data_9DA4
# 
_entry.id   9DA4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9DA4         pdb_00009da4 10.2210/pdb9da4/pdb 
WWPDB D_1000287633 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-05 ? 
2 'Structure model' 1 1 2025-02-26 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DA4 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-21 
_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           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'CRYSTAL STRUCTURE OF HUMAN DNPH1 (RCL) WITH 6-NAPHTHYL-PURINE-RIBOSIDE-MONOPHOSPHATE' 4P5E unspecified 
PDB 'Crystal structure of human DNPH1 bound to hmdUMP'                                     8QHQ unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              agnidipta.ghosh@einsteinmed.edu 
_pdbx_contact_author.name_first         Agnidipta 
_pdbx_contact_author.name_last          Ghosh 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7753-0240 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wagner, A.G.'  1 0000-0003-4786-7747 
'Schramm, V.L.' 2 0000-0002-8056-1929 
'Almo, S.C.'    3 0000-0003-2591-5234 
'Ghosh, A.'     4 0000-0002-7753-0240 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                3653 
_citation.page_last                 3672 
_citation.title                     'Transition State Analogs of Human DNPH1 Reveal Two Electrophile Migration Mechanisms.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02778 
_citation.pdbx_database_id_PubMed   39818772 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wagner, A.G.'         1  ? 
primary 'Lang, T.B.D.'         2  ? 
primary 'Ledingham, E.T.'      3  ? 
primary 'Ghosh, A.'            4  ? 
primary 'Brooks, D.'           5  ? 
primary 'Eskandari, R.'        6  ? 
primary 'Suthagar, K.'         7  ? 
primary 'Almo, S.C.'           8  ? 
primary 'Lamiable-Oulaidi, F.' 9  ? 
primary 'Tyler, P.C.'          10 ? 
primary 'Schramm, V.L.'        11 ? 
# 
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 '5-hydroxymethyl-dUMP N-hydrolase' 16224.247 1  3.2.2.- ? ? ? 
2 non-polymer syn 
'{(3R,4R)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-hydroxypyrrolidin-3-yl}methyl dihydrogen phosphate' 343.276   1  ? 
? ? ? 
3 water       nat water 18.015    78 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;2'-deoxynucleoside 5'-phosphate N-hydrolase 1,c-Myc-responsive protein RCL
;
# 
_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       
;SMRPALYFCGSIRGGREDRTLYERIVSRLRRFGTVLTEHVAAAELGARGEEAAGGDRLIHEQDLEWLQQADVVVAEVTQP
SLGVGYELGRAVAFNKRILCLFRPQSGRVLSAMIRGAADGSRFQVWDYEEGEVEALLDRYFEADP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMRPALYFCGSIRGGREDRTLYERIVSRLRRFGTVLTEHVAAAELGARGEEAAGGDRLIHEQDLEWLQQADVVVAEVTQP
SLGVGYELGRAVAFNKRILCLFRPQSGRVLSAMIRGAADGSRFQVWDYEEGEVEALLDRYFEADP
;
_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 '{(3R,4R)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-hydroxypyrrolidin-3-yl}methyl dihydrogen phosphate' A1BBE 
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   MET n 
1 3   ARG n 
1 4   PRO n 
1 5   ALA n 
1 6   LEU n 
1 7   TYR n 
1 8   PHE n 
1 9   CYS n 
1 10  GLY n 
1 11  SER n 
1 12  ILE n 
1 13  ARG n 
1 14  GLY n 
1 15  GLY n 
1 16  ARG n 
1 17  GLU n 
1 18  ASP n 
1 19  ARG n 
1 20  THR n 
1 21  LEU n 
1 22  TYR n 
1 23  GLU n 
1 24  ARG n 
1 25  ILE n 
1 26  VAL n 
1 27  SER n 
1 28  ARG n 
1 29  LEU n 
1 30  ARG n 
1 31  ARG n 
1 32  PHE n 
1 33  GLY n 
1 34  THR n 
1 35  VAL n 
1 36  LEU n 
1 37  THR n 
1 38  GLU n 
1 39  HIS n 
1 40  VAL n 
1 41  ALA n 
1 42  ALA n 
1 43  ALA n 
1 44  GLU n 
1 45  LEU n 
1 46  GLY n 
1 47  ALA n 
1 48  ARG n 
1 49  GLY n 
1 50  GLU n 
1 51  GLU n 
1 52  ALA n 
1 53  ALA n 
1 54  GLY n 
1 55  GLY n 
1 56  ASP n 
1 57  ARG n 
1 58  LEU n 
1 59  ILE n 
1 60  HIS n 
1 61  GLU n 
1 62  GLN n 
1 63  ASP n 
1 64  LEU n 
1 65  GLU n 
1 66  TRP n 
1 67  LEU n 
1 68  GLN n 
1 69  GLN n 
1 70  ALA n 
1 71  ASP n 
1 72  VAL n 
1 73  VAL n 
1 74  VAL n 
1 75  ALA n 
1 76  GLU n 
1 77  VAL n 
1 78  THR n 
1 79  GLN n 
1 80  PRO n 
1 81  SER n 
1 82  LEU n 
1 83  GLY n 
1 84  VAL n 
1 85  GLY n 
1 86  TYR n 
1 87  GLU n 
1 88  LEU n 
1 89  GLY n 
1 90  ARG n 
1 91  ALA n 
1 92  VAL n 
1 93  ALA n 
1 94  PHE n 
1 95  ASN n 
1 96  LYS n 
1 97  ARG n 
1 98  ILE n 
1 99  LEU n 
1 100 CYS n 
1 101 LEU n 
1 102 PHE n 
1 103 ARG n 
1 104 PRO n 
1 105 GLN n 
1 106 SER n 
1 107 GLY n 
1 108 ARG n 
1 109 VAL n 
1 110 LEU n 
1 111 SER n 
1 112 ALA n 
1 113 MET n 
1 114 ILE n 
1 115 ARG n 
1 116 GLY n 
1 117 ALA n 
1 118 ALA n 
1 119 ASP n 
1 120 GLY n 
1 121 SER n 
1 122 ARG n 
1 123 PHE n 
1 124 GLN n 
1 125 VAL n 
1 126 TRP n 
1 127 ASP n 
1 128 TYR n 
1 129 GLU n 
1 130 GLU n 
1 131 GLY n 
1 132 GLU n 
1 133 VAL n 
1 134 GLU n 
1 135 ALA n 
1 136 LEU n 
1 137 LEU n 
1 138 ASP n 
1 139 ARG n 
1 140 TYR n 
1 141 PHE n 
1 142 GLU n 
1 143 ALA n 
1 144 ASP n 
1 145 PRO 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                   145 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'DNPH1, C6orf108, RCL' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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              pRIL 
_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          Plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   LIC 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET-28a(+)' 
_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 
A1BBE non-polymer         . 
'{(3R,4R)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-hydroxypyrrolidin-3-yl}methyl dihydrogen phosphate' ? 
'C12 H18 N5 O5 P' 343.276 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'    121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER ? 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'     117.146 
# 
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   18  18  SER SER A . n 
A 1 2   MET 2   19  19  MET MET A . n 
A 1 3   ARG 3   20  20  ARG ARG A . n 
A 1 4   PRO 4   21  21  PRO PRO A . n 
A 1 5   ALA 5   22  22  ALA ALA A . n 
A 1 6   LEU 6   23  23  LEU LEU A . n 
A 1 7   TYR 7   24  24  TYR TYR A . n 
A 1 8   PHE 8   25  25  PHE PHE A . n 
A 1 9   CYS 9   26  26  CYS CYS A . n 
A 1 10  GLY 10  27  27  GLY GLY A . n 
A 1 11  SER 11  28  28  SER SER A . n 
A 1 12  ILE 12  29  29  ILE ILE A . n 
A 1 13  ARG 13  30  30  ARG ARG A . n 
A 1 14  GLY 14  31  31  GLY GLY A . n 
A 1 15  GLY 15  32  32  GLY GLY A . n 
A 1 16  ARG 16  33  33  ARG ARG A . n 
A 1 17  GLU 17  34  34  GLU GLU A . n 
A 1 18  ASP 18  35  35  ASP ASP A . n 
A 1 19  ARG 19  36  36  ARG ARG A . n 
A 1 20  THR 20  37  37  THR THR A . n 
A 1 21  LEU 21  38  38  LEU LEU A . n 
A 1 22  TYR 22  39  39  TYR TYR A . n 
A 1 23  GLU 23  40  40  GLU GLU A . n 
A 1 24  ARG 24  41  41  ARG ARG A . n 
A 1 25  ILE 25  42  42  ILE ILE A . n 
A 1 26  VAL 26  43  43  VAL VAL A . n 
A 1 27  SER 27  44  44  SER SER A . n 
A 1 28  ARG 28  45  45  ARG ARG A . n 
A 1 29  LEU 29  46  46  LEU LEU A . n 
A 1 30  ARG 30  47  47  ARG ARG A . n 
A 1 31  ARG 31  48  48  ARG ARG A . n 
A 1 32  PHE 32  49  49  PHE PHE A . n 
A 1 33  GLY 33  50  50  GLY GLY A . n 
A 1 34  THR 34  51  51  THR THR A . n 
A 1 35  VAL 35  52  52  VAL VAL A . n 
A 1 36  LEU 36  53  53  LEU LEU A . n 
A 1 37  THR 37  54  54  THR THR A . n 
A 1 38  GLU 38  55  55  GLU GLU A . n 
A 1 39  HIS 39  56  56  HIS HIS A . n 
A 1 40  VAL 40  57  57  VAL VAL A . n 
A 1 41  ALA 41  58  58  ALA ALA A . n 
A 1 42  ALA 42  59  59  ALA ALA A . n 
A 1 43  ALA 43  60  60  ALA ALA A . n 
A 1 44  GLU 44  61  61  GLU GLU A . n 
A 1 45  LEU 45  62  62  LEU LEU A . n 
A 1 46  GLY 46  63  63  GLY GLY A . n 
A 1 47  ALA 47  64  64  ALA ALA A . n 
A 1 48  ARG 48  65  65  ARG ARG A . n 
A 1 49  GLY 49  66  66  GLY GLY A . n 
A 1 50  GLU 50  67  67  GLU GLU A . n 
A 1 51  GLU 51  68  68  GLU GLU A . n 
A 1 52  ALA 52  69  69  ALA ALA A . n 
A 1 53  ALA 53  70  70  ALA ALA A . n 
A 1 54  GLY 54  71  71  GLY GLY A . n 
A 1 55  GLY 55  72  72  GLY GLY A . n 
A 1 56  ASP 56  73  73  ASP ASP A . n 
A 1 57  ARG 57  74  74  ARG ARG A . n 
A 1 58  LEU 58  75  75  LEU LEU A . n 
A 1 59  ILE 59  76  76  ILE ILE A . n 
A 1 60  HIS 60  77  77  HIS HIS A . n 
A 1 61  GLU 61  78  78  GLU GLU A . n 
A 1 62  GLN 62  79  79  GLN GLN A . n 
A 1 63  ASP 63  80  80  ASP ASP A . n 
A 1 64  LEU 64  81  81  LEU LEU A . n 
A 1 65  GLU 65  82  82  GLU GLU A . n 
A 1 66  TRP 66  83  83  TRP TRP A . n 
A 1 67  LEU 67  84  84  LEU LEU A . n 
A 1 68  GLN 68  85  85  GLN GLN A . n 
A 1 69  GLN 69  86  86  GLN GLN A . n 
A 1 70  ALA 70  87  87  ALA ALA A . n 
A 1 71  ASP 71  88  88  ASP ASP A . n 
A 1 72  VAL 72  89  89  VAL VAL A . n 
A 1 73  VAL 73  90  90  VAL VAL A . n 
A 1 74  VAL 74  91  91  VAL VAL A . n 
A 1 75  ALA 75  92  92  ALA ALA A . n 
A 1 76  GLU 76  93  93  GLU GLU A . n 
A 1 77  VAL 77  94  94  VAL VAL A . n 
A 1 78  THR 78  95  95  THR THR A . n 
A 1 79  GLN 79  96  96  GLN GLN A . n 
A 1 80  PRO 80  97  97  PRO PRO A . n 
A 1 81  SER 81  98  98  SER SER A . n 
A 1 82  LEU 82  99  99  LEU LEU A . n 
A 1 83  GLY 83  100 100 GLY GLY A . n 
A 1 84  VAL 84  101 101 VAL VAL A . n 
A 1 85  GLY 85  102 102 GLY GLY A . n 
A 1 86  TYR 86  103 103 TYR TYR A . n 
A 1 87  GLU 87  104 104 GLU GLU A . n 
A 1 88  LEU 88  105 105 LEU LEU A . n 
A 1 89  GLY 89  106 106 GLY GLY A . n 
A 1 90  ARG 90  107 107 ARG ARG A . n 
A 1 91  ALA 91  108 108 ALA ALA A . n 
A 1 92  VAL 92  109 109 VAL VAL A . n 
A 1 93  ALA 93  110 110 ALA ALA A . n 
A 1 94  PHE 94  111 111 PHE PHE A . n 
A 1 95  ASN 95  112 112 ASN ASN A . n 
A 1 96  LYS 96  113 113 LYS LYS A . n 
A 1 97  ARG 97  114 114 ARG ARG A . n 
A 1 98  ILE 98  115 115 ILE ILE A . n 
A 1 99  LEU 99  116 116 LEU LEU A . n 
A 1 100 CYS 100 117 117 CYS CYS A . n 
A 1 101 LEU 101 118 118 LEU LEU A . n 
A 1 102 PHE 102 119 119 PHE PHE A . n 
A 1 103 ARG 103 120 120 ARG ARG A . n 
A 1 104 PRO 104 121 121 PRO PRO A . n 
A 1 105 GLN 105 122 122 GLN GLN A . n 
A 1 106 SER 106 123 123 SER SER A . n 
A 1 107 GLY 107 124 124 GLY GLY A . n 
A 1 108 ARG 108 125 125 ARG ARG A . n 
A 1 109 VAL 109 126 126 VAL VAL A . n 
A 1 110 LEU 110 127 127 LEU LEU A . n 
A 1 111 SER 111 128 128 SER SER A . n 
A 1 112 ALA 112 129 129 ALA ALA A . n 
A 1 113 MET 113 130 130 MET MET A . n 
A 1 114 ILE 114 131 131 ILE ILE A . n 
A 1 115 ARG 115 132 132 ARG ARG A . n 
A 1 116 GLY 116 133 133 GLY GLY A . n 
A 1 117 ALA 117 134 134 ALA ALA A . n 
A 1 118 ALA 118 135 135 ALA ALA A . n 
A 1 119 ASP 119 136 136 ASP ASP A . n 
A 1 120 GLY 120 137 137 GLY GLY A . n 
A 1 121 SER 121 138 138 SER SER A . n 
A 1 122 ARG 122 139 139 ARG ARG A . n 
A 1 123 PHE 123 140 140 PHE PHE A . n 
A 1 124 GLN 124 141 141 GLN GLN A . n 
A 1 125 VAL 125 142 142 VAL VAL A . n 
A 1 126 TRP 126 143 143 TRP TRP A . n 
A 1 127 ASP 127 144 144 ASP ASP A . n 
A 1 128 TYR 128 145 145 TYR TYR A . n 
A 1 129 GLU 129 146 146 GLU GLU A . n 
A 1 130 GLU 130 147 147 GLU GLU A . n 
A 1 131 GLY 131 148 148 GLY GLY A . n 
A 1 132 GLU 132 149 149 GLU GLU A . n 
A 1 133 VAL 133 150 150 VAL VAL A . n 
A 1 134 GLU 134 151 151 GLU GLU A . n 
A 1 135 ALA 135 152 152 ALA ALA A . n 
A 1 136 LEU 136 153 153 LEU LEU A . n 
A 1 137 LEU 137 154 154 LEU LEU A . n 
A 1 138 ASP 138 155 155 ASP ASP A . n 
A 1 139 ARG 139 156 156 ARG ARG A . n 
A 1 140 TYR 140 157 157 TYR TYR A . n 
A 1 141 PHE 141 158 158 PHE PHE A . n 
A 1 142 GLU 142 159 159 GLU GLU A . n 
A 1 143 ALA 143 160 ?   ?   ?   A . n 
A 1 144 ASP 144 161 ?   ?   ?   A . n 
A 1 145 PRO 145 162 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BBE 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BBE 
_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 A1BBE 1  201 201 A1BBE DIP A . 
C 3 HOH   1  301 50  HOH   HOH A . 
C 3 HOH   2  302 33  HOH   HOH A . 
C 3 HOH   3  303 13  HOH   HOH A . 
C 3 HOH   4  304 24  HOH   HOH A . 
C 3 HOH   5  305 26  HOH   HOH A . 
C 3 HOH   6  306 25  HOH   HOH A . 
C 3 HOH   7  307 23  HOH   HOH A . 
C 3 HOH   8  308 77  HOH   HOH A . 
C 3 HOH   9  309 64  HOH   HOH A . 
C 3 HOH   10 310 48  HOH   HOH A . 
C 3 HOH   11 311 11  HOH   HOH A . 
C 3 HOH   12 312 34  HOH   HOH A . 
C 3 HOH   13 313 15  HOH   HOH A . 
C 3 HOH   14 314 76  HOH   HOH A . 
C 3 HOH   15 315 66  HOH   HOH A . 
C 3 HOH   16 316 44  HOH   HOH A . 
C 3 HOH   17 317 19  HOH   HOH A . 
C 3 HOH   18 318 45  HOH   HOH A . 
C 3 HOH   19 319 56  HOH   HOH A . 
C 3 HOH   20 320 4   HOH   HOH A . 
C 3 HOH   21 321 51  HOH   HOH A . 
C 3 HOH   22 322 65  HOH   HOH A . 
C 3 HOH   23 323 2   HOH   HOH A . 
C 3 HOH   24 324 37  HOH   HOH A . 
C 3 HOH   25 325 71  HOH   HOH A . 
C 3 HOH   26 326 75  HOH   HOH A . 
C 3 HOH   27 327 3   HOH   HOH A . 
C 3 HOH   28 328 62  HOH   HOH A . 
C 3 HOH   29 329 55  HOH   HOH A . 
C 3 HOH   30 330 12  HOH   HOH A . 
C 3 HOH   31 331 43  HOH   HOH A . 
C 3 HOH   32 332 20  HOH   HOH A . 
C 3 HOH   33 333 63  HOH   HOH A . 
C 3 HOH   34 334 18  HOH   HOH A . 
C 3 HOH   35 335 52  HOH   HOH A . 
C 3 HOH   36 336 42  HOH   HOH A . 
C 3 HOH   37 337 41  HOH   HOH A . 
C 3 HOH   38 338 5   HOH   HOH A . 
C 3 HOH   39 339 1   HOH   HOH A . 
C 3 HOH   40 340 46  HOH   HOH A . 
C 3 HOH   41 341 9   HOH   HOH A . 
C 3 HOH   42 342 10  HOH   HOH A . 
C 3 HOH   43 343 22  HOH   HOH A . 
C 3 HOH   44 344 72  HOH   HOH A . 
C 3 HOH   45 345 30  HOH   HOH A . 
C 3 HOH   46 346 6   HOH   HOH A . 
C 3 HOH   47 347 54  HOH   HOH A . 
C 3 HOH   48 348 31  HOH   HOH A . 
C 3 HOH   49 349 61  HOH   HOH A . 
C 3 HOH   50 350 59  HOH   HOH A . 
C 3 HOH   51 351 49  HOH   HOH A . 
C 3 HOH   52 352 14  HOH   HOH A . 
C 3 HOH   53 353 8   HOH   HOH A . 
C 3 HOH   54 354 47  HOH   HOH A . 
C 3 HOH   55 355 21  HOH   HOH A . 
C 3 HOH   56 356 74  HOH   HOH A . 
C 3 HOH   57 357 68  HOH   HOH A . 
C 3 HOH   58 358 36  HOH   HOH A . 
C 3 HOH   59 359 57  HOH   HOH A . 
C 3 HOH   60 360 16  HOH   HOH A . 
C 3 HOH   61 361 38  HOH   HOH A . 
C 3 HOH   62 362 27  HOH   HOH A . 
C 3 HOH   63 363 69  HOH   HOH A . 
C 3 HOH   64 364 7   HOH   HOH A . 
C 3 HOH   65 365 35  HOH   HOH A . 
C 3 HOH   66 366 40  HOH   HOH A . 
C 3 HOH   67 367 28  HOH   HOH A . 
C 3 HOH   68 368 17  HOH   HOH A . 
C 3 HOH   69 369 39  HOH   HOH A . 
C 3 HOH   70 370 78  HOH   HOH A . 
C 3 HOH   71 371 29  HOH   HOH A . 
C 3 HOH   72 372 53  HOH   HOH A . 
C 3 HOH   73 373 58  HOH   HOH A . 
C 3 HOH   74 374 67  HOH   HOH A . 
C 3 HOH   75 375 70  HOH   HOH A . 
C 3 HOH   76 376 32  HOH   HOH A . 
C 3 HOH   77 377 73  HOH   HOH A . 
C 3 HOH   78 378 60  HOH   HOH A . 
# 
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  ? ? ? 1.20.1_4487 1 
? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           2 
? phasing        ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           3 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DA4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     83.304 
_cell.length_a_esd                 ? 
_cell.length_b                     83.304 
_cell.length_b_esd                 ? 
_cell.length_c                     80.587 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9DA4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                178 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 61 2 2' 
_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                   9DA4 
_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             2.49 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.55 
_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              5.5 
_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    '25% (w/v) PEG 3350, 0.2 M Ammonium acetate and 0.1 M Bis-Tris' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_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 EIGER X 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         2023-12-13 
_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   0.92 
_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                        'NSLS-II BEAMLINE 17-ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.92 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-1 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DA4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.73 
_reflns.d_resolution_low                               27.27 
_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                                     17730 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                21.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.00 
_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                                0.104 
_reflns.pdbx_Rpim_I_all                                0.022 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       388195 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.101 
_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                                    1.73 
_reflns_shell.d_res_low                                     1.77 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           19254 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             951 
_reflns_shell.percent_possible_obs                          99.7 
_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                               20.2 
_reflns_shell.pdbx_chi_squared                              0.98 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     3.9 
_reflns_shell.pdbx_Rrim_I_all                               0.849 
_reflns_shell.pdbx_Rpim_I_all                               0.186 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.938 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.828 
_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                               ? 
_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                                 9DA4 
_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                            1.73 
_refine.ls_d_res_low                             27.27 
_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                     17684 
_refine.ls_number_reflns_R_free                  853 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.94 
_refine.ls_percent_reflns_R_free                 4.82 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1863 
_refine.ls_R_factor_R_free                       0.2296 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1840 
_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                          1.34 
_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       ML 
_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             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 23.63 
_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                            0.13 
_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                       1.73 
_refine_hist.d_res_low                        27.27 
_refine_hist.number_atoms_solvent             78 
_refine_hist.number_atoms_total               1222 
_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        1121 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         23 
_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' ? 0.006 ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.956 ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.834 ? 167 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.058 ? 167 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.011 ? 206 ? f_plane_restr      ? ? 
# 
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' 1.73 1.84  . . 130 2740 100.00 . . . . 0.1909 . . . . . . . . . . . 0.2485 
'X-RAY DIFFRACTION' 1.84 1.98  . . 149 2745 100.00 . . . . 0.2028 . . . . . . . . . . . 0.2494 
'X-RAY DIFFRACTION' 1.98 2.18  . . 115 2784 100.00 . . . . 0.1965 . . . . . . . . . . . 0.2602 
'X-RAY DIFFRACTION' 2.18 2.50  . . 128 2779 100.00 . . . . 0.1890 . . . . . . . . . . . 0.2318 
'X-RAY DIFFRACTION' 2.50 3.15  . . 167 2802 100.00 . . . . 0.2031 . . . . . . . . . . . 0.2499 
'X-RAY DIFFRACTION' 3.15 27.27 . . 164 2981 100.00 . . . . 0.1688 . . . . . . . . . . . 0.2102 
# 
_struct.entry_id                     9DA4 
_struct.title                        'Crystal structure of human DNPH1 bound to inhibitor 2b' 
_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        9DA4 
_struct_keywords.text            'Inhibitor, Complex, HYDROLASE, HYDROLASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   HYDROLASE/INHIBITOR 
# 
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                    UNP 
_struct_ref.db_code                    DNPH1_HUMAN 
_struct_ref.pdbx_db_accession          O43598 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;RPALYFCGSIRGGREDRTLYERIVSRLRRFGTVLTEHVAAAELGARGEEAAGGDRLIHEQDLEWLQQADVVVAEVTQPSL
GVGYELGRAVAFNKRILCLFRPQSGRVLSAMIRGAADGSRFQVWDYEEGEVEALLDRYFEADP
;
_struct_ref.pdbx_align_begin           20 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9DA4 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 3 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 145 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             O43598 
_struct_ref_seq.db_align_beg                  20 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  162 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       20 
_struct_ref_seq.pdbx_auth_seq_align_end       162 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9DA4 SER A 1 ? UNP O43598 ? ? 'expression tag' 18 1 
1 9DA4 MET A 2 ? UNP O43598 ? ? 'expression tag' 19 2 
# 
_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   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3180  ? 
1 MORE         -32   ? 
1 'SSA (A^2)'  12570 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                'Superdex S200' 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z          1.0000000000 0.0000000000 0.0000000000 0.0000000000   0.0000000000 
1.0000000000  0.0000000000 0.0000000000  0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 12_565 x,x-y+1,-z+1/6 0.5000000000 0.8660254038 0.0000000000 -41.6520000000 0.8660254038 
-0.5000000000 0.0000000000 72.1433802369 0.0000000000 0.0000000000 -1.0000000000 13.4311666667 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 18  ? ARG A 30  ? ASP A 35  ARG A 47  1 ? 13 
HELX_P HELX_P2 AA2 THR A 37  ? ALA A 41  ? THR A 54  ALA A 58  5 ? 5  
HELX_P HELX_P3 AA3 GLY A 46  ? ALA A 53  ? GLY A 63  ALA A 70  1 ? 8  
HELX_P HELX_P4 AA4 GLY A 55  ? ALA A 70  ? GLY A 72  ALA A 87  1 ? 16 
HELX_P HELX_P5 AA5 SER A 81  ? PHE A 94  ? SER A 98  PHE A 111 1 ? 14 
HELX_P HELX_P6 AA6 ARG A 103 ? GLY A 107 ? ARG A 120 GLY A 124 5 ? 5  
HELX_P HELX_P7 AA7 SER A 111 ? GLY A 116 ? SER A 128 GLY A 133 1 ? 6  
HELX_P HELX_P8 AA8 GLU A 129 ? GLY A 131 ? GLU A 146 GLY A 148 5 ? 3  
HELX_P HELX_P9 AA9 GLU A 132 ? PHE A 141 ? GLU A 149 PHE A 158 1 ? 10 
# 
_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   5 
_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 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? 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 THR A 34  ? VAL A 35  ? THR A 51  VAL A 52  
AA1 2 ALA A 5   ? CYS A 9   ? ALA A 22  CYS A 26  
AA1 3 VAL A 72  ? GLU A 76  ? VAL A 89  GLU A 93  
AA1 4 ARG A 97  ? PHE A 102 ? ARG A 114 PHE A 119 
AA1 5 PHE A 123 ? ASP A 127 ? PHE A 140 ASP A 144 
# 
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 THR A 34  ? O THR A 51  N LEU A 6   ? N LEU A 23  
AA1 2 3 N TYR A 7   ? N TYR A 24  O VAL A 74  ? O VAL A 91  
AA1 3 4 N ALA A 75  ? N ALA A 92  O LEU A 99  ? O LEU A 116 
AA1 4 5 N CYS A 100 ? N CYS A 117 O GLN A 124 ? O GLN A 141 
# 
_pdbx_entry_details.entry_id                   9DA4 
_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 
# 
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 ILE A 29  ? ? -122.81 -73.81 
2 1 SER A 128 ? ? -31.03  129.58 
3 1 SER A 138 ? ? -135.71 -80.92 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 339 ? C HOH . 
2 1 A HOH 375 ? C HOH . 
3 1 A HOH 376 ? C HOH . 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -19.1700 34.2146 -8.5775 0.2765 ? -0.0704 ? 0.0177  ? 0.3310 ? -0.0152 ? 0.2434 ? 1.6466 ? -0.9807 
? 0.2932  ? 2.0275 ? 0.0989  ? 2.2565 ? 0.0409  ? 0.1097  ? 0.0446  ? -0.0830 ? 0.0494 ? -0.1665 ? -0.0856 ? -0.0209 ? -0.0549 ? 
2 'X-RAY DIFFRACTION' ? refined -14.6664 28.2078 8.2295  0.2077 ? -0.0294 ? -0.0241 ? 0.2431 ? 0.0021  ? 0.2428 ? 2.2306 ? 0.0893  
? 0.1387  ? 3.3068 ? 0.5174  ? 4.0735 ? 0.0055  ? -0.1236 ? -0.2250 ? 0.1990  ? 0.0994 ? -0.3073 ? 0.4576  ? 0.1986  ? -0.1030 ? 
3 'X-RAY DIFFRACTION' ? refined -5.6788  17.5909 3.8050  0.5350 ? 0.1521  ? -0.0434 ? 0.5018 ? -0.0172 ? 0.5106 ? 7.6866 ? 0.4097  
? -0.3988 ? 6.6224 ? 1.5127  ? 9.0646 ? 0.2583  ? 0.1431  ? -0.5919 ? 0.6048  ? 0.1365 ? -1.1402 ? 1.3367  ? 1.4764  ? -0.3349 ? 
4 'X-RAY DIFFRACTION' ? refined -13.6579 29.0399 -3.6051 0.2297 ? -0.0792 ? 0.0587  ? 0.2903 ? -0.0623 ? 0.2991 ? 2.0784 ? 1.7632  
? 1.0155  ? 2.1111 ? -0.1874 ? 2.0598 ? -0.2448 ? 0.3704  ? -0.2351 ? -0.4186 ? 0.4441 ? -0.6535 ? 0.0176  ? 0.3346  ? -0.2005 ? 
