 89  TYR   A CG  
653  C CD1 . TYR   A 83  ? 1.1620 0.4337 0.5458 0.0467  -0.2171 -0.0404 89  TYR   A CD1 
654  C CD2 . TYR   A 83  ? 1.1602 0.4426 0.5486 0.0790  -0.1335 -0.0433 89  TYR   A CD2 
655  C CE1 . TYR   A 83  ? 1.2150 0.4249 0.5304 0.0271  -0.2410 -0.0396 89  TYR   A CE1 
656  C CE2 . TYR   A 83  ? 1.2168 0.4354 0.5294 0.0605  -0.1527 -0.0461 89  TYR   A CE2 
657  C CZ  . TYR   A 83  ? 1.2527 0.4339 0.5274 0.0335  -0.2088 -0.0436 89  TYR   A CZ  
658  O OH  . TYR   A 83  ? 1.3232 0.4399 0.5258 0.0113  -0.2350 -0.0418 89  TYR   A OH  
659  N N   . TYR   A 84  ? 0.9758 0.3644 0.5423 0.1342  -0.0582 -0.0237 90  TYR   A N   
660  C CA  . TYR   A 84  ? 0.9124 0.3696 0.5701 0.1475  -0.0463 -0.0091 90  TYR   A CA  
661  C C   . TYR   A 84  ? 0.9245 0.3458 0.5906 0.1710  0.0090  0.0005  90  TYR   A C   
662  O O   . TYR   A 84  ? 0.9535 0.3325 0.5898 0.1815  0.0486  0.0001  90  TYR   A O   
663  C CB  . TYR   A 84  ? 0.8411 0.3931 0.5839 0.1467  -0.0547 0.0029  90  TYR   A CB  
664  C CG  . TYR   A 84  ? 0.8091 0.4075 0.5650 0.1267  -0.0986 -0.0037 90  TYR   A CG  
665  C CD1 . TYR   A 84  ? 0.8097 0.4164 0.5548 0.1208  -0.1052 -0.0082 90  TYR   A CD1 
666  C CD2 . TYR   A 84  ? 0.7815 0.4175 0.5686 0.1147  -0.1287 -0.0037 90  TYR   A CD2 
667  C CE1 . TYR   A 84  ? 0.7922 0.4404 0.5598 0.1050  -0.1386 -0.0125 90  TYR   A CE1 
668  C CE2 . TYR   A 84  ? 0.7645 0.4396 0.5712 0.0983  -0.1588 -0.0087 90  TYR   A CE2 
669  C CZ  . TYR   A 84  ? 0.7713 0.4528 0.5714 0.0945  -0.1623 -0.0127 90  TYR   A CZ  
670  O OH  . TYR   A 84  ? 0.7502 0.4669 0.5769 0.0806  -0.1855 -0.0164 90  TYR   A OH  
671  N N   . PRO   A 85  ? 0.8893 0.3367 0.6125 0.1805  0.0156  0.0131  91  PRO   A N   
672  C CA  . PRO   A 85  ? 0.8859 0.3148 0.6504 0.2064  0.0723  0.0298  91  PRO   A CA  
673  C C   . PRO   A 85  ? 0.8310 0.3392 0.6941 0.2150  0.0854  0.0534  91  PRO   A C   
674  O O   . PRO   A 85  ? 0.7961 0.3702 0.6870 0.1991  0.0476  0.0546  91  PRO   A O   
675  C CB  . PRO   A 85  ? 0.8724 0.3177 0.6801 0.2095  0.0622  0.0396  91  PRO   A CB  
676  C CG  . PRO   A 85  ? 0.8415 0.3570 0.6724 0.1853  -0.0002 0.0366  91  PRO   A CG  
677  C CD  . PRO   A 85  ? 0.8486 0.3458 0.6104 0.1681  -0.0261 0.0159  91  PRO   A CD  
678  N N   . ALA   A 86  ? 0.8139 0.3140 0.7329 0.2389  0.1393  0.0742  92  ALA   A N   
679  C CA  . ALA   A 86  ? 0.7592 0.3351 0.7803 0.2447  0.1479  0.1026  92  ALA   A CA  
680  C C   . ALA   A 86  ? 0.6854 0.3560 0.7996 0.2301  0.0979  0.1256  92  ALA   A C   
681  O O   . ALA   A 86  ? 0.6741 0.3490 0.8214 0.2327  0.0909  0.1359  92  ALA   A O   
682  C CB  . ALA   A 86  ? 0.7551 0.3031 0.8334 0.2740  0.2179  0.1257  92  ALA   A CB  
683  N N   . ARG   A 87  ? 0.6350 0.3709 0.7771 0.2113  0.0616  0.1318  93  ARG   A N   
684  C CA  . ARG   A 87  ? 0.5705 0.3783 0.7728 0.1897  0.0124  0.1499  93  ARG   A CA  
685  C C   . ARG   A 87  ? 0.5282 0.3963 0.7760 0.1740  -0.0082 0.1679  93  ARG   A C   
686  O O   . ARG   A 87  ? 0.5449 0.4039 0.7814 0.1819  0.0152  0.1649  93  ARG   A O   
687  C CB  . ARG   A 87  ? 0.5914 0.3872 0.7198 0.1699  -0.0273 0.1196  93  ARG   A CB  
688  C CG  . ARG   A 87  ? 0.5934 0.3974 0.6691 0.1530  -0.0499 0.0973  93  ARG   A CG  
689  C CD  . ARG   A 87  ? 0.6373 0.3933 0.6270 0.1477  -0.0618 0.0647  93  ARG   A CD  
690  N NE  . ARG   A 87  ? 0.6280 0.4129 0.6011 0.1269  -0.0942 0.0517  93  ARG   A NE  
691  C CZ  . ARG   A 87  ? 0.6059 0.3878 0.5553 0.1249  -0.0922 0.0429  93  ARG   A CZ  
692  N NH1 . ARG   A 87  ? 0.5760 0.3828 0.5191 0.1075  -0.1179 0.0328  93  ARG   A NH1 
693  N NH2 . ARG   A 87  ? 0.5868 0.3374 0.5196 0.1404  -0.0608 0.0446  93  ARG   A NH2 
694  N N   . TYR   A 88  ? 0.4867 0.4075 0.7721 0.1480  -0.0533 0.1845  94  TYR   A N   
695  C CA  . TYR   A 88  ? 0.4605 0.4245 0.7631 0.1258  -0.0791 0.1963  94  TYR   A CA  
696  C C   . TYR   A 88  ? 0.4536 0.4086 0.6731 0.1049  -0.1067 0.1606  94  TYR   A C   
697  O O   . TYR   A 88  ? 0.4573 0.4066 0.6495 0.0922  -0.1285 0.1481  94  TYR   A O   
698  C CB  . TYR   A 88  ? 0.4366 0.4487 0.8131 0.1020  -0.1152 0.2364  94  TYR   A CB  
699  C CG  . TYR   A 88  ? 0.4278 0.4632 0.9142 0.1173  -0.0971 0.2832  94  TYR   A CG  
700  C CD1 . TYR   A 88  ? 0.4158 0.4851 0.9681 0.1139  -0.0954 0.3160  94  TYR   A CD1 
701  C CD2 . TYR   A 88  ? 0.4378 0.4650 0.9729 0.1323  -0.0856 0.2995  94  TYR   A CD2 
702  C CE1 . TYR   A 88  ? 0.3891 0.4866 1.0629 0.1261  -0.0814 0.3667  94  TYR   A CE1 
703  C CE2 . TYR   A 88  ? 0.4155 0.4669 1.0691 0.1471  -0.0677 0.3476  94  TYR   A CE2 
704  C CZ  . TYR   A 88  ? 0.3987 0.4871 1.1269 0.1443  -0.0653 0.3827  94  TYR   A CZ  
705  O OH  . TYR   A 88  ? 0.3896 0.5071 1.2542 0.1582  -0.0493 0.4373  94  TYR   A OH  
706  N N   . GLN   A 89  ? 0.4321 0.3853 0.6177 0.1020  -0.1035 0.1461  95  GLN   A N   
707  C CA  . GLN   A 89  ? 0.4238 0.3711 0.5483 0.0837  -0.1256 0.1173  95  GLN   A CA  
