data_8VEZ
# 
_entry.id   8VEZ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_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   8VEZ         pdb_00008vez 10.2210/pdb8vez/pdb 
WWPDB D_1000280078 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-15 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8VEZ 
_pdbx_database_status.recvd_initial_deposition_date   2023-12-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              dabaker@uw.edu 
_pdbx_contact_author.name_first         David 
_pdbx_contact_author.name_last          Baker 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7896-6217 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bera, A.K.' 1 ? 
'Lee, G.R.'  2 ? 
'Baker, D.'  3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Small-molecule binding and sensing with a designed protein family' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lee, G.R.'  1 ? 
primary 'Bera, A.K.' 2 ? 
primary 'Baker, D.'  3 ? 
# 
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 'De novo design apixaban-binding protein: apx1049' 13098.239 1  ? ? ? ? 
2 non-polymer syn 
'1-(4-METHOXYPHENYL)-7-OXO-6-[4-(2-OXOPIPERIDIN-1-YL)PHENYL]-4,5,6,7-TETRAHYDRO-1H-PYRAZOLO[3,4-C]PYRIDINE-3-CARBOXAMIDE' 459.497 
1  ? ? ? ? 
3 water       nat water 18.015    20 ? ? ? ? 
# 
_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       
;SGGSSARIAKAKKLIYKLEKLWNARDNDGILKLFKDDAVFNLNGVPYKGKEAIKKVLESAPKAKYKITKIDIKIVGNEII
VNVDVLATGPSGFTLKVKSTITFDEDMKITSYEVNLEGS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGGSSARIAKAKKLIYKLEKLWNARDNDGILKLFKDDAVFNLNGVPYKGKEAIKKVLESAPKAKYKITKIDIKIVGNEII
VNVDVLATGPSGFTLKVKSTITFDEDMKITSYEVNLEGS
;
_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 '1-(4-METHOXYPHENYL)-7-OXO-6-[4-(2-OXOPIPERIDIN-1-YL)PHENYL]-4,5,6,7-TETRAHYDRO-1H-PYRAZOLO[3,4-C]PYRIDINE-3-CARBOXAMIDE' GG2 
3 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   GLY n 
1 4   SER n 
1 5   SER n 
1 6   ALA n 
1 7   ARG n 
1 8   ILE n 
1 9   ALA n 
1 10  LYS n 
1 11  ALA n 
1 12  LYS n 
1 13  LYS n 
1 14  LEU n 
1 15  ILE n 
1 16  TYR n 
1 17  LYS n 
1 18  LEU n 
1 19  GLU n 
1 20  LYS n 
1 21  LEU n 
1 22  TRP n 
1 23  ASN n 
1 24  ALA n 
1 25  ARG n 
1 26  ASP n 
1 27  ASN n 
1 28  ASP n 
1 29  GLY n 
1 30  ILE n 
1 31  LEU n 
1 32  LYS n 
1 33  LEU n 
1 34  PHE n 
1 35  LYS n 
1 36  ASP n 
1 37  ASP n 
1 38  ALA n 
1 39  VAL n 
1 40  PHE n 
1 41  ASN n 
1 42  LEU n 
1 43  ASN n 
1 44  GLY n 
1 45  VAL n 
1 46  PRO n 
1 47  TYR n 
1 48  LYS n 
1 49  GLY n 
1 50  LYS n 
1 51  GLU n 
1 52  ALA n 
1 53  ILE n 
1 54  LYS n 
1 55  LYS n 
1 56  VAL n 
1 57  LEU n 
1 58  GLU n 
1 59  SER n 
1 60  ALA n 
1 61  PRO n 
1 62  LYS n 
1 63  ALA n 
1 64  LYS n 
1 65  TYR n 
1 66  LYS n 
1 67  ILE n 
1 68  THR n 
1 69  LYS n 
1 70  ILE n 
1 71  ASP n 
1 72  ILE n 
1 73  LYS n 
1 74  ILE n 
1 75  VAL n 
1 76  GLY n 
1 77  ASN n 
1 78  GLU n 
1 79  ILE n 
1 80  ILE n 
1 81  VAL n 
1 82  ASN n 
1 83  VAL n 
1 84  ASP n 
1 85  VAL n 
1 86  LEU n 
1 87  ALA n 
1 88  THR n 
1 89  GLY n 
1 90  PRO n 
1 91  SER n 
1 92  GLY n 
1 93  PHE n 
1 94  THR n 
1 95  LEU n 
1 96  LYS n 
1 97  VAL n 
1 98  LYS n 
1 99  SER n 
1 100 THR n 
1 101 ILE n 
1 102 THR n 
1 103 PHE n 
1 104 ASP n 
1 105 GLU n 
1 106 ASP n 
1 107 MET n 
1 108 LYS n 
1 109 ILE n 
1 110 THR n 
1 111 SER n 
1 112 TYR n 
1 113 GLU n 
1 114 VAL n 
1 115 ASN n 
1 116 LEU n 
1 117 GLU n 
1 118 GLY n 
1 119 SER 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                   119 
_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      'synthetic construct' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     32630 
_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 
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 
GG2 non-polymer         . 
'1-(4-METHOXYPHENYL)-7-OXO-6-[4-(2-OXOPIPERIDIN-1-YL)PHENYL]-4,5,6,7-TETRAHYDRO-1H-PYRAZOLO[3,4-C]PYRIDINE-3-CARBOXAMIDE' ? 
'C25 H25 N5 O4'  459.497 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE ? 'C2 H5 N O2'     75.067  
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 
# 
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   -3  ?   ?   ?   A . n 
A 1 2   GLY 2   -2  ?   ?   ?   A . n 
A 1 3   GLY 3   -1  ?   ?   ?   A . n 
A 1 4   SER 4   0   0   SER SER A . n 
A 1 5   SER 5   1   1   SER SER A . n 
A 1 6   ALA 6   2   2   ALA ALA A . n 
A 1 7   ARG 7   3   3   ARG ARG A . n 
A 1 8   ILE 8   4   4   ILE ILE A . n 
A 1 9   ALA 9   5   5   ALA ALA A . n 
A 1 10  LYS 10  6   6   LYS LYS A . n 
A 1 11  ALA 11  7   7   ALA ALA A . n 
A 1 12  LYS 12  8   8   LYS LYS A . n 
A 1 13  LYS 13  9   9   LYS LYS A . n 
A 1 14  LEU 14  10  10  LEU LEU A . n 
A 1 15  ILE 15  11  11  ILE ILE A . n 
A 1 16  TYR 16  12  12  TYR TYR A . n 
A 1 17  LYS 17  13  13  LYS LYS A . n 
A 1 18  LEU 18  14  14  LEU LEU A . n 
A 1 19  GLU 19  15  15  GLU GLU A . n 
A 1 20  LYS 20  16  16  LYS LYS A . n 
A 1 21  LEU 21  17  17  LEU LEU A . n 
A 1 22  TRP 22  18  18  TRP TRP A . n 
A 1 23  ASN 23  19  19  ASN ASN A . n 
A 1 24  ALA 24  20  20  ALA ALA A . n 
A 1 25  ARG 25  21  21  ARG ARG A . n 
A 1 26  ASP 26  22  22  ASP ASP A . n 
A 1 27  ASN 27  23  23  ASN ASN A . n 
A 1 28  ASP 28  24  24  ASP ASP A . n 
A 1 29  GLY 29  25  25  GLY GLY A . n 
A 1 30  ILE 30  26  26  ILE ILE A . n 
A 1 31  LEU 31  27  27  LEU LEU A . n 
A 1 32  LYS 32  28  28  LYS LYS A . n 
A 1 33  LEU 33  29  29  LEU LEU A . n 
A 1 34  PHE 34  30  30  PHE PHE A . n 
A 1 35  LYS 35  31  31  LYS LYS A . n 
A 1 36  ASP 36  32  32  ASP ASP A . n 
A 1 37  ASP 37  33  33  ASP ASP A . n 
A 1 38  ALA 38  34  34  ALA ALA A . n 
A 1 39  VAL 39  35  35  VAL VAL A . n 
A 1 40  PHE 40  36  36  PHE PHE A . n 
A 1 41  ASN 41  37  37  ASN ASN A . n 
A 1 42  LEU 42  38  38  LEU LEU A . n 
A 1 43  ASN 43  39  39  ASN ASN A . n 
A 1 44  GLY 44  40  40  GLY GLY A . n 
A 1 45  VAL 45  41  41  VAL VAL A . n 
A 1 46  PRO 46  42  42  PRO PRO A . n 
A 1 47  TYR 47  43  43  TYR TYR A . n 
A 1 48  LYS 48  44  44  LYS LYS A . n 
A 1 49  GLY 49  45  45  GLY GLY A . n 
A 1 50  LYS 50  46  46  LYS LYS A . n 
A 1 51  GLU 51  47  47  GLU GLU A . n 
A 1 52  ALA 52  48  48  ALA ALA A . n 
A 1 53  ILE 53  49  49  ILE ILE A . n 
A 1 54  LYS 54  50  50  LYS LYS A . n 
A 1 55  LYS 55  51  51  LYS LYS A . n 
A 1 56  VAL 56  52  52  VAL VAL A . n 
A 1 57  LEU 57  53  53  LEU LEU A . n 
A 1 58  GLU 58  54  54  GLU GLU A . n 
A 1 59  SER 59  55  55  SER SER A . n 
A 1 60  ALA 60  56  56  ALA ALA A . n 
A 1 61  PRO 61  57  57  PRO PRO A . n 
A 1 62  LYS 62  58  58  LYS LYS A . n 
A 1 63  ALA 63  59  59  ALA ALA A . n 
A 1 64  LYS 64  60  60  LYS LYS A . n 
A 1 65  TYR 65  61  61  TYR TYR A . n 
A 1 66  LYS 66  62  62  LYS LYS A . n 
A 1 67  ILE 67  63  63  ILE ILE A . n 
A 1 68  THR 68  64  64  THR THR A . n 
A 1 69  LYS 69  65  65  LYS LYS A . n 
A 1 70  ILE 70  66  66  ILE ILE A . n 
A 1 71  ASP 71  67  67  ASP ASP A . n 
A 1 72  ILE 72  68  68  ILE ILE A . n 
A 1 73  LYS 73  69  69  LYS LYS A . n 
A 1 74  ILE 74  70  70  ILE ILE A . n 
A 1 75  VAL 75  71  71  VAL VAL A . n 
A 1 76  GLY 76  72  72  GLY GLY A . n 
A 1 77  ASN 77  73  73  ASN ASN A . n 
A 1 78  GLU 78  74  74  GLU GLU A . n 
A 1 79  ILE 79  75  75  ILE ILE A . n 
A 1 80  ILE 80  76  76  ILE ILE A . n 
A 1 81  VAL 81  77  77  VAL VAL A . n 
A 1 82  ASN 82  78  78  ASN ASN A . n 
A 1 83  VAL 83  79  79  VAL VAL A . n 
A 1 84  ASP 84  80  80  ASP ASP A . n 
A 1 85  VAL 85  81  81  VAL VAL A . n 
A 1 86  LEU 86  82  82  LEU LEU A . n 
A 1 87  ALA 87  83  83  ALA ALA A . n 
A 1 88  THR 88  84  84  THR THR A . n 
A 1 89  GLY 89  85  85  GLY GLY A . n 
A 1 90  PRO 90  86  86  PRO PRO A . n 
A 1 91  SER 91  87  87  SER SER A . n 
A 1 92  GLY 92  88  88  GLY GLY A . n 
A 1 93  PHE 93  89  89  PHE PHE A . n 
A 1 94  THR 94  90  90  THR THR A . n 
A 1 95  LEU 95  91  91  LEU LEU A . n 
A 1 96  LYS 96  92  92  LYS LYS A . n 
A 1 97  VAL 97  93  93  VAL VAL A . n 
A 1 98  LYS 98  94  94  LYS LYS A . n 
A 1 99  SER 99  95  95  SER SER A . n 
A 1 100 THR 100 96  96  THR THR A . n 
A 1 101 ILE 101 97  97  ILE ILE A . n 
A 1 102 THR 102 98  98  THR THR A . n 
A 1 103 PHE 103 99  99  PHE PHE A . n 
A 1 104 ASP 104 100 100 ASP ASP A . n 
A 1 105 GLU 105 101 101 GLU GLU A . n 
A 1 106 ASP 106 102 102 ASP ASP A . n 
A 1 107 MET 107 103 103 MET MET A . n 
A 1 108 LYS 108 104 104 LYS LYS A . n 
A 1 109 ILE 109 105 105 ILE ILE A . n 
A 1 110 THR 110 106 106 THR THR A . n 
A 1 111 SER 111 107 107 SER SER A . n 
A 1 112 TYR 112 108 108 TYR TYR A . n 
A 1 113 GLU 113 109 109 GLU GLU A . n 
A 1 114 VAL 114 110 110 VAL VAL A . n 
A 1 115 ASN 115 111 111 ASN ASN A . n 
A 1 116 LEU 116 112 112 LEU LEU A . n 
A 1 117 GLU 117 113 113 GLU GLU A . n 
A 1 118 GLY 118 114 114 GLY GLY A . n 
A 1 119 SER 119 115 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        GG2 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   GG2 
_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 GG2 1  201 1  GG2 APX A . 
C 3 HOH 1  301 2  HOH HOH A . 
C 3 HOH 2  302 11 HOH HOH A . 
C 3 HOH 3  303 6  HOH HOH A . 
C 3 HOH 4  304 4  HOH HOH A . 
C 3 HOH 5  305 16 HOH HOH A . 
C 3 HOH 6  306 20 HOH HOH A . 
C 3 HOH 7  307 14 HOH HOH A . 
C 3 HOH 8  308 12 HOH HOH A . 
C 3 HOH 9  309 7  HOH HOH A . 
C 3 HOH 10 310 10 HOH HOH A . 
C 3 HOH 11 311 3  HOH HOH A . 
C 3 HOH 12 312 18 HOH HOH A . 
C 3 HOH 13 313 17 HOH HOH A . 
C 3 HOH 14 314 9  HOH HOH A . 
C 3 HOH 15 315 1  HOH HOH A . 
C 3 HOH 16 316 8  HOH HOH A . 
C 3 HOH 17 317 5  HOH HOH A . 
C 3 HOH 18 318 13 HOH HOH A . 
C 3 HOH 19 319 15 HOH HOH A . 
C 3 HOH 20 320 19 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A LYS 58 ? CG ? A LYS 62 CG 
2 1 Y 1 A LYS 58 ? CD ? A LYS 62 CD 
3 1 Y 1 A LYS 58 ? CE ? A LYS 62 CE 
4 1 Y 1 A LYS 58 ? NZ ? A LYS 62 NZ 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? dev_4761 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8VEZ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     54.971 
_cell.length_a_esd                 ? 
_cell.length_b                     64.176 
_cell.length_b_esd                 ? 
_cell.length_c                     60.108 
_cell.length_c_esd                 ? 
_cell.volume                       212050.138 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8VEZ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            'C 2c 2' 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8VEZ 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.03 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.22 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M potassium thiocyanate and 30% PEG 2000 MME' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-12-15 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.00009 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 8.2.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00009 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   8.2.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          47.40 
_reflns.entry_id                                       8VEZ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.15 
_reflns.d_resolution_low                               41.75 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     6020 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.70 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.67 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.075 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.221 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.15 
_reflns_shell.d_res_low                                     2.37 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.91 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1474 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               9.6 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.816 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.460 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.53 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.419 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               55.38 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8VEZ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.15 
_refine.ls_d_res_low                             41.75 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     6020 
_refine.ls_number_reflns_R_free                  603 
_refine.ls_number_reflns_R_work                  5417 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.70 
_refine.ls_percent_reflns_R_free                 10.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2280 
_refine.ls_R_factor_R_free                       0.2774 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2229 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 34.7164 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.3136 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.15 
_refine_hist.d_res_low                        41.75 
_refine_hist.number_atoms_solvent             20 
_refine_hist.number_atoms_total               951 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        897 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         34 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0020 ? 947  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6908 ? 1277 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0456 ? 145  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0021 ? 156  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 6.1092 ? 135  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.15 2.37  . . 148 1326 99.53 . . . . 0.3280 . . . . . . . . . . . 0.3627 
'X-RAY DIFFRACTION' 2.37 2.71  . . 147 1328 99.59 . . . . 0.2854 . . . . . . . . . . . 0.3573 
'X-RAY DIFFRACTION' 2.71 3.41  . . 150 1341 99.87 . . . . 0.2429 . . . . . . . . . . . 0.2999 
'X-RAY DIFFRACTION' 3.41 41.75 . . 158 1422 99.81 . . . . 0.1914 . . . . . . . . . . . 0.2436 
# 
_struct.entry_id                     8VEZ 
_struct.title                        'De novo design apixaban-binding protein: apx1049' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8VEZ 
_struct_keywords.text            'protein design, deep learning, small-molecule-binding, de novo design, apixaban, DE NOVO PROTEIN' 
_struct_keywords.pdbx_keywords   'DE NOVO 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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8VEZ 
_struct_ref.pdbx_db_accession          8VEZ 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8VEZ 
_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                 119 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             8VEZ 
_struct_ref_seq.db_align_beg                  -3 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  115 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       -3 
_struct_ref_seq.pdbx_auth_seq_align_end       115 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_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 
# 
_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 SER A 4  ? ARG A 25 ? SER A 0  ARG A 21 1 ? 22 
HELX_P HELX_P2 AA2 ASP A 26 ? LEU A 33 ? ASP A 22 LEU A 29 1 ? 8  
HELX_P HELX_P3 AA3 GLY A 49 ? SER A 59 ? GLY A 45 SER A 55 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   6 
_struct_sheet.details          ? 
# 
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 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? 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 VAL A 45  ? LYS A 48  ? VAL A 41  LYS A 44  
AA1 2 PHE A 34  ? LEU A 42  ? PHE A 30  LEU A 38  
AA1 3 ILE A 109 ? ASN A 115 ? ILE A 105 ASN A 111 
AA1 4 THR A 94  ? PHE A 103 ? THR A 90  PHE A 99  
AA1 5 GLU A 78  ? THR A 88  ? GLU A 74  THR A 84  
AA1 6 LYS A 64  ? VAL A 75  ? LYS A 60  VAL A 71  
# 
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 O TYR A 47  ? O TYR A 43  N PHE A 40  ? N PHE A 36  
AA1 2 3 N LYS A 35  ? N LYS A 31  O ILE A 109 ? O ILE A 105 
AA1 3 4 O ASN A 115 ? O ASN A 111 N LYS A 98  ? N LYS A 94  
AA1 4 5 O SER A 99  ? O SER A 95  N VAL A 83  ? N VAL A 79  
AA1 5 6 O ILE A 80  ? O ILE A 76  N LYS A 73  ? N LYS A 69  
# 
_pdbx_entry_details.entry_id                   8VEZ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   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    ILE 
_pdbx_validate_symm_contact.auth_seq_id_1     70 
_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    OG 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     87 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   5_545 
_pdbx_validate_symm_contact.dist              2.09 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 100 ? ? -106.20 -161.41 
2 1 ASP A 102 ? ? -68.87  3.06    
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z+1/2         
4 -x,-y,z+1/2         
5 x+1/2,y+1/2,z       
6 x+1/2,-y+1/2,-z     
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         12.1271201617 
_pdbx_refine_tls.origin_y         15.2716190389 
_pdbx_refine_tls.origin_z         -5.9767874216 
_pdbx_refine_tls.T[1][1]          0.351119229523 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.046812469952 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0174445853256 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.328496879202 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.00140199366816 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.321852996124 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.75448016404 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -1.14688109392 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.632700150036 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.749538133251 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.295786896783 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.42219770186 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.141532488683 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.182093708024 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0951547159201 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.00183255791125 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.00819835765149 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0819702783661 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.252762579016 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.246315685122 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -5.61185325223e-05 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     0 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   C 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    B 
_pdbx_refine_tls_group.end_auth_seq_id     20 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
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 SER -3  ? A SER 1   
2 1 Y 1 A GLY -2  ? A GLY 2   
3 1 Y 1 A GLY -1  ? A GLY 3   
4 1 Y 1 A SER 115 ? A SER 119 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
GG2 C1   C Y N 74  
GG2 C2   C Y N 75  
GG2 C3   C Y N 76  
GG2 O4   O N N 77  
GG2 N6   N N N 78  
GG2 C7   C Y N 79  
GG2 C8   C N N 80  
GG2 C10  C N N 81  
GG2 C11  C N N 82  
GG2 C12  C N N 83  
GG2 C13  C N N 84  
GG2 C14  C Y N 85  
GG2 C15  C N N 86  
GG2 C16  C Y N 87  
GG2 C19  C N N 88  
GG2 C20  C N N 89  
GG2 C21  C N N 90  
GG2 C22  C Y N 91  
GG2 C24  C N N 92  
GG2 C4   C Y N 93  
GG2 C5   C Y N 94  
GG2 C6   C Y N 95  
GG2 N1   N N N 96  
GG2 N5   N N N 97  
GG2 C44  C Y N 98  
GG2 N2   N N N 99  
GG2 C18  C Y N 100 
GG2 O3   O N N 101 
GG2 C25  C N N 102 
GG2 O2   O N N 103 
GG2 C23  C N N 104 
GG2 O1   O N N 105 
GG2 N3   N N N 106 
GG2 C17  C N N 107 
GG2 H2   H N N 108 
GG2 H3   H N N 109 
GG2 H14  H N N 110 
GG2 H151 H N N 111 
GG2 H152 H N N 112 
GG2 H153 H N N 113 
GG2 H201 H N N 114 
GG2 H202 H N N 115 
GG2 H211 H N N 116 
GG2 H212 H N N 117 
GG2 H22  H N N 118 
GG2 H241 H N N 119 
GG2 H242 H N N 120 
GG2 H5   H N N 121 
GG2 H6   H N N 122 
GG2 H44  H N N 123 
GG2 H18  H N N 124 
GG2 H251 H N N 125 
GG2 H252 H N N 126 
GG2 H231 H N N 127 
GG2 H232 H N N 128 
GG2 HN31 H N N 129 
GG2 HN32 H N N 130 
GG2 H171 H N N 131 
GG2 H172 H N N 132 
GLU N    N N N 133 
GLU CA   C N S 134 
GLU C    C N N 135 
GLU O    O N N 136 
GLU CB   C N N 137 
GLU CG   C N N 138 
GLU CD   C N N 139 
GLU OE1  O N N 140 
GLU OE2  O N N 141 
GLU OXT  O N N 142 
GLU H    H N N 143 
GLU H2   H N N 144 
GLU HA   H N N 145 
GLU HB2  H N N 146 
GLU HB3  H N N 147 
GLU HG2  H N N 148 
GLU HG3  H N N 149 
GLU HE2  H N N 150 
GLU HXT  H N N 151 
GLY N    N N N 152 
GLY CA   C N N 153 
GLY C    C N N 154 
GLY O    O N N 155 
GLY OXT  O N N 156 
GLY H    H N N 157 
GLY H2   H N N 158 
GLY HA2  H N N 159 
GLY HA3  H N N 160 
GLY HXT  H N N 161 
HOH O    O N N 162 
HOH H1   H N N 163 
HOH H2   H N N 164 
ILE N    N N N 165 
ILE CA   C N S 166 
ILE C    C N N 167 
ILE O    O N N 168 
ILE CB   C N S 169 
ILE CG1  C N N 170 
ILE CG2  C N N 171 
ILE CD1  C N N 172 
ILE OXT  O N N 173 
ILE H    H N N 174 
ILE H2   H N N 175 
ILE HA   H N N 176 
ILE HB   H N N 177 
ILE HG12 H N N 178 
ILE HG13 H N N 179 
ILE HG21 H N N 180 
ILE HG22 H N N 181 
ILE HG23 H N N 182 
ILE HD11 H N N 183 
ILE HD12 H N N 184 
ILE HD13 H N N 185 
ILE HXT  H N N 186 
LEU N    N N N 187 
LEU CA   C N S 188 
LEU C    C N N 189 
LEU O    O N N 190 
LEU CB   C N N 191 
LEU CG   C N N 192 
LEU CD1  C N N 193 
LEU CD2  C N N 194 
LEU OXT  O N N 195 
LEU H    H N N 196 
LEU H2   H N N 197 
LEU HA   H N N 198 
LEU HB2  H N N 199 
LEU HB3  H N N 200 
LEU HG   H N N 201 
LEU HD11 H N N 202 
LEU HD12 H N N 203 
LEU HD13 H N N 204 
LEU HD21 H N N 205 
LEU HD22 H N N 206 
LEU HD23 H N N 207 
LEU HXT  H N N 208 
LYS N    N N N 209 
LYS CA   C N S 210 
LYS C    C N N 211 
LYS O    O N N 212 
LYS CB   C N N 213 
LYS CG   C N N 214 
LYS CD   C N N 215 
LYS CE   C N N 216 
LYS NZ   N N N 217 
LYS OXT  O N N 218 
LYS H    H N N 219 
LYS H2   H N N 220 
LYS HA   H N N 221 
LYS HB2  H N N 222 
LYS HB3  H N N 223 
LYS HG2  H N N 224 
LYS HG3  H N N 225 
LYS HD2  H N N 226 
LYS HD3  H N N 227 
LYS HE2  H N N 228 
LYS HE3  H N N 229 
LYS HZ1  H N N 230 
LYS HZ2  H N N 231 
LYS HZ3  H N N 232 
LYS HXT  H N N 233 
MET N    N N N 234 
MET CA   C N S 235 
MET C    C N N 236 
MET O    O N N 237 
MET CB   C N N 238 
MET CG   C N N 239 
MET SD   S N N 240 
MET CE   C N N 241 
MET OXT  O N N 242 
MET H    H N N 243 
MET H2   H N N 244 
MET HA   H N N 245 
MET HB2  H N N 246 
MET HB3  H N N 247 
MET HG2  H N N 248 
MET HG3  H N N 249 
MET HE1  H N N 250 
MET HE2  H N N 251 
MET HE3  H N N 252 
MET HXT  H N N 253 
PHE N    N N N 254 
PHE CA   C N S 255 
PHE C    C N N 256 
PHE O    O N N 257 
PHE CB   C N N 258 
PHE CG   C Y N 259 
PHE CD1  C Y N 260 
PHE CD2  C Y N 261 
PHE CE1  C Y N 262 
PHE CE2  C Y N 263 
PHE CZ   C Y N 264 
PHE OXT  O N N 265 
PHE H    H N N 266 
PHE H2   H N N 267 
PHE HA   H N N 268 
PHE HB2  H N N 269 
PHE HB3  H N N 270 
PHE HD1  H N N 271 
PHE HD2  H N N 272 
PHE HE1  H N N 273 
PHE HE2  H N N 274 
PHE HZ   H N N 275 
PHE HXT  H N N 276 
PRO N    N N N 277 
PRO CA   C N S 278 
PRO C    C N N 279 
PRO O    O N N 280 
PRO CB   C N N 281 
PRO CG   C N N 282 
PRO CD   C N N 283 
PRO OXT  O N N 284 
PRO H    H N N 285 
PRO HA   H N N 286 
PRO HB2  H N N 287 
PRO HB3  H N N 288 
PRO HG2  H N N 289 
PRO HG3  H N N 290 
PRO HD2  H N N 291 
PRO HD3  H N N 292 
PRO HXT  H N N 293 
SER N    N N N 294 
SER CA   C N S 295 
SER C    C N N 296 
SER O    O N N 297 
SER CB   C N N 298 
SER OG   O N N 299 
SER OXT  O N N 300 
SER H    H N N 301 
SER H2   H N N 302 
SER HA   H N N 303 
SER HB2  H N N 304 
SER HB3  H N N 305 
SER HG   H N N 306 
SER HXT  H N N 307 
THR N    N N N 308 
THR CA   C N S 309 
THR C    C N N 310 
THR O    O N N 311 
THR CB   C N R 312 
THR OG1  O N N 313 
THR CG2  C N N 314 
THR OXT  O N N 315 
THR H    H N N 316 
THR H2   H N N 317 
THR HA   H N N 318 
THR HB   H N N 319 
THR HG1  H N N 320 
THR HG21 H N N 321 
THR HG22 H N N 322 
THR HG23 H N N 323 
THR HXT  H N N 324 
TRP N    N N N 325 
TRP CA   C N S 326 
TRP C    C N N 327 
TRP O    O N N 328 
TRP CB   C N N 329 
TRP CG   C Y N 330 
TRP CD1  C Y N 331 
TRP CD2  C Y N 332 
TRP NE1  N Y N 333 
TRP CE2  C Y N 334 
TRP CE3  C Y N 335 
TRP CZ2  C Y N 336 
TRP CZ3  C Y N 337 
TRP CH2  C Y N 338 
TRP OXT  O N N 339 
TRP H    H N N 340 
TRP H2   H N N 341 
TRP HA   H N N 342 
TRP HB2  H N N 343 
TRP HB3  H N N 344 
TRP HD1  H N N 345 
TRP HE1  H N N 346 
TRP HE3  H N N 347 
TRP HZ2  H N N 348 
TRP HZ3  H N N 349 
TRP HH2  H N N 350 
TRP HXT  H N N 351 
TYR N    N N N 352 
TYR CA   C N S 353 
TYR C    C N N 354 
TYR O    O N N 355 
TYR CB   C N N 356 
TYR CG   C Y N 357 
TYR CD1  C Y N 358 
TYR CD2  C Y N 359 
TYR CE1  C Y N 360 
TYR CE2  C Y N 361 
TYR CZ   C Y N 362 
TYR OH   O N N 363 
TYR OXT  O N N 364 
TYR H    H N N 365 
TYR H2   H N N 366 
TYR HA   H N N 367 
TYR HB2  H N N 368 
TYR HB3  H N N 369 
TYR HD1  H N N 370 
TYR HD2  H N N 371 
TYR HE1  H N N 372 
TYR HE2  H N N 373 
TYR HH   H N N 374 
TYR HXT  H N N 375 
VAL N    N N N 376 
VAL CA   C N S 377 
VAL C    C N N 378 
VAL O    O N N 379 
VAL CB   C N N 380 
VAL CG1  C N N 381 
VAL CG2  C N N 382 
VAL OXT  O N N 383 
VAL H    H N N 384 
VAL H2   H N N 385 
VAL HA   H N N 386 
VAL HB   H N N 387 
VAL HG11 H N N 388 
VAL HG12 H N N 389 
VAL HG13 H N N 390 
VAL HG21 H N N 391 
VAL HG22 H N N 392 
VAL HG23 H N N 393 
VAL HXT  H N N 394 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GG2 C1  C2   sing Y N 70  
GG2 C1  O4   sing N N 71  
GG2 C1  C6   doub Y N 72  
GG2 C2  C3   doub Y N 73  
GG2 C2  H2   sing N N 74  
GG2 C3  C4   sing Y N 75  
GG2 C3  H3   sing N N 76  
GG2 O4  C15  sing N N 77  
GG2 N6  N1   sing N N 78  
GG2 N6  C10  doub N N 79  
GG2 C7  C44  doub Y N 80  
GG2 C7  C22  sing Y N 81  
GG2 C7  N5   sing N N 82  
GG2 C8  N5   sing N N 83  
GG2 C8  O3   doub N N 84  
GG2 C8  C13  sing N N 85  
GG2 C10 C12  sing N N 86  
GG2 C10 C11  sing N N 87  
GG2 C11 O1   doub N N 88  
GG2 C11 N3   sing N N 89  
GG2 C12 C17  sing N N 90  
GG2 C12 C13  doub N N 91  
GG2 C13 N1   sing N N 92  
GG2 C14 C16  doub Y N 93  
GG2 C14 C44  sing Y N 94  
GG2 C14 H14  sing N N 95  
GG2 C15 H151 sing N N 96  
GG2 C15 H152 sing N N 97  
GG2 C15 H153 sing N N 98  
GG2 C16 N2   sing N N 99  
GG2 C16 C18  sing Y N 100 
GG2 C19 C23  sing N N 101 
GG2 C19 O2   doub N N 102 
GG2 C19 N2   sing N N 103 
GG2 C20 C21  sing N N 104 
GG2 C20 N2   sing N N 105 
GG2 C20 H201 sing N N 106 
GG2 C20 H202 sing N N 107 
GG2 C21 C25  sing N N 108 
GG2 C21 H211 sing N N 109 
GG2 C21 H212 sing N N 110 
GG2 C22 C18  doub Y N 111 