5 'X-RAY DIFFRACTION' ? refined -5.6204  24.9971 -4.5524 0.2672 ? 0.0152  ? 0.0694  ? 0.4336 ? -0.1042 ? 0.3974 ? 4.1164 ? 2.3010  
? 0.2052  ? 7.4243 ? 2.3151  ? 4.0562 ? 0.1129  ? 0.4216  ? -0.1779 ? -0.6274 ? 0.3469 ? -1.2076 ? 0.0367  ? 0.7175  ? -0.3533 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 49 through 86 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 87 through 146 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 147 through 159 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 18 through 35 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 36 through 48 )
;
# 
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 ALA 160 ? A ALA 143 
2 1 Y 1 A ASP 161 ? A ASP 144 
3 1 Y 1 A PRO 162 ? A PRO 145 
# 
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 
A1BBE C2   C Y N 1   
A1BBE C4   C Y N 2   
A1BBE C5   C Y N 3   
A1BBE C01  C N R 4   
A1BBE C02  C N R 5   
A1BBE C03  C N N 6   
A1BBE C04  C N N 7   
A1BBE C05  C N N 8   
A1BBE C12  C N N 9   
A1BBE C6   C Y N 10  
A1BBE C8   C Y N 11  
A1BBE C9   C Y N 12  
A1BBE N01  N N N 13  
A1BBE N1   N Y N 14  
A1BBE N3   N Y N 15  
A1BBE N6   N N N 16  
A1BBE N7   N Y N 17  
A1BBE O01  O N N 18  
A1BBE O02  O N N 19  
A1BBE O03  O N N 20  
A1BBE O04  O N N 21  
A1BBE O05  O N N 22  
A1BBE P01  P N N 23  
A1BBE H1   H N N 24  
A1BBE H2   H N N 25  
A1BBE H3   H N N 26  
A1BBE H4   H N N 27  
A1BBE H5   H N N 28  
A1BBE H6   H N N 29  
A1BBE H7   H N N 30  
A1BBE H8   H N N 31  
A1BBE H9   H N N 32  
A1BBE H10  H N N 33  
A1BBE H11  H N N 34  
A1BBE H12  H N N 35  
A1BBE H14  H N N 36  
A1BBE H15  H N N 37  
A1BBE H16  H N N 38  
A1BBE H17  H N N 39  
A1BBE H18  H N N 40  
A1BBE H19  H N N 41  
ALA   N    N N N 42  
ALA   CA   C N S 43  
ALA   C    C N N 44  
ALA   O    O N N 45  
ALA   CB   C N N 46  
ALA   OXT  O N N 47  
ALA   H    H N N 48  
ALA   H2   H N N 49  
ALA   HA   H N N 50  
ALA   HB1  H N N 51  
ALA   HB2  H N N 52  
ALA   HB3  H N N 53  
ALA   HXT  H N N 54  
ARG   N    N N N 55  
ARG   CA   C N S 56  
ARG   C    C N N 57  
ARG   O    O N N 58  
ARG   CB   C N N 59  
ARG   CG   C N N 60  
ARG   CD   C N N 61  
ARG   NE   N N N 62  
ARG   CZ   C N N 63  
ARG   NH1  N N N 64  
ARG   NH2  N N N 65  
ARG   OXT  O N N 66  
ARG   H    H N N 67  
ARG   H2   H N N 68  
ARG   HA   H N N 69  
ARG   HB2  H N N 70  
ARG   HB3  H N N 71  
ARG   HG2  H N N 72  
ARG   HG3  H N N 73  
ARG   HD2  H N N 74  
ARG   HD3  H N N 75  
ARG   HE   H N N 76  
ARG   HH11 H N N 77  
ARG   HH12 H N N 78  
ARG   HH21 H N N 79  
ARG   HH22 H N N 80  
ARG   HXT  H N N 81  
ASN   N    N N N 82  
ASN   CA   C N S 83  
ASN   C    C N N 84  
ASN   O    O N N 85  
ASN   CB   C N N 86  
ASN   CG   C N N 87  
ASN   OD1  O N N 88  
ASN   ND2  N N N 89  
ASN   OXT  O N N 90  
ASN   H    H N N 91  
ASN   H2   H N N 92  
ASN   HA   H N N 93  
ASN   HB2  H N N 94  
ASN   HB3  H N N 95  
ASN   HD21 H N N 96  
ASN   HD22 H N N 97  
ASN   HXT  H N N 98  
ASP   N    N N N 99  
ASP   CA   C N S 100 
ASP   C    C N N 101 
ASP   O    O N N 102 
ASP   CB   C N N 103 
ASP   CG   C N N 104 
ASP   OD1  O N N 105 
ASP   OD2  O N N 106 
ASP   OXT  O N N 107 
ASP   H    H N N 108 
ASP   H2   H N N 109 
ASP   HA   H N N 110 
ASP   HB2  H N N 111 
ASP   HB3  H N N 112 
ASP   HD2  H N N 113 
ASP   HXT  H N N 114 
CYS   N    N N N 115 
CYS   CA   C N R 116 
CYS   C    C N N 117 
CYS   O    O N N 118 
CYS   CB   C N N 119 
CYS   SG   S N N 120 
CYS   OXT  O N N 121 
CYS   H    H N N 122 
CYS   H2   H N N 123 
CYS   HA   H N N 124 
CYS   HB2  H N N 125 
CYS   HB3  H N N 126 
CYS   HG   H N N 127 
CYS   HXT  H N N 128 
GLN   N    N N N 129 
GLN   CA   C N S 130 
GLN   C    C N N 131 
GLN   O    O N N 132 
GLN   CB   C N N 133 
GLN   CG   C N N 134 
GLN   CD   C N N 135 
GLN   OE1  O N N 136 
GLN   NE2  N N N 137 
GLN   OXT  O N N 138 
GLN   H    H N N 139 
GLN   H2   H N N 140 
GLN   HA   H N N 141 
GLN   HB2  H N N 142 
GLN   HB3  H N N 143 
GLN   HG2  H N N 144 
GLN   HG3  H N N 145 
GLN   HE21 H N N 146 
GLN   HE22 H N N 147 
GLN   HXT  H N N 148 
GLU   N    N N N 149 
GLU   CA   C N S 150 
GLU   C    C N N 151 
GLU   O    O N N 152 
GLU   CB   C N N 153 
GLU   CG   C N N 154 
GLU   CD   C N N 155 
GLU   OE1  O N N 156 
GLU   OE2  O N N 157 
GLU   OXT  O N N 158 
GLU   H    H N N 159 
GLU   H2   H N N 160 
GLU   HA   H N N 161 
GLU   HB2  H N N 162 
GLU   HB3  H N N 163 
GLU   HG2  H N N 164 
GLU   HG3  H N N 165 
GLU   HE2  H N N 166 
GLU   HXT  H N N 167 
GLY   N    N N N 168 
GLY   CA   C N N 169 
GLY   C    C N N 170 
GLY   O    O N N 171 
GLY   OXT  O N N 172 
GLY   H    H N N 173 
GLY   H2   H N N 174 
GLY   HA2  H N N 175 
GLY   HA3  H N N 176 
GLY   HXT  H N N 177 
HIS   N    N N N 178 
HIS   CA   C N S 179 
HIS   C    C N N 180 
HIS   O    O N N 181 
HIS   CB   C N N 182 
HIS   CG   C Y N 183 
HIS   ND1  N Y N 184 
HIS   CD2  C Y N 185 
HIS   CE1  C Y N 186 
HIS   NE2  N Y N 187 
HIS   OXT  O N N 188 
HIS   H    H N N 189 
HIS   H2   H N N 190 
HIS   HA   H N N 191 
HIS   HB2  H N N 192 
HIS   HB3  H N N 193 
HIS   HD1  H N N 194 
HIS   HD2  H N N 195 
HIS   HE1  H N N 196 
HIS   HE2  H N N 197 
HIS   HXT  H N N 198 
HOH   O    O N N 199 
HOH   H1   H N N 200 
HOH   H2   H N N 201 
ILE   N    N N N 202 
ILE   CA   C N S 203 
ILE   C    C N N 204 
ILE   O    O N N 205 
ILE   CB   C N S 206 
ILE   CG1  C N N 207 
ILE   CG2  C N N 208 
ILE   CD1  C N N 209 
ILE   OXT  O N N 210 
ILE   H    H N N 211 
ILE   H2   H N N 212 
ILE   HA   H N N 213 
ILE   HB   H N N 214 
ILE   HG12 H N N 215 
ILE   HG13 H N N 216 
ILE   HG21 H N N 217 
ILE   HG22 H N N 218 
ILE   HG23 H N N 219 
ILE   HD11 H N N 220 
ILE   HD12 H N N 221 
ILE   HD13 H N N 222 
ILE   HXT  H N N 223 
LEU   N    N N N 224 
LEU   CA   C N S 225 
LEU   C    C N N 226 
LEU   O    O N N 227 
LEU   CB   C N N 228 
LEU   CG   C N N 229 
LEU   CD1  C N N 230 
LEU   CD2  C N N 231 
LEU   OXT  O N N 232 
LEU   H    H N N 233 
LEU   H2   H N N 234 
LEU   HA   H N N 235 
LEU   HB2  H N N 236 
LEU   HB3  H N N 237 
LEU   HG   H N N 238 
LEU   HD11 H N N 239 
LEU   HD12 H N N 240 
LEU   HD13 H N N 241 
LEU   HD21 H N N 242 
LEU   HD22 H N N 243 
LEU   HD23 H N N 244 
LEU   HXT  H N N 245 
LYS   N    N N N 246 
LYS   CA   C N S 247 
LYS   C    C N N 248 
LYS   O    O N N 249 
LYS   CB   C N N 250 
LYS   CG   C N N 251 
LYS   CD   C N N 252 
LYS   CE   C N N 253 
LYS   NZ   N N N 254 
LYS   OXT  O N N 255 
LYS   H    H N N 256 
LYS   H2   H N N 257 
LYS   HA   H N N 258 
LYS   HB2  H N N 259 
LYS   HB3  H N N 260 
LYS   HG2  H N N 261 
LYS   HG3  H N N 262 
LYS   HD2  H N N 263 
LYS   HD3  H N N 264 
LYS   HE2  H N N 265 
LYS   HE3  H N N 266 
LYS   HZ1  H N N 267 
LYS   HZ2  H N N 268 
LYS   HZ3  H N N 269 
LYS   HXT  H N N 270 
MET   N    N N N 271 
MET   CA   C N S 272 
MET   C    C N N 273 
MET   O    O N N 274 
MET   CB   C N N 275 
MET   CG   C N N 276 
MET   SD   S N N 277 
MET   CE   C N N 278 
MET   OXT  O N N 279 
MET   H    H N N 280 
MET   H2   H N N 281 
MET   HA   H N N 282 
MET   HB2  H N N 283 
MET   HB3  H N N 284 
MET   HG2  H N N 285 
MET   HG3  H N N 286 
MET   HE1  H N N 287 
MET   HE2  H N N 288 
MET   HE3  H N N 289 
MET   HXT  H N N 290 
PHE   N    N N N 291 
PHE   CA   C N S 292 
PHE   C    C N N 293 
PHE   O    O N N 294 
PHE   CB   C N N 295 
PHE   CG   C Y N 296 
PHE   CD1  C Y N 297 
PHE   CD2  C Y N 298 
PHE   CE1  C Y N 299 
PHE   CE2  C Y N 300 
PHE   CZ   C Y N 301 
PHE   OXT  O N N 302 
PHE   H    H N N 303 
PHE   H2   H N N 304 
PHE   HA   H N N 305 
PHE   HB2  H N N 306 
PHE   HB3  H N N 307 
PHE   HD1  H N N 308 
PHE   HD2  H N N 309 
PHE   HE1  H N N 310 
PHE   HE2  H N N 311 
PHE   HZ   H N N 312 
PHE   HXT  H N N 313 
PRO   N    N N N 314 
PRO   CA   C N S 315 
PRO   C    C N N 316 
PRO   O    O N N 317 
PRO   CB   C N N 318 
PRO   CG   C N N 319 
PRO   CD   C N N 320 
PRO   OXT  O N N 321 
PRO   H    H N N 322 
PRO   HA   H N N 323 
PRO   HB2  H N N 324 
PRO   HB3  H N N 325 
PRO   HG2  H N N 326 
PRO   HG3  H N N 327 
PRO   HD2  H N N 328 
PRO   HD3  H N N 329 
PRO   HXT  H N N 330 
SER   N    N N N 331 
SER   CA   C N S 332 
SER   C    C N N 333 
SER   O    O N N 334 
SER   CB   C N N 335 
SER   OG   O N N 336 
SER   OXT  O N N 337 
SER   H    H N N 338 
SER   H2   H N N 339 
SER   HA   H N N 340 
SER   HB2  H N N 341 
SER   HB3  H N N 342 
SER   HG   H N N 343 
SER   HXT  H N N 344 
THR   N    N N N 345 
THR   CA   C N S 346 
THR   C    C N N 347 
THR   O    O N N 348 
THR   CB   C N R 349 
THR   OG1  O N N 350 
THR   CG2  C N N 351 
THR   OXT  O N N 352 
THR   H    H N N 353 
THR   H2   H N N 354 
THR   HA   H N N 355 
THR   HB   H N N 356 
THR   HG1  H N N 357 
THR   HG21 H N N 358 
THR   HG22 H N N 359 
THR   HG23 H N N 360 
THR   HXT  H N N 361 
TRP   N    N N N 362 
TRP   CA   C N S 363 
TRP   C    C N N 364 
TRP   O    O N N 365 
TRP   CB   C N N 366 
TRP   CG   C Y N 367 
TRP   CD1  C Y N 368 
TRP   CD2  C Y N 369 
TRP   NE1  N Y N 370 
TRP   CE2  C Y N 371 
TRP   CE3  C Y N 372 
TRP   CZ2  C Y N 373 
TRP   CZ3  C Y N 374 
TRP   CH2  C Y N 375 
TRP   OXT  O N N 376 
TRP   H    H N N 377 
TRP   H2   H N N 378 
TRP   HA   H N N 379 
TRP   HB2  H N N 380 
TRP   HB3  H N N 381 
TRP   HD1  H N N 382 
TRP   HE1  H N N 383 
TRP   HE3  H N N 384 
TRP   HZ2  H N N 385 
TRP   HZ3  H N N 386 
TRP   HH2  H N N 387 
TRP   HXT  H N N 388 
TYR   N    N N N 389 
TYR   CA   C N S 390 
TYR   C    C N N 391 
TYR   O    O N N 392 
TYR   CB   C N N 393 
TYR   CG   C Y N 394 
TYR   CD1  C Y N 395 
TYR   CD2  C Y N 396 
TYR   CE1  C Y N 397 
TYR   CE2  C Y N 398 
TYR   CZ   C Y N 399 
TYR   OH   O N N 400 
TYR   OXT  O N N 401 
TYR   H    H N N 402 
TYR   H2   H N N 403 
TYR   HA   H N N 404 
TYR   HB2  H N N 405 
TYR   HB3  H N N 406 
TYR   HD1  H N N 407 
TYR   HD2  H N N 408 
TYR   HE1  H N N 409 
TYR   HE2  H N N 410 
TYR   HH   H N N 411 
TYR   HXT  H N N 412 
VAL   N    N N N 413 
VAL   CA   C N S 414 
VAL   C    C N N 415 
VAL   O    O N N 416 
VAL   CB   C N N 417 
VAL   CG1  C N N 418 
VAL   CG2  C N N 419 
VAL   OXT  O N N 420 
VAL   H    H N N 421 
VAL   H2   H N N 422 
VAL   HA   H N N 423 
VAL   HB   H N N 424 
VAL   HG11 H N N 425 
VAL   HG12 H N N 426 
VAL   HG13 H N N 427 
VAL   HG21 H N N 428 
VAL   HG22 H N N 429 
VAL   HG23 H N N 430 
VAL   HXT  H N N 431 
# 
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 
A1BBE N6  C6   sing N N 1   
A1BBE C6  N1   doub Y N 2   
A1BBE C6  C5   sing Y N 3   
A1BBE N7  C5   sing Y N 4   
A1BBE N7  C8   sing Y N 5   
A1BBE N1  C2   sing Y N 6   
A1BBE C5  C4   doub Y N 7   
A1BBE C8  C9   doub Y N 8   
A1BBE C2  N3   doub Y N 9   
A1BBE C4  C9   sing Y N 10  
A1BBE C4  N3   sing Y N 11  
A1BBE C9  C05  sing N N 12  
A1BBE C05 N01  sing N N 13  
A1BBE C12 N01  sing N N 14  
A1BBE C12 C01  sing N N 15  
A1BBE N01 C04  sing N N 16  
A1BBE C04 C02  sing N N 17  
A1BBE C01 C02  sing N N 18  
A1BBE C01 O01  sing N N 19  
A1BBE O05 P01  doub N N 20  
A1BBE C02 C03  sing N N 21  
A1BBE C03 O02  sing N N 22  
A1BBE O02 P01  sing N N 23  
A1BBE P01 O03  sing N N 24  
A1BBE P01 O04  sing N N 25  
A1BBE C2  H1   sing N N 26  
A1BBE C01 H2   sing N N 27  
A1BBE C02 H3   sing N N 28  
A1BBE C03 H4   sing N N 29  
A1BBE C03 H5   sing N N 30  
A1BBE C04 H6   sing N N 31  
A1BBE C04 H7   sing N N 32  
A1BBE C05 H8   sing N N 33  
A1BBE C05 H9   sing N N 34  
A1BBE C12 H10  sing N N 35  
A1BBE C12 H11  sing N N 36  
A1BBE C8  H12  sing N N 37  
A1BBE N6  H14  sing N N 38  
A1BBE N6  H15  sing N N 39  
A1BBE N7  H16  sing N N 40  
A1BBE O01 H17  sing N N 41  
A1BBE O03 H18  sing N N 42  
A1BBE O04 H19  sing N N 43  
ALA   N   CA   sing N N 44  
ALA   N   H    sing N N 45  
ALA   N   H2   sing N N 46  
ALA   CA  C    sing N N 47  
ALA   CA  CB   sing N N 48  
ALA   CA  HA   sing N N 49  
ALA   C   O    doub N N 50  
ALA   C   OXT  sing N N 51  
ALA   CB  HB1  sing N N 52  
ALA   CB  HB2  sing N N 53  
ALA   CB  HB3  sing N N 54  
ALA   OXT HXT  sing N N 55  
ARG   N   CA   sing N N 56  
ARG   N   H    sing N N 57  
ARG   N   H2   sing N N 58  
ARG   CA  C    sing N N 59  
ARG   CA  CB   sing N N 60  
ARG   CA  HA   sing N N 61  
ARG   C   O    doub N N 62  
ARG   C   OXT  sing N N 63  
ARG   CB  CG   sing N N 64  
ARG   CB  HB2  sing N N 65  
ARG   CB  HB3  sing N N 66  
ARG   CG  CD   sing N N 67  
ARG   CG  HG2  sing N N 68  
ARG   CG  HG3  sing N N 69  
ARG   CD  NE   sing N N 70  
ARG   CD  HD2  sing N N 71  
ARG   CD  HD3  sing N N 72  
ARG   NE  CZ   sing N N 73  
ARG   NE  HE   sing N N 74  
ARG   CZ  NH1  sing N N 75  
ARG   CZ  NH2  doub N N 76  
ARG   NH1 HH11 sing N N 77  
ARG   NH1 HH12 sing N N 78  
ARG   NH2 HH21 sing N N 79  
ARG   NH2 HH22 sing N N 80  
ARG   OXT HXT  sing N N 81  
ASN   N   CA   sing N N 82  
ASN   N   H    sing N N 83  
ASN   N   H2   sing N N 84  
ASN   CA  C    sing N N 85  
ASN   CA  CB   sing N N 86  
ASN   CA  HA   sing N N 87  
ASN   C   O    doub N N 88  
ASN   C   OXT  sing N N 89  
ASN   CB  CG   sing N N 90  
ASN   CB  HB2  sing N N 91  
ASN   CB  HB3  sing N N 92  
ASN   CG  OD1  doub N N 93  
ASN   CG  ND2  sing N N 94  
ASN   ND2 HD21 sing N N 95  
ASN   ND2 HD22 sing N N 96  
ASN   OXT HXT  sing N N 97  
ASP   N   CA   sing N N 98  
ASP   N   H    sing N N 99  
ASP   N   H2   sing N N 100 
ASP   CA  C    sing N N 101 
ASP   CA  CB   sing N N 102 
ASP   CA  HA   sing N N 103 
ASP   C   O    doub N N 104 
ASP   C   OXT  sing N N 105 
ASP   CB  CG   sing N N 106 
ASP   CB  HB2  sing N N 107 
ASP   CB  HB3  sing N N 108 
ASP   CG  OD1  doub N N 109 
ASP   CG  OD2  sing N N 110 
ASP   OD2 HD2  sing N N 111 
ASP   OXT HXT  sing N N 112 
CYS   N   CA   sing N N 113 
CYS   N   H    sing N N 114 
CYS   N   H2   sing N N 115 
CYS   CA  C    sing N N 116 
CYS   CA  CB   sing N N 117 
CYS   CA  HA   sing N N 118 
CYS   C   O    doub N N 119 
CYS   C   OXT  sing N N 120 
CYS   CB  SG   sing N N 121 
CYS   CB  HB2  sing N N 122 
CYS   CB  HB3  sing N N 123 
CYS   SG  HG   sing N N 124 
CYS   OXT HXT  sing N N 125 
GLN   N   CA   sing N N 126 
GLN   N   H    sing N N 127 
GLN   N   H2   sing N N 128 
GLN   CA  C    sing N N 129 
GLN   CA  CB   sing N N 130 
GLN   CA  HA   sing N N 131 
GLN   C   O    doub N N 132 
GLN   C   OXT  sing N N 133 
GLN   CB  CG   sing N N 134 
GLN   CB  HB2  sing N N 135 
GLN   CB  HB3  sing N N 136 
GLN   CG  CD   sing N N 137 
GLN   CG  HG2  sing N N 138 
GLN   CG  HG3  sing N N 139 
GLN   CD  OE1  doub N N 140 
GLN   CD  NE2  sing N N 141 
GLN   NE2 HE21 sing N N 142 
GLN   NE2 HE22 sing N N 143 
GLN   OXT HXT  sing N N 144 
GLU   N   CA   sing N N 145 
GLU   N   H    sing N N 146 
GLU   N   H2   sing N N 147 
GLU   CA  C    sing N N 148 
GLU   CA  CB   sing N N 149 
GLU   CA  HA   sing N N 150 
GLU   C   O    doub N N 151 
GLU   C   OXT  sing N N 152 
GLU   CB  CG   sing N N 153 
GLU   CB  HB2  sing N N 154 
GLU   CB  HB3  sing N N 155 
GLU   CG  CD   sing N N 156 
GLU   CG  HG2  sing N N 157 
GLU   CG  HG3  sing N N 158 
GLU   CD  OE1  doub N N 159 
GLU   CD  OE2  sing N N 160 
GLU   OE2 HE2  sing N N 161 
GLU   OXT HXT  sing N N 162 
GLY   N   CA   sing N N 163 
GLY   N   H    sing N N 164 
GLY   N   H2   sing N N 165 
GLY   CA  C    sing N N 166 
GLY   CA  HA2  sing N N 167 
GLY   CA  HA3  sing N N 168 
GLY   C   O    doub N N 169 
GLY   C   OXT  sing N N 170 
GLY   OXT HXT  sing N N 171 
HIS   N   CA   sing N N 172 
HIS   N   H    sing N N 173 
HIS   N   H2   sing N N 174 
HIS   CA  C    sing N N 175 
HIS   CA  CB   sing N N 176 
HIS   CA  HA   sing N N 177 
HIS   C   O    doub N N 178 
HIS   C   OXT  sing N N 179 
HIS   CB  CG   sing N N 180 
HIS   CB  HB2  sing N N 181 
HIS   CB  HB3  sing N N 182 
HIS   CG  ND1  sing Y N 183 
HIS   CG  CD2  doub Y N 184 
HIS   ND1 CE1  doub Y N 185 
HIS   ND1 HD1  sing N N 186 
HIS   CD2 NE2  sing Y N 187 
HIS   CD2 HD2  sing N N 188 
HIS   CE1 NE2  sing Y N 189 
HIS   CE1 HE1  sing N N 190 
HIS   NE2 HE2  sing N N 191 
HIS   OXT HXT  sing N N 192 
HOH   O   H1   sing N N 193 
HOH   O   H2   sing N N 194 
ILE   N   CA   sing N N 195 
ILE   N   H    sing N N 196 
ILE   N   H2   sing N N 197 
ILE   CA  C    sing N N 198 
ILE   CA  CB   sing N N 199 
ILE   CA  HA   sing N N 200 
ILE   C   O    doub N N 201 
ILE   C   OXT  sing N N 202 
ILE   CB  CG1  sing N N 203 
ILE   CB  CG2  sing N N 204 
ILE   CB  HB   sing N N 205 
ILE   CG1 CD1  sing N N 206 
ILE   CG1 HG12 sing N N 207 
ILE   CG1 HG13 sing N N 208 
ILE   CG2 HG21 sing N N 209 
ILE   CG2 HG22 sing N N 210 
ILE   CG2 HG23 sing N N 211 
ILE   CD1 HD11 sing N N 212 
ILE   CD1 HD12 sing N N 213 
ILE   CD1 HD13 sing N N 214 
ILE   OXT HXT  sing N N 215 
LEU   N   CA   sing N N 216 
LEU   N   H    sing N N 217 
LEU   N   H2   sing N N 218 
LEU   CA  C    sing N N 219 
LEU   CA  CB   sing N N 220 
LEU   CA  HA   sing N N 221 
LEU   C   O    doub N N 222 
LEU   C   OXT  sing N N 223 
LEU   CB  CG   sing N N 224 
LEU   CB  HB2  sing N N 225 
LEU   CB  HB3  sing N N 226 
LEU   CG  CD1  sing N N 227 
LEU   CG  CD2  sing N N 228 
LEU   CG  HG   sing N N 229 
LEU   CD1 HD11 sing N N 230 
LEU   CD1 HD12 sing N N 231 
LEU   CD1 HD13 sing N N 232 
LEU   CD2 HD21 sing N N 233 
LEU   CD2 HD22 sing N N 234 
LEU   CD2 HD23 sing N N 235 
LEU   OXT HXT  sing N N 236 
LYS   N   CA   sing N N 237 
LYS   N   H    sing N N 238 
LYS   N   H2   sing N N 239 
LYS   CA  C    sing N N 240 
LYS   CA  CB   sing N N 241 
LYS   CA  HA   sing N N 242 
LYS   C   O    doub N N 243 
LYS   C   OXT  sing N N 244 
LYS   CB  CG   sing N N 245 
LYS   CB  HB2  sing N N 246 
LYS   CB  HB3  sing N N 247 
LYS   CG  CD   sing N N 248 
LYS   CG  HG2  sing N N 249 
LYS   CG  HG3  sing N N 250 
LYS   CD  CE   sing N N 251 
LYS   CD  HD2  sing N N 252 
LYS   CD  HD3  sing N N 253 
LYS   CE  NZ   sing N N 254 
LYS   CE  HE2  sing N N 255 
LYS   CE  HE3  sing N N 256 
LYS   NZ  HZ1  sing N N 257 
LYS   NZ  HZ2  sing N N 258 
LYS   NZ  HZ3  sing N N 259 
LYS   OXT HXT  sing N N 260 
MET   N   CA   sing N N 261 
MET   N   H    sing N N 262 
MET   N   H2   sing N N 263 
MET   CA  C    sing N N 264 
MET   CA  CB   sing N N 265 
MET   CA  HA   sing N N 266 
MET   C   O    doub N N 267 
MET   C   OXT  sing N N 268 
MET   CB  CG   sing N N 269 
MET   CB  HB2  sing N N 270 
MET   CB  HB3  sing N N 271 
MET   CG  SD   sing N N 272 
MET   CG  HG2  sing N N 273 
MET   CG  HG3  sing N N 274 
MET   SD  CE   sing N N 275 
MET   CE  HE1  sing N N 276 
MET   CE  HE2  sing N N 277 
MET   CE  HE3  sing N N 278 
MET   OXT HXT  sing N N 279 
PHE   N   CA   sing N N 280 
PHE   N   H    sing N N 281 
PHE   N   H2   sing N N 282 
PHE   CA  C    sing N N 283 
PHE   CA  CB   sing N N 284 
PHE   CA  HA   sing N N 285 
PHE   C   O    doub N N 286 
PHE   C   OXT  sing N N 287 
PHE   CB  CG   sing N N 288 
PHE   CB  HB2  sing N N 289 
PHE   CB  HB3  sing N N 290 
PHE   CG  CD1  doub Y N 291 
PHE   CG  CD2  sing Y N 292 
PHE   CD1 CE1  sing Y N 293 
PHE   CD1 HD1  sing N N 294 
PHE   CD2 CE2  doub Y N 295 
PHE   CD2 HD2  sing N N 296 
PHE   CE1 CZ   doub Y N 297 
PHE   CE1 HE1  sing N N 298 
PHE   CE2 CZ   sing Y N 299 
PHE   CE2 HE2  sing N N 300 
PHE   CZ  HZ   sing N N 301 
PHE   OXT HXT  sing N N 302 
PRO   N   CA   sing N N 303 
PRO   N   CD   sing N N 304 
PRO   N   H    sing N N 305 
PRO   CA  C    sing N N 306 
PRO   CA  CB   sing N N 307 
PRO   CA  HA   sing N N 308 
PRO   C   O    doub N N 309 
PRO   C   OXT  sing N N 310 
PRO   CB  CG   sing N N 311 
PRO   CB  HB2  sing N N 312 
PRO   CB  HB3  sing N N 313 
PRO   CG  CD   sing N N 314 
PRO   CG  HG2  sing N N 315 
PRO   CG  HG3  sing N N 316 
PRO   CD  HD2  sing N N 317 
PRO   CD  HD3  sing N N 318 
PRO   OXT HXT  sing N N 319 
SER   N   CA   sing N N 320 
SER   N   H    sing N N 321 
SER   N   H2   sing N N 322 
SER   CA  C    sing N N 323 
SER   CA  CB   sing N N 324 
SER   CA  HA   sing N N 325 
SER   C   O    doub N N 326 
SER   C   OXT  sing N N 327 
SER   CB  OG   sing N N 328 
SER   CB  HB2  sing N N 329 
SER   CB  HB3  sing N N 330 
SER   OG  HG   sing N N 331 
SER   OXT HXT  sing N N 332 
THR   N   CA   sing N N 333 
THR   N   H    sing N N 334 
THR   N   H2   sing N N 335 
THR   CA  C    sing N N 336 
THR   CA  CB   sing N N 337 
THR   CA  HA   sing N N 338 
THR   C   O    doub N N 339 
THR   C   OXT  sing N N 340 
THR   CB  OG1  sing N N 341 
THR   CB  CG2  sing N N 342 
THR   CB  HB   sing N N 343 
THR   OG1 HG1  sing N N 344 
THR   CG2 HG21 sing N N 345 
THR   CG2 HG22 sing N N 346 
THR   CG2 HG23 sing N N 347 
THR   OXT HXT  sing N N 348 
TRP   N   CA   sing N N 349 
TRP   N   H    sing N N 350 
TRP   N   H2   sing N N 351 
TRP   CA  C    sing N N 352 
TRP   CA  CB   sing N N 353 
TRP   CA  HA   sing N N 354 
TRP   C   O    doub N N 355 
TRP   C   OXT  sing N N 356 
TRP   CB  CG   sing N N 357 
TRP   CB  HB2  sing N N 358 
TRP   CB  HB3  sing N N 359 
TRP   CG  CD1  doub Y N 360 
TRP   CG  CD2  sing Y N 361 
TRP   CD1 NE1  sing Y N 362 
TRP   CD1 HD1  sing N N 363 
TRP   CD2 CE2  doub Y N 364 
TRP   CD2 CE3  sing Y N 365 
TRP   NE1 CE2  sing Y N 366 
TRP   NE1 HE1  sing N N 367 
TRP   CE2 CZ2  sing Y N 368 
TRP   CE3 CZ3  doub Y N 369 
TRP   CE3 HE3  sing N N 370 
TRP   CZ2 CH2  doub Y N 371 
TRP   CZ2 HZ2  sing N N 372 
TRP   CZ3 CH2  sing Y N 373 
TRP   CZ3 HZ3  sing N N 374 
TRP   CH2 HH2  sing N N 375 
TRP   OXT HXT  sing N N 376 
TYR   N   CA   sing N N 377 
TYR   N   H    sing N N 378 
TYR   N   H2   sing N N 379 
TYR   CA  C    sing N N 380 
TYR   CA  CB   sing N N 381 
TYR   CA  HA   sing N N 382 
TYR   C   O    doub N N 383 
TYR   C   OXT  sing N N 384 
TYR   CB  CG   sing N N 385 
TYR   CB  HB2  sing N N 386 
TYR   CB  HB3  sing N N 387 
TYR   CG  CD1  doub Y N 388 
TYR   CG  CD2  sing Y N 389 
TYR   CD1 CE1  sing Y N 390 
TYR   CD1 HD1  sing N N 391 
TYR   CD2 CE2  doub Y N 392 
TYR   CD2 HD2  sing N N 393 
TYR   CE1 CZ   doub Y N 394 
TYR   CE1 HE1  sing N N 395 
TYR   CE2 CZ   sing Y N 396 
TYR   CE2 HE2  sing N N 397 
TYR   CZ  OH   sing N N 398 
TYR   OH  HH   sing N N 399 
TYR   OXT HXT  sing N N 400 
VAL   N   CA   sing N N 401 
VAL   N   H    sing N N 402 
VAL   N   H2   sing N N 403 
VAL   CA  C    sing N N 404 
VAL   CA  CB   sing N N 405 
VAL   CA  HA   sing N N 406 
VAL   C   O    doub N N 407 
VAL   C   OXT  sing N N 408 
VAL   CB  CG1  sing N N 409 
VAL   CB  CG2  sing N N 410 
VAL   CB  HB   sing N N 411 
VAL   CG1 HG11 sing N N 412 
VAL   CG1 HG12 sing N N 413 
VAL   CG1 HG13 sing N N 414 
VAL   CG2 HG21 sing N N 415 
VAL   CG2 HG22 sing N N 416 
VAL   CG2 HG23 sing N N 417 
VAL   OXT HXT  sing N N 418 
# 
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 of General Medical Sciences (NIH/NIGMS)' 'United States' GM041916       1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' 'S10 OD020068' 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4P5E 
_pdbx_initial_refinement_model.details          
'CRYSTAL STRUCTURE OF HUMAN DNPH1 (RCL) WITH 6-NAPHTHYL-PURINE-RIBOSIDE-MONOPHOSPHATE' 
# 
_atom_sites.entry_id                    9DA4 
_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]   0.012004 
_atom_sites.fract_transf_matrix[1][2]   0.006931 
_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]   0.013861 
_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]   0.012409 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . SER   A 1 1   ? -25.186 13.325 -8.511  1.00 36.03 ?  18  SER   A N   1 
ATOM   2    C CA  . SER   A 1 1   ? -24.131 13.792 -9.412  1.00 32.64 ?  18  SER   A CA  1 
ATOM   3    C C   . SER   A 1 1   ? -23.027 12.743 -9.567  1.00 34.60 ?  18  SER   A C   1 
ATOM   4    O O   . SER   A 1 1   ? -22.829 11.908 -8.687  1.00 36.12 ?  18  SER   A O   1 
ATOM   5    C CB  . SER   A 1 1   ? -23.561 15.124 -8.907  1.00 33.06 ?  18  SER   A CB  1 
ATOM   6    O OG  . SER   A 1 1   ? -22.944 14.979 -7.630  1.00 33.44 ?  18  SER   A OG  1 
ATOM   7    N N   . MET   A 1 2   ? -22.317 12.755 -10.699 1.00 33.98 ?  19  MET   A N   1 
ATOM   8    C CA  . MET   A 1 2   ? -21.236 11.791 -10.860 1.00 33.29 ?  19  MET   A CA  1 
ATOM   9    C C   . MET   A 1 2   ? -20.000 12.161 -10.061 1.00 36.17 ?  19  MET   A C   1 
ATOM   10   O O   . MET   A 1 2   ? -19.167 11.285 -9.803  1.00 37.54 ?  19  MET   A O   1 
ATOM   11   C CB  . MET   A 1 2   ? -20.891 11.592 -12.341 1.00 40.44 ?  19  MET   A CB  1 
ATOM   12   C CG  . MET   A 1 2   ? -22.127 11.334 -13.188 1.00 40.31 ?  19  MET   A CG  1 
ATOM   13   S SD  . MET   A 1 2   ? -22.595 9.622  -12.907 1.00 43.70 ?  19  MET   A SD  1 
ATOM   14   C CE  . MET   A 1 2   ? -21.032 8.745  -12.936 1.00 49.00 ?  19  MET   A CE  1 
ATOM   15   N N   . ARG   A 1 3   ? -19.883 13.417 -9.653  1.00 34.97 ?  20  ARG   A N   1 
ATOM   16   C CA  . ARG   A 1 3   ? -18.794 13.920 -8.828  1.00 37.22 ?  20  ARG   A CA  1 
ATOM   17   C C   . ARG   A 1 3   ? -19.355 14.851 -7.764  1.00 35.08 ?  20  ARG   A C   1 
ATOM   18   O O   . ARG   A 1 3   ? -20.360 15.535 -8.008  1.00 33.97 ?  20  ARG   A O   1 
ATOM   19   C CB  . ARG   A 1 3   ? -17.779 14.631 -9.731  1.00 39.83 ?  20  ARG   A CB  1 