708  C C   . GLN   A 89  ? 0.3809 0.3638 0.5241 0.0544  -0.1529 0.1340  95  GLN   A C   
709  O O   . GLN   A 89  ? 0.3589 0.3634 0.5405 0.0523  -0.1508 0.1577  95  GLN   A O   
710  C CB  . GLN   A 89  ? 0.4614 0.3784 0.5350 0.0961  -0.1083 0.0924  95  GLN   A CB  
711  C CG  . GLN   A 89  ? 0.4617 0.3740 0.4882 0.0800  -0.1287 0.0666  95  GLN   A CG  
712  C CD  . GLN   A 89  ? 0.5175 0.3935 0.4970 0.0916  -0.1176 0.0460  95  GLN   A CD  
713  O OE1 . GLN   A 89  ? 0.5617 0.3954 0.5107 0.1066  -0.1031 0.0379  95  GLN   A OE1 
714  N NE2 . GLN   A 89  ? 0.4977 0.3816 0.4637 0.0821  -0.1258 0.0375  95  GLN   A NE2 
715  N N   . SER   A 90  ? 0.3706 0.3537 0.4848 0.0296  -0.1772 0.1239  96  SER   A N   
716  C CA  . SER   A 90  ? 0.3566 0.3546 0.4666 -0.0045 -0.2022 0.1375  96  SER   A CA  
717  C C   . SER   A 90  ? 0.3855 0.3716 0.4472 -0.0140 -0.1992 0.1133  96  SER   A C   
718  O O   . SER   A 90  ? 0.4132 0.3826 0.4478 0.0026  -0.1846 0.0854  96  SER   A O   
719  C CB  . SER   A 90  ? 0.3571 0.3493 0.4527 -0.0300 -0.2245 0.1408  96  SER   A CB  
720  O OG  . SER   A 90  ? 0.4061 0.3763 0.4566 -0.0267 -0.2163 0.1070  96  SER   A OG  
721  N N   . HIS   A 91  ? 0.3737 0.3645 0.4253 -0.0424 -0.2149 0.1266  97  HIS   A N   
722  C CA  . HIS   A 91  ? 0.3796 0.3551 0.3870 -0.0536 -0.2103 0.1068  97  HIS   A CA  
723  C C   . HIS   A 91  ? 0.3724 0.3533 0.3891 -0.0270 -0.1915 0.0980  97  HIS   A C   
724  O O   . HIS   A 91  ? 0.3762 0.3418 0.3621 -0.0235 -0.1820 0.0737  97  HIS   A O   
725  C CB  . HIS   A 91  ? 0.4015 0.3517 0.3663 -0.0598 -0.2029 0.0764  97  HIS   A CB  
726  C CG  . HIS   A 91  ? 0.4391 0.3749 0.3819 -0.0897 -0.2175 0.0831  97  HIS   A CG  
727  N ND1 . HIS   A 91  ? 0.4882 0.3961 0.3818 -0.1273 -0.2248 0.0844  97  HIS   A ND1 
728  C CD2 . HIS   A 91  ? 0.4480 0.3870 0.4050 -0.0897 -0.2260 0.0901  97  HIS   A CD2 
729  C CE1 . HIS   A 91  ? 0.4982 0.3906 0.3731 -0.1504 -0.2375 0.0916  97  HIS   A CE1 
730  N NE2 . HIS   A 91  ? 0.4783 0.3929 0.3949 -0.1284 -0.2403 0.0962  97  HIS   A NE2 
731  N N   . LEU   A 92  ? 0.3640 0.3632 0.4261 -0.0079 -0.1836 0.1189  98  LEU   A N   
732  C CA  . LEU   A 92  ? 0.3728 0.3686 0.4361 0.0161  -0.1621 0.1113  98  LEU   A CA  
733  C C   . LEU   A 92  ? 0.3601 0.3735 0.4418 0.0046  -0.1670 0.1327  98  LEU   A C   
734  O O   . LEU   A 92  ? 0.3339 0.3704 0.4608 -0.0088 -0.1808 0.1671  98  LEU   A O   
735  C CB  . LEU   A 92  ? 0.3627 0.3537 0.4547 0.0459  -0.1393 0.1174  98  LEU   A CB  
736  C CG  . LEU   A 92  ? 0.3921 0.3637 0.4722 0.0700  -0.1110 0.1092  98  LEU   A CG  
737  C CD1 . LEU   A 92  ? 0.4267 0.3669 0.4460 0.0726  -0.1123 0.0757  98  LEU   A CD1 
738  C CD2 . LEU   A 92  ? 0.3956 0.3502 0.4987 0.0958  -0.0815 0.1181  98  LEU   A CD2 
739  N N   . MET   A 93  ? 0.3638 0.3661 0.4151 0.0082  -0.1588 0.1158  99  MET   A N   
740  C CA  . MET   A 93  ? 0.3593 0.3761 0.4240 -0.0036 -0.1641 0.1352  99  MET   A CA  
741  C C   . MET   A 93  ? 0.3574 0.3726 0.4336 0.0219  -0.1386 0.1349  99  MET   A C   
742  O O   . MET   A 93  ? 0.3935 0.3830 0.4295 0.0359  -0.1265 0.1071  99  MET   A O   
743  C CB  . MET   A 93  ? 0.3866 0.3865 0.4011 -0.0280 -0.1773 0.1191  99  MET   A CB  
744  C CG  . MET   A 93  ? 0.4135 0.3999 0.4005 -0.0565 -0.1951 0.1166  99  MET   A CG  
745  S SD  . MET   A 93  ? 0.5135 0.4622 0.4334 -0.0780 -0.1926 0.0880  99  MET   A SD  
746  C CE  . MET   A 93  ? 0.4821 0.4238 0.4020 -0.0437 -0.1701 0.0555  99  MET   A CE  
747  N N   . LEU   A 94  ? 0.3282 0.3670 0.4601 0.0265  -0.1303 0.1676  100 LEU   A N   
748  C CA  . LEU   A 94  ? 0.3327 0.3624 0.4702 0.0499  -0.0987 0.1671  100 LEU   A CA  
749  C C   . LEU   A 94  ? 0.3265 0.3641 0.4570 0.0379  -0.1045 0.1738  100 LEU   A C   
750  O O   . LEU   A 94  ? 0.3058 0.3648 0.4531 0.0117  -0.1310 0.1945  100 LEU   A O   
751  C CB  . LEU   A 94  ? 0.3100 0.3516 0.5162 0.0711  -0.0691 0.1959  100 LEU   A CB  
752  C CG  . LEU   A 94  ? 0.3380 0.3608 0.5441 0.0884  -0.0547 0.1865  100 LEU   A CG  
753  C CD1 . LEU   A 94  ? 0.3212 0.3497 0.5990 0.1111  -0.0175 0.2157  100 LEU   A CD1 
754  C CD2 . LEU   A 94  ? 0.3854 0.3580 0.5129 0.1025  -0.0396 0.1467  100 LEU   A CD2 
755  N N   . ALA   A 95  ? 0.3436 0.3558 0.4404 0.0546  -0.0810 0.1559  101 ALA   A N   
756  C CA  . ALA   A 95  ? 0.3425 0.3552 0.4270 0.0483  -0.0806 0.1586  101 ALA   A CA  
757  C C   . ALA   A 95  ? 0.3478 0.3395 0.4321 0.0717  -0.0408 0.1603  101 ALA   A C   
758  O O   . ALA   A 95  ? 0.3593 0.3175 0.4209 0.0913  -0.0148 0.1466  101 ALA   A O   
759  C CB  . ALA   A 95  ? 0.3680 0.3568 0.3872 0.0381  -0.0987 0.1263  101 ALA   A CB  
760  N N   . VAL   A 96  ? 0.3509 0.3558 0.4553 0.0674  -0.0343 0.1782  102 VAL   A N   
761  C CA  . VAL   A 96  ? 0.3856 0.3638 0.4801 0.0856  0.0065  0.1791  102 VAL   A CA  
762  C C   . VAL   A 96  ? 0.4584 0.3911 0.4613 0.0829  -0.0026 0.1423  102 VAL   A C   
763  O O   . VAL   A 96  ? 0.4593 0.4020 0.4423 0.0654  -0.0338 0.1342  102 VAL   A O   