GG2 C22 H22  sing N N 112 
GG2 C24 N5   sing N N 113 
GG2 C24 C17  sing N N 114 
GG2 C24 H241 sing N N 115 
GG2 C24 H242 sing N N 116 
GG2 C4  N1   sing N N 117 
GG2 C4  C5   doub Y N 118 
GG2 C5  C6   sing Y N 119 
GG2 C5  H5   sing N N 120 
GG2 C6  H6   sing N N 121 
GG2 C44 H44  sing N N 122 
GG2 C18 H18  sing N N 123 
GG2 C25 C23  sing N N 124 
GG2 C25 H251 sing N N 125 
GG2 C25 H252 sing N N 126 
GG2 C23 H231 sing N N 127 
GG2 C23 H232 sing N N 128 
GG2 N3  HN31 sing N N 129 
GG2 N3  HN32 sing N N 130 
GG2 C17 H171 sing N N 131 
GG2 C17 H172 sing N N 132 
GLU N   CA   sing N N 133 
GLU N   H    sing N N 134 
GLU N   H2   sing N N 135 
GLU CA  C    sing N N 136 
GLU CA  CB   sing N N 137 
GLU CA  HA   sing N N 138 
GLU C   O    doub N N 139 
GLU C   OXT  sing N N 140 
GLU CB  CG   sing N N 141 
GLU CB  HB2  sing N N 142 
GLU CB  HB3  sing N N 143 
GLU CG  CD   sing N N 144 
GLU CG  HG2  sing N N 145 
GLU CG  HG3  sing N N 146 
GLU CD  OE1  doub N N 147 
GLU CD  OE2  sing N N 148 
GLU OE2 HE2  sing N N 149 
GLU OXT HXT  sing N N 150 
GLY N   CA   sing N N 151 
GLY N   H    sing N N 152 
GLY N   H2   sing N N 153 
GLY CA  C    sing N N 154 
GLY CA  HA2  sing N N 155 
GLY CA  HA3  sing N N 156 
GLY C   O    doub N N 157 
GLY C   OXT  sing N N 158 
GLY OXT HXT  sing N N 159 
HOH O   H1   sing N N 160 
HOH O   H2   sing N N 161 
ILE N   CA   sing N N 162 
ILE N   H    sing N N 163 
ILE N   H2   sing N N 164 
ILE CA  C    sing N N 165 
ILE CA  CB   sing N N 166 
ILE CA  HA   sing N N 167 
ILE C   O    doub N N 168 
ILE C   OXT  sing N N 169 
ILE CB  CG1  sing N N 170 
ILE CB  CG2  sing N N 171 
ILE CB  HB   sing N N 172 
ILE CG1 CD1  sing N N 173 
ILE CG1 HG12 sing N N 174 
ILE CG1 HG13 sing N N 175 
ILE CG2 HG21 sing N N 176 
ILE CG2 HG22 sing N N 177 
ILE CG2 HG23 sing N N 178 
ILE CD1 HD11 sing N N 179 
ILE CD1 HD12 sing N N 180 
ILE CD1 HD13 sing N N 181 
ILE OXT HXT  sing N N 182 
LEU N   CA   sing N N 183 
LEU N   H    sing N N 184 
LEU N   H2   sing N N 185 
LEU CA  C    sing N N 186 
LEU CA  CB   sing N N 187 
LEU CA  HA   sing N N 188 
LEU C   O    doub N N 189 
LEU C   OXT  sing N N 190 
LEU CB  CG   sing N N 191 
LEU CB  HB2  sing N N 192 
LEU CB  HB3  sing N N 193 
LEU CG  CD1  sing N N 194 
LEU CG  CD2  sing N N 195 
LEU CG  HG   sing N N 196 
LEU CD1 HD11 sing N N 197 
LEU CD1 HD12 sing N N 198 
LEU CD1 HD13 sing N N 199 
LEU CD2 HD21 sing N N 200 
LEU CD2 HD22 sing N N 201 
LEU CD2 HD23 sing N N 202 
LEU OXT HXT  sing N N 203 
LYS N   CA   sing N N 204 
LYS N   H    sing N N 205 
LYS N   H2   sing N N 206 
LYS CA  C    sing N N 207 
LYS CA  CB   sing N N 208 
LYS CA  HA   sing N N 209 
LYS C   O    doub N N 210 
LYS C   OXT  sing N N 211 
LYS CB  CG   sing N N 212 
LYS CB  HB2  sing N N 213 
LYS CB  HB3  sing N N 214 
LYS CG  CD   sing N N 215 
LYS CG  HG2  sing N N 216 
LYS CG  HG3  sing N N 217 
LYS CD  CE   sing N N 218 
LYS CD  HD2  sing N N 219 
LYS CD  HD3  sing N N 220 
LYS CE  NZ   sing N N 221 
LYS CE  HE2  sing N N 222 
LYS CE  HE3  sing N N 223 
LYS NZ  HZ1  sing N N 224 
LYS NZ  HZ2  sing N N 225 
LYS NZ  HZ3  sing N N 226 
LYS OXT HXT  sing N N 227 
MET N   CA   sing N N 228 
MET N   H    sing N N 229 
MET N   H2   sing N N 230 
MET CA  C    sing N N 231 
MET CA  CB   sing N N 232 
MET CA  HA   sing N N 233 
MET C   O    doub N N 234 
MET C   OXT  sing N N 235 
MET CB  CG   sing N N 236 
MET CB  HB2  sing N N 237 
MET CB  HB3  sing N N 238 
MET CG  SD   sing N N 239 
MET CG  HG2  sing N N 240 
MET CG  HG3  sing N N 241 
MET SD  CE   sing N N 242 
MET CE  HE1  sing N N 243 
MET CE  HE2  sing N N 244 
MET CE  HE3  sing N N 245 
MET OXT HXT  sing N N 246 
PHE N   CA   sing N N 247 
PHE N   H    sing N N 248 
PHE N   H2   sing N N 249 
PHE CA  C    sing N N 250 
PHE CA  CB   sing N N 251 
PHE CA  HA   sing N N 252 
PHE C   O    doub N N 253 
PHE C   OXT  sing N N 254 
PHE CB  CG   sing N N 255 
PHE CB  HB2  sing N N 256 
PHE CB  HB3  sing N N 257 
PHE CG  CD1  doub Y N 258 
PHE CG  CD2  sing Y N 259 
PHE CD1 CE1  sing Y N 260 
PHE CD1 HD1  sing N N 261 
PHE CD2 CE2  doub Y N 262 
PHE CD2 HD2  sing N N 263 
PHE CE1 CZ   doub Y N 264 
PHE CE1 HE1  sing N N 265 
PHE CE2 CZ   sing Y N 266 
PHE CE2 HE2  sing N N 267 
PHE CZ  HZ   sing N N 268 
PHE OXT HXT  sing N N 269 
PRO N   CA   sing N N 270 
PRO N   CD   sing N N 271 
PRO N   H    sing N N 272 
PRO CA  C    sing N N 273 
PRO CA  CB   sing N N 274 
PRO CA  HA   sing N N 275 
PRO C   O    doub N N 276 
PRO C   OXT  sing N N 277 
PRO CB  CG   sing N N 278 
PRO CB  HB2  sing N N 279 
PRO CB  HB3  sing N N 280 
PRO CG  CD   sing N N 281 
PRO CG  HG2  sing N N 282 
PRO CG  HG3  sing N N 283 
PRO CD  HD2  sing N N 284 
PRO CD  HD3  sing N N 285 
PRO OXT HXT  sing N N 286 
SER N   CA   sing N N 287 
SER N   H    sing N N 288 
SER N   H2   sing N N 289 
SER CA  C    sing N N 290 
SER CA  CB   sing N N 291 
SER CA  HA   sing N N 292 
SER C   O    doub N N 293 
SER C   OXT  sing N N 294 
SER CB  OG   sing N N 295 
SER CB  HB2  sing N N 296 
SER CB  HB3  sing N N 297 
SER OG  HG   sing N N 298 
SER OXT HXT  sing N N 299 
THR N   CA   sing N N 300 
THR N   H    sing N N 301 
THR N   H2   sing N N 302 
THR CA  C    sing N N 303 
THR CA  CB   sing N N 304 
THR CA  HA   sing N N 305 
THR C   O    doub N N 306 
THR C   OXT  sing N N 307 
THR CB  OG1  sing N N 308 
THR CB  CG2  sing N N 309 
THR CB  HB   sing N N 310 
THR OG1 HG1  sing N N 311 
THR CG2 HG21 sing N N 312 
THR CG2 HG22 sing N N 313 
THR CG2 HG23 sing N N 314 
THR OXT HXT  sing N N 315 
TRP N   CA   sing N N 316 
TRP N   H    sing N N 317 
TRP N   H2   sing N N 318 
TRP CA  C    sing N N 319 
TRP CA  CB   sing N N 320 
TRP CA  HA   sing N N 321 
TRP C   O    doub N N 322 
TRP C   OXT  sing N N 323 
TRP CB  CG   sing N N 324 
TRP CB  HB2  sing N N 325 
TRP CB  HB3  sing N N 326 
TRP CG  CD1  doub Y N 327 
TRP CG  CD2  sing Y N 328 
TRP CD1 NE1  sing Y N 329 
TRP CD1 HD1  sing N N 330 
TRP CD2 CE2  doub Y N 331 
TRP CD2 CE3  sing Y N 332 
TRP NE1 CE2  sing Y N 333 
TRP NE1 HE1  sing N N 334 
TRP CE2 CZ2  sing Y N 335 
TRP CE3 CZ3  doub Y N 336 
TRP CE3 HE3  sing N N 337 
TRP CZ2 CH2  doub Y N 338 
TRP CZ2 HZ2  sing N N 339 
TRP CZ3 CH2  sing Y N 340 
TRP CZ3 HZ3  sing N N 341 
TRP CH2 HH2  sing N N 342 
TRP OXT HXT  sing N N 343 
TYR N   CA   sing N N 344 
TYR N   H    sing N N 345 
TYR N   H2   sing N N 346 
TYR CA  C    sing N N 347 
TYR CA  CB   sing N N 348 
TYR CA  HA   sing N N 349 
TYR C   O    doub N N 350 
TYR C   OXT  sing N N 351 
TYR CB  CG   sing N N 352 
TYR CB  HB2  sing N N 353 
TYR CB  HB3  sing N N 354 
TYR CG  CD1  doub Y N 355 
TYR CG  CD2  sing Y N 356 
TYR CD1 CE1  sing Y N 357 
TYR CD1 HD1  sing N N 358 
TYR CD2 CE2  doub Y N 359 
TYR CD2 HD2  sing N N 360 
TYR CE1 CZ   doub Y N 361 
TYR CE1 HE1  sing N N 362 
TYR CE2 CZ   sing Y N 363 
TYR CE2 HE2  sing N N 364 
TYR CZ  OH   sing N N 365 
TYR OH  HH   sing N N 366 
TYR OXT HXT  sing N N 367 
VAL N   CA   sing N N 368 
VAL N   H    sing N N 369 
VAL N   H2   sing N N 370 
VAL CA  C    sing N N 371 
VAL CA  CB   sing N N 372 
VAL CA  HA   sing N N 373 
VAL C   O    doub N N 374 
VAL C   OXT  sing N N 375 
VAL CB  CG1  sing N N 376 
VAL CB  CG2  sing N N 377 
VAL CB  HB   sing N N 378 
VAL CG1 HG11 sing N N 379 
VAL CG1 HG12 sing N N 380 
VAL CG1 HG13 sing N N 381 
VAL CG2 HG21 sing N N 382 
VAL CG2 HG22 sing N N 383 
VAL CG2 HG23 sing N N 384 
VAL OXT HXT  sing N N 385 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute on Aging (NIH/NIA)' 'United States' ? 1 
'Howard Hughes Medical Institute (HHMI)'                              'United States' ? 2 
'Department of Defense (DOD, United States)'                          'United States' ? 3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             other 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'In house de novo designed model' 
# 
_space_group.name_H-M_alt     'C 2 2 21' 
_space_group.name_Hall        'C 2c 2' 
_space_group.IT_number        20 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8VEZ 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.018191 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.015582 
_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]   0.016637 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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 4   ? 24.25692 -0.43069 -14.52701 1.000 59.91402  ? 0   SER A N   1 
ATOM   2   C CA  . SER A 1 4   ? 24.74978 0.55857  -13.57595 1.000 57.72027  ? 0   SER A CA  1 
ATOM   3   C C   . SER A 1 4   ? 24.94470 1.91117  -14.25356 1.000 53.38132  ? 0   SER A C   1 
ATOM   4   O O   . SER A 1 4   ? 24.60494 2.95239  -13.69158 1.000 62.44978  ? 0   SER A O   1 
ATOM   5   C CB  . SER A 1 4   ? 26.05919 0.08772  -12.94275 1.000 60.13851  ? 0   SER A CB  1 
ATOM   6   O OG  . SER A 1 4   ? 26.98490 -0.32497 -13.93220 1.000 69.41562  ? 0   SER A OG  1 
ATOM   7   N N   . SER A 1 5   ? 25.50037 1.88920  -15.46714 1.000 66.18065  ? 1   SER A N   1 
ATOM   8   C CA  . SER A 1 5   ? 25.63373 3.12257  -16.23537 1.000 47.17056  ? 1   SER A CA  1 
ATOM   9   C C   . SER A 1 5   ? 24.28055 3.59030  -16.75322 1.000 47.17307  ? 1   SER A C   1 
ATOM   10  O O   . SER A 1 5   ? 24.00983 4.79593  -16.80258 1.000 56.82202  ? 1   SER A O   1 
ATOM   11  C CB  . SER A 1 5   ? 26.60863 2.91945  -17.39330 1.000 58.68993  ? 1   SER A CB  1 
ATOM   12  O OG  . SER A 1 5   ? 26.34260 1.70529  -18.07263 1.000 58.24895  ? 1   SER A OG  1 
ATOM   13  N N   . ALA A 1 6   ? 23.42027 2.64827  -17.14867 1.000 45.81877  ? 2   ALA A N   1 
ATOM   14  C CA  . ALA A 1 6   ? 22.06429 3.00246  -17.55144 1.000 54.51083  ? 2   ALA A CA  1 
ATOM   15  C C   . ALA A 1 6   ? 21.28508 3.61035  -16.39622 1.000 46.78768  ? 2   ALA A C   1 
ATOM   16  O O   . ALA A 1 6   ? 20.38391 4.42820  -16.61479 1.000 53.78942  ? 2   ALA A O   1 
ATOM   17  C CB  . ALA A 1 6   ? 21.33634 1.77029  -18.08721 1.000 52.30266  ? 2   ALA A CB  1 
ATOM   18  N N   . ARG A 1 7   ? 21.61691 3.22205  -15.16366 1.000 57.36667  ? 3   ARG A N   1 
ATOM   19  C CA  . ARG A 1 7   ? 20.94270 3.78235  -13.99879 1.000 57.93937  ? 3   ARG A CA  1 
ATOM   20  C C   . ARG A 1 7   ? 21.26476 5.26225  -13.83607 1.000 50.18717  ? 3   ARG A C   1 
ATOM   21  O O   . ARG A 1 7   ? 20.40132 6.05083  -13.43334 1.000 56.14706  ? 3   ARG A O   1 
ATOM   22  C CB  . ARG A 1 7   ? 21.33685 2.99832  -12.74834 1.000 61.85866  ? 3   ARG A CB  1 
ATOM   23  C CG  . ARG A 1 7   ? 20.79306 1.57792  -12.72062 1.000 53.84443  ? 3   ARG A CG  1 
ATOM   24  C CD  . ARG A 1 7   ? 21.27633 0.82356  -11.49374 1.000 67.90063  ? 3   ARG A CD  1 
ATOM   25  N NE  . ARG A 1 7   ? 20.76662 1.40919  -10.25999 1.000 81.47825  ? 3   ARG A NE  1 
ATOM   26  C CZ  . ARG A 1 7   ? 21.47849 1.55643  -9.15122  1.000 80.14153  ? 3   ARG A CZ  1 
ATOM   27  N NH1 . ARG A 1 7   ? 22.74170 1.16853  -9.08407  1.000 79.47930  ? 3   ARG A NH1 1 
ATOM   28  N NH2 . ARG A 1 7   ? 20.90860 2.10620  -8.08276  1.000 73.11820  ? 3   ARG A NH2 1 
ATOM   29  N N   . ILE A 1 8   ? 22.50180 5.65672  -14.14550 1.000 49.94430  ? 4   ILE A N   1 
ATOM   30  C CA  . ILE A 1 8   ? 22.86187 7.07213  -14.12403 1.000 47.67288  ? 4   ILE A CA  1 
ATOM   31  C C   . ILE A 1 8   ? 22.05403 7.83448  -15.16660 1.000 59.89859  ? 4   ILE A C   1 
ATOM   32  O O   . ILE A 1 8   ? 21.50673 8.90993  -14.89370 1.000 50.29061  ? 4   ILE A O   1 
ATOM   33  C CB  . ILE A 1 8   ? 24.37557 7.24383  -14.34641 1.000 53.38641  ? 4   ILE A CB  1 
ATOM   34  C CG1 . ILE A 1 8   ? 25.15174 6.82092  -13.09652 1.000 44.88114  ? 4   ILE A CG1 1 
ATOM   35  C CG2 . ILE A 1 8   ? 24.70253 8.68183  -14.73095 1.000 53.06849  ? 4   ILE A CG2 1 
ATOM   36  C CD1 . ILE A 1 8   ? 26.58674 7.30277  -13.07249 1.000 61.93300  ? 4   ILE A CD1 1 
ATOM   37  N N   . ALA A 1 9   ? 21.96200 7.28019  -16.37819 1.000 47.02855  ? 5   ALA A N   1 
ATOM   38  C CA  . ALA A 1 9   ? 21.17799 7.92002  -17.42919 1.000 45.91259  ? 5   ALA A CA  1 
ATOM   39  C C   . ALA A 1 9   ? 19.69198 7.90903  -17.09507 1.000 42.25857  ? 5   ALA A C   1 
ATOM   40  O O   . ALA A 1 9   ? 18.99033 8.89971  -17.33296 1.000 50.90829  ? 5   ALA A O   1 
ATOM   41  C CB  . ALA A 1 9   ? 21.43398 7.23051  -18.76879 1.000 45.24838  ? 5   ALA A CB  1 
ATOM   42  N N   . LYS A 1 10  ? 19.19370 6.79618  -16.54883 1.000 53.72911  ? 6   LYS A N   1 
ATOM   43  C CA  . LYS A 1 10  ? 17.80280 6.74810  -16.11099 1.000 53.52491  ? 6   LYS A CA  1 
ATOM   44  C C   . LYS A 1 10  ? 17.52491 7.81395  -15.06074 1.000 46.58954  ? 6   LYS A C   1 
ATOM   45  O O   . LYS A 1 10  ? 16.47639 8.46773  -15.09123 1.000 51.42331  ? 6   LYS A O   1 
ATOM   46  C CB  . LYS A 1 10  ? 17.46870 5.36024  -15.56359 1.000 54.15807  ? 6   LYS A CB  1 
ATOM   47  C CG  . LYS A 1 10  ? 16.45424 4.58787  -16.38851 1.000 64.52988  ? 6   LYS A CG  1 
ATOM   48  C CD  . LYS A 1 10  ? 16.97400 4.30989  -17.78726 1.000 62.93509  ? 6   LYS A CD  1 
ATOM   49  C CE  . LYS A 1 10  ? 16.32594 3.06739  -18.37296 1.000 64.35190  ? 6   LYS A CE  1 
ATOM   50  N NZ  . LYS A 1 10  ? 14.85384 3.22832  -18.53200 1.000 63.29167  ? 6   LYS A NZ  1 
ATOM   51  N N   . ALA A 1 11  ? 18.46053 8.00961  -14.12827 1.000 43.91811  ? 7   ALA A N   1 
ATOM   52  C CA  . ALA A 1 11  ? 18.27329 9.01781  -13.09083 1.000 48.08251  ? 7   ALA A CA  1 
ATOM   53  C C   . ALA A 1 11  ? 18.17466 10.41494 -13.68903 1.000 52.04635  ? 7   ALA A C   1 
ATOM   54  O O   . ALA A 1 11  ? 17.31653 11.20890 -13.28787 1.000 50.77146  ? 7   ALA A O   1 
ATOM   55  C CB  . ALA A 1 11  ? 19.41456 8.94534  -12.07664 1.000 49.23791  ? 7   ALA A CB  1 
ATOM   56  N N   . LYS A 1 12  ? 19.03986 10.73089 -14.65658 1.000 40.27334  ? 8   LYS A N   1 
ATOM   57  C CA  . LYS A 1 12  ? 19.00398 12.05079 -15.27960 1.000 47.21043  ? 8   LYS A CA  1 
ATOM   58  C C   . LYS A 1 12  ? 17.67097 12.29889 -15.97414 1.000 42.65529  ? 8   LYS A C   1 
ATOM   59  O O   . LYS A 1 12  ? 17.11710 13.40196 -15.89569 1.000 46.50189  ? 8   LYS A O   1 
ATOM   60  C CB  . LYS A 1 12  ? 20.15921 12.19506 -16.26993 1.000 52.10268  ? 8   LYS A CB  1 
ATOM   61  C CG  . LYS A 1 12  ? 20.83730 13.55450 -16.23992 1.000 50.19402  ? 8   LYS A CG  1 
ATOM   62  C CD  . LYS A 1 12  ? 21.39099 13.92706 -17.60638 1.000 60.38877  ? 8   LYS A CD  1 
ATOM   63  C CE  . LYS A 1 12  ? 21.85766 15.37438 -17.63879 1.000 63.39284  ? 8   LYS A CE  1 
ATOM   64  N NZ  . LYS A 1 12  ? 22.51779 15.72034 -18.92878 1.000 62.90033  ? 8   LYS A NZ  1 
ATOM   65  N N   . LYS A 1 13  ? 17.13805 11.28194 -16.65568 1.000 51.61584  ? 9   LYS A N   1 
ATOM   66  C CA  . LYS A 1 13  ? 15.84162 11.42709 -17.30968 1.000 37.41853  ? 9   LYS A CA  1 
ATOM   67  C C   . LYS A 1 13  ? 14.71872 11.56081 -16.28939 1.000 48.37191  ? 9   LYS A C   1 
ATOM   68  O O   . LYS A 1 13  ? 13.78824 12.35373 -16.48077 1.000 34.30797  ? 9   LYS A O   1 
ATOM   69  C CB  . LYS A 1 13  ? 15.58480 10.23645 -18.23288 1.000 45.16769  ? 9   LYS A CB  1 
ATOM   70  C CG  . LYS A 1 13  ? 14.14917 10.12861 -18.72319 1.000 52.33325  ? 9   LYS A CG  1 
ATOM   71  C CD  . LYS A 1 13  ? 14.06038 9.30723  -19.99653 1.000 61.44883  ? 9   LYS A CD  1 
ATOM   72  C CE  . LYS A 1 13  ? 14.70430 7.94114  -19.82804 1.000 82.64082  ? 9   LYS A CE  1 
ATOM   73  N NZ  . LYS A 1 13  ? 15.53124 7.57948  -21.01262 1.000 62.63193  ? 9   LYS A NZ  1 
ATOM   74  N N   . LEU A 1 14  ? 14.78640 10.79142 -15.19970 1.000 44.06265  ? 10  LEU A N   1 
ATOM   75  C CA  . LEU A 1 14  ? 13.72596 10.83798 -14.19872 1.000 40.47745  ? 10  LEU A CA  1 
ATOM   76  C C   . LEU A 1 14  ? 13.68966 12.18125 -13.48229 1.000 40.06847  ? 10  LEU A C   1 
ATOM   77  O O   . LEU A 1 14  ? 12.63134 12.59421 -12.99485 1.000 45.90722  ? 10  LEU A O   1 
ATOM   78  C CB  . LEU A 1 14  ? 13.90117 9.70298  -13.18980 1.000 35.85107  ? 10  LEU A CB  1 
ATOM   79  C CG  . LEU A 1 14  ? 13.64833 8.28768  -13.72267 1.000 45.05115  ? 10  LEU A CG  1 
ATOM   80  C CD1 . LEU A 1 14  ? 14.37053 7.25227  -12.86496 1.000 47.11053  ? 10  LEU A CD1 1 
ATOM   81  C CD2 . LEU A 1 14  ? 12.16837 7.96470  -13.86311 1.000 50.81089  ? 10  LEU A CD2 1 
ATOM   82  N N   . ILE A 1 15  ? 14.82551 12.87614 -13.41300 1.000 38.52109  ? 11  ILE A N   1 
ATOM   83  C CA  . ILE A 1 15  ? 14.84845 14.20295 -12.80621 1.000 32.15838  ? 11  ILE A CA  1 
ATOM   84  C C   . ILE A 1 15  ? 14.09562 15.19603 -13.68102 1.000 40.37882  ? 11  ILE A C   1 
ATOM   85  O O   . ILE A 1 15  ? 13.25370 15.96153 -13.19688 1.000 39.51155  ? 11  ILE A O   1 
ATOM   86  C CB  . ILE A 1 15  ? 16.29767 14.65836 -12.55576 1.000 37.85044  ? 11  ILE A CB  1 
ATOM   87  C CG1 . ILE A 1 15  ? 16.99011 13.73947 -11.54362 1.000 46.10130  ? 11  ILE A CG1 1 
ATOM   88  C CG2 . ILE A 1 15  ? 16.32350 16.08768 -12.05846 1.000 35.07620  ? 11  ILE A CG2 1 
ATOM   89  C CD1 . ILE A 1 15  ? 16.11382 13.32204 -10.38669 1.000 38.36556  ? 11  ILE A CD1 1 
ATOM   90  N N   . TYR A 1 16  ? 14.38749 15.19793 -14.98459 1.000 39.68029  ? 12  TYR A N   1 
ATOM   91  C CA  . TYR A 1 16  ? 13.67426 16.08673 -15.89499 1.000 42.28554  ? 12  TYR A CA  1 
ATOM   92  C C   . TYR A 1 16  ? 12.20955 15.69353 -16.02529 1.000 34.95025  ? 12  TYR A C   1 
ATOM   93  O O   . TYR A 1 16  ? 11.35243 16.56145 -16.22823 1.000 40.72655  ? 12  TYR A O   1 
ATOM   94  C CB  . TYR A 1 16  ? 14.35295 16.09571 -17.26397 1.000 38.49873  ? 12  TYR A CB  1 
ATOM   95  C CG  . TYR A 1 16  ? 15.64455 16.87929 -17.28468 1.000 39.91586  ? 12  TYR A CG  1 
ATOM   96  C CD1 . TYR A 1 16  ? 15.63748 18.26688 -17.22633 1.000 31.55708  ? 12  TYR A CD1 1 
ATOM   97  C CD2 . TYR A 1 16  ? 16.87075 16.23259 -17.35487 1.000 42.02983  ? 12  TYR A CD2 1 
ATOM   98  C CE1 . TYR A 1 16  ? 16.81556 18.98903 -17.24051 1.000 37.89142  ? 12  TYR A CE1 1 
ATOM   99  C CE2 . TYR A 1 16  ? 18.05440 16.94597 -17.37083 1.000 37.20947  ? 12  TYR A CE2 1 
ATOM   100 C CZ  . TYR A 1 16  ? 18.02061 18.32372 -17.31319 1.000 38.37490  ? 12  TYR A CZ  1 
ATOM   101 O OH  . TYR A 1 16  ? 19.19498 19.04006 -17.32861 1.000 39.16719  ? 12  TYR A OH  1 
ATOM   102 N N   . LYS A 1 17  ? 11.90340 14.39923 -15.91497 1.000 31.09173  ? 13  LYS A N   1 
ATOM   103 C CA  . LYS A 1 17  ? 10.50869 13.97726 -15.84953 1.000 42.59787  ? 13  LYS A CA  1 
ATOM   104 C C   . LYS A 1 17  ? 9.84154  14.52295 -14.59472 1.000 37.53787  ? 13  LYS A C   1 
ATOM   105 O O   . LYS A 1 17  ? 8.72782  15.05648 -14.65118 1.000 41.59654  ? 13  LYS A O   1 
ATOM   106 C CB  . LYS A 1 17  ? 10.41536 12.45124 -15.89279 1.000 47.22217  ? 13  LYS A CB  1 
ATOM   107 C CG  . LYS A 1 17  ? 8.99554  11.91510 -15.77056 1.000 41.50077  ? 13  LYS A CG  1 
ATOM   108 C CD  . LYS A 1 17  ? 8.89448  10.48422 -16.27372 1.000 63.42302  ? 13  LYS A CD  1 
ATOM   109 C CE  . LYS A 1 17  ? 7.80329  10.34276 -17.32336 1.000 75.69356  ? 13  LYS A CE  1 
ATOM   110 N NZ  . LYS A 1 17  ? 8.14062  9.31229  -18.34448 1.000 79.04404  ? 13  LYS A NZ  1 
ATOM   111 N N   . LEU A 1 18  ? 10.52161 14.41027 -13.44949 1.000 44.79907  ? 14  LEU A N   1 
ATOM   112 C CA  . LEU A 1 18  ? 9.98095  14.93852 -12.20079 1.000 41.93063  ? 14  LEU A CA  1 
ATOM   113 C C   . LEU A 1 18  ? 9.70216  16.43219 -12.30645 1.000 41.41830  ? 14  LEU A C   1 
ATOM   114 O O   . LEU A 1 18  ? 8.72113  16.92955 -11.74197 1.000 46.84224  ? 14  LEU A O   1 
ATOM   115 C CB  . LEU A 1 18  ? 10.94972 14.65724 -11.05212 1.000 41.46896  ? 14  LEU A CB  1 
ATOM   116 C CG  . LEU A 1 18  ? 10.68766 13.41380 -10.20187 1.000 44.68668  ? 14  LEU A CG  1 
ATOM   117 C CD1 . LEU A 1 18  ? 11.68661 13.33564 -9.06065  1.000 54.72489  ? 14  LEU A CD1 1 
ATOM   118 C CD2 . LEU A 1 18  ? 9.26298  13.41373 -9.67024  1.000 38.56599  ? 14  LEU A CD2 1 
ATOM   119 N N   . GLU A 1 19  ? 10.55552 17.16287 -13.02818 1.000 36.94160  ? 15  GLU A N   1 
ATOM   120 C CA  . GLU A 1 19  ? 10.33990 18.59523 -13.20502 1.000 40.43262  ? 15  GLU A CA  1 
ATOM   121 C C   . GLU A 1 19  ? 9.02886  18.87008 -13.92627 1.000 51.56160  ? 15  GLU A C   1 
ATOM   122 O O   . GLU A 1 19  ? 8.28955  19.79121 -13.55880 1.000 44.17104  ? 15  GLU A O   1 
ATOM   123 C CB  . GLU A 1 19  ? 11.51288 19.20747 -13.96834 1.000 50.35507  ? 15  GLU A CB  1 
ATOM   124 C CG  . GLU A 1 19  ? 11.50763 20.72434 -14.01813 1.000 55.61547  ? 15  GLU A CG  1 
ATOM   125 C CD  . GLU A 1 19  ? 12.22557 21.26339 -15.23990 1.000 67.49526  ? 15  GLU A CD  1 
ATOM   126 O OE1 . GLU A 1 19  ? 11.90363 20.82103 -16.36287 1.000 82.39638  ? 15  GLU A OE1 1 
ATOM   127 O OE2 . GLU A 1 19  ? 13.11461 22.12527 -15.07739 1.000 69.66423  ? 15  GLU A OE2 1 
ATOM   128 N N   . LYS A 1 20  ? 8.72140  18.07775 -14.95431 1.000 53.78668  ? 16  LYS A N   1 
ATOM   129 C CA  . LYS A 1 20  ? 7.46196  18.25370 -15.66681 1.000 56.86091  ? 16  LYS A CA  1 
ATOM   130 C C   . LYS A 1 20  ? 6.27621  17.86320 -14.79366 1.000 49.34921  ? 16  LYS A C   1 
ATOM   131 O O   . LYS A 1 20  ? 5.26175  18.56835 -14.76834 1.000 55.73825  ? 16  LYS A O   1 
ATOM   132 C CB  . LYS A 1 20  ? 7.47366  17.43996 -16.96002 1.000 41.70497  ? 16  LYS A CB  1 
ATOM   133 C CG  . LYS A 1 20  ? 6.79101  18.12816 -18.12988 1.000 60.49569  ? 16  LYS A CG  1 
ATOM   134 C CD  . LYS A 1 20  ? 7.16266  17.46940 -19.44742 1.000 59.89256  ? 16  LYS A CD  1 
ATOM   135 C CE  . LYS A 1 20  ? 6.20382  16.34156 -19.78949 1.000 52.35357  ? 16  LYS A CE  1 
ATOM   136 N NZ  . LYS A 1 20  ? 6.52478  15.72265 -21.10487 1.000 57.38102  ? 16  LYS A NZ  1 
ATOM   137 N N   . LEU A 1 21  ? 6.38879  16.75022 -14.06226 1.000 47.35072  ? 17  LEU A N   1 
ATOM   138 C CA  . LEU A 1 21  ? 5.29351  16.32010 -13.19749 1.000 49.56378  ? 17  LEU A CA  1 
ATOM   139 C C   . LEU A 1 21  ? 5.04703  17.32023 -12.07454 1.000 51.05232  ? 17  LEU A C   1 
ATOM   140 O O   . LEU A 1 21  ? 3.89386  17.59431 -11.72146 1.000 51.60138  ? 17  LEU A O   1 
ATOM   141 C CB  . LEU A 1 21  ? 5.58527  14.93423 -12.62147 1.000 54.63184  ? 17  LEU A CB  1 
ATOM   142 C CG  . LEU A 1 21  ? 6.07267  13.84388 -13.57701 1.000 50.77659  ? 17  LEU A CG  1 
ATOM   143 C CD1 . LEU A 1 21  ? 6.58802  12.64417 -12.79732 1.000 37.61330  ? 17  LEU A CD1 1 
ATOM   144 C CD2 . LEU A 1 21  ? 4.97033  13.43002 -14.53838 1.000 53.04523  ? 17  LEU A CD2 1 
ATOM   145 N N   . TRP A 1 22  ? 6.11825  17.86991 -11.49570 1.000 44.80658  ? 18  TRP A N   1 
ATOM   146 C CA  . TRP A 1 22  ? 5.96383  18.87155 -10.44418 1.000 52.58367  ? 18  TRP A CA  1 
ATOM   147 C C   . TRP A 1 22  ? 5.24110  20.10560 -10.96860 1.000 53.80463  ? 18  TRP A C   1 
ATOM   148 O O   . TRP A 1 22  ? 4.26575  20.57259 -10.36861 1.000 50.60186  ? 18  TRP A O   1 
ATOM   149 C CB  . TRP A 1 22  ? 7.33114  19.25509 -9.87706  1.000 48.97981  ? 18  TRP A CB  1 
ATOM   150 C CG  . TRP A 1 22  ? 7.79796  18.39210 -8.74453  1.000 42.17008  ? 18  TRP A CG  1 
ATOM   151 C CD1 . TRP A 1 22  ? 8.79494  17.46062 -8.78094  1.000 42.43254  ? 18  TRP A CD1 1 
ATOM   152 C CD2 . TRP A 1 22  ? 7.29636  18.38973 -7.40238  1.000 53.96736  ? 18  TRP A CD2 1 
ATOM   153 N NE1 . TRP A 1 22  ? 8.94250  16.87550 -7.54704  1.000 45.48271  ? 18  TRP A NE1 1 
ATOM   154 C CE2 . TRP A 1 22  ? 8.03505  17.42885 -6.68264  1.000 50.37431  ? 18  TRP A CE2 1 
ATOM   155 C CE3 . TRP A 1 22  ? 6.29571  19.10679 -6.73944  1.000 47.98640  ? 18  TRP A CE3 1 
ATOM   156 C CZ2 . TRP A 1 22  ? 7.80275  17.16515 -5.33506  1.000 52.88021  ? 18  TRP A CZ2 1 
ATOM   157 C CZ3 . TRP A 1 22  ? 6.06729  18.84352 -5.40103  1.000 57.66694  ? 18  TRP A CZ3 1 
ATOM   158 C CH2 . TRP A 1 22  ? 6.81859  17.88246 -4.71325  1.000 53.61294  ? 18  TRP A CH2 1 
ATOM   159 N N   . ASN A 1 23  ? 5.70963  20.64851 -12.09493 1.000 55.42778  ? 19  ASN A N   1 
ATOM   160 C CA  . ASN A 1 23  ? 5.06546  21.81167 -12.69096 1.000 51.42799  ? 19  ASN A CA  1 
ATOM   161 C C   . ASN A 1 23  ? 3.67017  21.49320 -13.20935 1.000 48.23732  ? 19  ASN A C   1 
ATOM   162 O O   . ASN A 1 23  ? 2.84720  22.40506 -13.33893 1.000 51.72227  ? 19  ASN A O   1 
ATOM   163 C CB  . ASN A 1 23  ? 5.93337  22.36656 -13.82043 1.000 37.21839  ? 19  ASN A CB  1 
ATOM   164 C CG  . ASN A 1 23  ? 7.14920  23.11024 -13.30613 1.000 44.95836  ? 19  ASN A CG  1 
ATOM   165 O OD1 . ASN A 1 23  ? 7.29479  23.32530 -12.10366 1.000 54.75986  ? 19  ASN A OD1 1 
ATOM   166 N ND2 . ASN A 1 23  ? 8.03043  23.50779 -14.21633 1.000 49.73941  ? 19  ASN A ND2 1 
ATOM   167 N N   . ALA A 1 24  ? 3.38791  20.22680 -13.50815 1.000 45.58910  ? 20  ALA A N   1 
ATOM   168 C CA  . ALA A 1 24  ? 2.05582  19.79999 -13.90853 1.000 59.39598  ? 20  ALA A CA  1 
ATOM   169 C C   . ALA A 1 24  ? 1.20168  19.34275 -12.73503 1.000 68.32650  ? 20  ALA A C   1 
ATOM   170 O O   . ALA A 1 24  ? 0.01045  19.07808 -12.92549 1.000 66.86880  ? 20  ALA A O   1 
ATOM   171 C CB  . ALA A 1 24  ? 2.14847  18.66650 -14.93317 1.000 53.36158  ? 20  ALA A CB  1 
ATOM   172 N N   . ARG A 1 25  ? 1.78241  19.23961 -11.53747 1.000 57.24844  ? 21  ARG A N   1 
ATOM   173 C CA  . ARG A 1 25  ? 1.07934  18.77488 -10.34060 1.000 68.22317  ? 21  ARG A CA  1 
ATOM   174 C C   . ARG A 1 25  ? 0.53139  17.36197 -10.51500 1.000 71.04491  ? 21  ARG A C   1 
ATOM   175 O O   . ARG A 1 25  ? -0.45397 16.98210 -9.87648  1.000 69.52028  ? 21  ARG A O   1 
ATOM   176 C CB  . ARG A 1 25  ? -0.04246 19.73597 -9.93836  1.000 65.30205  ? 21  ARG A CB  1 
ATOM   177 C CG  . ARG A 1 25  ? 0.44111  21.12812 -9.57649  1.000 55.85401  ? 21  ARG A CG  1 
ATOM   178 C CD  . ARG A 1 25  ? -0.65257 21.92222 -8.88582  1.000 66.27126  ? 21  ARG A CD  1 
ATOM   179 N NE  . ARG A 1 25  ? -0.73094 21.60665 -7.46491  1.000 65.42438  ? 21  ARG A NE  1 
ATOM   180 C CZ  . ARG A 1 25  ? -0.06213 22.24712 -6.51615  1.000 59.95966  ? 21  ARG A CZ  1 
ATOM   181 N NH1 . ARG A 1 25  ? 0.74948  23.25271 -6.80050  1.000 61.24567  ? 21  ARG A NH1 1 
ATOM   182 N NH2 . ARG A 1 25  ? -0.20728 21.86542 -5.25064  1.000 64.34728  ? 21  ARG A NH2 1 
ATOM   183 N N   . ASP A 1 26  ? 1.16813  16.56910 -11.37771 1.000 63.65115  ? 22  ASP A N   1 
ATOM   184 C CA  . ASP A 1 26  ? 0.82413  15.15632 -11.53655 1.000 71.62599  ? 22  ASP A CA  1 
ATOM   185 C C   . ASP A 1 26  ? 1.27075  14.43226 -10.26980 1.000 75.31481  ? 22  ASP A C   1 
ATOM   186 O O   . ASP A 1 26  ? 2.27365  13.71670 -10.23954 1.000 76.90428  ? 22  ASP A O   1 
ATOM   187 C CB  . ASP A 1 26  ? 1.48755  14.56690 -12.77927 1.000 76.66341  ? 22  ASP A CB  1 
ATOM   188 C CG  . ASP A 1 26  ? 1.02686  13.14341 -13.08456 1.000 90.01677  ? 22  ASP A CG  1 
ATOM   189 O OD1 . ASP A 1 26  ? 0.60911  12.41480 -12.16193 1.000 95.60163  ? 22  ASP A OD1 1 