ATOM   20   C CG  . ARG   A 1 3   ? -17.089 13.633 -10.660 1.00 44.23 ?  20  ARG   A CG  1 
ATOM   21   C CD  . ARG   A 1 3   ? -16.037 14.264 -11.547 1.00 54.59 ?  20  ARG   A CD  1 
ATOM   22   N NE  . ARG   A 1 3   ? -15.446 13.301 -12.470 1.00 56.45 ?  20  ARG   A NE  1 
ATOM   23   C CZ  . ARG   A 1 3   ? -14.584 13.602 -13.435 1.00 58.19 ?  20  ARG   A CZ  1 
ATOM   24   N NH1 . ARG   A 1 3   ? -14.278 14.860 -13.728 1.00 55.01 ?  20  ARG   A NH1 1 
ATOM   25   N NH2 . ARG   A 1 3   ? -14.020 12.615 -14.131 1.00 52.43 ?  20  ARG   A NH2 1 
ATOM   26   N N   . PRO   A 1 4   ? -18.762 14.878 -6.565  1.00 33.40 ?  21  PRO   A N   1 
ATOM   27   C CA  . PRO   A 1 4   ? -19.203 15.844 -5.558  1.00 32.56 ?  21  PRO   A CA  1 
ATOM   28   C C   . PRO   A 1 4   ? -19.022 17.268 -6.064  1.00 33.06 ?  21  PRO   A C   1 
ATOM   29   O O   . PRO   A 1 4   ? -18.098 17.566 -6.820  1.00 34.29 ?  21  PRO   A O   1 
ATOM   30   C CB  . PRO   A 1 4   ? -18.283 15.551 -4.360  1.00 33.17 ?  21  PRO   A CB  1 
ATOM   31   C CG  . PRO   A 1 4   ? -17.886 14.125 -4.556  1.00 34.11 ?  21  PRO   A CG  1 
ATOM   32   C CD  . PRO   A 1 4   ? -17.658 14.050 -6.059  1.00 31.72 ?  21  PRO   A CD  1 
ATOM   33   N N   . ALA   A 1 5   ? -19.946 18.139 -5.668  1.00 30.35 ?  22  ALA   A N   1 
ATOM   34   C CA  . ALA   A 1 5   ? -19.871 19.566 -5.946  1.00 28.14 ?  22  ALA   A CA  1 
ATOM   35   C C   . ALA   A 1 5   ? -19.247 20.260 -4.746  1.00 28.68 ?  22  ALA   A C   1 
ATOM   36   O O   . ALA   A 1 5   ? -19.725 20.096 -3.619  1.00 31.17 ?  22  ALA   A O   1 
ATOM   37   C CB  . ALA   A 1 5   ? -21.259 20.148 -6.217  1.00 31.18 ?  22  ALA   A CB  1 
ATOM   38   N N   . LEU   A 1 6   ? -18.182 21.019 -4.987  1.00 24.88 ?  23  LEU   A N   1 
ATOM   39   C CA  . LEU   A 1 6   ? -17.452 21.711 -3.927  1.00 28.35 ?  23  LEU   A CA  1 
ATOM   40   C C   . LEU   A 1 6   ? -17.501 23.216 -4.145  1.00 28.82 ?  23  LEU   A C   1 
ATOM   41   O O   . LEU   A 1 6   ? -17.346 23.694 -5.270  1.00 26.96 ?  23  LEU   A O   1 
ATOM   42   C CB  . LEU   A 1 6   ? -15.990 21.230 -3.869  1.00 24.88 ?  23  LEU   A CB  1 
ATOM   43   C CG  . LEU   A 1 6   ? -15.795 19.716 -3.951  1.00 27.16 ?  23  LEU   A CG  1 
ATOM   44   C CD1 . LEU   A 1 6   ? -14.337 19.355 -3.933  1.00 32.88 ?  23  LEU   A CD1 1 
ATOM   45   C CD2 . LEU   A 1 6   ? -16.464 19.105 -2.719  1.00 30.49 ?  23  LEU   A CD2 1 
ATOM   46   N N   . TYR   A 1 7   ? -17.701 23.964 -3.061  1.00 24.78 ?  24  TYR   A N   1 
ATOM   47   C CA  . TYR   A 1 7   ? -17.711 25.422 -3.093  1.00 22.77 ?  24  TYR   A CA  1 
ATOM   48   C C   . TYR   A 1 7   ? -16.534 25.900 -2.263  1.00 25.50 ?  24  TYR   A C   1 
ATOM   49   O O   . TYR   A 1 7   ? -16.473 25.591 -1.071  1.00 27.70 ?  24  TYR   A O   1 
ATOM   50   C CB  . TYR   A 1 7   ? -19.027 25.969 -2.531  1.00 25.91 ?  24  TYR   A CB  1 
ATOM   51   C CG  . TYR   A 1 7   ? -19.261 27.454 -2.723  1.00 24.73 ?  24  TYR   A CG  1 
ATOM   52   C CD1 . TYR   A 1 7   ? -18.591 28.396 -1.935  1.00 22.37 ?  24  TYR   A CD1 1 
ATOM   53   C CD2 . TYR   A 1 7   ? -20.201 27.915 -3.643  1.00 24.54 ?  24  TYR   A CD2 1 
ATOM   54   C CE1 . TYR   A 1 7   ? -18.811 29.763 -2.097  1.00 24.81 ?  24  TYR   A CE1 1 
ATOM   55   C CE2 . TYR   A 1 7   ? -20.427 29.278 -3.820  1.00 26.71 ?  24  TYR   A CE2 1 
ATOM   56   C CZ  . TYR   A 1 7   ? -19.730 30.195 -3.048  1.00 28.44 ?  24  TYR   A CZ  1 
ATOM   57   O OH  . TYR   A 1 7   ? -19.974 31.541 -3.204  1.00 27.45 ?  24  TYR   A OH  1 
ATOM   58   N N   . PHE   A 1 8   ? -15.602 26.634 -2.879  1.00 23.96 ?  25  PHE   A N   1 
ATOM   59   C CA  . PHE   A 1 8   ? -14.440 27.167 -2.164  1.00 26.25 ?  25  PHE   A CA  1 
ATOM   60   C C   . PHE   A 1 8   ? -14.614 28.645 -1.861  1.00 26.11 ?  25  PHE   A C   1 
ATOM   61   O O   . PHE   A 1 8   ? -14.893 29.440 -2.765  1.00 24.96 ?  25  PHE   A O   1 
ATOM   62   C CB  . PHE   A 1 8   ? -13.129 26.985 -2.939  1.00 26.01 ?  25  PHE   A CB  1 
ATOM   63   C CG  . PHE   A 1 8   ? -11.964 27.643 -2.248  1.00 27.46 ?  25  PHE   A CG  1 
ATOM   64   C CD1 . PHE   A 1 8   ? -11.399 27.064 -1.114  1.00 27.90 ?  25  PHE   A CD1 1 
ATOM   65   C CD2 . PHE   A 1 8   ? -11.491 28.879 -2.667  1.00 26.42 ?  25  PHE   A CD2 1 
ATOM   66   C CE1 . PHE   A 1 8   ? -10.359 27.689 -0.429  1.00 29.52 ?  25  PHE   A CE1 1 
ATOM   67   C CE2 . PHE   A 1 8   ? -10.453 29.514 -1.992  1.00 28.64 ?  25  PHE   A CE2 1 
ATOM   68   C CZ  . PHE   A 1 8   ? -9.872  28.908 -0.875  1.00 29.02 ?  25  PHE   A CZ  1 
ATOM   69   N N   . CYS   A 1 9   ? -14.395 29.015 -0.594  1.00 22.15 ?  26  CYS   A N   1 
ATOM   70   C CA  . CYS   A 1 9   ? -14.454 30.394 -0.125  1.00 24.28 ?  26  CYS   A CA  1 
ATOM   71   C C   . CYS   A 1 9   ? -13.061 30.875 0.253   1.00 23.10 ?  26  CYS   A C   1 
ATOM   72   O O   . CYS   A 1 9   ? -12.327 30.169 0.957   1.00 24.64 ?  26  CYS   A O   1 
ATOM   73   C CB  . CYS   A 1 9   ? -15.345 30.523 1.120   1.00 22.12 ?  26  CYS   A CB  1 
ATOM   74   S SG  . CYS   A 1 9   ? -16.932 29.691 1.048   1.00 24.13 ?  26  CYS   A SG  1 
ATOM   75   N N   . GLY   A 1 10  ? -12.712 32.086 -0.190  1.00 21.89 ?  27  GLY   A N   1 
ATOM   76   C CA  . GLY   A 1 10  ? -11.502 32.761 0.249   1.00 24.82 ?  27  GLY   A CA  1 
ATOM   77   C C   . GLY   A 1 10  ? -11.602 34.225 -0.103  1.00 25.36 ?  27  GLY   A C   1 
ATOM   78   O O   . GLY   A 1 10  ? -12.212 34.589 -1.111  1.00 25.54 ?  27  GLY   A O   1 
ATOM   79   N N   . SER   A 1 11  ? -10.982 35.073 0.718   1.00 22.62 ?  28  SER   A N   1 
ATOM   80   C CA  . SER   A 1 11  ? -11.120 36.518 0.553   1.00 22.98 ?  28  SER   A CA  1 
ATOM   81   C C   . SER   A 1 11  ? -10.747 36.956 -0.868  1.00 25.52 ?  28  SER   A C   1 
ATOM   82   O O   . SER   A 1 11  ? -9.759  36.488 -1.438  1.00 25.87 ?  28  SER   A O   1 
ATOM   83   C CB  . SER   A 1 11  ? -10.232 37.228 1.578   1.00 22.80 ?  28  SER   A CB  1 
ATOM   84   O OG  . SER   A 1 11  ? -10.158 38.623 1.365   1.00 23.45 ?  28  SER   A OG  1 
ATOM   85   N N   . ILE   A 1 12  ? -11.566 37.849 -1.443  1.00 23.59 ?  29  ILE   A N   1 
ATOM   86   C CA  . ILE   A 1 12  ? -11.261 38.507 -2.714  1.00 23.80 ?  29  ILE   A CA  1 
ATOM   87   C C   . ILE   A 1 12  ? -11.275 40.017 -2.507  1.00 26.63 ?  29  ILE   A C   1 
ATOM   88   O O   . ILE   A 1 12  ? -10.216 40.650 -2.437  1.00 26.71 ?  29  ILE   A O   1 
ATOM   89   C CB  . ILE   A 1 12  ? -12.246 38.076 -3.819  1.00 25.16 ?  29  ILE   A CB  1 
ATOM   90   C CG1 . ILE   A 1 12  ? -12.186 36.557 -4.031  1.00 25.64 ?  29  ILE   A CG1 1 
ATOM   91   C CG2 . ILE   A 1 12  ? -11.952 38.845 -5.125  1.00 25.64 ?  29  ILE   A CG2 1 
ATOM   92   C CD1 . ILE   A 1 12  ? -13.196 36.026 -5.034  1.00 22.98 ?  29  ILE   A CD1 1 
ATOM   93   N N   . ARG   A 1 13  ? -12.463 40.614 -2.357  1.00 24.33 ?  30  ARG   A N   1 
ATOM   94   C CA  . ARG   A 1 13  ? -12.487 42.055 -2.087  1.00 24.26 ?  30  ARG   A CA  1 
ATOM   95   C C   . ARG   A 1 13  ? -11.996 42.389 -0.681  1.00 23.90 ?  30  ARG   A C   1 
ATOM   96   O O   . ARG   A 1 13  ? -11.534 43.521 -0.449  1.00 27.10 ?  30  ARG   A O   1 
ATOM   97   C CB  . ARG   A 1 13  ? -13.891 42.619 -2.331  1.00 25.76 ?  30  ARG   A CB  1 
ATOM   98   C CG  . ARG   A 1 13  ? -14.344 42.386 -3.770  1.00 27.70 ?  30  ARG   A CG  1 
ATOM   99   C CD  . ARG   A 1 13  ? -15.371 43.374 -4.264  1.00 29.02 ?  30  ARG   A CD  1 
ATOM   100  N NE  . ARG   A 1 13  ? -15.835 43.001 -5.601  0.92 30.54 ?  30  ARG   A NE  1 
ATOM   101  C CZ  . ARG   A 1 13  ? -16.987 43.376 -6.140  1.00 32.26 ?  30  ARG   A CZ  1 
ATOM   102  N NH1 . ARG   A 1 13  ? -17.874 44.076 -5.457  1.00 28.92 ?  30  ARG   A NH1 1 
ATOM   103  N NH2 . ARG   A 1 13  ? -17.253 43.041 -7.401  1.00 30.76 ?  30  ARG   A NH2 1 
ATOM   104  N N   . GLY   A 1 14  ? -12.027 41.424 0.241   1.00 23.66 ?  31  GLY   A N   1 
ATOM   105  C CA  . GLY   A 1 14  ? -11.389 41.618 1.531   1.00 23.18 ?  31  GLY   A CA  1 
ATOM   106  C C   . GLY   A 1 14  ? -9.890  41.760 1.433   1.00 27.63 ?  31  GLY   A C   1 
ATOM   107  O O   . GLY   A 1 14  ? -9.255  42.273 2.366   1.00 29.70 ?  31  GLY   A O   1 
ATOM   108  N N   . GLY   A 1 15  ? -9.314  41.361 0.301   1.00 27.18 ?  32  GLY   A N   1 
ATOM   109  C CA  . GLY   A 1 15  ? -7.872  41.385 0.143   1.00 26.15 ?  32  GLY   A CA  1 
ATOM   110  C C   . GLY   A 1 15  ? -7.416  40.097 -0.504  1.00 29.80 ?  32  GLY   A C   1 
ATOM   111  O O   . GLY   A 1 15  ? -7.965  39.032 -0.222  1.00 29.08 ?  32  GLY   A O   1 
ATOM   112  N N   . ARG   A 1 16  ? -6.409  40.184 -1.375  1.00 33.30 ?  33  ARG   A N   1 
ATOM   113  C CA  . ARG   A 1 16  ? -5.970  39.062 -2.192  1.00 33.32 ?  33  ARG   A CA  1 
ATOM   114  C C   . ARG   A 1 16  ? -4.667  38.446 -1.687  1.00 35.25 ?  33  ARG   A C   1 
ATOM   115  O O   . ARG   A 1 16  ? -4.024  37.683 -2.420  1.00 37.19 ?  33  ARG   A O   1 
ATOM   116  C CB  . ARG   A 1 16  ? -5.814  39.528 -3.638  1.00 38.41 ?  33  ARG   A CB  1 
ATOM   117  C CG  . ARG   A 1 16  ? -6.840  40.597 -4.015  1.00 45.30 ?  33  ARG   A CG  1 
ATOM   118  C CD  . ARG   A 1 16  ? -7.449  40.312 -5.359  1.00 49.81 ?  33  ARG   A CD  1 
ATOM   119  N NE  . ARG   A 1 16  ? -7.838  38.913 -5.447  1.00 45.51 ?  33  ARG   A NE  1 
ATOM   120  C CZ  . ARG   A 1 16  ? -8.211  38.315 -6.564  1.00 43.08 ?  33  ARG   A CZ  1 
ATOM   121  N NH1 . ARG   A 1 16  ? -8.204  38.956 -7.725  1.00 47.22 ?  33  ARG   A NH1 1 
ATOM   122  N NH2 . ARG   A 1 16  ? -8.581  37.037 -6.521  1.00 33.32 ?  33  ARG   A NH2 1 
ATOM   123  N N   . GLU   A 1 17  ? -4.265  38.782 -0.454  1.00 33.69 ?  34  GLU   A N   1 
ATOM   124  C CA  . GLU   A 1 17  ? -2.992  38.325 0.108   1.00 34.79 ?  34  GLU   A CA  1 
ATOM   125  C C   . GLU   A 1 17  ? -2.766  36.820 -0.012  1.00 34.50 ?  34  GLU   A C   1 
ATOM   126  O O   . GLU   A 1 17  ? -1.631  36.380 -0.248  1.00 35.72 ?  34  GLU   A O   1 
ATOM   127  C CB  . GLU   A 1 17  ? -2.887  38.773 1.567   1.00 36.68 ?  34  GLU   A CB  1 
ATOM   128  C CG  . GLU   A 1 17  ? -2.908  40.295 1.740   1.00 37.52 ?  34  GLU   A CG  1 
ATOM   129  C CD  . GLU   A 1 17  ? -4.244  40.859 2.156   1.00 33.36 ?  34  GLU   A CD  1 
ATOM   130  O OE1 . GLU   A 1 17  ? -5.265  40.331 1.692   1.00 33.33 ?  34  GLU   A OE1 1 
ATOM   131  O OE2 . GLU   A 1 17  ? -4.265  41.854 2.910   1.00 39.36 ?  34  GLU   A OE2 1 
ATOM   132  N N   . ASP   A 1 18  ? -3.815  36.016 0.154   1.00 32.46 ?  35  ASP   A N   1 
ATOM   133  C CA  . ASP   A 1 18  ? -3.683  34.565 0.152   1.00 32.35 ?  35  ASP   A CA  1 
ATOM   134  C C   . ASP   A 1 18  ? -4.101  33.926 -1.170  1.00 32.50 ?  35  ASP   A C   1 
ATOM   135  O O   . ASP   A 1 18  ? -4.300  32.711 -1.211  1.00 32.16 ?  35  ASP   A O   1 
ATOM   136  C CB  . ASP   A 1 18  ? -4.497  33.957 1.295   1.00 30.61 ?  35  ASP   A CB  1 
ATOM   137  C CG  . ASP   A 1 18  ? -3.832  34.136 2.656   1.00 31.80 ?  35  ASP   A CG  1 
ATOM   138  O OD1 . ASP   A 1 18  ? -2.624  34.453 2.707   1.00 35.06 ?  35  ASP   A OD1 1 
ATOM   139  O OD2 . ASP   A 1 18  ? -4.533  33.933 3.675   1.00 31.46 ?  35  ASP   A OD2 1 
ATOM   140  N N   . ARG   A 1 19  ? -4.205  34.713 -2.247  1.00 34.22 ?  36  ARG   A N   1 
ATOM   141  C CA  . ARG   A 1 19  ? -4.707  34.197 -3.523  1.00 33.67 ?  36  ARG   A CA  1 
ATOM   142  C C   . ARG   A 1 19  ? -3.935  32.971 -4.006  1.00 34.41 ?  36  ARG   A C   1 
ATOM   143  O O   . ARG   A 1 19  ? -4.534  32.019 -4.519  1.00 35.85 ?  36  ARG   A O   1 
ATOM   144  C CB  . ARG   A 1 19  ? -4.662  35.299 -4.579  1.00 38.36 ?  36  ARG   A CB  1 
ATOM   145  C CG  . ARG   A 1 19  ? -5.142  34.855 -5.949  1.00 43.88 ?  36  ARG   A CG  1 
ATOM   146  C CD  . ARG   A 1 19  ? -5.324  36.042 -6.874  1.00 46.37 ?  36  ARG   A CD  1 
ATOM   147  N NE  . ARG   A 1 19  ? -5.194  35.659 -8.274  1.00 49.51 ?  36  ARG   A NE  1 
ATOM   148  C CZ  . ARG   A 1 19  ? -5.106  36.521 -9.277  1.00 50.83 ?  36  ARG   A CZ  1 
ATOM   149  N NH1 . ARG   A 1 19  ? -5.113  37.830 -9.066  1.00 59.03 ?  36  ARG   A NH1 1 
ATOM   150  N NH2 . ARG   A 1 19  ? -4.982  36.062 -10.521 1.00 57.29 ?  36  ARG   A NH2 1 
ATOM   151  N N   . THR   A 1 20  ? -2.604  32.973 -3.866  1.00 35.95 ?  37  THR   A N   1 
ATOM   152  C CA  . THR   A 1 20  ? -1.820  31.847 -4.377  1.00 38.78 ?  37  THR   A CA  1 
ATOM   153  C C   . THR   A 1 20  ? -2.099  30.580 -3.581  1.00 37.89 ?  37  THR   A C   1 
ATOM   154  O O   . THR   A 1 20  ? -2.168  29.482 -4.148  1.00 40.64 ?  37  THR   A O   1 
ATOM   155  C CB  . THR   A 1 20  ? -0.328  32.177 -4.342  1.00 41.14 ?  37  THR   A CB  1 
ATOM   156  O OG1 . THR   A 1 20  ? -0.093  33.363 -5.102  1.00 43.46 ?  37  THR   A OG1 1 
ATOM   157  C CG2 . THR   A 1 20  ? 0.494   31.041 -4.943  1.00 43.99 ?  37  THR   A CG2 1 
ATOM   158  N N   . LEU   A 1 21  ? -2.251  30.716 -2.262  1.00 36.35 ?  38  LEU   A N   1 
ATOM   159  C CA  . LEU   A 1 21  ? -2.596  29.573 -1.430  1.00 35.79 ?  38  LEU   A CA  1 
ATOM   160  C C   . LEU   A 1 21  ? -3.967  29.018 -1.799  1.00 33.54 ?  38  LEU   A C   1 
ATOM   161  O O   . LEU   A 1 21  ? -4.172  27.801 -1.794  1.00 35.67 ?  38  LEU   A O   1 
ATOM   162  C CB  . LEU   A 1 21  ? -2.563  29.990 0.039   1.00 36.21 ?  38  LEU   A CB  1 
ATOM   163  C CG  . LEU   A 1 21  ? -3.128  28.996 1.044   1.00 38.35 ?  38  LEU   A CG  1 
ATOM   164  C CD1 . LEU   A 1 21  ? -2.311  27.723 1.009   1.00 40.20 ?  38  LEU   A CD1 1 
ATOM   165  C CD2 . LEU   A 1 21  ? -3.158  29.607 2.439   1.00 39.94 ?  38  LEU   A CD2 1 
ATOM   166  N N   . TYR   A 1 22  ? -4.925  29.898 -2.101  1.00 33.74 ?  39  TYR   A N   1 
ATOM   167  C CA  . TYR   A 1 22  ? -6.251  29.431 -2.503  1.00 29.91 ?  39  TYR   A CA  1 
ATOM   168  C C   . TYR   A 1 22  ? -6.174  28.577 -3.759  1.00 32.99 ?  39  TYR   A C   1 
ATOM   169  O O   . TYR   A 1 22  ? -6.874  27.564 -3.879  1.00 33.18 ?  39  TYR   A O   1 
ATOM   170  C CB  . TYR   A 1 22  ? -7.189  30.608 -2.769  1.00 30.00 ?  39  TYR   A CB  1 
ATOM   171  C CG  . TYR   A 1 22  ? -7.426  31.577 -1.627  1.00 27.33 ?  39  TYR   A CG  1 
ATOM   172  C CD1 . TYR   A 1 22  ? -7.191  31.227 -0.287  1.00 28.42 ?  39  TYR   A CD1 1 
ATOM   173  C CD2 . TYR   A 1 22  ? -7.882  32.856 -1.906  1.00 26.90 ?  39  TYR   A CD2 1 
ATOM   174  C CE1 . TYR   A 1 22  ? -7.394  32.154 0.731   1.00 28.54 ?  39  TYR   A CE1 1 
ATOM   175  C CE2 . TYR   A 1 22  ? -8.091  33.779 -0.908  1.00 27.91 ?  39  TYR   A CE2 1 
ATOM   176  C CZ  . TYR   A 1 22  ? -7.849  33.426 0.410   1.00 28.94 ?  39  TYR   A CZ  1 
ATOM   177  O OH  . TYR   A 1 22  ? -8.068  34.378 1.366   1.00 25.46 ?  39  TYR   A OH  1 
ATOM   178  N N   . GLU   A 1 23  ? -5.350  28.993 -4.724  1.00 34.50 ?  40  GLU   A N   1 
ATOM   179  C CA  . GLU   A 1 23  ? -5.175  28.205 -5.938  1.00 34.84 ?  40  GLU   A CA  1 
ATOM   180  C C   . GLU   A 1 23  ? -4.605  26.833 -5.608  1.00 37.73 ?  40  GLU   A C   1 
ATOM   181  O O   . GLU   A 1 23  ? -5.000  25.825 -6.201  1.00 34.76 ?  40  GLU   A O   1 
ATOM   182  C CB  . GLU   A 1 23  ? -4.254  28.940 -6.915  1.00 36.36 ?  40  GLU   A CB  1 
ATOM   183  C CG  . GLU   A 1 23  ? -4.877  30.160 -7.596  1.00 40.99 ?  40  GLU   A CG  1 
ATOM   184  C CD  . GLU   A 1 23  ? -3.852  31.006 -8.364  1.00 45.68 ?  40  GLU   A CD  1 
ATOM   185  O OE1 . GLU   A 1 23  ? -4.038  32.239 -8.462  1.00 50.35 ?  40  GLU   A OE1 1 
ATOM   186  O OE2 . GLU   A 1 23  ? -2.864  30.445 -8.886  1.00 56.16 ?  40  GLU   A OE2 1 
ATOM   187  N N   . ARG   A 1 24  ? -3.669  26.780 -4.662  1.00 35.28 ?  41  ARG   A N   1 
ATOM   188  C CA  . ARG   A 1 24  ? -3.114  25.507 -4.221  1.00 36.52 ?  41  ARG   A CA  1 
ATOM   189  C C   . ARG   A 1 24  ? -4.191  24.639 -3.582  1.00 37.13 ?  41  ARG   A C   1 
ATOM   190  O O   . ARG   A 1 24  ? -4.267  23.433 -3.846  1.00 37.11 ?  41  ARG   A O   1 
ATOM   191  C CB  . ARG   A 1 24  ? -1.965  25.775 -3.244  1.00 41.97 ?  41  ARG   A CB  1 
ATOM   192  C CG  . ARG   A 1 24  ? -1.277  24.560 -2.669  1.00 46.69 ?  41  ARG   A CG  1 
ATOM   193  C CD  . ARG   A 1 24  ? -0.398  24.967 -1.492  1.00 50.65 ?  41  ARG   A CD  1 
ATOM   194  N NE  . ARG   A 1 24  ? -0.023  23.817 -0.684  1.00 55.25 ?  41  ARG   A NE  1 
ATOM   195  C CZ  . ARG   A 1 24  ? 0.864   23.849 0.299   1.00 58.94 ?  41  ARG   A CZ  1 
ATOM   196  N NH1 . ARG   A 1 24  ? 1.418   24.985 0.690   1.00 57.43 ?  41  ARG   A NH1 1 
ATOM   197  N NH2 . ARG   A 1 24  ? 1.186   22.716 0.919   1.00 62.43 ?  41  ARG   A NH2 1 
ATOM   198  N N   . ILE   A 1 25  ? -5.045  25.237 -2.747  1.00 33.16 ?  42  ILE   A N   1 
ATOM   199  C CA  . ILE   A 1 25  ? -6.104  24.468 -2.103  1.00 31.84 ?  42  ILE   A CA  1 
ATOM   200  C C   . ILE   A 1 25  ? -7.102  23.966 -3.142  1.00 32.56 ?  42  ILE   A C   1 
ATOM   201  O O   . ILE   A 1 25  ? -7.515  22.799 -3.112  1.00 33.58 ?  42  ILE   A O   1 
ATOM   202  C CB  . ILE   A 1 25  ? -6.797  25.316 -1.025  1.00 31.83 ?  42  ILE   A CB  1 
ATOM   203  C CG1 . ILE   A 1 25  ? -5.858  25.552 0.158   1.00 36.07 ?  42  ILE   A CG1 1 
ATOM   204  C CG2 . ILE   A 1 25  ? -8.045  24.600 -0.527  1.00 31.71 ?  42  ILE   A CG2 1 
ATOM   205  C CD1 . ILE   A 1 25  ? -6.460  26.477 1.188   1.00 32.33 ?  42  ILE   A CD1 1 
ATOM   206  N N   . VAL   A 1 26  ? -7.481  24.825 -4.091  1.00 31.82 ?  43  VAL   A N   1 
ATOM   207  C CA  . VAL   A 1 26  ? -8.466  24.433 -5.096  1.00 33.27 ?  43  VAL   A CA  1 
ATOM   208  C C   . VAL   A 1 26  ? -7.910  23.323 -5.980  1.00 36.01 ?  43  VAL   A C   1 
ATOM   209  O O   . VAL   A 1 26  ? -8.636  22.396 -6.358  1.00 34.98 ?  43  VAL   A O   1 
ATOM   210  C CB  . VAL   A 1 26  ? -8.910  25.654 -5.927  1.00 32.56 ?  43  VAL   A CB  1 
ATOM   211  C CG1 . VAL   A 1 26  ? -9.595  25.217 -7.215  1.00 34.87 ?  43  VAL   A CG1 1 
ATOM   212  C CG2 . VAL   A 1 26  ? -9.844  26.544 -5.108  1.00 29.38 ?  43  VAL   A CG2 1 
ATOM   213  N N   . SER   A 1 27  ? -6.615  23.394 -6.318  1.00 35.67 ?  44  SER   A N   1 
ATOM   214  C CA  . SER   A 1 27  ? -5.989  22.334 -7.103  1.00 36.50 ?  44  SER   A CA  1 
ATOM   215  C C   . SER   A 1 27  ? -6.123  20.984 -6.410  1.00 38.06 ?  44  SER   A C   1 
ATOM   216  O O   . SER   A 1 27  ? -6.377  19.966 -7.064  1.00 41.61 ?  44  SER   A O   1 
ATOM   217  C CB  A SER   A 1 27  ? -4.511  22.650 -7.349  0.55 38.90 ?  44  SER   A CB  1 
ATOM   218  C CB  B SER   A 1 27  ? -4.518  22.669 -7.362  0.45 38.91 ?  44  SER   A CB  1 
ATOM   219  O OG  A SER   A 1 27  ? -4.346  23.566 -8.414  0.55 41.20 ?  44  SER   A OG  1 
ATOM   220  O OG  B SER   A 1 27  ? -3.866  21.622 -8.058  0.45 40.10 ?  44  SER   A OG  1 
ATOM   221  N N   . ARG   A 1 28  ? -5.949  20.950 -5.087  1.00 39.30 ?  45  ARG   A N   1 
ATOM   222  C CA  . ARG   A 1 28  ? -6.082  19.683 -4.377  1.00 40.18 ?  45  ARG   A CA  1 
ATOM   223  C C   . ARG   A 1 28  ? -7.541  19.275 -4.248  1.00 38.20 ?  45  ARG   A C   1 
ATOM   224  O O   . ARG   A 1 28  ? -7.861  18.084 -4.338  1.00 38.77 ?  45  ARG   A O   1 
ATOM   225  C CB  . ARG   A 1 28  ? -5.415  19.777 -3.001  1.00 41.74 ?  45  ARG   A CB  1 
ATOM   226  C CG  . ARG   A 1 28  ? -5.474  18.495 -2.173  1.00 46.95 ?  45  ARG   A CG  1 
ATOM   227  C CD  . ARG   A 1 28  ? -5.035  17.296 -3.004  1.00 52.34 ?  45  ARG   A CD  1 
ATOM   228  N NE  . ARG   A 1 28  ? -3.599  17.288 -3.249  1.00 57.26 ?  45  ARG   A NE  1 
ATOM   229  C CZ  . ARG   A 1 28  ? -2.747  16.416 -2.730  1.00 57.26 ?  45  ARG   A CZ  1 
ATOM   230  N NH1 . ARG   A 1 28  ? -3.153  15.452 -1.921  1.00 59.14 ?  45  ARG   A NH1 1 
ATOM   231  N NH2 . ARG   A 1 28  ? -1.458  16.511 -3.036  1.00 59.82 ?  45  ARG   A NH2 1 
ATOM   232  N N   . LEU   A 1 29  ? -8.437  20.252 -4.079  1.00 35.05 ?  46  LEU   A N   1 
ATOM   233  C CA  . LEU   A 1 29  ? -9.863  19.956 -4.018  1.00 35.72 ?  46  LEU   A CA  1 
ATOM   234  C C   . LEU   A 1 29  ? -10.349 19.295 -5.300  1.00 36.11 ?  46  LEU   A C   1 
ATOM   235  O O   . LEU   A 1 29  ? -11.264 18.467 -5.260  1.00 36.93 ?  46  LEU   A O   1 
ATOM   236  C CB  . LEU   A 1 29  ? -10.647 21.243 -3.750  1.00 35.88 ?  46  LEU   A CB  1 
ATOM   237  C CG  . LEU   A 1 29  ? -10.581 21.852 -2.351  1.00 32.97 ?  46  LEU   A CG  1 
ATOM   238  C CD1 . LEU   A 1 29  ? -11.482 23.087 -2.263  1.00 30.04 ?  46  LEU   A CD1 1 
ATOM   239  C CD2 . LEU   A 1 29  ? -10.981 20.831 -1.280  1.00 32.13 ?  46  LEU   A CD2 1 
ATOM   240  N N   . ARG   A 1 30  ? -9.739  19.625 -6.439  1.00 34.85 ?  47  ARG   A N   1 
ATOM   241  C CA  . ARG   A 1 30  ? -10.177 19.042 -7.702  1.00 37.37 ?  47  ARG   A CA  1 
ATOM   242  C C   . ARG   A 1 30  ? -9.994  17.532 -7.726  1.00 39.08 ?  47  ARG   A C   1 
ATOM   243  O O   . ARG   A 1 30  ? -10.658 16.850 -8.513  1.00 40.38 ?  47  ARG   A O   1 
ATOM   244  C CB  . ARG   A 1 30  ? -9.427  19.688 -8.869  1.00 37.89 ?  47  ARG   A CB  1 
ATOM   245  C CG  . ARG   A 1 30  ? -9.946  21.084 -9.177  1.00 40.66 ?  47  ARG   A CG  1 
ATOM   246  C CD  . ARG   A 1 30  ? -9.473  21.659 -10.501 1.00 47.33 ?  47  ARG   A CD  1 
ATOM   247  N NE  . ARG   A 1 30  ? -8.027  21.591 -10.657 1.00 50.65 ?  47  ARG   A NE  1 
ATOM   248  C CZ  . ARG   A 1 30  ? -7.216  22.640 -10.589 1.00 49.97 ?  47  ARG   A CZ  1 
ATOM   249  N NH1 . ARG   A 1 30  ? -7.648  23.824 -10.173 1.00 44.01 ?  47  ARG   A NH1 1 
ATOM   250  N NH2 . ARG   A 1 30  ? -5.928  22.485 -10.890 1.00 51.41 ?  47  ARG   A NH2 1 
ATOM   251  N N   . ARG   A 1 31  ? -9.117  16.990 -6.878  1.00 40.43 ?  48  ARG   A N   1 
ATOM   252  C CA  . ARG   A 1 31  ? -8.996  15.540 -6.798  1.00 41.81 ?  48  ARG   A CA  1 
ATOM   253  C C   . ARG   A 1 31  ? -10.254 14.900 -6.232  1.00 44.13 ?  48  ARG   A C   1 
ATOM   254  O O   . ARG   A 1 31  ? -10.472 13.700 -6.432  1.00 41.77 ?  48  ARG   A O   1 
ATOM   255  C CB  . ARG   A 1 31  ? -7.799  15.138 -5.935  1.00 45.28 ?  48  ARG   A CB  1 
ATOM   256  C CG  . ARG   A 1 31  ? -6.453  15.594 -6.452  1.00 48.09 ?  48  ARG   A CG  1 
ATOM   257  C CD  . ARG   A 1 31  ? -5.358  14.734 -5.850  1.00 53.86 ?  48  ARG   A CD  1 
ATOM   258  N NE  . ARG   A 1 31  ? -4.026  15.140 -6.279  1.00 60.52 ?  48  ARG   A NE  1 
ATOM   259  C CZ  . ARG   A 1 31  ? -2.902  14.664 -5.760  1.00 63.29 ?  48  ARG   A CZ  1 
ATOM   260  N NH1 . ARG   A 1 31  ? -2.917  13.746 -4.808  1.00 64.72 ?  48  ARG   A NH1 1 
ATOM   261  N NH2 . ARG   A 1 31  ? -1.735  15.106 -6.221  1.00 63.29 ?  48  ARG   A NH2 1 
ATOM   262  N N   . PHE   A 1 32  ? -11.083 15.672 -5.534  1.00 38.18 ?  49  PHE   A N   1 
ATOM   263  C CA  . PHE   A 1 32  ? -12.189 15.118 -4.781  1.00 40.45 ?  49  PHE   A CA  1 
ATOM   264  C C   . PHE   A 1 32  ? -13.551 15.550 -5.293  1.00 38.22 ?  49  PHE   A C   1 
ATOM   265  O O   . PHE   A 1 32  ? -14.563 15.069 -4.771  1.00 39.01 ?  49  PHE   A O   1 
ATOM   266  C CB  . PHE   A 1 32  ? -12.050 15.516 -3.307  1.00 38.91 ?  49  PHE   A CB  1 
ATOM   267  C CG  . PHE   A 1 32  ? -10.794 14.995 -2.677  1.00 42.51 ?  49  PHE   A CG  1 
ATOM   268  C CD1 . PHE   A 1 32  ? -10.563 13.635 -2.582  1.00 43.43 ?  49  PHE   A CD1 1 
ATOM   269  C CD2 . PHE   A 1 32  ? -9.821  15.869 -2.222  1.00 43.50 ?  49  PHE   A CD2 1 
ATOM   270  C CE1 . PHE   A 1 32  ? -9.397  13.157 -2.021  1.00 48.17 ?  49  PHE   A CE1 1 
ATOM   271  C CE2 . PHE   A 1 32  ? -8.653  15.393 -1.654  1.00 44.81 ?  49  PHE   A CE2 1 
ATOM   272  C CZ  . PHE   A 1 32  ? -8.443  14.037 -1.554  1.00 46.30 ?  49  PHE   A CZ  1 
ATOM   273  N N   . GLY   A 1 33  ? -13.610 16.437 -6.277  1.00 35.98 ?  50  GLY   A N   1 
ATOM   274  C CA  . GLY   A 1 33  ? -14.885 16.873 -6.809  1.00 35.60 ?  50  GLY   A CA  1 
ATOM   275  C C   . GLY   A 1 33  ? -14.711 18.072 -7.713  1.00 35.29 ?  50  GLY   A C   1 
ATOM   276  O O   . GLY   A 1 33  ? -13.597 18.539 -7.967  1.00 35.46 ?  50  GLY   A O   1 
ATOM   277  N N   . THR   A 1 34  ? -15.846 18.552 -8.211  1.00 32.02 ?  51  THR   A N   1 
ATOM   278  C CA  . THR   A 1 34  ? -15.892 19.727 -9.074  1.00 32.08 ?  51  THR   A CA  1 
ATOM   279  C C   . THR   A 1 34  ? -15.934 20.975 -8.206  1.00 32.09 ?  51  THR   A C   1 
ATOM   280  O O   . THR   A 1 34  ? -16.795 21.084 -7.330  1.00 32.33 ?  51  THR   A O   1 
ATOM   281  C CB  . THR   A 1 34  ? -17.141 19.702 -9.952  1.00 35.03 ?  51  THR   A CB  1 
ATOM   282  O OG1 . THR   A 1 34  ? -17.294 18.404 -10.528 1.00 43.46 ?  51  THR   A OG1 1 
ATOM   283  C CG2 . THR   A 1 34  ? -16.983 20.695 -11.060 1.00 36.04 ?  51  THR   A CG2 1 
ATOM   284  N N   . VAL   A 1 35  ? -15.035 21.926 -8.458  1.00 32.11 ?  52  VAL   A N   1 
ATOM   285  C CA  . VAL   A 1 35  ? -14.964 23.139 -7.644  1.00 26.85 ?  52  VAL   A CA  1 
ATOM   286  C C   . VAL   A 1 35  ? -15.732 24.239 -8.376  1.00 28.99 ?  52  VAL   A C   1 
ATOM   287  O O   . VAL   A 1 35  ? -15.215 24.860 -9.316  1.00 30.12 ?  52  VAL   A O   1 
ATOM   288  C CB  . VAL   A 1 35  ? -13.520 23.547 -7.356  1.00 26.88 ?  52  VAL   A CB  1 
ATOM   289  C CG1 . VAL   A 1 35  ? -13.506 24.785 -6.464  1.00 27.35 ?  52  VAL   A CG1 1 
ATOM   290  C CG2 . VAL   A 1 35  ? -12.763 22.400 -6.689  1.00 29.82 ?  52  VAL   A CG2 1 