764  C CB  . VAL   A 96  ? 0.3547 0.3711 0.5189 0.0797  0.0145  0.2181  102 VAL   A CB  
765  C CG1 . VAL   A 96  ? 0.3713 0.3546 0.5156 0.0955  0.0596  0.2167  102 VAL   A CG1 
766  C CG2 . VAL   A 96  ? 0.2995 0.3608 0.5675 0.0815  0.0184  0.2602  102 VAL   A CG2 
767  N N   . GLY   A 97  ? 0.5104 0.3886 0.4573 0.0977  0.0204  0.1207  103 GLY   A N   
768  C CA  . GLY   A 97  ? 0.5719 0.4014 0.4366 0.0932  0.0066  0.0911  103 GLY   A CA  
769  C C   . GLY   A 97  ? 0.6335 0.3946 0.4327 0.1043  0.0274  0.0727  103 GLY   A C   
770  O O   . GLY   A 97  ? 0.6345 0.3890 0.4475 0.1151  0.0435  0.0745  103 GLY   A O   
771  N N   . HIS   A 98  ? 0.6847 0.3874 0.4061 0.0988  0.0251  0.0565  104 HIS   A N   
772  C CA  . HIS   A 98  ? 0.7445 0.3662 0.3828 0.1009  0.0365  0.0394  104 HIS   A CA  
773  C C   . HIS   A 98  ? 0.7444 0.3627 0.3710 0.0955  -0.0015 0.0242  104 HIS   A C   
774  O O   . HIS   A 98  ? 0.7124 0.3682 0.3651 0.0858  -0.0413 0.0193  104 HIS   A O   
775  C CB  . HIS   A 98  ? 0.8107 0.3666 0.3641 0.0891  0.0340  0.0298  104 HIS   A CB  
776  C CG  . HIS   A 98  ? 0.9171 0.3771 0.3683 0.0819  0.0328  0.0134  104 HIS   A CG  
777  N ND1 . HIS   A 98  ? 0.9909 0.3779 0.3837 0.0895  0.0841  0.0122  104 HIS   A ND1 
778  C CD2 . HIS   A 98  ? 0.9642 0.3881 0.3655 0.0658  -0.0144 0.0007  104 HIS   A CD2 
779  C CE1 . HIS   A 98  ? 1.0577 0.3600 0.3530 0.0747  0.0635  -0.0030 104 HIS   A CE1 
780  N NE2 . HIS   A 98  ? 1.0444 0.3698 0.3473 0.0596  0.0009  -0.0081 104 HIS   A NE2 
781  N N   . SER   A 99  ? 0.7735 0.3398 0.3585 0.1016  0.0154  0.0172  105 SER   A N   
782  C CA  . SER   A 99  ? 0.7959 0.3442 0.3591 0.0959  -0.0162 0.0045  105 SER   A CA  
783  C C   . SER   A 99  ? 0.8769 0.3326 0.3547 0.0975  0.0083  -0.0039 105 SER   A C   
784  O O   . SER   A 99  ? 0.8898 0.3112 0.3503 0.1096  0.0602  0.0013  105 SER   A O   
785  C CB  . SER   A 99  ? 0.7417 0.3635 0.3879 0.1021  -0.0275 0.0103  105 SER   A CB  
786  O OG  . SER   A 99  ? 0.7364 0.3826 0.4308 0.1174  0.0110  0.0257  105 SER   A OG  
787  N N   . GLU   A 100 ? 0.9293 0.3408 0.3553 0.0840  -0.0279 -0.0153 106 GLU   A N   
788  C CA  . GLU   A 100 ? 1.0208 0.3318 0.3492 0.0780  -0.0168 -0.0243 106 GLU   A CA  
789  C C   . GLU   A 100 ? 1.0220 0.3502 0.3728 0.0741  -0.0537 -0.0282 106 GLU   A C   
790  O O   . GLU   A 100 ? 0.9786 0.3846 0.4070 0.0727  -0.0886 -0.0253 106 GLU   A O   
791  C CB  . GLU   A 100 ? 1.1372 0.3552 0.3555 0.0540  -0.0364 -0.0301 106 GLU   A CB  
792  C CG  . GLU   A 100 ? 1.2913 0.4178 0.4183 0.0553  0.0216  -0.0327 106 GLU   A CG  
793  C CD  . GLU   A 100 ? 1.4082 0.4624 0.4427 0.0313  0.0061  -0.0347 106 GLU   A CD  
794  O OE1 . GLU   A 100 ? 1.5084 0.4710 0.4402 0.0036  -0.0315 -0.0397 106 GLU   A OE1 
795  O OE2 . GLU   A 100 ? 1.3816 0.4684 0.4453 0.0376  0.0279  -0.0287 106 GLU   A OE2 
796  N N   . PRO   A 101 ? 1.0669 0.3235 0.3534 0.0721  -0.0442 -0.0345 107 PRO   A N   
797  C CA  . PRO   A 101 ? 1.0370 0.3188 0.3556 0.0689  -0.0789 -0.0361 107 PRO   A CA  
798  C C   . PRO   A 101 ? 1.0149 0.3142 0.3484 0.0481  -0.1446 -0.0348 107 PRO   A C   
799  O O   . PRO   A 101 ? 0.9727 0.3368 0.3807 0.0508  -0.1678 -0.0325 107 PRO   A O   
800  C CB  . PRO   A 101 ? 1.1132 0.2937 0.3375 0.0664  -0.0561 -0.0432 107 PRO   A CB  
801  C CG  . PRO   A 101 ? 1.1545 0.2839 0.3351 0.0798  0.0110  -0.0438 107 PRO   A CG  
802  C CD  . PRO   A 101 ? 1.1331 0.2803 0.3159 0.0731  0.0048  -0.0403 107 PRO   A CD  
803  N N   . GLY   A 102 ? 1.0348 0.2817 0.3087 0.0278  -0.1722 -0.0335 108 GLY   A N   
804  C CA  . GLY   A 102 ? 0.9977 0.2671 0.3064 0.0095  -0.2334 -0.0261 108 GLY   A CA  
805  C C   . GLY   A 102 ? 0.9070 0.2797 0.3258 0.0202  -0.2390 -0.0220 108 GLY   A C   
806  O O   . GLY   A 102 ? 0.8752 0.2754 0.3431 0.0094  -0.2810 -0.0146 108 GLY   A O   
807  N N   . ASP   A 103 ? 0.8559 0.2841 0.3180 0.0403  -0.1958 -0.0244 109 ASP   A N   
808  C CA  . ASP   A 103 ? 0.7758 0.2882 0.3245 0.0469  -0.1981 -0.0212 109 ASP   A CA  
809  C C   . ASP   A 103 ? 0.7075 0.2902 0.3388 0.0535  -0.2033 -0.0212 109 ASP   A C   
810  O O   . ASP   A 103 ? 0.6721 0.3063 0.3634 0.0524  -0.2133 -0.0195 109 ASP   A O   
811  C CB  . ASP   A 103 ? 0.7712 0.3048 0.3246 0.0583  -0.1588 -0.0192 109 ASP   A CB  
812  C CG  . ASP   A 103 ? 0.8334 0.3135 0.3239 0.0474  -0.1633 -0.0184 109 ASP   A CG  
813  O OD1 . ASP   A 103 ? 0.8295 0.2970 0.3163 0.0324  -0.2036 -0.0164 109 ASP   A OD1 
814  O OD2 . ASP   A 103 ? 0.8883 0.3368 0.3363 0.0532  -0.1258 -0.0178 109 ASP   A OD2 
815  N N   . CYS   A 104 ? 0.6981 0.2751 0.3269 0.0584  -0.1963 -0.0233 110 CYS   A N   
816  C CA  . CYS   A 104 ? 0.6535 0.2857 0.3491 0.0613  -0.2027 -0.0234 110 CYS   A CA  
817  C C   . CYS   A 104 ? 0.6237 0.2825 0.3705 0.0512  -0.2348 -0.0215 110 CYS   A C   
818  O O   . CYS   A 104 ? 0.6524 0.2721 0.3790 0.0394  -0.2663 -0.0173 110 CYS   A O   