ATOM   190 O OD2 . ASP A 1 26  ? 1.12128  12.73820 -14.26061 1.000 88.94241  ? 22  ASP A OD2 1 
ATOM   191 N N   . ASN A 1 27  ? 0.50172  14.62550 -9.19789  1.000 69.95400  ? 23  ASN A N   1 
ATOM   192 C CA  . ASN A 1 27  ? 0.85475  14.01022 -7.92480  1.000 66.10636  ? 23  ASN A CA  1 
ATOM   193 C C   . ASN A 1 27  ? 0.73862  12.49459 -7.98570  1.000 79.42615  ? 23  ASN A C   1 
ATOM   194 O O   . ASN A 1 27  ? 1.48340  11.79106 -7.29438  1.000 85.65003  ? 23  ASN A O   1 
ATOM   195 C CB  . ASN A 1 27  ? -0.02556 14.57218 -6.80902  1.000 63.58674  ? 23  ASN A CB  1 
ATOM   196 C CG  . ASN A 1 27  ? 0.00026  16.08614 -6.75651  1.000 67.44222  ? 23  ASN A CG  1 
ATOM   197 O OD1 . ASN A 1 27  ? -1.04045 16.73149 -6.63890  1.000 78.09780  ? 23  ASN A OD1 1 
ATOM   198 N ND2 . ASN A 1 27  ? 1.19431  16.66200 -6.84484  1.000 67.45493  ? 23  ASN A ND2 1 
ATOM   199 N N   . ASP A 1 28  ? -0.18003 11.97670 -8.80388  1.000 88.31828  ? 24  ASP A N   1 
ATOM   200 C CA  . ASP A 1 28  ? -0.31065 10.53141 -8.95310  1.000 95.57177  ? 24  ASP A CA  1 
ATOM   201 C C   . ASP A 1 28  ? 0.92749  9.93931  -9.61135  1.000 89.16648  ? 24  ASP A C   1 
ATOM   202 O O   . ASP A 1 28  ? 1.45585  8.91648  -9.15957  1.000 88.84220  ? 24  ASP A O   1 
ATOM   203 C CB  . ASP A 1 28  ? -1.56266 10.19821 -9.76461  1.000 96.40427  ? 24  ASP A CB  1 
ATOM   204 C CG  . ASP A 1 28  ? -2.84144 10.48231 -9.00490  1.000 112.39222 ? 24  ASP A CG  1 
ATOM   205 O OD1 . ASP A 1 28  ? -2.77334 10.66094 -7.77070  1.000 119.00968 ? 24  ASP A OD1 1 
ATOM   206 O OD2 . ASP A 1 28  ? -3.91438 10.52825 -9.64254  1.000 115.21403 ? 24  ASP A OD2 1 
ATOM   207 N N   . GLY A 1 29  ? 1.40409  10.57159 -10.68463 1.000 68.47214  ? 25  GLY A N   1 
ATOM   208 C CA  . GLY A 1 29  ? 2.60739  10.08755 -11.33974 1.000 65.17885  ? 25  GLY A CA  1 
ATOM   209 C C   . GLY A 1 29  ? 3.83554  10.20781 -10.45725 1.000 66.06309  ? 25  GLY A C   1 
ATOM   210 O O   . GLY A 1 29  ? 4.64901  9.28553  -10.38161 1.000 60.91804  ? 25  GLY A O   1 
ATOM   211 N N   . ILE A 1 30  ? 3.97602  11.34933 -9.77260  1.000 71.73715  ? 26  ILE A N   1 
ATOM   212 C CA  . ILE A 1 30  ? 5.11256  11.56417 -8.87498  1.000 53.24108  ? 26  ILE A CA  1 
ATOM   213 C C   . ILE A 1 30  ? 5.21712  10.43352 -7.86170  1.000 64.71240  ? 26  ILE A C   1 
ATOM   214 O O   . ILE A 1 30  ? 6.31334  9.94344  -7.56202  1.000 68.71824  ? 26  ILE A O   1 
ATOM   215 C CB  . ILE A 1 30  ? 4.99564  12.93462 -8.17915  1.000 62.38136  ? 26  ILE A CB  1 
ATOM   216 C CG1 . ILE A 1 30  ? 5.20074  14.06912 -9.18344  1.000 54.83608  ? 26  ILE A CG1 1 
ATOM   217 C CG2 . ILE A 1 30  ? 6.00275  13.05180 -7.04275  1.000 54.93005  ? 26  ILE A CG2 1 
ATOM   218 C CD1 . ILE A 1 30  ? 4.72887  15.41914 -8.68488  1.000 54.32658  ? 26  ILE A CD1 1 
ATOM   219 N N   . LEU A 1 31  ? 4.07620  9.98988  -7.33067  1.000 68.90683  ? 27  LEU A N   1 
ATOM   220 C CA  . LEU A 1 31  ? 4.08481  8.90815  -6.35321  1.000 59.97699  ? 27  LEU A CA  1 
ATOM   221 C C   . LEU A 1 31  ? 4.55788  7.59499  -6.96185  1.000 65.84853  ? 27  LEU A C   1 
ATOM   222 O O   . LEU A 1 31  ? 5.19091  6.78876  -6.27198  1.000 65.85653  ? 27  LEU A O   1 
ATOM   223 C CB  . LEU A 1 31  ? 2.69080  8.73035  -5.75686  1.000 67.08118  ? 27  LEU A CB  1 
ATOM   224 C CG  . LEU A 1 31  ? 2.35991  9.53806  -4.50360  1.000 76.77016  ? 27  LEU A CG  1 
ATOM   225 C CD1 . LEU A 1 31  ? 1.02018  9.09066  -3.95116  1.000 70.56312  ? 27  LEU A CD1 1 
ATOM   226 C CD2 . LEU A 1 31  ? 3.45599  9.40154  -3.45760  1.000 62.96615  ? 27  LEU A CD2 1 
ATOM   227 N N   . LYS A 1 32  ? 4.26714  7.36178  -8.24389  1.000 64.39317  ? 28  LYS A N   1 
ATOM   228 C CA  . LYS A 1 32  ? 4.59018  6.07293  -8.84620  1.000 68.74902  ? 28  LYS A CA  1 
ATOM   229 C C   . LYS A 1 32  ? 6.09512  5.84828  -8.93650  1.000 63.40614  ? 28  LYS A C   1 
ATOM   230 O O   . LYS A 1 32  ? 6.54567  4.69747  -8.93848  1.000 61.26407  ? 28  LYS A O   1 
ATOM   231 C CB  . LYS A 1 32  ? 3.94279  5.96039  -10.22614 1.000 63.51197  ? 28  LYS A CB  1 
ATOM   232 C CG  . LYS A 1 32  ? 2.62157  5.20281  -10.21579 1.000 67.14045  ? 28  LYS A CG  1 
ATOM   233 C CD  . LYS A 1 32  ? 2.43141  4.38043  -11.47869 1.000 75.52005  ? 28  LYS A CD  1 
ATOM   234 C CE  . LYS A 1 32  ? 1.54762  5.10328  -12.48029 1.000 80.01688  ? 28  LYS A CE  1 
ATOM   235 N NZ  . LYS A 1 32  ? 0.54969  4.18964  -13.10597 1.000 70.46536  ? 28  LYS A NZ  1 
ATOM   236 N N   . LEU A 1 33  ? 6.88755  6.92132  -9.00941  1.000 61.80635  ? 29  LEU A N   1 
ATOM   237 C CA  . LEU A 1 33  ? 8.33583  6.77421  -8.92475  1.000 56.64665  ? 29  LEU A CA  1 
ATOM   238 C C   . LEU A 1 33  ? 8.81207  6.55695  -7.49701  1.000 57.18987  ? 29  LEU A C   1 
ATOM   239 O O   . LEU A 1 33  ? 9.95371  6.12799  -7.29574  1.000 55.78135  ? 29  LEU A O   1 
ATOM   240 C CB  . LEU A 1 33  ? 9.05123  7.99790  -9.50449  1.000 55.28321  ? 29  LEU A CB  1 
ATOM   241 C CG  . LEU A 1 33  ? 8.56913  8.62108  -10.81231 1.000 66.17890  ? 29  LEU A CG  1 
ATOM   242 C CD1 . LEU A 1 33  ? 7.65458  9.78387  -10.54453 1.000 71.23955  ? 29  LEU A CD1 1 
ATOM   243 C CD2 . LEU A 1 33  ? 9.75219  9.08597  -11.62814 1.000 68.40026  ? 29  LEU A CD2 1 
ATOM   244 N N   . PHE A 1 34  ? 7.97029  6.84501  -6.50961  1.000 59.11408  ? 30  PHE A N   1 
ATOM   245 C CA  . PHE A 1 34  ? 8.34812  6.67933  -5.11548  1.000 59.84860  ? 30  PHE A CA  1 
ATOM   246 C C   . PHE A 1 34  ? 8.17234  5.23129  -4.68072  1.000 59.57506  ? 30  PHE A C   1 
ATOM   247 O O   . PHE A 1 34  ? 7.21857  4.55795  -5.08187  1.000 60.80841  ? 30  PHE A O   1 
ATOM   248 C CB  . PHE A 1 34  ? 7.49651  7.58062  -4.22221  1.000 50.85733  ? 30  PHE A CB  1 
ATOM   249 C CG  . PHE A 1 34  ? 8.07464  8.94543  -3.99895  1.000 49.98808  ? 30  PHE A CG  1 
ATOM   250 C CD1 . PHE A 1 34  ? 9.01325  9.15929  -3.00513  1.000 46.97508  ? 30  PHE A CD1 1 
ATOM   251 C CD2 . PHE A 1 34  ? 7.66990  10.01830 -4.77416  1.000 55.81527  ? 30  PHE A CD2 1 
ATOM   252 C CE1 . PHE A 1 34  ? 9.54287  10.41555 -2.79329  1.000 53.24104  ? 30  PHE A CE1 1 
ATOM   253 C CE2 . PHE A 1 34  ? 8.19617  11.27592 -4.56807  1.000 52.03855  ? 30  PHE A CE2 1 
ATOM   254 C CZ  . PHE A 1 34  ? 9.13231  11.47444 -3.57533  1.000 57.50580  ? 30  PHE A CZ  1 
ATOM   255 N N   . LYS A 1 35  ? 9.10181  4.75141  -3.85930  1.000 60.50698  ? 31  LYS A N   1 
ATOM   256 C CA  . LYS A 1 35  ? 8.87342  3.50018  -3.15448  1.000 60.99121  ? 31  LYS A CA  1 
ATOM   257 C C   . LYS A 1 35  ? 7.71148  3.67407  -2.18376  1.000 63.56059  ? 31  LYS A C   1 
ATOM   258 O O   . LYS A 1 35  ? 7.47806  4.76218  -1.65044  1.000 69.55017  ? 31  LYS A O   1 
ATOM   259 C CB  . LYS A 1 35  ? 10.13545 3.06380  -2.40821  1.000 56.35578  ? 31  LYS A CB  1 
ATOM   260 C CG  . LYS A 1 35  ? 11.09172 2.22408  -3.24183  1.000 63.66747  ? 31  LYS A CG  1 
ATOM   261 C CD  . LYS A 1 35  ? 12.08366 1.47803  -2.36338  1.000 70.69517  ? 31  LYS A CD  1 
ATOM   262 C CE  . LYS A 1 35  ? 12.21274 0.02300  -2.78448  1.000 70.90046  ? 31  LYS A CE  1 
ATOM   263 N NZ  . LYS A 1 35  ? 12.58057 -0.11624 -4.22008  1.000 79.95315  ? 31  LYS A NZ  1 
ATOM   264 N N   . ASP A 1 36  ? 6.96919  2.58766  -1.96144  1.000 67.39329  ? 32  ASP A N   1 
ATOM   265 C CA  . ASP A 1 36  ? 5.76914  2.67127  -1.13567  1.000 75.70965  ? 32  ASP A CA  1 
ATOM   266 C C   . ASP A 1 36  ? 6.07581  3.06384  0.30454   1.000 63.94346  ? 32  ASP A C   1 
ATOM   267 O O   . ASP A 1 36  ? 5.17155  3.51147  1.01870   1.000 56.22783  ? 32  ASP A O   1 
ATOM   268 C CB  . ASP A 1 36  ? 5.01760  1.34049  -1.16890  1.000 79.06286  ? 32  ASP A CB  1 
ATOM   269 C CG  . ASP A 1 36  ? 4.49476  1.00086  -2.55120  1.000 80.86046  ? 32  ASP A CG  1 
ATOM   270 O OD1 . ASP A 1 36  ? 4.97251  1.60515  -3.53451  1.000 80.75345  ? 32  ASP A OD1 1 
ATOM   271 O OD2 . ASP A 1 36  ? 3.60590  0.12938  -2.65468  1.000 79.89934  ? 32  ASP A OD2 1 
ATOM   272 N N   . ASP A 1 37  ? 7.32481  2.91394  0.74442   1.000 69.28100  ? 33  ASP A N   1 
ATOM   273 C CA  . ASP A 1 37  ? 7.74310  3.29167  2.08874   1.000 60.16578  ? 33  ASP A CA  1 
ATOM   274 C C   . ASP A 1 37  ? 8.84236  4.34898  2.05162   1.000 58.48335  ? 33  ASP A C   1 
ATOM   275 O O   . ASP A 1 37  ? 9.71130  4.38405  2.92518   1.000 61.00584  ? 33  ASP A O   1 
ATOM   276 C CB  . ASP A 1 37  ? 8.20638  2.06416  2.87112   1.000 67.55540  ? 33  ASP A CB  1 
ATOM   277 C CG  . ASP A 1 37  ? 8.92745  1.05773  1.99742   1.000 74.00473  ? 33  ASP A CG  1 
ATOM   278 O OD1 . ASP A 1 37  ? 9.78049  1.47693  1.18720   1.000 75.17934  ? 33  ASP A OD1 1 
ATOM   279 O OD2 . ASP A 1 37  ? 8.63988  -0.15158 2.11839   1.000 75.13770  ? 33  ASP A OD2 1 
ATOM   280 N N   . ALA A 1 38  ? 8.81464  5.21609  1.04385   1.000 65.29056  ? 34  ALA A N   1 
ATOM   281 C CA  . ALA A 1 38  ? 9.84572  6.22729  0.88510   1.000 61.27155  ? 34  ALA A CA  1 
ATOM   282 C C   . ALA A 1 38  ? 9.66529  7.35133  1.90139   1.000 52.79396  ? 34  ALA A C   1 
ATOM   283 O O   . ALA A 1 38  ? 8.61385  7.49936  2.52924   1.000 53.05275  ? 34  ALA A O   1 
ATOM   284 C CB  . ALA A 1 38  ? 9.82869  6.79602  -0.53316  1.000 52.40412  ? 34  ALA A CB  1 
ATOM   285 N N   . VAL A 1 39  ? 10.71788 8.15035  2.05555   1.000 49.11740  ? 35  VAL A N   1 
ATOM   286 C CA  . VAL A 1 39  ? 10.73844 9.26876  2.99066   1.000 51.27933  ? 35  VAL A CA  1 
ATOM   287 C C   . VAL A 1 39  ? 10.88545 10.55843 2.19771   1.000 53.67253  ? 35  VAL A C   1 
ATOM   288 O O   . VAL A 1 39  ? 11.82054 10.70093 1.40235   1.000 46.30294  ? 35  VAL A O   1 
ATOM   289 C CB  . VAL A 1 39  ? 11.87752 9.13333  4.01806   1.000 55.20573  ? 35  VAL A CB  1 
ATOM   290 C CG1 . VAL A 1 39  ? 11.70289 10.14452 5.14175   1.000 44.61531  ? 35  VAL A CG1 1 
ATOM   291 C CG2 . VAL A 1 39  ? 11.93191 7.71744  4.57221   1.000 44.75099  ? 35  VAL A CG2 1 
ATOM   292 N N   . PHE A 1 40  ? 9.96055  11.48960 2.41343   1.000 47.36838  ? 36  PHE A N   1 
ATOM   293 C CA  . PHE A 1 40  ? 10.02572 12.82665 1.82958   1.000 44.97892  ? 36  PHE A CA  1 
ATOM   294 C C   . PHE A 1 40  ? 10.40169 13.79024 2.94952   1.000 42.37970  ? 36  PHE A C   1 
ATOM   295 O O   . PHE A 1 40  ? 9.56825  14.13043 3.79437   1.000 41.63588  ? 36  PHE A O   1 
ATOM   296 C CB  . PHE A 1 40  ? 8.70130  13.21139 1.17446   1.000 41.83777  ? 36  PHE A CB  1 
ATOM   297 C CG  . PHE A 1 40  ? 8.80537  14.37563 0.22775   1.000 50.08845  ? 36  PHE A CG  1 
ATOM   298 C CD1 . PHE A 1 40  ? 8.94492  15.66881 0.70694   1.000 47.78284  ? 36  PHE A CD1 1 
ATOM   299 C CD2 . PHE A 1 40  ? 8.76358  14.17560 -1.14208  1.000 38.80830  ? 36  PHE A CD2 1 
ATOM   300 C CE1 . PHE A 1 40  ? 9.04025  16.73899 -0.16160  1.000 42.90917  ? 36  PHE A CE1 1 
ATOM   301 C CE2 . PHE A 1 40  ? 8.85842  15.24299 -2.01549  1.000 42.44087  ? 36  PHE A CE2 1 
ATOM   302 C CZ  . PHE A 1 40  ? 8.99720  16.52533 -1.52464  1.000 42.51612  ? 36  PHE A CZ  1 
ATOM   303 N N   . ASN A 1 41  ? 11.66074 14.22146 2.95643   1.000 41.69870  ? 37  ASN A N   1 
ATOM   304 C CA  . ASN A 1 41  ? 12.15755 15.16065 3.95959   1.000 51.32249  ? 37  ASN A CA  1 
ATOM   305 C C   . ASN A 1 41  ? 11.89958 16.57352 3.45008   1.000 44.30107  ? 37  ASN A C   1 
ATOM   306 O O   . ASN A 1 41  ? 12.65025 17.09683 2.62296   1.000 41.56504  ? 37  ASN A O   1 
ATOM   307 C CB  . ASN A 1 41  ? 13.63678 14.91757 4.23773   1.000 38.29027  ? 37  ASN A CB  1 
ATOM   308 C CG  . ASN A 1 41  ? 14.11337 15.59671 5.50799   1.000 57.57963  ? 37  ASN A CG  1 
ATOM   309 O OD1 . ASN A 1 41  ? 13.80836 16.76245 5.75531   1.000 58.35342  ? 37  ASN A OD1 1 
ATOM   310 N ND2 . ASN A 1 41  ? 14.86366 14.86447 6.32423   1.000 60.75600  ? 37  ASN A ND2 1 
ATOM   311 N N   . LEU A 1 42  ? 10.83117 17.19401 3.94667   1.000 35.62231  ? 38  LEU A N   1 
ATOM   312 C CA  . LEU A 1 42  ? 10.42663 18.53439 3.52464   1.000 33.81305  ? 38  LEU A CA  1 
ATOM   313 C C   . LEU A 1 42  ? 10.99912 19.54135 4.51624   1.000 53.17468  ? 38  LEU A C   1 
ATOM   314 O O   . LEU A 1 42  ? 10.36720 19.88590 5.51610   1.000 43.29896  ? 38  LEU A O   1 
ATOM   315 C CB  . LEU A 1 42  ? 8.90953  18.63943 3.42962   1.000 40.82199  ? 38  LEU A CB  1 
ATOM   316 C CG  . LEU A 1 42  ? 8.36862  20.00336 2.99727   1.000 40.37884  ? 38  LEU A CG  1 
ATOM   317 C CD1 . LEU A 1 42  ? 8.90571  20.37632 1.62828   1.000 45.25460  ? 38  LEU A CD1 1 
ATOM   318 C CD2 . LEU A 1 42  ? 6.84883  20.00074 3.00082   1.000 53.47892  ? 38  LEU A CD2 1 
ATOM   319 N N   . ASN A 1 43  ? 12.21421 20.01156 4.22807   1.000 49.34087  ? 39  ASN A N   1 
ATOM   320 C CA  . ASN A 1 43  ? 12.88180 21.03971 5.02741   1.000 45.78405  ? 39  ASN A CA  1 
ATOM   321 C C   . ASN A 1 43  ? 12.98895 20.62461 6.49480   1.000 44.71101  ? 39  ASN A C   1 
ATOM   322 O O   . ASN A 1 43  ? 12.60632 21.36321 7.40351   1.000 54.53587  ? 39  ASN A O   1 
ATOM   323 C CB  . ASN A 1 43  ? 12.16986 22.38833 4.88989   1.000 44.87054  ? 39  ASN A CB  1 
ATOM   324 C CG  . ASN A 1 43  ? 13.13442 23.55705 4.86986   1.000 55.98328  ? 39  ASN A CG  1 
ATOM   325 O OD1 . ASN A 1 43  ? 14.23847 23.45683 4.33385   1.000 49.68499  ? 39  ASN A OD1 1 
ATOM   326 N ND2 . ASN A 1 43  ? 12.72165 24.67491 5.45669   1.000 46.64585  ? 39  ASN A ND2 1 
ATOM   327 N N   . GLY A 1 44  ? 13.50916 19.42006 6.72217   1.000 43.04799  ? 40  GLY A N   1 
ATOM   328 C CA  . GLY A 1 44  ? 13.75467 18.92500 8.05959   1.000 43.99179  ? 40  GLY A CA  1 
ATOM   329 C C   . GLY A 1 44  ? 12.65160 18.06970 8.64774   1.000 41.38976  ? 40  GLY A C   1 
ATOM   330 O O   . GLY A 1 44  ? 12.88069 17.42305 9.67722   1.000 49.97590  ? 40  GLY A O   1 
ATOM   331 N N   . VAL A 1 45  ? 11.47368 18.04417 8.03597   1.000 48.71532  ? 41  VAL A N   1 
ATOM   332 C CA  . VAL A 1 45  ? 10.33917 17.27467 8.53385   1.000 50.79579  ? 41  VAL A CA  1 
ATOM   333 C C   . VAL A 1 45  ? 10.15882 16.06301 7.61198   1.000 44.59294  ? 41  VAL A C   1 
ATOM   334 O O   . VAL A 1 45  ? 9.69581  16.21889 6.47474   1.000 42.75926  ? 41  VAL A O   1 
ATOM   335 C CB  . VAL A 1 45  ? 9.06175  18.11881 8.59810   1.000 49.16375  ? 41  VAL A CB  1 
ATOM   336 C CG1 . VAL A 1 45  ? 7.87785  17.25956 9.01775   1.000 45.23813  ? 41  VAL A CG1 1 
ATOM   337 C CG2 . VAL A 1 45  ? 9.24831  19.28311 9.55765   1.000 52.73411  ? 41  VAL A CG2 1 
ATOM   338 N N   . PRO A 1 46  ? 10.50799 14.85882 8.05718   1.000 47.25917  ? 42  PRO A N   1 
ATOM   339 C CA  . PRO A 1 46  ? 10.34915 13.68259 7.19272   1.000 44.33787  ? 42  PRO A CA  1 
ATOM   340 C C   . PRO A 1 46  ? 8.90431  13.21274 7.13109   1.000 48.68364  ? 42  PRO A C   1 
ATOM   341 O O   . PRO A 1 46  ? 8.18012  13.21607 8.12987   1.000 57.80212  ? 42  PRO A O   1 
ATOM   342 C CB  . PRO A 1 46  ? 11.24391 12.63377 7.86471   1.000 54.38329  ? 42  PRO A CB  1 
ATOM   343 C CG  . PRO A 1 46  ? 11.23546 13.02049 9.30348   1.000 42.75091  ? 42  PRO A CG  1 
ATOM   344 C CD  . PRO A 1 46  ? 11.16319 14.52575 9.33318   1.000 45.03160  ? 42  PRO A CD  1 
ATOM   345 N N   . TYR A 1 47  ? 8.48972  12.80610 5.93327   1.000 45.49556  ? 43  TYR A N   1 
ATOM   346 C CA  . TYR A 1 47  ? 7.16599  12.24019 5.69283   1.000 43.17059  ? 43  TYR A CA  1 
ATOM   347 C C   . TYR A 1 47  ? 7.35592  10.85465 5.09034   1.000 49.78972  ? 43  TYR A C   1 
ATOM   348 O O   . TYR A 1 47  ? 7.78020  10.72730 3.93658   1.000 53.71077  ? 43  TYR A O   1 
ATOM   349 C CB  . TYR A 1 47  ? 6.34223  13.13941 4.77272   1.000 39.01438  ? 43  TYR A CB  1 
ATOM   350 C CG  . TYR A 1 47  ? 5.92102  14.44467 5.41052   1.000 40.11957  ? 43  TYR A CG  1 
ATOM   351 C CD1 . TYR A 1 47  ? 4.95209  14.47395 6.40529   1.000 55.90472  ? 43  TYR A CD1 1 
ATOM   352 C CD2 . TYR A 1 47  ? 6.49935  15.64675 5.02410   1.000 51.54708  ? 43  TYR A CD2 1 
ATOM   353 C CE1 . TYR A 1 47  ? 4.56522  15.66514 6.99146   1.000 60.54570  ? 43  TYR A CE1 1 
ATOM   354 C CE2 . TYR A 1 47  ? 6.11913  16.84278 5.60465   1.000 57.47626  ? 43  TYR A CE2 1 
ATOM   355 C CZ  . TYR A 1 47  ? 5.15216  16.84580 6.58769   1.000 55.99071  ? 43  TYR A CZ  1 
ATOM   356 O OH  . TYR A 1 47  ? 4.77183  18.03431 7.16780   1.000 72.16412  ? 43  TYR A OH  1 
ATOM   357 N N   . LYS A 1 48  ? 7.04528  9.82233  5.86857   1.000 52.31813  ? 44  LYS A N   1 
ATOM   358 C CA  . LYS A 1 48  ? 7.28495  8.44018  5.47632   1.000 46.43991  ? 44  LYS A CA  1 
ATOM   359 C C   . LYS A 1 48  ? 5.98242  7.79018  5.02902   1.000 52.88214  ? 44  LYS A C   1 
ATOM   360 O O   . LYS A 1 48  ? 4.94866  7.93977  5.68879   1.000 51.88323  ? 44  LYS A O   1 
ATOM   361 C CB  . LYS A 1 48  ? 7.90003  7.65074  6.63319   1.000 48.00084  ? 44  LYS A CB  1 
ATOM   362 C CG  . LYS A 1 48  ? 8.07902  6.16891  6.35363   1.000 56.05985  ? 44  LYS A CG  1 
ATOM   363 C CD  . LYS A 1 48  ? 9.49505  5.71747  6.66861   1.000 60.39774  ? 44  LYS A CD  1 
ATOM   364 C CE  . LYS A 1 48  ? 9.53902  4.23390  6.99189   1.000 60.40289  ? 44  LYS A CE  1 
ATOM   365 N NZ  . LYS A 1 48  ? 8.51367  3.47205  6.22741   1.000 69.49195  ? 44  LYS A NZ  1 
ATOM   366 N N   . GLY A 1 49  ? 6.03777  7.07289  3.91934   1.000 60.91792  ? 45  GLY A N   1 
ATOM   367 C CA  . GLY A 1 49  ? 4.87830  6.37091  3.41027   1.000 53.55959  ? 45  GLY A CA  1 
ATOM   368 C C   . GLY A 1 49  ? 4.27072  7.06403  2.20600   1.000 43.88385  ? 45  GLY A C   1 
ATOM   369 O O   . GLY A 1 49  ? 4.30232  8.29297  2.07484   1.000 43.19774  ? 45  GLY A O   1 
ATOM   370 N N   . LYS A 1 50  ? 3.70244  6.25839  1.30500   1.000 56.55551  ? 46  LYS A N   1 
ATOM   371 C CA  . LYS A 1 50  ? 3.07764  6.80762  0.10575   1.000 50.05329  ? 46  LYS A CA  1 
ATOM   372 C C   . LYS A 1 50  ? 1.90612  7.71476  0.45777   1.000 54.15538  ? 46  LYS A C   1 
ATOM   373 O O   . LYS A 1 50  ? 1.71698  8.76585  -0.16476  1.000 51.68852  ? 46  LYS A O   1 
ATOM   374 C CB  . LYS A 1 50  ? 2.61830  5.67389  -0.81052  1.000 61.34361  ? 46  LYS A CB  1 
ATOM   375 C CG  . LYS A 1 50  ? 2.77696  5.96260  -2.29328  1.000 64.22408  ? 46  LYS A CG  1 
ATOM   376 C CD  . LYS A 1 50  ? 3.32828  4.75304  -3.03029  1.000 74.96966  ? 46  LYS A CD  1 
ATOM   377 C CE  . LYS A 1 50  ? 3.29237  4.95786  -4.53503  1.000 74.10928  ? 46  LYS A CE  1 
ATOM   378 N NZ  . LYS A 1 50  ? 4.51914  4.43522  -5.19915  1.000 65.58545  ? 46  LYS A NZ  1 
ATOM   379 N N   . GLU A 1 51  ? 1.11039  7.32713  1.45740   1.000 52.34152  ? 47  GLU A N   1 
ATOM   380 C CA  . GLU A 1 51  ? -0.04349 8.13346  1.84049   1.000 55.79986  ? 47  GLU A CA  1 
ATOM   381 C C   . GLU A 1 51  ? 0.37460  9.46394  2.45371   1.000 50.94642  ? 47  GLU A C   1 
ATOM   382 O O   . GLU A 1 51  ? -0.34273 10.46102 2.31313   1.000 51.12697  ? 47  GLU A O   1 
ATOM   383 C CB  . GLU A 1 51  ? -0.92682 7.35149  2.81245   1.000 61.30636  ? 47  GLU A CB  1 
ATOM   384 C CG  . GLU A 1 51  ? -1.07991 5.88104  2.45631   1.000 68.67004  ? 47  GLU A CG  1 
ATOM   385 C CD  . GLU A 1 51  ? -2.19738 5.20573  3.22639   1.000 94.10622  ? 47  GLU A CD  1 
ATOM   386 O OE1 . GLU A 1 51  ? -2.06747 5.06170  4.46037   1.000 110.16098 ? 47  GLU A OE1 1 
ATOM   387 O OE2 . GLU A 1 51  ? -3.20458 4.81688  2.59780   1.000 96.58213  ? 47  GLU A OE2 1 
ATOM   388 N N   . ALA A 1 52  ? 1.52428  9.50243  3.13022   1.000 56.34561  ? 48  ALA A N   1 
ATOM   389 C CA  . ALA A 1 52  ? 1.99618  10.74567 3.73048   1.000 54.66144  ? 48  ALA A CA  1 
ATOM   390 C C   . ALA A 1 52  ? 2.67209  11.63921 2.69646   1.000 46.72267  ? 48  ALA A C   1 
ATOM   391 O O   . ALA A 1 52  ? 2.41196  12.84661 2.64592   1.000 47.96806  ? 48  ALA A O   1 
ATOM   392 C CB  . ALA A 1 52  ? 2.94951  10.44255 4.88742   1.000 47.73904  ? 48  ALA A CB  1 
ATOM   393 N N   . ILE A 1 53  ? 3.54699  11.06046 1.86797   1.000 52.35462  ? 49  ILE A N   1 
ATOM   394 C CA  . ILE A 1 53  ? 4.17891  11.81955 0.78980   1.000 45.92853  ? 49  ILE A CA  1 
ATOM   395 C C   . ILE A 1 53  ? 3.12062  12.42067 -0.12293  1.000 41.15139  ? 49  ILE A C   1 
ATOM   396 O O   . ILE A 1 53  ? 3.25412  13.55482 -0.60064  1.000 54.56689  ? 49  ILE A O   1 
ATOM   397 C CB  . ILE A 1 53  ? 5.15365  10.91858 0.00704   1.000 53.13222  ? 49  ILE A CB  1 
ATOM   398 C CG1 . ILE A 1 53  ? 6.33087  10.49884 0.88844   1.000 50.87092  ? 49  ILE A CG1 1 
ATOM   399 C CG2 . ILE A 1 53  ? 5.65633  11.62278 -1.24328  1.000 51.92677  ? 49  ILE A CG2 1 
ATOM   400 C CD1 . ILE A 1 53  ? 7.15878  9.37868  0.29540   1.000 55.83386  ? 49  ILE A CD1 1 
ATOM   401 N N   . LYS A 1 54  ? 2.04902  11.66990 -0.37347  1.000 53.17709  ? 50  LYS A N   1 
ATOM   402 C CA  . LYS A 1 54  ? 0.94030  12.15959 -1.18222  1.000 56.11920  ? 50  LYS A CA  1 
ATOM   403 C C   . LYS A 1 54  ? 0.36339  13.45152 -0.61333  1.000 58.74360  ? 50  LYS A C   1 
ATOM   404 O O   . LYS A 1 54  ? 0.39253  14.49939 -1.26791  1.000 66.22972  ? 50  LYS A O   1 
ATOM   405 C CB  . LYS A 1 54  ? -0.12174 11.06817 -1.26873  1.000 57.84036  ? 50  LYS A CB  1 
ATOM   406 C CG  . LYS A 1 54  ? -1.42238 11.43686 -1.93858  1.000 67.36277  ? 50  LYS A CG  1 
ATOM   407 C CD  . LYS A 1 54  ? -2.47964 10.49227 -1.40516  1.000 63.32206  ? 50  LYS A CD  1 
ATOM   408 C CE  . LYS A 1 54  ? -1.96997 9.05588  -1.56160  1.000 74.00214  ? 50  LYS A CE  1 
ATOM   409 N NZ  . LYS A 1 54  ? -2.49968 8.11298  -0.53788  1.000 76.54352  ? 50  LYS A NZ  1 
ATOM   410 N N   . LYS A 1 55  ? -0.14922 13.39466 0.62290   1.000 56.96511  ? 51  LYS A N   1 
ATOM   411 C CA  . LYS A 1 55  ? -0.77907 14.56178 1.24130   1.000 59.94674  ? 51  LYS A CA  1 
ATOM   412 C C   . LYS A 1 55  ? 0.08474  15.81321 1.13230   1.000 50.28534  ? 51  LYS A C   1 
ATOM   413 O O   . LYS A 1 55  ? -0.44165 16.92783 1.03232   1.000 54.73874  ? 51  LYS A O   1 
ATOM   414 C CB  . LYS A 1 55  ? -1.08784 14.27179 2.71059   1.000 35.36813  ? 51  LYS A CB  1 
ATOM   415 C CG  . LYS A 1 55  ? -2.22081 13.28405 2.92670   1.000 44.46385  ? 51  LYS A CG  1 
ATOM   416 C CD  . LYS A 1 55  ? -2.20010 12.73754 4.34598   1.000 55.11318  ? 51  LYS A CD  1 
ATOM   417 C CE  . LYS A 1 55  ? -2.96349 11.42780 4.45208   1.000 59.62451  ? 51  LYS A CE  1 
ATOM   418 N NZ  . LYS A 1 55  ? -3.48047 11.20552 5.83214   1.000 64.19514  ? 51  LYS A NZ  1 
ATOM   419 N N   . VAL A 1 56  ? 1.40902  15.65065 1.14364   1.000 48.05580  ? 52  VAL A N   1 
ATOM   420 C CA  . VAL A 1 56  ? 2.29961  16.79101 0.96042   1.000 51.32569  ? 52  VAL A CA  1 
ATOM   421 C C   . VAL A 1 56  ? 2.28905  17.25762 -0.49156  1.000 52.79256  ? 52  VAL A C   1 
ATOM   422 O O   . VAL A 1 56  ? 2.41967  18.45749 -0.76698  1.000 47.83482  ? 52  VAL A O   1 
ATOM   423 C CB  . VAL A 1 56  ? 3.71855  16.42379 1.43567   1.000 50.61289  ? 52  VAL A CB  1 
ATOM   424 C CG1 . VAL A 1 56  ? 4.71760  17.51251 1.07215   1.000 52.73134  ? 52  VAL A CG1 1 
ATOM   425 C CG2 . VAL A 1 56  ? 3.72130  16.16599 2.93381   1.000 50.28049  ? 52  VAL A CG2 1 
ATOM   426 N N   . LEU A 1 57  ? 2.10902  16.33226 -1.43789  1.000 51.16161  ? 53  LEU A N   1 
ATOM   427 C CA  . LEU A 1 57  ? 2.14873  16.68990 -2.85314  1.000 52.17003  ? 53  LEU A CA  1 
ATOM   428 C C   . LEU A 1 57  ? 0.99221  17.61022 -3.22984  1.000 55.19547  ? 53  LEU A C   1 
ATOM   429 O O   . LEU A 1 57  ? 1.20083  18.65384 -3.85742  1.000 53.61820  ? 53  LEU A O   1 
ATOM   430 C CB  . LEU A 1 57  ? 2.13519  15.42576 -3.71259  1.000 58.78363  ? 53  LEU A CB  1 
ATOM   431 C CG  . LEU A 1 57  ? 3.43498  14.62010 -3.77199  1.000 56.77122  ? 53  LEU A CG  1 
ATOM   432 C CD1 . LEU A 1 57  ? 3.17992  13.22851 -4.32648  1.000 63.28393  ? 53  LEU A CD1 1 
ATOM   433 C CD2 . LEU A 1 57  ? 4.47016  15.34528 -4.60799  1.000 47.31648  ? 53  LEU A CD2 1 
ATOM   434 N N   . GLU A 1 58  ? -0.23884 17.24377 -2.86195  1.000 59.29900  ? 54  GLU A N   1 
ATOM   435 C CA  . GLU A 1 58  ? -1.37404 18.10058 -3.18813  1.000 62.45946  ? 54  GLU A CA  1 
ATOM   436 C C   . GLU A 1 58  ? -1.42836 19.34659 -2.31573  1.000 56.36550  ? 54  GLU A C   1 
ATOM   437 O O   . GLU A 1 58  ? -2.14293 20.29500 -2.65723  1.000 65.14239  ? 54  GLU A O   1 
ATOM   438 C CB  . GLU A 1 58  ? -2.69044 17.32899 -3.07035  1.000 71.24151  ? 54  GLU A CB  1 
ATOM   439 C CG  . GLU A 1 58  ? -2.74986 16.06210 -3.91352  1.000 79.42508  ? 54  GLU A CG  1 
ATOM   440 C CD  . GLU A 1 58  ? -2.64442 14.79967 -3.08492  1.000 82.85380  ? 54  GLU A CD  1 
ATOM   441 O OE1 . GLU A 1 58  ? -2.10079 14.86365 -1.96373  1.000 83.76303  ? 54  GLU A OE1 1 
ATOM   442 O OE2 . GLU A 1 58  ? -3.09228 13.73334 -3.55871  1.000 87.62088  ? 54  GLU A OE2 1 
ATOM   443 N N   . SER A 1 59  ? -0.70194 19.36563 -1.20201  1.000 50.80272  ? 55  SER A N   1 
ATOM   444 C CA  . SER A 1 59  ? -0.59183 20.55690 -0.37281  1.000 55.51025  ? 55  SER A CA  1 
ATOM   445 C C   . SER A 1 59  ? 0.59708  21.42705 -0.75439  1.000 52.43222  ? 55  SER A C   1 
ATOM   446 O O   . SER A 1 59  ? 0.80330  22.47606 -0.13471  1.000 47.28513  ? 55  SER A O   1 
ATOM   447 C CB  . SER A 1 59  ? -0.49263 20.16956 1.10627   1.000 61.09009  ? 55  SER A CB  1 
ATOM   448 O OG  . SER A 1 59  ? -1.77608 19.95848 1.66922   1.000 64.99581  ? 55  SER A OG  1 
ATOM   449 N N   . ALA A 1 60  ? 1.38089  21.01644 -1.74712  1.000 61.45249  ? 56  ALA A N   1 
ATOM   450 C CA  . ALA A 1 60  ? 2.49872  21.83105 -2.19424  1.000 52.14567  ? 56  ALA A CA  1 
ATOM   451 C C   . ALA A 1 60  ? 1.98264  23.13208 -2.80489  1.000 48.33570  ? 56  ALA A C   1 
ATOM   452 O O   . ALA A 1 60  ? 0.95651  23.13226 -3.49281  1.000 44.83971  ? 56  ALA A O   1 
ATOM   453 C CB  . ALA A 1 60  ? 3.34673  21.07273 -3.21443  1.000 54.58319  ? 56  ALA A CB  1 
ATOM   454 N N   . PRO A 1 61  ? 2.66217  24.25085 -2.56995  1.000 47.30694  ? 57  PRO A N   1 
ATOM   455 C CA  . PRO A 1 61  ? 2.17007  25.53373 -3.08038  1.000 57.29135  ? 57  PRO A CA  1 
ATOM   456 C C   . PRO A 1 61  ? 2.23581  25.59611 -4.59783  1.000 56.66826  ? 57  PRO A C   1 
ATOM   457 O O   . PRO A 1 61  ? 2.96232  24.84529 -5.25314  1.000 52.71535  ? 57  PRO A O   1 
ATOM   458 C CB  . PRO A 1 61  ? 3.11543  26.56257 -2.44516  1.000 54.95569  ? 57  PRO A CB  1 
ATOM   459 C CG  . PRO A 1 61  ? 3.83630  25.82323 -1.35156  1.000 59.90998  ? 57  PRO A CG  1 
ATOM   460 C CD  . PRO A 1 61  ? 3.90878  24.40437 -1.80529  1.000 55.97409  ? 57  PRO A CD  1 
ATOM   461 N N   . LYS A 1 62  ? 1.44664  26.51245 -5.15432  1.000 54.84876  ? 58  LYS A N   1 
ATOM   462 C CA  . LYS A 1 62  ? 1.48446  26.77989 -6.58723  1.000 52.70052  ? 58  LYS A CA  1 
ATOM   463 C C   . LYS A 1 62  ? 2.84912  27.35541 -6.94171  1.000 55.38464  ? 58  LYS A C   1 
ATOM   464 O O   . LYS A 1 62  ? 3.17182  28.48504 -6.56191  1.000 56.75848  ? 58  LYS A O   1 
ATOM   465 C CB  . LYS A 1 62  ? 0.36274  27.73805 -6.97593  1.000 47.11885  ? 58  LYS A CB  1 