ATOM   291  N N   . LEU   A 1 36  ? -16.971 24.502 -7.932  1.00 26.42 ?  53  LEU   A N   1 
ATOM   292  C CA  . LEU   A 1 36  ? -17.870 25.373 -8.691  1.00 27.36 ?  53  LEU   A CA  1 
ATOM   293  C C   . LEU   A 1 36  ? -17.360 26.802 -8.802  1.00 28.17 ?  53  LEU   A C   1 
ATOM   294  O O   . LEU   A 1 36  ? -17.678 27.501 -9.772  1.00 28.11 ?  53  LEU   A O   1 
ATOM   295  C CB  . LEU   A 1 36  ? -19.267 25.346 -8.065  1.00 30.00 ?  53  LEU   A CB  1 
ATOM   296  C CG  . LEU   A 1 36  ? -19.894 23.964 -7.918  1.00 29.81 ?  53  LEU   A CG  1 
ATOM   297  C CD1 . LEU   A 1 36  ? -21.184 24.057 -7.115  1.00 29.22 ?  53  LEU   A CD1 1 
ATOM   298  C CD2 . LEU   A 1 36  ? -20.185 23.438 -9.300  1.00 33.19 ?  53  LEU   A CD2 1 
ATOM   299  N N   . THR   A 1 37  ? -16.553 27.250 -7.848  1.00 27.36 ?  54  THR   A N   1 
ATOM   300  C CA  . THR   A 1 37  ? -16.104 28.634 -7.798  1.00 25.70 ?  54  THR   A CA  1 
ATOM   301  C C   . THR   A 1 37  ? -14.744 28.832 -8.461  1.00 26.44 ?  54  THR   A C   1 
ATOM   302  O O   . THR   A 1 37  ? -14.218 29.947 -8.428  1.00 26.90 ?  54  THR   A O   1 
ATOM   303  C CB  . THR   A 1 37  ? -16.010 29.074 -6.345  1.00 26.37 ?  54  THR   A CB  1 
ATOM   304  O OG1 . THR   A 1 37  ? -15.346 28.035 -5.630  1.00 27.11 ?  54  THR   A OG1 1 
ATOM   305  C CG2 . THR   A 1 37  ? -17.413 29.223 -5.759  1.00 25.61 ?  54  THR   A CG2 1 
ATOM   306  N N   . GLU   A 1 38  ? -14.180 27.773 -9.054  1.00 27.34 ?  55  GLU   A N   1 
ATOM   307  C CA  . GLU   A 1 38  ? -12.795 27.764 -9.526  1.00 29.24 ?  55  GLU   A CA  1 
ATOM   308  C C   . GLU   A 1 38  ? -12.474 28.924 -10.464 1.00 30.77 ?  55  GLU   A C   1 
ATOM   309  O O   . GLU   A 1 38  ? -11.462 29.617 -10.295 1.00 28.69 ?  55  GLU   A O   1 
ATOM   310  C CB  . GLU   A 1 38  ? -12.523 26.454 -10.266 1.00 34.08 ?  55  GLU   A CB  1 
ATOM   311  C CG  . GLU   A 1 38  ? -11.178 26.438 -10.953 1.00 39.18 ?  55  GLU   A CG  1 
ATOM   312  C CD  . GLU   A 1 38  ? -10.699 25.039 -11.285 1.00 44.29 ?  55  GLU   A CD  1 
ATOM   313  O OE1 . GLU   A 1 38  ? -11.558 24.150 -11.500 1.00 44.37 ?  55  GLU   A OE1 1 
ATOM   314  O OE2 . GLU   A 1 38  ? -9.460  24.842 -11.343 1.00 49.93 ?  55  GLU   A OE2 1 
ATOM   315  N N   . HIS   A 1 39  ? -13.286 29.107 -11.498 1.00 26.96 ?  56  HIS   A N   1 
ATOM   316  C CA  . HIS   A 1 39  ? -12.918 30.011 -12.592 1.00 27.92 ?  56  HIS   A CA  1 
ATOM   317  C C   . HIS   A 1 39  ? -13.321 31.458 -12.378 1.00 27.10 ?  56  HIS   A C   1 
ATOM   318  O O   . HIS   A 1 39  ? -12.981 32.303 -13.216 1.00 25.81 ?  56  HIS   A O   1 
ATOM   319  C CB  . HIS   A 1 39  ? -13.510 29.526 -13.922 1.00 26.67 ?  56  HIS   A CB  1 
ATOM   320  C CG  . HIS   A 1 39  ? -13.269 28.081 -14.199 1.00 29.63 ?  56  HIS   A CG  1 
ATOM   321  N ND1 . HIS   A 1 39  ? -12.000 27.561 -14.339 1.00 32.48 ?  56  HIS   A ND1 1 
ATOM   322  C CD2 . HIS   A 1 39  ? -14.121 27.039 -14.336 1.00 30.31 ?  56  HIS   A CD2 1 
ATOM   323  C CE1 . HIS   A 1 39  ? -12.085 26.263 -14.568 1.00 33.36 ?  56  HIS   A CE1 1 
ATOM   324  N NE2 . HIS   A 1 39  ? -13.360 25.921 -14.565 1.00 33.38 ?  56  HIS   A NE2 1 
ATOM   325  N N   . VAL   A 1 40  ? -14.035 31.774 -11.303 1.00 27.25 ?  57  VAL   A N   1 
ATOM   326  C CA  . VAL   A 1 40  ? -14.359 33.155 -10.974 1.00 27.94 ?  57  VAL   A CA  1 
ATOM   327  C C   . VAL   A 1 40  ? -13.545 33.660 -9.788  1.00 27.91 ?  57  VAL   A C   1 
ATOM   328  O O   . VAL   A 1 40  ? -13.780 34.772 -9.307  1.00 27.41 ?  57  VAL   A O   1 
ATOM   329  C CB  . VAL   A 1 40  ? -15.870 33.325 -10.736 1.00 28.96 ?  57  VAL   A CB  1 
ATOM   330  C CG1 . VAL   A 1 40  ? -16.617 33.068 -12.035 1.00 28.69 ?  57  VAL   A CG1 1 
ATOM   331  C CG2 . VAL   A 1 40  ? -16.347 32.340 -9.677  1.00 26.25 ?  57  VAL   A CG2 1 
ATOM   332  N N   . ALA   A 1 41  ? -12.549 32.892 -9.343  1.00 26.05 ?  58  ALA   A N   1 
ATOM   333  C CA  . ALA   A 1 41  ? -11.758 33.264 -8.165  1.00 29.00 ?  58  ALA   A CA  1 
ATOM   334  C C   . ALA   A 1 41  ? -10.751 34.380 -8.450  1.00 28.95 ?  58  ALA   A C   1 
ATOM   335  O O   . ALA   A 1 41  ? -10.380 35.129 -7.535  1.00 30.93 ?  58  ALA   A O   1 
ATOM   336  C CB  . ALA   A 1 41  ? -11.025 32.028 -7.647  1.00 27.73 ?  58  ALA   A CB  1 
ATOM   337  N N   . ALA   A 1 42  ? -10.291 34.509 -9.700  1.00 28.92 ?  59  ALA   A N   1 
ATOM   338  C CA  . ALA   A 1 42  ? -9.190  35.412 -10.006 1.00 31.74 ?  59  ALA   A CA  1 
ATOM   339  C C   . ALA   A 1 42  ? -9.626  36.871 -10.123 1.00 30.43 ?  59  ALA   A C   1 
ATOM   340  O O   . ALA   A 1 42  ? -8.791  37.769 -9.953  1.00 30.75 ?  59  ALA   A O   1 
ATOM   341  C CB  . ALA   A 1 42  ? -8.496  34.976 -11.303 1.00 32.58 ?  59  ALA   A CB  1 
ATOM   342  N N   . ALA   A 1 43  ? -10.897 37.126 -10.452 1.00 28.71 ?  60  ALA   A N   1 
ATOM   343  C CA  . ALA   A 1 43  ? -11.449 38.485 -10.516 1.00 27.66 ?  60  ALA   A CA  1 
ATOM   344  C C   . ALA   A 1 43  ? -10.601 39.382 -11.411 1.00 29.09 ?  60  ALA   A C   1 
ATOM   345  O O   . ALA   A 1 43  ? -10.173 40.474 -11.029 1.00 31.42 ?  60  ALA   A O   1 
ATOM   346  C CB  . ALA   A 1 43  ? -11.592 39.091 -9.118  1.00 29.36 ?  60  ALA   A CB  1 
ATOM   347  N N   . GLU   A 1 44  ? -10.354 38.897 -12.629 1.00 30.00 ?  61  GLU   A N   1 
ATOM   348  C CA  . GLU   A 1 44  ? -9.424  39.568 -13.529 1.00 31.19 ?  61  GLU   A CA  1 
ATOM   349  C C   . GLU   A 1 44  ? -9.845  40.995 -13.855 1.00 31.92 ?  61  GLU   A C   1 
ATOM   350  O O   . GLU   A 1 44  ? -8.987  41.841 -14.136 1.00 34.84 ?  61  GLU   A O   1 
ATOM   351  C CB  . GLU   A 1 44  ? -9.280  38.751 -14.813 1.00 32.77 ?  61  GLU   A CB  1 
ATOM   352  C CG  . GLU   A 1 44  ? -8.592  37.405 -14.607 1.00 34.23 ?  61  GLU   A CG  1 
ATOM   353  C CD  . GLU   A 1 44  ? -9.570  36.268 -14.444 1.00 31.34 ?  61  GLU   A CD  1 
ATOM   354  O OE1 . GLU   A 1 44  ? -10.745 36.542 -14.111 1.00 30.75 ?  61  GLU   A OE1 1 
ATOM   355  O OE2 . GLU   A 1 44  ? -9.165  35.101 -14.667 1.00 33.93 ?  61  GLU   A OE2 1 
ATOM   356  N N   . LEU   A 1 45  ? -11.145 41.284 -13.853 1.00 30.99 ?  62  LEU   A N   1 
ATOM   357  C CA  . LEU   A 1 45  ? -11.596 42.634 -14.166 1.00 31.79 ?  62  LEU   A CA  1 
ATOM   358  C C   . LEU   A 1 45  ? -11.240 43.635 -13.077 1.00 35.76 ?  62  LEU   A C   1 
ATOM   359  O O   . LEU   A 1 45  ? -11.331 44.846 -13.305 1.00 35.68 ?  62  LEU   A O   1 
ATOM   360  C CB  . LEU   A 1 45  ? -13.110 42.616 -14.380 1.00 32.29 ?  62  LEU   A CB  1 
ATOM   361  C CG  . LEU   A 1 45  ? -13.654 41.795 -15.550 1.00 32.60 ?  62  LEU   A CG  1 
ATOM   362  C CD1 . LEU   A 1 45  ? -15.172 41.840 -15.539 1.00 30.81 ?  62  LEU   A CD1 1 
ATOM   363  C CD2 . LEU   A 1 45  ? -13.137 42.351 -16.873 1.00 33.60 ?  62  LEU   A CD2 1 
ATOM   364  N N   . GLY   A 1 46  ? -10.849 43.159 -11.908 1.00 34.17 ?  63  GLY   A N   1 
ATOM   365  C CA  . GLY   A 1 46  ? -10.656 44.023 -10.766 1.00 35.61 ?  63  GLY   A CA  1 
ATOM   366  C C   . GLY   A 1 46  ? -11.970 44.301 -10.059 1.00 34.85 ?  63  GLY   A C   1 
ATOM   367  O O   . GLY   A 1 46  ? -13.059 44.158 -10.616 1.00 31.97 ?  63  GLY   A O   1 
ATOM   368  N N   . ALA   A 1 47  ? -11.857 44.685 -8.782  1.00 33.91 ?  64  ALA   A N   1 
ATOM   369  C CA  . ALA   A 1 47  ? -13.055 45.005 -8.018  1.00 37.56 ?  64  ALA   A CA  1 
ATOM   370  C C   . ALA   A 1 47  ? -13.780 46.210 -8.608  1.00 34.40 ?  64  ALA   A C   1 
ATOM   371  O O   . ALA   A 1 47  ? -15.004 46.183 -8.783  1.00 33.28 ?  64  ALA   A O   1 
ATOM   372  C CB  . ALA   A 1 47  ? -12.695 45.246 -6.549  1.00 36.60 ?  64  ALA   A CB  1 
ATOM   373  N N   . ARG   A 1 48  ? -13.044 47.285 -8.918  1.00 36.91 ?  65  ARG   A N   1 
ATOM   374  C CA  . ARG   A 1 48  ? -13.683 48.441 -9.544  1.00 36.87 ?  65  ARG   A CA  1 
ATOM   375  C C   . ARG   A 1 48  ? -14.294 48.069 -10.884 1.00 36.22 ?  65  ARG   A C   1 
ATOM   376  O O   . ARG   A 1 48  ? -15.386 48.536 -11.221 1.00 38.97 ?  65  ARG   A O   1 
ATOM   377  C CB  . ARG   A 1 48  ? -12.696 49.599 -9.721  1.00 41.73 ?  65  ARG   A CB  1 
ATOM   378  C CG  . ARG   A 1 48  ? -11.885 49.942 -8.486  1.00 44.96 ?  65  ARG   A CG  1 
ATOM   379  C CD  . ARG   A 1 48  ? -10.379 49.800 -8.745  1.00 52.57 ?  65  ARG   A CD  1 
ATOM   380  N NE  . ARG   A 1 48  ? -10.004 48.394 -8.890  1.00 54.13 ?  65  ARG   A NE  1 
ATOM   381  C CZ  . ARG   A 1 48  ? -9.832  47.560 -7.874  1.00 45.42 ?  65  ARG   A CZ  1 
ATOM   382  N NH1 . ARG   A 1 48  ? -10.034 47.944 -6.623  1.00 55.89 ?  65  ARG   A NH1 1 
ATOM   383  N NH2 . ARG   A 1 48  ? -9.439  46.313 -8.115  1.00 50.21 ?  65  ARG   A NH2 1 
ATOM   384  N N   . GLY   A 1 49  ? -13.610 47.219 -11.656 1.00 37.46 ?  66  GLY   A N   1 
ATOM   385  C CA  . GLY   A 1 49  ? -14.141 46.814 -12.951 1.00 35.54 ?  66  GLY   A CA  1 
ATOM   386  C C   . GLY   A 1 49  ? -15.425 46.011 -12.844 1.00 34.71 ?  66  GLY   A C   1 
ATOM   387  O O   . GLY   A 1 49  ? -16.366 46.224 -13.615 1.00 35.22 ?  66  GLY   A O   1 
ATOM   388  N N   . GLU   A 1 50  ? -15.479 45.066 -11.894 1.00 31.55 ?  67  GLU   A N   1 
ATOM   389  C CA  . GLU   A 1 50  ? -16.698 44.289 -11.710 1.00 31.53 ?  67  GLU   A CA  1 
ATOM   390  C C   . GLU   A 1 50  ? -17.836 45.172 -11.226 1.00 32.85 ?  67  GLU   A C   1 
ATOM   391  O O   . GLU   A 1 50  ? -18.974 45.060 -11.704 1.00 31.99 ?  67  GLU   A O   1 
ATOM   392  C CB  . GLU   A 1 50  ? -16.455 43.144 -10.724 1.00 30.98 ?  67  GLU   A CB  1 
ATOM   393  C CG  . GLU   A 1 50  ? -15.536 42.075 -11.246 1.00 28.83 ?  67  GLU   A CG  1 
ATOM   394  C CD  . GLU   A 1 50  ? -15.274 40.982 -10.229 1.00 30.97 ?  67  GLU   A CD  1 
ATOM   395  O OE1 . GLU   A 1 50  ? -15.627 41.163 -9.041  1.00 30.26 ?  67  GLU   A OE1 1 
ATOM   396  O OE2 . GLU   A 1 50  ? -14.743 39.925 -10.636 1.00 30.12 ?  67  GLU   A OE2 1 
ATOM   397  N N   . GLU   A 1 51  ? -17.545 46.056 -10.269 1.00 33.75 ?  68  GLU   A N   1 
ATOM   398  C CA  . GLU   A 1 51  ? -18.549 47.006 -9.816  1.00 36.85 ?  68  GLU   A CA  1 
ATOM   399  C C   . GLU   A 1 51  ? -19.053 47.852 -10.978 1.00 34.69 ?  68  GLU   A C   1 
ATOM   400  O O   . GLU   A 1 51  ? -20.265 48.032 -11.142 1.00 40.66 ?  68  GLU   A O   1 
ATOM   401  C CB  . GLU   A 1 51  ? -17.957 47.882 -8.709  1.00 37.30 ?  68  GLU   A CB  1 
ATOM   402  C CG  . GLU   A 1 51  ? -18.953 48.478 -7.743  1.00 41.19 ?  68  GLU   A CG  1 
ATOM   403  C CD  . GLU   A 1 51  ? -18.283 49.420 -6.751  1.00 46.37 ?  68  GLU   A CD  1 
ATOM   404  O OE1 . GLU   A 1 51  ? -17.346 50.154 -7.152  1.00 45.60 ?  68  GLU   A OE1 1 
ATOM   405  O OE2 . GLU   A 1 51  ? -18.679 49.417 -5.565  1.00 48.43 ?  68  GLU   A OE2 1 
ATOM   406  N N   . ALA   A 1 52  ? -18.137 48.334 -11.825 1.00 34.07 ?  69  ALA   A N   1 
ATOM   407  C CA  . ALA   A 1 52  ? -18.514 49.184 -12.951 1.00 37.01 ?  69  ALA   A CA  1 
ATOM   408  C C   . ALA   A 1 52  ? -19.393 48.445 -13.952 1.00 34.39 ?  69  ALA   A C   1 
ATOM   409  O O   . ALA   A 1 52  ? -20.243 49.061 -14.602 1.00 34.90 ?  69  ALA   A O   1 
ATOM   410  C CB  . ALA   A 1 52  ? -17.265 49.717 -13.654 1.00 40.73 ?  69  ALA   A CB  1 
ATOM   411  N N   . ALA   A 1 53  ? -19.206 47.134 -14.097 1.00 33.82 ?  70  ALA   A N   1 
ATOM   412  C CA  . ALA   A 1 53  ? -20.088 46.369 -14.977 1.00 32.11 ?  70  ALA   A CA  1 
ATOM   413  C C   . ALA   A 1 53  ? -21.472 46.168 -14.366 1.00 31.14 ?  70  ALA   A C   1 
ATOM   414  O O   . ALA   A 1 53  ? -22.374 45.669 -15.049 1.00 29.62 ?  70  ALA   A O   1 
ATOM   415  C CB  . ALA   A 1 53  ? -19.460 45.011 -15.307 1.00 30.86 ?  70  ALA   A CB  1 
ATOM   416  N N   . GLY   A 1 54  ? -21.670 46.562 -13.113 1.00 29.48 ?  71  GLY   A N   1 
ATOM   417  C CA  . GLY   A 1 54  ? -22.954 46.371 -12.466 1.00 31.75 ?  71  GLY   A CA  1 
ATOM   418  C C   . GLY   A 1 54  ? -23.290 44.927 -12.181 1.00 32.50 ?  71  GLY   A C   1 
ATOM   419  O O   . GLY   A 1 54  ? -24.471 44.567 -12.139 1.00 30.25 ?  71  GLY   A O   1 
ATOM   420  N N   . GLY   A 1 55  ? -22.283 44.085 -11.964 1.00 29.06 ?  72  GLY   A N   1 
ATOM   421  C CA  . GLY   A 1 55  ? -22.494 42.657 -11.863 1.00 28.87 ?  72  GLY   A CA  1 
ATOM   422  C C   . GLY   A 1 55  ? -22.627 42.103 -10.461 1.00 25.99 ?  72  GLY   A C   1 
ATOM   423  O O   . GLY   A 1 55  ? -22.740 40.884 -10.311 1.00 28.90 ?  72  GLY   A O   1 
ATOM   424  N N   . ASP   A 1 56  ? -22.656 42.944 -9.429  1.00 28.50 ?  73  ASP   A N   1 
ATOM   425  C CA  . ASP   A 1 56  ? -22.623 42.380 -8.077  1.00 25.92 ?  73  ASP   A CA  1 
ATOM   426  C C   . ASP   A 1 56  ? -23.888 41.592 -7.741  1.00 26.61 ?  73  ASP   A C   1 
ATOM   427  O O   . ASP   A 1 56  ? -23.815 40.599 -7.004  1.00 26.26 ?  73  ASP   A O   1 
ATOM   428  C CB  . ASP   A 1 56  ? -22.381 43.481 -7.049  1.00 27.88 ?  73  ASP   A CB  1 
ATOM   429  C CG  . ASP   A 1 56  ? -20.953 44.017 -7.094  1.00 28.34 ?  73  ASP   A CG  1 
ATOM   430  O OD1 . ASP   A 1 56  ? -20.618 44.855 -6.250  1.00 34.65 ?  73  ASP   A OD1 1 
ATOM   431  O OD2 . ASP   A 1 56  ? -20.157 43.574 -7.954  1.00 36.67 ?  73  ASP   A OD2 1 
ATOM   432  N N   . ARG   A 1 57  ? -25.054 42.000 -8.246  1.00 27.52 ?  74  ARG   A N   1 
ATOM   433  C CA  . ARG   A 1 57  ? -26.254 41.216 -7.954  1.00 27.61 ?  74  ARG   A CA  1 
ATOM   434  C C   . ARG   A 1 57  ? -26.153 39.837 -8.599  1.00 26.85 ?  74  ARG   A C   1 
ATOM   435  O O   . ARG   A 1 57  ? -26.458 38.827 -7.961  1.00 26.04 ?  74  ARG   A O   1 
ATOM   436  C CB  . ARG   A 1 57  ? -27.501 41.961 -8.436  1.00 28.55 ?  74  ARG   A CB  1 
ATOM   437  C CG  . ARG   A 1 57  ? -28.838 41.237 -8.270  1.00 25.59 ?  74  ARG   A CG  1 
ATOM   438  C CD  . ARG   A 1 57  ? -29.031 40.832 -6.802  1.00 27.10 ?  74  ARG   A CD  1 
ATOM   439  N NE  . ARG   A 1 57  ? -30.367 40.305 -6.538  1.00 30.67 ?  74  ARG   A NE  1 
ATOM   440  C CZ  . ARG   A 1 57  ? -30.836 40.041 -5.326  1.00 34.03 ?  74  ARG   A CZ  1 
ATOM   441  N NH1 . ARG   A 1 57  ? -30.071 40.142 -4.252  1.00 33.25 ?  74  ARG   A NH1 1 
ATOM   442  N NH2 . ARG   A 1 57  ? -32.098 39.636 -5.188  1.00 36.44 ?  74  ARG   A NH2 1 
ATOM   443  N N   . LEU   A 1 58  ? -25.688 39.771 -9.853  1.00 25.17 ?  75  LEU   A N   1 
ATOM   444  C CA  . LEU   A 1 58  ? -25.483 38.468 -10.489 1.00 23.97 ?  75  LEU   A CA  1 
ATOM   445  C C   . LEU   A 1 58  ? -24.437 37.635 -9.739  1.00 25.54 ?  75  LEU   A C   1 
ATOM   446  O O   . LEU   A 1 58  ? -24.622 36.422 -9.547  1.00 24.65 ?  75  LEU   A O   1 
ATOM   447  C CB  . LEU   A 1 58  ? -25.097 38.643 -11.965 1.00 26.32 ?  75  LEU   A CB  1 
ATOM   448  C CG  . LEU   A 1 58  ? -24.810 37.324 -12.689 1.00 25.05 ?  75  LEU   A CG  1 
ATOM   449  C CD1 . LEU   A 1 58  ? -26.054 36.424 -12.775 1.00 27.57 ?  75  LEU   A CD1 1 
ATOM   450  C CD2 . LEU   A 1 58  ? -24.249 37.569 -14.054 1.00 26.03 ?  75  LEU   A CD2 1 
ATOM   451  N N   . ILE   A 1 59  ? -23.337 38.261 -9.295  1.00 23.73 ?  76  ILE   A N   1 
ATOM   452  C CA  . ILE   A 1 59  ? -22.354 37.531 -8.492  1.00 23.69 ?  76  ILE   A CA  1 
ATOM   453  C C   . ILE   A 1 59  ? -23.022 36.916 -7.269  1.00 26.06 ?  76  ILE   A C   1 
ATOM   454  O O   . ILE   A 1 59  ? -22.798 35.744 -6.955  1.00 26.24 ?  76  ILE   A O   1 
ATOM   455  C CB  . ILE   A 1 59  ? -21.176 38.439 -8.095  1.00 24.86 ?  76  ILE   A CB  1 
ATOM   456  C CG1 . ILE   A 1 59  ? -20.385 38.845 -9.344  1.00 25.32 ?  76  ILE   A CG1 1 
ATOM   457  C CG2 . ILE   A 1 59  ? -20.259 37.721 -7.111  1.00 25.62 ?  76  ILE   A CG2 1 
ATOM   458  C CD1 . ILE   A 1 59  ? -19.380 39.970 -9.082  1.00 26.60 ?  76  ILE   A CD1 1 
ATOM   459  N N   . HIS   A 1 60  ? -23.849 37.693 -6.563  1.00 23.47 ?  77  HIS   A N   1 
ATOM   460  C CA  . HIS   A 1 60  ? -24.545 37.157 -5.395  1.00 23.77 ?  77  HIS   A CA  1 
ATOM   461  C C   . HIS   A 1 60  ? -25.486 36.024 -5.782  1.00 24.85 ?  77  HIS   A C   1 
ATOM   462  O O   . HIS   A 1 60  ? -25.456 34.943 -5.184  1.00 24.86 ?  77  HIS   A O   1 
ATOM   463  C CB  . HIS   A 1 60  ? -25.317 38.268 -4.675  1.00 23.32 ?  77  HIS   A CB  1 
ATOM   464  C CG  . HIS   A 1 60  ? -26.093 37.790 -3.486  1.00 25.66 ?  77  HIS   A CG  1 
ATOM   465  N ND1 . HIS   A 1 60  ? -27.385 37.315 -3.576  1.00 26.89 ?  77  HIS   A ND1 1 
ATOM   466  C CD2 . HIS   A 1 60  ? -25.760 37.730 -2.177  1.00 23.68 ?  77  HIS   A CD2 1 
ATOM   467  C CE1 . HIS   A 1 60  ? -27.816 36.991 -2.370  1.00 25.82 ?  77  HIS   A CE1 1 
ATOM   468  N NE2 . HIS   A 1 60  ? -26.848 37.227 -1.501  1.00 26.26 ?  77  HIS   A NE2 1 
ATOM   469  N N   . GLU   A 1 61  ? -26.347 36.249 -6.778  1.00 24.03 ?  78  GLU   A N   1 
ATOM   470  C CA  . GLU   A 1 61  ? -27.340 35.221 -7.086  1.00 27.05 ?  78  GLU   A CA  1 
ATOM   471  C C   . GLU   A 1 61  ? -26.719 33.954 -7.655  1.00 26.82 ?  78  GLU   A C   1 
ATOM   472  O O   . GLU   A 1 61  ? -27.110 32.848 -7.265  1.00 26.34 ?  78  GLU   A O   1 
ATOM   473  C CB  . GLU   A 1 61  ? -28.434 35.753 -8.010  1.00 25.69 ?  78  GLU   A CB  1 
ATOM   474  C CG  . GLU   A 1 61  ? -28.999 37.027 -7.492  1.00 30.20 ?  78  GLU   A CG  1 
ATOM   475  C CD  . GLU   A 1 61  ? -30.003 36.713 -6.405  1.00 34.38 ?  78  GLU   A CD  1 
ATOM   476  O OE1 . GLU   A 1 61  ? -31.127 36.243 -6.686  1.00 35.97 ?  78  GLU   A OE1 1 
ATOM   477  O OE2 . GLU   A 1 61  ? -29.613 36.870 -5.226  1.00 30.92 ?  78  GLU   A OE2 1 
ATOM   478  N N   . GLN   A 1 62  ? -25.779 34.079 -8.588  1.00 24.23 ?  79  GLN   A N   1 
ATOM   479  C CA  . GLN   A 1 62  ? -25.155 32.877 -9.136  1.00 23.79 ?  79  GLN   A CA  1 
ATOM   480  C C   . GLN   A 1 62  ? -24.370 32.128 -8.074  1.00 27.02 ?  79  GLN   A C   1 
ATOM   481  O O   . GLN   A 1 62  ? -24.383 30.894 -8.031  1.00 26.69 ?  79  GLN   A O   1 
ATOM   482  C CB  . GLN   A 1 62  ? -24.227 33.228 -10.293 1.00 25.32 ?  79  GLN   A CB  1 
ATOM   483  C CG  . GLN   A 1 62  ? -23.578 32.003 -10.917 1.00 28.47 ?  79  GLN   A CG  1 
ATOM   484  C CD  . GLN   A 1 62  ? -24.583 31.085 -11.585 1.00 28.44 ?  79  GLN   A CD  1 
ATOM   485  O OE1 . GLN   A 1 62  ? -25.421 31.532 -12.378 1.00 32.85 ?  79  GLN   A OE1 1 
ATOM   486  N NE2 . GLN   A 1 62  ? -24.519 29.803 -11.264 1.00 26.87 ?  79  GLN   A NE2 1 
ATOM   487  N N   . ASP   A 1 63  ? -23.658 32.851 -7.221  1.00 26.20 ?  80  ASP   A N   1 
ATOM   488  C CA  . ASP   A 1 63  ? -22.890 32.145 -6.206  1.00 24.27 ?  80  ASP   A CA  1 
ATOM   489  C C   . ASP   A 1 63  ? -23.810 31.454 -5.204  1.00 27.39 ?  80  ASP   A C   1 
ATOM   490  O O   . ASP   A 1 63  ? -23.459 30.390 -4.669  1.00 25.48 ?  80  ASP   A O   1 
ATOM   491  C CB  . ASP   A 1 63  ? -21.925 33.115 -5.523  1.00 24.18 ?  80  ASP   A CB  1 
ATOM   492  C CG  . ASP   A 1 63  ? -20.658 33.340 -6.360  1.00 28.68 ?  80  ASP   A CG  1 
ATOM   493  O OD1 . ASP   A 1 63  ? -20.612 34.317 -7.141  1.00 31.34 ?  80  ASP   A OD1 1 
ATOM   494  O OD2 . ASP   A 1 63  ? -19.743 32.494 -6.341  1.00 31.01 ?  80  ASP   A OD2 1 
ATOM   495  N N   . LEU   A 1 64  ? -24.995 32.026 -4.950  1.00 25.39 ?  81  LEU   A N   1 
ATOM   496  C CA  . LEU   A 1 64  ? -25.938 31.366 -4.051  1.00 26.58 ?  81  LEU   A CA  1 
ATOM   497  C C   . LEU   A 1 64  ? -26.507 30.087 -4.664  1.00 28.01 ?  81  LEU   A C   1 
ATOM   498  O O   . LEU   A 1 64  ? -26.814 29.142 -3.925  1.00 26.87 ?  81  LEU   A O   1 
ATOM   499  C CB  . LEU   A 1 64  ? -27.074 32.316 -3.659  1.00 29.40 ?  81  LEU   A CB  1 
ATOM   500  C CG  . LEU   A 1 64  ? -27.038 32.941 -2.262  1.00 33.44 ?  81  LEU   A CG  1 
ATOM   501  C CD1 . LEU   A 1 64  ? -27.290 31.898 -1.164  1.00 31.48 ?  81  LEU   A CD1 1 
ATOM   502  C CD2 . LEU   A 1 64  ? -25.741 33.696 -2.012  1.00 32.58 ?  81  LEU   A CD2 1 
ATOM   503  N N   . GLU   A 1 65  ? -26.659 30.036 -5.997  1.00 26.77 ?  82  GLU   A N   1 
ATOM   504  C CA  . GLU   A 1 65  ? -27.021 28.783 -6.667  1.00 26.35 ?  82  GLU   A CA  1 
ATOM   505  C C   . GLU   A 1 65  ? -25.942 27.727 -6.474  1.00 27.06 ?  82  GLU   A C   1 
ATOM   506  O O   . GLU   A 1 65  ? -26.235 26.581 -6.126  1.00 28.86 ?  82  GLU   A O   1 
ATOM   507  C CB  . GLU   A 1 65  ? -27.271 29.007 -8.171  1.00 31.43 ?  82  GLU   A CB  1 
ATOM   508  C CG  . GLU   A 1 65  ? -28.507 29.817 -8.471  1.00 32.88 ?  82  GLU   A CG  1 
ATOM   509  C CD  . GLU   A 1 65  ? -29.767 29.131 -7.995  1.00 40.01 ?  82  GLU   A CD  1 
ATOM   510  O OE1 . GLU   A 1 65  ? -30.659 29.821 -7.439  1.00 41.69 ?  82  GLU   A OE1 1 
ATOM   511  O OE2 . GLU   A 1 65  ? -29.879 27.907 -8.221  1.00 38.31 ?  82  GLU   A OE2 1 
ATOM   512  N N   . TRP   A 1 66  ? -24.680 28.088 -6.709  1.00 27.20 ?  83  TRP   A N   1 
ATOM   513  C CA  . TRP   A 1 66  ? -23.603 27.128 -6.486  1.00 26.02 ?  83  TRP   A CA  1 
ATOM   514  C C   . TRP   A 1 66  ? -23.530 26.696 -5.023  1.00 25.37 ?  83  TRP   A C   1 
ATOM   515  O O   . TRP   A 1 66  ? -23.239 25.532 -4.724  1.00 25.38 ?  83  TRP   A O   1 
ATOM   516  C CB  . TRP   A 1 66  ? -22.270 27.727 -6.895  1.00 26.07 ?  83  TRP   A CB  1 
ATOM   517  C CG  . TRP   A 1 66  ? -22.064 27.879 -8.374  1.00 24.44 ?  83  TRP   A CG  1 
ATOM   518  C CD1 . TRP   A 1 66  ? -22.561 27.097 -9.374  1.00 25.00 ?  83  TRP   A CD1 1 
ATOM   519  C CD2 . TRP   A 1 66  ? -21.277 28.894 -8.998  1.00 26.59 ?  83  TRP   A CD2 1 
ATOM   520  N NE1 . TRP   A 1 66  ? -22.117 27.574 -10.607 1.00 27.33 ?  83  TRP   A NE1 1 
ATOM   521  C CE2 . TRP   A 1 66  ? -21.331 28.676 -10.388 1.00 26.96 ?  83  TRP   A CE2 1 
ATOM   522  C CE3 . TRP   A 1 66  ? -20.524 29.970 -8.507  1.00 27.23 ?  83  TRP   A CE3 1 
ATOM   523  C CZ2 . TRP   A 1 66  ? -20.666 29.500 -11.299 1.00 29.74 ?  83  TRP   A CZ2 1 
ATOM   524  C CZ3 . TRP   A 1 66  ? -19.867 30.783 -9.406  1.00 25.93 ?  83  TRP   A CZ3 1 
ATOM   525  C CH2 . TRP   A 1 66  ? -19.947 30.546 -10.793 1.00 25.75 ?  83  TRP   A CH2 1 
ATOM   526  N N   . LEU   A 1 67  ? -23.734 27.636 -4.095  1.00 25.31 ?  84  LEU   A N   1 
ATOM   527  C CA  . LEU   A 1 67  ? -23.667 27.290 -2.678  1.00 23.82 ?  84  LEU   A CA  1 
ATOM   528  C C   . LEU   A 1 67  ? -24.724 26.255 -2.322  1.00 26.02 ?  84  LEU   A C   1 
ATOM   529  O O   . LEU   A 1 67  ? -24.469 25.339 -1.532  1.00 26.07 ?  84  LEU   A O   1 
ATOM   530  C CB  . LEU   A 1 67  ? -23.849 28.546 -1.830  1.00 24.92 ?  84  LEU   A CB  1 
ATOM   531  C CG  . LEU   A 1 67  ? -23.437 28.422 -0.363  1.00 27.53 ?  84  LEU   A CG  1 
ATOM   532  C CD1 . LEU   A 1 67  ? -21.933 28.144 -0.281  1.00 27.23 ?  84  LEU   A CD1 1 
ATOM   533  C CD2 . LEU   A 1 67  ? -23.811 29.689 0.373   1.00 27.96 ?  84  LEU   A CD2 1 
ATOM   534  N N   . GLN   A 1 68  ? -25.907 26.347 -2.932  1.00 27.43 ?  85  GLN   A N   1 
ATOM   535  C CA  . GLN   A 1 68  ? -26.919 25.359 -2.585  1.00 29.57 ?  85  GLN   A CA  1 
ATOM   536  C C   . GLN   A 1 68  ? -26.642 24.015 -3.243  1.00 27.70 ?  85  GLN   A C   1 
ATOM   537  O O   . GLN   A 1 68  ? -27.047 22.975 -2.710  1.00 31.60 ?  85  GLN   A O   1 
ATOM   538  C CB  . GLN   A 1 68  ? -28.326 25.829 -2.954  1.00 29.88 ?  85  GLN   A CB  1 
ATOM   539  C CG  . GLN   A 1 68  ? -28.788 26.945 -2.039  1.00 35.09 ?  85  GLN   A CG  1 
ATOM   540  C CD  . GLN   A 1 68  ? -29.925 27.776 -2.593  1.00 37.14 ?  85  GLN   A CD  1 
ATOM   541  O OE1 . GLN   A 1 68  ? -31.090 27.413 -2.388  1.00 38.93 ?  85  GLN   A OE1 1 
ATOM   542  N NE2 . GLN   A 1 68  ? -29.611 28.822 -3.373  1.00 33.41 ?  85  GLN   A NE2 1 
ATOM   543  N N   . GLN   A 1 69  ? -25.983 24.017 -4.407  1.00 27.19 ?  86  GLN   A N   1 
ATOM   544  C CA  . GLN   A 1 69  ? -25.592 22.767 -5.051  1.00 27.61 ?  86  GLN   A CA  1 
ATOM   545  C C   . GLN   A 1 69  ? -24.503 22.036 -4.283  1.00 28.68 ?  86  GLN   A C   1 
ATOM   546  O O   . GLN   A 1 69  ? -24.401 20.805 -4.381  1.00 30.51 ?  86  GLN   A O   1 
ATOM   547  C CB  . GLN   A 1 69  ? -25.093 23.061 -6.466  1.00 29.55 ?  86  GLN   A CB  1 
ATOM   548  C CG  . GLN   A 1 69  ? -26.142 23.434 -7.472  1.00 31.24 ?  86  GLN   A CG  1 
ATOM   549  C CD  . GLN   A 1 69  ? -25.489 24.001 -8.717  1.00 35.68 ?  86  GLN   A CD  1 
ATOM   550  O OE1 . GLN   A 1 69  ? -24.480 23.471 -9.189  1.00 34.32 ?  86  GLN   A OE1 1 
ATOM   551  N NE2 . GLN   A 1 69  ? -26.127 25.005 -9.324  1.00 36.87 ?  86  GLN   A NE2 1 
ATOM   552  N N   . ALA   A 1 70  ? -23.695 22.762 -3.513  1.00 28.32 ?  87  ALA   A N   1 
ATOM   553  C CA  . ALA   A 1 70  ? -22.461 22.209 -2.984  1.00 30.22 ?  87  ALA   A CA  1 
ATOM   554  C C   . ALA   A 1 70  ? -22.728 21.048 -2.034  1.00 32.83 ?  87  ALA   A C   1 
ATOM   555  O O   . ALA   A 1 70  ? -23.629 21.104 -1.190  1.00 32.45 ?  87  ALA   A O   1 
ATOM   556  C CB  . ALA   A 1 70  ? -21.665 23.297 -2.261  1.00 27.80 ?  87  ALA   A CB  1 
ATOM   557  N N   . ASP   A 1 71  ? -21.949 19.976 -2.205  1.00 28.77 ?  88  ASP   A N   1 
ATOM   558  C CA  . ASP   A 1 71  ? -21.917 18.907 -1.211  1.00 30.43 ?  88  ASP   A CA  1 
ATOM   559  C C   . ASP   A 1 71  ? -21.036 19.253 -0.025  1.00 30.48 ?  88  ASP   A C   1 
ATOM   560  O O   . ASP   A 1 71  ? -21.313 18.810 1.097   1.00 32.23 ?  88  ASP   A O   1 
ATOM   561  C CB  . ASP   A 1 71  ? -21.427 17.619 -1.856  1.00 34.26 ?  88  ASP   A CB  1 