819  C CB  . CYS   A 104 ? 0.6771 0.2775 0.3450 0.0632  -0.2011 -0.0255 110 CYS   A CB  
820  S SG  . CYS   A 104 ? 0.7279 0.3194 0.3766 0.0811  -0.1522 -0.0243 110 CYS   A SG  
821  N N   . GLY   A 105 ? 0.5703 0.2889 0.3820 0.0540  -0.2257 -0.0222 111 GLY   A N   
822  C CA  . GLY   A 105 ? 0.5383 0.2795 0.4067 0.0472  -0.2439 -0.0202 111 GLY   A CA  
823  C C   . GLY   A 105 ? 0.5202 0.2786 0.4107 0.0461  -0.2397 -0.0196 111 GLY   A C   
824  O O   . GLY   A 105 ? 0.5071 0.2901 0.4532 0.0436  -0.2399 -0.0190 111 GLY   A O   
825  N N   . GLY   A 106 ? 0.5177 0.2604 0.3658 0.0481  -0.2316 -0.0195 112 GLY   A N   
826  C CA  . GLY   A 106 ? 0.4863 0.2443 0.3490 0.0467  -0.2262 -0.0189 112 GLY   A CA  
827  C C   . GLY   A 106 ? 0.4218 0.2241 0.3212 0.0473  -0.2032 -0.0224 112 GLY   A C   
828  O O   . GLY   A 106 ? 0.4030 0.2219 0.2956 0.0494  -0.1872 -0.0224 112 GLY   A O   
829  N N   . ILE   A 107 ? 0.3945 0.2092 0.3324 0.0433  -0.2022 -0.0239 113 ILE   A N   
830  C CA  . ILE   A 107 ? 0.3839 0.2225 0.3415 0.0383  -0.1798 -0.0285 113 ILE   A CA  
831  C C   . ILE   A 107 ? 0.3949 0.2421 0.3244 0.0338  -0.1676 -0.0263 113 ILE   A C   
832  O O   . ILE   A 107 ? 0.4047 0.2422 0.3184 0.0353  -0.1733 -0.0233 113 ILE   A O   
833  C CB  . ILE   A 107 ? 0.3759 0.2121 0.3842 0.0365  -0.1776 -0.0305 113 ILE   A CB  
834  C CG1 . ILE   A 107 ? 0.3641 0.2039 0.4132 0.0377  -0.1798 -0.0302 113 ILE   A CG1 
835  C CG2 . ILE   A 107 ? 0.3833 0.2218 0.3942 0.0289  -0.1518 -0.0364 113 ILE   A CG2 
836  C CD1 . ILE   A 107 ? 0.3434 0.1791 0.4618 0.0396  -0.1848 -0.0239 113 ILE   A CD1 
837  N N   . LEU   A 108 ? 0.3984 0.2615 0.3208 0.0259  -0.1544 -0.0250 114 LEU   A N   
838  C CA  . LEU   A 108 ? 0.4198 0.2917 0.3235 0.0148  -0.1470 -0.0183 114 LEU   A CA  
839  C C   . LEU   A 108 ? 0.4344 0.2943 0.3388 -0.0003 -0.1340 -0.0264 114 LEU   A C   
840  O O   . LEU   A 108 ? 0.4284 0.2823 0.3434 -0.0048 -0.1244 -0.0335 114 LEU   A O   
841  C CB  . LEU   A 108 ? 0.4232 0.3129 0.3211 0.0103  -0.1460 -0.0065 114 LEU   A CB  
842  C CG  . LEU   A 108 ? 0.4245 0.3245 0.3106 -0.0078 -0.1460 0.0082  114 LEU   A CG  
843  C CD1 . LEU   A 108 ? 0.4235 0.3287 0.3066 -0.0021 -0.1472 0.0182  114 LEU   A CD1 
844  C CD2 . LEU   A 108 ? 0.4154 0.3335 0.3111 -0.0148 -0.1504 0.0245  114 LEU   A CD2 
845  N N   . ARG   A 109 ? 0.4520 0.3017 0.3417 -0.0083 -0.1303 -0.0259 115 ARG   A N   
846  C CA  . ARG   A 109 ? 0.4765 0.3005 0.3564 -0.0226 -0.1121 -0.0350 115 ARG   A CA  
847  C C   . ARG   A 109 ? 0.5175 0.3315 0.3553 -0.0429 -0.1133 -0.0271 115 ARG   A C   
848  O O   . ARG   A 109 ? 0.4970 0.3271 0.3307 -0.0398 -0.1273 -0.0156 115 ARG   A O   
849  C CB  . ARG   A 109 ? 0.4938 0.3049 0.4069 -0.0099 -0.1073 -0.0424 115 ARG   A CB  
850  C CG  . ARG   A 109 ? 0.5531 0.3508 0.5084 -0.0049 -0.0881 -0.0516 115 ARG   A CG  
851  C CD  . ARG   A 109 ? 0.6001 0.3838 0.5986 0.0046  -0.0818 -0.0528 115 ARG   A CD  
852  N NE  . ARG   A 109 ? 0.6341 0.4030 0.6849 0.0087  -0.0538 -0.0582 115 ARG   A NE  
853  C CZ  . ARG   A 109 ? 0.6711 0.4558 0.7842 0.0209  -0.0629 -0.0523 115 ARG   A CZ  
854  N NH1 . ARG   A 109 ? 0.6708 0.4437 0.8417 0.0246  -0.0324 -0.0541 115 ARG   A NH1 
855  N NH2 . ARG   A 109 ? 0.6682 0.4754 0.7840 0.0279  -0.1003 -0.0434 115 ARG   A NH2 
856  N N   . CYS   A 110 ? 0.5640 0.3446 0.3659 -0.0662 -0.0977 -0.0324 116 CYS   A N   
857  C CA  . CYS   A 110 ? 0.6114 0.3660 0.3619 -0.0927 -0.0998 -0.0255 116 CYS   A CA  
858  C C   . CYS   A 110 ? 0.6744 0.3762 0.4034 -0.1004 -0.0687 -0.0436 116 CYS   A C   
859  O O   . CYS   A 110 ? 0.6708 0.3687 0.4419 -0.0815 -0.0481 -0.0567 116 CYS   A O   
860  C CB  . CYS   A 110 ? 0.6329 0.3805 0.3442 -0.1215 -0.1118 -0.0118 116 CYS   A CB  
861  S SG  . CYS   A 110 ? 0.6982 0.4065 0.3820 -0.1369 -0.0882 -0.0266 116 CYS   A SG  
862  N N   . GLN   A 111 ? 0.7284 0.3864 0.3964 -0.1280 -0.0641 -0.0422 117 GLN   A N   
863  C CA  . GLN   A 111 ? 0.7869 0.3837 0.4279 -0.1353 -0.0273 -0.0599 117 GLN   A CA  
864  C C   . GLN   A 111 ? 0.8154 0.3736 0.4488 -0.1398 0.0103  -0.0758 117 GLN   A C   
865  O O   . GLN   A 111 ? 0.8277 0.3498 0.4794 -0.1301 0.0501  -0.0910 117 GLN   A O   
866  C CB  . GLN   A 111 ? 0.8750 0.4182 0.4312 -0.1717 -0.0308 -0.0548 117 GLN   A CB  
867  C CG  . GLN   A 111 ? 0.9813 0.5087 0.4731 -0.2096 -0.0546 -0.0388 117 GLN   A CG  
868  C CD  . GLN   A 111 ? 1.1317 0.5922 0.5284 -0.2537 -0.0622 -0.0312 117 GLN   A CD  
869  O OE1 . GLN   A 111 ? 1.1755 0.6390 0.5364 -0.2850 -0.1003 -0.0062 117 GLN   A OE1 
870  N NE2 . GLN   A 111 ? 1.1749 0.5685 0.5289 -0.2598 -0.0272 -0.0497 117 GLN   A NE2 
871  N N   . HIS   A 112 ? 0.8140 0.3785 0.4250 -0.1544 -0.0004 -0.0703 118 HIS   A N   
872  C CA  . HIS   A 112 ? 0.8287 0.3548 0.4188 -0.1653 0.0314  -0.0826 118 HIS   A CA  
873  C C   . HIS   A 112 ? 0.7693 0.3348 0.4475 -0.1313 0.0457  -0.0897 118 HIS   A C   
874  O O   . HIS   A 112 ? 0.7985 0.3290 0.4744 -0.1353 0.0833  -0.1017 118 HIS   A O   