ATOM   466 N N   . ALA A 1 63  ? 3.65857  26.58018 -7.65869  1.000 51.91884  ? 59  ALA A N   1 
ATOM   467 C CA  . ALA A 1 63  ? 5.01178  27.00137 -7.98380  1.000 38.21484  ? 59  ALA A CA  1 
ATOM   468 C C   . ALA A 1 63  ? 5.47571  26.29947 -9.24921  1.000 48.04891  ? 59  ALA A C   1 
ATOM   469 O O   . ALA A 1 63  ? 5.12907  25.13973 -9.48997  1.000 48.58052  ? 59  ALA A O   1 
ATOM   470 C CB  . ALA A 1 63  ? 5.98068  26.70508 -6.83360  1.000 47.63628  ? 59  ALA A CB  1 
ATOM   471 N N   . LYS A 1 64  ? 6.25739  27.01475 -10.05170 1.000 43.41231  ? 60  LYS A N   1 
ATOM   472 C CA  . LYS A 1 64  ? 6.90443  26.46156 -11.23095 1.000 45.24226  ? 60  LYS A CA  1 
ATOM   473 C C   . LYS A 1 64  ? 8.38487  26.26327 -10.93771 1.000 43.05760  ? 60  LYS A C   1 
ATOM   474 O O   . LYS A 1 64  ? 9.02486  27.12040 -10.32007 1.000 44.40468  ? 60  LYS A O   1 
ATOM   475 C CB  . LYS A 1 64  ? 6.72258  27.37602 -12.44602 1.000 59.90522  ? 60  LYS A CB  1 
ATOM   476 C CG  . LYS A 1 64  ? 5.67196  26.89304 -13.43357 1.000 58.45177  ? 60  LYS A CG  1 
ATOM   477 C CD  . LYS A 1 64  ? 4.28791  26.87842 -12.80427 1.000 53.96341  ? 60  LYS A CD  1 
ATOM   478 C CE  . LYS A 1 64  ? 3.27360  26.19416 -13.70644 1.000 60.29733  ? 60  LYS A CE  1 
ATOM   479 N NZ  . LYS A 1 64  ? 3.70909  24.82565 -14.09791 1.000 70.28330  ? 60  LYS A NZ  1 
ATOM   480 N N   . TYR A 1 65  ? 8.92451  25.13038 -11.37641 1.000 39.17439  ? 61  TYR A N   1 
ATOM   481 C CA  . TYR A 1 65  ? 10.29224 24.74386 -11.06528 1.000 47.23088  ? 61  TYR A CA  1 
ATOM   482 C C   . TYR A 1 65  ? 11.10341 24.60213 -12.34427 1.000 47.87588  ? 61  TYR A C   1 
ATOM   483 O O   . TYR A 1 65  ? 10.61177 24.08013 -13.34976 1.000 41.76454  ? 61  TYR A O   1 
ATOM   484 C CB  . TYR A 1 65  ? 10.32279 23.43133 -10.27620 1.000 49.12819  ? 61  TYR A CB  1 
ATOM   485 C CG  . TYR A 1 65  ? 9.45224  23.45031 -9.04105  1.000 37.53824  ? 61  TYR A CG  1 
ATOM   486 C CD1 . TYR A 1 65  ? 9.93468  23.94378 -7.83742  1.000 36.76187  ? 61  TYR A CD1 1 
ATOM   487 C CD2 . TYR A 1 65  ? 8.14692  22.97700 -9.07931  1.000 40.58944  ? 61  TYR A CD2 1 
ATOM   488 C CE1 . TYR A 1 65  ? 9.14246  23.96595 -6.70598  1.000 42.26227  ? 61  TYR A CE1 1 
ATOM   489 C CE2 . TYR A 1 65  ? 7.34664  22.99502 -7.95254  1.000 45.21762  ? 61  TYR A CE2 1 
ATOM   490 C CZ  . TYR A 1 65  ? 7.84988  23.49076 -6.76870  1.000 47.51750  ? 61  TYR A CZ  1 
ATOM   491 O OH  . TYR A 1 65  ? 7.05899  23.51016 -5.64294  1.000 47.07151  ? 61  TYR A OH  1 
ATOM   492 N N   . LYS A 1 66  ? 12.34874 25.07097 -12.29762 1.000 47.67616  ? 62  LYS A N   1 
ATOM   493 C CA  . LYS A 1 66  ? 13.28220 24.94772 -13.41020 1.000 44.07765  ? 62  LYS A CA  1 
ATOM   494 C C   . LYS A 1 66  ? 14.59856 24.40335 -12.88039 1.000 49.48801  ? 62  LYS A C   1 
ATOM   495 O O   . LYS A 1 66  ? 15.21227 25.00952 -11.99570 1.000 48.25333  ? 62  LYS A O   1 
ATOM   496 C CB  . LYS A 1 66  ? 13.50147 26.29188 -14.11026 1.000 48.66652  ? 62  LYS A CB  1 
ATOM   497 C CG  . LYS A 1 66  ? 14.52103 26.23444 -15.23866 1.000 54.89856  ? 62  LYS A CG  1 
ATOM   498 C CD  . LYS A 1 66  ? 14.60414 27.55267 -15.99272 1.000 52.44462  ? 62  LYS A CD  1 
ATOM   499 C CE  . LYS A 1 66  ? 14.73860 28.73111 -15.04248 1.000 70.12017  ? 62  LYS A CE  1 
ATOM   500 N NZ  . LYS A 1 66  ? 13.85015 29.86110 -15.43041 1.000 69.58624  ? 62  LYS A NZ  1 
ATOM   501 N N   . ILE A 1 67  ? 15.02667 23.26048 -13.41716 1.000 45.66303  ? 63  ILE A N   1 
ATOM   502 C CA  . ILE A 1 67  ? 16.30201 22.67756 -13.02367 1.000 48.63160  ? 63  ILE A CA  1 
ATOM   503 C C   . ILE A 1 67  ? 17.44003 23.53583 -13.55792 1.000 43.86443  ? 63  ILE A C   1 
ATOM   504 O O   . ILE A 1 67  ? 17.41687 23.98481 -14.71204 1.000 53.35587  ? 63  ILE A O   1 
ATOM   505 C CB  . ILE A 1 67  ? 16.41072 21.23115 -13.53513 1.000 48.95069  ? 63  ILE A CB  1 
ATOM   506 C CG1 . ILE A 1 67  ? 15.39598 20.33415 -12.82735 1.000 33.82174  ? 63  ILE A CG1 1 
ATOM   507 C CG2 . ILE A 1 67  ? 17.81977 20.69436 -13.34383 1.000 39.52980  ? 63  ILE A CG2 1 
ATOM   508 C CD1 . ILE A 1 67  ? 15.06164 19.08534 -13.60185 1.000 48.14255  ? 63  ILE A CD1 1 
ATOM   509 N N   . THR A 1 68  ? 18.44426 23.77778 -12.71236 1.000 49.55585  ? 64  THR A N   1 
ATOM   510 C CA  . THR A 1 68  ? 19.61693 24.54341 -13.10629 1.000 55.20275  ? 64  THR A CA  1 
ATOM   511 C C   . THR A 1 68  ? 20.93213 23.79852 -12.93895 1.000 45.83162  ? 64  THR A C   1 
ATOM   512 O O   . THR A 1 68  ? 21.93363 24.22254 -13.52599 1.000 40.59469  ? 64  THR A O   1 
ATOM   513 C CB  . THR A 1 68  ? 19.69288 25.85992 -12.31628 1.000 57.70597  ? 64  THR A CB  1 
ATOM   514 O OG1 . THR A 1 68  ? 19.83019 25.57842 -10.91750 1.000 57.59068  ? 64  THR A OG1 1 
ATOM   515 C CG2 . THR A 1 68  ? 18.44086 26.69033 -12.55078 1.000 61.93615  ? 64  THR A CG2 1 
ATOM   516 N N   . LYS A 1 69  ? 20.96318 22.71229 -12.16960 1.000 43.76560  ? 65  LYS A N   1 
ATOM   517 C CA  . LYS A 1 69  ? 22.17583 21.92264 -12.01262 1.000 45.60157  ? 65  LYS A CA  1 
ATOM   518 C C   . LYS A 1 69  ? 21.80010 20.53946 -11.50413 1.000 47.36565  ? 65  LYS A C   1 
ATOM   519 O O   . LYS A 1 69  ? 20.95458 20.40765 -10.61557 1.000 45.14331  ? 65  LYS A O   1 
ATOM   520 C CB  . LYS A 1 69  ? 23.16635 22.59249 -11.05287 1.000 56.78804  ? 65  LYS A CB  1 
ATOM   521 C CG  . LYS A 1 69  ? 24.58574 22.05822 -11.16267 1.000 55.29311  ? 65  LYS A CG  1 
ATOM   522 C CD  . LYS A 1 69  ? 25.46570 22.57963 -10.03883 1.000 69.62032  ? 65  LYS A CD  1 
ATOM   523 C CE  . LYS A 1 69  ? 26.30415 23.76145 -10.49754 1.000 62.91027  ? 65  LYS A CE  1 
ATOM   524 N NZ  . LYS A 1 69  ? 25.48629 24.99427 -10.66595 1.000 63.36578  ? 65  LYS A NZ  1 
ATOM   525 N N   . ILE A 1 70  ? 22.43390 19.51707 -12.07359 1.000 47.53979  ? 66  ILE A N   1 
ATOM   526 C CA  . ILE A 1 70  ? 22.19131 18.12776 -11.70622 1.000 43.91875  ? 66  ILE A CA  1 
ATOM   527 C C   . ILE A 1 70  ? 23.53059 17.46083 -11.43338 1.000 53.21843  ? 66  ILE A C   1 
ATOM   528 O O   . ILE A 1 70  ? 24.43037 17.49512 -12.28042 1.000 47.63125  ? 66  ILE A O   1 
ATOM   529 C CB  . ILE A 1 70  ? 21.42595 17.36616 -12.80543 1.000 43.18188  ? 66  ILE A CB  1 
ATOM   530 C CG1 . ILE A 1 70  ? 19.97440 17.83858 -12.87179 1.000 40.74322  ? 66  ILE A CG1 1 
ATOM   531 C CG2 . ILE A 1 70  ? 21.48378 15.86586 -12.55833 1.000 42.93392  ? 66  ILE A CG2 1 
ATOM   532 C CD1 . ILE A 1 70  ? 19.19705 17.24691 -14.02379 1.000 47.37828  ? 66  ILE A CD1 1 
ATOM   533 N N   . ASP A 1 71  ? 23.66261 16.86105 -10.25292 1.000 41.85035  ? 67  ASP A N   1 
ATOM   534 C CA  . ASP A 1 71  ? 24.84773 16.10192 -9.88000  1.000 50.31148  ? 67  ASP A CA  1 
ATOM   535 C C   . ASP A 1 71  ? 24.41461 14.70730 -9.46056  1.000 47.78011  ? 67  ASP A C   1 
ATOM   536 O O   . ASP A 1 71  ? 23.53624 14.55950 -8.60496  1.000 48.25648  ? 67  ASP A O   1 
ATOM   537 C CB  . ASP A 1 71  ? 25.61861 16.78429 -8.74440  1.000 58.19379  ? 67  ASP A CB  1 
ATOM   538 C CG  . ASP A 1 71  ? 25.73552 18.28358 -8.93730  1.000 71.76189  ? 67  ASP A CG  1 
ATOM   539 O OD1 . ASP A 1 71  ? 24.81496 19.01299 -8.51212  1.000 74.03891  ? 67  ASP A OD1 1 
ATOM   540 O OD2 . ASP A 1 71  ? 26.74789 18.73222 -9.51480  1.000 83.61769  ? 67  ASP A OD2 1 
ATOM   541 N N   . ILE A 1 72  ? 25.02410 13.69125 -10.06346 1.000 48.09347  ? 68  ILE A N   1 
ATOM   542 C CA  . ILE A 1 72  ? 24.69175 12.29769 -9.79353  1.000 43.64782  ? 68  ILE A CA  1 
ATOM   543 C C   . ILE A 1 72  ? 25.88094 11.64958 -9.10072  1.000 58.92382  ? 68  ILE A C   1 
ATOM   544 O O   . ILE A 1 72  ? 26.98363 11.59637 -9.65981  1.000 65.43915  ? 68  ILE A O   1 
ATOM   545 C CB  . ILE A 1 72  ? 24.32232 11.54121 -11.07801 1.000 49.36304  ? 68  ILE A CB  1 
ATOM   546 C CG1 . ILE A 1 72  ? 23.02590 12.09831 -11.66960 1.000 54.26192  ? 68  ILE A CG1 1 
ATOM   547 C CG2 . ILE A 1 72  ? 24.18535 10.05399 -10.79597 1.000 42.46412  ? 68  ILE A CG2 1 
ATOM   548 C CD1 . ILE A 1 72  ? 22.71615 11.58266 -13.05808 1.000 47.75956  ? 68  ILE A CD1 1 
ATOM   549 N N   . LYS A 1 73  ? 25.65755 11.16172 -7.88441  1.000 57.95791  ? 69  LYS A N   1 
ATOM   550 C CA  . LYS A 1 73  ? 26.66065 10.43022 -7.12905  1.000 53.88276  ? 69  LYS A CA  1 
ATOM   551 C C   . LYS A 1 73  ? 26.19880 8.99442  -6.92968  1.000 60.79651  ? 69  LYS A C   1 
ATOM   552 O O   . LYS A 1 73  ? 24.99779 8.71032  -6.89233  1.000 57.46600  ? 69  LYS A O   1 
ATOM   553 C CB  . LYS A 1 73  ? 26.92624 11.08154 -5.76574  1.000 61.94411  ? 69  LYS A CB  1 
ATOM   554 C CG  . LYS A 1 73  ? 27.96371 12.19006 -5.79328  1.000 70.01745  ? 69  LYS A CG  1 
ATOM   555 C CD  . LYS A 1 73  ? 27.94959 12.98404 -4.49753  1.000 59.36291  ? 69  LYS A CD  1 
ATOM   556 C CE  . LYS A 1 73  ? 27.52726 14.42360 -4.73518  1.000 60.30063  ? 69  LYS A CE  1 
ATOM   557 N NZ  . LYS A 1 73  ? 28.68501 15.28388 -5.09944  1.000 56.08586  ? 69  LYS A NZ  1 
ATOM   558 N N   . ILE A 1 74  ? 27.16428 8.08992  -6.80398  1.000 63.31174  ? 70  ILE A N   1 
ATOM   559 C CA  . ILE A 1 74  ? 26.89825 6.67853  -6.55832  1.000 64.76051  ? 70  ILE A CA  1 
ATOM   560 C C   . ILE A 1 74  ? 27.50864 6.31797  -5.21268  1.000 71.65746  ? 70  ILE A C   1 
ATOM   561 O O   . ILE A 1 74  ? 28.71512 6.49463  -5.00538  1.000 77.05379  ? 70  ILE A O   1 
ATOM   562 C CB  . ILE A 1 74  ? 27.45998 5.78641  -7.67583  1.000 70.59914  ? 70  ILE A CB  1 
ATOM   563 C CG1 . ILE A 1 74  ? 26.64136 5.96413  -8.95546  1.000 73.25611  ? 70  ILE A CG1 1 
ATOM   564 C CG2 . ILE A 1 74  ? 27.46414 4.32806  -7.24081  1.000 70.70105  ? 70  ILE A CG2 1 
ATOM   565 C CD1 . ILE A 1 74  ? 26.97515 4.96807  -10.04016 1.000 76.70837  ? 70  ILE A CD1 1 
ATOM   566 N N   . VAL A 1 75  ? 26.67557 5.83776  -4.29384  1.000 59.49781  ? 71  VAL A N   1 
ATOM   567 C CA  . VAL A 1 75  ? 27.11956 5.35717  -2.99054  1.000 69.50867  ? 71  VAL A CA  1 
ATOM   568 C C   . VAL A 1 75  ? 26.56742 3.94920  -2.82518  1.000 74.48793  ? 71  VAL A C   1 
ATOM   569 O O   . VAL A 1 75  ? 25.36792 3.77340  -2.57529  1.000 72.79937  ? 71  VAL A O   1 
ATOM   570 C CB  . VAL A 1 75  ? 26.66449 6.26482  -1.83893  1.000 73.93259  ? 71  VAL A CB  1 
ATOM   571 C CG1 . VAL A 1 75  ? 27.51627 6.01425  -0.60546  1.000 74.20082  ? 71  VAL A CG1 1 
ATOM   572 C CG2 . VAL A 1 75  ? 26.74581 7.72631  -2.24647  1.000 67.48929  ? 71  VAL A CG2 1 
ATOM   573 N N   . GLY A 1 76  ? 27.43280 2.95099  -2.96645  1.000 80.44627  ? 72  GLY A N   1 
ATOM   574 C CA  . GLY A 1 76  ? 26.97337 1.57391  -2.88408  1.000 78.70571  ? 72  GLY A CA  1 
ATOM   575 C C   . GLY A 1 76  ? 26.12805 1.22372  -4.09262  1.000 80.42332  ? 72  GLY A C   1 
ATOM   576 O O   . GLY A 1 76  ? 26.53896 1.41481  -5.24279  1.000 76.35941  ? 72  GLY A O   1 
ATOM   577 N N   . ASN A 1 77  ? 24.92710 0.70563  -3.83609  1.000 80.91619  ? 73  ASN A N   1 
ATOM   578 C CA  . ASN A 1 77  ? 23.98316 0.34667  -4.88443  1.000 78.39381  ? 73  ASN A CA  1 
ATOM   579 C C   . ASN A 1 77  ? 22.88247 1.39086  -5.05005  1.000 78.54643  ? 73  ASN A C   1 
ATOM   580 O O   . ASN A 1 77  ? 21.85779 1.11345  -5.68246  1.000 92.03720  ? 73  ASN A O   1 
ATOM   581 C CB  . ASN A 1 77  ? 23.38154 -1.02996 -4.59220  1.000 79.96821  ? 73  ASN A CB  1 
ATOM   582 C CG  . ASN A 1 77  ? 22.69956 -1.64263 -5.80320  1.000 102.45863 ? 73  ASN A CG  1 
ATOM   583 O OD1 . ASN A 1 77  ? 23.09959 -1.40492 -6.94299  1.000 112.38480 ? 73  ASN A OD1 1 
ATOM   584 N ND2 . ASN A 1 77  ? 21.65880 -2.43060 -5.55985  1.000 105.15829 ? 73  ASN A ND2 1 
ATOM   585 N N   . GLU A 1 78  ? 23.07750 2.58851  -4.50471  1.000 74.27778  ? 74  GLU A N   1 
ATOM   586 C CA  . GLU A 1 78  ? 22.06543 3.63355  -4.52189  1.000 70.15570  ? 74  GLU A CA  1 
ATOM   587 C C   . GLU A 1 78  ? 22.54669 4.81780  -5.34758  1.000 59.53647  ? 74  GLU A C   1 
ATOM   588 O O   . GLU A 1 78  ? 23.71819 5.20330  -5.27683  1.000 54.09450  ? 74  GLU A O   1 
ATOM   589 C CB  . GLU A 1 78  ? 21.72100 4.08541  -3.09924  1.000 65.97617  ? 74  GLU A CB  1 
ATOM   590 C CG  . GLU A 1 78  ? 21.35379 2.93660  -2.17241  1.000 82.33605  ? 74  GLU A CG  1 
ATOM   591 C CD  . GLU A 1 78  ? 20.02378 3.14516  -1.47656  1.000 87.51687  ? 74  GLU A CD  1 
ATOM   592 O OE1 . GLU A 1 78  ? 19.81472 4.23545  -0.90498  1.000 81.23241  ? 74  GLU A OE1 1 
ATOM   593 O OE2 . GLU A 1 78  ? 19.18642 2.21819  -1.50063  1.000 88.08014  ? 74  GLU A OE2 1 
ATOM   594 N N   . ILE A 1 79  ? 21.63462 5.38844  -6.12825  1.000 58.17923  ? 75  ILE A N   1 
ATOM   595 C CA  . ILE A 1 79  ? 21.92054 6.53868  -6.97753  1.000 54.71151  ? 75  ILE A CA  1 
ATOM   596 C C   . ILE A 1 79  ? 21.50874 7.79242  -6.21718  1.000 47.60530  ? 75  ILE A C   1 
ATOM   597 O O   . ILE A 1 79  ? 20.32258 8.00358  -5.94380  1.000 50.43470  ? 75  ILE A O   1 
ATOM   598 C CB  . ILE A 1 79  ? 21.19151 6.44412  -8.32431  1.000 51.05460  ? 75  ILE A CB  1 
ATOM   599 C CG1 . ILE A 1 79  ? 21.68630 5.23700  -9.12322  1.000 62.73438  ? 75  ILE A CG1 1 
ATOM   600 C CG2 . ILE A 1 79  ? 21.37871 7.72738  -9.12024  1.000 48.23039  ? 75  ILE A CG2 1 
ATOM   601 C CD1 . ILE A 1 79  ? 23.11870 5.35920  -9.59188  1.000 56.45284  ? 75  ILE A CD1 1 
ATOM   602 N N   . ILE A 1 80  ? 22.48356 8.62840  -5.87465  1.000 39.48606  ? 76  ILE A N   1 
ATOM   603 C CA  . ILE A 1 80  ? 22.23445 9.90109  -5.20796  1.000 45.92700  ? 76  ILE A CA  1 
ATOM   604 C C   . ILE A 1 80  ? 22.26257 10.99802 -6.26130  1.000 52.86619  ? 76  ILE A C   1 
ATOM   605 O O   . ILE A 1 80  ? 23.26536 11.16811 -6.96549  1.000 60.12796  ? 76  ILE A O   1 
ATOM   606 C CB  . ILE A 1 80  ? 23.26698 10.17271 -4.10341  1.000 46.28633  ? 76  ILE A CB  1 
ATOM   607 C CG1 . ILE A 1 80  ? 23.51117 8.90980  -3.27729  1.000 46.77727  ? 76  ILE A CG1 1 
ATOM   608 C CG2 . ILE A 1 80  ? 22.80537 11.31947 -3.21573  1.000 41.03171  ? 76  ILE A CG2 1 
ATOM   609 C CD1 . ILE A 1 80  ? 22.33102 8.49544  -2.43428  1.000 53.95144  ? 76  ILE A CD1 1 
ATOM   610 N N   . VAL A 1 81  ? 21.16603 11.74161 -6.37432  1.000 44.16665  ? 77  VAL A N   1 
ATOM   611 C CA  . VAL A 1 81  ? 21.05041 12.83719 -7.32897  1.000 41.01298  ? 77  VAL A CA  1 
ATOM   612 C C   . VAL A 1 81  ? 20.80075 14.11894 -6.54854  1.000 45.37244  ? 77  VAL A C   1 
ATOM   613 O O   . VAL A 1 81  ? 19.78947 14.23774 -5.84504  1.000 41.80145  ? 77  VAL A O   1 
ATOM   614 C CB  . VAL A 1 81  ? 19.93159 12.59404 -8.35390  1.000 42.90089  ? 77  VAL A CB  1 
ATOM   615 C CG1 . VAL A 1 81  ? 19.93235 13.69497 -9.40013  1.000 43.40062  ? 77  VAL A CG1 1 
ATOM   616 C CG2 . VAL A 1 81  ? 20.09618 11.23241 -9.00955  1.000 37.74412  ? 77  VAL A CG2 1 
ATOM   617 N N   . ASN A 1 82  ? 21.72193 15.07005 -6.66726  1.000 43.03572  ? 78  ASN A N   1 
ATOM   618 C CA  . ASN A 1 82  ? 21.57060 16.39498 -6.08177  1.000 37.46122  ? 78  ASN A CA  1 
ATOM   619 C C   . ASN A 1 82  ? 21.14016 17.35595 -7.18240  1.000 46.11134  ? 78  ASN A C   1 
ATOM   620 O O   . ASN A 1 82  ? 21.86093 17.53549 -8.17024  1.000 45.20739  ? 78  ASN A O   1 
ATOM   621 C CB  . ASN A 1 82  ? 22.87378 16.86000 -5.43283  1.000 50.41420  ? 78  ASN A CB  1 
ATOM   622 C CG  . ASN A 1 82  ? 23.15056 16.16252 -4.11588  1.000 46.44546  ? 78  ASN A CG  1 
ATOM   623 O OD1 . ASN A 1 82  ? 22.51849 16.45489 -3.10125  1.000 45.25635  ? 78  ASN A OD1 1 
ATOM   624 N ND2 . ASN A 1 82  ? 24.10078 15.23481 -4.12530  1.000 42.99293  ? 78  ASN A ND2 1 
ATOM   625 N N   . VAL A 1 83  ? 19.96900 17.96423 -7.01612  1.000 36.68151  ? 79  VAL A N   1 
ATOM   626 C CA  . VAL A 1 83  ? 19.36929 18.80964 -8.04150  1.000 41.46121  ? 79  VAL A CA  1 
ATOM   627 C C   . VAL A 1 83  ? 19.22627 20.21805 -7.48463  1.000 39.76967  ? 79  VAL A C   1 
ATOM   628 O O   . VAL A 1 83  ? 18.59166 20.41914 -6.44157  1.000 43.82192  ? 79  VAL A O   1 
ATOM   629 C CB  . VAL A 1 83  ? 18.00815 18.26832 -8.50470  1.000 39.93000  ? 79  VAL A CB  1 
ATOM   630 C CG1 . VAL A 1 83  ? 17.45600 19.12805 -9.62998  1.000 41.17299  ? 79  VAL A CG1 1 
ATOM   631 C CG2 . VAL A 1 83  ? 18.13297 16.81799 -8.93985  1.000 46.24063  ? 79  VAL A CG2 1 
ATOM   632 N N   . ASP A 1 84  ? 19.81399 21.18736 -8.18019  1.000 39.44879  ? 80  ASP A N   1 
ATOM   633 C CA  . ASP A 1 84  ? 19.63261 22.59713 -7.86143  1.000 40.73485  ? 80  ASP A CA  1 
ATOM   634 C C   . ASP A 1 84  ? 18.44078 23.12106 -8.65290  1.000 46.35029  ? 80  ASP A C   1 
ATOM   635 O O   . ASP A 1 84  ? 18.45348 23.09907 -9.88845  1.000 45.80875  ? 80  ASP A O   1 
ATOM   636 C CB  . ASP A 1 84  ? 20.89405 23.39488 -8.18766  1.000 45.24157  ? 80  ASP A CB  1 
ATOM   637 C CG  . ASP A 1 84  ? 21.96710 23.25094 -7.12617  1.000 76.13458  ? 80  ASP A CG  1 
ATOM   638 O OD1 . ASP A 1 84  ? 23.00952 23.93023 -7.23903  1.000 73.93605  ? 80  ASP A OD1 1 
ATOM   639 O OD2 . ASP A 1 84  ? 21.77007 22.46007 -6.17927  1.000 77.39447  ? 80  ASP A OD2 1 
ATOM   640 N N   . VAL A 1 85  ? 17.41242 23.58216 -7.94572  1.000 42.80336  ? 81  VAL A N   1 
ATOM   641 C CA  . VAL A 1 85  ? 16.15985 24.00213 -8.56029  1.000 39.36343  ? 81  VAL A CA  1 
ATOM   642 C C   . VAL A 1 85  ? 15.89952 25.46239 -8.22284  1.000 47.44876  ? 81  VAL A C   1 
ATOM   643 O O   . VAL A 1 85  ? 16.21929 25.92444 -7.12234  1.000 51.15887  ? 81  VAL A O   1 
ATOM   644 C CB  . VAL A 1 85  ? 14.97705 23.12665 -8.09663  1.000 38.32596  ? 81  VAL A CB  1 
ATOM   645 C CG1 . VAL A 1 85  ? 13.73829 23.42676 -8.92438  1.000 44.76629  ? 81  VAL A CG1 1 
ATOM   646 C CG2 . VAL A 1 85  ? 15.33762 21.65272 -8.16628  1.000 35.58704  ? 81  VAL A CG2 1 
ATOM   647 N N   . LEU A 1 86  ? 15.31739 26.18541 -9.17422  1.000 43.51529  ? 82  LEU A N   1 
ATOM   648 C CA  . LEU A 1 86  ? 14.81211 27.53237 -8.94924  1.000 37.85195  ? 82  LEU A CA  1 
ATOM   649 C C   . LEU A 1 86  ? 13.29052 27.47782 -8.97571  1.000 44.61934  ? 82  LEU A C   1 
ATOM   650 O O   . LEU A 1 86  ? 12.69503 27.15632 -10.00996 1.000 50.24028  ? 82  LEU A O   1 
ATOM   651 C CB  . LEU A 1 86  ? 15.34267 28.50784 -9.99962  1.000 45.28385  ? 82  LEU A CB  1 
ATOM   652 C CG  . LEU A 1 86  ? 16.58655 29.30072 -9.59176  1.000 58.00738  ? 82  LEU A CG  1 
ATOM   653 C CD1 . LEU A 1 86  ? 16.35988 29.99815 -8.26452  1.000 54.12695  ? 82  LEU A CD1 1 
ATOM   654 C CD2 . LEU A 1 86  ? 17.80525 28.40348 -9.51370  1.000 66.79400  ? 82  LEU A CD2 1 
ATOM   655 N N   . ALA A 1 87  ? 12.66868 27.77779 -7.83972  1.000 44.97734  ? 83  ALA A N   1 
ATOM   656 C CA  . ALA A 1 87  ? 11.22094 27.71555 -7.69554  1.000 45.10187  ? 83  ALA A CA  1 
ATOM   657 C C   . ALA A 1 87  ? 10.63211 29.11340 -7.82239  1.000 41.03459  ? 83  ALA A C   1 
ATOM   658 O O   . ALA A 1 87  ? 11.06247 30.03916 -7.12697  1.000 47.92961  ? 83  ALA A O   1 
ATOM   659 C CB  . ALA A 1 87  ? 10.83352 27.09705 -6.35199  1.000 40.39985  ? 83  ALA A CB  1 
ATOM   660 N N   . THR A 1 88  ? 9.64814  29.25984 -8.70450  1.000 45.16616  ? 84  THR A N   1 
ATOM   661 C CA  . THR A 1 88  ? 9.00359  30.53948 -8.96928  1.000 43.83153  ? 84  THR A CA  1 
ATOM   662 C C   . THR A 1 88  ? 7.56107  30.47811 -8.48660  1.000 46.26333  ? 84  THR A C   1 
ATOM   663 O O   . THR A 1 88  ? 6.79724  29.60462 -8.91209  1.000 47.40674  ? 84  THR A O   1 
ATOM   664 C CB  . THR A 1 88  ? 9.05132  30.88197 -10.45889 1.000 59.73262  ? 84  THR A CB  1 
ATOM   665 O OG1 . THR A 1 88  ? 8.88712  29.68626 -11.23180 1.000 63.77008  ? 84  THR A OG1 1 
ATOM   666 C CG2 . THR A 1 88  ? 10.37902 31.52797 -10.81394 1.000 53.59879  ? 84  THR A CG2 1 
ATOM   667 N N   . GLY A 1 89  ? 7.19313  31.40196 -7.60258  1.000 53.63672  ? 85  GLY A N   1 
ATOM   668 C CA  . GLY A 1 89  ? 5.82518  31.52959 -7.15976  1.000 51.00850  ? 85  GLY A CA  1 
ATOM   669 C C   . GLY A 1 89  ? 5.02566  32.40080 -8.10652  1.000 49.91614  ? 85  GLY A C   1 
ATOM   670 O O   . GLY A 1 89  ? 5.58384  33.07401 -8.97767  1.000 48.48190  ? 85  GLY A O   1 
ATOM   671 N N   . PRO A 1 90  ? 3.69796  32.40367 -7.95803  1.000 53.22086  ? 86  PRO A N   1 
ATOM   672 C CA  . PRO A 1 90  ? 2.86501  33.21832 -8.85782  1.000 58.19141  ? 86  PRO A CA  1 
ATOM   673 C C   . PRO A 1 90  ? 3.18863  34.70011 -8.79976  1.000 57.13825  ? 86  PRO A C   1 
ATOM   674 O O   . PRO A 1 90  ? 2.99771  35.40834 -9.79637  1.000 66.73672  ? 86  PRO A O   1 
ATOM   675 C CB  . PRO A 1 90  ? 1.44042  32.93282 -8.36382  1.000 65.88217  ? 86  PRO A CB  1 
ATOM   676 C CG  . PRO A 1 90  ? 1.53577  31.60698 -7.68402  1.000 60.98181  ? 86  PRO A CG  1 
ATOM   677 C CD  . PRO A 1 90  ? 2.88695  31.59393 -7.03572  1.000 56.76009  ? 86  PRO A CD  1 
ATOM   678 N N   . SER A 1 91  ? 3.67565  35.19022 -7.66100  1.000 68.75248  ? 87  SER A N   1 
ATOM   679 C CA  . SER A 1 91  ? 4.06679  36.58535 -7.51239  1.000 62.83861  ? 87  SER A CA  1 
ATOM   680 C C   . SER A 1 91  ? 5.39747  36.90452 -8.17586  1.000 61.78692  ? 87  SER A C   1 
ATOM   681 O O   . SER A 1 91  ? 5.83904  38.05686 -8.11400  1.000 58.40726  ? 87  SER A O   1 
ATOM   682 C CB  . SER A 1 91  ? 4.14587  36.94912 -6.02875  1.000 63.42422  ? 87  SER A CB  1 
ATOM   683 O OG  . SER A 1 91  ? 2.93230  37.51489 -5.57912  1.000 83.00174  ? 87  SER A OG  1 
ATOM   684 N N   . GLY A 1 92  ? 6.04086  35.92624 -8.80648  1.000 57.75997  ? 88  GLY A N   1 
ATOM   685 C CA  . GLY A 1 92  ? 7.38663  36.10379 -9.29809  1.000 55.64543  ? 88  GLY A CA  1 
ATOM   686 C C   . GLY A 1 92  ? 8.46628  35.86790 -8.26844  1.000 57.29976  ? 88  GLY A C   1 
ATOM   687 O O   . GLY A 1 92  ? 9.65258  35.98231 -8.60332  1.000 58.48045  ? 88  GLY A O   1 
ATOM   688 N N   . PHE A 1 93  ? 8.09664  35.55041 -7.02844  1.000 50.54546  ? 89  PHE A N   1 
ATOM   689 C CA  . PHE A 1 93  ? 9.08522  35.25604 -6.00146  1.000 58.21996  ? 89  PHE A CA  1 
ATOM   690 C C   . PHE A 1 93  ? 9.88254  34.01748 -6.38400  1.000 49.26546  ? 89  PHE A C   1 
ATOM   691 O O   . PHE A 1 93  ? 9.31429  32.97019 -6.70718  1.000 53.24212  ? 89  PHE A O   1 
ATOM   692 C CB  . PHE A 1 93  ? 8.40322  35.05360 -4.64867  1.000 51.83581  ? 89  PHE A CB  1 
ATOM   693 C CG  . PHE A 1 93  ? 9.32463  34.54476 -3.57742  1.000 50.97448  ? 89  PHE A CG  1 
ATOM   694 C CD1 . PHE A 1 93  ? 10.47537 35.24156 -3.24650  1.000 54.36737  ? 89  PHE A CD1 1 
ATOM   695 C CD2 . PHE A 1 93  ? 9.04181  33.36870 -2.90281  1.000 45.20946  ? 89  PHE A CD2 1 
ATOM   696 C CE1 . PHE A 1 93  ? 11.32701 34.77539 -2.26247  1.000 57.76124  ? 89  PHE A CE1 1 
ATOM   697 C CE2 . PHE A 1 93  ? 9.88924  32.89705 -1.91765  1.000 47.10362  ? 89  PHE A CE2 1 
ATOM   698 C CZ  . PHE A 1 93  ? 11.03339 33.60173 -1.59719  1.000 51.20937  ? 89  PHE A CZ  1 
ATOM   699 N N   . THR A 1 94  ? 11.20485 34.14395 -6.34688  1.000 56.36219  ? 90  THR A N   1 
ATOM   700 C CA  . THR A 1 94  ? 12.11519 33.10148 -6.79569  1.000 53.04508  ? 90  THR A CA  1 
ATOM   701 C C   . THR A 1 94  ? 12.97369 32.64877 -5.62420  1.000 48.02038  ? 90  THR A C   1 
ATOM   702 O O   . THR A 1 94  ? 13.59469 33.47652 -4.94854  1.000 45.66170  ? 90  THR A O   1 
ATOM   703 C CB  . THR A 1 94  ? 12.99068 33.60946 -7.94563  1.000 58.20262  ? 90  THR A CB  1 
ATOM   704 O OG1 . THR A 1 94  ? 12.25482 33.53777 -9.17234  1.000 59.29855  ? 90  THR A OG1 1 
ATOM   705 C CG2 . THR A 1 94  ? 14.25013 32.78039 -8.07271  1.000 43.69754  ? 90  THR A CG2 1 
ATOM   706 N N   . LEU A 1 95  ? 13.00150 31.33938 -5.38195  1.000 51.89627  ? 91  LEU A N   1 
ATOM   707 C CA  . LEU A 1 95  ? 13.76174 30.76638 -4.27980  1.000 47.10215  ? 91  LEU A CA  1 
ATOM   708 C C   . LEU A 1 95  ? 14.67972 29.67446 -4.80470  1.000 43.00683  ? 91  LEU A C   1 
ATOM   709 O O   . LEU A 1 95  ? 14.23357 28.77530 -5.52493  1.000 44.82551  ? 91  LEU A O   1 
ATOM   710 C CB  . LEU A 1 95  ? 12.83609 30.19847 -3.19910  1.000 42.13159  ? 91  LEU A CB  1 
ATOM   711 C CG  . LEU A 1 95  ? 13.54534 29.49604 -2.03947  1.000 48.50978  ? 91  LEU A CG  1 
ATOM   712 C CD1 . LEU A 1 95  ? 14.35123 30.49358 -1.22357  1.000 36.93555  ? 91  LEU A CD1 1 
ATOM   713 C CD2 . LEU A 1 95  ? 12.55065 28.76022 -1.15787  1.000 57.38720  ? 91  LEU A CD2 1 
ATOM   714 N N   . LYS A 1 96  ? 15.95713 29.75607 -4.43985  1.000 37.18730  ? 92  LYS A N   1 
ATOM   715 C CA  . LYS A 1 96  ? 16.93716 28.72945 -4.78460  1.000 38.78143  ? 92  LYS A CA  1 
ATOM   716 C C   . LYS A 1 96  ? 16.75302 27.55587 -3.83296  1.000 47.05487  ? 92  LYS A C   1 
ATOM   717 O O   . LYS A 1 96  ? 17.22465 27.58283 -2.69421  1.000 52.45864  ? 92  LYS A O   1 
ATOM   718 C CB  . LYS A 1 96  ? 18.35256 29.28981 -4.70676  1.000 39.56566  ? 92  LYS A CB  1 
ATOM   719 C CG  . LYS A 1 96  ? 19.44551 28.27247 -4.99789  1.000 50.39512  ? 92  LYS A CG  1 
ATOM   720 C CD  . LYS A 1 96  ? 19.23963 27.61748 -6.35056  1.000 66.01750  ? 92  LYS A CD  1 
ATOM   721 C CE  . LYS A 1 96  ? 20.42238 26.74742 -6.73331  1.000 67.07682  ? 92  LYS A CE  1 
ATOM   722 N NZ  . LYS A 1 96  ? 20.57402 26.66179 -8.21212  1.000 69.80353  ? 92  LYS A NZ  1 
ATOM   723 N N   . VAL A 1 97  ? 16.05592 26.52331 -4.29235  1.000 42.79404  ? 93  VAL A N   1 
ATOM   724 C CA  . VAL A 1 97  ? 15.84955 25.32482 -3.50174  1.000 46.54669  ? 93  VAL A CA  1 
ATOM   725 C C   . VAL A 1 97  ? 16.77465 24.23610 -4.02188  1.000 40.92116  ? 93  VAL A C   1 
ATOM   726 O O   . VAL A 1 97  ? 17.23506 24.26226 -5.16563  1.000 38.90345  ? 93  VAL A O   1 
ATOM   727 C CB  . VAL A 1 97  ? 14.37637 24.85668 -3.51690  1.000 40.70896  ? 93  VAL A CB  1 
ATOM   728 C CG1 . VAL A 1 97  ? 13.44076 26.04247 -3.35609  1.000 35.98704  ? 93  VAL A CG1 1 
ATOM   729 C CG2 . VAL A 1 97  ? 14.06227 24.08884 -4.78579  1.000 43.02741  ? 93  VAL A CG2 1 
ATOM   730 N N   . LYS A 1 98  ? 17.07039 23.27410 -3.15702  1.000 38.38908  ? 94  LYS A N   1 
ATOM   731 C CA  . LYS A 1 98  ? 17.95818 22.17212 -3.48709  1.000 41.37040  ? 94  LYS A CA  1 
ATOM   732 C C   . LYS A 1 98  ? 17.29036 20.86438 -3.10980  1.000 38.55166  ? 94  LYS A C   1 
ATOM   733 O O   . LYS A 1 98  ? 16.65863 20.76299 -2.05440  1.000 44.66399  ? 94  LYS A O   1 
ATOM   734 C CB  . LYS A 1 98  ? 19.28766 22.29467 -2.75874  1.000 47.99104  ? 94  LYS A CB  1 
ATOM   735 C CG  . LYS A 1 98  ? 20.04470 23.56833 -3.05633  1.000 50.77778  ? 94  LYS A CG  1 
ATOM   736 C CD  . LYS A 1 98  ? 21.35606 23.54069 -2.31572  1.000 73.16638  ? 94  LYS A CD  1 
ATOM   737 C CE  . LYS A 1 98  ? 21.06811 23.60915 -0.82122  1.000 76.03026  ? 94  LYS A CE  1 
ATOM   738 N NZ  . LYS A 1 98  ? 22.29010 23.57050 0.01483   1.000 74.91513  ? 94  LYS A NZ  1 
ATOM   739 N N   . SER A 1 99  ? 17.43964 19.86481 -3.97018  1.000 37.13769  ? 95  SER A N   1 
ATOM   740 C CA  . SER A 1 99  ? 16.80850 18.57327 -3.76234  1.000 33.81956  ? 95  SER A CA  1 
ATOM   741 C C   . SER A 1 99  ? 17.84078 17.46312 -3.86667  1.000 37.10175  ? 95  SER A C   1 