ATOM   562  C CG  . ASP   A 1 71  ? -22.385 17.100 -2.890  1.00 36.00 ?  88  ASP   A CG  1 
ATOM   563  O OD1 . ASP   A 1 71  ? -23.519 16.725 -2.515  1.00 37.22 ?  88  ASP   A OD1 1 
ATOM   564  O OD2 . ASP   A 1 71  ? -22.026 17.117 -4.082  1.00 35.17 ?  88  ASP   A OD2 1 
ATOM   565  N N   . VAL   A 1 72  ? -19.963 20.005 -0.252  1.00 28.12 ?  89  VAL   A N   1 
ATOM   566  C CA  . VAL   A 1 72  ? -19.080 20.458 0.820   1.00 27.18 ?  89  VAL   A CA  1 
ATOM   567  C C   . VAL   A 1 72  ? -18.710 21.897 0.513   1.00 28.59 ?  89  VAL   A C   1 
ATOM   568  O O   . VAL   A 1 72  ? -18.478 22.259 -0.652  1.00 28.05 ?  89  VAL   A O   1 
ATOM   569  C CB  . VAL   A 1 72  ? -17.811 19.588 0.947   1.00 28.76 ?  89  VAL   A CB  1 
ATOM   570  C CG1 . VAL   A 1 72  ? -16.860 20.139 2.045   1.00 29.06 ?  89  VAL   A CG1 1 
ATOM   571  C CG2 . VAL   A 1 72  ? -18.173 18.123 1.187   1.00 32.69 ?  89  VAL   A CG2 1 
ATOM   572  N N   . VAL   A 1 73  ? -18.689 22.722 1.552   1.00 24.93 ?  90  VAL   A N   1 
ATOM   573  C CA  . VAL   A 1 73  ? -18.197 24.092 1.483   1.00 25.49 ?  90  VAL   A CA  1 
ATOM   574  C C   . VAL   A 1 73  ? -16.855 24.117 2.196   1.00 28.45 ?  90  VAL   A C   1 
ATOM   575  O O   . VAL   A 1 73  ? -16.768 23.734 3.373   1.00 28.21 ?  90  VAL   A O   1 
ATOM   576  C CB  . VAL   A 1 73  ? -19.191 25.070 2.129   1.00 23.46 ?  90  VAL   A CB  1 
ATOM   577  C CG1 . VAL   A 1 73  ? -18.631 26.496 2.090   1.00 24.87 ?  90  VAL   A CG1 1 
ATOM   578  C CG2 . VAL   A 1 73  ? -20.553 24.968 1.428   1.00 24.94 ?  90  VAL   A CG2 1 
ATOM   579  N N   . VAL   A 1 74  ? -15.807 24.549 1.493   1.00 25.56 ?  91  VAL   A N   1 
ATOM   580  C CA  . VAL   A 1 74  ? -14.462 24.640 2.066   1.00 26.26 ?  91  VAL   A CA  1 
ATOM   581  C C   . VAL   A 1 74  ? -14.054 26.108 2.073   1.00 25.62 ?  91  VAL   A C   1 
ATOM   582  O O   . VAL   A 1 74  ? -14.059 26.760 1.023   1.00 25.02 ?  91  VAL   A O   1 
ATOM   583  C CB  . VAL   A 1 74  ? -13.443 23.802 1.276   1.00 26.31 ?  91  VAL   A CB  1 
ATOM   584  C CG1 . VAL   A 1 74  ? -12.038 23.950 1.867   1.00 28.53 ?  91  VAL   A CG1 1 
ATOM   585  C CG2 . VAL   A 1 74  ? -13.879 22.333 1.212   1.00 29.25 ?  91  VAL   A CG2 1 
ATOM   586  N N   . ALA   A 1 75  ? -13.682 26.628 3.243   1.00 24.22 ?  92  ALA   A N   1 
ATOM   587  C CA  . ALA   A 1 75  ? -13.332 28.037 3.361   1.00 26.03 ?  92  ALA   A CA  1 
ATOM   588  C C   . ALA   A 1 75  ? -11.960 28.176 4.001   1.00 28.16 ?  92  ALA   A C   1 
ATOM   589  O O   . ALA   A 1 75  ? -11.675 27.533 5.014   1.00 29.33 ?  92  ALA   A O   1 
ATOM   590  C CB  . ALA   A 1 75  ? -14.387 28.807 4.183   1.00 24.37 ?  92  ALA   A CB  1 
ATOM   591  N N   . GLU   A 1 76  ? -11.109 29.003 3.408   1.00 25.54 ?  93  GLU   A N   1 
ATOM   592  C CA  . GLU   A 1 76  ? -9.848  29.390 4.029   1.00 24.82 ?  93  GLU   A CA  1 
ATOM   593  C C   . GLU   A 1 76  ? -10.151 30.724 4.704   1.00 26.90 ?  93  GLU   A C   1 
ATOM   594  O O   . GLU   A 1 76  ? -10.421 31.718 4.024   1.00 26.81 ?  93  GLU   A O   1 
ATOM   595  C CB  . GLU   A 1 76  ? -8.739  29.494 2.986   1.00 27.29 ?  93  GLU   A CB  1 
ATOM   596  C CG  . GLU   A 1 76  ? -7.287  29.220 3.429   1.00 27.17 ?  93  GLU   A CG  1 
ATOM   597  C CD  . GLU   A 1 76  ? -6.783  30.111 4.548   1.00 31.80 ?  93  GLU   A CD  1 
ATOM   598  O OE1 . GLU   A 1 76  ? -5.924  29.643 5.334   1.00 31.88 ?  93  GLU   A OE1 1 
ATOM   599  O OE2 . GLU   A 1 76  ? -7.297  31.244 4.688   1.00 28.74 ?  93  GLU   A OE2 1 
ATOM   600  N N   . VAL   A 1 77  ? -10.147 30.739 6.037   1.00 26.34 ?  94  VAL   A N   1 
ATOM   601  C CA  . VAL   A 1 77  ? -10.706 31.848 6.807   1.00 24.97 ?  94  VAL   A CA  1 
ATOM   602  C C   . VAL   A 1 77  ? -9.615  32.657 7.512   1.00 26.77 ?  94  VAL   A C   1 
ATOM   603  O O   . VAL   A 1 77  ? -9.885  33.346 8.499   1.00 26.89 ?  94  VAL   A O   1 
ATOM   604  C CB  . VAL   A 1 77  ? -11.759 31.354 7.816   1.00 22.33 ?  94  VAL   A CB  1 
ATOM   605  C CG1 . VAL   A 1 77  ? -12.948 30.732 7.088   1.00 23.78 ?  94  VAL   A CG1 1 
ATOM   606  C CG2 . VAL   A 1 77  ? -11.134 30.364 8.785   1.00 26.79 ?  94  VAL   A CG2 1 
ATOM   607  N N   . THR   A 1 78  ? -8.379  32.602 7.023   1.00 25.95 ?  95  THR   A N   1 
ATOM   608  C CA  . THR   A 1 78  ? -7.312  33.356 7.671   1.00 27.13 ?  95  THR   A CA  1 
ATOM   609  C C   . THR   A 1 78  ? -7.446  34.858 7.410   1.00 30.60 ?  95  THR   A C   1 
ATOM   610  O O   . THR   A 1 78  ? -7.310  35.677 8.331   1.00 29.38 ?  95  THR   A O   1 
ATOM   611  C CB  . THR   A 1 78  ? -5.958  32.835 7.204   1.00 29.91 ?  95  THR   A CB  1 
ATOM   612  O OG1 . THR   A 1 78  ? -5.868  31.430 7.487   1.00 31.37 ?  95  THR   A OG1 1 
ATOM   613  C CG2 . THR   A 1 78  ? -4.836  33.553 7.913   1.00 32.05 ?  95  THR   A CG2 1 
ATOM   614  N N   . GLN   A 1 79  ? -7.719  35.239 6.168   1.00 26.93 ?  96  GLN   A N   1 
ATOM   615  C CA  . GLN   A 1 79  ? -7.867  36.647 5.813   1.00 24.43 ?  96  GLN   A CA  1 
ATOM   616  C C   . GLN   A 1 79  ? -9.304  37.084 6.070   1.00 27.28 ?  96  GLN   A C   1 
ATOM   617  O O   . GLN   A 1 79  ? -10.230 36.479 5.507   1.00 24.78 ?  96  GLN   A O   1 
ATOM   618  C CB  . GLN   A 1 79  ? -7.495  36.870 4.345   1.00 28.25 ?  96  GLN   A CB  1 
ATOM   619  C CG  . GLN   A 1 79  ? -7.457  38.339 3.986   1.00 27.99 ?  96  GLN   A CG  1 
ATOM   620  C CD  . GLN   A 1 79  ? -6.241  39.054 4.545   1.00 31.97 ?  96  GLN   A CD  1 
ATOM   621  O OE1 . GLN   A 1 79  ? -5.143  38.476 4.695   1.00 34.03 ?  96  GLN   A OE1 1 
ATOM   622  N NE2 . GLN   A 1 79  ? -6.447  40.305 4.943   1.00 33.83 ?  96  GLN   A NE2 1 
ATOM   623  N N   . PRO   A 1 80  ? -9.552  38.091 6.916   1.00 23.38 ?  97  PRO   A N   1 
ATOM   624  C CA  . PRO   A 1 80  ? -10.948 38.476 7.173   1.00 22.25 ?  97  PRO   A CA  1 
ATOM   625  C C   . PRO   A 1 80  ? -11.638 38.965 5.902   1.00 24.59 ?  97  PRO   A C   1 
ATOM   626  O O   . PRO   A 1 80  ? -11.056 39.699 5.093   1.00 25.33 ?  97  PRO   A O   1 
ATOM   627  C CB  . PRO   A 1 80  ? -10.841 39.583 8.229   1.00 25.72 ?  97  PRO   A CB  1 
ATOM   628  C CG  . PRO   A 1 80  ? -9.488  39.446 8.823   1.00 26.67 ?  97  PRO   A CG  1 
ATOM   629  C CD  . PRO   A 1 80  ? -8.597  38.827 7.759   1.00 25.96 ?  97  PRO   A CD  1 
ATOM   630  N N   . SER   A 1 81  ? -12.903 38.573 5.757   1.00 23.54 ?  98  SER   A N   1 
ATOM   631  C CA  . SER   A 1 81  ? -13.650 38.823 4.523   1.00 22.91 ?  98  SER   A CA  1 
ATOM   632  C C   . SER   A 1 81  ? -15.139 38.784 4.814   1.00 21.39 ?  98  SER   A C   1 
ATOM   633  O O   . SER   A 1 81  ? -15.628 37.795 5.358   1.00 20.27 ?  98  SER   A O   1 
ATOM   634  C CB  . SER   A 1 81  ? -13.312 37.782 3.458   1.00 23.93 ?  98  SER   A CB  1 
ATOM   635  O OG  . SER   A 1 81  ? -14.251 37.819 2.383   1.00 23.41 ?  98  SER   A OG  1 
ATOM   636  N N   . LEU   A 1 82  ? -15.857 39.837 4.404   1.00 20.09 ?  99  LEU   A N   1 
ATOM   637  C CA  . LEU   A 1 82  ? -17.313 39.844 4.538   1.00 19.31 ?  99  LEU   A CA  1 
ATOM   638  C C   . LEU   A 1 82  ? -17.947 38.746 3.700   1.00 22.00 ?  99  LEU   A C   1 
ATOM   639  O O   . LEU   A 1 82  ? -18.870 38.052 4.154   1.00 21.14 ?  99  LEU   A O   1 
ATOM   640  C CB  . LEU   A 1 82  ? -17.854 41.205 4.099   1.00 20.49 ?  99  LEU   A CB  1 
ATOM   641  C CG  . LEU   A 1 82  ? -17.476 42.417 4.958   1.00 20.99 ?  99  LEU   A CG  1 
ATOM   642  C CD1 . LEU   A 1 82  ? -17.964 43.655 4.210   1.00 21.95 ?  99  LEU   A CD1 1 
ATOM   643  C CD2 . LEU   A 1 82  ? -18.121 42.327 6.336   1.00 23.28 ?  99  LEU   A CD2 1 
ATOM   644  N N   . GLY   A 1 83  ? -17.485 38.592 2.453   1.00 19.21 ?  100 GLY   A N   1 
ATOM   645  C CA  . GLY   A 1 83  ? -18.100 37.609 1.580   1.00 21.88 ?  100 GLY   A CA  1 
ATOM   646  C C   . GLY   A 1 83  ? -17.916 36.189 2.076   1.00 20.77 ?  100 GLY   A C   1 
ATOM   647  O O   . GLY   A 1 83  ? -18.833 35.372 1.985   1.00 21.26 ?  100 GLY   A O   1 
ATOM   648  N N   . VAL   A 1 84  ? -16.712 35.858 2.536   1.00 20.02 ?  101 VAL   A N   1 
ATOM   649  C CA  . VAL   A 1 84  ? -16.471 34.523 3.090   1.00 22.68 ?  101 VAL   A CA  1 
ATOM   650  C C   . VAL   A 1 84  ? -17.389 34.275 4.285   1.00 21.71 ?  101 VAL   A C   1 
ATOM   651  O O   . VAL   A 1 84  ? -18.022 33.216 4.395   1.00 20.63 ?  101 VAL   A O   1 
ATOM   652  C CB  . VAL   A 1 84  ? -14.988 34.361 3.479   1.00 21.71 ?  101 VAL   A CB  1 
ATOM   653  C CG1 . VAL   A 1 84  ? -14.778 33.047 4.241   1.00 23.60 ?  101 VAL   A CG1 1 
ATOM   654  C CG2 . VAL   A 1 84  ? -14.121 34.412 2.231   1.00 22.66 ?  101 VAL   A CG2 1 
ATOM   655  N N   . GLY   A 1 85  ? -17.465 35.239 5.212   1.00 20.78 ?  102 GLY   A N   1 
ATOM   656  C CA  . GLY   A 1 85  ? -18.359 35.068 6.351   1.00 19.19 ?  102 GLY   A CA  1 
ATOM   657  C C   . GLY   A 1 85  ? -19.807 34.915 5.920   1.00 20.82 ?  102 GLY   A C   1 
ATOM   658  O O   . GLY   A 1 85  ? -20.543 34.076 6.449   1.00 20.89 ?  102 GLY   A O   1 
ATOM   659  N N   . TYR   A 1 86  ? -20.234 35.724 4.950   1.00 21.27 ?  103 TYR   A N   1 
ATOM   660  C CA  . TYR   A 1 86  ? -21.604 35.651 4.464   1.00 20.49 ?  103 TYR   A CA  1 
ATOM   661  C C   . TYR   A 1 86  ? -21.889 34.293 3.834   1.00 20.88 ?  103 TYR   A C   1 
ATOM   662  O O   . TYR   A 1 86  ? -22.958 33.704 4.057   1.00 21.53 ?  103 TYR   A O   1 
ATOM   663  C CB  . TYR   A 1 86  ? -21.846 36.791 3.461   1.00 19.81 ?  103 TYR   A CB  1 
ATOM   664  C CG  . TYR   A 1 86  ? -23.213 36.783 2.834   1.00 21.10 ?  103 TYR   A CG  1 
ATOM   665  C CD1 . TYR   A 1 86  ? -24.283 37.405 3.464   1.00 20.70 ?  103 TYR   A CD1 1 
ATOM   666  C CD2 . TYR   A 1 86  ? -23.447 36.176 1.590   1.00 21.61 ?  103 TYR   A CD2 1 
ATOM   667  C CE1 . TYR   A 1 86  ? -25.547 37.410 2.898   1.00 21.12 ?  103 TYR   A CE1 1 
ATOM   668  C CE2 . TYR   A 1 86  ? -24.716 36.187 1.016   1.00 22.74 ?  103 TYR   A CE2 1 
ATOM   669  C CZ  . TYR   A 1 86  ? -25.758 36.809 1.672   1.00 21.95 ?  103 TYR   A CZ  1 
ATOM   670  O OH  . TYR   A 1 86  ? -27.015 36.813 1.123   1.00 22.19 ?  103 TYR   A OH  1 
ATOM   671  N N   . GLU   A 1 87  ? -20.951 33.789 3.024   1.00 20.06 ?  104 GLU   A N   1 
ATOM   672  C CA  . GLU   A 1 87  ? -21.121 32.458 2.441   1.00 19.26 ?  104 GLU   A CA  1 
ATOM   673  C C   . GLU   A 1 87  ? -21.248 31.400 3.533   1.00 21.06 ?  104 GLU   A C   1 
ATOM   674  O O   . GLU   A 1 87  ? -22.087 30.497 3.444   1.00 22.12 ?  104 GLU   A O   1 
ATOM   675  C CB  . GLU   A 1 87  ? -19.950 32.168 1.509   1.00 21.92 ?  104 GLU   A CB  1 
ATOM   676  C CG  . GLU   A 1 87  ? -20.072 32.995 0.245   1.00 21.48 ?  104 GLU   A CG  1 
ATOM   677  C CD  . GLU   A 1 87  ? -18.795 33.106 -0.569  1.00 23.58 ?  104 GLU   A CD  1 
ATOM   678  O OE1 . GLU   A 1 87  ? -17.697 32.836 -0.045  1.00 24.67 ?  104 GLU   A OE1 1 
ATOM   679  O OE2 . GLU   A 1 87  ? -18.904 33.487 -1.746  1.00 26.42 ?  104 GLU   A OE2 1 
ATOM   680  N N   . LEU   A 1 88  ? -20.443 31.514 4.584   1.00 21.08 ?  105 LEU   A N   1 
ATOM   681  C CA  . LEU   A 1 88  ? -20.538 30.555 5.676   1.00 19.96 ?  105 LEU   A CA  1 
ATOM   682  C C   . LEU   A 1 88  ? -21.866 30.680 6.407   1.00 23.02 ?  105 LEU   A C   1 
ATOM   683  O O   . LEU   A 1 88  ? -22.450 29.667 6.808   1.00 22.44 ?  105 LEU   A O   1 
ATOM   684  C CB  . LEU   A 1 88  ? -19.349 30.733 6.640   1.00 21.57 ?  105 LEU   A CB  1 
ATOM   685  C CG  . LEU   A 1 88  ? -17.998 30.288 6.058   1.00 21.80 ?  105 LEU   A CG  1 
ATOM   686  C CD1 . LEU   A 1 88  ? -16.823 30.770 6.901   1.00 20.93 ?  105 LEU   A CD1 1 
ATOM   687  C CD2 . LEU   A 1 88  ? -17.962 28.770 5.914   1.00 24.02 ?  105 LEU   A CD2 1 
ATOM   688  N N   . GLY   A 1 89  ? -22.360 31.906 6.605   1.00 20.95 ?  106 GLY   A N   1 
ATOM   689  C CA  . GLY   A 1 89  ? -23.648 32.067 7.275   1.00 20.27 ?  106 GLY   A CA  1 
ATOM   690  C C   . GLY   A 1 89  ? -24.789 31.463 6.475   1.00 20.49 ?  106 GLY   A C   1 
ATOM   691  O O   . GLY   A 1 89  ? -25.676 30.796 7.017   1.00 22.11 ?  106 GLY   A O   1 
ATOM   692  N N   . ARG   A 1 90  ? -24.804 31.720 5.171   1.00 21.54 ?  107 ARG   A N   1 
ATOM   693  C CA  . ARG   A 1 90  ? -25.826 31.118 4.329   1.00 21.87 ?  107 ARG   A CA  1 
ATOM   694  C C   . ARG   A 1 90  ? -25.666 29.605 4.313   1.00 21.83 ?  107 ARG   A C   1 
ATOM   695  O O   . ARG   A 1 90  ? -26.657 28.868 4.285   1.00 25.01 ?  107 ARG   A O   1 
ATOM   696  C CB  . ARG   A 1 90  ? -25.700 31.678 2.903   1.00 20.29 ?  107 ARG   A CB  1 
ATOM   697  C CG  . ARG   A 1 90  ? -26.023 33.187 2.768   1.00 22.42 ?  107 ARG   A CG  1 
ATOM   698  C CD  . ARG   A 1 90  ? -27.400 33.600 3.281   1.00 22.55 ?  107 ARG   A CD  1 
ATOM   699  N NE  . ARG   A 1 90  ? -28.474 32.903 2.587   1.00 24.28 ?  107 ARG   A NE  1 
ATOM   700  C CZ  . ARG   A 1 90  ? -29.086 33.383 1.514   1.00 24.12 ?  107 ARG   A CZ  1 
ATOM   701  N NH1 . ARG   A 1 90  ? -28.685 34.509 0.940   1.00 26.05 ?  107 ARG   A NH1 1 
ATOM   702  N NH2 . ARG   A 1 90  ? -30.123 32.722 0.997   1.00 29.78 ?  107 ARG   A NH2 1 
ATOM   703  N N   . ALA   A 1 91  ? -24.424 29.123 4.285   1.00 21.00 ?  108 ALA   A N   1 
ATOM   704  C CA  . ALA   A 1 91  ? -24.226 27.679 4.206   1.00 22.23 ?  108 ALA   A CA  1 
ATOM   705  C C   . ALA   A 1 91  ? -24.703 26.985 5.476   1.00 23.86 ?  108 ALA   A C   1 
ATOM   706  O O   . ALA   A 1 91  ? -25.256 25.886 5.409   1.00 23.71 ?  108 ALA   A O   1 
ATOM   707  C CB  . ALA   A 1 91  ? -22.760 27.353 3.944   1.00 23.58 ?  108 ALA   A CB  1 
ATOM   708  N N   . VAL   A 1 92  ? -24.483 27.596 6.643   1.00 23.37 ?  109 VAL   A N   1 
ATOM   709  C CA  . VAL   A 1 92  ? -25.000 26.996 7.876   1.00 22.95 ?  109 VAL   A CA  1 
ATOM   710  C C   . VAL   A 1 92  ? -26.517 26.898 7.824   1.00 25.88 ?  109 VAL   A C   1 
ATOM   711  O O   . VAL   A 1 92  ? -27.116 25.887 8.225   1.00 25.91 ?  109 VAL   A O   1 
ATOM   712  C CB  . VAL   A 1 92  ? -24.535 27.816 9.098   1.00 22.05 ?  109 VAL   A CB  1 
ATOM   713  C CG1 . VAL   A 1 92  ? -25.384 27.481 10.333  1.00 28.24 ?  109 VAL   A CG1 1 
ATOM   714  C CG2 . VAL   A 1 92  ? -23.066 27.586 9.348   1.00 26.49 ?  109 VAL   A CG2 1 
ATOM   715  N N   . ALA   A 1 93  ? -27.172 27.953 7.349   1.00 24.13 ?  110 ALA   A N   1 
ATOM   716  C CA  . ALA   A 1 93  ? -28.624 27.929 7.302   1.00 27.70 ?  110 ALA   A CA  1 
ATOM   717  C C   . ALA   A 1 93  ? -29.144 26.922 6.272   1.00 27.73 ?  110 ALA   A C   1 
ATOM   718  O O   . ALA   A 1 93  ? -30.262 26.405 6.421   1.00 30.14 ?  110 ALA   A O   1 
ATOM   719  C CB  . ALA   A 1 93  ? -29.141 29.336 7.017   1.00 28.98 ?  110 ALA   A CB  1 
ATOM   720  N N   . PHE   A 1 94  ? -28.346 26.622 5.236   1.00 26.31 ?  111 PHE   A N   1 
ATOM   721  C CA  . PHE   A 1 94  ? -28.634 25.556 4.277   1.00 28.98 ?  111 PHE   A CA  1 
ATOM   722  C C   . PHE   A 1 94  ? -28.250 24.169 4.793   1.00 30.70 ?  111 PHE   A C   1 
ATOM   723  O O   . PHE   A 1 94  ? -28.419 23.185 4.059   1.00 31.36 ?  111 PHE   A O   1 
ATOM   724  C CB  . PHE   A 1 94  ? -27.906 25.807 2.944   1.00 27.81 ?  111 PHE   A CB  1 
ATOM   725  C CG  . PHE   A 1 94  ? -28.471 26.951 2.111   1.00 28.16 ?  111 PHE   A CG  1 
ATOM   726  C CD1 . PHE   A 1 94  ? -29.837 27.118 1.946   1.00 33.85 ?  111 PHE   A CD1 1 
ATOM   727  C CD2 . PHE   A 1 94  ? -27.611 27.843 1.482   1.00 29.41 ?  111 PHE   A CD2 1 
ATOM   728  C CE1 . PHE   A 1 94  ? -30.338 28.164 1.171   1.00 32.45 ?  111 PHE   A CE1 1 
ATOM   729  C CE2 . PHE   A 1 94  ? -28.106 28.885 0.696   1.00 30.80 ?  111 PHE   A CE2 1 
ATOM   730  C CZ  . PHE   A 1 94  ? -29.461 29.049 0.557   1.00 30.00 ?  111 PHE   A CZ  1 
ATOM   731  N N   . ASN   A 1 95  ? -27.725 24.086 6.014   1.00 29.82 ?  112 ASN   A N   1 
ATOM   732  C CA  . ASN   A 1 95  ? -27.293 22.847 6.683   1.00 33.50 ?  112 ASN   A CA  1 
ATOM   733  C C   . ASN   A 1 95  ? -26.211 22.129 5.863   1.00 33.91 ?  112 ASN   A C   1 
ATOM   734  O O   . ASN   A 1 95  ? -26.249 20.916 5.651   1.00 35.70 ?  112 ASN   A O   1 
ATOM   735  C CB  . ASN   A 1 95  ? -28.483 21.925 6.982   1.00 35.12 ?  112 ASN   A CB  1 
ATOM   736  C CG  . ASN   A 1 95  ? -28.076 20.650 7.733   1.00 43.27 ?  112 ASN   A CG  1 
ATOM   737  O OD1 . ASN   A 1 95  ? -27.056 20.638 8.440   1.00 44.25 ?  112 ASN   A OD1 1 
ATOM   738  N ND2 . ASN   A 1 95  ? -28.885 19.590 7.613   1.00 47.70 ?  112 ASN   A ND2 1 
ATOM   739  N N   . LYS   A 1 96  ? -25.222 22.895 5.412   1.00 29.59 ?  113 LYS   A N   1 
ATOM   740  C CA  . LYS   A 1 96  ? -24.146 22.342 4.599   1.00 30.81 ?  113 LYS   A CA  1 
ATOM   741  C C   . LYS   A 1 96  ? -23.025 21.753 5.452   1.00 33.71 ?  113 LYS   A C   1 
ATOM   742  O O   . LYS   A 1 96  ? -22.728 22.229 6.555   1.00 32.33 ?  113 LYS   A O   1 
ATOM   743  C CB  . LYS   A 1 96  ? -23.551 23.421 3.693   1.00 28.21 ?  113 LYS   A CB  1 
ATOM   744  C CG  . LYS   A 1 96  ? -24.508 23.909 2.637   1.00 26.01 ?  113 LYS   A CG  1 
ATOM   745  C CD  . LYS   A 1 96  ? -24.872 22.773 1.688   1.00 30.65 ?  113 LYS   A CD  1 
ATOM   746  C CE  . LYS   A 1 96  ? -25.841 23.236 0.633   1.00 28.38 ?  113 LYS   A CE  1 
ATOM   747  N NZ  . LYS   A 1 96  ? -26.175 22.126 -0.290  1.00 29.07 ?  113 LYS   A NZ  1 
ATOM   748  N N   . ARG   A 1 97  ? -22.419 20.688 4.924   1.00 29.33 ?  114 ARG   A N   1 
ATOM   749  C CA  . ARG   A 1 97  ? -21.105 20.238 5.363   1.00 29.59 ?  114 ARG   A CA  1 
ATOM   750  C C   . ARG   A 1 97  ? -20.072 21.327 5.093   1.00 30.84 ?  114 ARG   A C   1 
ATOM   751  O O   . ARG   A 1 97  ? -19.911 21.760 3.947   1.00 29.34 ?  114 ARG   A O   1 
ATOM   752  C CB  . ARG   A 1 97  ? -20.742 18.963 4.601   1.00 34.71 ?  114 ARG   A CB  1 
ATOM   753  C CG  . ARG   A 1 97  ? -19.567 18.194 5.130   1.00 38.99 ?  114 ARG   A CG  1 
ATOM   754  C CD  . ARG   A 1 97  ? -19.486 16.835 4.453   1.00 39.30 ?  114 ARG   A CD  1 
ATOM   755  N NE  . ARG   A 1 97  ? -18.113 16.347 4.471   1.00 44.81 ?  114 ARG   A NE  1 
ATOM   756  C CZ  . ARG   A 1 97  ? -17.717 15.196 3.946   1.00 49.43 ?  114 ARG   A CZ  1 
ATOM   757  N NH1 . ARG   A 1 97  ? -18.567 14.384 3.338   1.00 45.54 ?  114 ARG   A NH1 1 
ATOM   758  N NH2 . ARG   A 1 97  ? -16.431 14.861 4.016   1.00 48.80 ?  114 ARG   A NH2 1 
ATOM   759  N N   . ILE   A 1 98  ? -19.363 21.764 6.142   1.00 28.47 ?  115 ILE   A N   1 
ATOM   760  C CA  . ILE   A 1 98  ? -18.484 22.931 6.069   1.00 25.11 ?  115 ILE   A CA  1 
ATOM   761  C C   . ILE   A 1 98  ? -17.141 22.604 6.703   1.00 29.60 ?  115 ILE   A C   1 
ATOM   762  O O   . ILE   A 1 98  ? -17.086 22.106 7.835   1.00 27.04 ?  115 ILE   A O   1 
ATOM   763  C CB  . ILE   A 1 98  ? -19.111 24.153 6.773   1.00 26.27 ?  115 ILE   A CB  1 
ATOM   764  C CG1 . ILE   A 1 98  ? -20.368 24.615 6.030   1.00 25.80 ?  115 ILE   A CG1 1 
ATOM   765  C CG2 . ILE   A 1 98  ? -18.065 25.275 6.989   1.00 24.03 ?  115 ILE   A CG2 1 
ATOM   766  C CD1 . ILE   A 1 98  ? -21.238 25.540 6.872   1.00 27.99 ?  115 ILE   A CD1 1 
ATOM   767  N N   . LEU   A 1 99  ? -16.062 22.917 5.990   1.00 26.25 ?  116 LEU   A N   1 
ATOM   768  C CA  . LEU   A 1 99  ? -14.703 22.848 6.522   1.00 30.17 ?  116 LEU   A CA  1 
ATOM   769  C C   . LEU   A 1 99  ? -14.040 24.210 6.381   1.00 28.72 ?  116 LEU   A C   1 
ATOM   770  O O   . LEU   A 1 99  ? -13.890 24.712 5.261   1.00 27.58 ?  116 LEU   A O   1 
ATOM   771  C CB  . LEU   A 1 99  ? -13.873 21.795 5.793   1.00 31.54 ?  116 LEU   A CB  1 
ATOM   772  C CG  . LEU   A 1 99  ? -12.402 21.758 6.220   1.00 31.37 ?  116 LEU   A CG  1 
ATOM   773  C CD1 . LEU   A 1 99  ? -12.228 21.309 7.671   1.00 33.74 ?  116 LEU   A CD1 1 
ATOM   774  C CD2 . LEU   A 1 99  ? -11.600 20.868 5.265   1.00 33.78 ?  116 LEU   A CD2 1 
ATOM   775  N N   . CYS   A 1 100 ? -13.629 24.798 7.512   1.00 27.27 ?  117 CYS   A N   1 
ATOM   776  C CA  . CYS   A 1 100 ? -12.845 26.025 7.524   1.00 28.76 ?  117 CYS   A CA  1 
ATOM   777  C C   . CYS   A 1 100 ? -11.403 25.716 7.889   1.00 32.66 ?  117 CYS   A C   1 
ATOM   778  O O   . CYS   A 1 100 ? -11.133 24.860 8.738   1.00 30.70 ?  117 CYS   A O   1 
ATOM   779  C CB  . CYS   A 1 100 ? -13.413 27.052 8.510   1.00 27.55 ?  117 CYS   A CB  1 
ATOM   780  S SG  . CYS   A 1 100 ? -15.107 27.554 8.157   1.00 26.03 ?  117 CYS   A SG  1 
ATOM   781  N N   . LEU   A 1 101 ? -10.480 26.425 7.249   1.00 29.20 ?  118 LEU   A N   1 
ATOM   782  C CA  . LEU   A 1 101 ? -9.056  26.229 7.452   1.00 29.67 ?  118 LEU   A CA  1 
ATOM   783  C C   . LEU   A 1 101 ? -8.450  27.562 7.861   1.00 30.37 ?  118 LEU   A C   1 
ATOM   784  O O   . LEU   A 1 101 ? -8.639  28.569 7.176   1.00 29.51 ?  118 LEU   A O   1 
ATOM   785  C CB  . LEU   A 1 101 ? -8.394  25.698 6.181   1.00 31.62 ?  118 LEU   A CB  1 
ATOM   786  C CG  . LEU   A 1 101 ? -9.005  24.401 5.631   1.00 30.37 ?  118 LEU   A CG  1 
ATOM   787  C CD1 . LEU   A 1 101 ? -8.622  24.215 4.163   1.00 35.70 ?  118 LEU   A CD1 1 
ATOM   788  C CD2 . LEU   A 1 101 ? -8.575  23.216 6.467   1.00 35.26 ?  118 LEU   A CD2 1 
ATOM   789  N N   . PHE   A 1 102 ? -7.748  27.576 8.992   1.00 30.70 ?  119 PHE   A N   1 
ATOM   790  C CA  . PHE   A 1 102 ? -7.214  28.801 9.568   1.00 30.31 ?  119 PHE   A CA  1 
ATOM   791  C C   . PHE   A 1 102 ? -5.741  28.621 9.895   1.00 33.86 ?  119 PHE   A C   1 
ATOM   792  O O   . PHE   A 1 102 ? -5.346  27.590 10.449  1.00 34.64 ?  119 PHE   A O   1 
ATOM   793  C CB  . PHE   A 1 102 ? -7.990  29.189 10.837  1.00 30.23 ?  119 PHE   A CB  1 
ATOM   794  C CG  . PHE   A 1 102 ? -7.465  30.421 11.508  1.00 31.91 ?  119 PHE   A CG  1 
ATOM   795  C CD1 . PHE   A 1 102 ? -7.725  31.673 10.980  1.00 30.40 ?  119 PHE   A CD1 1 
ATOM   796  C CD2 . PHE   A 1 102 ? -6.713  30.327 12.668  1.00 32.83 ?  119 PHE   A CD2 1 
ATOM   797  C CE1 . PHE   A 1 102 ? -7.237  32.806 11.593  1.00 30.23 ?  119 PHE   A CE1 1 
ATOM   798  C CE2 . PHE   A 1 102 ? -6.224  31.452 13.286  1.00 31.98 ?  119 PHE   A CE2 1 
ATOM   799  C CZ  . PHE   A 1 102 ? -6.481  32.693 12.760  1.00 31.86 ?  119 PHE   A CZ  1 
ATOM   800  N N   . ARG   A 1 103 ? -4.932  29.645 9.594   1.00 33.86 ?  120 ARG   A N   1 
ATOM   801  C CA  . ARG   A 1 103 ? -3.503  29.561 9.858   1.00 37.86 ?  120 ARG   A CA  1 
ATOM   802  C C   . ARG   A 1 103 ? -3.149  30.383 11.091  1.00 39.99 ?  120 ARG   A C   1 
ATOM   803  O O   . ARG   A 1 103 ? -3.128  31.622 11.011  1.00 35.64 ?  120 ARG   A O   1 
ATOM   804  C CB  . ARG   A 1 103 ? -2.708  30.058 8.654   1.00 37.03 ?  120 ARG   A CB  1 
ATOM   805  C CG  . ARG   A 1 103 ? -2.951  29.252 7.397   1.00 38.10 ?  120 ARG   A CG  1 
ATOM   806  C CD  . ARG   A 1 103 ? -1.918  29.538 6.318   1.00 41.19 ?  120 ARG   A CD  1 
ATOM   807  N NE  . ARG   A 1 103 ? -1.586  30.950 6.159   1.00 42.66 ?  120 ARG   A NE  1 
ATOM   808  C CZ  . ARG   A 1 103 ? -2.317  31.847 5.506   1.00 36.81 ?  120 ARG   A CZ  1 
ATOM   809  N NH1 . ARG   A 1 103 ? -3.515  31.553 5.028   1.00 34.91 ?  120 ARG   A NH1 1 
ATOM   810  N NH2 . ARG   A 1 103 ? -1.828  33.074 5.332   1.00 38.70 ?  120 ARG   A NH2 1 
ATOM   811  N N   . PRO   A 1 104 ? -2.854  29.758 12.236  1.00 39.66 ?  121 PRO   A N   1 
ATOM   812  C CA  . PRO   A 1 104 ? -2.436  30.533 13.415  1.00 42.35 ?  121 PRO   A CA  1 
ATOM   813  C C   . PRO   A 1 104 ? -1.173  31.351 13.203  1.00 45.89 ?  121 PRO   A C   1 
ATOM   814  O O   . PRO   A 1 104 ? -0.965  32.345 13.915  1.00 43.08 ?  121 PRO   A O   1 
ATOM   815  C CB  . PRO   A 1 104 ? -2.222  29.446 14.478  1.00 40.57 ?  121 PRO   A CB  1 
ATOM   816  C CG  . PRO   A 1 104 ? -3.103  28.338 14.063  1.00 42.30 ?  121 PRO   A CG  1 
ATOM   817  C CD  . PRO   A 1 104 ? -3.079  28.339 12.559  1.00 41.93 ?  121 PRO   A CD  1 
ATOM   818  N N   . GLN   A 1 105 ? -0.307  30.962 12.264  1.00 43.53 ?  122 GLN   A N   1 
ATOM   819  C CA  . GLN   A 1 105 ? 0.922   31.720 12.080  1.00 47.90 ?  122 GLN   A CA  1 
ATOM   820  C C   . GLN   A 1 105 ? 0.652   33.096 11.480  1.00 47.32 ?  122 GLN   A C   1 
ATOM   821  O O   . GLN   A 1 105 ? 1.561   33.938 11.446  1.00 49.15 ?  122 GLN   A O   1 
ATOM   822  C CB  . GLN   A 1 105 ? 1.903   30.910 11.226  1.00 53.32 ?  122 GLN   A CB  1 
ATOM   823  C CG  . GLN   A 1 105 ? 3.286   31.520 11.089  1.00 59.46 ?  122 GLN   A CG  1 
ATOM   824  C CD  . GLN   A 1 105 ? 4.256   30.590 10.391  1.00 69.61 ?  122 GLN   A CD  1 
ATOM   825  O OE1 . GLN   A 1 105 ? 3.918   29.442 10.084  1.00 73.58 ?  122 GLN   A OE1 1 
ATOM   826  N NE2 . GLN   A 1 105 ? 5.481   31.066 10.161  1.00 66.22 ?  122 GLN   A NE2 1 
ATOM   827  N N   . SER   A 1 106 ? -0.588  33.353 11.055  1.00 44.78 ?  123 SER   A N   1 
ATOM   828  C CA  . SER   A 1 106 ? -1.012  34.696 10.676  1.00 44.01 ?  123 SER   A CA  1 
ATOM   829  C C   . SER   A 1 106 ? -0.898  35.697 11.821  1.00 45.22 ?  123 SER   A C   1 
ATOM   830  O O   . SER   A 1 106 ? -0.911  36.908 11.573  1.00 45.98 ?  123 SER   A O   1 
ATOM   831  C CB  . SER   A 1 106 ? -2.454  34.653 10.179  1.00 44.26 ?  123 SER   A CB  1 
ATOM   832  O OG  . SER   A 1 106 ? -3.358  34.466 11.262  1.00 40.68 ?  123 SER   A OG  1 