875  C CB  . HIS   A 112 ? 0.8720 0.3917 0.4035 -0.1973 0.0047  -0.0691 118 HIS   A CB  
876  C CG  . HIS   A 112 ? 0.9800 0.4505 0.4197 -0.2399 -0.0141 -0.0570 118 HIS   A CG  
877  N ND1 . HIS   A 112 ? 0.9988 0.5136 0.4465 -0.2471 -0.0627 -0.0309 118 HIS   A ND1 
878  C CD2 . HIS   A 112 ? 1.0651 0.4410 0.4039 -0.2785 0.0104  -0.0660 118 HIS   A CD2 
879  C CE1 . HIS   A 112 ? 1.0509 0.5031 0.4090 -0.2909 -0.0732 -0.0219 118 HIS   A CE1 
880  N NE2 . HIS   A 112 ? 1.1074 0.4699 0.3888 -0.3127 -0.0311 -0.0436 118 HIS   A NE2 
881  N N   . GLY   A 113 ? 0.6892 0.3218 0.4383 -0.1018 0.0153  -0.0805 119 GLY   A N   
882  C CA  . GLY   A 113 ? 0.6248 0.2922 0.4536 -0.0740 0.0188  -0.0828 119 GLY   A CA  
883  C C   . GLY   A 113 ? 0.5631 0.2892 0.4238 -0.0581 -0.0220 -0.0705 119 GLY   A C   
884  O O   . GLY   A 113 ? 0.5536 0.3026 0.3997 -0.0575 -0.0500 -0.0598 119 GLY   A O   
885  N N   . VAL   A 114 ? 0.5222 0.2684 0.4282 -0.0448 -0.0220 -0.0714 120 VAL   A N   
886  C CA  . VAL   A 114 ? 0.4939 0.2829 0.4231 -0.0305 -0.0550 -0.0619 120 VAL   A CA  
887  C C   . VAL   A 114 ? 0.4976 0.2929 0.3814 -0.0474 -0.0675 -0.0549 120 VAL   A C   
888  O O   . VAL   A 114 ? 0.5053 0.2790 0.3644 -0.0646 -0.0521 -0.0592 120 VAL   A O   
889  C CB  . VAL   A 114 ? 0.4762 0.2793 0.4700 -0.0128 -0.0545 -0.0630 120 VAL   A CB  
890  C CG1 . VAL   A 114 ? 0.4754 0.3078 0.4724 -0.0039 -0.0847 -0.0552 120 VAL   A CG1 
891  C CG2 . VAL   A 114 ? 0.4533 0.2578 0.5045 0.0035  -0.0567 -0.0605 120 VAL   A CG2 
892  N N   . VAL   A 115 ? 0.4812 0.3032 0.3572 -0.0432 -0.0937 -0.0421 121 VAL   A N   
893  C CA  . VAL   A 115 ? 0.4909 0.3246 0.3426 -0.0569 -0.1086 -0.0287 121 VAL   A CA  
894  C C   . VAL   A 115 ? 0.4867 0.3459 0.3681 -0.0405 -0.1196 -0.0254 121 VAL   A C   
895  O O   . VAL   A 115 ? 0.4965 0.3565 0.3682 -0.0520 -0.1230 -0.0204 121 VAL   A O   
896  C CB  . VAL   A 115 ? 0.4904 0.3392 0.3308 -0.0602 -0.1256 -0.0123 121 VAL   A CB  
897  C CG1 . VAL   A 115 ? 0.4878 0.3546 0.3237 -0.0729 -0.1435 0.0091  121 VAL   A CG1 
898  C CG2 . VAL   A 115 ? 0.5105 0.3299 0.3157 -0.0785 -0.1178 -0.0149 121 VAL   A CG2 
899  N N   . GLY   A 116 ? 0.4671 0.3404 0.3771 -0.0167 -0.1272 -0.0269 122 GLY   A N   
900  C CA  . GLY   A 116 ? 0.4490 0.3352 0.3760 -0.0020 -0.1374 -0.0244 122 GLY   A CA  
901  C C   . GLY   A 116 ? 0.4335 0.3176 0.3712 0.0175  -0.1471 -0.0256 122 GLY   A C   
902  O O   . GLY   A 116 ? 0.4280 0.3034 0.3698 0.0201  -0.1473 -0.0292 122 GLY   A O   
903  N N   . ILE   A 117 ? 0.4143 0.2983 0.3514 0.0290  -0.1557 -0.0226 123 ILE   A N   
904  C CA  . ILE   A 117 ? 0.4159 0.2810 0.3437 0.0422  -0.1669 -0.0234 123 ILE   A CA  
905  C C   . ILE   A 117 ? 0.4154 0.2732 0.3184 0.0519  -0.1632 -0.0159 123 ILE   A C   
906  O O   . ILE   A 117 ? 0.4120 0.2814 0.3210 0.0525  -0.1575 -0.0104 123 ILE   A O   
907  C CB  . ILE   A 117 ? 0.4186 0.2711 0.3649 0.0439  -0.1800 -0.0283 123 ILE   A CB  
908  C CG1 . ILE   A 117 ? 0.4277 0.2876 0.3795 0.0426  -0.1781 -0.0284 123 ILE   A CG1 
909  C CG2 . ILE   A 117 ? 0.4006 0.2554 0.3857 0.0389  -0.1796 -0.0321 123 ILE   A CG2 
910  C CD1 . ILE   A 117 ? 0.4590 0.2968 0.4125 0.0465  -0.1974 -0.0286 123 ILE   A CD1 
911  N N   . VAL   A 118 ? 0.4205 0.2532 0.2951 0.0591  -0.1639 -0.0148 124 VAL   A N   
912  C CA  . VAL   A 118 ? 0.4430 0.2529 0.2871 0.0698  -0.1504 -0.0091 124 VAL   A CA  
913  C C   . VAL   A 118 ? 0.4678 0.2594 0.3026 0.0745  -0.1521 -0.0116 124 VAL   A C   
914  O O   . VAL   A 118 ? 0.4557 0.2298 0.2852 0.0701  -0.1716 -0.0186 124 VAL   A O   
915  C CB  . VAL   A 118 ? 0.4878 0.2528 0.2845 0.0724  -0.1512 -0.0114 124 VAL   A CB  
916  C CG1 . VAL   A 118 ? 0.5144 0.2469 0.2754 0.0833  -0.1244 -0.0063 124 VAL   A CG1 
917  C CG2 . VAL   A 118 ? 0.4933 0.2737 0.2985 0.0670  -0.1530 -0.0095 124 VAL   A CG2 
918  N N   . SER   A 119 ? 0.4926 0.2909 0.3342 0.0829  -0.1327 -0.0029 125 SER   A N   
919  C CA  . SER   A 119 ? 0.5245 0.3054 0.3588 0.0880  -0.1313 -0.0043 125 SER   A CA  
920  C C   . SER   A 119 ? 0.5637 0.3139 0.3771 0.1026  -0.1015 0.0029  125 SER   A C   
921  O O   . SER   A 119 ? 0.5852 0.2944 0.3669 0.1076  -0.0974 -0.0020 125 SER   A O   
922  C CB  . SER   A 119 ? 0.5281 0.3524 0.4073 0.0810  -0.1385 0.0001  125 SER   A CB  
923  O OG  . SER   A 119 ? 0.5796 0.4022 0.4684 0.0888  -0.1275 0.0081  125 SER   A OG  
924  N N   . THR   A 120 ? 0.5649 0.3338 0.4012 0.1092  -0.0780 0.0165  126 THR   A N   
925  C CA  . THR   A 120 ? 0.6064 0.3445 0.4341 0.1257  -0.0387 0.0262  126 THR   A CA  
926  C C   . THR   A 120 ? 0.6321 0.3656 0.4519 0.1277  -0.0204 0.0321  126 THR   A C   
927  O O   . THR   A 120 ? 0.6247 0.3841 0.4502 0.1162  -0.0421 0.0295  126 THR   A O   
928  C CB  . THR   A 120 ? 0.5932 0.3633 0.4848 0.1359  -0.0205 0.0465  126 THR   A CB  
929  O OG1 . THR   A 120 ? 0.5759 0.3842 0.5265 0.1406  -0.0014 0.0710  126 THR   A OG1 