ATOM   742 O O   . SER A 1 99  ? 18.69321 17.47392 -4.75960  1.000 38.17722  ? 95  SER A O   1 
ATOM   743 C CB  . SER A 1 99  ? 15.68857 18.33599 -4.77554  1.000 34.91994  ? 95  SER A CB  1 
ATOM   744 O OG  . SER A 1 99  ? 14.77187 19.41857 -4.79368  1.000 40.25436  ? 95  SER A OG  1 
ATOM   745 N N   . THR A 1 100 ? 17.75360 16.50474 -2.94861  1.000 40.84599  ? 96  THR A N   1 
ATOM   746 C CA  . THR A 1 100 ? 18.58797 15.30839 -2.96100  1.000 38.81292  ? 96  THR A CA  1 
ATOM   747 C C   . THR A 1 100 ? 17.66122 14.10744 -3.08495  1.000 32.28715  ? 96  THR A C   1 
ATOM   748 O O   . THR A 1 100 ? 16.89496 13.81007 -2.16213  1.000 46.87900  ? 96  THR A O   1 
ATOM   749 C CB  . THR A 1 100 ? 19.44960 15.21399 -1.70229  1.000 39.04715  ? 96  THR A CB  1 
ATOM   750 O OG1 . THR A 1 100 ? 20.22959 16.40839 -1.56453  1.000 45.41412  ? 96  THR A OG1 1 
ATOM   751 C CG2 . THR A 1 100 ? 20.38165 14.01267 -1.78601  1.000 38.36793  ? 96  THR A CG2 1 
ATOM   752 N N   . ILE A 1 101 ? 17.72261 13.42853 -4.22565  1.000 36.64068  ? 97  ILE A N   1 
ATOM   753 C CA  . ILE A 1 101 ? 16.84811 12.30318 -4.52851  1.000 45.75092  ? 97  ILE A CA  1 
ATOM   754 C C   . ILE A 1 101 ? 17.69789 11.04301 -4.60217  1.000 43.39456  ? 97  ILE A C   1 
ATOM   755 O O   . ILE A 1 101 ? 18.76117 11.03867 -5.23329  1.000 47.26621  ? 97  ILE A O   1 
ATOM   756 C CB  . ILE A 1 101 ? 16.07414 12.53196 -5.83762  1.000 42.80170  ? 97  ILE A CB  1 
ATOM   757 C CG1 . ILE A 1 101 ? 15.33926 13.87306 -5.78252  1.000 43.96066  ? 97  ILE A CG1 1 
ATOM   758 C CG2 . ILE A 1 101 ? 15.09916 11.39383 -6.08854  1.000 41.78761  ? 97  ILE A CG2 1 
ATOM   759 C CD1 . ILE A 1 101 ? 15.11056 14.50557 -7.13342  1.000 39.23222  ? 97  ILE A CD1 1 
ATOM   760 N N   . THR A 1 102 ? 17.22939 9.98122  -3.95446  1.000 44.88786  ? 98  THR A N   1 
ATOM   761 C CA  . THR A 1 102 ? 17.94746 8.71654  -3.88563  1.000 48.13151  ? 98  THR A CA  1 
ATOM   762 C C   . THR A 1 102 ? 17.16842 7.64198  -4.63054  1.000 49.61813  ? 98  THR A C   1 
ATOM   763 O O   . THR A 1 102 ? 15.97400 7.44822  -4.38100  1.000 47.74278  ? 98  THR A O   1 
ATOM   764 C CB  . THR A 1 102 ? 18.17221 8.29268  -2.43248  1.000 47.64072  ? 98  THR A CB  1 
ATOM   765 O OG1 . THR A 1 102 ? 18.83741 9.34604  -1.72367  1.000 51.91743  ? 98  THR A OG1 1 
ATOM   766 C CG2 . THR A 1 102 ? 19.01712 7.03098  -2.37132  1.000 48.54174  ? 98  THR A CG2 1 
ATOM   767 N N   . PHE A 1 103 ? 17.84630 6.95170  -5.54255  1.000 55.11810  ? 99  PHE A N   1 
ATOM   768 C CA  . PHE A 1 103 ? 17.27737 5.83678  -6.28243  1.000 57.30574  ? 99  PHE A CA  1 
ATOM   769 C C   . PHE A 1 103 ? 17.99015 4.54654  -5.90071  1.000 61.47504  ? 99  PHE A C   1 
ATOM   770 O O   . PHE A 1 103 ? 19.17874 4.55024  -5.56962  1.000 61.60042  ? 99  PHE A O   1 
ATOM   771 C CB  . PHE A 1 103 ? 17.39602 6.05143  -7.79509  1.000 55.35781  ? 99  PHE A CB  1 
ATOM   772 C CG  . PHE A 1 103 ? 16.65060 7.25159  -8.30356  1.000 52.08768  ? 99  PHE A CG  1 
ATOM   773 C CD1 . PHE A 1 103 ? 15.32726 7.14626  -8.69743  1.000 53.63044  ? 99  PHE A CD1 1 
ATOM   774 C CD2 . PHE A 1 103 ? 17.27794 8.48243  -8.40035  1.000 49.88958  ? 99  PHE A CD2 1 
ATOM   775 C CE1 . PHE A 1 103 ? 14.64147 8.24710  -9.17210  1.000 43.67964  ? 99  PHE A CE1 1 
ATOM   776 C CE2 . PHE A 1 103 ? 16.59786 9.58793  -8.87313  1.000 50.40184  ? 99  PHE A CE2 1 
ATOM   777 C CZ  . PHE A 1 103 ? 15.27695 9.47019  -9.25943  1.000 32.91730  ? 99  PHE A CZ  1 
ATOM   778 N N   . ASP A 1 104 ? 17.25374 3.43877  -5.94921  1.000 67.56621  ? 100 ASP A N   1 
ATOM   779 C CA  . ASP A 1 104 ? 17.83054 2.12196  -5.75300  1.000 78.62925  ? 100 ASP A CA  1 
ATOM   780 C C   . ASP A 1 104 ? 17.90280 1.40459  -7.10416  1.000 80.69895  ? 100 ASP A C   1 
ATOM   781 O O   . ASP A 1 104 ? 17.83668 2.04465  -8.16425  1.000 76.85683  ? 100 ASP A O   1 
ATOM   782 C CB  . ASP A 1 104 ? 17.01995 1.35506  -4.70213  1.000 76.43826  ? 100 ASP A CB  1 
ATOM   783 C CG  . ASP A 1 104 ? 15.59013 1.10050  -5.13415  1.000 80.66489  ? 100 ASP A CG  1 
ATOM   784 O OD1 . ASP A 1 104 ? 15.09858 1.81135  -6.03565  1.000 88.02409  ? 100 ASP A OD1 1 
ATOM   785 O OD2 . ASP A 1 104 ? 14.95627 0.18511  -4.56838  1.000 81.55859  ? 100 ASP A OD2 1 
ATOM   786 N N   . GLU A 1 105 ? 18.04063 0.07716  -7.06700  1.000 83.11216  ? 101 GLU A N   1 
ATOM   787 C CA  . GLU A 1 105 ? 18.16124 -0.68463 -8.30670  1.000 83.35277  ? 101 GLU A CA  1 
ATOM   788 C C   . GLU A 1 105 ? 16.87836 -0.61579 -9.12731  1.000 83.35177  ? 101 GLU A C   1 
ATOM   789 O O   . GLU A 1 105 ? 16.92702 -0.50282 -10.35802 1.000 76.81222  ? 101 GLU A O   1 
ATOM   790 C CB  . GLU A 1 105 ? 18.52774 -2.13678 -7.99713  1.000 95.65372  ? 101 GLU A CB  1 
ATOM   791 C CG  . GLU A 1 105 ? 18.25457 -3.10638 -9.13690  1.000 105.31036 ? 101 GLU A CG  1 
ATOM   792 C CD  . GLU A 1 105 ? 17.71071 -4.43595 -8.65371  1.000 100.77357 ? 101 GLU A CD  1 
ATOM   793 O OE1 . GLU A 1 105 ? 18.46275 -5.18287 -7.99289  1.000 93.70887  ? 101 GLU A OE1 1 
ATOM   794 O OE2 . GLU A 1 105 ? 16.53081 -4.73489 -8.93400  1.000 93.77568  ? 101 GLU A OE2 1 
ATOM   795 N N   . ASP A 1 106 ? 15.72151 -0.66359 -8.46447  1.000 84.29245  ? 102 ASP A N   1 
ATOM   796 C CA  . ASP A 1 106 ? 14.43372 -0.61498 -9.14962  1.000 81.28440  ? 102 ASP A CA  1 
ATOM   797 C C   . ASP A 1 106 ? 14.14108 0.73999  -9.78274  1.000 76.75823  ? 102 ASP A C   1 
ATOM   798 O O   . ASP A 1 106 ? 13.05144 0.91236  -10.33734 1.000 76.23407  ? 102 ASP A O   1 
ATOM   799 C CB  . ASP A 1 106 ? 13.30668 -0.97110 -8.17553  1.000 81.97013  ? 102 ASP A CB  1 
ATOM   800 C CG  . ASP A 1 106 ? 13.59894 -2.22373 -7.37408  1.000 94.19429  ? 102 ASP A CG  1 
ATOM   801 O OD1 . ASP A 1 106 ? 14.77249 -2.43461 -7.00249  1.000 99.70020  ? 102 ASP A OD1 1 
ATOM   802 O OD2 . ASP A 1 106 ? 12.65392 -2.99743 -7.11252  1.000 103.62147 ? 102 ASP A OD2 1 
ATOM   803 N N   . MET A 1 107 ? 15.07088 1.69231  -9.71255  1.000 67.92836  ? 103 MET A N   1 
ATOM   804 C CA  . MET A 1 107 ? 14.87968 3.06038  -10.18717 1.000 66.25553  ? 103 MET A CA  1 
ATOM   805 C C   . MET A 1 107 ? 13.69643 3.74643  -9.51345  1.000 63.33345  ? 103 MET A C   1 
ATOM   806 O O   . MET A 1 107 ? 13.11019 4.67600  -10.07829 1.000 56.76443  ? 103 MET A O   1 
ATOM   807 C CB  . MET A 1 107 ? 14.73398 3.10373  -11.71326 1.000 64.93701  ? 103 MET A CB  1 
ATOM   808 C CG  . MET A 1 107 ? 16.02996 3.41492  -12.44022 1.000 74.26298  ? 103 MET A CG  1 
ATOM   809 S SD  . MET A 1 107 ? 16.98427 4.69928  -11.61056 1.000 76.78986  ? 103 MET A SD  1 
ATOM   810 C CE  . MET A 1 107 ? 18.35304 3.74761  -10.95393 1.000 57.22039  ? 103 MET A CE  1 
ATOM   811 N N   . LYS A 1 108 ? 13.33736 3.29884  -8.31337  1.000 63.84370  ? 104 LYS A N   1 
ATOM   812 C CA  . LYS A 1 108 ? 12.28879 3.91857  -7.52105  1.000 56.75914  ? 104 LYS A CA  1 
ATOM   813 C C   . LYS A 1 108 ? 12.91215 4.79414  -6.44146  1.000 51.93114  ? 104 LYS A C   1 
ATOM   814 O O   . LYS A 1 108 ? 13.99053 4.49748  -5.92088  1.000 44.13032  ? 104 LYS A O   1 
ATOM   815 C CB  . LYS A 1 108 ? 11.38321 2.86088  -6.88650  1.000 60.83757  ? 104 LYS A CB  1 
ATOM   816 C CG  . LYS A 1 108 ? 10.19474 2.46657  -7.74760  1.000 64.17327  ? 104 LYS A CG  1 
ATOM   817 C CD  . LYS A 1 108 ? 9.02760  1.99833  -6.89589  1.000 64.51475  ? 104 LYS A CD  1 
ATOM   818 C CE  . LYS A 1 108 ? 7.73708  1.96455  -7.69708  1.000 69.68095  ? 104 LYS A CE  1 
ATOM   819 N NZ  . LYS A 1 108 ? 6.60944  1.37162  -6.92536  1.000 67.48495  ? 104 LYS A NZ  1 
ATOM   820 N N   . ILE A 1 109 ? 12.22372 5.88242  -6.11392  1.000 50.23468  ? 105 ILE A N   1 
ATOM   821 C CA  . ILE A 1 109 ? 12.74771 6.86431  -5.17100  1.000 50.48248  ? 105 ILE A CA  1 
ATOM   822 C C   . ILE A 1 109 ? 12.61806 6.31587  -3.75481  1.000 53.39460  ? 105 ILE A C   1 
ATOM   823 O O   . ILE A 1 109 ? 11.51298 6.02432  -3.28802  1.000 53.45506  ? 105 ILE A O   1 
ATOM   824 C CB  . ILE A 1 109 ? 12.01998 8.20813  -5.31024  1.000 48.74494  ? 105 ILE A CB  1 
ATOM   825 C CG1 . ILE A 1 109 ? 12.13219 8.72306  -6.74610  1.000 45.97074  ? 105 ILE A CG1 1 
ATOM   826 C CG2 . ILE A 1 109 ? 12.58642 9.22121  -4.32582  1.000 49.15861  ? 105 ILE A CG2 1 
ATOM   827 C CD1 . ILE A 1 109 ? 11.70032 10.16213 -6.92167  1.000 52.13208  ? 105 ILE A CD1 1 
ATOM   828 N N   . THR A 1 110 ? 13.75392 6.17221  -3.07223  1.000 47.62700  ? 106 THR A N   1 
ATOM   829 C CA  . THR A 1 110 ? 13.76197 5.76472  -1.67274  1.000 49.69753  ? 106 THR A CA  1 
ATOM   830 C C   . THR A 1 110 ? 13.74350 6.96253  -0.73200  1.000 51.08086  ? 106 THR A C   1 
ATOM   831 O O   . THR A 1 110 ? 13.06972 6.92697  0.30346   1.000 50.41391  ? 106 THR A O   1 
ATOM   832 C CB  . THR A 1 110 ? 14.98948 4.89828  -1.37561  1.000 56.39874  ? 106 THR A CB  1 
ATOM   833 O OG1 . THR A 1 110 ? 16.17671 5.69162  -1.49705  1.000 60.48978  ? 106 THR A OG1 1 
ATOM   834 C CG2 . THR A 1 110 ? 15.06600 3.73019  -2.34771  1.000 56.79035  ? 106 THR A CG2 1 
ATOM   835 N N   . SER A 1 111 ? 14.47203 8.02357  -1.07437  1.000 51.02861  ? 107 SER A N   1 
ATOM   836 C CA  . SER A 1 111 ? 14.52814 9.23015  -0.26373  1.000 50.71145  ? 107 SER A CA  1 
ATOM   837 C C   . SER A 1 111 ? 14.44838 10.45039 -1.16713  1.000 43.02764  ? 107 SER A C   1 
ATOM   838 O O   . SER A 1 111 ? 15.01581 10.46113 -2.26319  1.000 37.00828  ? 107 SER A O   1 
ATOM   839 C CB  . SER A 1 111 ? 15.80982 9.28427  0.57729   1.000 39.67205  ? 107 SER A CB  1 
ATOM   840 O OG  . SER A 1 111 ? 15.65454 10.15857 1.68094   1.000 60.70395  ? 107 SER A OG  1 
ATOM   841 N N   . TYR A 1 112 ? 13.74342 11.47621 -0.69560  1.000 40.45790  ? 108 TYR A N   1 
ATOM   842 C CA  . TYR A 1 112 ? 13.55554 12.71737 -1.44164  1.000 42.39174  ? 108 TYR A CA  1 
ATOM   843 C C   . TYR A 1 112 ? 13.57911 13.85879 -0.43595  1.000 39.87054  ? 108 TYR A C   1 
ATOM   844 O O   . TYR A 1 112 ? 12.61891 14.04174 0.31804   1.000 45.57728  ? 108 TYR A O   1 
ATOM   845 C CB  . TYR A 1 112 ? 12.24119 12.69307 -2.22431  1.000 39.63305  ? 108 TYR A CB  1 
ATOM   846 C CG  . TYR A 1 112 ? 12.12780 13.70535 -3.34796  1.000 40.49722  ? 108 TYR A CG  1 
ATOM   847 C CD1 . TYR A 1 112 ? 12.44088 15.04496 -3.15059  1.000 39.29818  ? 108 TYR A CD1 1 
ATOM   848 C CD2 . TYR A 1 112 ? 11.68972 13.31754 -4.60663  1.000 48.92101  ? 108 TYR A CD2 1 
ATOM   849 C CE1 . TYR A 1 112 ? 12.32701 15.96368 -4.17713  1.000 40.60612  ? 108 TYR A CE1 1 
ATOM   850 C CE2 . TYR A 1 112 ? 11.57154 14.22688 -5.63484  1.000 50.83911  ? 108 TYR A CE2 1 
ATOM   851 C CZ  . TYR A 1 112 ? 11.89170 15.54730 -5.41635  1.000 48.18022  ? 108 TYR A CZ  1 
ATOM   852 O OH  . TYR A 1 112 ? 11.77222 16.44897 -6.44591  1.000 49.05813  ? 108 TYR A OH  1 
ATOM   853 N N   . GLU A 1 113 ? 14.66759 14.62099 -0.42186  1.000 43.32921  ? 109 GLU A N   1 
ATOM   854 C CA  . GLU A 1 113 ? 14.84101 15.72828 0.50775   1.000 46.85131  ? 109 GLU A CA  1 
ATOM   855 C C   . GLU A 1 113 ? 14.78941 17.04487 -0.25313  1.000 42.52026  ? 109 GLU A C   1 
ATOM   856 O O   . GLU A 1 113 ? 15.49518 17.21609 -1.25154  1.000 42.43996  ? 109 GLU A O   1 
ATOM   857 C CB  . GLU A 1 113 ? 16.16537 15.60549 1.26426   1.000 42.45094  ? 109 GLU A CB  1 
ATOM   858 C CG  . GLU A 1 113 ? 16.30784 16.57864 2.42294   1.000 59.29409  ? 109 GLU A CG  1 
ATOM   859 C CD  . GLU A 1 113 ? 17.71891 17.11198 2.56742   1.000 74.52327  ? 109 GLU A CD  1 
ATOM   860 O OE1 . GLU A 1 113 ? 18.67036 16.30474 2.50964   1.000 86.34783  ? 109 GLU A OE1 1 
ATOM   861 O OE2 . GLU A 1 113 ? 17.87706 18.33892 2.73991   1.000 71.36613  ? 109 GLU A OE2 1 
ATOM   862 N N   . VAL A 1 114 ? 13.95669 17.96808 0.21923   1.000 34.02102  ? 110 VAL A N   1 
ATOM   863 C CA  . VAL A 1 114 ? 13.82471 19.29633 -0.36830  1.000 40.62467  ? 110 VAL A CA  1 
ATOM   864 C C   . VAL A 1 114 ? 14.32295 20.31124 0.65035   1.000 41.03583  ? 110 VAL A C   1 
ATOM   865 O O   . VAL A 1 114 ? 13.77694 20.41297 1.75647   1.000 41.11752  ? 110 VAL A O   1 
ATOM   866 C CB  . VAL A 1 114 ? 12.37664 19.59568 -0.78337  1.000 38.26700  ? 110 VAL A CB  1 
ATOM   867 C CG1 . VAL A 1 114 ? 12.23822 21.05091 -1.20091  1.000 38.79537  ? 110 VAL A CG1 1 
ATOM   868 C CG2 . VAL A 1 114 ? 11.94735 18.67389 -1.91261  1.000 36.07003  ? 110 VAL A CG2 1 
ATOM   869 N N   . ASN A 1 115 ? 15.35568 21.06140 0.27747   1.000 48.38782  ? 111 ASN A N   1 
ATOM   870 C CA  . ASN A 1 115 ? 15.96574 22.06540 1.14025   1.000 46.23791  ? 111 ASN A CA  1 
ATOM   871 C C   . ASN A 1 115 ? 15.54644 23.44767 0.65803   1.000 48.11274  ? 111 ASN A C   1 
ATOM   872 O O   . ASN A 1 115 ? 15.86408 23.83739 -0.47070  1.000 42.10867  ? 111 ASN A O   1 
ATOM   873 C CB  . ASN A 1 115 ? 17.48788 21.92111 1.13870   1.000 47.10402  ? 111 ASN A CB  1 
ATOM   874 C CG  . ASN A 1 115 ? 18.18135 22.99644 1.94780   1.000 58.61344  ? 111 ASN A CG  1 
ATOM   875 O OD1 . ASN A 1 115 ? 18.28991 24.14421 1.51657   1.000 66.39064  ? 111 ASN A OD1 1 
ATOM   876 N ND2 . ASN A 1 115 ? 18.65814 22.62771 3.13059   1.000 55.77393  ? 111 ASN A ND2 1 
ATOM   877 N N   . LEU A 1 116 ? 14.83494 24.18371 1.51112   1.000 43.11382  ? 112 LEU A N   1 
ATOM   878 C CA  . LEU A 1 116 ? 14.30185 25.49247 1.15589   1.000 45.69882  ? 112 LEU A CA  1 
ATOM   879 C C   . LEU A 1 116 ? 15.02857 26.63573 1.85078   1.000 52.71773  ? 112 LEU A C   1 
ATOM   880 O O   . LEU A 1 116 ? 14.62056 27.79252 1.70806   1.000 55.96616  ? 112 LEU A O   1 
ATOM   881 C CB  . LEU A 1 116 ? 12.80537 25.55929 1.47127   1.000 41.14640  ? 112 LEU A CB  1 
ATOM   882 C CG  . LEU A 1 116 ? 11.93323 24.42169 0.93820   1.000 46.37913  ? 112 LEU A CG  1 
ATOM   883 C CD1 . LEU A 1 116 ? 10.70261 24.23031 1.80910   1.000 36.71228  ? 112 LEU A CD1 1 
ATOM   884 C CD2 . LEU A 1 116 ? 11.53463 24.68602 -0.50740  1.000 39.17149  ? 112 LEU A CD2 1 
ATOM   885 N N   . GLU A 1 117 ? 16.09367 26.34526 2.59766   1.000 51.40276  ? 113 GLU A N   1 
ATOM   886 C CA  . GLU A 1 117 ? 16.82655 27.40872 3.27468   1.000 67.85216  ? 113 GLU A CA  1 
ATOM   887 C C   . GLU A 1 117 ? 17.79680 28.10732 2.33202   1.000 79.95350  ? 113 GLU A C   1 
ATOM   888 O O   . GLU A 1 117 ? 17.97570 29.32520 2.42027   1.000 86.94276  ? 113 GLU A O   1 
ATOM   889 C CB  . GLU A 1 117 ? 17.54113 26.84480 4.51209   1.000 61.23786  ? 113 GLU A CB  1 
ATOM   890 C CG  . GLU A 1 117 ? 18.51272 25.68991 4.25997   1.000 79.24364  ? 113 GLU A CG  1 
ATOM   891 C CD  . GLU A 1 117 ? 19.94505 26.11126 3.96811   1.000 98.29571  ? 113 GLU A CD  1 
ATOM   892 O OE1 . GLU A 1 117 ? 20.19224 27.29163 3.66353   1.000 98.43169  ? 113 GLU A OE1 1 
ATOM   893 O OE2 . GLU A 1 117 ? 20.84337 25.24037 4.02148   1.000 96.01322  ? 113 GLU A OE2 1 
ATOM   894 N N   . GLY A 1 118 ? 18.43316 27.36150 1.43720   1.000 77.47489  ? 114 GLY A N   1 
ATOM   895 C CA  . GLY A 1 118 ? 19.36731 27.94006 0.49510   1.000 77.05989  ? 114 GLY A CA  1 
ATOM   896 C C   . GLY A 1 118 ? 20.70563 27.23482 0.52956   1.000 80.91337  ? 114 GLY A C   1 
ATOM   897 O O   . GLY A 1 118 ? 21.64254 27.68985 1.18929   1.000 82.57846  ? 114 GLY A O   1 
HETATM 898 C C1  . GG2 B 2 .   ? 8.85455  28.48846 -2.99472  1.000 51.15529  ? 201 GG2 A C1  1 
HETATM 899 C C2  . GG2 B 2 .   ? 9.12028  28.14759 -1.67866  1.000 47.22647  ? 201 GG2 A C2  1 
HETATM 900 C C3  . GG2 B 2 .   ? 8.76777  26.89639 -1.20031  1.000 51.94620  ? 201 GG2 A C3  1 
HETATM 901 O O4  . GG2 B 2 .   ? 9.21425  29.75419 -3.47254  1.000 52.70246  ? 201 GG2 A O4  1 
HETATM 902 N N6  . GG2 B 2 .   ? 6.96295  24.54837 -0.56621  1.000 41.12583  ? 201 GG2 A N6  1 
HETATM 903 C C7  . GG2 B 2 .   ? 9.87143  21.20162 -4.73690  1.000 35.72275  ? 201 GG2 A C7  1 
HETATM 904 C C8  . GG2 B 2 .   ? 9.11293  23.04975 -3.15258  1.000 33.70365  ? 201 GG2 A C8  1 
HETATM 905 C C10 . GG2 B 2 .   ? 6.81637  23.26761 -0.36911  1.000 47.98673  ? 201 GG2 A C10 1 
HETATM 906 C C11 . GG2 B 2 .   ? 5.91886  22.69135 0.72349   1.000 44.32814  ? 201 GG2 A C11 1 
HETATM 907 C C12 . GG2 B 2 .   ? 7.61638  22.42094 -1.32487  1.000 45.92325  ? 201 GG2 A C12 1 
HETATM 908 C C13 . GG2 B 2 .   ? 8.20357  23.47371 -2.05717  1.000 46.95304  ? 201 GG2 A C13 1 
HETATM 909 C C14 . GG2 B 2 .   ? 10.04949 20.14462 -6.88379  1.000 42.84793  ? 201 GG2 A C14 1 
HETATM 910 C C15 . GG2 B 2 .   ? 8.41936  30.21974 -4.52699  1.000 46.08801  ? 201 GG2 A C15 1 
HETATM 911 C C16 . GG2 B 2 .   ? 11.42584 20.26619 -6.83249  1.000 37.24933  ? 201 GG2 A C16 1 
HETATM 912 C C19 . GG2 B 2 .   ? 13.16796 18.69197 -7.73367  1.000 40.65380  ? 201 GG2 A C19 1 
HETATM 913 C C20 . GG2 B 2 .   ? 12.10727 20.34532 -9.25656  1.000 39.65143  ? 201 GG2 A C20 1 
HETATM 914 C C21 . GG2 B 2 .   ? 12.10227 19.22658 -10.29401 1.000 42.16084  ? 201 GG2 A C21 1 
HETATM 915 C C22 . GG2 B 2 .   ? 11.25041 21.31814 -4.68002  1.000 34.52755  ? 201 GG2 A C22 1 
HETATM 916 C C24 . GG2 B 2 .   ? 8.07534  20.68584 -3.03936  1.000 49.71535  ? 201 GG2 A C24 1 
HETATM 917 C C4  . GG2 B 2 .   ? 8.15543  25.98309 -2.04250  1.000 44.81265  ? 201 GG2 A C4  1 
HETATM 918 C C5  . GG2 B 2 .   ? 7.88354  26.32447 -3.35668  1.000 42.36168  ? 201 GG2 A C5  1 
HETATM 919 C C6  . GG2 B 2 .   ? 8.23724  27.57507 -3.83420  1.000 48.07934  ? 201 GG2 A C6  1 
HETATM 920 N N1  . GG2 B 2 .   ? 7.77136  24.67616 -1.54542  1.000 47.98712  ? 201 GG2 A N1  1 
HETATM 921 N N5  . GG2 B 2 .   ? 9.03344  21.67064 -3.64802  1.000 48.82229  ? 201 GG2 A N5  1 
HETATM 922 C C44 . GG2 B 2 .   ? 9.27474  20.60793 -5.83523  1.000 42.78777  ? 201 GG2 A C44 1 
HETATM 923 N N2  . GG2 B 2 .   ? 12.23087 19.77403 -7.93439  1.000 44.88860  ? 201 GG2 A N2  1 
HETATM 924 C C18 . GG2 B 2 .   ? 12.02704 20.85420 -5.72989  1.000 40.57204  ? 201 GG2 A C18 1 
HETATM 925 O O3  . GG2 B 2 .   ? 10.03762 23.95300 -3.68795  1.000 43.37880  ? 201 GG2 A O3  1 
HETATM 926 C C25 . GG2 B 2 .   ? 13.22527 18.18991 -10.22296 1.000 41.08082  ? 201 GG2 A C25 1 
HETATM 927 O O2  . GG2 B 2 .   ? 13.28323 18.19930 -6.66605  1.000 36.17054  ? 201 GG2 A O2  1 
HETATM 928 C C23 . GG2 B 2 .   ? 14.00039 18.18944 -8.90806  1.000 32.33990  ? 201 GG2 A C23 1 
HETATM 929 O O1  . GG2 B 2 .   ? 5.40266  21.63527 0.57130   1.000 44.78434  ? 201 GG2 A O1  1 
HETATM 930 N N3  . GG2 B 2 .   ? 5.69232  23.44202 1.94442   1.000 63.27837  ? 201 GG2 A N3  1 
HETATM 931 C C17 . GG2 B 2 .   ? 7.78408  20.93283 -1.51718  1.000 35.47582  ? 201 GG2 A C17 1 
HETATM 932 O O   . HOH C 3 .   ? 4.82669  22.96414 -5.56751  1.000 41.55741  ? 301 HOH A O   1 
HETATM 933 O O   . HOH C 3 .   ? 12.45804 31.68618 -14.30618 1.000 66.30940  ? 302 HOH A O   1 
HETATM 934 O O   . HOH C 3 .   ? 1.95701  19.30792 -6.59351  1.000 54.69799  ? 303 HOH A O   1 
HETATM 935 O O   . HOH C 3 .   ? 0.67514  28.59854 -3.42964  1.000 50.42367  ? 304 HOH A O   1 
HETATM 936 O O   . HOH C 3 .   ? 15.56446 15.01615 9.08466   1.000 39.77223  ? 305 HOH A O   1 
HETATM 937 O O   . HOH C 3 .   ? 23.73604 -3.04985 -13.33457 1.000 65.44474  ? 306 HOH A O   1 
HETATM 938 O O   . HOH C 3 .   ? 9.74826  6.86506  -17.51565 1.000 53.95337  ? 307 HOH A O   1 
HETATM 939 O O   . HOH C 3 .   ? -0.55592 11.07071 6.72658   1.000 69.95220  ? 308 HOH A O   1 
HETATM 940 O O   . HOH C 3 .   ? 18.56566 18.94313 -0.39398  1.000 40.87228  ? 309 HOH A O   1 
HETATM 941 O O   . HOH C 3 .   ? 24.07621 20.25688 -14.62543 1.000 46.32531  ? 310 HOH A O   1 
HETATM 942 O O   . HOH C 3 .   ? 11.58815 26.52341 7.93308   1.000 65.96232  ? 311 HOH A O   1 
HETATM 943 O O   . HOH C 3 .   ? 8.53268  39.58379 -6.58172  1.000 56.51082  ? 312 HOH A O   1 
HETATM 944 O O   . HOH C 3 .   ? 24.19197 16.44464 -15.61345 1.000 47.13472  ? 313 HOH A O   1 
HETATM 945 O O   . HOH C 3 .   ? 9.29193  28.43361 -14.58257 1.000 51.95978  ? 314 HOH A O   1 
HETATM 946 O O   . HOH C 3 .   ? 5.32278  27.08829 2.28435   1.000 48.83641  ? 315 HOH A O   1 
HETATM 947 O O   . HOH C 3 .   ? -2.11041 25.12623 -3.91330  1.000 48.52632  ? 316 HOH A O   1 
HETATM 948 O O   . HOH C 3 .   ? 3.23151  30.27395 -3.20631  1.000 51.88595  ? 317 HOH A O   1 
HETATM 949 O O   . HOH C 3 .   ? -3.70150 23.37441 -4.53509  1.000 45.90500  ? 318 HOH A O   1 
HETATM 950 O O   . HOH C 3 .   ? 9.97848  8.86910  9.26975   1.000 56.54690  ? 319 HOH A O   1 
HETATM 951 O O   . HOH C 3 .   ? 5.79232  30.14233 -0.36104  1.000 68.14063  ? 320 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 4   ? 0.91418 0.66604 0.69624 -0.01032 0.08806  -0.04828 0   SER A N   
2   C CA  . SER A 4   ? 0.88050 0.64344 0.66917 -0.00380 0.08539  -0.03522 0   SER A CA  
3   C C   . SER A 4   ? 0.81093 0.60615 0.61117 -0.00208 0.07467  -0.03065 0   SER A C   
4   O O   . SER A 4   ? 0.91637 0.72626 0.73018 -0.00449 0.07008  -0.02488 0   SER A O   
5   C CB  . SER A 4   ? 0.92070 0.66887 0.69542 0.01064  0.09135  -0.02734 0   SER A CB  
6   O OG  . SER A 4   ? 1.04202 0.79052 0.80494 0.01883  0.09100  -0.02918 0   SER A OG  
7   N N   . SER A 5   ? 0.97154 0.77701 0.76601 0.00294  0.07149  -0.03284 1   SER A N   
8   C CA  . SER A 5   ? 0.71745 0.55241 0.52241 0.00509  0.06324  -0.02776 1   SER A CA  
9   C C   . SER A 5   ? 0.70887 0.55912 0.52438 -0.00556 0.05789  -0.03454 1   SER A C   
10  O O   . SER A 5   ? 0.81975 0.69101 0.64821 -0.00629 0.05228  -0.02832 1   SER A O   
11  C CB  . SER A 5   ? 0.86443 0.70648 0.65904 0.01509  0.06260  -0.02721 1   SER A CB  
12  O OG  . SER A 5   ? 0.86830 0.69576 0.64913 0.01351  0.06570  -0.03942 1   SER A OG  
13  N N   . ALA A 6   ? 0.69656 0.53697 0.50738 -0.01364 0.05979  -0.04792 2   ALA A N   
14  C CA  . ALA A 6   ? 0.79772 0.65407 0.61938 -0.02408 0.05474  -0.05622 2   ALA A CA  
15  C C   . ALA A 6   ? 0.69518 0.55226 0.53029 -0.03159 0.05470  -0.05154 2   ALA A C   
16  O O   . ALA A 6   ? 0.77310 0.65092 0.61973 -0.03663 0.04886  -0.05254 2   ALA A O   
17  C CB  . ALA A 6   ? 0.77553 0.61995 0.59178 -0.03233 0.05745  -0.07361 2   ALA A CB  
18  N N   . ARG A 7   ? 0.83712 0.67269 0.66986 -0.03092 0.06132  -0.04620 3   ARG A N   
19  C CA  . ARG A 7   ? 0.84039 0.67661 0.68443 -0.03605 0.06163  -0.04122 3   ARG A CA  
20  C C   . ARG A 7   ? 0.73146 0.58958 0.58585 -0.03050 0.05449  -0.03035 3   ARG A C   
21  O O   . ARG A 7   ? 0.79887 0.66912 0.66534 -0.03577 0.05086  -0.02887 3   ARG A O   
22  C CB  . ARG A 7   ? 0.90160 0.71058 0.73817 -0.03329 0.07098  -0.03722 3   ARG A CB  
23  C CG  . ARG A 7   ? 0.81080 0.59461 0.64043 -0.04084 0.08030  -0.04722 3   ARG A CG  
24  C CD  . ARG A 7   ? 1.00130 0.75731 0.82131 -0.03499 0.09116  -0.04073 3   ARG A CD  
25  N NE  . ARG A 7   ? 1.16938 0.92825 0.99817 -0.03597 0.09205  -0.03335 3   ARG A NE  
26  C CZ  . ARG A 7   ? 1.15665 0.90846 0.97990 -0.02480 0.09526  -0.02309 3   ARG A CZ  
27  N NH1 . ARG A 7   ? 1.15610 0.89812 0.96563 -0.01193 0.09806  -0.01860 3   ARG A NH1 
28  N NH2 . ARG A 7   ? 1.06342 0.81993 0.89481 -0.02555 0.09540  -0.01778 3   ARG A NH2 
29  N N   . ILE A 8   ? 0.72788 0.59112 0.57866 -0.01997 0.05296  -0.02290 4   ILE A N   
30  C CA  . ILE A 8   ? 0.68834 0.57178 0.55123 -0.01543 0.04712  -0.01331 4   ILE A CA  
31  C C   . ILE A 8   ? 0.83318 0.73914 0.70355 -0.01891 0.04125  -0.01512 4   ILE A C   
32  O O   . ILE A 8   ? 0.70277 0.62239 0.58566 -0.02093 0.03721  -0.01066 4   ILE A O   
33  C CB  . ILE A 8   ? 0.76142 0.64643 0.62059 -0.00428 0.04787  -0.00592 4   ILE A CB  
34  C CG1 . ILE A 8   ? 0.66055 0.52934 0.51539 0.00115  0.05222  -0.00266 4   ILE A CG1 
35  C CG2 . ILE A 8   ? 0.74520 0.65252 0.61864 -0.00091 0.04282  0.00274  4   ILE A CG2 
36  C CD1 . ILE A 8   ? 0.87308 0.74960 0.73050 0.01154  0.05151  0.00487  4   ILE A CD1 
37  N N   . ALA A 9   ? 0.67145 0.58211 0.53332 -0.01835 0.04076  -0.02204 5   ALA A N   
38  C CA  . ALA A 9   ? 0.64790 0.58210 0.51447 -0.01934 0.03529  -0.02456 5   ALA A CA  
39  C C   . ALA A 9   ? 0.59759 0.53641 0.47163 -0.03019 0.03314  -0.03273 5   ALA A C   
40  O O   . ALA A 9   ? 0.69739 0.65629 0.58061 -0.03057 0.02839  -0.02998 5   ALA A O   
41  C CB  . ALA A 9   ? 0.64194 0.58109 0.49620 -0.01472 0.03498  -0.03183 5   ALA A CB  
42  N N   . LYS A 10  ? 0.75012 0.67056 0.62078 -0.03871 0.03741  -0.04240 6   LYS A N   
43  C CA  . LYS A 10  ? 0.74309 0.66755 0.62307 -0.04989 0.03662  -0.04977 6   LYS A CA  
44  C C   . LYS A 10  ? 0.64986 0.57928 0.54106 -0.05001 0.03502  -0.03954 6   LYS A C   
45  O O   . LYS A 10  ? 0.70209 0.64886 0.60290 -0.05438 0.03083  -0.04115 6   LYS A O   
46  C CB  . LYS A 10  ? 0.76073 0.66038 0.63665 -0.05879 0.04411  -0.05961 6   LYS A CB  
47  C CG  . LYS A 10  ? 0.88939 0.79534 0.76712 -0.06846 0.04320  -0.07688 6   LYS A CG  
48  C CD  . LYS A 10  ? 0.86939 0.78478 0.73708 -0.06178 0.03950  -0.08353 6   LYS A CD  
49  C CE  . LYS A 10  ? 0.88996 0.79891 0.75622 -0.07111 0.04151  -0.10318 6   LYS A CE  
50  N NZ  . LYS A 10  ? 0.86496 0.79432 0.74552 -0.08230 0.03733  -0.11496 6   LYS A NZ  
51  N N   . ALA A 11  ? 0.62097 0.53675 0.51097 -0.04432 0.03795  -0.02973 7   ALA A N   
52  C CA  . ALA A 11  ? 0.66875 0.58894 0.56922 -0.04336 0.03598  -0.02136 7   ALA A CA  
53  C C   . ALA A 11  ? 0.70809 0.65175 0.61769 -0.03908 0.02937  -0.01499 7   ALA A C   
54  O O   . ALA A 11  ? 0.68509 0.63961 0.60439 -0.04183 0.02621  -0.01330 7   ALA A O   
55  C CB  . ALA A 11  ? 0.68985 0.59401 0.58696 -0.03627 0.03953  -0.01391 7   ALA A CB  
56  N N   . LYS A 12  ? 0.55751 0.50881 0.46389 -0.03160 0.02811  -0.01070 8   LYS A N   
57  C CA  . LYS A 12  ? 0.63581 0.60741 0.55056 -0.02634 0.02395  -0.00292 8   LYS A CA  
58  C C   . LYS A 12  ? 0.57114 0.56161 0.48795 -0.02993 0.02007  -0.00865 8   LYS A C   
59  O O   . LYS A 12  ? 0.61229 0.61634 0.53823 -0.02838 0.01704  -0.00318 8   LYS A O   
60  C CB  . LYS A 12  ? 0.69783 0.67389 0.60794 -0.01734 0.02515  0.00298  8   LYS A CB  
61  C CG  . LYS A 12  ? 0.66689 0.65136 0.58889 -0.01076 0.02475  0.01578  8   LYS A CG  
62  C CD  . LYS A 12  ? 0.79242 0.79055 0.71152 -0.00219 0.02591  0.02200  8   LYS A CD  
63  C CE  . LYS A 12  ? 0.82273 0.82942 0.75649 0.00317  0.02700  0.03517  8   LYS A CE  
64  N NZ  . LYS A 12  ? 0.81336 0.83198 0.74459 0.01269  0.03031  0.04351  8   LYS A NZ  
65  N N   . LYS A 13  ? 0.68672 0.67895 0.59550 -0.03430 0.02007  -0.02055 9   LYS A N   
66  C CA  . LYS A 13  ? 0.49899 0.51233 0.41041 -0.03770 0.01575  -0.02859 9   LYS A CA  
67  C C   . LYS A 13  ? 0.63450 0.64784 0.55557 -0.04675 0.01510  -0.03172 9   LYS A C   
68  O O   . LYS A 13  ? 0.44744 0.48097 0.37514 -0.04631 0.01095  -0.03129 9   LYS A O   
69  C CB  . LYS A 13  ? 0.59952 0.61482 0.50183 -0.04093 0.01561  -0.04330 9   LYS A CB  