ATOM   833  N N   . GLY   A 1 107 ? -0.797  35.230 13.066  1.00 44.40 ?  124 GLY   A N   1 
ATOM   834  C CA  . GLY   A 1 107 ? -0.848  36.109 14.213  1.00 43.16 ?  124 GLY   A CA  1 
ATOM   835  C C   . GLY   A 1 107 ? -2.227  36.633 14.576  1.00 42.04 ?  124 GLY   A C   1 
ATOM   836  O O   . GLY   A 1 107 ? -2.353  37.342 15.584  1.00 44.75 ?  124 GLY   A O   1 
ATOM   837  N N   . ARG   A 1 108 ? -3.256  36.325 13.793  1.00 40.04 ?  125 ARG   A N   1 
ATOM   838  C CA  . ARG   A 1 108 ? -4.621  36.729 14.103  1.00 40.36 ?  125 ARG   A CA  1 
ATOM   839  C C   . ARG   A 1 108 ? -5.285  35.719 15.037  1.00 37.22 ?  125 ARG   A C   1 
ATOM   840  O O   . ARG   A 1 108 ? -4.892  34.550 15.117  1.00 34.08 ?  125 ARG   A O   1 
ATOM   841  C CB  . ARG   A 1 108 ? -5.482  36.836 12.835  1.00 40.13 ?  125 ARG   A CB  1 
ATOM   842  C CG  . ARG   A 1 108 ? -5.053  37.860 11.793  1.00 43.94 ?  125 ARG   A CG  1 
ATOM   843  C CD  . ARG   A 1 108 ? -5.697  37.522 10.441  1.00 41.02 ?  125 ARG   A CD  1 
ATOM   844  N NE  . ARG   A 1 108 ? -5.148  38.300 9.333   1.00 44.62 ?  125 ARG   A NE  1 
ATOM   845  C CZ  . ARG   A 1 108 ? -5.342  39.600 9.147   1.00 44.06 ?  125 ARG   A CZ  1 
ATOM   846  N NH1 . ARG   A 1 108 ? -6.152  40.299 9.927   1.00 44.91 ?  125 ARG   A NH1 1 
ATOM   847  N NH2 . ARG   A 1 108 ? -4.715  40.212 8.143   1.00 46.59 ?  125 ARG   A NH2 1 
ATOM   848  N N   . VAL   A 1 109 ? -6.309  36.186 15.751  1.00 37.28 ?  126 VAL   A N   1 
ATOM   849  C CA  . VAL   A 1 109 ? -7.253  35.310 16.438  1.00 33.44 ?  126 VAL   A CA  1 
ATOM   850  C C   . VAL   A 1 109 ? -8.500  35.211 15.573  1.00 31.04 ?  126 VAL   A C   1 
ATOM   851  O O   . VAL   A 1 109 ? -9.114  36.233 15.242  1.00 29.11 ?  126 VAL   A O   1 
ATOM   852  C CB  . VAL   A 1 109 ? -7.595  35.820 17.847  1.00 34.00 ?  126 VAL   A CB  1 
ATOM   853  C CG1 . VAL   A 1 109 ? -8.483  34.806 18.543  1.00 33.87 ?  126 VAL   A CG1 1 
ATOM   854  C CG2 . VAL   A 1 109 ? -6.321  36.048 18.654  1.00 37.64 ?  126 VAL   A CG2 1 
ATOM   855  N N   . LEU   A 1 110 ? -8.874  33.987 15.201  1.00 27.66 ?  127 LEU   A N   1 
ATOM   856  C CA  . LEU   A 1 110 ? -10.007 33.789 14.310  1.00 28.64 ?  127 LEU   A CA  1 
ATOM   857  C C   . LEU   A 1 110 ? -11.300 34.246 14.971  1.00 26.93 ?  127 LEU   A C   1 
ATOM   858  O O   . LEU   A 1 110 ? -11.521 34.007 16.161  1.00 29.63 ?  127 LEU   A O   1 
ATOM   859  C CB  . LEU   A 1 110 ? -10.123 32.316 13.904  1.00 25.64 ?  127 LEU   A CB  1 
ATOM   860  C CG  . LEU   A 1 110 ? -11.374 31.918 13.112  1.00 25.70 ?  127 LEU   A CG  1 
ATOM   861  C CD1 . LEU   A 1 110 ? -11.409 32.641 11.737  1.00 23.81 ?  127 LEU   A CD1 1 
ATOM   862  C CD2 . LEU   A 1 110 ? -11.406 30.421 12.913  1.00 26.59 ?  127 LEU   A CD2 1 
ATOM   863  N N   . SER   A 1 111 ? -12.134 34.926 14.181  1.00 23.58 ?  128 SER   A N   1 
ATOM   864  C CA  . SER   A 1 111 ? -13.503 35.311 14.524  1.00 24.73 ?  128 SER   A CA  1 
ATOM   865  C C   . SER   A 1 111 ? -14.174 34.314 15.460  1.00 25.59 ?  128 SER   A C   1 
ATOM   866  O O   . SER   A 1 111 ? -14.203 33.111 15.169  1.00 25.04 ?  128 SER   A O   1 
ATOM   867  C CB  . SER   A 1 111 ? -14.335 35.420 13.246  1.00 23.36 ?  128 SER   A CB  1 
ATOM   868  O OG  . SER   A 1 111 ? -15.665 35.815 13.519  1.00 24.65 ?  128 SER   A OG  1 
ATOM   869  N N   . ALA   A 1 112 ? -14.757 34.798 16.552  1.00 23.13 ?  129 ALA   A N   1 
ATOM   870  C CA  . ALA   A 1 112 ? -15.507 33.897 17.420  1.00 22.52 ?  129 ALA   A CA  1 
ATOM   871  C C   . ALA   A 1 112 ? -16.773 33.403 16.733  1.00 25.31 ?  129 ALA   A C   1 
ATOM   872  O O   . ALA   A 1 112 ? -17.300 32.343 17.098  1.00 25.40 ?  129 ALA   A O   1 
ATOM   873  C CB  . ALA   A 1 112 ? -15.836 34.600 18.751  1.00 23.54 ?  129 ALA   A CB  1 
ATOM   874  N N   . MET   A 1 113 ? -17.252 34.114 15.716  1.00 24.87 ?  130 MET   A N   1 
ATOM   875  C CA  . MET   A 1 113 ? -18.480 33.676 15.076  1.00 24.22 ?  130 MET   A CA  1 
ATOM   876  C C   . MET   A 1 113 ? -18.212 32.503 14.151  1.00 27.88 ?  130 MET   A C   1 
ATOM   877  O O   . MET   A 1 113 ? -19.138 31.736 13.841  1.00 27.18 ?  130 MET   A O   1 
ATOM   878  C CB  . MET   A 1 113 ? -19.137 34.822 14.315  1.00 24.26 ?  130 MET   A CB  1 
ATOM   879  C CG  . MET   A 1 113 ? -19.611 35.922 15.293  1.00 24.18 ?  130 MET   A CG  1 
ATOM   880  S SD  . MET   A 1 113 ? -20.768 35.418 16.534  1.00 25.97 ?  130 MET   A SD  1 
ATOM   881  C CE  . MET   A 1 113 ? -22.279 35.359 15.548  1.00 25.44 ?  130 MET   A CE  1 
ATOM   882  N N   . ILE   A 1 114 ? -16.965 32.342 13.703  1.00 23.19 ?  131 ILE   A N   1 
ATOM   883  C CA  . ILE   A 1 114 ? -16.577 31.174 12.922  1.00 22.98 ?  131 ILE   A CA  1 
ATOM   884  C C   . ILE   A 1 114 ? -16.035 30.064 13.816  1.00 24.36 ?  131 ILE   A C   1 
ATOM   885  O O   . ILE   A 1 114 ? -16.455 28.908 13.712  1.00 25.85 ?  131 ILE   A O   1 
ATOM   886  C CB  . ILE   A 1 114 ? -15.553 31.591 11.846  1.00 23.79 ?  131 ILE   A CB  1 
ATOM   887  C CG1 . ILE   A 1 114 ? -16.129 32.720 10.979  1.00 22.21 ?  131 ILE   A CG1 1 
ATOM   888  C CG2 . ILE   A 1 114 ? -15.151 30.374 11.006  1.00 25.08 ?  131 ILE   A CG2 1 
ATOM   889  C CD1 . ILE   A 1 114 ? -17.472 32.386 10.356  1.00 21.24 ?  131 ILE   A CD1 1 
ATOM   890  N N   . ARG   A 1 115 ? -15.100 30.385 14.717  1.00 24.64 ?  132 ARG   A N   1 
ATOM   891  C CA  . ARG   A 1 115 ? -14.599 29.369 15.640  1.00 23.16 ?  132 ARG   A CA  1 
ATOM   892  C C   . ARG   A 1 115 ? -15.742 28.761 16.447  1.00 28.76 ?  132 ARG   A C   1 
ATOM   893  O O   . ARG   A 1 115 ? -15.795 27.538 16.654  1.00 29.22 ?  132 ARG   A O   1 
ATOM   894  C CB  . ARG   A 1 115 ? -13.545 29.987 16.572  1.00 27.29 ?  132 ARG   A CB  1 
ATOM   895  C CG  . ARG   A 1 115 ? -12.847 29.008 17.505  1.00 32.17 ?  132 ARG   A CG  1 
ATOM   896  C CD  . ARG   A 1 115 ? -11.822 28.174 16.754  1.00 34.70 ?  132 ARG   A CD  1 
ATOM   897  N NE  . ARG   A 1 115 ? -10.614 28.925 16.423  1.00 32.25 ?  132 ARG   A NE  1 
ATOM   898  C CZ  . ARG   A 1 115 ? -9.590  28.414 15.752  1.00 36.05 ?  132 ARG   A CZ  1 
ATOM   899  N NH1 . ARG   A 1 115 ? -9.586  27.152 15.360  1.00 34.72 ?  132 ARG   A NH1 1 
ATOM   900  N NH2 . ARG   A 1 115 ? -8.524  29.174 15.513  1.00 35.21 ?  132 ARG   A NH2 1 
ATOM   901  N N   . GLY   A 1 116 ? -16.667 29.607 16.920  1.00 25.15 ?  133 GLY   A N   1 
ATOM   902  C CA  . GLY   A 1 116 ? -17.757 29.144 17.758  1.00 26.02 ?  133 GLY   A CA  1 
ATOM   903  C C   . GLY   A 1 116 ? -18.923 28.537 17.006  1.00 25.25 ?  133 GLY   A C   1 
ATOM   904  O O   . GLY   A 1 116 ? -19.809 27.970 17.649  1.00 27.55 ?  133 GLY   A O   1 
ATOM   905  N N   . ALA   A 1 117 ? -18.959 28.669 15.677  1.00 25.20 ?  134 ALA   A N   1 
ATOM   906  C CA  . ALA   A 1 117 ? -19.947 27.957 14.868  1.00 27.42 ?  134 ALA   A CA  1 
ATOM   907  C C   . ALA   A 1 117 ? -19.627 26.474 14.763  1.00 30.67 ?  134 ALA   A C   1 
ATOM   908  O O   . ALA   A 1 117 ? -20.519 25.670 14.456  1.00 29.94 ?  134 ALA   A O   1 
ATOM   909  C CB  . ALA   A 1 117 ? -20.035 28.578 13.463  1.00 25.76 ?  134 ALA   A CB  1 
ATOM   910  N N   . ALA   A 1 118 ? -18.389 26.092 15.049  1.00 28.62 ?  135 ALA   A N   1 
ATOM   911  C CA  . ALA   A 1 118 ? -17.961 24.717 14.853  1.00 33.33 ?  135 ALA   A CA  1 
ATOM   912  C C   . ALA   A 1 118 ? -18.627 23.778 15.848  1.00 37.08 ?  135 ALA   A C   1 
ATOM   913  O O   . ALA   A 1 118 ? -18.853 24.116 17.018  1.00 35.96 ?  135 ALA   A O   1 
ATOM   914  C CB  . ALA   A 1 118 ? -16.438 24.611 14.971  1.00 35.20 ?  135 ALA   A CB  1 
ATOM   915  N N   . ASP   A 1 119 ? -18.938 22.583 15.370  1.00 36.18 ?  136 ASP   A N   1 
ATOM   916  C CA  . ASP   A 1 119 ? -19.409 21.498 16.212  1.00 40.86 ?  136 ASP   A CA  1 
ATOM   917  C C   . ASP   A 1 119 ? -18.545 20.257 16.061  1.00 43.16 ?  136 ASP   A C   1 
ATOM   918  O O   . ASP   A 1 119 ? -18.906 19.197 16.582  1.00 46.13 ?  136 ASP   A O   1 
ATOM   919  C CB  . ASP   A 1 119 ? -20.876 21.190 15.898  1.00 43.52 ?  136 ASP   A CB  1 
ATOM   920  C CG  . ASP   A 1 119 ? -21.109 20.889 14.426  1.00 42.30 ?  136 ASP   A CG  1 
ATOM   921  O OD1 . ASP   A 1 119 ? -20.261 20.224 13.796  1.00 42.76 ?  136 ASP   A OD1 1 
ATOM   922  O OD2 . ASP   A 1 119 ? -22.157 21.317 13.899  1.00 46.31 ?  136 ASP   A OD2 1 
ATOM   923  N N   . GLY   A 1 120 ? -17.423 20.360 15.343  1.00 40.97 ?  137 GLY   A N   1 
ATOM   924  C CA  . GLY   A 1 120 ? -16.472 19.275 15.244  1.00 43.38 ?  137 GLY   A CA  1 
ATOM   925  C C   . GLY   A 1 120 ? -16.868 18.165 14.301  1.00 47.03 ?  137 GLY   A C   1 
ATOM   926  O O   . GLY   A 1 120 ? -16.140 17.166 14.209  1.00 49.61 ?  137 GLY   A O   1 
ATOM   927  N N   . SER   A 1 121 ? -17.993 18.305 13.601  1.00 45.75 ?  138 SER   A N   1 
ATOM   928  C CA  . SER   A 1 121 ? -18.462 17.287 12.669  1.00 44.07 ?  138 SER   A CA  1 
ATOM   929  C C   . SER   A 1 121 ? -18.934 17.927 11.373  1.00 41.70 ?  138 SER   A C   1 
ATOM   930  O O   . SER   A 1 121 ? -18.199 17.954 10.379  1.00 45.48 ?  138 SER   A O   1 
ATOM   931  C CB  A SER   A 1 121 ? -19.607 16.484 13.286  0.49 48.53 ?  138 SER   A CB  1 
ATOM   932  C CB  B SER   A 1 121 ? -19.584 16.454 13.282  0.51 48.53 ?  138 SER   A CB  1 
ATOM   933  O OG  A SER   A 1 121 ? -20.774 17.287 13.421  0.49 46.53 ?  138 SER   A OG  1 
ATOM   934  O OG  B SER   A 1 121 ? -19.945 15.398 12.407  0.51 48.49 ?  138 SER   A OG  1 
ATOM   935  N N   . ARG   A 1 122 ? -20.165 18.445 11.373  1.00 41.20 ?  139 ARG   A N   1 
ATOM   936  C CA  . ARG   A 1 122 ? -20.691 19.052 10.152  1.00 39.01 ?  139 ARG   A CA  1 
ATOM   937  C C   . ARG   A 1 122 ? -20.123 20.445 9.899   1.00 37.53 ?  139 ARG   A C   1 
ATOM   938  O O   . ARG   A 1 122 ? -20.028 20.869 8.744   1.00 31.99 ?  139 ARG   A O   1 
ATOM   939  C CB  . ARG   A 1 122 ? -22.209 19.124 10.213  1.00 40.61 ?  139 ARG   A CB  1 
ATOM   940  C CG  . ARG   A 1 122 ? -22.807 19.355 8.853   1.00 36.80 ?  139 ARG   A CG  1 
ATOM   941  C CD  . ARG   A 1 122 ? -24.134 18.653 8.746   1.00 39.24 ?  139 ARG   A CD  1 
ATOM   942  N NE  . ARG   A 1 122 ? -24.707 18.839 7.423   1.00 38.46 ?  139 ARG   A NE  1 
ATOM   943  C CZ  . ARG   A 1 122 ? -24.560 17.977 6.430   1.00 38.72 ?  139 ARG   A CZ  1 
ATOM   944  N NH1 . ARG   A 1 122 ? -23.923 16.833 6.605   1.00 39.32 ?  139 ARG   A NH1 1 
ATOM   945  N NH2 . ARG   A 1 122 ? -25.084 18.260 5.241   1.00 41.71 ?  139 ARG   A NH2 1 
ATOM   946  N N   . PHE   A 1 123 ? -19.767 21.181 10.946  1.00 34.18 ?  140 PHE   A N   1 
ATOM   947  C CA  . PHE   A 1 123 ? -19.050 22.449 10.809  1.00 32.46 ?  140 PHE   A CA  1 
ATOM   948  C C   . PHE   A 1 123 ? -17.735 22.278 11.555  1.00 35.39 ?  140 PHE   A C   1 
ATOM   949  O O   . PHE   A 1 123 ? -17.721 22.190 12.784  1.00 33.41 ?  140 PHE   A O   1 
ATOM   950  C CB  . PHE   A 1 123 ? -19.879 23.620 11.345  1.00 32.32 ?  140 PHE   A CB  1 
ATOM   951  C CG  . PHE   A 1 123 ? -19.340 24.996 10.979  1.00 29.32 ?  140 PHE   A CG  1 
ATOM   952  C CD1 . PHE   A 1 123 ? -18.038 25.375 11.274  1.00 28.39 ?  140 PHE   A CD1 1 
ATOM   953  C CD2 . PHE   A 1 123 ? -20.142 25.896 10.301  1.00 26.88 ?  140 PHE   A CD2 1 
ATOM   954  C CE1 . PHE   A 1 123 ? -17.563 26.635 10.933  1.00 27.56 ?  140 PHE   A CE1 1 
ATOM   955  C CE2 . PHE   A 1 123 ? -19.674 27.157 9.945   1.00 25.90 ?  140 PHE   A CE2 1 
ATOM   956  C CZ  . PHE   A 1 123 ? -18.387 27.529 10.256  1.00 26.42 ?  140 PHE   A CZ  1 
ATOM   957  N N   . GLN   A 1 124 ? -16.635 22.202 10.816  1.00 32.89 ?  141 GLN   A N   1 
ATOM   958  C CA  . GLN   A 1 124 ? -15.338 21.919 11.406  1.00 34.93 ?  141 GLN   A CA  1 
ATOM   959  C C   . GLN   A 1 124 ? -14.402 23.082 11.112  1.00 31.95 ?  141 GLN   A C   1 
ATOM   960  O O   . GLN   A 1 124 ? -14.417 23.628 10.007  1.00 31.31 ?  141 GLN   A O   1 
ATOM   961  C CB  . GLN   A 1 124 ? -14.762 20.625 10.832  1.00 39.41 ?  141 GLN   A CB  1 
ATOM   962  C CG  . GLN   A 1 124 ? -15.043 19.405 11.686  1.00 42.26 ?  141 GLN   A CG  1 
ATOM   963  C CD  . GLN   A 1 124 ? -14.528 18.120 11.065  1.00 47.04 ?  141 GLN   A CD  1 
ATOM   964  O OE1 . GLN   A 1 124 ? -15.279 17.366 10.444  1.00 48.70 ?  141 GLN   A OE1 1 
ATOM   965  N NE2 . GLN   A 1 124 ? -13.270 17.815 11.318  1.00 49.08 ?  141 GLN   A NE2 1 
ATOM   966  N N   . VAL   A 1 125 ? -13.603 23.481 12.100  1.00 30.90 ?  142 VAL   A N   1 
ATOM   967  C CA  . VAL   A 1 125 ? -12.572 24.501 11.908  1.00 32.79 ?  142 VAL   A CA  1 
ATOM   968  C C   . VAL   A 1 125 ? -11.227 23.900 12.298  1.00 35.33 ?  142 VAL   A C   1 
ATOM   969  O O   . VAL   A 1 125 ? -11.020 23.531 13.464  1.00 33.97 ?  142 VAL   A O   1 
ATOM   970  C CB  . VAL   A 1 125 ? -12.840 25.771 12.729  1.00 33.18 ?  142 VAL   A CB  1 
ATOM   971  C CG1 . VAL   A 1 125 ? -11.734 26.795 12.471  1.00 32.43 ?  142 VAL   A CG1 1 
ATOM   972  C CG2 . VAL   A 1 125 ? -14.210 26.340 12.416  1.00 32.16 ?  142 VAL   A CG2 1 
ATOM   973  N N   . TRP   A 1 126 ? -10.306 23.831 11.341  1.00 32.62 ?  143 TRP   A N   1 
ATOM   974  C CA  . TRP   A 1 126 ? -8.985  23.264 11.582  1.00 36.50 ?  143 TRP   A CA  1 
ATOM   975  C C   . TRP   A 1 126 ? -7.902  24.328 11.492  1.00 39.11 ?  143 TRP   A C   1 
ATOM   976  O O   . TRP   A 1 126 ? -7.802  25.035 10.482  1.00 37.78 ?  143 TRP   A O   1 
ATOM   977  C CB  . TRP   A 1 126 ? -8.651  22.150 10.593  1.00 40.06 ?  143 TRP   A CB  1 
ATOM   978  C CG  . TRP   A 1 126 ? -9.527  20.974 10.693  1.00 39.08 ?  143 TRP   A CG  1 
ATOM   979  C CD1 . TRP   A 1 126 ? -10.510 20.758 11.609  1.00 41.45 ?  143 TRP   A CD1 1 
ATOM   980  C CD2 . TRP   A 1 126 ? -9.458  19.797 9.888   1.00 42.37 ?  143 TRP   A CD2 1 
ATOM   981  N NE1 . TRP   A 1 126 ? -11.091 19.535 11.395  1.00 41.93 ?  143 TRP   A NE1 1 
ATOM   982  C CE2 . TRP   A 1 126 ? -10.454 18.918 10.350  1.00 42.12 ?  143 TRP   A CE2 1 
ATOM   983  C CE3 . TRP   A 1 126 ? -8.657  19.406 8.813   1.00 45.14 ?  143 TRP   A CE3 1 
ATOM   984  C CZ2 . TRP   A 1 126 ? -10.673 17.669 9.772   1.00 44.55 ?  143 TRP   A CZ2 1 
ATOM   985  C CZ3 . TRP   A 1 126 ? -8.874  18.159 8.239   1.00 48.26 ?  143 TRP   A CZ3 1 
ATOM   986  C CH2 . TRP   A 1 126 ? -9.875  17.309 8.719   1.00 45.43 ?  143 TRP   A CH2 1 
ATOM   987  N N   . ASP   A 1 127 ? -7.078  24.409 12.538  1.00 39.15 ?  144 ASP   A N   1 
ATOM   988  C CA  . ASP   A 1 127 ? -5.816  25.125 12.441  1.00 40.31 ?  144 ASP   A CA  1 
ATOM   989  C C   . ASP   A 1 127 ? -4.828  24.316 11.614  1.00 42.43 ?  144 ASP   A C   1 
ATOM   990  O O   . ASP   A 1 127 ? -4.812  23.083 11.658  1.00 45.13 ?  144 ASP   A O   1 
ATOM   991  C CB  . ASP   A 1 127 ? -5.207  25.384 13.819  1.00 39.24 ?  144 ASP   A CB  1 
ATOM   992  C CG  . ASP   A 1 127 ? -6.025  26.328 14.675  1.00 40.68 ?  144 ASP   A CG  1 
ATOM   993  O OD1 . ASP   A 1 127 ? -6.852  27.077 14.135  1.00 37.80 ?  144 ASP   A OD1 1 
ATOM   994  O OD2 . ASP   A 1 127 ? -5.787  26.353 15.910  1.00 45.30 ?  144 ASP   A OD2 1 
ATOM   995  N N   . TYR   A 1 128 ? -3.978  25.018 10.872  1.00 45.44 ?  145 TYR   A N   1 
ATOM   996  C CA  . TYR   A 1 128 ? -2.970  24.334 10.077  1.00 46.38 ?  145 TYR   A CA  1 
ATOM   997  C C   . TYR   A 1 128 ? -1.851  25.301 9.728   1.00 47.26 ?  145 TYR   A C   1 
ATOM   998  O O   . TYR   A 1 128 ? -2.009  26.522 9.797   1.00 43.08 ?  145 TYR   A O   1 
ATOM   999  C CB  . TYR   A 1 128 ? -3.577  23.732 8.806   1.00 45.38 ?  145 TYR   A CB  1 
ATOM   1000 C CG  . TYR   A 1 128 ? -3.833  24.734 7.700   1.00 42.54 ?  145 TYR   A CG  1 
ATOM   1001 C CD1 . TYR   A 1 128 ? -4.846  25.673 7.809   1.00 39.12 ?  145 TYR   A CD1 1 
ATOM   1002 C CD2 . TYR   A 1 128 ? -3.059  24.740 6.551   1.00 47.76 ?  145 TYR   A CD2 1 
ATOM   1003 C CE1 . TYR   A 1 128 ? -5.082  26.589 6.806   1.00 37.00 ?  145 TYR   A CE1 1 
ATOM   1004 C CE2 . TYR   A 1 128 ? -3.286  25.656 5.540   1.00 43.45 ?  145 TYR   A CE2 1 
ATOM   1005 C CZ  . TYR   A 1 128 ? -4.298  26.577 5.675   1.00 39.23 ?  145 TYR   A CZ  1 
ATOM   1006 O OH  . TYR   A 1 128 ? -4.536  27.496 4.680   1.00 37.43 ?  145 TYR   A OH  1 
ATOM   1007 N N   . GLU   A 1 129 ? -0.708  24.727 9.377   1.00 51.48 ?  146 GLU   A N   1 
ATOM   1008 C CA  . GLU   A 1 129 ? 0.403   25.451 8.780   1.00 56.69 ?  146 GLU   A CA  1 
ATOM   1009 C C   . GLU   A 1 129 ? 0.435   25.182 7.280   1.00 56.87 ?  146 GLU   A C   1 
ATOM   1010 O O   . GLU   A 1 129 ? -0.007  24.132 6.814   1.00 56.58 ?  146 GLU   A O   1 
ATOM   1011 C CB  . GLU   A 1 129 ? 1.716   25.065 9.467   1.00 59.03 ?  146 GLU   A CB  1 
ATOM   1012 C CG  . GLU   A 1 129 ? 2.125   23.610 9.306   1.00 66.74 ?  146 GLU   A CG  1 
ATOM   1013 C CD  . GLU   A 1 129 ? 3.373   23.413 8.465   1.00 72.45 ?  146 GLU   A CD  1 
ATOM   1014 O OE1 . GLU   A 1 129 ? 3.868   22.260 8.395   1.00 74.32 ?  146 GLU   A OE1 1 
ATOM   1015 O OE2 . GLU   A 1 129 ? 3.837   24.398 7.850   1.00 72.87 ?  146 GLU   A OE2 1 
ATOM   1016 N N   . GLU   A 1 130 ? 0.928   26.160 6.518   1.00 61.62 ?  147 GLU   A N   1 
ATOM   1017 C CA  . GLU   A 1 130 ? 0.642   26.173 5.085   1.00 63.80 ?  147 GLU   A CA  1 
ATOM   1018 C C   . GLU   A 1 130 ? 1.165   24.928 4.379   1.00 63.66 ?  147 GLU   A C   1 
ATOM   1019 O O   . GLU   A 1 130 ? 0.530   24.442 3.436   1.00 62.43 ?  147 GLU   A O   1 
ATOM   1020 C CB  . GLU   A 1 130 ? 1.217   27.428 4.424   1.00 61.36 ?  147 GLU   A CB  1 
ATOM   1021 C CG  . GLU   A 1 130 ? 0.404   27.828 3.203   1.00 63.73 ?  147 GLU   A CG  1 
ATOM   1022 C CD  . GLU   A 1 130 ? 1.212   28.491 2.115   0.67 62.17 ?  147 GLU   A CD  1 
ATOM   1023 O OE1 . GLU   A 1 130 ? 1.461   27.842 1.071   0.78 63.16 ?  147 GLU   A OE1 1 
ATOM   1024 O OE2 . GLU   A 1 130 ? 1.577   29.669 2.300   1.00 65.17 ?  147 GLU   A OE2 1 
ATOM   1025 N N   . GLY   A 1 131 ? 2.298   24.387 4.828   1.00 64.61 ?  148 GLY   A N   1 
ATOM   1026 C CA  . GLY   A 1 131 ? 2.904   23.262 4.135   1.00 65.91 ?  148 GLY   A CA  1 
ATOM   1027 C C   . GLY   A 1 131 ? 2.094   21.978 4.167   1.00 62.74 ?  148 GLY   A C   1 
ATOM   1028 O O   . GLY   A 1 131 ? 2.334   21.093 3.341   1.00 67.64 ?  148 GLY   A O   1 
ATOM   1029 N N   . GLU   A 1 132 ? 1.142   21.850 5.092   1.00 62.95 ?  149 GLU   A N   1 
ATOM   1030 C CA  . GLU   A 1 132 ? 0.438   20.587 5.291   1.00 61.76 ?  149 GLU   A CA  1 
ATOM   1031 C C   . GLU   A 1 132 ? -0.996  20.619 4.774   1.00 56.62 ?  149 GLU   A C   1 
ATOM   1032 O O   . GLU   A 1 132 ? -1.818  19.799 5.193   1.00 54.33 ?  149 GLU   A O   1 
ATOM   1033 C CB  . GLU   A 1 132 ? 0.453   20.199 6.771   1.00 64.72 ?  149 GLU   A CB  1 
ATOM   1034 C CG  . GLU   A 1 132 ? 0.096   21.337 7.703   1.00 64.36 ?  149 GLU   A CG  1 
ATOM   1035 C CD  . GLU   A 1 132 ? -0.410  20.893 9.067   1.00 67.93 ?  149 GLU   A CD  1 
ATOM   1036 O OE1 . GLU   A 1 132 ? -0.541  21.761 9.960   1.00 70.54 ?  149 GLU   A OE1 1 
ATOM   1037 O OE2 . GLU   A 1 132 ? -0.655  19.683 9.257   1.00 74.15 ?  149 GLU   A OE2 1 
ATOM   1038 N N   . VAL   A 1 133 ? -1.313  21.527 3.853   1.00 57.51 ?  150 VAL   A N   1 
ATOM   1039 C CA  . VAL   A 1 133 ? -2.708  21.682 3.460   1.00 55.67 ?  150 VAL   A CA  1 
ATOM   1040 C C   . VAL   A 1 133 ? -3.182  20.477 2.644   1.00 51.36 ?  150 VAL   A C   1 
ATOM   1041 O O   . VAL   A 1 133 ? -4.317  20.016 2.809   1.00 49.58 ?  150 VAL   A O   1 
ATOM   1042 C CB  . VAL   A 1 133 ? -2.918  23.026 2.731   1.00 51.77 ?  150 VAL   A CB  1 
ATOM   1043 C CG1 . VAL   A 1 133 ? -2.623  22.923 1.250   1.00 55.63 ?  150 VAL   A CG1 1 
ATOM   1044 C CG2 . VAL   A 1 133 ? -4.334  23.540 2.972   1.00 45.76 ?  150 VAL   A CG2 1 
ATOM   1045 N N   . GLU   A 1 134 ? -2.318  19.909 1.797   1.00 52.44 ?  151 GLU   A N   1 
ATOM   1046 C CA  . GLU   A 1 134 ? -2.731  18.746 1.014   1.00 52.02 ?  151 GLU   A CA  1 
ATOM   1047 C C   . GLU   A 1 134 ? -2.995  17.538 1.900   1.00 53.54 ?  151 GLU   A C   1 
ATOM   1048 O O   . GLU   A 1 134 ? -3.983  16.821 1.699   1.00 51.95 ?  151 GLU   A O   1 
ATOM   1049 C CB  . GLU   A 1 134 ? -1.678  18.409 -0.041  1.00 54.71 ?  151 GLU   A CB  1 
ATOM   1050 C CG  . GLU   A 1 134 ? -1.606  19.411 -1.176  1.00 56.92 ?  151 GLU   A CG  1 
ATOM   1051 C CD  . GLU   A 1 134 ? -0.714  20.595 -0.869  1.00 59.29 ?  151 GLU   A CD  1 
ATOM   1052 O OE1 . GLU   A 1 134 ? 0.060   20.534 0.116   1.00 59.40 ?  151 GLU   A OE1 1 
ATOM   1053 O OE2 . GLU   A 1 134 ? -0.780  21.582 -1.631  1.00 56.51 ?  151 GLU   A OE2 1 
ATOM   1054 N N   . ALA   A 1 135 ? -2.122  17.289 2.876   1.00 54.86 ?  152 ALA   A N   1 
ATOM   1055 C CA  . ALA   A 1 135 ? -2.318  16.149 3.765   1.00 55.00 ?  152 ALA   A CA  1 
ATOM   1056 C C   . ALA   A 1 135 ? -3.637  16.261 4.523   1.00 53.84 ?  152 ALA   A C   1 
ATOM   1057 O O   . ALA   A 1 135 ? -4.349  15.265 4.694   1.00 53.41 ?  152 ALA   A O   1 
ATOM   1058 C CB  . ALA   A 1 135 ? -1.140  16.034 4.730   1.00 57.91 ?  152 ALA   A CB  1 
ATOM   1059 N N   . LEU   A 1 136 ? -3.988  17.470 4.972   1.00 51.87 ?  153 LEU   A N   1 
ATOM   1060 C CA  . LEU   A 1 136 ? -5.234  17.638 5.710   1.00 50.75 ?  153 LEU   A CA  1 
ATOM   1061 C C   . LEU   A 1 136 ? -6.442  17.406 4.818   1.00 49.74 ?  153 LEU   A C   1 
ATOM   1062 O O   . LEU   A 1 136 ? -7.429  16.797 5.248   1.00 50.45 ?  153 LEU   A O   1 
ATOM   1063 C CB  . LEU   A 1 136 ? -5.300  19.027 6.337   1.00 50.87 ?  153 LEU   A CB  1 
ATOM   1064 C CG  . LEU   A 1 136 ? -4.412  19.227 7.562   1.00 56.67 ?  153 LEU   A CG  1 
ATOM   1065 C CD1 . LEU   A 1 136 ? -4.741  20.552 8.206   1.00 56.07 ?  153 LEU   A CD1 1 
ATOM   1066 C CD2 . LEU   A 1 136 ? -4.582  18.087 8.558   1.00 59.91 ?  153 LEU   A CD2 1 
ATOM   1067 N N   . LEU   A 1 137 ? -6.395  17.889 3.578   1.00 45.31 ?  154 LEU   A N   1 
ATOM   1068 C CA  . LEU   A 1 137 ? -7.538  17.681 2.700   1.00 48.61 ?  154 LEU   A CA  1 
ATOM   1069 C C   . LEU   A 1 137 ? -7.698  16.209 2.355   1.00 50.97 ?  154 LEU   A C   1 
ATOM   1070 O O   . LEU   A 1 137 ? -8.826  15.703 2.281   1.00 50.69 ?  154 LEU   A O   1 
ATOM   1071 C CB  . LEU   A 1 137 ? -7.409  18.522 1.432   1.00 45.96 ?  154 LEU   A CB  1 
ATOM   1072 C CG  . LEU   A 1 137 ? -7.548  20.017 1.705   1.00 43.80 ?  154 LEU   A CG  1 
ATOM   1073 C CD1 . LEU   A 1 137 ? -6.708  20.836 0.733   1.00 43.93 ?  154 LEU   A CD1 1 
ATOM   1074 C CD2 . LEU   A 1 137 ? -9.001  20.457 1.731   1.00 43.28 ?  154 LEU   A CD2 1 
ATOM   1075 N N   . ASP   A 1 138 ? -6.582  15.503 2.147   1.00 51.05 ?  155 ASP   A N   1 
ATOM   1076 C CA  . ASP   A 1 138 ? -6.662  14.064 1.928   1.00 51.53 ?  155 ASP   A CA  1 
ATOM   1077 C C   . ASP   A 1 138 ? -7.357  13.388 3.099   1.00 55.79 ?  155 ASP   A C   1 
ATOM   1078 O O   . ASP   A 1 138 ? -8.203  12.507 2.909   1.00 57.65 ?  155 ASP   A O   1 
ATOM   1079 C CB  . ASP   A 1 138 ? -5.264  13.474 1.747   1.00 51.95 ?  155 ASP   A CB  1 
ATOM   1080 C CG  . ASP   A 1 138 ? -4.639  13.836 0.416   1.00 55.74 ?  155 ASP   A CG  1 
ATOM   1081 O OD1 . ASP   A 1 138 ? -5.366  14.303 -0.491  1.00 54.37 ?  155 ASP   A OD1 1 
ATOM   1082 O OD2 . ASP   A 1 138 ? -3.413  13.626 0.274   1.00 55.56 ?  155 ASP   A OD2 1 
ATOM   1083 N N   . ARG   A 1 139 ? -7.011  13.801 4.322   1.00 53.93 ?  156 ARG   A N   1 
ATOM   1084 C CA  . ARG   A 1 139 ? -7.608  13.216 5.515   1.00 56.17 ?  156 ARG   A CA  1 
ATOM   1085 C C   . ARG   A 1 139 ? -9.100  13.519 5.585   1.00 51.41 ?  156 ARG   A C   1 
ATOM   1086 O O   . ARG   A 1 139 ? -9.907  12.631 5.881   1.00 57.36 ?  156 ARG   A O   1 
ATOM   1087 C CB  . ARG   A 1 139 ? -6.876  13.741 6.754   1.00 56.86 ?  156 ARG   A CB  1 
ATOM   1088 C CG  . ARG   A 1 139 ? -7.262  13.135 8.095   1.00 65.67 ?  156 ARG   A CG  1 
ATOM   1089 C CD  . ARG   A 1 139 ? -6.370  13.732 9.191   1.00 70.87 ?  156 ARG   A CD  1 
ATOM   1090 N NE  . ARG   A 1 139 ? -5.103  14.189 8.627   1.00 73.02 ?  156 ARG   A NE  1 
ATOM   1091 C CZ  . ARG   A 1 139 ? -4.111  14.741 9.314   1.00 74.42 ?  156 ARG   A CZ  1 
ATOM   1092 N NH1 . ARG   A 1 139 ? -4.191  14.920 10.623  1.00 75.67 ?  156 ARG   A NH1 1 
ATOM   1093 N NH2 . ARG   A 1 139 ? -3.011  15.125 8.668   1.00 71.19 ?  156 ARG   A NH2 1 
ATOM   1094 N N   . TYR   A 1 140 ? -9.487  14.760 5.283   1.00 50.21 ?  157 TYR   A N   1 
ATOM   1095 C CA  . TYR   A 1 140 ? -10.895 15.141 5.370   1.00 48.93 ?  157 TYR   A CA  1 
ATOM   1096 C C   . TYR   A 1 140 ? -11.752 14.407 4.341   1.00 49.20 ?  157 TYR   A C   1 
ATOM   1097 O O   . TYR   A 1 140 ? -12.891 14.032 4.637   1.00 49.17 ?  157 TYR   A O   1 
ATOM   1098 C CB  . TYR   A 1 140 ? -11.036 16.651 5.207   1.00 45.88 ?  157 TYR   A CB  1 
ATOM   1099 C CG  . TYR   A 1 140 ? -12.457 17.147 5.311   1.00 44.49 ?  157 TYR   A CG  1 
ATOM   1100 C CD1 . TYR   A 1 140 ? -13.020 17.429 6.545   1.00 43.40 ?  157 TYR   A CD1 1 
ATOM   1101 C CD2 . TYR   A 1 140 ? -13.229 17.356 4.174   1.00 42.98 ?  157 TYR   A CD2 1 
ATOM   1102 C CE1 . TYR   A 1 140 ? -14.317 17.888 6.652   1.00 45.14 ?  157 TYR   A CE1 1 
ATOM   1103 C CE2 . TYR   A 1 140 ? -14.532 17.814 4.272   1.00 43.27 ?  157 TYR   A CE2 1 