930  C CG2 . THR   A 120 ? 0.5805 0.3924 0.5079 0.1246  -0.0509 0.0483  126 THR   A CG2 
931  N N   . GLY   A 121 ? 0.6685 0.3672 0.4777 0.1423  0.0227  0.0404  127 GLY   A N   
932  C CA  . GLY   A 121 ? 0.7070 0.3986 0.5124 0.1455  0.0478  0.0485  127 GLY   A CA  
933  C C   . GLY   A 121 ? 0.7734 0.4051 0.5536 0.1631  0.1057  0.0538  127 GLY   A C   
934  O O   . GLY   A 121 ? 0.8035 0.3962 0.5667 0.1731  0.1263  0.0505  127 GLY   A O   
935  N N   . GLY   A 122 ? 0.8007 0.4181 0.5742 0.1667  0.1360  0.0615  128 GLY   A N   
936  C CA  . GLY   A 122 ? 0.8655 0.4166 0.6117 0.1835  0.2025  0.0665  128 GLY   A CA  
937  C C   . GLY   A 122 ? 0.8491 0.4483 0.6881 0.1959  0.2411  0.0977  128 GLY   A C   
938  O O   . GLY   A 122 ? 0.7992 0.4874 0.7380 0.1929  0.2148  0.1210  128 GLY   A O   
939  N N   . ASN   A 123 ? 0.8925 0.4301 0.6986 0.2069  0.3026  0.1007  129 ASN   A N   
940  C CA  . ASN   A 123 ? 0.8483 0.4297 0.7523 0.2198  0.3452  0.1344  129 ASN   A CA  
941  C C   . ASN   A 123 ? 0.7894 0.4472 0.7427 0.2041  0.3034  0.1483  129 ASN   A C   
942  O O   . ASN   A 123 ? 0.7456 0.4699 0.8118 0.2097  0.3150  0.1845  129 ASN   A O   
943  C CB  . ASN   A 123 ? 0.8194 0.4549 0.8506 0.2385  0.3675  0.1672  129 ASN   A CB  
944  C CG  . ASN   A 123 ? 0.9286 0.4813 0.9237 0.2591  0.4306  0.1597  129 ASN   A CG  
945  O OD1 . ASN   A 123 ? 1.0121 0.4718 0.9264 0.2663  0.4911  0.1469  129 ASN   A OD1 
946  N ND2 . ASN   A 123 ? 0.9090 0.4858 0.9557 0.2672  0.4195  0.1670  129 ASN   A ND2 
947  N N   . GLY   A 124 ? 0.7810 0.4267 0.6551 0.1839  0.2554  0.1231  130 GLY   A N   
948  C CA  . GLY   A 124 ? 0.7194 0.4282 0.6300 0.1683  0.2161  0.1332  130 GLY   A CA  
949  C C   . GLY   A 124 ? 0.6472 0.4369 0.6244 0.1561  0.1588  0.1423  130 GLY   A C   
950  O O   . GLY   A 124 ? 0.6266 0.4727 0.6526 0.1433  0.1324  0.1592  130 GLY   A O   
951  N N   . LEU   A 125 ? 0.6137 0.4028 0.5859 0.1573  0.1397  0.1312  131 LEU   A N   
952  C CA  . LEU   A 125 ? 0.5671 0.4174 0.5828 0.1427  0.0879  0.1354  131 LEU   A CA  
953  C C   . LEU   A 125 ? 0.5806 0.4012 0.5208 0.1331  0.0525  0.1010  131 LEU   A C   
954  O O   . LEU   A 125 ? 0.6401 0.3960 0.5082 0.1392  0.0663  0.0801  131 LEU   A O   
955  C CB  . LEU   A 125 ? 0.5298 0.4175 0.6285 0.1504  0.0933  0.1603  131 LEU   A CB  
956  C CG  . LEU   A 125 ? 0.5139 0.4223 0.7046 0.1666  0.1370  0.1986  131 LEU   A CG  
957  C CD1 . LEU   A 125 ? 0.4827 0.4197 0.7447 0.1723  0.1331  0.2189  131 LEU   A CD1 
958  C CD2 . LEU   A 125 ? 0.4877 0.4515 0.7460 0.1538  0.1235  0.2302  131 LEU   A CD2 
959  N N   . VAL   A 126 ? 0.5276 0.3904 0.4858 0.1166  0.0087  0.0980  132 VAL   A N   
960  C CA  . VAL   A 126 ? 0.5219 0.3657 0.4323 0.1086  -0.0214 0.0713  132 VAL   A CA  
961  C C   . VAL   A 126 ? 0.4753 0.3646 0.4315 0.0982  -0.0468 0.0786  132 VAL   A C   
962  O O   . VAL   A 126 ? 0.4539 0.3859 0.4519 0.0846  -0.0610 0.0964  132 VAL   A O   
963  C CB  . VAL   A 126 ? 0.5371 0.3620 0.3972 0.0971  -0.0443 0.0523  132 VAL   A CB  
964  C CG1 . VAL   A 126 ? 0.5125 0.3753 0.4013 0.0856  -0.0533 0.0648  132 VAL   A CG1 
965  C CG2 . VAL   A 126 ? 0.5357 0.3540 0.3754 0.0883  -0.0760 0.0324  132 VAL   A CG2 
966  N N   . GLY   A 127 ? 0.4613 0.3353 0.4037 0.1014  -0.0531 0.0666  133 GLY   A N   
967  C CA  . GLY   A 127 ? 0.4330 0.3400 0.4073 0.0900  -0.0755 0.0710  133 GLY   A CA  
968  C C   . GLY   A 127 ? 0.4347 0.3337 0.3772 0.0781  -0.1012 0.0477  133 GLY   A C   
969  O O   . GLY   A 127 ? 0.4591 0.3218 0.3625 0.0842  -0.1031 0.0296  133 GLY   A O   
970  N N   . PHE   A 128 ? 0.4116 0.3386 0.3703 0.0591  -0.1200 0.0504  134 PHE   A N   
971  C CA  . PHE   A 128 ? 0.4109 0.3311 0.3508 0.0475  -0.1358 0.0310  134 PHE   A CA  
972  C C   . PHE   A 128 ? 0.3999 0.3322 0.3531 0.0353  -0.1452 0.0327  134 PHE   A C   
973  O O   . PHE   A 128 ? 0.3845 0.3364 0.3553 0.0207  -0.1512 0.0502  134 PHE   A O   
974  C CB  . PHE   A 128 ? 0.3950 0.3210 0.3274 0.0326  -0.1418 0.0283  134 PHE   A CB  
975  C CG  . PHE   A 128 ? 0.3938 0.3118 0.3146 0.0394  -0.1356 0.0295  134 PHE   A CG  
976  C CD1 . PHE   A 128 ? 0.4027 0.2946 0.2998 0.0466  -0.1383 0.0134  134 PHE   A CD1 
977  C CD2 . PHE   A 128 ? 0.3903 0.3268 0.3270 0.0353  -0.1307 0.0497  134 PHE   A CD2 
978  C CE1 . PHE   A 128 ? 0.4091 0.2895 0.2899 0.0500  -0.1345 0.0150  134 PHE   A CE1 
979  C CE2 . PHE   A 128 ? 0.3931 0.3214 0.3175 0.0400  -0.1241 0.0507  134 PHE   A CE2 
980  C CZ  . PHE   A 128 ? 0.3927 0.2912 0.2849 0.0472  -0.1255 0.0319  134 PHE   A CZ  
981  N N   . ALA   A 129 ? 0.4069 0.3242 0.3500 0.0380  -0.1494 0.0164  135 ALA   A N   
982  C CA  . ALA   A 129 ? 0.4104 0.3336 0.3602 0.0258  -0.1558 0.0152  135 ALA   A CA  
983  C C   . ALA   A 129 ? 0.4359 0.3580 0.3757 0.0045  -0.1567 0.0084  135 ALA   A C   
984  O O   . ALA   A 129 ? 0.4481 0.3581 0.3839 0.0066  -0.1527 -0.0061 135 ALA   A O   
985  C CB  . ALA   A 129 ? 0.4191 0.3245 0.3642 0.0359  -0.1589 0.0014  135 ALA   A CB  