70  C CG  . LYS A 13  ? 0.68159 0.71834 0.58849 -0.04700 0.01109  -0.05609 9   LYS A CG  
71  C CD  . LYS A 13  ? 0.79645 0.84380 0.69453 -0.04546 0.00885  -0.06995 9   LYS A CD  
72  C CE  . LYS A 13  ? 1.07634 1.09690 0.96673 -0.05073 0.01421  -0.07802 9   LYS A CE  
73  N NZ  . LYS A 13  ? 0.82597 0.85052 0.70324 -0.04073 0.01327  -0.08051 9   LYS A NZ  
74  N N   . LEU A 14  ? 0.58718 0.57859 0.50841 -0.05374 0.01979  -0.03420 10  LEU A N   
75  C CA  . LEU A 14  ? 0.53898 0.53001 0.46897 -0.06183 0.02042  -0.03661 10  LEU A CA  
76  C C   . LEU A 14  ? 0.52881 0.52654 0.46706 -0.05657 0.01756  -0.02506 10  LEU A C   
77  O O   . LEU A 14  ? 0.59683 0.60451 0.54292 -0.06059 0.01577  -0.02623 10  LEU A O   
78  C CB  . LEU A 14  ? 0.49025 0.45479 0.41713 -0.06821 0.02787  -0.03978 10  LEU A CB  
79  C CG  . LEU A 14  ? 0.61177 0.56664 0.53333 -0.07629 0.03215  -0.05329 10  LEU A CG  
80  C CD1 . LEU A 14  ? 0.65083 0.57435 0.56480 -0.07706 0.04114  -0.05173 10  LEU A CD1 
81  C CD2 . LEU A 14  ? 0.67698 0.64533 0.60827 -0.08793 0.03142  -0.06545 10  LEU A CD2 
82  N N   . ILE A 15  ? 0.51102 0.50392 0.44869 -0.04776 0.01727  -0.01459 11  ILE A N   
83  C CA  . ILE A 15  ? 0.42538 0.42404 0.37245 -0.04278 0.01454  -0.00491 11  ILE A CA  
84  C C   . ILE A 15  ? 0.52011 0.54247 0.47163 -0.03926 0.01010  -0.00267 11  ILE A C   
85  O O   . ILE A 15  ? 0.50362 0.53510 0.46254 -0.03964 0.00760  -0.00070 11  ILE A O   
86  C CB  . ILE A 15  ? 0.50060 0.48888 0.44867 -0.03526 0.01580  0.00399  11  ILE A CB  
87  C CG1 . ILE A 15  ? 0.61394 0.58083 0.55687 -0.03652 0.01997  0.00211  11  ILE A CG1 
88  C CG2 . ILE A 15  ? 0.45936 0.45405 0.41933 -0.03059 0.01296  0.01238  11  ILE A CG2 
89  C CD1 . ILE A 15  ? 0.51803 0.47764 0.46204 -0.04221 0.02166  -0.00180 11  ILE A CD1 
90  N N   . TYR A 16  ? 0.50948 0.54278 0.45541 -0.03424 0.00939  -0.00253 12  TYR A N   
91  C CA  . TYR A 16  ? 0.53392 0.59109 0.48165 -0.02841 0.00596  0.00012  12  TYR A CA  
92  C C   . TYR A 16  ? 0.43539 0.50876 0.38379 -0.03489 0.00275  -0.01122 12  TYR A C   
93  O O   . TYR A 16  ? 0.50083 0.59314 0.45345 -0.03106 -0.00040 -0.00879 12  TYR A O   
94  C CB  . TYR A 16  ? 0.48562 0.55164 0.42551 -0.01970 0.00670  0.00309  12  TYR A CB  
95  C CG  . TYR A 16  ? 0.50534 0.56259 0.44870 -0.01179 0.01011  0.01682  12  TYR A CG  
96  C CD1 . TYR A 16  ? 0.39439 0.45770 0.34694 -0.00525 0.01056  0.02857  12  TYR A CD1 
97  C CD2 . TYR A 16  ? 0.53849 0.58136 0.47710 -0.01099 0.01344  0.01771  12  TYR A CD2 
98  C CE1 . TYR A 16  ? 0.47512 0.53033 0.43425 0.00050  0.01457  0.04024  12  TYR A CE1 
99  C CE2 . TYR A 16  ? 0.47740 0.51456 0.42182 -0.00459 0.01682  0.02946  12  TYR A CE2 
100 C CZ  . TYR A 16  ? 0.48631 0.52964 0.44211 0.00044  0.01753  0.04038  12  TYR A CZ  
101 O OH  . TYR A 16  ? 0.49525 0.53284 0.46009 0.00540  0.02175  0.05122  12  TYR A OH  
102 N N   . LYS A 17  ? 0.38989 0.45638 0.33507 -0.04457 0.00403  -0.02382 13  LYS A N   
103 C CA  . LYS A 17  ? 0.52931 0.61001 0.47920 -0.05320 0.00188  -0.03569 13  LYS A CA  
104 C C   . LYS A 17  ? 0.46295 0.54111 0.42220 -0.05690 0.00214  -0.03141 13  LYS A C   
105 O O   . LYS A 17  ? 0.50548 0.60449 0.47051 -0.05713 -0.00135 -0.03359 13  LYS A O   
106 C CB  . LYS A 17  ? 0.59273 0.66184 0.53965 -0.06400 0.00506  -0.04984 13  LYS A CB  
107 C CG  . LYS A 17  ? 0.51290 0.59569 0.46825 -0.07527 0.00407  -0.06356 13  LYS A CG  
108 C CD  . LYS A 17  ? 0.79337 0.86986 0.74655 -0.08473 0.00657  -0.07987 13  LYS A CD  
109 C CE  . LYS A 17  ? 0.93667 1.04511 0.89423 -0.08734 0.00058  -0.09537 13  LYS A CE  
110 N NZ  . LYS A 17  ? 0.98169 1.08919 0.93243 -0.08896 0.00019  -0.10941 13  LYS A NZ  
111 N N   . LEU A 18  ? 0.56258 0.61685 0.52273 -0.05838 0.00611  -0.02538 14  LEU A N   
112 C CA  . LEU A 18  ? 0.52468 0.57607 0.49242 -0.05995 0.00638  -0.02101 14  LEU A CA  
113 C C   . LEU A 18  ? 0.51130 0.57842 0.48399 -0.05105 0.00181  -0.01214 14  LEU A C   
114 O O   . LEU A 18  ? 0.57449 0.65191 0.55339 -0.05211 0.00001  -0.01205 14  LEU A O   
115 C CB  . LEU A 18  ? 0.52816 0.55337 0.49410 -0.05929 0.01078  -0.01557 14  LEU A CB  
116 C CG  . LEU A 18  ? 0.57498 0.58355 0.53937 -0.06808 0.01704  -0.02169 14  LEU A CG  
117 C CD1 . LEU A 18  ? 0.71059 0.69705 0.67166 -0.06321 0.02071  -0.01468 14  LEU A CD1 
118 C CD2 . LEU A 18  ? 0.49080 0.51120 0.46333 -0.07500 0.01731  -0.02602 14  LEU A CD2 
119 N N   . GLU A 19  ? 0.45493 0.52348 0.42520 -0.04182 0.00078  -0.00412 15  GLU A N   
120 C CA  . GLU A 19  ? 0.49345 0.57424 0.46856 -0.03268 -0.00186 0.00524  15  GLU A CA  
121 C C   . GLU A 19  ? 0.62536 0.73338 0.60037 -0.03115 -0.00543 0.00084  15  GLU A C   
122 O O   . GLU A 19  ? 0.52669 0.64482 0.50679 -0.02730 -0.00750 0.00496  15  GLU A O   
123 C CB  . GLU A 19  ? 0.62101 0.69790 0.59435 -0.02362 -0.00025 0.01482  15  GLU A CB  
124 C CG  . GLU A 19  ? 0.68352 0.76603 0.66358 -0.01416 -0.00063 0.02633  15  GLU A CG  
125 C CD  . GLU A 19  ? 0.83306 0.92111 0.81034 -0.00449 0.00202  0.03514  15  GLU A CD  
126 O OE1 . GLU A 19  ? 1.01946 1.12328 0.98794 -0.00154 0.00139  0.03153  15  GLU A OE1 
127 O OE2 . GLU A 19  ? 0.86166 0.93901 0.84625 0.00044  0.00508  0.04531  15  GLU A OE2 
128 N N   . LYS A 20  ? 0.65101 0.77245 0.62018 -0.03333 -0.00649 -0.00845 16  LYS A N   
129 C CA  . LYS A 20  ? 0.67992 0.83123 0.64930 -0.03142 -0.01064 -0.01503 16  LYS A CA  
130 C C   . LYS A 20  ? 0.58011 0.73762 0.55731 -0.04174 -0.01166 -0.02376 16  LYS A C   
131 O O   . LYS A 20  ? 0.65281 0.83104 0.63394 -0.03807 -0.01477 -0.02320 16  LYS A O   
132 C CB  . LYS A 20  ? 0.48583 0.65114 0.44764 -0.03101 -0.01217 -0.02524 16  LYS A CB  
133 C CG  . LYS A 20  ? 0.71441 0.91210 0.67205 -0.01910 -0.01630 -0.02509 16  LYS A CG  
134 C CD  . LYS A 20  ? 0.70632 0.91511 0.65421 -0.01462 -0.01751 -0.03249 16  LYS A CD  
135 C CE  . LYS A 20  ? 0.60413 0.83078 0.55429 -0.02482 -0.02151 -0.05370 16  LYS A CE  
136 N NZ  . LYS A 20  ? 0.66676 0.90648 0.60697 -0.01912 -0.02370 -0.06283 16  LYS A NZ  
137 N N   . LEU A 21  ? 0.55997 0.69967 0.53947 -0.05390 -0.00816 -0.03101 17  LEU A N   
138 C CA  . LEU A 21  ? 0.58364 0.72783 0.57173 -0.06410 -0.00719 -0.03820 17  LEU A CA  
139 C C   . LEU A 21  ? 0.60217 0.74254 0.59504 -0.05960 -0.00732 -0.02781 17  LEU A C   
140 O O   . LEU A 21  ? 0.60114 0.75891 0.60057 -0.06151 -0.00900 -0.03055 17  LEU A O   
141 C CB  . LEU A 21  ? 0.65511 0.77673 0.64392 -0.07653 -0.00114 -0.04566 17  LEU A CB  
142 C CG  . LEU A 21  ? 0.60972 0.72675 0.59281 -0.08103 0.00010  -0.05582 17  LEU A CG  
143 C CD1 . LEU A 21  ? 0.45330 0.54037 0.43547 -0.09047 0.00787  -0.05872 17  LEU A CD1 
144 C CD2 . LEU A 21  ? 0.62715 0.77330 0.61503 -0.08630 -0.00386 -0.07129 17  LEU A CD2 
145 N N   . TRP A 22  ? 0.53105 0.64999 0.52140 -0.05342 -0.00578 -0.01680 18  TRP A N   
146 C CA  . TRP A 22  ? 0.62937 0.74428 0.62429 -0.04804 -0.00658 -0.00821 18  TRP A CA  
147 C C   . TRP A 22  ? 0.63671 0.77430 0.63332 -0.03858 -0.01102 -0.00353 18  TRP A C   
148 O O   . TRP A 22  ? 0.59077 0.73976 0.59211 -0.03779 -0.01261 -0.00337 18  TRP A O   
149 C CB  . TRP A 22  ? 0.59240 0.68286 0.58576 -0.04277 -0.00490 0.00049  18  TRP A CB  
150 C CG  . TRP A 22  ? 0.51359 0.58245 0.50623 -0.04846 -0.00068 -0.00139 18  TRP A CG  
151 C CD1 . TRP A 22  ? 0.52482 0.57545 0.51198 -0.05150 0.00310  -0.00315 18  TRP A CD1 
152 C CD2 . TRP A 22  ? 0.66353 0.72730 0.65968 -0.04973 0.00079  -0.00084 18  TRP A CD2 
153 N NE1 . TRP A 22  ? 0.56909 0.60339 0.55565 -0.05406 0.00718  -0.00339 18  TRP A NE1 
154 C CE2 . TRP A 22  ? 0.62657 0.66884 0.61858 -0.05288 0.00593  -0.00185 18  TRP A CE2 
155 C CE3 . TRP A 22  ? 0.58198 0.65786 0.58342 -0.04719 -0.00141 0.00084  18  TRP A CE3 
156 C CZ2 . TRP A 22  ? 0.66118 0.69424 0.65379 -0.05287 0.00930  -0.00075 18  TRP A CZ2 
157 C CZ3 . TRP A 22  ? 0.70720 0.77408 0.70980 -0.04790 0.00153  0.00146  18  TRP A CZ3 
158 C CH2 . TRP A 22  ? 0.66438 0.71024 0.66242 -0.05038 0.00700  0.00092  18  TRP A CH2 
159 N N   . ASN A 23  ? 0.65650 0.80097 0.64853 -0.03009 -0.01232 0.00112  19  ASN A N   
160 C CA  . ASN A 23  ? 0.59901 0.76429 0.59074 -0.01890 -0.01516 0.00693  19  ASN A CA  
161 C C   . ASN A 23  ? 0.54816 0.74435 0.54029 -0.02102 -0.01855 -0.00293 19  ASN A C   
162 O O   . ASN A 23  ? 0.58576 0.80091 0.57854 -0.01243 -0.02102 0.00078  19  ASN A O   
163 C CB  . ASN A 23  ? 0.42105 0.58598 0.40711 -0.00850 -0.01392 0.01518  19  ASN A CB  
164 C CG  . ASN A 23  ? 0.52629 0.66601 0.51591 -0.00420 -0.01074 0.02652  19  ASN A CG  
165 O OD1 . ASN A 23  ? 0.65345 0.77801 0.64917 -0.00737 -0.01064 0.02769  19  ASN A OD1 
166 N ND2 . ASN A 23  ? 0.58889 0.72545 0.57552 0.00345  -0.00795 0.03441  19  ASN A ND2 
167 N N   . ALA A 24  ? 0.51253 0.71461 0.50504 -0.03205 -0.01854 -0.01603 20  ALA A N   
168 C CA  . ALA A 24  ? 0.67594 0.90841 0.67243 -0.03665 -0.02180 -0.02844 20  ALA A CA  
169 C C   . ALA A 24  ? 0.78596 1.01774 0.79239 -0.04799 -0.02016 -0.03402 20  ALA A C   
170 O O   . ALA A 24  ? 0.75639 1.01505 0.76926 -0.05253 -0.02249 -0.04412 20  ALA A O   
171 C CB  . ALA A 24  ? 0.59750 0.83866 0.59133 -0.04303 -0.02259 -0.04189 20  ALA A CB  
172 N N   . ARG A 25  ? 0.65451 0.85804 0.66263 -0.05190 -0.01597 -0.02785 21  ARG A N   
173 C CA  . ARG A 25  ? 0.79197 0.99192 0.80827 -0.06118 -0.01275 -0.03105 21  ARG A CA  
174 C C   . ARG A 25  ? 0.82372 1.02903 0.84663 -0.07657 -0.00949 -0.04558 21  ARG A C   
175 O O   . ARG A 25  ? 0.79800 1.01285 0.83061 -0.08481 -0.00699 -0.05081 21  ARG A O   
176 C CB  . ARG A 25  ? 0.74605 0.96811 0.76702 -0.05489 -0.01591 -0.02783 21  ARG A CB  
177 C CG  . ARG A 25  ? 0.63103 0.84390 0.64727 -0.04057 -0.01797 -0.01403 21  ARG A CG  
178 C CD  . ARG A 25  ? 0.75602 0.98529 0.77669 -0.03535 -0.01989 -0.01119 21  ARG A CD  
179 N NE  . ARG A 25  ? 0.74902 0.96281 0.77400 -0.04059 -0.01617 -0.00986 21  ARG A NE  
180 C CZ  . ARG A 25  ? 0.68773 0.88008 0.71038 -0.03375 -0.01565 -0.00123 21  ARG A CZ  
181 N NH1 . ARG A 25  ? 0.70892 0.89085 0.72728 -0.02316 -0.01813 0.00663  21  ARG A NH1 
182 N NH2 . ARG A 25  ? 0.74594 0.92762 0.77134 -0.03729 -0.01212 -0.00084 21  ARG A NH2 
183 N N   . ASP A 26  ? 0.73367 0.93249 0.75229 -0.08066 -0.00888 -0.05239 22  ASP A N   
184 C CA  . ASP A 26  ? 0.83286 1.03053 0.85808 -0.09593 -0.00477 -0.06694 22  ASP A CA  
185 C C   . ASP A 26  ? 0.88986 1.05520 0.91656 -0.10354 0.00404  -0.06269 22  ASP A C   
186 O O   . ASP A 26  ? 0.92086 1.06003 0.94113 -0.10589 0.00843  -0.06206 22  ASP A O   
187 C CB  . ASP A 26  ? 0.89912 1.09632 0.91742 -0.09604 -0.00668 -0.07486 22  ASP A CB  
188 C CG  . ASP A 26  ? 1.06494 1.26373 1.09156 -0.11190 -0.00317 -0.09271 22  ASP A CG  
189 O OD1 . ASP A 26  ? 1.13662 1.32304 1.17276 -0.12395 0.00403  -0.09573 22  ASP A OD1 
190 O OD2 . ASP A 26  ? 1.04811 1.25952 1.07177 -0.11184 -0.00700 -0.10380 22  ASP A OD2 
191 N N   . ASN A 27  ? 0.81843 0.98668 0.85282 -0.10595 0.00704  -0.05921 23  ASN A N   
192 C CA  . ASN A 27  ? 0.77909 0.91895 0.81370 -0.11038 0.01606  -0.05364 23  ASN A CA  
193 C C   . ASN A 27  ? 0.95000 1.07734 0.99049 -0.12555 0.02469  -0.06439 23  ASN A C   
194 O O   . ASN A 27  ? 1.04063 1.13770 1.07599 -0.12724 0.03279  -0.05979 23  ASN A O   
195 C CB  . ASN A 27  ? 0.74194 0.89086 0.78320 -0.10825 0.01757  -0.04753 23  ASN A CB  
196 C CG  . ASN A 27  ? 0.78842 0.94930 0.82478 -0.09338 0.00933  -0.03810 23  ASN A CG  
197 O OD1 . ASN A 27  ? 0.91324 1.09839 0.95573 -0.09090 0.00610  -0.03826 23  ASN A OD1 
198 N ND2 . ASN A 27  ? 0.79772 0.94145 0.82381 -0.08340 0.00644  -0.03001 23  ASN A ND2 
199 N N   . ASP A 28  ? 1.05127 1.20164 1.10278 -0.13609 0.02336  -0.07924 24  ASP A N   
200 C CA  . ASP A 28  ? 1.14463 1.28266 1.20400 -0.15167 0.03179  -0.09154 24  ASP A CA  
201 C C   . ASP A 28  ? 1.07541 1.19016 1.12235 -0.14997 0.03226  -0.09343 24  ASP A C   
202 O O   . ASP A 28  ? 1.08198 1.16674 1.12688 -0.15621 0.04211  -0.09339 24  ASP A O   
203 C CB  . ASP A 28  ? 1.13834 1.31038 1.21420 -0.16302 0.02859  -0.10957 24  ASP A CB  
204 C CG  . ASP A 28  ? 1.32879 1.52169 1.41991 -0.16791 0.03107  -0.10913 24  ASP A CG  
205 O OD1 . ASP A 28  ? 1.41883 1.59468 1.50832 -0.16488 0.03782  -0.09578 24  ASP A OD1 
206 O OD2 . ASP A 28  ? 1.34829 1.57646 1.45286 -0.17387 0.02613  -0.12248 24  ASP A OD2 
207 N N   . GLY A 29  ? 0.81185 0.94005 0.84973 -0.14043 0.02246  -0.09431 25  GLY A N   
208 C CA  . GLY A 29  ? 0.78090 0.88925 0.80635 -0.13720 0.02259  -0.09514 25  GLY A CA  
209 C C   . GLY A 29  ? 0.80708 0.88249 0.82053 -0.12907 0.02738  -0.07963 25  GLY A C   
210 O O   . GLY A 29  ? 0.75301 0.80168 0.75992 -0.13178 0.03383  -0.08054 25  GLY A O   
211 N N   . ILE A 30  ? 0.87904 0.95692 0.88973 -0.11845 0.02415  -0.06608 26  ILE A N   
212 C CA  . ILE A 30  ? 0.65699 0.70791 0.65802 -0.10984 0.02746  -0.05280 26  ILE A CA  
213 C C   . ILE A 30  ? 0.81110 0.83536 0.81233 -0.11685 0.03910  -0.05237 26  ILE A C   
214 O O   . ILE A 30  ? 0.87378 0.87229 0.86491 -0.11285 0.04376  -0.04761 26  ILE A O   
215 C CB  . ILE A 30  ? 0.76946 0.82952 0.77123 -0.09918 0.02245  -0.04129 26  ILE A CB  
216 C CG1 . ILE A 30  ? 0.66849 0.74755 0.66749 -0.08968 0.01302  -0.03862 26  ILE A CG1 
217 C CG2 . ILE A 30  ? 0.68594 0.72050 0.68065 -0.09152 0.02623  -0.03034 26  ILE A CG2 
218 C CD1 . ILE A 30  ? 0.65623 0.74916 0.65877 -0.08098 0.00810  -0.03029 26  ILE A CD1 
219 N N   . LEU A 31  ? 0.85825 0.88881 0.87108 -0.12675 0.04481  -0.05688 27  LEU A N   
220 C CA  . LEU A 31  ? 0.75342 0.75828 0.76715 -0.13294 0.05806  -0.05504 27  LEU A CA  
221 C C   . LEU A 31  ? 0.83544 0.82019 0.84632 -0.14140 0.06487  -0.06417 27  LEU A C   
222 O O   . LEU A 31  ? 0.84786 0.80282 0.85156 -0.14041 0.07532  -0.05893 27  LEU A O   
223 C CB  . LEU A 31  ? 0.83370 0.85210 0.86298 -0.14262 0.06362  -0.05806 27  LEU A CB  
224 C CG  . LEU A 31  ? 0.95509 0.97728 0.98455 -0.13387 0.06436  -0.04555 27  LEU A CG  
225 C CD1 . LEU A 31  ? 0.86760 0.90042 0.91305 -0.14501 0.07270  -0.04893 27  LEU A CD1 
226 C CD2 . LEU A 31  ? 0.79471 0.78750 0.81022 -0.12267 0.07031  -0.03306 27  LEU A CD2 
227 N N   . LYS A 32  ? 0.81013 0.81089 0.82563 -0.14841 0.05922  -0.07803 28  LYS A N   
228 C CA  . LYS A 32  ? 0.87172 0.85436 0.88608 -0.15740 0.06562  -0.08920 28  LYS A CA  
229 C C   . LYS A 32  ? 0.81885 0.77545 0.81485 -0.14700 0.06664  -0.08201 28  LYS A C   
230 O O   . LYS A 32  ? 0.80188 0.73234 0.79353 -0.15168 0.07591  -0.08601 28  LYS A O   
231 C CB  . LYS A 32  ? 0.79344 0.80330 0.81642 -0.16525 0.05758  -0.10714 28  LYS A CB  
232 C CG  . LYS A 32  ? 0.82884 0.84973 0.87246 -0.18289 0.06343  -0.12187 28  LYS A CG  
233 C CD  . LYS A 32  ? 0.93028 0.95951 0.97963 -0.19270 0.06077  -0.14301 28  LYS A CD  
234 C CE  . LYS A 32  ? 0.96919 1.04381 1.02728 -0.19257 0.04739  -0.15502 28  LYS A CE  
235 N NZ  . LYS A 32  ? 0.83638 0.92686 0.91413 -0.20978 0.04882  -0.17881 28  LYS A NZ  
236 N N   . LEU A 33  ? 0.79979 0.76282 0.78575 -0.13294 0.05790  -0.07161 29  LEU A N   
237 C CA  . LEU A 33  ? 0.74735 0.68733 0.71763 -0.12251 0.05939  -0.06358 29  LEU A CA  
238 C C   . LEU A 33  ? 0.76436 0.67981 0.72878 -0.11668 0.06843  -0.05146 29  LEU A C   
239 O O   . LEU A 33  ? 0.75811 0.65144 0.70988 -0.10922 0.07239  -0.04630 29  LEU A O   
240 C CB  . LEU A 33  ? 0.72688 0.68252 0.69111 -0.11018 0.04796  -0.05696 29  LEU A CB  
241 C CG  . LEU A 33  ? 0.85350 0.83912 0.82187 -0.11047 0.03781  -0.06443 29  LEU A CG  
242 C CD1 . LEU A 33  ? 0.90622 0.91677 0.88379 -0.10841 0.03169  -0.06046 29  LEU A CD1 
243 C CD2 . LEU A 33  ? 0.88514 0.87104 0.84271 -0.09939 0.03238  -0.05954 29  LEU A CD2 
244 N N   . PHE A 34  ? 0.78429 0.70489 0.75688 -0.11851 0.07174  -0.04682 30  PHE A N   
245 C CA  . PHE A 34  ? 0.80241 0.70290 0.76866 -0.11085 0.08026  -0.03518 30  PHE A CA  
246 C C   . PHE A 34  ? 0.80799 0.68192 0.77367 -0.11860 0.09606  -0.03731 30  PHE A C   
247 O O   . PHE A 34  ? 0.81855 0.69550 0.79639 -0.13324 0.10118  -0.04753 30  PHE A O   
248 C CB  . PHE A 34  ? 0.68020 0.59753 0.65461 -0.10820 0.07788  -0.02899 30  PHE A CB  
249 C CG  . PHE A 34  ? 0.66650 0.59609 0.63672 -0.09477 0.06672  -0.02120 30  PHE A CG  
250 C CD1 . PHE A 34  ? 0.63641 0.55181 0.59662 -0.08155 0.06829  -0.01149 30  PHE A CD1 
251 C CD2 . PHE A 34  ? 0.72939 0.68506 0.70627 -0.09482 0.05508  -0.02408 30  PHE A CD2 
252 C CE1 . PHE A 34  ? 0.71239 0.63894 0.67159 -0.07043 0.05817  -0.00627 30  PHE A CE1 
253 C CE2 . PHE A 34  ? 0.67940 0.64369 0.65414 -0.08318 0.04623  -0.01702 30  PHE A CE2 
254 C CZ  . PHE A 34  ? 0.75613 0.70563 0.72319 -0.07187 0.04763  -0.00883 30  PHE A CZ  
255 N N   . LYS A 35  ? 0.83290 0.68105 0.78504 -0.10836 0.10429  -0.02794 31  LYS A N   
256 C CA  . LYS A 35  ? 0.84844 0.66964 0.79930 -0.11263 0.12171  -0.02580 31  LYS A CA  
257 C C   . LYS A 35  ? 0.87441 0.70376 0.83685 -0.11643 0.12810  -0.02107 31  LYS A C   
258 O O   . LYS A 35  ? 0.94320 0.79190 0.90748 -0.10887 0.12007  -0.01500 31  LYS A O   
259 C CB  . LYS A 35  ? 0.80491 0.59971 0.73663 -0.09708 0.12881  -0.01510 31  LYS A CB  
260 C CG  . LYS A 35  ? 0.90759 0.68302 0.82846 -0.09694 0.13106  -0.02042 31  LYS A CG  
261 C CD  . LYS A 35  ? 1.01245 0.75829 0.91536 -0.08297 0.14296  -0.00995 31  LYS A CD  
262 C CE  . LYS A 35  ? 1.02661 0.74235 0.92494 -0.09011 0.15681  -0.01540 31  LYS A CE  
263 N NZ  . LYS A 35  ? 1.13962 0.86016 1.03807 -0.09699 0.14806  -0.02810 31  LYS A NZ  
264 N N   . ASP A 36  ? 0.92510 0.73925 0.89628 -0.12836 0.14330  -0.02406 32  ASP A N   
265 C CA  . ASP A 36  ? 1.02277 0.84623 1.00762 -0.13391 0.15077  -0.02022 32  ASP A CA  
266 C C   . ASP A 36  ? 0.87965 0.69673 0.85318 -0.11644 0.15565  -0.00346 32  ASP A C   
267 O O   . ASP A 36  ? 0.77399 0.60584 0.75657 -0.11664 0.15752  0.00130  32  ASP A O   
268 C CB  . ASP A 36  ? 1.06709 0.87207 1.06487 -0.15051 0.16846  -0.02632 32  ASP A CB  
269 C CG  . ASP A 36  ? 1.08076 0.89800 1.09357 -0.16890 0.16268  -0.04591 32  ASP A CG  
270 O OD1 . ASP A 36  ? 1.07576 0.90904 1.08347 -0.16616 0.14673  -0.05312 32  ASP A OD1 
271 O OD2 . ASP A 36  ? 1.06459 0.87625 1.09497 -0.18572 0.17442  -0.05445 32  ASP A OD2 
272 N N   . ASP A 37  ? 0.96031 0.75791 0.91414 -0.10039 0.15736  0.00495  33  ASP A N   
273 C CA  . ASP A 37  ? 0.85038 0.64403 0.79162 -0.08117 0.16054  0.01929  33  ASP A CA  
274 C C   . ASP A 37  ? 0.82899 0.63448 0.75863 -0.06578 0.14411  0.02104  33  ASP A C   
275 O O   . ASP A 37  ? 0.86924 0.66499 0.78371 -0.04798 0.14632  0.03002  33  ASP A O   
276 C CB  . ASP A 37  ? 0.95967 0.71918 0.88794 -0.07345 0.18037  0.02877  33  ASP A CB  
277 C CG  . ASP A 37  ? 1.05153 0.78695 0.97336 -0.07914 0.18540  0.02229  33  ASP A CG  
278 O OD1 . ASP A 37  ? 1.06624 0.80837 0.98186 -0.07631 0.17175  0.01629  33  ASP A OD1 
279 O OD2 . ASP A 37  ? 1.07410 0.78334 0.99745 -0.08623 0.20366  0.02334  33  ASP A OD2 
280 N N   . ALA A 38  ? 0.90535 0.73266 0.84273 -0.07201 0.12808  0.01232  34  ALA A N   
281 C CA  . ALA A 38  ? 0.85337 0.69140 0.78327 -0.05977 0.11346  0.01326  34  ALA A CA  
282 C C   . ALA A 38  ? 0.74015 0.59497 0.67080 -0.04762 0.10671  0.01976  34  ALA A C   
283 O O   . ALA A 38  ? 0.73808 0.60146 0.67623 -0.05000 0.11081  0.02255  34  ALA A O   
284 C CB  . ALA A 38  ? 0.73262 0.58783 0.67066 -0.06949 0.10040  0.00328  34  ALA A CB  
285 N N   . VAL A 39  ? 0.69416 0.55425 0.61782 -0.03446 0.09630  0.02144  35  VAL A N   
286 C CA  . VAL A 39  ? 0.71634 0.59160 0.64044 -0.02158 0.08837  0.02552  35  VAL A CA  
287 C C   . VAL A 39  ? 0.73676 0.63243 0.67012 -0.02387 0.07230  0.02016  35  VAL A C   
288 O O   . VAL A 39  ? 0.64460 0.53856 0.57614 -0.02382 0.06637  0.01700  35  VAL A O   
289 C CB  . VAL A 39  ? 0.77449 0.63923 0.68384 -0.00235 0.09059  0.03131  35  VAL A CB  
290 C CG1 . VAL A 39  ? 0.63491 0.51518 0.54509 0.01114  0.08419  0.03433  35  VAL A CG1 
291 C CG2 . VAL A 39  ? 0.65422 0.49445 0.55167 0.00083  0.10821  0.03751  35  VAL A CG2 
292 N N   . PHE A 40  ? 0.64739 0.56189 0.59050 -0.02518 0.06625  0.01989  36  PHE A N   
293 C CA  . PHE A 40  ? 0.60813 0.54110 0.55977 -0.02493 0.05230  0.01655  36  PHE A CA  
294 C C   . PHE A 40  ? 0.57355 0.51293 0.52375 -0.00958 0.04606  0.01944  36  PHE A C   
295 O O   . PHE A 40  ? 0.56068 0.50836 0.51294 -0.00549 0.04694  0.02196  36  PHE A O   
296 C CB  . PHE A 40  ? 0.55861 0.50907 0.52197 -0.03665 0.04964  0.01326  36  PHE A CB  
297 C CG  . PHE A 40  ? 0.65543 0.62169 0.62602 -0.03773 0.03758  0.01021  36  PHE A CG  
298 C CD1 . PHE A 40  ? 0.62163 0.59809 0.59581 -0.02795 0.02884  0.01216  36  PHE A CD1 
299 C CD2 . PHE A 40  ? 0.51013 0.48065 0.48376 -0.04760 0.03564  0.00539  36  PHE A CD2 
300 C CE1 . PHE A 40  ? 0.55362 0.54206 0.53468 -0.02841 0.01975  0.01071  36  PHE A CE1 
301 C CE2 . PHE A 40  ? 0.54958 0.53431 0.52867 -0.04671 0.02615  0.00435  36  PHE A CE2 
302 C CZ  . PHE A 40  ? 0.54660 0.53921 0.52961 -0.03730 0.01888  0.00770  36  PHE A CZ  
303 N N   . ASN A 41  ? 0.56675 0.50341 0.51420 -0.00094 0.03973  0.01824  37  ASN A N   
304 C CA  . ASN A 41  ? 0.68611 0.62986 0.63404 0.01355  0.03251  0.01810  37  ASN A CA  
305 C C   . ASN A 41  ? 0.58760 0.54698 0.54865 0.01103  0.02118  0.01494  37  ASN A C   
306 O O   . ASN A 41  ? 0.55057 0.51131 0.51740 0.00862  0.01523  0.01246  37  ASN A O   
307 C CB  . ASN A 41  ? 0.52629 0.46146 0.46710 0.02379  0.03152  0.01698  37  ASN A CB  
308 C CG  . ASN A 41  ? 0.76862 0.71103 0.70811 0.04050  0.02595  0.01540  37  ASN A CG  
309 O OD1 . ASN A 41  ? 0.77085 0.72625 0.72007 0.04308  0.01717  0.01232  37  ASN A OD1 
310 N ND2 . ASN A 41  ? 0.81569 0.75012 0.74264 0.05300  0.03108  0.01697  37  ASN A ND2 
311 N N   . LEU A 42  ? 0.47236 0.44315 0.43798 0.01231  0.01914  0.01579  38  LEU A N   
312 C CA  . LEU A 42  ? 0.44104 0.42567 0.41803 0.01105  0.00974  0.01372  38  LEU A CA  
313 C C   . LEU A 42  ? 0.68399 0.67258 0.66382 0.02484  0.00207  0.01094  38  LEU A C   
314 O O   . LEU A 42  ? 0.55716 0.55237 0.53563 0.03292  0.00116  0.01132  38  LEU A O   
315 C CB  . LEU A 42  ? 0.52475 0.52102 0.50527 0.00483  0.01170  0.01550  38  LEU A CB  
316 C CG  . LEU A 42  ? 0.51103 0.52173 0.50145 0.00502  0.00304  0.01438  38  LEU A CG  
317 C CD1 . LEU A 42  ? 0.57097 0.58170 0.56680 -0.00156 -0.00070 0.01327  38  LEU A CD1 
318 C CD2 . LEU A 42  ? 0.67155 0.69599 0.66441 0.00021  0.00548  0.01598  38  LEU A CD2 
319 N N   . ASN A 43  ? 0.63485 0.62030 0.61957 0.02758  -0.00343 0.00736  39  ASN A N   
320 C CA  . ASN A 43  ? 0.58605 0.57614 0.57740 0.03901  -0.01173 0.00194  39  ASN A CA  
321 C C   . ASN A 43  ? 0.57569 0.56611 0.55702 0.05304  -0.01020 0.00062  39  ASN A C   
322 O O   . ASN A 43  ? 0.69664 0.69544 0.68003 0.06261  -0.01515 -0.00235 39  ASN A O   
323 C CB  . ASN A 43  ? 0.56745 0.56720 0.57023 0.03863  -0.01848 0.00061  39  ASN A CB  
324 C CG  . ASN A 43  ? 0.70332 0.70401 0.71979 0.04275  -0.02666 -0.00560 39  ASN A CG  
325 O OD1 . ASN A 43  ? 0.62367 0.61928 0.64486 0.03998  -0.02699 -0.00729 39  ASN A OD1 
326 N ND2 . ASN A 43  ? 0.58041 0.58755 0.60437 0.04925  -0.03286 -0.00937 39  ASN A ND2 
327 N N   . GLY A 44  ? 0.56172 0.54291 0.53099 0.05559  -0.00282 0.00313  40  GLY A N   
328 C CA  . GLY A 44  ? 0.57768 0.55870 0.53512 0.07118  0.00003  0.00311  40  GLY A CA  
329 C C   . GLY A 44  ? 0.54952 0.52759 0.49551 0.07264  0.01055  0.01087  40  GLY A C   
330 O O   . GLY A 44  ? 0.66345 0.63870 0.59671 0.08615  0.01612  0.01340  40  GLY A O   
331 N N   . VAL A 45  ? 0.64024 0.61996 0.59077 0.05992  0.01401  0.01480  41  VAL A N   
332 C CA  . VAL A 45  ? 0.66932 0.64778 0.61291 0.05900  0.02476  0.02189  41  VAL A CA  
333 C C   . VAL A 45  ? 0.59592 0.56126 0.53715 0.04412  0.03536  0.02573  41  VAL A C   
334 O O   . VAL A 45  ? 0.56867 0.53705 0.51893 0.02924  0.03339  0.02397  41  VAL A O   
335 C CB  . VAL A 45  ? 0.64102 0.63401 0.59297 0.05596  0.02102  0.02223  41  VAL A CB  
336 C CG1 . VAL A 45  ? 0.59285 0.58570 0.54029 0.05290  0.03336  0.02967  41  VAL A CG1 
337 C CG2 . VAL A 45  ? 0.68193 0.68619 0.63554 0.07160  0.01083  0.01746  41  VAL A CG2 
338 N N   . PRO A 46  ? 0.63856 0.58946 0.56762 0.04853  0.04676  0.03053  42  PRO A N   
339 C CA  . PRO A 46  ? 0.60693 0.54328 0.53443 0.03422  0.05725  0.03288  42  PRO A CA  
340 C C   . PRO A 46  ? 0.65946 0.59802 0.59227 0.02292  0.06646  0.03656  42  PRO A C   
341 O O   . PRO A 46  ? 0.77401 0.71758 0.70463 0.03038  0.07175  0.04166  42  PRO A O   
342 C CB  . PRO A 46  ? 0.74507 0.66435 0.65689 0.04598  0.06697  0.03734  42  PRO A CB  
343 C CG  . PRO A 46  ? 0.59756 0.52476 0.50202 0.06561  0.06636  0.04036  42  PRO A CG  
344 C CD  . PRO A 46  ? 0.61617 0.56309 0.53173 0.06819  0.05043  0.03339  42  PRO A CD  
345 N N   . TYR A 47  ? 0.61719 0.55368 0.55775 0.00509  0.06832  0.03331  43  TYR A N   
346 C CA  . TYR A 47  ? 0.58405 0.52359 0.53264 -0.00857 0.07723  0.03433  43  TYR A CA  
347 C C   . TYR A 47  ? 0.67544 0.59498 0.62136 -0.01960 0.08911  0.03378  43  TYR A C   
348 O O   . TYR A 47  ? 0.72514 0.64202 0.67360 -0.02904 0.08463  0.02755  43  TYR A O   
349 C CB  . TYR A 47  ? 0.51982 0.48028 0.48227 -0.01957 0.06706  0.02843  43  TYR A CB  
350 C CG  . TYR A 47  ? 0.52654 0.50547 0.49235 -0.00946 0.05752  0.02939  43  TYR A CG  
351 C CD1 . TYR A 47  ? 0.72346 0.71051 0.69016 -0.00455 0.06313  0.03433  43  TYR A CD1 
352 C CD2 . TYR A 47  ? 0.66754 0.65498 0.63603 -0.00446 0.04373  0.02555  43  TYR A CD2 
353 C CE1 . TYR A 47  ? 0.77600 0.77958 0.74488 0.00563  0.05424  0.03463  43  TYR A CE1 
354 C CE2 . TYR A 47  ? 0.73662 0.73873 0.70848 0.00488  0.03544  0.02566  43  TYR A CE2 
355 C CZ  . TYR A 47  ? 0.71525 0.72554 0.68661 0.01022  0.04023  0.02982  43  TYR A CZ  
356 O OH  . TYR A 47  ? 0.91449 0.93908 0.88833 0.02042  0.03179  0.02936  43  TYR A OH  
357 N N   . LYS A 48  ? 0.71411 0.61900 0.65474 -0.01766 0.10488  0.04052  44  LYS A N   
358 C CA  . LYS A 48  ? 0.64878 0.53007 0.58566 -0.02603 0.11842  0.04084  44  LYS A CA  
359 C C   . LYS A 48  ? 0.72476 0.60799 0.67653 -0.04514 0.12802  0.03785  44  LYS A C   
360 O O   . LYS A 48  ? 0.70605 0.60005 0.66523 -0.04583 0.13318  0.04198  44  LYS A O   
361 C CB  . LYS A 48  ? 0.68091 0.54144 0.60146 -0.00995 0.13175  0.05106  44  LYS A CB  
362 C CG  . LYS A 48  ? 0.79383 0.62639 0.70979 -0.01729 0.14852  0.05296  44  LYS A CG  
363 C CD  . LYS A 48  ? 0.86142 0.67537 0.75804 -0.00119 0.15095  0.05702  44  LYS A CD  