ATOM   1104 C CZ  . TYR   A 1 140 ? -15.067 18.081 5.513   1.00 40.52 ?  157 TYR   A CZ  1 
ATOM   1105 O OH  . TYR   A 1 140 ? -16.360 18.542 5.626   1.00 41.05 ?  157 TYR   A OH  1 
ATOM   1106 N N   . PHE   A 1 141 ? -11.235 14.195 3.131   1.00 50.08 ?  158 PHE   A N   1 
ATOM   1107 C CA  . PHE   A 1 141 ? -12.014 13.575 2.066   1.00 51.37 ?  158 PHE   A CA  1 
ATOM   1108 C C   . PHE   A 1 141 ? -11.786 12.068 1.957   1.00 56.89 ?  158 PHE   A C   1 
ATOM   1109 O O   . PHE   A 1 141 ? -12.217 11.452 0.975   1.00 59.12 ?  158 PHE   A O   1 
ATOM   1110 C CB  . PHE   A 1 141 ? -11.714 14.262 0.731   1.00 47.34 ?  158 PHE   A CB  1 
ATOM   1111 C CG  . PHE   A 1 141 ? -12.324 15.629 0.614   1.00 46.13 ?  158 PHE   A CG  1 
ATOM   1112 C CD1 . PHE   A 1 141 ? -13.673 15.780 0.333   1.00 43.93 ?  158 PHE   A CD1 1 
ATOM   1113 C CD2 . PHE   A 1 141 ? -11.552 16.764 0.798   1.00 44.51 ?  158 PHE   A CD2 1 
ATOM   1114 C CE1 . PHE   A 1 141 ? -14.240 17.039 0.233   1.00 40.70 ?  158 PHE   A CE1 1 
ATOM   1115 C CE2 . PHE   A 1 141 ? -12.115 18.026 0.708   1.00 42.97 ?  158 PHE   A CE2 1 
ATOM   1116 C CZ  . PHE   A 1 141 ? -13.462 18.162 0.421   1.00 39.49 ?  158 PHE   A CZ  1 
ATOM   1117 N N   . GLU   A 1 142 ? -11.140 11.456 2.943   1.00 58.41 ?  159 GLU   A N   1 
ATOM   1118 C CA  . GLU   A 1 142 ? -10.929 10.012 2.925   1.00 65.05 ?  159 GLU   A CA  1 
ATOM   1119 C C   . GLU   A 1 142 ? -11.941 9.304  3.818   1.00 67.10 ?  159 GLU   A C   1 
ATOM   1120 O O   . GLU   A 1 142 ? -13.007 8.894  3.358   1.00 72.47 ?  159 GLU   A O   1 
ATOM   1121 C CB  . GLU   A 1 142 ? -9.508  9.667  3.370   1.00 69.30 ?  159 GLU   A CB  1 
ATOM   1122 C CG  . GLU   A 1 142 ? -8.572  9.279  2.233   1.00 75.22 ?  159 GLU   A CG  1 
ATOM   1123 C CD  . GLU   A 1 142 ? -7.123  9.193  2.681   0.26 75.88 ?  159 GLU   A CD  1 
ATOM   1124 O OE1 . GLU   A 1 142 ? -6.223  9.307  1.822   1.00 78.15 ?  159 GLU   A OE1 1 
ATOM   1125 O OE2 . GLU   A 1 142 ? -6.884  9.018  3.896   0.91 78.17 ?  159 GLU   A OE2 1 
HETATM 1126 C C2  . A1BBE B 2 .   ? -16.512 39.075 -6.381  1.00 28.50 ?  201 A1BBE A C2  1 
HETATM 1127 C C4  . A1BBE B 2 .   ? -16.773 36.790 -6.176  1.00 26.49 ?  201 A1BBE A C4  1 
HETATM 1128 C C5  . A1BBE B 2 .   ? -16.046 36.602 -7.340  1.00 25.44 ?  201 A1BBE A C5  1 
HETATM 1129 C C01 . A1BBE B 2 .   ? -15.284 34.443 -2.085  1.00 22.67 ?  201 A1BBE A C01 1 
HETATM 1130 C C02 . A1BBE B 2 .   ? -15.876 35.443 -1.502  1.00 23.96 ?  201 A1BBE A C02 1 
HETATM 1131 C C03 . A1BBE B 2 .   ? -14.868 36.564 -1.000  1.00 26.40 ?  201 A1BBE A C03 1 
HETATM 1132 C C04 . A1BBE B 2 .   ? -16.849 36.102 -2.643  1.00 24.16 ?  201 A1BBE A C04 1 
HETATM 1133 C C05 . A1BBE B 2 .   ? -18.008 35.103 -4.525  1.00 25.20 ?  201 A1BBE A C05 1 
HETATM 1134 C C12 . A1BBE B 2 .   ? -16.253 34.028 -3.390  1.00 22.50 ?  201 A1BBE A C12 1 
HETATM 1135 C C6  . A1BBE B 2 .   ? -15.529 37.736 -7.993  1.00 26.22 ?  201 A1BBE A C6  1 
HETATM 1136 C C8  . A1BBE B 2 .   ? -16.595 34.606 -6.671  1.00 26.23 ?  201 A1BBE A C8  1 
HETATM 1137 C C9  . A1BBE B 2 .   ? -17.121 35.490 -5.727  1.00 23.26 ?  201 A1BBE A C9  1 
HETATM 1138 N N01 . A1BBE B 2 .   ? -17.340 34.813 -3.263  1.00 21.92 ?  201 A1BBE A N01 1 
HETATM 1139 N N1  . A1BBE B 2 .   ? -15.810 38.931 -7.508  1.00 28.03 ?  201 A1BBE A N1  1 
HETATM 1140 N N3  . A1BBE B 2 .   ? -16.993 38.032 -5.713  1.00 25.72 ?  201 A1BBE A N3  1 
HETATM 1141 N N6  . A1BBE B 2 .   ? -14.765 37.593 -9.221  1.00 27.73 ?  201 A1BBE A N6  1 
HETATM 1142 N N7  . A1BBE B 2 .   ? -15.949 35.292 -7.602  1.00 24.99 ?  201 A1BBE A N7  1 
HETATM 1143 O O01 . A1BBE B 2 .   ? -15.226 33.274 -1.222  1.00 22.39 ?  201 A1BBE A O01 1 
HETATM 1144 O O02 . A1BBE B 2 .   ? -15.648 37.605 -0.440  1.00 23.38 ?  201 A1BBE A O02 1 
HETATM 1145 O O03 . A1BBE B 2 .   ? -13.638 39.027 0.196   1.00 23.36 -1 201 A1BBE A O03 1 
HETATM 1146 O O04 . A1BBE B 2 .   ? -15.945 39.992 0.397   1.00 23.80 -1 201 A1BBE A O04 1 
HETATM 1147 O O05 . A1BBE B 2 .   ? -14.928 39.585 -1.865  1.00 24.43 ?  201 A1BBE A O05 1 
HETATM 1148 P P01 . A1BBE B 2 .   ? -15.018 39.133 -0.423  1.00 22.89 ?  201 A1BBE A P01 1 
HETATM 1149 O O   . HOH   C 3 .   ? -8.452  44.347 -7.730  1.00 49.15 ?  301 HOH   A O   1 
HETATM 1150 O O   . HOH   C 3 .   ? -18.138 49.554 -3.114  1.00 34.39 ?  302 HOH   A O   1 
HETATM 1151 O O   . HOH   C 3 .   ? -7.206  33.597 3.805   1.00 28.90 ?  303 HOH   A O   1 
HETATM 1152 O O   . HOH   C 3 .   ? -8.935  37.796 13.211  1.00 27.85 ?  304 HOH   A O   1 
HETATM 1153 O O   . HOH   C 3 .   ? -10.170 32.738 -14.546 1.00 38.96 ?  305 HOH   A O   1 
HETATM 1154 O O   . HOH   C 3 .   ? -9.111  41.447 4.970   1.00 30.55 ?  306 HOH   A O   1 
HETATM 1155 O O   . HOH   C 3 .   ? -23.705 43.405 -15.230 1.00 28.06 ?  307 HOH   A O   1 
HETATM 1156 O O   . HOH   C 3 .   ? -27.130 14.817 -7.545  1.00 47.47 ?  308 HOH   A O   1 
HETATM 1157 O O   . HOH   C 3 .   ? -6.401  38.828 15.719  1.00 44.95 ?  309 HOH   A O   1 
HETATM 1158 O O   . HOH   C 3 .   ? -31.233 36.173 -3.240  1.00 37.17 ?  310 HOH   A O   1 
HETATM 1159 O O   . HOH   C 3 .   ? -17.239 39.678 -3.185  1.00 25.14 ?  311 HOH   A O   1 
HETATM 1160 O O   . HOH   C 3 .   ? -27.600 31.422 -13.907 1.00 27.92 ?  312 HOH   A O   1 
HETATM 1161 O O   . HOH   C 3 .   ? -12.035 34.884 -12.457 1.00 29.39 ?  313 HOH   A O   1 
HETATM 1162 O O   . HOH   C 3 .   ? -16.404 17.975 -13.020 1.00 53.03 ?  314 HOH   A O   1 
HETATM 1163 O O   . HOH   C 3 .   ? -31.769 35.339 -9.130  1.00 42.91 ?  315 HOH   A O   1 
HETATM 1164 O O   . HOH   C 3 .   ? -4.092  36.121 5.544   1.00 35.67 ?  316 HOH   A O   1 
HETATM 1165 O O   . HOH   C 3 .   ? -9.428  35.564 10.032  1.00 29.94 ?  317 HOH   A O   1 
HETATM 1166 O O   . HOH   C 3 .   ? -10.190 31.798 -11.335 1.00 32.63 ?  318 HOH   A O   1 
HETATM 1167 O O   . HOH   C 3 .   ? -6.484  34.687 -14.283 1.00 36.81 ?  319 HOH   A O   1 
HETATM 1168 O O   . HOH   C 3 .   ? -14.828 41.583 2.330   1.00 23.03 ?  320 HOH   A O   1 
HETATM 1169 O O   . HOH   C 3 .   ? -20.864 17.778 -9.507  1.00 39.97 ?  321 HOH   A O   1 
HETATM 1170 O O   . HOH   C 3 .   ? -16.191 47.116 -16.209 1.00 37.41 ?  322 HOH   A O   1 
HETATM 1171 O O   . HOH   C 3 .   ? -29.158 30.469 3.693   1.00 25.39 ?  323 HOH   A O   1 
HETATM 1172 O O   . HOH   C 3 .   ? -17.153 19.363 8.184   1.00 37.20 ?  324 HOH   A O   1 
HETATM 1173 O O   . HOH   C 3 .   ? -16.092 28.710 -11.698 1.00 31.34 ?  325 HOH   A O   1 
HETATM 1174 O O   . HOH   C 3 .   ? -0.716  27.984 -5.974  1.00 42.81 ?  326 HOH   A O   1 
HETATM 1175 O O   . HOH   C 3 .   ? -8.268  36.141 -3.767  1.00 27.91 ?  327 HOH   A O   1 
HETATM 1176 O O   . HOH   C 3 .   ? -2.019  38.352 -4.237  1.00 41.19 ?  328 HOH   A O   1 
HETATM 1177 O O   . HOH   C 3 .   ? -13.852 25.595 17.128  1.00 38.18 ?  329 HOH   A O   1 
HETATM 1178 O O   . HOH   C 3 .   ? -23.572 19.546 2.558   1.00 28.22 ?  330 HOH   A O   1 
HETATM 1179 O O   . HOH   C 3 .   ? -11.351 24.818 15.920  1.00 35.03 ?  331 HOH   A O   1 
HETATM 1180 O O   . HOH   C 3 .   ? -10.678 34.481 3.606   1.00 25.74 ?  332 HOH   A O   1 
HETATM 1181 O O   . HOH   C 3 .   ? -0.183  28.449 10.671  1.00 45.77 ?  333 HOH   A O   1 
HETATM 1182 O O   . HOH   C 3 .   ? -13.751 41.554 -7.002  1.00 30.58 ?  334 HOH   A O   1 
HETATM 1183 O O   . HOH   C 3 .   ? -10.496 22.744 -13.675 1.00 42.82 ?  335 HOH   A O   1 
HETATM 1184 O O   . HOH   C 3 .   ? -10.574 31.746 17.545  1.00 31.22 ?  336 HOH   A O   1 
HETATM 1185 O O   . HOH   C 3 .   ? -6.640  43.363 2.779   1.00 35.45 ?  337 HOH   A O   1 
HETATM 1186 O O   . HOH   C 3 .   ? -6.531  36.705 0.543   1.00 28.63 ?  338 HOH   A O   1 
HETATM 1187 O O   . HOH   C 3 .   ? -20.785 12.000 -6.716  0.50 32.37 ?  339 HOH   A O   1 
HETATM 1188 O O   . HOH   C 3 .   ? -0.918  35.211 -2.752  1.00 39.51 ?  340 HOH   A O   1 
HETATM 1189 O O   . HOH   C 3 .   ? -13.638 31.572 -4.195  1.00 28.95 ?  341 HOH   A O   1 
HETATM 1190 O O   . HOH   C 3 .   ? -11.555 32.956 -3.371  1.00 26.64 ?  342 HOH   A O   1 
HETATM 1191 O O   . HOH   C 3 .   ? -29.700 32.289 -6.154  1.00 31.77 ?  343 HOH   A O   1 
HETATM 1192 O O   . HOH   C 3 .   ? -22.298 16.215 1.853   1.00 34.96 ?  344 HOH   A O   1 
HETATM 1193 O O   . HOH   C 3 .   ? -23.831 23.320 9.004   1.00 37.23 ?  345 HOH   A O   1 
HETATM 1194 O O   . HOH   C 3 .   ? -14.437 32.293 -6.720  1.00 26.68 ?  346 HOH   A O   1 
HETATM 1195 O O   . HOH   C 3 .   ? -5.808  26.027 -8.992  1.00 41.43 ?  347 HOH   A O   1 
HETATM 1196 O O   . HOH   C 3 .   ? -14.074 36.482 -11.834 1.00 30.46 ?  348 HOH   A O   1 
HETATM 1197 O O   . HOH   C 3 .   ? -12.618 29.036 -5.965  1.00 35.24 ?  349 HOH   A O   1 
HETATM 1198 O O   . HOH   C 3 .   ? -7.635  22.719 14.872  1.00 45.53 ?  350 HOH   A O   1 
HETATM 1199 O O   . HOH   C 3 .   ? -13.306 21.701 -10.833 1.00 37.17 ?  351 HOH   A O   1 
HETATM 1200 O O   . HOH   C 3 .   ? -23.199 25.916 13.252  1.00 37.09 ?  352 HOH   A O   1 
HETATM 1201 O O   . HOH   C 3 .   ? -11.042 36.549 11.960  1.00 25.34 ?  353 HOH   A O   1 
HETATM 1202 O O   . HOH   C 3 .   ? 1.189   15.187 -3.101  1.00 63.82 ?  354 HOH   A O   1 
HETATM 1203 O O   . HOH   C 3 .   ? -5.160  42.845 -1.727  1.00 35.12 ?  355 HOH   A O   1 
HETATM 1204 O O   . HOH   C 3 .   ? -12.306 18.636 -10.640 1.00 43.86 ?  356 HOH   A O   1 
HETATM 1205 O O   . HOH   C 3 .   ? -32.146 39.843 -8.878  1.00 36.12 ?  357 HOH   A O   1 
HETATM 1206 O O   . HOH   C 3 .   ? -6.861  33.189 -8.438  1.00 39.49 ?  358 HOH   A O   1 
HETATM 1207 O O   . HOH   C 3 .   ? -0.673  32.810 -0.819  1.00 39.19 ?  359 HOH   A O   1 
HETATM 1208 O O   . HOH   C 3 .   ? -9.292  33.953 -4.984  1.00 28.87 ?  360 HOH   A O   1 
HETATM 1209 O O   . HOH   C 3 .   ? -30.710 36.178 -0.565  1.00 38.15 ?  361 HOH   A O   1 
HETATM 1210 O O   . HOH   C 3 .   ? -32.283 31.217 2.516   1.00 39.89 ?  362 HOH   A O   1 
HETATM 1211 O O   . HOH   C 3 .   ? -23.365 14.787 -12.727 1.00 39.99 ?  363 HOH   A O   1 
HETATM 1212 O O   . HOH   C 3 .   ? -13.875 21.724 14.600  1.00 32.44 ?  364 HOH   A O   1 
HETATM 1213 O O   . HOH   C 3 .   ? -25.632 44.894 -9.183  1.00 31.56 ?  365 HOH   A O   1 
HETATM 1214 O O   . HOH   C 3 .   ? 1.440   28.771 8.267   1.00 53.31 ?  366 HOH   A O   1 
HETATM 1215 O O   . HOH   C 3 .   ? -7.325  32.268 -5.983  1.00 35.57 ?  367 HOH   A O   1 
HETATM 1216 O O   . HOH   C 3 .   ? -22.460 46.113 -9.323  1.00 31.13 ?  368 HOH   A O   1 
HETATM 1217 O O   . HOH   C 3 .   ? -20.906 15.788 -11.532 1.00 41.82 ?  369 HOH   A O   1 
HETATM 1218 O O   . HOH   C 3 .   ? 1.150   28.453 -2.054  1.00 47.10 ?  370 HOH   A O   1 
HETATM 1219 O O   . HOH   C 3 .   ? -11.023 41.985 -6.620  1.00 35.23 ?  371 HOH   A O   1 
HETATM 1220 O O   . HOH   C 3 .   ? -8.647  29.775 -6.119  1.00 38.53 ?  372 HOH   A O   1 
HETATM 1221 O O   . HOH   C 3 .   ? -17.206 52.264 -3.579  1.00 45.97 ?  373 HOH   A O   1 
HETATM 1222 O O   . HOH   C 3 .   ? -31.679 29.120 4.208   1.00 33.68 ?  374 HOH   A O   1 
HETATM 1223 O O   . HOH   C 3 .   ? -32.924 29.087 6.716   0.50 40.65 ?  375 HOH   A O   1 
HETATM 1224 O O   . HOH   C 3 .   ? -8.337  43.282 6.716   0.50 31.96 ?  376 HOH   A O   1 
HETATM 1225 O O   . HOH   C 3 .   ? -32.996 35.524 0.507   1.00 33.99 ?  377 HOH   A O   1 
HETATM 1226 O O   . HOH   C 3 .   ? -7.434  31.368 -10.589 1.00 39.31 ?  378 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 1   ? 0.6182 0.4107 0.3403 -0.1559 -0.0388 -0.0094 18  SER A N   
2    C CA  . SER A 1   ? 0.5721 0.3661 0.3020 -0.1576 -0.0121 -0.0348 18  SER A CA  
3    C C   . SER A 1   ? 0.5962 0.3698 0.3485 -0.1466 -0.0035 -0.0662 18  SER A C   
4    O O   . SER A 1   ? 0.6107 0.3746 0.3871 -0.1313 -0.0197 -0.0676 18  SER A O   
5    C CB  . SER A 1   ? 0.5562 0.3824 0.3174 -0.1465 -0.0041 -0.0331 18  SER A CB  
6    O OG  . SER A 1   ? 0.5429 0.3799 0.3478 -0.1236 -0.0143 -0.0359 18  SER A OG  
7    N N   . MET A 2   ? 0.5933 0.3598 0.3379 -0.1553 0.0217  -0.0917 19  MET A N   
8    C CA  . MET A 2   ? 0.5812 0.3310 0.3527 -0.1427 0.0321  -0.1245 19  MET A CA  
9    C C   . MET A 2   ? 0.5897 0.3632 0.4214 -0.1184 0.0373  -0.1383 19  MET A C   
10   O O   . MET A 2   ? 0.5991 0.3612 0.4660 -0.1016 0.0372  -0.1600 19  MET A O   
11   C CB  . MET A 2   ? 0.6862 0.4215 0.4288 -0.1612 0.0592  -0.1503 19  MET A CB  
12   C CG  . MET A 2   ? 0.7134 0.4259 0.3924 -0.1892 0.0535  -0.1343 19  MET A CG  
13   S SD  . MET A 2   ? 0.7725 0.4447 0.4431 -0.1830 0.0318  -0.1356 19  MET A SD  
14   C CE  . MET A 2   ? 0.8262 0.4876 0.5478 -0.1590 0.0482  -0.1801 19  MET A CE  
15   N N   . ARG A 3   ? 0.5596 0.3644 0.4047 -0.1162 0.0400  -0.1255 20  ARG A N   
16   C CA  . ARG A 3   ? 0.5618 0.3916 0.4608 -0.0958 0.0427  -0.1339 20  ARG A CA  
17   C C   . ARG A 3   ? 0.5261 0.3769 0.4298 -0.0912 0.0253  -0.1049 20  ARG A C   
18   O O   . ARG A 3   ? 0.5225 0.3775 0.3906 -0.1058 0.0220  -0.0836 20  ARG A O   
19   C CB  . ARG A 3   ? 0.5854 0.4330 0.4948 -0.1015 0.0734  -0.1573 20  ARG A CB  
20   C CG  . ARG A 3   ? 0.6419 0.4741 0.5643 -0.0986 0.0917  -0.1925 20  ARG A CG  
21   C CD  . ARG A 3   ? 0.7607 0.6154 0.6981 -0.1042 0.1236  -0.2182 20  ARG A CD  
22   N NE  . ARG A 3   ? 0.7902 0.6614 0.6932 -0.1260 0.1328  -0.2027 20  ARG A NE  
23   C CZ  . ARG A 3   ? 0.7959 0.6968 0.7181 -0.1282 0.1480  -0.2075 20  ARG A CZ  
24   N NH1 . ARG A 3   ? 0.7299 0.6518 0.7082 -0.1089 0.1548  -0.2249 20  ARG A NH1 
25   N NH2 . ARG A 3   ? 0.7326 0.6419 0.6176 -0.1512 0.1547  -0.1932 20  ARG A NH2 
26   N N   . PRO A 4   ? 0.4862 0.3497 0.4332 -0.0716 0.0130  -0.1033 21  PRO A N   
27   C CA  . PRO A 4   ? 0.4671 0.3518 0.4184 -0.0679 -0.0003 -0.0795 21  PRO A CA  
28   C C   . PRO A 4   ? 0.4684 0.3745 0.4131 -0.0763 0.0175  -0.0783 21  PRO A C   
29   O O   . PRO A 4   ? 0.4780 0.3909 0.4341 -0.0791 0.0390  -0.0986 21  PRO A O   
30   C CB  . PRO A 4   ? 0.4553 0.3481 0.4567 -0.0474 -0.0124 -0.0847 21  PRO A CB  
31   C CG  . PRO A 4   ? 0.4709 0.3389 0.4860 -0.0407 -0.0169 -0.1014 21  PRO A CG  
32   C CD  . PRO A 4   ? 0.4503 0.3095 0.4455 -0.0524 0.0098  -0.1229 21  PRO A CD  
33   N N   . ALA A 5   ? 0.4370 0.3535 0.3627 -0.0813 0.0080  -0.0544 22  ALA A N   
34   C CA  . ALA A 5   ? 0.4044 0.3390 0.3258 -0.0878 0.0189  -0.0492 22  ALA A CA  
35   C C   . ALA A 5   ? 0.3927 0.3468 0.3504 -0.0721 0.0124  -0.0469 22  ALA A C   
36   O O   . ALA A 5   ? 0.4210 0.3780 0.3855 -0.0630 -0.0062 -0.0332 22  ALA A O   
37   C CB  . ALA A 5   ? 0.4559 0.3895 0.3392 -0.1010 0.0114  -0.0250 22  ALA A CB  
38   N N   . LEU A 6   ? 0.3329 0.3007 0.3118 -0.0711 0.0277  -0.0603 23  LEU A N   
39   C CA  . LEU A 6   ? 0.3595 0.3450 0.3726 -0.0583 0.0227  -0.0598 23  LEU A CA  
40   C C   . LEU A 6   ? 0.3648 0.3623 0.3679 -0.0662 0.0300  -0.0521 23  LEU A C   
41   O O   . LEU A 6   ? 0.3469 0.3441 0.3334 -0.0806 0.0458  -0.0577 23  LEU A O   
42   C CB  . LEU A 6   ? 0.2991 0.2917 0.3547 -0.0483 0.0316  -0.0827 23  LEU A CB  
43   C CG  . LEU A 6   ? 0.3291 0.3059 0.3970 -0.0412 0.0276  -0.0952 23  LEU A CG  
44   C CD1 . LEU A 6   ? 0.3821 0.3692 0.4980 -0.0300 0.0373  -0.1185 23  LEU A CD1 
45   C CD2 . LEU A 6   ? 0.3733 0.3420 0.4432 -0.0319 0.0007  -0.0781 23  LEU A CD2 
46   N N   . TYR A 7   ? 0.3074 0.3143 0.3198 -0.0580 0.0177  -0.0396 24  TYR A N   
47   C CA  . TYR A 7   ? 0.2809 0.2964 0.2877 -0.0630 0.0215  -0.0325 24  TYR A CA  
48   C C   . TYR A 7   ? 0.2992 0.3283 0.3414 -0.0533 0.0215  -0.0409 24  TYR A C   
49   O O   . TYR A 7   ? 0.3199 0.3526 0.3799 -0.0413 0.0076  -0.0374 24  TYR A O   
50   C CB  . TYR A 7   ? 0.3281 0.3419 0.3145 -0.0617 0.0077  -0.0117 24  TYR A CB  
51   C CG  . TYR A 7   ? 0.3153 0.3323 0.2921 -0.0672 0.0101  -0.0032 24  TYR A CG  
52   C CD1 . TYR A 7   ? 0.2759 0.3015 0.2726 -0.0602 0.0085  -0.0056 24  TYR A CD1 
53   C CD2 . TYR A 7   ? 0.3251 0.3344 0.2728 -0.0797 0.0113  0.0086  24  TYR A CD2 
54   C CE1 . TYR A 7   ? 0.3102 0.3345 0.2980 -0.0650 0.0089  0.0019  24  TYR A CE1 
55   C CE2 . TYR A 7   ? 0.3549 0.3640 0.2961 -0.0844 0.0106  0.0173  24  TYR A CE2 
56   C CZ  . TYR A 7   ? 0.3680 0.3836 0.3292 -0.0765 0.0095  0.0134  24  TYR A CZ  
57   O OH  . TYR A 7   ? 0.3590 0.3705 0.3136 -0.0806 0.0071  0.0219  24  TYR A OH  
58   N N   . PHE A 8   ? 0.2739 0.3113 0.3251 -0.0607 0.0360  -0.0510 25  PHE A N   
59   C CA  . PHE A 8   ? 0.2870 0.3388 0.3716 -0.0540 0.0361  -0.0581 25  PHE A CA  
60   C C   . PHE A 8   ? 0.2880 0.3417 0.3624 -0.0582 0.0327  -0.0472 25  PHE A C   
61   O O   . PHE A 8   ? 0.2825 0.3318 0.3340 -0.0717 0.0406  -0.0432 25  PHE A O   
62   C CB  . PHE A 8   ? 0.2720 0.3361 0.3800 -0.0590 0.0544  -0.0781 25  PHE A CB  
63   C CG  . PHE A 8   ? 0.2734 0.3545 0.4153 -0.0544 0.0537  -0.0829 25  PHE A CG  
64   C CD1 . PHE A 8   ? 0.2651 0.3528 0.4421 -0.0394 0.0411  -0.0852 25  PHE A CD1 
65   C CD2 . PHE A 8   ? 0.2594 0.3484 0.3959 -0.0667 0.0626  -0.0825 25  PHE A CD2 
66   C CE1 . PHE A 8   ? 0.2705 0.3737 0.4776 -0.0366 0.0383  -0.0875 25  PHE A CE1 
67   C CE2 . PHE A 8   ? 0.2729 0.3769 0.4386 -0.0640 0.0602  -0.0853 25  PHE A CE2 
68   C CZ  . PHE A 8   ? 0.2631 0.3749 0.4647 -0.0488 0.0485  -0.0880 25  PHE A CZ  
69   N N   . CYS A 9   ? 0.2306 0.2893 0.3219 -0.0479 0.0204  -0.0429 26  CYS A N   
70   C CA  . CYS A 9   ? 0.2598 0.3181 0.3448 -0.0497 0.0159  -0.0351 26  CYS A CA  
71   C C   . CYS A 9   ? 0.2309 0.3018 0.3450 -0.0500 0.0188  -0.0442 26  CYS A C   
72   O O   . CYS A 9   ? 0.2376 0.3178 0.3809 -0.0414 0.0138  -0.0507 26  CYS A O   
73   C CB  . CYS A 9   ? 0.2361 0.2902 0.3142 -0.0394 -0.0004 -0.0237 26  CYS A CB  
74   S SG  . CYS A 9   ? 0.2728 0.3186 0.3254 -0.0365 -0.0074 -0.0124 26  CYS A SG  
75   N N   . GLY A 10  ? 0.2182 0.2888 0.3247 -0.0607 0.0247  -0.0431 27  GLY A N   
76   C CA  . GLY A 10  ? 0.2438 0.3256 0.3736 -0.0630 0.0251  -0.0485 27  GLY A CA  
77   C C   . GLY A 10  ? 0.2604 0.3332 0.3699 -0.0748 0.0258  -0.0416 27  GLY A C   
78   O O   . GLY A 10  ? 0.2744 0.3376 0.3584 -0.0855 0.0315  -0.0367 27  GLY A O   
79   N N   . SER A 11  ? 0.2217 0.2958 0.3419 -0.0744 0.0185  -0.0405 28  SER A N   
80   C CA  . SER A 11  ? 0.2373 0.2978 0.3380 -0.0843 0.0154  -0.0332 28  SER A CA  
81   C C   . SER A 11  ? 0.2725 0.3351 0.3619 -0.1038 0.0282  -0.0344 28  SER A C   
82   O O   . SER A 11  ? 0.2646 0.3465 0.3720 -0.1117 0.0409  -0.0449 28  SER A O   
83   C CB  . SER A 11  ? 0.2286 0.2922 0.3454 -0.0836 0.0071  -0.0346 28  SER A CB  
84   O OG  . SER A 11  ? 0.2472 0.2965 0.3473 -0.0949 0.0040  -0.0290 28  SER A OG  
85   N N   . ILE A 12  ? 0.2644 0.3075 0.3245 -0.1124 0.0246  -0.0236 29  ILE A N   
86   C CA  . ILE A 12  ? 0.2732 0.3142 0.3168 -0.1352 0.0326  -0.0212 29  ILE A CA  
87   C C   . ILE A 12  ? 0.3197 0.3417 0.3502 -0.1428 0.0209  -0.0114 29  ILE A C   
88   O O   . ILE A 12  ? 0.3154 0.3441 0.3553 -0.1537 0.0220  -0.0145 29  ILE A O   
89   C CB  . ILE A 12  ? 0.3018 0.3344 0.3198 -0.1427 0.0374  -0.0155 29  ILE A CB  
90   C CG1 . ILE A 12  ? 0.2986 0.3470 0.3284 -0.1358 0.0489  -0.0267 29  ILE A CG1 
91   C CG2 . ILE A 12  ? 0.3164 0.3451 0.3127 -0.1704 0.0437  -0.0109 29  ILE A CG2 
92   C CD1 . ILE A 12  ? 0.2771 0.3160 0.2799 -0.1432 0.0526  -0.0212 29  ILE A CD1 
93   N N   . ARG A 13  ? 0.3051 0.3031 0.3163 -0.1365 0.0086  0.0002  30  ARG A N   
94   C CA  . ARG A 13  ? 0.3148 0.2908 0.3160 -0.1414 -0.0042 0.0082  30  ARG A CA  
95   C C   . ARG A 13  ? 0.3049 0.2804 0.3226 -0.1282 -0.0117 0.0023  30  ARG A C   
96   O O   . ARG A 13  ? 0.3516 0.3130 0.3651 -0.1360 -0.0197 0.0049  30  ARG A O   
97   C CB  . ARG A 13  ? 0.3489 0.2998 0.3299 -0.1368 -0.0157 0.0213  30  ARG A CB  
98   C CG  . ARG A 13  ? 0.3806 0.3299 0.3420 -0.1543 -0.0109 0.0297  30  ARG A CG  
99   C CD  . ARG A 13  ? 0.4129 0.3345 0.3550 -0.1592 -0.0257 0.0461  30  ARG A CD  
100  N NE  . ARG A 13  ? 0.4389 0.3604 0.3609 -0.1773 -0.0219 0.0551  30  ARG A NE  
101  C CZ  . ARG A 13  ? 0.4718 0.3749 0.3789 -0.1797 -0.0339 0.0708  30  ARG A CZ  
102  N NH1 . ARG A 13  ? 0.4333 0.3184 0.3471 -0.1617 -0.0492 0.0779  30  ARG A NH1 
103  N NH2 . ARG A 13  ? 0.4576 0.3651 0.3459 -0.1936 -0.0303 0.0760  30  ARG A NH2 
104  N N   . GLY A 14  ? 0.2916 0.2813 0.3263 -0.1110 -0.0102 -0.0052 31  GLY A N   
105  C CA  . GLY A 14  ? 0.2795 0.2720 0.3293 -0.1030 -0.0167 -0.0109 31  GLY A CA  
106  C C   . GLY A 14  ? 0.3245 0.3334 0.3918 -0.1167 -0.0119 -0.0164 31  GLY A C   
107  O O   . GLY A 14  ? 0.3488 0.3556 0.4243 -0.1161 -0.0197 -0.0185 31  GLY A O   
108  N N   . GLY A 15  ? 0.3116 0.3375 0.3838 -0.1307 0.0010  -0.0191 32  GLY A N   
109  C CA  . GLY A 15  ? 0.2837 0.3323 0.3775 -0.1437 0.0081  -0.0257 32  GLY A CA  
110  C C   . GLY A 15  ? 0.3134 0.3907 0.4281 -0.1435 0.0243  -0.0359 32  GLY A C   
111  O O   . GLY A 15  ? 0.3008 0.3815 0.4227 -0.1276 0.0254  -0.0394 32  GLY A O   
112  N N   . ARG A 16  ? 0.3477 0.4457 0.4721 -0.1618 0.0373  -0.0416 33  ARG A N   
113  C CA  . ARG A 16  ? 0.3330 0.4576 0.4753 -0.1640 0.0559  -0.0540 33  ARG A CA  
114  C C   . ARG A 16  ? 0.3314 0.4884 0.5197 -0.1587 0.0614  -0.0660 33  ARG A C   
115  O O   . ARG A 16  ? 0.3401 0.5236 0.5495 -0.1629 0.0790  -0.0791 33  ARG A O   
116  C CB  . ARG A 16  ? 0.4036 0.5320 0.5237 -0.1901 0.0693  -0.0537 33  ARG A CB  
117  C CG  . ARG A 16  ? 0.5164 0.6107 0.5940 -0.2004 0.0574  -0.0373 33  ARG A CG  
118  C CD  . ARG A 16  ? 0.5847 0.6737 0.6340 -0.2118 0.0671  -0.0354 33  ARG A CD  
119  N NE  . ARG A 16  ? 0.5227 0.6230 0.5835 -0.2001 0.0780  -0.0459 33  ARG A NE  
120  C CZ  . ARG A 16  ? 0.4988 0.5985 0.5394 -0.2058 0.0887  -0.0488 33  ARG A CZ  
121  N NH1 . ARG A 16  ? 0.5647 0.6560 0.5736 -0.2227 0.0899  -0.0426 33  ARG A NH1 
122  N NH2 . ARG A 16  ? 0.3691 0.4761 0.4209 -0.1947 0.0970  -0.0585 33  ARG A NH2 
123  N N   . GLU A 17  ? 0.3066 0.4620 0.5114 -0.1502 0.0465  -0.0621 34  GLU A N   
124  C CA  . GLU A 17  ? 0.2950 0.4808 0.5459 -0.1466 0.0476  -0.0702 34  GLU A CA  
125  C C   . GLU A 17  ? 0.2726 0.4802 0.5580 -0.1318 0.0574  -0.0833 34  GLU A C   
126  O O   . GLU A 17  ? 0.2659 0.5035 0.5877 -0.1326 0.0672  -0.0933 34  GLU A O   
127  C CB  . GLU A 17  ? 0.3211 0.4951 0.5775 -0.1383 0.0266  -0.0620 34  GLU A CB  
128  C CG  . GLU A 17  ? 0.3487 0.5011 0.5758 -0.1533 0.0166  -0.0515 34  GLU A CG  
129  C CD  . GLU A 17  ? 0.3220 0.4358 0.5097 -0.1457 0.0045  -0.0425 34  GLU A CD  
130  O OE1 . GLU A 17  ? 0.3301 0.4342 0.5020 -0.1374 0.0093  -0.0425 34  GLU A OE1 
131  O OE2 . GLU A 17  ? 0.4096 0.5032 0.5826 -0.1488 -0.0094 -0.0359 34  GLU A OE2 
132  N N   . ASP A 18  ? 0.2568 0.4472 0.5294 -0.1164 0.0535  -0.0823 35  ASP A N   
133  C CA  . ASP A 18  ? 0.2404 0.4448 0.5438 -0.1011 0.0588  -0.0935 35  ASP A CA  
134  C C   . ASP A 18  ? 0.2465 0.4523 0.5359 -0.1056 0.0782  -0.1034 35  ASP A C   
135  O O   . ASP A 18  ? 0.2365 0.4442 0.5412 -0.0922 0.0810  -0.1117 35  ASP A O   
136  C CB  . ASP A 18  ? 0.2257 0.4113 0.5259 -0.0824 0.0398  -0.0857 35  ASP A CB  
137  C CG  . ASP A 18  ? 0.2303 0.4215 0.5562 -0.0768 0.0217  -0.0802 35  ASP A CG  
138  O OD1 . ASP A 18  ? 0.2538 0.4678 0.6107 -0.0838 0.0241  -0.0841 35  ASP A OD1 
139  O OD2 . ASP A 18  ? 0.2357 0.4096 0.5500 -0.0667 0.0049  -0.0716 35  ASP A OD2 
140  N N   . ARG A 19  ? 0.3196 0.4621 0.5186 -0.1131 0.1455  -0.0718 36  ARG A N   
141  C CA  . ARG A 19  ? 0.3380 0.4550 0.4864 -0.1050 0.1548  -0.0574 36  ARG A CA  
142  C C   . ARG A 19  ? 0.3287 0.4821 0.4967 -0.0972 0.1625  -0.0735 36  ARG A C   
143  O O   . ARG A 19  ? 0.3611 0.5047 0.4963 -0.0812 0.1531  -0.0683 36  ARG A O   
144  C CB  . ARG A 19  ? 0.4252 0.4981 0.5341 -0.1255 0.1836  -0.0416 36  ARG A CB  
145  C CG  . ARG A 19  ? 0.5282 0.5680 0.5711 -0.1221 0.1917  -0.0258 36  ARG A CG  
146  C CD  . ARG A 19  ? 0.5986 0.5777 0.5855 -0.1423 0.2102  -0.0025 36  ARG A CD  
147  N NE  . ARG A 19  ? 0.6681 0.6222 0.5910 -0.1521 0.2309  0.0055  36  ARG A NE  
148  C CZ  . ARG A 19  ? 0.7249 0.6223 0.5840 -0.1761 0.2530  0.0255  36  ARG A CZ  
149  N NH1 . ARG A 19  ? 0.8429 0.7009 0.6991 -0.1911 0.2572  0.0403  36  ARG A NH1 
150  N NH2 . ARG A 19  ? 0.8371 0.7114 0.6285 -0.1878 0.2724  0.0300  36  ARG A NH2 
151  N N   . THR A 20  ? 0.3139 0.5106 0.5416 -0.1081 0.1798  -0.0961 37  THR A N   
152  C CA  . THR A 20  ? 0.3272 0.5602 0.5862 -0.0990 0.1905  -0.1163 37  THR A CA  
153  C C   . THR A 20  ? 0.3030 0.5548 0.5820 -0.0706 0.1512  -0.1216 37  THR A C   
154  O O   . THR A 20  ? 0.3401 0.5937 0.6103 -0.0552 0.1512  -0.1273 37  THR A O   
155  C CB  . THR A 20  ? 0.3231 0.5941 0.6460 -0.1125 0.2088  -0.1394 37  THR A CB  
156  O OG1 . THR A 20  ? 0.3748 0.6132 0.6633 -0.1393 0.2411  -0.1305 37  THR A OG1 
157  C CG2 . THR A 20  ? 0.3396 0.6384 0.6934 -0.0995 0.2171  -0.1606 37  THR A CG2 
158  N N   . LEU A 21  ? 0.2735 0.5339 0.5736 -0.0661 0.1184  -0.1202 38  LEU A N   
159  C CA  . LEU A 21  ? 0.2638 0.5288 0.5671 -0.0437 0.0795  -0.1203 38  LEU A CA  
160  C C   . LEU A 21  ? 0.2716 0.4951 0.5076 -0.0324 0.0708  -0.1015 38  LEU A C   