986  N N   . ASP   A 130 ? 0.4470 0.3751 0.3810 -0.0176 -0.1616 0.0208  136 ASP   A N   
987  C CA  . ASP   A 130 ? 0.4722 0.3827 0.3784 -0.0428 -0.1579 0.0141  136 ASP   A CA  
988  C C   . ASP   A 130 ? 0.4795 0.3710 0.3773 -0.0494 -0.1472 -0.0030 136 ASP   A C   
989  O O   . ASP   A 130 ? 0.4860 0.3832 0.3961 -0.0442 -0.1514 -0.0027 136 ASP   A O   
990  C CB  . ASP   A 130 ? 0.5090 0.4202 0.4002 -0.0708 -0.1722 0.0363  136 ASP   A CB  
991  C CG  . ASP   A 130 ? 0.6269 0.5065 0.4714 -0.1012 -0.1691 0.0325  136 ASP   A CG  
992  O OD1 . ASP   A 130 ? 0.6508 0.5226 0.4874 -0.0962 -0.1592 0.0231  136 ASP   A OD1 
993  O OD2 . ASP   A 130 ? 0.7045 0.5602 0.5135 -0.1327 -0.1770 0.0397  136 ASP   A OD2 
994  N N   . VAL   A 131 ? 0.4795 0.3465 0.3602 -0.0596 -0.1297 -0.0175 137 VAL   A N   
995  C CA  . VAL   A 131 ? 0.4779 0.3225 0.3576 -0.0664 -0.1094 -0.0327 137 VAL   A CA  
996  C C   . VAL   A 131 ? 0.5166 0.3162 0.3435 -0.0982 -0.0878 -0.0388 137 VAL   A C   
997  O O   . VAL   A 131 ? 0.5294 0.2997 0.3507 -0.1057 -0.0593 -0.0524 137 VAL   A O   
998  C CB  . VAL   A 131 ? 0.4543 0.3046 0.3797 -0.0423 -0.0998 -0.0442 137 VAL   A CB  
999  C CG1 . VAL   A 131 ? 0.4377 0.3130 0.3916 -0.0182 -0.1224 -0.0385 137 VAL   A CG1 
1000 C CG2 . VAL   A 131 ? 0.4530 0.2899 0.3790 -0.0408 -0.0862 -0.0502 137 VAL   A CG2 
1001 N N   . ARG   A 132 ? 0.5350 0.3226 0.3209 -0.1188 -0.0993 -0.0277 138 ARG   A N   
1002 C CA  . ARG   A 132 ? 0.6046 0.3345 0.3223 -0.1537 -0.0808 -0.0333 138 ARG   A CA  
1003 C C   . ARG   A 132 ? 0.6644 0.3554 0.3297 -0.1863 -0.0774 -0.0319 138 ARG   A C   
1004 O O   . ARG   A 132 ? 0.7201 0.3496 0.3269 -0.2114 -0.0475 -0.0446 138 ARG   A O   
1005 C CB  . ARG   A 132 ? 0.6196 0.3407 0.3023 -0.1716 -0.0990 -0.0192 138 ARG   A CB  
1006 C CG  . ARG   A 132 ? 0.5973 0.3448 0.3211 -0.1428 -0.0955 -0.0242 138 ARG   A CG  
1007 C CD  . ARG   A 132 ? 0.6069 0.3560 0.3073 -0.1579 -0.1174 -0.0065 138 ARG   A CD  
1008 N NE  . ARG   A 132 ? 0.5843 0.3804 0.3196 -0.1517 -0.1498 0.0191  138 ARG   A NE  
1009 C CZ  . ARG   A 132 ? 0.5887 0.3949 0.3190 -0.1672 -0.1741 0.0439  138 ARG   A CZ  
1010 N NH1 . ARG   A 132 ? 0.6378 0.4075 0.3186 -0.1926 -0.1746 0.0452  138 ARG   A NH1 
1011 N NH2 . ARG   A 132 ? 0.5278 0.3779 0.3057 -0.1582 -0.1965 0.0696  138 ARG   A NH2 
1012 N N   . ASP   A 133 ? 0.6560 0.3764 0.3408 -0.1853 -0.1032 -0.0179 139 ASP   A N   
1013 C CA  . ASP   A 133 ? 0.6916 0.3786 0.3306 -0.2160 -0.1057 -0.0140 139 ASP   A CA  
1014 C C   . ASP   A 133 ? 0.7031 0.3774 0.3572 -0.2055 -0.0715 -0.0348 139 ASP   A C   
1015 O O   . ASP   A 133 ? 0.7318 0.3601 0.3318 -0.2356 -0.0603 -0.0375 139 ASP   A O   
1016 C CB  . ASP   A 133 ? 0.6870 0.4153 0.3553 -0.2156 -0.1476 0.0121  139 ASP   A CB  
1017 C CG  . ASP   A 133 ? 0.7049 0.4908 0.4525 -0.1719 -0.1514 0.0100  139 ASP   A CG  
1018 O OD1 . ASP   A 133 ? 0.6761 0.4890 0.4651 -0.1402 -0.1434 0.0017  139 ASP   A OD1 
1019 O OD2 . ASP   A 133 ? 0.7305 0.5286 0.4923 -0.1720 -0.1645 0.0179  139 ASP   A OD2 
1020 N N   . LEU   A 134 ? 0.6799 0.3921 0.4070 -0.1661 -0.0576 -0.0463 140 LEU   A N   
1021 C CA  . LEU   A 134 ? 0.6866 0.3961 0.4491 -0.1537 -0.0294 -0.0602 140 LEU   A CA  
1022 C C   . LEU   A 134 ? 0.7341 0.3895 0.4736 -0.1651 0.0220  -0.0776 140 LEU   A C   
1023 O O   . LEU   A 134 ? 0.7107 0.3781 0.5078 -0.1404 0.0440  -0.0856 140 LEU   A O   
1024 C CB  . LEU   A 134 ? 0.6397 0.4039 0.4879 -0.1129 -0.0417 -0.0600 140 LEU   A CB  
1025 C CG  . LEU   A 134 ? 0.6257 0.4335 0.4937 -0.0971 -0.0828 -0.0453 140 LEU   A CG  
1026 C CD1 . LEU   A 134 ? 0.5915 0.4311 0.5201 -0.0639 -0.0918 -0.0471 140 LEU   A CD1 
1027 C CD2 . LEU   A 134 ? 0.6380 0.4471 0.4874 -0.1114 -0.1000 -0.0354 140 LEU   A CD2 
1028 N N   . LEU   A 135 ? 0.8022 0.3912 0.4553 -0.2043 0.0424  -0.0817 141 LEU   A N   
1029 C CA  . LEU   A 135 ? 0.8692 0.3868 0.4794 -0.2205 0.1003  -0.0992 141 LEU   A CA  
1030 C C   . LEU   A 135 ? 0.8744 0.3909 0.5518 -0.2003 0.1498  -0.1116 141 LEU   A C   
1031 O O   . LEU   A 135 ? 0.8838 0.3614 0.5708 -0.1964 0.2020  -0.1239 141 LEU   A O   
1032 C CB  . LEU   A 135 ? 0.9457 0.3761 0.4257 -0.2746 0.1079  -0.0996 141 LEU   A CB  
1033 C CG  . LEU   A 135 ? 0.9858 0.4169 0.4055 -0.3024 0.0501  -0.0784 141 LEU   A CG  
1034 C CD1 . LEU   A 135 ? 1.0721 0.4023 0.3564 -0.3616 0.0572  -0.0774 141 LEU   A CD1 
1035 C CD2 . LEU   A 135 ? 0.9719 0.4326 0.4182 -0.2850 0.0340  -0.0739 141 LEU   A CD2 
1036 N N   . TRP   A 136 ? 0.8531 0.4153 0.5878 -0.1853 0.1329  -0.1055 142 TRP   A N   
1037 C CA  . TRP   A 136 ? 0.8507 0.4203 0.6624 -0.1673 0.1719  -0.1108 142 TRP   A CA  
1038 C C   . TRP   A 136 ? 0.8239 0.4391 0.7486 -0.1286 0.1779  -0.1080 142 TRP   A C   
1039 O O   . TRP   A 136 ? 0.8026 0.4189 0.8028 -0.1153 0.2155  -0.1083 142 TRP   A O   
1040 C CB  . TRP   A 136 ? 0.8329 0.4358 0.6681 -0.1658 0.1456  -0.1028 142 TRP   A CB  