364 C CE  . LYS A 48  ? 0.87455 0.65807 0.76242 -0.00084 0.17259  0.06433  44  LYS A CE  
365 N NZ  . LYS A 48  ? 0.98700 0.76253 0.89085 -0.02424 0.18245  0.05925  44  LYS A NZ  
366 N N   . GLY A 49  ? 0.82785 0.70205 0.78471 -0.06027 0.13030  0.02993  45  GLY A N   
367 C CA  . GLY A 49  ? 0.72858 0.60482 0.70161 -0.07972 0.13915  0.02413  45  GLY A CA  
368 C C   . GLY A 49  ? 0.59268 0.49487 0.57984 -0.09276 0.12521  0.01211  45  GLY A C   
369 O O   . GLY A 49  ? 0.57689 0.50017 0.56427 -0.08615 0.11051  0.01150  45  GLY A O   
370 N N   . LYS A 50  ? 0.74960 0.65038 0.74887 -0.11095 0.13027  0.00193  46  LYS A N   
371 C CA  . LYS A 50  ? 0.65403 0.58154 0.66623 -0.12252 0.11772  -0.01056 46  LYS A CA  
372 C C   . LYS A 50  ? 0.69209 0.64927 0.71630 -0.12313 0.11255  -0.00959 46  LYS A C   
373 O O   . LYS A 50  ? 0.65176 0.63349 0.67868 -0.12122 0.09792  -0.01383 46  LYS A O   
374 C CB  . LYS A 50  ? 0.79503 0.71654 0.81921 -0.14160 0.12509  -0.02336 46  LYS A CB  
375 C CG  . LYS A 50  ? 0.82532 0.76281 0.85210 -0.14792 0.11146  -0.03678 46  LYS A CG  
376 C CD  . LYS A 50  ? 0.96998 0.88435 0.99418 -0.15657 0.11825  -0.04554 46  LYS A CD  
377 C CE  . LYS A 50  ? 0.95110 0.88515 0.97957 -0.16339 0.10552  -0.06047 46  LYS A CE  
378 N NZ  . LYS A 50  ? 0.85503 0.76791 0.86901 -0.15934 0.10465  -0.06290 46  LYS A NZ  
379 N N   . GLU A 51  ? 0.66752 0.62269 0.69853 -0.12474 0.12522  -0.00319 47  GLU A N   
380 C CA  . GLU A 51  ? 0.69792 0.68185 0.74038 -0.12487 0.12135  -0.00191 47  GLU A CA  
381 C C   . GLU A 51  ? 0.63703 0.63113 0.66757 -0.10583 0.10937  0.00646  47  GLU A C   
382 O O   . GLU A 51  ? 0.62797 0.64930 0.66533 -0.10445 0.09938  0.00450  47  GLU A O   
383 C CB  . GLU A 51  ? 0.76634 0.74430 0.81873 -0.13020 0.13952  0.00432  47  GLU A CB  
384 C CG  . GLU A 51  ? 0.86330 0.82025 0.92560 -0.14706 0.15540  -0.00167 47  GLU A CG  
385 C CD  . GLU A 51  ? 1.17987 1.13711 1.25863 -0.15613 0.17343  0.00270  47  GLU A CD  
386 O OE1 . GLU A 51  ? 1.39106 1.33390 1.46065 -0.14359 0.18511  0.01791  47  GLU A OE1 
387 O OE2 . GLU A 51  ? 1.19836 1.17153 1.29979 -0.17531 0.17622  -0.00930 47  GLU A OE2 
388 N N   . ALA A 52  ? 0.71809 0.69141 0.73138 -0.09069 0.11014  0.01493  48  ALA A N   
389 C CA  . ALA A 52  ? 0.69708 0.67916 0.70064 -0.07293 0.09860  0.02077  48  ALA A CA  
390 C C   . ALA A 52  ? 0.59440 0.58520 0.59565 -0.07139 0.08234  0.01442  48  ALA A C   
391 O O   . ALA A 52  ? 0.60289 0.61319 0.60649 -0.06531 0.07079  0.01419  48  ALA A O   
392 C CB  . ALA A 52  ? 0.62221 0.58216 0.60949 -0.05651 0.10544  0.03080  48  ALA A CB  
393 N N   . ILE A 53  ? 0.67233 0.64811 0.66879 -0.07612 0.08218  0.00988  49  ILE A N   
394 C CA  . ILE A 53  ? 0.58869 0.57265 0.58374 -0.07527 0.06864  0.00460  49  ILE A CA  
395 C C   . ILE A 53  ? 0.51477 0.52638 0.52242 -0.08419 0.06096  -0.00253 49  ILE A C   
396 O O   . ILE A 53  ? 0.67977 0.70609 0.68744 -0.07831 0.04914  -0.00294 49  ILE A O   
397 C CB  . ILE A 53  ? 0.68866 0.65298 0.67714 -0.08003 0.07168  0.00054  49  ILE A CB  
398 C CG1 . ILE A 53  ? 0.67298 0.61276 0.64712 -0.06775 0.07739  0.00803  49  ILE A CG1 
399 C CG2 . ILE A 53  ? 0.66966 0.64501 0.65831 -0.08051 0.05924  -0.00486 49  ILE A CG2 
400 C CD1 . ILE A 53  ? 0.74563 0.66328 0.71252 -0.07230 0.08389  0.00501  49  ILE A CD1 
401 N N   . LYS A 54  ? 0.66058 0.68016 0.67975 -0.09807 0.06813  -0.00838 50  LYS A N   
402 C CA  . LYS A 54  ? 0.68359 0.73322 0.71546 -0.10602 0.06134  -0.01623 50  LYS A CA  
403 C C   . LYS A 54  ? 0.70958 0.77954 0.74287 -0.09555 0.05386  -0.01050 50  LYS A C   
404 O O   . LYS A 54  ? 0.79930 0.88536 0.83177 -0.09005 0.04233  -0.01177 50  LYS A O   
405 C CB  . LYS A 54  ? 0.69900 0.75332 0.74535 -0.12256 0.07208  -0.02361 50  LYS A CB  
406 C CG  . LYS A 54  ? 0.80290 0.89181 0.86476 -0.13128 0.06660  -0.03284 50  LYS A CG  
407 C CD  . LYS A 54  ? 0.74568 0.83697 0.82330 -0.14460 0.08002  -0.03577 50  LYS A CD  
408 C CE  . LYS A 54  ? 0.89038 0.95272 0.96864 -0.15566 0.09227  -0.04019 50  LYS A CE  
409 N NZ  . LYS A 54  ? 0.92457 0.97219 1.01155 -0.16259 0.11018  -0.03512 50  LYS A NZ  
410 N N   . LYS A 55  ? 0.68710 0.75557 0.72174 -0.09147 0.06108  -0.00351 51  LYS A N   
411 C CA  . LYS A 55  ? 0.71803 0.80576 0.75391 -0.08111 0.05475  0.00146  51  LYS A CA  
412 C C   . LYS A 55  ? 0.59914 0.68597 0.62550 -0.06701 0.04230  0.00467  51  LYS A C   
413 O O   . LYS A 55  ? 0.64817 0.75455 0.67710 -0.06082 0.03384  0.00521  51  LYS A O   
414 C CB  . LYS A 55  ? 0.40993 0.48996 0.44394 -0.07473 0.06488  0.01026  51  LYS A CB  
415 C CG  . LYS A 55  ? 0.51849 0.60498 0.56595 -0.08815 0.07794  0.00858  51  LYS A CG  
416 C CD  . LYS A 55  ? 0.66049 0.73078 0.70278 -0.08072 0.09133  0.01936  51  LYS A CD  
417 C CE  . LYS A 55  ? 0.71494 0.78019 0.77033 -0.09624 0.10833  0.01825  51  LYS A CE  
418 N NZ  . LYS A 55  ? 0.77382 0.83657 0.82874 -0.08841 0.12111  0.02988  51  LYS A NZ  
419 N N   . VAL A 56  ? 0.58176 0.64613 0.59802 -0.06178 0.04161  0.00668  52  VAL A N   
420 C CA  . VAL A 56  ? 0.62563 0.68846 0.63605 -0.05040 0.03075  0.00865  52  VAL A CA  
421 C C   . VAL A 56  ? 0.63874 0.71430 0.65284 -0.05533 0.02296  0.00341  52  VAL A C   
422 O O   . VAL A 56  ? 0.57300 0.65740 0.58710 -0.04720 0.01422  0.00525  52  VAL A O   
423 C CB  . VAL A 56  ? 0.62845 0.66604 0.62856 -0.04345 0.03288  0.01172  52  VAL A CB  
424 C CG1 . VAL A 56  ? 0.65662 0.69266 0.65428 -0.03464 0.02242  0.01211  52  VAL A CG1 
425 C CG2 . VAL A 56  ? 0.62909 0.65770 0.62364 -0.03405 0.03943  0.01767  52  VAL A CG2 
426 N N   . LEU A 57  ? 0.61656 0.69351 0.63385 -0.06781 0.02649  -0.00325 53  LEU A N   
427 C CA  . LEU A 57  ? 0.62442 0.71448 0.64332 -0.07069 0.01947  -0.00842 53  LEU A CA  
428 C C   . LEU A 57  ? 0.65065 0.77014 0.67639 -0.06878 0.01325  -0.00982 53  LEU A C   
429 O O   . LEU A 57  ? 0.62844 0.75677 0.65204 -0.06082 0.00556  -0.00757 53  LEU A O   
430 C CB  . LEU A 57  ? 0.70867 0.79523 0.72961 -0.08396 0.02453  -0.01715 53  LEU A CB  
431 C CG  . LEU A 57  ? 0.69537 0.75426 0.70742 -0.08440 0.02892  -0.01643 53  LEU A CG  
432 C CD1 . LEU A 57  ? 0.77859 0.83189 0.79403 -0.09840 0.03632  -0.02567 53  LEU A CD1 
433 C CD2 . LEU A 57  ? 0.57830 0.63550 0.58402 -0.07676 0.02111  -0.01438 53  LEU A CD2 
434 N N   . GLU A 58  ? 0.69449 0.82978 0.72882 -0.07545 0.01724  -0.01307 54  GLU A N   
435 C CA  . GLU A 58  ? 0.72234 0.88800 0.76283 -0.07257 0.01137  -0.01459 54  GLU A CA  
436 C C   . GLU A 58  ? 0.64596 0.81288 0.68280 -0.05826 0.00704  -0.00572 54  GLU A C   
437 O O   . GLU A 58  ? 0.74911 0.93802 0.78798 -0.05207 0.00103  -0.00518 54  GLU A O   
438 C CB  . GLU A 58  ? 0.82294 1.00793 0.87598 -0.08462 0.01707  -0.02165 54  GLU A CB  
439 C CG  . GLU A 58  ? 0.92455 1.10921 0.98403 -0.10015 0.02163  -0.03297 54  GLU A CG  
440 C CD  . GLU A 58  ? 0.97421 1.13651 1.03735 -0.11013 0.03427  -0.03291 54  GLU A CD  
441 O OE1 . GLU A 58  ? 0.99524 1.13635 1.05102 -0.10256 0.03885  -0.02284 54  GLU A OE1 
442 O OE2 . GLU A 58  ? 1.03001 1.19572 1.10346 -0.12495 0.04006  -0.04325 54  GLU A OE2 
443 N N   . SER A 59  ? 0.58481 0.72950 0.61597 -0.05190 0.00988  0.00057  55  SER A N   
444 C CA  . SER A 59  ? 0.64602 0.78958 0.67354 -0.03759 0.00495  0.00718  55  SER A CA  
445 C C   . SER A 59  ? 0.61334 0.74341 0.63543 -0.02891 -0.00156 0.01001  55  SER A C   
446 O O   . SER A 59  ? 0.54967 0.67681 0.57013 -0.01733 -0.00607 0.01406  55  SER A O   
447 C CB  . SER A 59  ? 0.72207 0.85236 0.74671 -0.03335 0.01102  0.01142  55  SER A CB  
448 O OG  . SER A 59  ? 0.76369 0.91145 0.79441 -0.03585 0.01557  0.01176  55  SER A OG  
449 N N   . ALA A 60  ? 0.73093 0.85284 0.75115 -0.03425 -0.00172 0.00760  56  ALA A N   
450 C CA  . ALA A 60  ? 0.61784 0.72841 0.63505 -0.02691 -0.00667 0.01078  56  ALA A CA  
451 C C   . ALA A 60  ? 0.56337 0.69035 0.58281 -0.01913 -0.01269 0.01351  56  ALA A C   
452 O O   . ALA A 60  ? 0.51098 0.66013 0.53259 -0.02187 -0.01356 0.01105  56  ALA A O   
453 C CB  . ALA A 60  ? 0.65268 0.75405 0.66719 -0.03393 -0.00488 0.00803  56  ALA A CB  
454 N N   . PRO A 61  ? 0.55362 0.67068 0.57315 -0.00899 -0.01650 0.01815  57  PRO A N   
455 C CA  . PRO A 61  ? 0.67539 0.80483 0.69659 -0.00018 -0.02067 0.02203  57  PRO A CA  
456 C C   . PRO A 61  ? 0.66479 0.80373 0.68462 -0.00153 -0.02095 0.02292  57  PRO A C   
457 O O   . PRO A 61  ? 0.61779 0.74941 0.63574 -0.00793 -0.01889 0.02097  57  PRO A O   
458 C CB  . PRO A 61  ? 0.65119 0.76214 0.67474 0.00909  -0.02322 0.02557  57  PRO A CB  
459 C CG  . PRO A 61  ? 0.71966 0.81443 0.74221 0.00657  -0.02154 0.02249  57  PRO A CG  
460 C CD  . PRO A 61  ? 0.67107 0.76555 0.69014 -0.00474 -0.01683 0.01940  57  PRO A CD  
461 N N   . LYS A 62  ? 0.63599 0.79237 0.65564 0.00622  -0.02334 0.02615  58  LYS A N   
462 C CA  . LYS A 62  ? 0.60609 0.77340 0.62289 0.00925  -0.02352 0.02860  58  LYS A CA  
463 C C   . LYS A 62  ? 0.64712 0.79263 0.66461 0.01363  -0.02213 0.03490  58  LYS A C   
464 O O   . LYS A 62  ? 0.66708 0.80156 0.68793 0.02230  -0.02258 0.04075  58  LYS A O   
465 C CB  . LYS A 62  ? 0.52832 0.71835 0.54362 0.01962  -0.02576 0.03202  58  LYS A CB  
466 N N   . ALA A 63  ? 0.60604 0.74519 0.62145 0.00747  -0.02007 0.03324  59  ALA A N   
467 C CA  . ALA A 63  ? 0.43833 0.55783 0.45583 0.01037  -0.01796 0.03892  59  ALA A CA  
468 C C   . ALA A 63  ? 0.56303 0.68714 0.57547 0.00714  -0.01589 0.03832  59  ALA A C   
469 O O   . ALA A 63  ? 0.56818 0.70094 0.57672 -0.00132 -0.01610 0.03048  59  ALA A O   
470 C CB  . ALA A 63  ? 0.56375 0.66047 0.58574 0.00605  -0.01775 0.03643  59  ALA A CB  
471 N N   . LYS A 64  ? 0.50613 0.62409 0.51925 0.01417  -0.01328 0.04653  60  LYS A N   
472 C CA  . LYS A 64  ? 0.53028 0.65036 0.53836 0.01329  -0.01078 0.04747  60  LYS A CA  
473 C C   . LYS A 64  ? 0.50894 0.60528 0.52177 0.00957  -0.00811 0.04925  60  LYS A C   
474 O O   . LYS A 64  ? 0.52818 0.60915 0.54985 0.01274  -0.00706 0.05408  60  LYS A O   
475 C CB  . LYS A 64  ? 0.71297 0.84568 0.71747 0.02568  -0.00833 0.05694  60  LYS A CB  
476 C CG  . LYS A 64  ? 0.68798 0.84982 0.68310 0.02815  -0.01063 0.05206  60  LYS A CG  
477 C CD  . LYS A 64  ? 0.62519 0.80422 0.62095 0.02646  -0.01502 0.04548  60  LYS A CD  
478 C CE  . LYS A 64  ? 0.69719 0.90743 0.68640 0.02609  -0.01815 0.03673  60  LYS A CE  
479 N NZ  . LYS A 64  ? 0.82484 1.03371 0.81189 0.01490  -0.01843 0.02659  60  LYS A NZ  
480 N N   . TYR A 65  ? 0.46219 0.55640 0.46985 0.00301  -0.00714 0.04434  61  TYR A N   
481 C CA  . TYR A 65  ? 0.56983 0.64401 0.58071 -0.00078 -0.00490 0.04459  61  TYR A CA  
482 C C   . TYR A 65  ? 0.57885 0.65437 0.58585 0.00248  -0.00127 0.04947  61  TYR A C   
483 O O   . TYR A 65  ? 0.49924 0.59038 0.49724 0.00340  -0.00152 0.04701  61  TYR A O   
484 C CB  . TYR A 65  ? 0.59755 0.66438 0.60472 -0.01063 -0.00592 0.03484  61  TYR A CB  
485 C CG  . TYR A 65  ? 0.44973 0.51718 0.45937 -0.01313 -0.00846 0.03057  61  TYR A CG  
486 C CD1 . TYR A 65  ? 0.44226 0.49594 0.45859 -0.01114 -0.00940 0.03151  61  TYR A CD1 
487 C CD2 . TYR A 65  ? 0.48419 0.56783 0.49019 -0.01698 -0.00987 0.02499  61  TYR A CD2 
488 C CE1 . TYR A 65  ? 0.51104 0.56635 0.52839 -0.01166 -0.01145 0.02813  61  TYR A CE1 
489 C CE2 . TYR A 65  ? 0.54142 0.62662 0.55002 -0.01871 -0.01124 0.02214  61  TYR A CE2 
490 C CZ  . TYR A 65  ? 0.57385 0.64448 0.58712 -0.01541 -0.01190 0.02429  61  TYR A CZ  
491 O OH  . TYR A 65  ? 0.56692 0.64006 0.58153 -0.01544 -0.01302 0.02192  61  TYR A OH  
492 N N   . LYS A 66  ? 0.57875 0.63940 0.59332 0.00460  0.00206  0.05570  62  LYS A N   
493 C CA  . LYS A 66  ? 0.53410 0.59435 0.54630 0.00801  0.00657  0.06150  62  LYS A CA  
494 C C   . LYS A 66  ? 0.60673 0.65004 0.62355 0.00279  0.00786  0.05911  62  LYS A C   
495 O O   . LYS A 66  ? 0.59111 0.62216 0.62013 0.00220  0.00792  0.06026  62  LYS A O   
496 C CB  . LYS A 66  ? 0.58939 0.65136 0.60835 0.01819  0.01162  0.07464  62  LYS A CB  
497 C CG  . LYS A 66  ? 0.66891 0.73054 0.68644 0.02284  0.01774  0.08253  62  LYS A CG  
498 C CD  . LYS A 66  ? 0.63516 0.69892 0.65858 0.03408  0.02473  0.09720  62  LYS A CD  
499 C CE  . LYS A 66  ? 0.85819 0.90743 0.89862 0.03375  0.02610  0.10092  62  LYS A CE  
500 N NZ  . LYS A 66  ? 0.84930 0.90537 0.88929 0.04425  0.02918  0.11012  62  LYS A NZ  
501 N N   . ILE A 67  ? 0.56140 0.60506 0.56853 -0.00030 0.00865  0.05485  63  ILE A N   
502 C CA  . ILE A 67  ? 0.60296 0.63238 0.61244 -0.00361 0.01027  0.05299  63  ILE A CA  
503 C C   . ILE A 67  ? 0.54026 0.56599 0.56040 0.00185  0.01533  0.06323  63  ILE A C   
504 O O   . ILE A 67  ? 0.65812 0.69292 0.67624 0.00835  0.01924  0.07156  63  ILE A O   
505 C CB  . ILE A 67  ? 0.61151 0.64165 0.60675 -0.00738 0.01045  0.04596  63  ILE A CB  
506 C CG1 . ILE A 67  ? 0.42220 0.45225 0.41062 -0.01464 0.00712  0.03546  63  ILE A CG1 
507 C CG2 . ILE A 67  ? 0.49620 0.51339 0.49236 -0.00813 0.01305  0.04597  63  ILE A CG2 
508 C CD1 . ILE A 67  ? 0.60616 0.64130 0.58174 -0.01835 0.00741  0.02769  63  ILE A CD1 
509 N N   . THR A 68  ? 0.61232 0.62592 0.64465 -0.00020 0.01572  0.06258  64  THR A N   
510 C CA  . THR A 68  ? 0.68044 0.69021 0.72681 0.00306  0.02112  0.07093  64  THR A CA  
511 C C   . THR A 68  ? 0.56344 0.56675 0.61120 0.00082  0.02237  0.06786  64  THR A C   
512 O O   . THR A 68  ? 0.49385 0.49707 0.55149 0.00344  0.02788  0.07512  64  THR A O   
513 C CB  . THR A 68  ? 0.70764 0.71123 0.77369 0.00347  0.02105  0.07308  64  THR A CB  
514 O OG1 . THR A 68  ? 0.70720 0.70368 0.77730 -0.00091 0.01528  0.06264  64  THR A OG1 
515 C CG2 . THR A 68  ? 0.75975 0.76944 0.82410 0.00754  0.02079  0.07770  64  THR A CG2 
516 N N   . LYS A 69  ? 0.54213 0.54033 0.58043 -0.00316 0.01836  0.05810  65  LYS A N   
517 C CA  . LYS A 69  ? 0.56768 0.56044 0.60454 -0.00362 0.01964  0.05513  65  LYS A CA  
518 C C   . LYS A 69  ? 0.59765 0.58513 0.61689 -0.00655 0.01689  0.04608  65  LYS A C   
519 O O   . LYS A 69  ? 0.57135 0.55617 0.58772 -0.00913 0.01329  0.04058  65  LYS A O   
520 C CB  . LYS A 69  ? 0.70443 0.69259 0.76067 -0.00380 0.01880  0.05323  65  LYS A CB  
521 C CG  . LYS A 69  ? 0.68502 0.67206 0.74381 -0.00250 0.02141  0.05267  65  LYS A CG  
522 C CD  . LYS A 69  ? 0.86074 0.84623 0.93828 -0.00279 0.01882  0.04699  65  LYS A CD  
523 C CE  . LYS A 69  ? 0.76623 0.75555 0.86852 -0.00297 0.02348  0.05344  65  LYS A CE  
524 N NZ  . LYS A 69  ? 0.76851 0.75705 0.88205 -0.00378 0.02467  0.05883  65  LYS A NZ  
525 N N   . ILE A 70  ? 0.60443 0.58972 0.61214 -0.00567 0.01949  0.04506  66  ILE A N   
526 C CA  . ILE A 70  ? 0.56684 0.54416 0.55772 -0.00813 0.01891  0.03717  66  ILE A CA  
527 C C   . ILE A 70  ? 0.68779 0.65801 0.67626 -0.00507 0.02105  0.03580  66  ILE A C   
528 O O   . ILE A 70  ? 0.61526 0.58931 0.60520 -0.00171 0.02417  0.04054  66  ILE A O   
529 C CB  . ILE A 70  ? 0.56109 0.54275 0.53688 -0.00974 0.02002  0.03531  66  ILE A CB  
530 C CG1 . ILE A 70  ? 0.52702 0.51729 0.50374 -0.01276 0.01714  0.03418  66  ILE A CG1 
531 C CG2 . ILE A 70  ? 0.56700 0.53717 0.52712 -0.01225 0.02147  0.02744  66  ILE A CG2 
532 C CD1 . ILE A 70  ? 0.61191 0.61156 0.57669 -0.01365 0.01724  0.03093  66  ILE A CD1 
533 N N   . ASP A 71  ? 0.54828 0.50932 0.53253 -0.00495 0.01985  0.02989  67  ASP A N   
534 C CA  . ASP A 71  ? 0.65933 0.61396 0.63832 -0.00043 0.02184  0.02780  67  ASP A CA  
535 C C   . ASP A 71  ? 0.63814 0.57965 0.59763 -0.00113 0.02408  0.02230  67  ASP A C   
536 O O   . ASP A 71  ? 0.64669 0.58329 0.60355 -0.00354 0.02302  0.01900  67  ASP A O   
537 C CB  . ASP A 71  ? 0.75336 0.71056 0.74718 0.00325  0.01893  0.02603  67  ASP A CB  
538 C CG  . ASP A 71  ? 0.91427 0.88169 0.93067 0.00183  0.01695  0.03003  67  ASP A CG  
539 O OD1 . ASP A 71  ? 0.94045 0.90923 0.96346 -0.00077 0.01391  0.02945  67  ASP A OD1 
540 O OD2 . ASP A 71  ? 1.05850 1.03207 1.08652 0.00347  0.01920  0.03406  67  ASP A OD2 
541 N N   . ILE A 72  ? 0.64864 0.58384 0.59486 0.00128  0.02801  0.02166  68  ILE A N   
542 C CA  . ILE A 72  ? 0.60366 0.52337 0.53139 0.00063  0.03197  0.01672  68  ILE A CA  
543 C C   . ILE A 72  ? 0.80217 0.71372 0.72294 0.00907  0.03469  0.01626  68  ILE A C   
544 O O   . ILE A 72  ? 0.88334 0.79899 0.80406 0.01416  0.03573  0.01857  68  ILE A O   
545 C CB  . ILE A 72  ? 0.68066 0.59819 0.59672 -0.00285 0.03457  0.01464  68  ILE A CB  
546 C CG1 . ILE A 72  ? 0.73743 0.66528 0.65899 -0.01002 0.03155  0.01365  68  ILE A CG1 
547 C CG2 . ILE A 72  ? 0.60553 0.50395 0.50397 -0.00335 0.04003  0.00904  68  ILE A CG2 
548 C CD1 . ILE A 72  ? 0.65661 0.58879 0.56924 -0.01181 0.03245  0.01071  68  ILE A CD1 
549 N N   . LYS A 73  ? 0.79542 0.69678 0.70994 0.01175  0.03626  0.01377  69  LYS A N   
550 C CA  . LYS A 73  ? 0.74982 0.64308 0.65440 0.02184  0.03954  0.01324  69  LYS A CA  
551 C C   . LYS A 73  ? 0.85129 0.72319 0.73551 0.02201  0.04725  0.01127  69  LYS A C   
552 O O   . LYS A 73  ? 0.81238 0.67687 0.69419 0.01403  0.04930  0.00940  69  LYS A O   
553 C CB  . LYS A 73  ? 0.84660 0.74677 0.76023 0.02834  0.03571  0.01236  69  LYS A CB  
554 C CG  . LYS A 73  ? 0.93647 0.85491 0.86897 0.03181  0.02996  0.01260  69  LYS A CG  
555 C CD  . LYS A 73  ? 0.79471 0.72183 0.73897 0.03623  0.02463  0.00920  69  LYS A CD  
556 C CE  . LYS A 73  ? 0.79492 0.73468 0.76156 0.02885  0.01875  0.00943  69  LYS A CE  
557 N NZ  . LYS A 73  ? 0.73025 0.68446 0.71630 0.03007  0.01587  0.00924  69  LYS A NZ  
558 N N   . ILE A 74  ? 0.89103 0.75305 0.76148 0.03125  0.05217  0.01166  70  ILE A N   
559 C CA  . ILE A 74  ? 0.92386 0.76230 0.77444 0.03326  0.06132  0.01052  70  ILE A CA  
560 C C   . ILE A 74  ? 1.01601 0.84858 0.85807 0.04679  0.06473  0.01258  70  ILE A C   
561 O O   . ILE A 74  ? 1.08117 0.92317 0.92336 0.05767  0.06250  0.01354  70  ILE A O   
562 C CB  . ILE A 74  ? 1.00510 0.83427 0.84308 0.03417  0.06556  0.00926  70  ILE A CB  
563 C CG1 . ILE A 74  ? 1.03539 0.86937 0.87864 0.02181  0.06301  0.00592  70  ILE A CG1 
564 C CG2 . ILE A 74  ? 1.02221 0.82465 0.83946 0.03936  0.07618  0.00855  70  ILE A CG2 
565 C CD1 . ILE A 74  ? 1.08736 0.91059 0.91662 0.02232  0.06736  0.00266  70  ILE A CD1 
566 N N   . VAL A 75  ? 0.86879 0.68783 0.70403 0.04693  0.07032  0.01330  71  VAL A N   
567 C CA  . VAL A 75  ? 1.00195 0.81360 0.82547 0.06176  0.07543  0.01617  71  VAL A CA  
568 C C   . VAL A 75  ? 1.08093 0.86337 0.88590 0.06173  0.08878  0.01808  71  VAL A C   
569 O O   . VAL A 75  ? 1.06189 0.83510 0.86905 0.05265  0.09304  0.01814  71  VAL A O   
570 C CB  . VAL A 75  ? 1.04996 0.87497 0.88417 0.06472  0.07016  0.01650  71  VAL A CB  
571 C CG1 . VAL A 75  ? 1.05624 0.88303 0.88002 0.08415  0.07221  0.01833  71  VAL A CG1 
572 C CG2 . VAL A 75  ? 0.95255 0.80232 0.80942 0.05797  0.05786  0.01354  71  VAL A CG2 
573 N N   . GLY A 76  ? 1.16707 0.93477 0.95475 0.07177  0.09605  0.01964  72  GLY A N   
574 C CA  . GLY A 76  ? 1.16112 0.89772 0.93162 0.07162  0.11021  0.02136  72  GLY A CA  
575 C C   . GLY A 76  ? 1.18446 0.91157 0.95969 0.05341  0.11152  0.01564  72  GLY A C   
576 O O   . GLY A 76  ? 1.12895 0.86474 0.90762 0.04873  0.10558  0.01157  72  GLY A O   
577 N N   . ASN A 77  ? 1.19588 0.90663 0.97194 0.04348  0.11952  0.01488  73  ASN A N   
578 C CA  . ASN A 77  ? 1.16412 0.86781 0.94668 0.02557  0.12071  0.00730  73  ASN A CA  
579 C C   . ASN A 77  ? 1.15221 0.87724 0.95495 0.01174  0.11161  0.00406  73  ASN A C   
580 O O   . ASN A 77  ? 1.32187 1.04337 1.13176 -0.00321 0.11312  -0.00261 73  ASN A O   
581 C CB  . ASN A 77  ? 1.19868 0.86902 0.97073 0.02228  0.13700  0.00704  73  ASN A CB  
582 C CG  . ASN A 77  ? 1.48524 1.14605 1.26167 0.00578  0.13881  -0.00365 73  ASN A CG  
583 O OD1 . ASN A 77  ? 1.60645 1.27921 1.38446 0.00291  0.13032  -0.00973 73  ASN A OD1 
584 N ND2 . ASN A 77  ? 1.52526 1.16573 1.30455 -0.00484 0.15013  -0.00646 73  ASN A ND2 
585 N N   . GLU A 78  ? 1.08730 0.83513 0.89978 0.01679  0.10208  0.00776  74  GLU A N   
586 C CA  . GLU A 78  ? 1.02265 0.79002 0.85292 0.00621  0.09397  0.00593  74  GLU A CA  
587 C C   . GLU A 78  ? 0.87582 0.66857 0.71773 0.00504  0.08088  0.00442  74  GLU A C   
588 O O   . GLU A 78  ? 0.80478 0.60555 0.64501 0.01569  0.07675  0.00720  74  GLU A O   
589 C CB  . GLU A 78  ? 0.96758 0.73871 0.80051 0.01302  0.09492  0.01153  74  GLU A CB  
590 C CG  . GLU A 78  ? 1.18746 0.93320 1.00773 0.01737  0.10981  0.01575  74  GLU A CG  
591 C CD  . GLU A 78  ? 1.24941 0.99695 1.07888 0.00993  0.11297  0.01717  74  GLU A CD  
592 O OE1 . GLU A 78  ? 1.15996 0.92761 0.99889 0.01295  0.10437  0.01886  74  GLU A OE1 
593 O OE2 . GLU A 78  ? 1.26320 0.99210 1.09134 0.00094  0.12443  0.01623  74  GLU A OE2 
594 N N   . ILE A 79  ? 0.85010 0.65605 0.70439 -0.00746 0.07511  0.00017  75  ILE A N   
595 C CA  . ILE A 79  ? 0.79465 0.62368 0.66046 -0.00893 0.06440  -0.00003 75  ILE A CA  
596 C C   . ILE A 79  ? 0.69447 0.54008 0.57424 -0.00834 0.05763  0.00314  75  ILE A C   
597 O O   . ILE A 79  ? 0.72704 0.57589 0.61336 -0.01594 0.05746  0.00172  75  ILE A O   
598 C CB  . ILE A 79  ? 0.74505 0.58044 0.61435 -0.02023 0.06215  -0.00638 75  ILE A CB  
599 C CG1 . ILE A 79  ? 0.90288 0.72242 0.75832 -0.01978 0.06799  -0.01095 75  ILE A CG1 
600 C CG2 . ILE A 79  ? 0.69729 0.55685 0.57840 -0.02015 0.05247  -0.00436 75  ILE A CG2 
601 C CD1 . ILE A 79  ? 0.82416 0.64724 0.67355 -0.00910 0.06585  -0.00726 75  ILE A CD1 
602 N N   . ILE A 80  ? 0.58609 0.44280 0.47141 0.00062  0.05209  0.00667  76  ILE A N   
603 C CA  . ILE A 80  ? 0.65761 0.53005 0.55736 0.00192  0.04497  0.00843  76  ILE A CA  
604 C C   . ILE A 80  ? 0.73506 0.62510 0.64851 -0.00292 0.03771  0.00893  76  ILE A C   
605 O O   . ILE A 80  ? 0.82497 0.71983 0.73979 0.00047  0.03630  0.01035  76  ILE A O   
606 C CB  . ILE A 80  ? 0.66142 0.53614 0.56111 0.01486  0.04341  0.01022  76  ILE A CB  
607 C CG1 . ILE A 80  ? 0.67990 0.53587 0.56156 0.02311  0.05245  0.01125  76  ILE A CG1 
608 C CG2 . ILE A 80  ? 0.58610 0.47379 0.49913 0.01623  0.03698  0.01014  76  ILE A CG2 
609 C CD1 . ILE A 80  ? 0.77543 0.62166 0.65283 0.02055  0.05810  0.01218  76  ILE A CD1 
610 N N   . VAL A 81  ? 0.61831 0.51824 0.54158 -0.00987 0.03396  0.00856  77  VAL A N   
611 C CA  . VAL A 81  ? 0.56890 0.48501 0.50440 -0.01312 0.02826  0.01038  77  VAL A CA  
612 C C   . VAL A 81  ? 0.61583 0.54238 0.56574 -0.01113 0.02269  0.01226  77  VAL A C   
613 O O   . VAL A 81  ? 0.57010 0.49699 0.52118 -0.01355 0.02215  0.01103  77  VAL A O   
614 C CB  . VAL A 81  ? 0.59201 0.51262 0.52541 -0.02198 0.02865  0.00761  77  VAL A CB  
615 C CG1 . VAL A 81  ? 0.58939 0.52687 0.53276 -0.02213 0.02395  0.01109  77  VAL A CG1 
616 C CG2 . VAL A 81  ? 0.53546 0.44391 0.45474 -0.02433 0.03422  0.00331  77  VAL A CG2 
617 N N   . ASN A 82  ? 0.57951 0.51444 0.54122 -0.00677 0.01903  0.01489  78  ASN A N   
618 C CA  . ASN A 82  ? 0.50038 0.44483 0.47815 -0.00526 0.01367  0.01575  78  ASN A CA  
619 C C   . ASN A 82  ? 0.60313 0.55810 0.59079 -0.00937 0.01190  0.01991  78  ASN A C   
620 O O   . ASN A 82  ? 0.58943 0.54807 0.58018 -0.00870 0.01334  0.02354  78  ASN A O   
621 C CB  . ASN A 82  ? 0.66037 0.60738 0.64777 0.00192  0.01133  0.01462  78  ASN A CB  
622 C CG  . ASN A 82  ? 0.61533 0.55565 0.59374 0.00899  0.01196  0.01051  78  ASN A CG  
623 O OD1 . ASN A 82  ? 0.59950 0.54072 0.57931 0.01123  0.00958  0.00828  78  ASN A OD1 
624 N ND2 . ASN A 82  ? 0.57712 0.51127 0.54514 0.01409  0.01558  0.00997  78  ASN A ND2 
625 N N   . VAL A 83  ? 0.48049 0.44093 0.47231 -0.01232 0.00943  0.02009  79  VAL A N   
626 C CA  . VAL A 83  ? 0.53543 0.50627 0.53363 -0.01460 0.00844  0.02450  79  VAL A CA  
627 C C   . VAL A 83  ? 0.50698 0.48291 0.52117 -0.01212 0.00471  0.02654  79  VAL A C   
628 O O   . VAL A 83  ? 0.55809 0.53333 0.57361 -0.01153 0.00192  0.02326  79  VAL A O   
629 C CB  . VAL A 83  ? 0.51784 0.49295 0.50637 -0.01987 0.00900  0.02230  79  VAL A CB  
630 C CG1 . VAL A 83  ? 0.52756 0.51603 0.52079 -0.01955 0.00797  0.02704  79  VAL A CG1 
631 C CG2 . VAL A 83  ? 0.60510 0.57272 0.57911 -0.02309 0.01294  0.01814  79  VAL A CG2 
632 N N   . ASP A 84  ? 0.49733 0.47772 0.52382 -0.01025 0.00542  0.03213  80  ASP A N   
633 C CA  . ASP A 84  ? 0.50708 0.49072 0.54993 -0.00833 0.00319  0.03459  80  ASP A CA  
634 C C   . ASP A 84  ? 0.57640 0.56806 0.61663 -0.00865 0.00370  0.03968  80  ASP A C   
635 O O   . ASP A 84  ? 0.56902 0.56610 0.60540 -0.00791 0.00712  0.04546  80  ASP A O   
636 C CB  . ASP A 84  ? 0.55869 0.54177 0.61852 -0.00642 0.00543  0.03841  80  ASP A CB  
637 C CG  . ASP A 84  ? 0.94858 0.92774 1.01644 -0.00491 0.00297  0.03134  80  ASP A CG  
638 O OD1 . ASP A 84  ? 0.91458 0.89478 0.99987 -0.00428 0.00434  0.03240  80  ASP A OD1 
639 O OD2 . ASP A 84  ? 0.96909 0.94515 1.02639 -0.00381 0.00014  0.02469  80  ASP A OD2 
640 N N   . VAL A 85  ? 0.53028 0.52434 0.57171 -0.00837 0.00029  0.03749  81  VAL A N   
641 C CA  . VAL A 85  ? 0.48472 0.48869 0.52222 -0.00775 0.00012  0.04111  81  VAL A CA  
642 C C   . VAL A 85  ? 0.58244 0.58675 0.63364 -0.00347 -0.00113 0.04480  81  VAL A C   
643 O O   . VAL A 85  ? 0.62837 0.62624 0.68919 -0.00245 -0.00404 0.04054  81  VAL A O   
644 C CB  . VAL A 85  ? 0.47416 0.48251 0.49954 -0.01147 -0.00207 0.03503  81  VAL A CB  
645 C CG1 . VAL A 85  ? 0.55236 0.57520 0.57335 -0.01080 -0.00236 0.03768  81  VAL A CG1 
646 C CG2 . VAL A 85  ? 0.44518 0.44810 0.45887 -0.01608 -0.00002 0.03010  81  VAL A CG2 
647 N N   . LEU A 86  ? 0.52993 0.54200 0.58145 0.00012  0.00123  0.05233  82  LEU A N   
648 C CA  . LEU A 86  ? 0.45479 0.46702 0.51639 0.00510  0.00095  0.05657  82  LEU A CA  
649 C C   . LEU A 86  ? 0.53984 0.56463 0.59087 0.00669  -0.00179 0.05568  82  LEU A C   
650 O O   . LEU A 86  ? 0.61026 0.64740 0.65123 0.00804  -0.00022 0.05880  82  LEU A O   
651 C CB  . LEU A 86  ? 0.54639 0.55717 0.61703 0.01007  0.00745  0.06765  82  LEU A CB  
652 C CG  . LEU A 86  ? 0.70516 0.70272 0.79614 0.00951  0.01008  0.06861  82  LEU A CG  
653 C CD1 . LEU A 86  ? 0.65461 0.64553 0.75644 0.00964  0.00505  0.06141  82  LEU A CD1 
654 C CD2 . LEU A 86  ? 0.81734 0.81099 0.90954 0.00466  0.01033  0.06423  82  LEU A CD2 
655 N N   . ALA A 87  ? 0.54393 0.56756 0.59744 0.00715  -0.00608 0.05071  83  ALA A N   
656 C CA  . ALA A 87  ? 0.54395 0.58064 0.58908 0.00837  -0.00880 0.04910  83  ALA A CA  
657 C C   . ALA A 87  ? 0.48953 0.52897 0.54063 0.01660  -0.00829 0.05554  83  ALA A C   
658 O O   . ALA A 87  ? 0.57676 0.60465 0.63969 0.01963  -0.00881 0.05568  83  ALA A O   
659 C CB  . ALA A 87  ? 0.48592 0.52069 0.52840 0.00491  -0.01285 0.04054  83  ALA A CB  
660 N N   . THR A 88  ? 0.53931 0.59448 0.58232 0.02084  -0.00727 0.06007  84  THR A N   
661 C CA  . THR A 88  ? 0.52019 0.57931 0.56589 0.03066  -0.00572 0.06760  84  THR A CA  
662 C C   . THR A 88  ? 0.54808 0.62300 0.58671 0.03253  -0.01022 0.06349  84  THR A C   
663 O O   . THR A 88  ? 0.55990 0.65243 0.58891 0.02925  -0.01185 0.05962  84  THR A O   
664 C CB  . THR A 88  ? 0.72041 0.78755 0.76162 0.03756  -0.00002 0.07783  84  THR A CB  
665 O OG1 . THR A 88  ? 0.77059 0.85197 0.80040 0.03314  -0.00091 0.07400  84  THR A OG1 
666 C CG2 . THR A 88  ? 0.64474 0.69410 0.69768 0.03912  0.00639  0.08549  84  THR A CG2 
667 N N   . GLY A 89  ? 0.64138 0.71074 0.68583 0.03770  -0.01212 0.06355  85  GLY A N   
668 C CA  . GLY A 89  ? 0.60484 0.68982 0.64342 0.04144  -0.01572 0.06119  85  GLY A CA  
669 C C   . GLY A 89  ? 0.58816 0.68651 0.62192 0.05261  -0.01312 0.06991  85  GLY A C   
670 O O   . GLY A 89  ? 0.57152 0.66306 0.60751 0.05869  -0.00770 0.07899  85  GLY A O   
671 N N   . PRO A 90  ? 0.62551 0.74413 0.65251 0.05646  -0.01625 0.06789  86  PRO A N   
672 C CA  . PRO A 90  ? 0.68526 0.81988 0.70587 0.06923  -0.01400 0.07604  86  PRO A CA  
673 C C   . PRO A 90  ? 0.67593 0.79271 0.70235 0.08076  -0.00958 0.08571  86  PRO A C   
674 O O   . PRO A 90  ? 0.79727 0.91933 0.81909 0.09220  -0.00442 0.09596  86  PRO A O   
675 C CB  . PRO A 90  ? 0.77653 0.93497 0.79173 0.06991  -0.01902 0.06993  86  PRO A CB  
676 C CG  . PRO A 90  ? 0.71368 0.87283 0.73052 0.05520  -0.02225 0.05918  86  PRO A CG  
677 C CD  . PRO A 90  ? 0.66731 0.79739 0.69193 0.04977  -0.02111 0.05853  86  PRO A CD  
678 N N   . SER A 91  ? 0.82666 0.92242 0.86320 0.07880  -0.01102 0.08242  87  SER A N   
679 C CA  . SER A 91  ? 0.75565 0.83098 0.80095 0.08792  -0.00658 0.08941  87  SER A CA  
680 C C   . SER A 91  ? 0.74567 0.80111 0.80084 0.08601  0.00062  0.09604  87  SER A C   
681 O O   . SER A 91  ? 0.70589 0.74183 0.77148 0.09208  0.00597  0.10192  87  SER A O   
682 C CB  . SER A 91  ? 0.76481 0.82637 0.81865 0.08624  -0.01160 0.08084  87  SER A CB  
683 O OG  . SER A 91  ? 1.01117 1.08387 1.05865 0.09591  -0.01432 0.08102  87  SER A OG  
684 N N   . GLY A 92  ? 0.69401 0.75355 0.74706 0.07781  0.00150  0.09516  88  GLY A N   
685 C CA  . GLY A 92  ? 0.66966 0.71120 0.73342 0.07454  0.00792  0.10023  88  GLY A CA  
686 C C   . GLY A 92  ? 0.69193 0.71529 0.76991 0.06395  0.00478  0.09068  88  GLY A C   
687 O O   . GLY A 92  ? 0.70774 0.71730 0.79695 0.06013  0.00982  0.09358  88  GLY A O   
688 N N   . PHE A 93  ? 0.60601 0.63059 0.68390 0.06013  -0.00310 0.07951  89  PHE A N   
689 C CA  . PHE A 93  ? 0.70393 0.71487 0.79329 0.05206  -0.00691 0.06935  89  PHE A CA  
690 C C   . PHE A 93  ? 0.59070 0.60430 0.67686 0.04265  -0.00675 0.06682  89  PHE A C   
691 O O   . PHE A 93  ? 0.64064 0.66930 0.71302 0.03939  -0.00866 0.06537  89  PHE A O   
692 C CB  . PHE A 93  ? 0.62272 0.63814 0.70866 0.05229  -0.01494 0.05898  89  PHE A CB  
693 C CG  . PHE A 93  ? 0.61226 0.61867 0.70587 0.04584  -0.01957 0.04786  89  PHE A CG  
694 C CD1 . PHE A 93  ? 0.65492 0.64430 0.76649 0.04487  -0.01863 0.04434  89  PHE A CD1 
695 C CD2 . PHE A 93  ? 0.53951 0.55524 0.62300 0.04132  -0.02425 0.04077  89  PHE A CD2 
696 C CE1 . PHE A 93  ? 0.69729 0.68187 0.81550 0.04056  -0.02355 0.03308  89  PHE A CE1 
697 C CE2 . PHE A 93  ? 0.56420 0.57281 0.65272 0.03793  -0.02798 0.03136  89  PHE A CE2 
698 C CZ  . PHE A 93  ? 0.61532 0.60973 0.72067 0.03809  -0.02826 0.02707  89  PHE A CZ  
699 N N   . THR A 94  ? 0.68080 0.67993 0.78077 0.03825  -0.00421 0.06564  90  THR A N   
700 C CA  . THR A 94  ? 0.63921 0.63901 0.73726 0.03079  -0.00291 0.06452  90  THR A CA  
701 C C   . THR A 94  ? 0.57553 0.56748 0.68155 0.02506  -0.00807 0.05278  90  THR A C   
702 O O   . THR A 94  ? 0.54393 0.52448 0.66653 0.02594  -0.00897 0.04830  90  THR A O   
703 C CB  . THR A 94  ? 0.70391 0.69671 0.81081 0.03199  0.00592  0.07507  90  THR A CB  
704 O OG1 . THR A 94  ? 0.71813 0.72360 0.81135 0.03770  0.01025  0.08531  90  THR A OG1 
705 C CG2 . THR A 94  ? 0.52003 0.50898 0.63129 0.02445  0.00679  0.07180  90  THR A CG2 
706 N N   . LEU A 95  ? 0.62633 0.62473 0.72076 0.01992  -0.01119 0.04730  91  LEU A N   
707 C CA  . LEU A 95  ? 0.56613 0.55932 0.66423 0.01666  -0.01567 0.03689  91  LEU A CA  
708 C C   . LEU A 95  ? 0.51591 0.50861 0.60955 0.01100  -0.01318 0.03696  91  LEU A C   
709 O O   . LEU A 95  ? 0.54124 0.54126 0.62066 0.00837  -0.01126 0.04019  91  LEU A O   
710 C CB  . LEU A 95  ? 0.50475 0.50454 0.59152 0.01804  -0.02121 0.03007  91  LEU A CB  
711 C CG  . LEU A 95  ? 0.58675 0.58287 0.67353 0.01727  -0.02514 0.02029  91  LEU A CG  
712 C CD1 . LEU A 95  ? 0.43680 0.42524 0.54134 0.02109  -0.02869 0.01320  91  LEU A CD1 
713 C CD2 . LEU A 95  ? 0.70142 0.70471 0.77432 0.01893  -0.02795 0.01663  91  LEU A CD2 
714 N N   . LYS A 96  ? 0.44051 0.42555 0.54689 0.00940  -0.01341 0.03239  92  LYS A N   
715 C CA  . LYS A 96  ? 0.46222 0.44658 0.56472 0.00526  -0.01143 0.03152  92  LYS A CA  
716 C C   . LYS A 96  ? 0.57091 0.55728 0.65969 0.00481  -0.01553 0.02369  92  LYS A C   
717 O O   . LYS A 96  ? 0.63834 0.62248 0.73237 0.00748  -0.01983 0.01523  92  LYS A O   
718 C CB  . LYS A 96  ? 0.46756 0.44551 0.59024 0.00427  -0.01008 0.02907  92  LYS A CB  
719 C CG  . LYS A 96  ? 0.60573 0.58406 0.72500 0.00123  -0.00822 0.02786  92  LYS A CG  
720 C CD  . LYS A 96  ? 0.80701 0.78859 0.91276 -0.00068 -0.00258 0.03747  92  LYS A CD  
721 C CE  . LYS A 96  ? 0.82122 0.80223 0.92516 -0.00279 -0.00000 0.03702  92  LYS A CE  
722 N NZ  . LYS A 96  ? 0.85618 0.83986 0.95618 -0.00315 0.00675  0.04757  92  LYS A NZ  
723 N N   . VAL A 97  ? 0.52118 0.51213 0.59267 0.00208  -0.01375 0.02619  93  VAL A N   
724 C CA  . VAL A 97  ? 0.57325 0.56388 0.63143 0.00126  -0.01507 0.02061  93  VAL A CA  
725 C C   . VAL A 97  ? 0.50563 0.49221 0.55697 -0.00194 -0.01157 0.02077  93  VAL A C   
726 O O   . VAL A 97  ? 0.47935 0.46643 0.53237 -0.00421 -0.00814 0.02593  93  VAL A O   
727 C CB  . VAL A 97  ? 0.50114 0.49890 0.54672 -0.00053 -0.01480 0.02172  93  VAL A CB  
728 C CG1 . VAL A 97  ? 0.43726 0.44089 0.48920 0.00328  -0.01745 0.02368  93  VAL A CG1 
729 C CG2 . VAL A 97  ? 0.53222 0.53441 0.56821 -0.00597 -0.01076 0.02559  93  VAL A CG2 
730 N N   . LYS A 98  ? 0.47780 0.46026 0.52055 -0.00069 -0.01191 0.01556  94  LYS A N   
731 C CA  . LYS A 98  ? 0.52006 0.49721 0.55461 -0.00219 -0.00842 0.01513  94  LYS A CA  
732 C C   . LYS A 98  ? 0.49134 0.46474 0.50870 -0.00389 -0.00547 0.01351  94  LYS A C   
733 O O   . LYS A 98  ? 0.56995 0.54341 0.58367 -0.00092 -0.00667 0.01090  94  LYS A O   
734 C CB  . LYS A 98  ? 0.60210 0.57660 0.64474 0.00293  -0.01053 0.01026  94  LYS A CB  
735 C CG  . LYS A 98  ? 0.62949 0.60684 0.69300 0.00335  -0.01249 0.01058  94  LYS A CG  
736 C CD  . LYS A 98  ? 0.91001 0.88782 0.98215 0.00785  -0.01493 0.00355  94  LYS A CD  
737 C CE  . LYS A 98  ? 0.94620 0.92600 1.01661 0.01481  -0.02032 -0.00466 94  LYS A CE  
738 N NZ  . LYS A 98  ? 0.92821 0.91206 1.00616 0.02126  -0.02387 -0.01349 94  LYS A NZ  
739 N N   . SER A 99  ? 0.47802 0.44771 0.48533 -0.00837 -0.00094 0.01504  95  SER A N   
740 C CA  . SER A 99  ? 0.44278 0.40669 0.43553 -0.01164 0.00350  0.01331  95  SER A CA  
741 C C   . SER A 99  ? 0.49113 0.44435 0.47422 -0.01034 0.00782  0.01231  95  SER A C   
742 O O   . SER A 99  ? 0.50418 0.45747 0.48891 -0.01074 0.00831  0.01387  95  SER A O   
743 C CB  . SER A 99  ? 0.45570 0.42612 0.44498 -0.01934 0.00511  0.01421  95  SER A CB  
744 O OG  . SER A 99  ? 0.51666 0.49854 0.51428 -0.01915 0.00120  0.01586  95  SER A OG  
745 N N   . THR A 100 ? 0.54520 0.48913 0.51762 -0.00776 0.01176  0.01050  96  THR A N   
746 C CA  . THR A 100 ? 0.52762 0.45919 0.48790 -0.00546 0.01732  0.00996  96  THR A CA  
747 C C   . THR A 100 ? 0.45195 0.37408 0.40074 -0.01204 0.02455  0.00928  96  THR A C   
748 O O   . THR A 100 ? 0.63894 0.55781 0.58444 -0.01128 0.02765  0.00943  96  THR A O   
749 C CB  . THR A 100 ? 0.53276 0.46062 0.49023 0.00585  0.01697  0.00876  96  THR A CB  
750 O OG1 . THR A 100 ? 0.60497 0.54348 0.57708 0.01041  0.00973  0.00718  96  THR A OG1 
751 C CG2 . THR A 100 ? 0.53278 0.44830 0.47673 0.00991  0.02306  0.00899  96  THR A CG2 
752 N N   . ILE A 101 ? 0.51009 0.42830 0.45379 -0.01843 0.02759  0.00814  97  ILE A N   
753 C CA  . ILE A 101 ? 0.63086 0.54068 0.56678 -0.02671 0.03428  0.00529  97  ILE A CA  
754 C C   . ILE A 101 ? 0.61151 0.50321 0.53408 -0.02415 0.04148  0.00459  97  ILE A C   
755 O O   . ILE A 101 ? 0.66157 0.55269 0.58163 -0.02039 0.03992  0.00508  97  ILE A O   
756 C CB  . ILE A 101 ? 0.58772 0.50976 0.52879 -0.03600 0.03139  0.00224  97  ILE A CB  
757 C CG1 . ILE A 101 ? 0.59235 0.53238 0.54557 -0.03608 0.02446  0.00416  97  ILE A CG1 
758 C CG2 . ILE A 101 ? 0.57857 0.49415 0.51502 -0.04578 0.03777  -0.00331 97  ILE A CG2 
759 C CD1 . ILE A 101 ? 0.52577 0.48085 0.48403 -0.03899 0.01995  0.00393  97  ILE A CD1 
760 N N   . THR A 102 ? 0.63825 0.51481 0.55247 -0.02565 0.05022  0.00406  98  THR A N   
761 C CA  . THR A 102 ? 0.69090 0.54686 0.59101 -0.02206 0.05892  0.00413  98  THR A CA  
762 C C   . THR A 102 ? 0.71431 0.55967 0.61129 -0.03397 0.06593  -0.00136 98  THR A C   
763 O O   . THR A 102 ? 0.68849 0.53452 0.59100 -0.04242 0.06943  -0.00342 98  THR A O   
764 C CB  . THR A 102 ? 0.69150 0.53540 0.58324 -0.01152 0.06552  0.00888  98  THR A CB  
765 O OG1 . THR A 102 ? 0.73970 0.59663 0.63629 -0.00059 0.05764  0.01139  98  THR A OG1 
766 C CG2 . THR A 102 ? 0.71555 0.53764 0.59118 -0.00532 0.07504  0.01011  98  THR A CG2 
767 N N   . PHE A 103 ? 0.78949 0.62610 0.67865 -0.03461 0.06791  -0.00454 99  PHE A N   
768 C CA  . PHE A 103 ? 0.82234 0.64699 0.70803 -0.04507 0.07456  -0.01186 99  PHE A CA  
769 C C   . PHE A 103 ? 0.88949 0.68643 0.75985 -0.03941 0.08588  -0.01045 99  PHE A C   
770 O O   . PHE A 103 ? 0.89596 0.68767 0.75690 -0.02682 0.08590  -0.00517 99  PHE A O   
771 C CB  . PHE A 103 ? 0.79252 0.63022 0.68060 -0.04985 0.06758  -0.01816 99  PHE A CB  
772 C CG  . PHE A 103 ? 0.73776 0.60209 0.63924 -0.05435 0.05775  -0.01922 99  PHE A CG  
773 C CD1 . PHE A 103 ? 0.75128 0.62530 0.66113 -0.06593 0.05728  -0.02663 99  PHE A CD1 
774 C CD2 . PHE A 103 ? 0.70309 0.58300 0.60949 -0.04670 0.04955  -0.01303 99  PHE A CD2 
775 C CE1 . PHE A 103 ? 0.61327 0.51259 0.53377 -0.06810 0.04856  -0.02709 99  PHE A CE1 
776 C CE2 . PHE A 103 ? 0.69840 0.60062 0.61602 -0.04949 0.04185  -0.01289 99  PHE A CE2 
777 C CZ  . PHE A 103 ? 0.47167 0.38390 0.39514 -0.05936 0.04123  -0.01955 99  PHE A CZ  
778 N N   . ASP A 104 ? 0.97302 0.75247 0.84172 -0.04864 0.09602  -0.01551 100 ASP A N   
779 C CA  . ASP A 104 ? 1.12780 0.87787 0.98187 -0.04441 0.10834  -0.01491 100 ASP A CA  
780 C C   . ASP A 104 ? 1.15680 0.90110 1.00829 -0.05235 0.10841  -0.02558 100 ASP A C   
781 O O   . ASP A 104 ? 1.09889 0.86443 0.95689 -0.05652 0.09761  -0.03128 100 ASP A O   
782 C CB  . ASP A 104 ? 1.10648 0.83716 0.96066 -0.04768 0.12215  -0.01176 100 ASP A CB  
783 C CG  . ASP A 104 ? 1.15362 0.88828 1.02300 -0.06618 0.12453  -0.02093 100 ASP A CG  
784 O OD1 . ASP A 104 ? 1.23498 0.99383 1.11571 -0.07456 0.11311  -0.02843 100 ASP A OD1 
785 O OD2 . ASP A 104 ? 1.17137 0.88563 1.04186 -0.07187 0.13846  -0.02056 100 ASP A OD2 
786 N N   . GLU A 105 ? 1.20037 0.91570 1.04181 -0.05333 0.12105  -0.02822 101 GLU A N   
787 C CA  . GLU A 105 ? 1.20714 0.91493 1.04495 -0.05970 0.12147  -0.03968 101 GLU A CA  
788 C C   . GLU A 105 ? 1.19662 0.91951 1.05086 -0.07721 0.11708  -0.05295 101 GLU A C   
789 O O   . GLU A 105 ? 1.10869 0.84559 0.96424 -0.08061 0.10880  -0.06260 101 GLU A O   
790 C CB  . GLU A 105 ? 1.37993 1.05045 1.20403 -0.05694 0.13731  -0.03980 101 GLU A CB  
791 C CG  . GLU A 105 ? 1.50624 1.16467 1.33040 -0.06771 0.14037  -0.05482 101 GLU A CG  
792 C CD  . GLU A 105 ? 1.46061 1.08413 1.28419 -0.07524 0.15826  -0.05806 101 GLU A CD  
793 O OE1 . GLU A 105 ? 1.38603 0.98103 1.19344 -0.06360 0.17036  -0.04933 101 GLU A OE1 
794 O OE2 . GLU A 105 ? 1.36607 0.99099 1.20599 -0.09247 0.16084  -0.06931 101 GLU A OE2 
795 N N   . ASP A 106 ? 1.20435 0.92705 1.07133 -0.08743 0.12242  -0.05371 102 ASP A N   
796 C CA  . ASP A 106 ? 1.15477 0.89442 1.03924 -0.10421 0.11859  -0.06712 102 ASP A CA  
797 C C   . ASP A 106 ? 1.08189 0.85940 0.97518 -0.10396 0.10227  -0.06831 102 ASP A C   
798 O O   . ASP A 106 ? 1.06408 0.86085 0.97162 -0.11590 0.09771  -0.07903 102 ASP A O   
799 C CB  . ASP A 106 ? 1.16223 0.89321 1.05905 -0.11431 0.12949  -0.06591 102 ASP A CB  
800 C CG  . ASP A 106 ? 1.33321 1.02491 1.22084 -0.11224 0.14803  -0.06089 102 ASP A CG  
801 O OD1 . ASP A 106 ? 1.41474 1.08936 1.28406 -0.09703 0.15148  -0.05116 102 ASP A OD1 
802 O OD2 . ASP A 106 ? 1.45323 1.13147 1.35244 -0.12543 0.15983  -0.06645 102 ASP A OD2 
803 N N   . MET A 107 ? 0.96871 0.75752 0.85474 -0.09054 0.09406  -0.05788 103 MET A N   
804 C CA  . MET A 107 ? 0.93403 0.75540 0.82799 -0.08837 0.08048  -0.05602 103 MET A CA  
805 C C   . MET A 107 ? 0.88697 0.72398 0.79544 -0.09483 0.07872  -0.05425 103 MET A C   
806 O O   . MET A 107 ? 0.79156 0.65601 0.70922 -0.09709 0.06888  -0.05683 103 MET A O   
807 C CB  . MET A 107 ? 0.91084 0.75023 0.80624 -0.09218 0.07240  -0.06768 103 MET A CB  
808 C CG  . MET A 107 ? 1.03188 0.87433 0.91545 -0.07986 0.06711  -0.06309 103 MET A CG  
809 S SD  . MET A 107 ? 1.06185 0.91134 0.94447 -0.06617 0.06261  -0.04545 103 MET A SD  
810 C CE  . MET A 107 ? 0.82978 0.64850 0.69583 -0.05600 0.07198  -0.03938 103 MET A CE  
811 N N   . LYS A 108 ? 0.89860 0.71880 0.80837 -0.09651 0.08877  -0.04919 104 LYS A N   
812 C CA  . LYS A 108 ? 0.80033 0.63383 0.72243 -0.10072 0.08831  -0.04582 104 LYS A CA  
813 C C   . LYS A 108 ? 0.74046 0.57508 0.65761 -0.08694 0.08587  -0.03190 104 LYS A C   
814 O O   . LYS A 108 ? 0.65171 0.46880 0.55624 -0.07594 0.09002  -0.02483 104 LYS A O   
815 C CB  . LYS A 108 ? 0.85565 0.67171 0.78419 -0.11165 0.10208  -0.04928 104 LYS A CB  
816 C CG  . LYS A 108 ? 0.88846 0.71756 0.83227 -0.12870 0.10141  -0.06488 104 LYS A CG  
817 C CD  . LYS A 108 ? 0.88996 0.71405 0.84726 -0.13957 0.11246  -0.06539 104 LYS A CD  
818 C CE  . LYS A 108 ? 0.94096 0.78907 0.91753 -0.15589 0.10835  -0.08120 104 LYS A CE  
819 N NZ  . LYS A 108 ? 0.90985 0.75216 0.90211 -0.16837 0.12094  -0.08280 104 LYS A NZ  
820 N N   . ILE A 109 ? 0.70825 0.56487 0.63557 -0.08696 0.07876  -0.02896 105 ILE A N   
821 C CA  . ILE A 109 ? 0.71054 0.57205 0.63552 -0.07427 0.07436  -0.01821 105 ILE A CA  
822 C C   . ILE A 109 ? 0.75477 0.59863 0.67536 -0.06978 0.08537  -0.01122 105 ILE A C   
823 O O   . ILE A 109 ? 0.75277 0.59714 0.68114 -0.07754 0.09169  -0.01213 105 ILE A O   
824 C CB  . ILE A 109 ? 0.67527 0.56470 0.61212 -0.07518 0.06363  -0.01778 105 ILE A CB  
825 C CG1 . ILE A 109 ? 0.63335 0.54025 0.57308 -0.07770 0.05426  -0.02336 105 ILE A CG1 
826 C CG2 . ILE A 109 ? 0.67965 0.57287 0.61528 -0.06233 0.05897  -0.00849 105 ILE A CG2 
827 C CD1 . ILE A 109 ? 0.70005 0.63203 0.64871 -0.07466 0.04404  -0.02050 105 ILE A CD1 
828 N N   . THR A 110 ? 0.69057 0.52031 0.59873 -0.05628 0.08808  -0.00405 106 THR A N   
829 C CA  . THR A 110 ? 0.72386 0.53923 0.62519 -0.04750 0.09797  0.00407  106 THR A CA  
830 C C   . THR A 110 ? 0.73461 0.56683 0.63940 -0.03710 0.09025  0.00992  106 THR A C   
831 O O   . THR A 110 ? 0.72613 0.55739 0.63197 -0.03430 0.09616  0.01475  106 THR A O   
832 C CB  . THR A 110 ? 0.82212 0.61430 0.70647 -0.03611 0.10561  0.00822  106 THR A CB  
833 O OG1 . THR A 110 ? 0.87180 0.67439 0.75214 -0.02470 0.09499  0.00984  106 THR A OG1 
834 C CG2 . THR A 110 ? 0.83448 0.60855 0.71474 -0.04565 0.11291  0.00159  106 THR A CG2 
835 N N   . SER A 111 ? 0.72805 0.57548 0.63532 -0.03117 0.07769  0.00938  107 SER A N   
836 C CA  . SER A 111 ? 0.71713 0.58035 0.62932 -0.02169 0.06933  0.01286  107 SER A CA  
837 C C   . SER A 111 ? 0.60886 0.49295 0.53304 -0.02632 0.05655  0.00930  107 SER A C   
838 O O   . SER A 111 ? 0.53209 0.41755 0.45650 -0.02980 0.05293  0.00632  107 SER A O   
839 C CB  . SER A 111 ? 0.58262 0.44000 0.48474 -0.00488 0.06878  0.01687  107 SER A CB  
840 O OG  . SER A 111 ? 0.84397 0.71309 0.74941 0.00506  0.06397  0.01942  107 SER A OG  
841 N N   . TYR A 112 ? 0.56800 0.46787 0.50135 -0.02516 0.05054  0.01032  108 TYR A N   
842 C CA  . TYR A 112 ? 0.58241 0.50120 0.52709 -0.02806 0.03973  0.00838  108 TYR A CA  
843 C C   . TYR A 112 ? 0.54540 0.47410 0.49539 -0.01815 0.03329  0.01086  108 TYR A C   
844 O O   . TYR A 112 ? 0.61512 0.54919 0.56743 -0.01760 0.03460  0.01217  108 TYR A O   
845 C CB  . TYR A 112 ? 0.54134 0.47123 0.49331 -0.04064 0.03972  0.00477  108 TYR A CB  
846 C CG  . TYR A 112 ? 0.54373 0.49105 0.50394 -0.04346 0.03063  0.00299  108 TYR A CG  
847 C CD1 . TYR A 112 ? 0.52292 0.48051 0.48973 -0.03599 0.02261  0.00610  108 TYR A CD1 
848 C CD2 . TYR A 112 ? 0.64792 0.60149 0.60936 -0.05281 0.03065  -0.00203 108 TYR A CD2 
849 C CE1 . TYR A 112 ? 0.53251 0.50411 0.50623 -0.03739 0.01629  0.00621  108 TYR A CE1 
850 C CE2 . TYR A 112 ? 0.66474 0.63508 0.63183 -0.05302 0.02336  -0.00245 108 TYR A CE2 
851 C CZ  . TYR A 112 ? 0.62646 0.60483 0.59935 -0.04511 0.01690  0.00267  108 TYR A CZ  
852 O OH  . TYR A 112 ? 0.63094 0.62419 0.60886 -0.04416 0.01150  0.00390  108 TYR A OH  
853 N N   . GLU A 113 ? 0.58724 0.51893 0.54015 -0.01042 0.02657  0.01085  109 GLU A N   
854 C CA  . GLU A 113 ? 0.62673 0.56729 0.58612 -0.00076 0.01972  0.01092  109 GLU A CA  
855 C C   . GLU A 113 ? 0.56307 0.51662 0.53589 -0.00367 0.01122  0.01006  109 GLU A C   
856 O O   . GLU A 113 ? 0.56086 0.51460 0.53706 -0.00662 0.00946  0.01003  109 GLU A O   
857 C CB  . GLU A 113 ? 0.57450 0.50932 0.52912 0.01126  0.01895  0.01007  109 GLU A CB  
858 C CG  . GLU A 113 ? 0.78283 0.72689 0.74318 0.02253  0.01229  0.00787  109 GLU A CG  
859 C CD  . GLU A 113 ? 0.97262 0.92007 0.93886 0.03042  0.00620  0.00376  109 GLU A CD  
860 O OE1 . GLU A 113 ? 1.12763 1.06758 1.08561 0.03422  0.00991  0.00382  109 GLU A OE1 
861 O OE2 . GLU A 113 ? 0.92459 0.88239 0.90460 0.03279  -0.00200 0.00001  109 GLU A OE2 
862 N N   . VAL A 114 ? 0.44961 0.41350 0.42954 -0.00188 0.00685  0.01012  110 VAL A N   
863 C CA  . VAL A 114 ? 0.52554 0.50014 0.51787 -0.00283 -0.00011 0.01025  110 VAL A CA  
864 C C   . VAL A 114 ? 0.52725 0.50467 0.52725 0.00728  -0.00628 0.00772  110 VAL A C   
865 O O   . VAL A 114 ? 0.52825 0.50826 0.52577 0.01348  -0.00705 0.00660  110 VAL A O   
866 C CB  . VAL A 114 ? 0.49128 0.47672 0.48597 -0.00881 -0.00030 0.01165  110 VAL A CB  
867 C CG1 . VAL A 114 ? 0.49096 0.48602 0.49707 -0.00658 -0.00671 0.01288  110 VAL A CG1 
868 C CG2 . VAL A 114 ? 0.46505 0.45069 0.45475 -0.01905 0.00444  0.01155  110 VAL A CG2 
869 N N   . ASN A 115 ? 0.61691 0.59453 0.62708 0.00907  -0.01040 0.00629  111 ASN A N   
870 C CA  . ASN A 115 ? 0.58506 0.56573 0.60605 0.01747  -0.01673 0.00146  111 ASN A CA  
871 C C   . ASN A 115 ? 0.60218 0.58865 0.63723 0.01562  -0.02091 0.00251  111 ASN A C   
872 O O   . ASN A 115 ? 0.52390 0.51005 0.56598 0.01037  -0.01980 0.00611  111 ASN A O   
873 C CB  . ASN A 115 ? 0.59573 0.57294 0.62107 0.02058  -0.01761 -0.00201 111 ASN A CB  
874 C CG  . ASN A 115 ? 0.73482 0.71721 0.77501 0.02802  -0.02471 -0.00946 111 ASN A CG  
875 O OD1 . ASN A 115 ? 0.82710 0.81194 0.88350 0.02538  -0.02787 -0.01012 111 ASN A OD1 
876 N ND2 . ASN A 115 ? 0.69996 0.68421 0.73498 0.03803  -0.02683 -0.01552 111 ASN A ND2 
877 N N   . LEU A 116 ? 0.53615 0.52753 0.57444 0.02111  -0.02497 0.00002  112 LEU A N   
878 C CA  . LEU A 116 ? 0.56366 0.55912 0.61357 0.02085  -0.02819 0.00139  112 LEU A CA  
879 C C   . LEU A 116 ? 0.64761 0.64229 0.71313 0.02732  -0.03418 -0.00573 112 LEU A C   
880 O O   . LEU A 116 ? 0.68496 0.68060 0.76090 0.02839  -0.03651 -0.00529 112 LEU A O   
881 C CB  . LEU A 116 ? 0.50605 0.50858 0.54875 0.02192  -0.02813 0.00385  112 LEU A CB  
882 C CG  . LEU A 116 ? 0.57562 0.58115 0.60542 0.01490  -0.02239 0.00853  112 LEU A CG  
883 C CD1 . LEU A 116 ? 0.45309 0.46573 0.47608 0.01803  -0.02196 0.00857  112 LEU A CD1 
884 C CD2 . LEU A 116 ? 0.48203 0.49210 0.51421 0.00799  -0.02058 0.01377  112 LEU A CD2 
885 N N   . GLU A 117 ? 0.63058 0.62403 0.69846 0.03212  -0.03663 -0.01301 113 GLU A N   
886 C CA  . GLU A 117 ? 0.83271 0.82750 0.91786 0.03774  -0.04302 -0.02258 113 GLU A CA  
887 C C   . GLU A 117 ? 0.98108 0.97174 1.08506 0.03137  -0.04177 -0.02200 113 GLU A C   
888 O O   . GLU A 117 ? 1.06396 1.05325 1.18621 0.03206  -0.04474 -0.02636 113 GLU A O   
889 C CB  . GLU A 117 ? 0.74911 0.74817 0.82948 0.04725  -0.04681 -0.03201 113 GLU A CB  
890 C CG  . GLU A 117 ? 0.98042 0.97754 1.05293 0.04602  -0.04296 -0.03087 113 GLU A CG  
891 C CD  . GLU A 117 ? 1.21526 1.21373 1.30580 0.04433  -0.04521 -0.03717 113 GLU A CD  
892 O OE1 . GLU A 117 ? 1.21012 1.20844 1.32140 0.04078  -0.04782 -0.04041 113 GLU A OE1 
893 O OE2 . GLU A 117 ? 1.18801 1.18751 1.27254 0.04655  -0.04353 -0.03858 113 GLU A OE2 
894 N N   . GLY A 118 ? 0.95173 0.93981 1.05215 0.02547  -0.03670 -0.01660 114 GLY A N   
895 C CA  . GLY A 118 ? 0.94176 0.92677 1.05940 0.01982  -0.03399 -0.01436 114 GLY A CA  
896 C C   . GLY A 118 ? 0.98932 0.97593 1.10909 0.01982  -0.03347 -0.01855 114 GLY A C   
897 O O   . GLY A 118 ? 1.00389 0.99439 1.13933 0.02302  -0.03786 -0.02876 114 GLY A O   
898 C C1  . GG2 B .   ? 0.61910 0.65749 0.66708 0.01673  -0.02357 0.03093  201 GG2 A C1  
899 C C2  . GG2 B .   ? 0.57129 0.60382 0.61929 0.01791  -0.02619 0.02448  201 GG2 A C2  
900 C C3  . GG2 B .   ? 0.63314 0.66906 0.67151 0.01357  -0.02481 0.02138  201 GG2 A C3  
901 O O4  . GG2 B .   ? 0.63728 0.67018 0.69499 0.02196  -0.02293 0.03576  201 GG2 A O4  
902 N N6  . GG2 B .   ? 0.49697 0.54807 0.51755 0.00322  -0.01837 0.01836  201 GG2 A N6  
903 C C7  . GG2 B .   ? 0.44069 0.46967 0.44693 -0.02337 -0.00566 0.01655  201 GG2 A C7  
904 C C8  . GG2 B .   ? 0.40977 0.44476 0.42605 -0.01135 -0.01211 0.01916  201 GG2 A C8  
905 C C10 . GG2 B .   ? 0.58660 0.63565 0.60102 -0.00315 -0.01343 0.01661  201 GG2 A C10 
906 C C11 . GG2 B .   ? 0.54002 0.59359 0.55066 -0.00248 -0.01017 0.01592  201 GG2 A C11 
907 C C12 . GG2 B .   ? 0.56403 0.60520 0.57564 -0.01059 -0.01022 0.01594  201 GG2 A C12 
908 C C13 . GG2 B .   ? 0.57521 0.61612 0.59267 -0.00689 -0.01408 0.01842  201 GG2 A C13 
909 C C14 . GG2 B .   ? 0.53119 0.56689 0.52995 -0.03170 -0.00252 0.01411  201 GG2 A C14 
910 C C15 . GG2 B .   ? 0.55112 0.59477 0.60525 0.02497  -0.02058 0.04296  201 GG2 A C15 
911 C C16 . GG2 B .   ? 0.46465 0.48660 0.46406 -0.02802 -0.00191 0.01703  201 GG2 A C16 
912 C C19 . GG2 B .   ? 0.51728 0.52150 0.50587 -0.03158 0.00365  0.01469  201 GG2 A C19 
913 C C20 . GG2 B .   ? 0.49296 0.52508 0.48853 -0.02664 -0.00084 0.02093  201 GG2 A C20 
914 C C21 . GG2 B .   ? 0.52663 0.56218 0.51310 -0.03135 0.00124  0.01585  201 GG2 A C21 
915 C C22 . GG2 B .   ? 0.42934 0.44542 0.43713 -0.02003 -0.00565 0.01802  201 GG2 A C22 
916 C C24 . GG2 B .   ? 0.61585 0.65268 0.62043 -0.02535 -0.00362 0.01305  201 GG2 A C24 
917 C C4  . GG2 B .   ? 0.54238 0.58709 0.57321 0.00630  -0.02132 0.02302  201 GG2 A C4  
918 C C5  . GG2 B .   ? 0.50851 0.56132 0.53972 0.00497  -0.02023 0.02744  201 GG2 A C5  
919 C C6  . GG2 B .   ? 0.57942 0.62923 0.61815 0.01103  -0.02108 0.03225  201 GG2 A C6  
920 N N1  . GG2 B .   ? 0.58483 0.63073 0.60773 0.00082  -0.01827 0.01979  201 GG2 A N1  
921 N N5  . GG2 B .   ? 0.60413 0.63789 0.61301 -0.01992 -0.00747 0.01636  201 GG2 A N5  
922 C C44 . GG2 B .   ? 0.52799 0.56726 0.53049 -0.02967 -0.00410 0.01430  201 GG2 A C44 
923 N N2  . GG2 B .   ? 0.56377 0.58303 0.55877 -0.02930 0.00012  0.01738  201 GG2 A N2  
924 C C18 . GG2 B .   ? 0.50803 0.52073 0.51278 -0.02261 -0.00351 0.01871  201 GG2 A C18 
925 O O3  . GG2 B .   ? 0.53171 0.56183 0.55466 -0.00730 -0.01395 0.02238  201 GG2 A O3  
926 C C25 . GG2 B .   ? 0.52059 0.53931 0.50099 -0.03364 0.00473  0.01355  201 GG2 A C25 
927 O O2  . GG2 B .   ? 0.46461 0.45855 0.45116 -0.03191 0.00529  0.01267  201 GG2 A O2  
928 C C23 . GG2 B .   ? 0.41443 0.41669 0.39765 -0.03188 0.00569  0.01502  201 GG2 A C23 
929 O O1  . GG2 B .   ? 0.54604 0.60188 0.55368 -0.01049 -0.00449 0.01510  201 GG2 A O1  
930 N N3  . GG2 B .   ? 0.77923 0.83442 0.79064 0.00826  -0.01347 0.01609  201 GG2 A N3  
931 C C17 . GG2 B .   ? 0.43629 0.47036 0.44127 -0.01899 -0.00391 0.01363  201 GG2 A C17 
932 O O   . HOH C .   ? 0.48774 0.59010 0.50115 -0.02137 -0.01318 0.01597  301 HOH A O   
933 O O   . HOH C .   ? 0.80622 0.85685 0.85639 0.05143  0.02761  0.11344  302 HOH A O   
934 O O   . HOH C .   ? 0.63869 0.78284 0.65674 -0.05698 -0.00425 -0.01127 303 HOH A O   
935 O O   . HOH C .   ? 0.57961 0.73374 0.60251 0.02583  -0.02793 0.03262  304 HOH A O   
936 O O   . HOH C .   ? 0.55217 0.49676 0.46223 0.09165  0.02978  0.01619  305 HOH A O   
937 O O   . HOH C .   ? 1.01306 0.69617 0.77737 -0.01621 0.11312  -0.05705 306 HOH A O   
938 O O   . HOH C .   ? 0.69100 0.72792 0.63105 -0.10197 0.01646  -0.11547 307 HOH A O   
939 O O   . HOH C .   ? 0.87824 0.88739 0.89224 -0.05856 0.11900  0.04149  308 HOH A O   
940 O O   . HOH C .   ? 0.53256 0.49105 0.52935 0.01190  -0.00262 0.00460  309 HOH A O   
941 O O   . HOH C .   ? 0.58181 0.58123 0.59711 0.00405  0.03035  0.06378  310 HOH A O   
942 O O   . HOH C .   ? 0.81831 0.84190 0.84605 0.07491  -0.04576 -0.02080 311 HOH A O   
943 O O   . HOH C .   ? 0.68634 0.66076 0.80006 0.08129  0.01052  0.09259  312 HOH A O   
944 O O   . HOH C .   ? 0.61339 0.60206 0.57546 0.00429  0.03045  0.04629  313 HOH A O   
945 O O   . HOH C .   ? 0.61847 0.73060 0.62516 0.04084  0.00593  0.08123  314 HOH A O   
946 O O   . HOH C .   ? 0.58825 0.65279 0.61452 0.03036  -0.02925 0.01661  315 HOH A O   
947 O O   . HOH C .   ? 0.53468 0.74783 0.56127 -0.00616 -0.02166 0.01323  316 HOH A O   
948 O O   . HOH C .   ? 0.61109 0.71701 0.64333 0.03595  -0.02839 0.03924  317 HOH A O   
949 O O   . HOH C .   ? 0.48589 0.73583 0.52246 -0.02606 -0.01764 -0.00115 318 HOH A O   
950 O O   . HOH C .   ? 0.79771 0.66632 0.68449 0.04714  0.12063  0.06223  319 HOH A O   
951 O O   . HOH C .   ? 0.82805 0.88833 0.87265 0.03637  -0.03298 0.02649  320 HOH A O   
# 