1041 C CG  . TRP   A 136 ? 0.8085 0.4785 0.6770 -0.1461 0.0809  -0.0890 142 TRP   A CG  
1042 C CD1 . TRP   A 136 ? 0.8334 0.5116 0.6476 -0.1599 0.0375  -0.0794 142 TRP   A CD1 
1043 C CD2 . TRP   A 136 ? 0.7622 0.4917 0.7239 -0.1111 0.0552  -0.0814 142 TRP   A CD2 
1044 N NE1 . TRP   A 136 ? 0.8009 0.5382 0.6692 -0.1323 -0.0050 -0.0690 142 TRP   A NE1 
1045 C CE2 . TRP   A 136 ? 0.7627 0.5271 0.7113 -0.1045 0.0034  -0.0713 142 TRP   A CE2 
1046 C CE3 . TRP   A 136 ? 0.7357 0.4876 0.7915 -0.0874 0.0699  -0.0792 142 TRP   A CE3 
1047 C CZ2 . TRP   A 136 ? 0.7405 0.5496 0.7476 -0.0767 -0.0296 -0.0635 142 TRP   A CZ2 
1048 C CZ3 . TRP   A 136 ? 0.7129 0.5130 0.8293 -0.0631 0.0272  -0.0680 142 TRP   A CZ3 
1049 C CH2 . TRP   A 136 ? 0.7167 0.5396 0.7997 -0.0589 -0.0200 -0.0624 142 TRP   A CH2 
1050 N N   . LEU   A 137 ? 0.8205 0.4717 0.7606 -0.1125 0.1400  -0.1020 143 LEU   A N   
1051 C CA  . LEU   A 137 ? 0.8036 0.4912 0.8385 -0.0812 0.1372  -0.0967 143 LEU   A CA  
1052 C C   . LEU   A 137 ? 0.8599 0.5028 0.9149 -0.0805 0.1979  -0.1055 143 LEU   A C   
1053 O O   . LEU   A 137 ? 0.8229 0.4908 0.9788 -0.0561 0.2070  -0.0978 143 LEU   A O   
1054 C CB  . LEU   A 137 ? 0.7876 0.5090 0.8102 -0.0705 0.0877  -0.0902 143 LEU   A CB  
1055 C CG  . LEU   A 137 ? 0.7757 0.5402 0.7908 -0.0645 0.0328  -0.0800 143 LEU   A CG  
1056 C CD1 . LEU   A 137 ? 0.7730 0.5598 0.7751 -0.0544 -0.0014 -0.0743 143 LEU   A CD1 
1057 C CD2 . LEU   A 137 ? 0.7361 0.5357 0.8279 -0.0451 0.0155  -0.0718 143 LEU   A CD2 
1058 N N   . ASP   A 138 ? 0.9481 0.5193 0.9055 -0.1092 0.2378  -0.1195 144 ASP   A N   
1059 C CA  . ASP   A 138 ? 1.0073 0.5180 0.9643 -0.1118 0.3048  -0.1307 144 ASP   A CA  
1060 C C   . ASP   A 138 ? 1.0656 0.5168 1.0137 -0.1257 0.3753  -0.1403 144 ASP   A C   
1061 O O   . ASP   A 138 ? 1.1077 0.4873 1.0275 -0.1344 0.4413  -0.1525 144 ASP   A O   
1062 C CB  . ASP   A 138 ? 1.1039 0.5541 0.9401 -0.1396 0.3083  -0.1409 144 ASP   A CB  
1063 C CG  . ASP   A 138 ? 1.1584 0.6553 1.0018 -0.1272 0.2532  -0.1323 144 ASP   A CG  
1064 O OD1 . ASP   A 138 ? 1.1215 0.6762 1.0672 -0.0942 0.2347  -0.1231 144 ASP   A OD1 
1065 O OD2 . ASP   A 138 ? 1.2256 0.6978 0.9717 -0.1530 0.2273  -0.1323 144 ASP   A OD2 
1066 N N   . GLU   A 139 ? 1.0741 0.5452 1.0381 -0.1295 0.3670  -0.1357 145 GLU   A N   
1067 C CA  . GLU   A 139 ? 1.1263 0.5357 1.0742 -0.1455 0.4373  -0.1448 145 GLU   A CA  
1068 C C   . GLU   A 139 ? 1.0865 0.5483 1.1392 -0.1283 0.4345  -0.1321 145 GLU   A C   
1069 O O   . GLU   A 139 ? 1.1127 0.5286 1.1528 -0.1426 0.4894  -0.1379 145 GLU   A O   
1070 C CB  . GLU   A 139 ? 1.2596 0.5871 1.0411 -0.1932 0.4446  -0.1582 145 GLU   A CB  
1071 C CG  . GLU   A 139 ? 1.3419 0.7127 1.0729 -0.2069 0.3645  -0.1482 145 GLU   A CG  
1072 C CD  . GLU   A 139 ? 1.5185 0.8097 1.0875 -0.2573 0.3562  -0.1543 145 GLU   A CD  
1073 O OE1 . GLU   A 139 ? 1.5344 0.8425 1.0626 -0.2754 0.3082  -0.1448 145 GLU   A OE1 
1074 O OE2 . GLU   A 139 ? 1.6123 0.8198 1.0943 -0.2810 0.3956  -0.1663 145 GLU   A OE2 
1075 N N1  . A1B4L B .   ? 0.9966 0.4779 0.5985 0.1397  0.0027  -0.0098 201 A1B4L A N1  
1076 C C4  . A1B4L B .   ? 1.0554 0.4520 0.5644 0.1272  -0.0151 -0.0245 201 A1B4L A C4  
1077 C C5  . A1B4L B .   ? 0.9883 0.4754 0.5925 0.1424  0.0219  -0.0049 201 A1B4L A C5  
1078 C C6  . A1B4L B .   ? 1.0516 0.4427 0.5484 0.1344  0.0351  -0.0166 201 A1B4L A C6  
1079 C C7  . A1B4L B .   ? 1.0348 0.4479 0.5437 0.1334  0.0442  -0.0112 201 A1B4L A C7  
1080 C C8  . A1B4L B .   ? 1.0619 0.4248 0.5368 0.1435  0.0982  -0.0073 201 A1B4L A C8  
1081 C C10 . A1B4L B .   ? 1.0088 0.4630 0.5401 0.1297  0.0577  0.0000  201 A1B4L A C10 
1082 C C13 . A1B4L B .   ? 0.9287 0.5053 0.5548 0.1049  -0.0641 -0.0107 201 A1B4L A C13 
1083 C C15 . A1B4L B .   ? 0.9384 0.4969 0.6301 0.1452  -0.0065 0.0018  201 A1B4L A C15 
1084 O O1  . A1B4L B .   ? 0.9362 0.4965 0.6194 0.1479  0.0266  0.0095  201 A1B4L A O1  
1085 C C3  . A1B4L B .   ? 1.0337 0.4696 0.5673 0.1110  -0.0716 -0.0284 201 A1B4L A C3  
1086 C C2  . A1B4L B .   ? 0.9729 0.4940 0.6010 0.1187  -0.0761 -0.0196 201 A1B4L A C2  
1087 C C1  . A1B4L B .   ? 0.9191 0.5137 0.6239 0.1278  -0.0581 -0.0061 201 A1B4L A C1  
1088 C C   . A1B4L B .   ? 0.8633 0.5296 0.6473 0.1281  -0.0685 0.0049  201 A1B4L A C   
1089 O O   . A1B4L B .   ? 0.8566 0.5170 0.6551 0.1360  -0.0571 0.0105  201 A1B4L A O   
1090 N N   . A1B4L B .   ? 0.8266 0.5534 0.6559 0.1174  -0.0893 0.0084  201 A1B4L A N   
1091 C C14 . A1B4L B .   ? 0.9905 0.4709 0.5448 0.1226  0.0030  -0.0097 201 A1B4L A C14 
1092 O O2  . A1B4L B .   ? 0.9551 0.4838 0.5473 0.1125  -0.0432 -0.0130 201 A1B4L A O2  
1093 C C12 . A1B4L B .   ? 0.9406 0.5054 0.5525 0.1088  -0.0384 -0.0056 201 A1B4L A C12 
1094 C C11 . A1B4L B .   ? 0.9792 0.4810 0.5452 0.1205  0.0078  -0.0045 201 A1B4L A C11 
1095 C C9  . A1B4L B .   ? 1.0494 0.4339 0.5364 0.1414  0.1049  -0.0014 201 A1B4L A C9  
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