161  O O   . LEU A 21  ? 0.3010 0.5227 0.5317 -0.0147 0.0539  -0.1035 38  LEU A O   
162  C CB  . LEU A 21  ? 0.2612 0.5335 0.5810 -0.0489 0.0495  -0.1208 38  LEU A CB  
163  C CG  . LEU A 21  ? 0.2992 0.5595 0.5984 -0.0334 0.0088  -0.1145 38  LEU A CG  
164  C CD1 . LEU A 21  ? 0.3003 0.5853 0.6420 -0.0130 -0.0095 -0.1267 38  LEU A CD1 
165  C CD2 . LEU A 21  ? 0.3203 0.5797 0.6177 -0.0465 -0.0146 -0.1151 38  LEU A CD2 
166  N N   . TYR A 22  ? 0.3013 0.4905 0.4903 -0.0421 0.0798  -0.0843 39  TYR A N   
167  C CA  . TYR A 22  ? 0.2818 0.4377 0.4169 -0.0321 0.0697  -0.0690 39  TYR A CA  
168  C C   . TYR A 22  ? 0.3300 0.4807 0.4428 -0.0248 0.0831  -0.0718 39  TYR A C   
169  O O   . TYR A 22  ? 0.3443 0.4832 0.4333 -0.0118 0.0675  -0.0696 39  TYR A O   
170  C CB  . TYR A 22  ? 0.3055 0.4279 0.4063 -0.0414 0.0758  -0.0520 39  TYR A CB  
171  C CG  . TYR A 22  ? 0.2666 0.3869 0.3849 -0.0502 0.0680  -0.0521 39  TYR A CG  
172  C CD1 . TYR A 22  ? 0.2653 0.4060 0.4083 -0.0501 0.0490  -0.0633 39  TYR A CD1 
173  C CD2 . TYR A 22  ? 0.2750 0.3668 0.3801 -0.0597 0.0791  -0.0413 39  TYR A CD2 
174  C CE1 . TYR A 22  ? 0.2655 0.4015 0.4174 -0.0621 0.0457  -0.0671 39  TYR A CE1 
175  C CE2 . TYR A 22  ? 0.2834 0.3704 0.4067 -0.0683 0.0759  -0.0455 39  TYR A CE2 
176  C CZ  . TYR A 22  ? 0.2811 0.3920 0.4266 -0.0707 0.0613  -0.0602 39  TYR A CZ  
177  O OH  . TYR A 22  ? 0.2359 0.3389 0.3927 -0.0826 0.0616  -0.0677 39  TYR A OH  
178  N N   . GLU A 23  ? 0.3461 0.5025 0.4621 -0.0368 0.1153  -0.0783 40  GLU A N   
179  C CA  . GLU A 23  ? 0.3606 0.5116 0.4514 -0.0341 0.1341  -0.0860 40  GLU A CA  
180  C C   . GLU A 23  ? 0.3728 0.5528 0.5081 -0.0154 0.1232  -0.1072 40  GLU A C   
181  O O   . GLU A 23  ? 0.3488 0.5150 0.4570 -0.0048 0.1209  -0.1112 40  GLU A O   
182  C CB  . GLU A 23  ? 0.3801 0.5335 0.4678 -0.0563 0.1771  -0.0933 40  GLU A CB  
183  C CG  . GLU A 23  ? 0.4762 0.5825 0.4988 -0.0752 0.1884  -0.0681 40  GLU A CG  
184  C CD  . GLU A 23  ? 0.5374 0.6415 0.5566 -0.1039 0.2335  -0.0742 40  GLU A CD  
185  O OE1 . GLU A 23  ? 0.6168 0.6877 0.6084 -0.1214 0.2404  -0.0552 40  GLU A OE1 
186  O OE2 . GLU A 23  ? 0.6518 0.7850 0.6972 -0.1105 0.2645  -0.0995 40  GLU A OE2 
187  N N   . ARG A 24  ? 0.3061 0.5234 0.5108 -0.0107 0.1135  -0.1212 41  ARG A N   
188  C CA  . ARG A 24  ? 0.2983 0.5380 0.5513 0.0108  0.0940  -0.1387 41  ARG A CA  
189  C C   . ARG A 24  ? 0.3284 0.5378 0.5445 0.0255  0.0572  -0.1240 41  ARG A C   
190  O O   . ARG A 24  ? 0.3316 0.5320 0.5465 0.0415  0.0491  -0.1319 41  ARG A O   
191  C CB  . ARG A 24  ? 0.3263 0.6094 0.6591 0.0119  0.0814  -0.1530 41  ARG A CB  
192  C CG  . ARG A 24  ? 0.3587 0.6641 0.7514 0.0368  0.0524  -0.1694 41  ARG A CG  
193  C CD  . ARG A 24  ? 0.3751 0.7163 0.8331 0.0364  0.0254  -0.1763 41  ARG A CD  
194  N NE  . ARG A 24  ? 0.4190 0.7646 0.9155 0.0621  -0.0196 -0.1812 41  ARG A NE  
195  C CZ  . ARG A 24  ? 0.4466 0.8077 0.9850 0.0654  -0.0519 -0.1842 41  ARG A CZ  
196  N NH1 . ARG A 24  ? 0.4146 0.7969 0.9706 0.0452  -0.0451 -0.1866 41  ARG A NH1 
197  N NH2 . ARG A 24  ? 0.4906 0.8371 1.0444 0.0883  -0.0930 -0.1827 41  ARG A NH2 
198  N N   . ILE A 25  ? 0.2939 0.4855 0.4805 0.0183  0.0381  -0.1049 42  ILE A N   
199  C CA  . ILE A 25  ? 0.2986 0.4619 0.4493 0.0261  0.0091  -0.0930 42  ILE A CA  
200  C C   . ILE A 25  ? 0.3339 0.4695 0.4338 0.0281  0.0178  -0.0876 42  ILE A C   
201  O O   . ILE A 25  ? 0.3571 0.4758 0.4430 0.0387  0.0029  -0.0894 42  ILE A O   
202  C CB  . ILE A 25  ? 0.3074 0.4612 0.4407 0.0138  -0.0048 -0.0796 42  ILE A CB  
203  C CG1 . ILE A 25  ? 0.3400 0.5160 0.5143 0.0114  -0.0227 -0.0862 42  ILE A CG1 
204  C CG2 . ILE A 25  ? 0.3300 0.4537 0.4211 0.0156  -0.0244 -0.0694 42  ILE A CG2 
205  C CD1 . ILE A 25  ? 0.3027 0.4687 0.4567 -0.0048 -0.0302 -0.0782 42  ILE A CD1 
206  N N   . VAL A 26  ? 0.3375 0.4644 0.4070 0.0169  0.0397  -0.0807 43  VAL A N   
207  C CA  . VAL A 26  ? 0.3824 0.4824 0.3993 0.0172  0.0418  -0.0749 43  VAL A CA  
208  C C   . VAL A 26  ? 0.4173 0.5178 0.4332 0.0252  0.0545  -0.0928 43  VAL A C   
209  O O   . VAL A 26  ? 0.4213 0.5014 0.4066 0.0307  0.0445  -0.0945 43  VAL A O   
210  C CB  . VAL A 26  ? 0.3910 0.4750 0.3710 0.0038  0.0565  -0.0608 43  VAL A CB  
211  C CG1 . VAL A 26  ? 0.4478 0.5059 0.3711 0.0026  0.0592  -0.0579 43  VAL A CG1 
212  C CG2 . VAL A 26  ? 0.3535 0.4293 0.3334 0.0004  0.0396  -0.0453 43  VAL A CG2 
213  N N   . SER A 27  ? 0.3918 0.5172 0.4462 0.0247  0.0786  -0.1104 44  SER A N   
214  C CA  . SER A 27  ? 0.3972 0.5269 0.4630 0.0333  0.0953  -0.1344 44  SER A CA  
215  C C   . SER A 27  ? 0.4115 0.5341 0.5003 0.0538  0.0664  -0.1411 44  SER A C   
216  O O   . SER A 27  ? 0.4697 0.5733 0.5378 0.0605  0.0694  -0.1530 44  SER A O   
217  C CB  A SER A 27  ? 0.3951 0.5626 0.5204 0.0299  0.1264  -0.1572 44  SER A CB  
218  C CB  B SER A 27  ? 0.3955 0.5628 0.5199 0.0295  0.1268  -0.1569 44  SER A CB  
219  O OG  A SER A 27  ? 0.4391 0.6006 0.5257 0.0069  0.1640  -0.1563 44  SER A OG  
220  O OG  B SER A 27  ? 0.3999 0.5754 0.5482 0.0394  0.1461  -0.1863 44  SER A OG  
221  N N   . ARG A 28  ? 0.4120 0.5437 0.5376 0.0620  0.0376  -0.1336 45  ARG A N   
222  C CA  . ARG A 28  ? 0.4255 0.5388 0.5624 0.0790  0.0070  -0.1351 45  ARG A CA  
223  C C   . ARG A 28  ? 0.4340 0.5087 0.5089 0.0727  -0.0095 -0.1184 45  ARG A C   
224  O O   . ARG A 28  ? 0.4541 0.5021 0.5169 0.0817  -0.0208 -0.1239 45  ARG A O   
225  C CB  . ARG A 28  ? 0.4245 0.5530 0.6083 0.0864  -0.0221 -0.1304 45  ARG A CB  
226  C CG  . ARG A 28  ? 0.4990 0.5980 0.6870 0.1030  -0.0591 -0.1271 45  ARG A CG  
227  C CD  . ARG A 28  ? 0.5620 0.6520 0.7746 0.1222  -0.0511 -0.1492 45  ARG A CD  
228  N NE  . ARG A 28  ? 0.5826 0.7144 0.8786 0.1377  -0.0407 -0.1747 45  ARG A NE  
229  C CZ  . ARG A 28  ? 0.5613 0.6948 0.9197 0.1628  -0.0681 -0.1862 45  ARG A CZ  
230  N NH1 . ARG A 28  ? 0.6081 0.6946 0.9443 0.1744  -0.1091 -0.1707 45  ARG A NH1 
231  N NH2 . ARG A 28  ? 0.5480 0.7298 0.9953 0.1761  -0.0545 -0.2144 45  ARG A NH2 
232  N N   . LEU A 29  ? 0.4062 0.4781 0.4474 0.0571  -0.0094 -0.1008 46  LEU A N   
233  C CA  . LEU A 29  ? 0.4394 0.4839 0.4340 0.0494  -0.0220 -0.0894 46  LEU A CA  
234  C C   . LEU A 29  ? 0.4612 0.4889 0.4218 0.0496  -0.0117 -0.0988 46  LEU A C   
235  O O   . LEU A 29  ? 0.4880 0.4917 0.4235 0.0477  -0.0253 -0.0981 46  LEU A O   
236  C CB  . LEU A 29  ? 0.4443 0.4951 0.4239 0.0355  -0.0207 -0.0742 46  LEU A CB  
237  C CG  . LEU A 29  ? 0.3986 0.4574 0.3966 0.0296  -0.0326 -0.0660 46  LEU A CG  
238  C CD1 . LEU A 29  ? 0.3643 0.4260 0.3510 0.0175  -0.0272 -0.0560 46  LEU A CD1 
239  C CD2 . LEU A 29  ? 0.3991 0.4356 0.3860 0.0290  -0.0552 -0.0633 46  LEU A CD2 
240  N N   . ARG A 30  ? 0.4435 0.4813 0.3993 0.0485  0.0137  -0.1094 47  ARG A N   
241  C CA  . ARG A 30  ? 0.4965 0.5150 0.4085 0.0448  0.0239  -0.1200 47  ARG A CA  
242  C C   . ARG A 30  ? 0.5207 0.5214 0.4429 0.0568  0.0185  -0.1388 47  ARG A C   
243  O O   . ARG A 30  ? 0.5581 0.5359 0.4404 0.0522  0.0185  -0.1473 47  ARG A O   
244  C CB  . ARG A 30  ? 0.5052 0.5330 0.4016 0.0367  0.0570  -0.1292 47  ARG A CB  
245  C CG  . ARG A 30  ? 0.5526 0.5780 0.4144 0.0219  0.0588  -0.1072 47  ARG A CG  
246  C CD  . ARG A 30  ? 0.6546 0.6716 0.4723 0.0070  0.0897  -0.1115 47  ARG A CD  
247  N NE  . ARG A 30  ? 0.6751 0.7157 0.5337 0.0068  0.1240  -0.1337 47  ARG A NE  
248  C CZ  . ARG A 30  ? 0.6533 0.7117 0.5338 -0.0034 0.1461  -0.1304 47  ARG A CZ  
249  N NH1 . ARG A 30  ? 0.5826 0.6358 0.4538 -0.0110 0.1343  -0.1047 47  ARG A NH1 
250  N NH2 . ARG A 30  ? 0.6493 0.7333 0.5709 -0.0061 0.1813  -0.1566 47  ARG A NH2 
251  N N   . ARG A 31  ? 0.5179 0.5254 0.4928 0.0723  0.0105  -0.1456 48  ARG A N   
252  C CA  . ARG A 31  ? 0.5403 0.5214 0.5268 0.0860  -0.0001 -0.1606 48  ARG A CA  
253  C C   . ARG A 31  ? 0.5935 0.5394 0.5437 0.0786  -0.0260 -0.1465 48  ARG A C   
254  O O   . ARG A 31  ? 0.5776 0.4911 0.5184 0.0835  -0.0321 -0.1582 48  ARG A O   
255  C CB  . ARG A 31  ? 0.5582 0.5501 0.6122 0.1068  -0.0121 -0.1673 48  ARG A CB  
256  C CG  . ARG A 31  ? 0.5618 0.5946 0.6708 0.1147  0.0152  -0.1888 48  ARG A CG  
257  C CD  . ARG A 31  ? 0.6082 0.6457 0.7924 0.1414  -0.0014 -0.2046 48  ARG A CD  
258  N NE  . ARG A 31  ? 0.6530 0.7387 0.9079 0.1491  0.0257  -0.2306 48  ARG A NE  
259  C CZ  . ARG A 31  ? 0.6524 0.7586 0.9939 0.1736  0.0110  -0.2471 48  ARG A CZ  
260  N NH1 . ARG A 31  ? 0.6751 0.7495 1.0344 0.1941  -0.0339 -0.2370 48  ARG A NH1 
261  N NH2 . ARG A 31  ? 0.6172 0.7704 1.0170 0.1703  0.0393  -0.2664 48  ARG A NH2 
262  N N   . PHE A 32  ? 0.5409 0.4419 0.4679 0.0127  -0.0555 -0.0672 49  PHE A N   
263  C CA  . PHE A 32  ? 0.5822 0.4572 0.4974 0.0030  -0.0583 -0.0567 49  PHE A CA  
264  C C   . PHE A 32  ? 0.5525 0.4296 0.4700 -0.0147 -0.0538 -0.0523 49  PHE A C   
265  O O   . PHE A 32  ? 0.5710 0.4292 0.4820 -0.0247 -0.0550 -0.0432 49  PHE A O   
266  C CB  . PHE A 32  ? 0.5619 0.4408 0.4758 0.0051  -0.0591 -0.0476 49  PHE A CB  
267  C CG  . PHE A 32  ? 0.6101 0.4850 0.5203 0.0234  -0.0659 -0.0514 49  PHE A CG  
268  C CD1 . PHE A 32  ? 0.6372 0.4803 0.5325 0.0331  -0.0726 -0.0518 49  PHE A CD1 
269  C CD2 . PHE A 32  ? 0.6089 0.5119 0.5318 0.0312  -0.0664 -0.0553 49  PHE A CD2 
270  C CE1 . PHE A 32  ? 0.6995 0.5397 0.5910 0.0522  -0.0796 -0.0556 49  PHE A CE1 
271  C CE2 . PHE A 32  ? 0.6261 0.5288 0.5478 0.0490  -0.0740 -0.0597 49  PHE A CE2 
272  C CZ  . PHE A 32  ? 0.6606 0.5325 0.5661 0.0604  -0.0805 -0.0597 49  PHE A CZ  
273  N N   . GLY A 33  ? 0.5134 0.4134 0.4402 -0.0186 -0.0486 -0.0576 50  GLY A N   
274  C CA  . GLY A 33  ? 0.5066 0.4105 0.4356 -0.0334 -0.0456 -0.0543 50  GLY A CA  
275  C C   . GLY A 33  ? 0.4904 0.4220 0.4283 -0.0343 -0.0390 -0.0588 50  GLY A C   
276  O O   . GLY A 33  ? 0.4852 0.4331 0.4291 -0.0250 -0.0358 -0.0642 50  GLY A O   
277  N N   . THR A 34  ? 0.4468 0.3837 0.3862 -0.0457 -0.0370 -0.0560 51  THR A N   
278  C CA  . THR A 34  ? 0.4382 0.3979 0.3829 -0.0474 -0.0306 -0.0582 51  THR A CA  
279  C C   . THR A 34  ? 0.4294 0.4069 0.3829 -0.0509 -0.0253 -0.0507 51  THR A C   
280  O O   . THR A 34  ? 0.4334 0.4078 0.3873 -0.0580 -0.0259 -0.0427 51  THR A O   
281  C CB  . THR A 34  ? 0.4775 0.4347 0.4188 -0.0565 -0.0326 -0.0588 51  THR A CB  
282  O OG1 . THR A 34  ? 0.5947 0.5296 0.5269 -0.0551 -0.0403 -0.0656 51  THR A OG1 
283  C CG2 . THR A 34  ? 0.4843 0.4598 0.4255 -0.0540 -0.0268 -0.0625 51  THR A CG2 
284  N N   . VAL A 35  ? 0.4211 0.4170 0.3819 -0.0463 -0.0197 -0.0533 52  VAL A N   
285  C CA  . VAL A 35  ? 0.3471 0.3571 0.3160 -0.0491 -0.0160 -0.0480 52  VAL A CA  
286  C C   . VAL A 35  ? 0.3702 0.3913 0.3401 -0.0557 -0.0105 -0.0454 52  VAL A C   
287  O O   . VAL A 35  ? 0.3801 0.4119 0.3526 -0.0537 -0.0051 -0.0485 52  VAL A O   
288  C CB  . VAL A 35  ? 0.3398 0.3624 0.3191 -0.0417 -0.0145 -0.0522 52  VAL A CB  
289  C CG1 . VAL A 35  ? 0.3395 0.3732 0.3263 -0.0454 -0.0129 -0.0480 52  VAL A CG1 
290  C CG2 . VAL A 35  ? 0.3814 0.3931 0.3585 -0.0326 -0.0211 -0.0553 52  VAL A CG2 
291  N N   . LEU A 36  ? 0.3391 0.3582 0.3065 -0.0629 -0.0113 -0.0390 53  LEU A N   
292  C CA  . LEU A 36  ? 0.3485 0.3761 0.3149 -0.0676 -0.0079 -0.0367 53  LEU A CA  
293  C C   . LEU A 36  ? 0.3530 0.3932 0.3242 -0.0665 -0.0016 -0.0356 53  LEU A C   
294  O O   . LEU A 36  ? 0.3513 0.3971 0.3196 -0.0673 0.0023  -0.0352 53  LEU A O   
295  C CB  . LEU A 36  ? 0.3826 0.4088 0.3485 -0.0744 -0.0099 -0.0299 53  LEU A CB  
296  C CG  . LEU A 36  ? 0.3854 0.3982 0.3492 -0.0786 -0.0156 -0.0294 53  LEU A CG  
297  C CD1 . LEU A 36  ? 0.3756 0.3918 0.3428 -0.0857 -0.0151 -0.0208 53  LEU A CD1 
298  C CD2 . LEU A 36  ? 0.4305 0.4398 0.3905 -0.0796 -0.0192 -0.0359 53  LEU A CD2 
299  N N   . THR A 37  ? 0.3394 0.3828 0.3172 -0.0645 -0.0011 -0.0353 54  THR A N   
300  C CA  . THR A 37  ? 0.3134 0.3659 0.2974 -0.0653 0.0036  -0.0343 54  THR A CA  
301  C C   . THR A 37  ? 0.3170 0.3777 0.3101 -0.0626 0.0080  -0.0389 54  THR A C   
302  O O   . THR A 37  ? 0.3177 0.3854 0.3189 -0.0649 0.0121  -0.0381 54  THR A O   
303  C CB  . THR A 37  ? 0.3212 0.3728 0.3080 -0.0649 0.0002  -0.0326 54  THR A CB  
304  O OG1 . THR A 37  ? 0.3318 0.3789 0.3196 -0.0604 -0.0051 -0.0354 54  THR A OG1 
305  C CG2 . THR A 37  ? 0.3155 0.3633 0.2941 -0.0672 -0.0007 -0.0265 54  THR A CG2 
306  N N   . GLU A 38  ? 0.3289 0.3887 0.3211 -0.0579 0.0074  -0.0438 55  GLU A N   
307  C CA  . GLU A 38  ? 0.3458 0.4165 0.3488 -0.0535 0.0118  -0.0485 55  GLU A CA  
308  C C   . GLU A 38  ? 0.3601 0.4413 0.3677 -0.0567 0.0220  -0.0459 55  GLU A C   
309  O O   . GLU A 38  ? 0.3246 0.4176 0.3481 -0.0583 0.0262  -0.0464 55  GLU A O   
310  C CB  . GLU A 38  ? 0.4111 0.4769 0.4070 -0.0463 0.0105  -0.0541 55  GLU A CB  
311  C CG  . GLU A 38  ? 0.4673 0.5476 0.4735 -0.0401 0.0173  -0.0588 55  GLU A CG  
312  C CD  . GLU A 38  ? 0.5359 0.6104 0.5365 -0.0297 0.0137  -0.0660 55  GLU A CD  
313  O OE1 . GLU A 38  ? 0.5481 0.6048 0.5328 -0.0287 0.0077  -0.0674 55  GLU A OE1 
314  O OE2 . GLU A 38  ? 0.5987 0.6866 0.6118 -0.0224 0.0166  -0.0706 55  GLU A OE2 
315  N N   . HIS A 39  ? 0.3177 0.3947 0.3118 -0.0575 0.0259  -0.0431 56  HIS A N   
316  C CA  . HIS A 39  ? 0.3274 0.4120 0.3212 -0.0583 0.0369  -0.0398 56  HIS A CA  
317  C C   . HIS A 39  ? 0.3170 0.4002 0.3125 -0.0651 0.0403  -0.0328 56  HIS A C   
318  O O   . HIS A 39  ? 0.2995 0.3865 0.2948 -0.0666 0.0501  -0.0284 56  HIS A O   
319  C CB  . HIS A 39  ? 0.3196 0.3995 0.2943 -0.0533 0.0391  -0.0407 56  HIS A CB  
320  C CG  . HIS A 39  ? 0.3602 0.4364 0.3293 -0.0459 0.0342  -0.0486 56  HIS A CG  
321  N ND1 . HIS A 39  ? 0.3903 0.4756 0.3684 -0.0395 0.0382  -0.0536 56  HIS A ND1 
322  C CD2 . HIS A 39  ? 0.3772 0.4408 0.3335 -0.0438 0.0252  -0.0528 56  HIS A CD2 
323  C CE1 . HIS A 39  ? 0.4077 0.4837 0.3760 -0.0324 0.0318  -0.0608 56  HIS A CE1 
324  N NE2 . HIS A 39  ? 0.4172 0.4788 0.3724 -0.0358 0.0235  -0.0604 56  HIS A NE2 
325  N N   . VAL A 40  ? 0.3210 0.3977 0.3168 -0.0684 0.0332  -0.0313 57  VAL A N   
326  C CA  . VAL A 40  ? 0.3305 0.4036 0.3275 -0.0733 0.0353  -0.0260 57  VAL A CA  
327  C C   . VAL A 40  ? 0.3237 0.3996 0.3373 -0.0768 0.0320  -0.0285 57  VAL A C   
328  O O   . VAL A 40  ? 0.3190 0.3890 0.3336 -0.0805 0.0315  -0.0259 57  VAL A O   
329  C CB  . VAL A 40  ? 0.3509 0.4155 0.3340 -0.0726 0.0304  -0.0227 57  VAL A CB  
330  C CG1 . VAL A 40  ? 0.3529 0.4162 0.3211 -0.0695 0.0329  -0.0207 57  VAL A CG1 
331  C CG2 . VAL A 40  ? 0.3171 0.3798 0.3004 -0.0714 0.0215  -0.0256 57  VAL A CG2 
332  N N   . ALA A 41  ? 0.2932 0.3774 0.3194 -0.0748 0.0289  -0.0344 58  ALA A N   
333  C CA  . ALA A 41  ? 0.3239 0.4121 0.3658 -0.0768 0.0230  -0.0384 58  ALA A CA  
334  C C   . ALA A 41  ? 0.3144 0.4107 0.3749 -0.0838 0.0292  -0.0378 58  ALA A C   
335  O O   . ALA A 41  ? 0.3362 0.4315 0.4076 -0.0879 0.0237  -0.0405 58  ALA A O   
336  C CB  . ALA A 41  ? 0.3033 0.3983 0.3521 -0.0707 0.0167  -0.0448 58  ALA A CB  
337  N N   . ALA A 42  ? 0.3103 0.4142 0.3745 -0.0855 0.0408  -0.0344 59  ALA A N   
338  C CA  . ALA A 42  ? 0.3351 0.4498 0.4211 -0.0933 0.0486  -0.0329 59  ALA A CA  
339  C C   . ALA A 42  ? 0.3243 0.4252 0.4067 -0.1015 0.0525  -0.0262 59  ALA A C   
340  O O   . ALA A 42  ? 0.3202 0.4252 0.4230 -0.1105 0.0551  -0.0258 59  ALA A O   
341  C CB  . ALA A 42  ? 0.3394 0.4686 0.4297 -0.0909 0.0616  -0.0306 59  ALA A CB  
342  N N   . ALA A 43  ? 0.3161 0.4009 0.3740 -0.0985 0.0529  -0.0208 60  ALA A N   
343  C CA  . ALA A 43  ? 0.3109 0.3790 0.3612 -0.1034 0.0554  -0.0145 60  ALA A CA  
344  C C   . ALA A 43  ? 0.3244 0.3945 0.3864 -0.1118 0.0685  -0.0076 60  ALA A C   
345  O O   . ALA A 43  ? 0.3521 0.4147 0.4269 -0.1209 0.0686  -0.0063 60  ALA A O   
346  C CB  . ALA A 43  ? 0.3339 0.3925 0.3891 -0.1057 0.0437  -0.0198 60  ALA A CB  
347  N N   . GLU A 44  ? 0.3345 0.4140 0.3914 -0.1087 0.0800  -0.0030 61  GLU A N   
348  C CA  . GLU A 44  ? 0.3433 0.4291 0.4125 -0.1161 0.0952  0.0047  61  GLU A CA  
349  C C   . GLU A 44  ? 0.3630 0.4270 0.4226 -0.1225 0.1009  0.0149  61  GLU A C   
350  O O   . GLU A 44  ? 0.3940 0.4588 0.4710 -0.1333 0.1108  0.0209  61  GLU A O   
351  C CB  . GLU A 44  ? 0.3633 0.4608 0.4208 -0.1081 0.1066  0.0079  61  GLU A CB  
352  C CG  . GLU A 44  ? 0.3706 0.4894 0.4406 -0.1019 0.1031  -0.0018 61  GLU A CG  
353  C CD  . GLU A 44  ? 0.3432 0.4558 0.3918 -0.0909 0.0919  -0.0082 61  GLU A CD  
354  O OE1 . GLU A 44  ? 0.3472 0.4428 0.3784 -0.0899 0.0840  -0.0070 61  GLU A OE1 
355  O OE2 . GLU A 44  ? 0.3716 0.4963 0.4214 -0.0833 0.0913  -0.0145 61  GLU A OE2 
356  N N   . LEU A 45  ? 0.3667 0.4112 0.3997 -0.1159 0.0953  0.0174  62  LEU A N   
357  C CA  . LEU A 45  ? 0.3887 0.4096 0.4095 -0.1195 0.1000  0.0271  62  LEU A CA  
358  C C   . LEU A 45  ? 0.4372 0.4457 0.4756 -0.1297 0.0928  0.0237  62  LEU A C   
359  O O   . LEU A 45  ? 0.4451 0.4321 0.4785 -0.1352 0.0974  0.0316  62  LEU A O   
360  C CB  . LEU A 45  ? 0.4103 0.4169 0.3997 -0.1076 0.0941  0.0291  62  LEU A CB  
361  C CG  . LEU A 45  ? 0.4191 0.4329 0.3868 -0.0970 0.0990  0.0321  62  LEU A CG  
362  C CD1 . LEU A 45  ? 0.4083 0.4108 0.3514 -0.0867 0.0899  0.0323  62  LEU A CD1 
363  C CD2 . LEU A 45  ? 0.4358 0.4458 0.3950 -0.0984 0.1158  0.0443  62  LEU A CD2 
364  N N   . GLY A 46  ? 0.4075 0.4268 0.4640 -0.1314 0.0810  0.0120  63  GLY A N   
365  C CA  . GLY A 46  ? 0.4261 0.4323 0.4946 -0.1384 0.0707  0.0062  63  GLY A CA  
366  C C   . GLY A 46  ? 0.4310 0.4180 0.4752 -0.1287 0.0597  0.0034  63  GLY A C   
367  O O   . GLY A 46  ? 0.4049 0.3854 0.4244 -0.1190 0.0620  0.0088  63  GLY A O   
368  N N   . ALA A 47  ? 0.4190 0.3986 0.4710 -0.1304 0.0469  -0.0060 64  ALA A N   
369  C CA  . ALA A 47  ? 0.4783 0.4410 0.5079 -0.1202 0.0373  -0.0091 64  ALA A CA  
370  C C   . ALA A 47  ? 0.4535 0.3893 0.4642 -0.1186 0.0423  -0.0002 64  ALA A C   
371  O O   . ALA A 47  ? 0.4494 0.3788 0.4364 -0.1068 0.0417  0.0032  64  ALA A O   
372  C CB  . ALA A 47  ? 0.4642 0.4229 0.5036 -0.1213 0.0229  -0.0214 64  ALA A CB  
373  N N   . ARG A 48  ? 0.4870 0.4068 0.5087 -0.1303 0.0472  0.0041  65  ARG A N   
374  C CA  . ARG A 48  ? 0.5029 0.3934 0.5047 -0.1284 0.0527  0.0140  65  ARG A CA  
375  C C   . ARG A 48  ? 0.4992 0.3948 0.4821 -0.1211 0.0646  0.0260  65  ARG A C   
376  O O   . ARG A 48  ? 0.5482 0.4272 0.5054 -0.1101 0.0644  0.0315  65  ARG A O   
377  C CB  . ARG A 48  ? 0.5653 0.4364 0.5840 -0.1445 0.0573  0.0181  65  ARG A CB  
378  C CG  . ARG A 48  ? 0.5992 0.4677 0.6415 -0.1542 0.0445  0.0048  65  ARG A CG  
379  C CD  . ARG A 48  ? 0.6766 0.5646 0.7561 -0.1724 0.0507  0.0050  65  ARG A CD  
380  N NE  . ARG A 48  ? 0.6801 0.6057 0.7709 -0.1688 0.0534  0.0020  65  ARG A NE  
381  C CZ  . ARG A 48  ? 0.5607 0.5048 0.6603 -0.1639 0.0407  -0.0111 65  ARG A CZ  
382  N NH1 . ARG A 48  ? 0.6987 0.6295 0.7954 -0.1609 0.0246  -0.0228 65  ARG A NH1 
383  N NH2 . ARG A 48  ? 0.6079 0.5827 0.7171 -0.1607 0.0442  -0.0126 65  ARG A NH2 
384  N N   . GLY A 49  ? 0.5034 0.4224 0.4976 -0.1254 0.0741  0.0293  66  GLY A N   
385  C CA  . GLY A 49  ? 0.4841 0.4080 0.4583 -0.1174 0.0843  0.0392  66  GLY A CA  
386  C C   . GLY A 49  ? 0.4774 0.4097 0.4317 -0.1023 0.0763  0.0352  66  GLY A C   
387  O O   . GLY A 49  ? 0.4948 0.4183 0.4251 -0.0924 0.0788  0.0423  66  GLY A O   
388  N N   . GLU A 50  ? 0.4282 0.3779 0.3928 -0.1003 0.0665  0.0241  67  GLU A N   
389  C CA  . GLU A 50  ? 0.4301 0.3884 0.3796 -0.0882 0.0593  0.0207  67  GLU A CA  
390  C C   . GLU A 50  ? 0.4584 0.3985 0.3911 -0.0795 0.0530  0.0215  67  GLU A C   
391  O O   . GLU A 50  ? 0.4532 0.3942 0.3679 -0.0688 0.0519  0.0249  67  GLU A O   
392  C CB  . GLU A 50  ? 0.4120 0.3894 0.3758 -0.0887 0.0512  0.0103  67  GLU A CB  
393  C CG  . GLU A 50  ? 0.3738 0.3709 0.3508 -0.0931 0.0563  0.0087  67  GLU A CG  
394  C CD  . GLU A 50  ? 0.3917 0.4039 0.3810 -0.0925 0.0476  -0.0010 67  GLU A CD  
395  O OE1 . GLU A 50  ? 0.3845 0.3916 0.3738 -0.0905 0.0385  -0.0062 67  GLU A OE1 
396  O OE2 . GLU A 50  ? 0.3736 0.4012 0.3698 -0.0927 0.0501  -0.0031 67  GLU A OE2 
397  N N   . GLU A 51  ? 0.4733 0.3972 0.4119 -0.0830 0.0478  0.0174  68  GLU A N   
398  C CA  . GLU A 51  ? 0.5250 0.4288 0.4463 -0.0733 0.0423  0.0177  68  GLU A CA  
399  C C   . GLU A 51  ? 0.5102 0.3957 0.4121 -0.0683 0.0494  0.0292  68  GLU A C   
400  O O   . GLU A 51  ? 0.5930 0.4756 0.4763 -0.0549 0.0465  0.0315  68  GLU A O   
401  C CB  . GLU A 51  ? 0.5340 0.4195 0.4639 -0.0788 0.0356  0.0106  68  GLU A CB  
402  C CG  . GLU A 51  ? 0.5930 0.4648 0.5075 -0.0663 0.0265  0.0052  68  GLU A CG  
403  C CD  . GLU A 51  ? 0.6639 0.5133 0.5847 -0.0717 0.0189  -0.0029 68  GLU A CD  
404  O OE1 . GLU A 51  ? 0.6563 0.4888 0.5874 -0.0844 0.0225  0.0001  68  GLU A OE1 
405  O OE2 . GLU A 51  ? 0.6920 0.5406 0.6075 -0.0635 0.0094  -0.0123 68  GLU A OE2 
406  N N   . ALA A 52  ? 0.5044 0.3793 0.4107 -0.0784 0.0593  0.0372  69  ALA A N   
407  C CA  . ALA A 52  ? 0.5556 0.4096 0.4409 -0.0736 0.0672  0.0499  69  ALA A CA  
408  C C   . ALA A 52  ? 0.5230 0.3929 0.3907 -0.0617 0.0695  0.0545  69  ALA A C   
409  O O   . ALA A 52  ? 0.5422 0.3974 0.3866 -0.0503 0.0702  0.0621  69  ALA A O   
410  C CB  . ALA A 52  ? 0.6030 0.4459 0.4986 -0.0883 0.0796  0.0587  69  ALA A CB  
411  N N   . ALA A 53  ? 0.5029 0.4014 0.3806 -0.0634 0.0695  0.0496  70  ALA A N   
412  C CA  . ALA A 53  ? 0.4815 0.3949 0.3435 -0.0525 0.0689  0.0516  70  ALA A CA  
413  C C   . ALA A 53  ? 0.4691 0.3899 0.3241 -0.0404 0.0574  0.0460  70  ALA A C   
414  O O   . ALA A 53  ? 0.4500 0.3825 0.2928 -0.0307 0.0546  0.0470  70  ALA A O   
415  C CB  . ALA A 53  ? 0.4532 0.3919 0.3275 -0.0578 0.0715  0.0470  70  ALA A CB  
416  N N   . GLY A 54  ? 0.4474 0.3628 0.3099 -0.0402 0.0507  0.0399  71  GLY A N   
417  C CA  . GLY A 54  ? 0.4743 0.3999 0.3322 -0.0286 0.0418  0.0352  71  GLY A CA  
418  C C   . GLY A 54  ? 0.4701 0.4253 0.3397 -0.0297 0.0375  0.0287  71  GLY A C   
419  O O   . GLY A 54  ? 0.4382 0.4076 0.3037 -0.0205 0.0322  0.0275  71  GLY A O   
420  N N   . GLY A 55  ? 0.4181 0.3830 0.3033 -0.0408 0.0395  0.0246  72  GLY A N   
421  C CA  . GLY A 55  ? 0.4047 0.3932 0.2991 -0.0425 0.0361  0.0195  72  GLY A CA  
422  C C   . GLY A 55  ? 0.3610 0.3592 0.2674 -0.0440 0.0302  0.0126  72  GLY A C   
423  O O   . GLY A 55  ? 0.3896 0.4044 0.3039 -0.0465 0.0278  0.0091  72  GLY A O   
424  N N   . ASP A 56  ? 0.3967 0.3834 0.3026 -0.0416 0.0278  0.0105  73  ASP A N   
425  C CA  . ASP A 56  ? 0.3583 0.3534 0.2730 -0.0425 0.0230  0.0041  73  ASP A CA  
426  C C   . ASP A 56  ? 0.3609 0.3749 0.2750 -0.0360 0.0200  0.0041  73  ASP A C   
427  O O   . ASP A 56  ? 0.3499 0.3757 0.2722 -0.0391 0.0180  0.0010  73  ASP A O   
428  C CB  . ASP A 56  ? 0.3902 0.3675 0.3016 -0.0398 0.0200  0.0006  73  ASP A CB  
429  C CG  . ASP A 56  ? 0.3981 0.3605 0.3181 -0.0501 0.0214  -0.0013 73  ASP A CG  
430  O OD1 . ASP A 56  ? 0.4836 0.4303 0.4028 -0.0497 0.0173  -0.0059 73  ASP A OD1 
431  O OD2 . ASP A 56  ? 0.4991 0.4666 0.4275 -0.0585 0.0264  0.0011  73  ASP A OD2 
432  N N   . ARG A 57  ? 0.3742 0.3921 0.2795 -0.0271 0.0197  0.0080  74  ARG A N   
433  C CA  . ARG A 57  ? 0.3665 0.4064 0.2762 -0.0227 0.0172  0.0082  74  ARG A CA  
434  C C   . ARG A 57  ? 0.3489 0.4035 0.2679 -0.0310 0.0164  0.0077  74  ARG A C   
435  O O   . ARG A 57  ? 0.3310 0.3993 0.2593 -0.0344 0.0149  0.0063  74  ARG A O   
436  C CB  . ARG A 57  ? 0.3799 0.4239 0.2808 -0.0107 0.0160  0.0118  74  ARG A CB  
437  C CG  . ARG A 57  ? 0.3304 0.4017 0.2400 -0.0066 0.0136  0.0126  74  ARG A CG  
438  C CD  . ARG A 57  ? 0.3441 0.4246 0.2610 -0.0067 0.0148  0.0108  74  ARG A CD  
439  N NE  . ARG A 57  ? 0.3769 0.4845 0.3038 -0.0026 0.0145  0.0130  74  ARG A NE  
440  C CZ  . ARG A 57  ? 0.4139 0.5334 0.3458 0.0000  0.0174  0.0136  74  ARG A CZ  
441  N NH1 . ARG A 57  ? 0.4105 0.5165 0.3362 -0.0005 0.0193  0.0113  74  ARG A NH1 
442  N NH2 . ARG A 57  ? 0.4314 0.5782 0.3751 0.0033  0.0184  0.0167  74  ARG A NH2 
443  N N   . LEU A 58  ? 0.3306 0.3803 0.2453 -0.0339 0.0178  0.0089  75  LEU A N   
444  C CA  . LEU A 58  ? 0.3099 0.3700 0.2309 -0.0406 0.0164  0.0068  75  LEU A CA  
445  C C   . LEU A 58  ? 0.3268 0.3856 0.2579 -0.0489 0.0171  0.0029  75  LEU A C   
446  O O   . LEU A 58  ? 0.3098 0.3785 0.2485 -0.0531 0.0142  0.0006  75  LEU A O   
447  C CB  . LEU A 58  ? 0.3453 0.3989 0.2559 -0.0397 0.0186  0.0085  75  LEU A CB  
448  C CG  . LEU A 58  ? 0.3255 0.3870 0.2394 -0.0448 0.0167  0.0047  75  LEU A CG  
449  C CD1 . LEU A 58  ? 0.3499 0.4282 0.2693 -0.0442 0.0090  0.0024  75  LEU A CD1 
450  C CD2 . LEU A 58  ? 0.3449 0.3986 0.2456 -0.0426 0.0207  0.0065  75  LEU A CD2 
451  N N   . ILE A 59  ? 0.3079 0.3539 0.2398 -0.0513 0.0200  0.0019  76  ILE A N   
452  C CA  . ILE A 59  ? 0.3040 0.3503 0.2457 -0.0572 0.0192  -0.0024 76  ILE A CA  
453  C C   . ILE A 59  ? 0.3303 0.3844 0.2754 -0.0557 0.0156  -0.0033 76  ILE A C   
454  O O   . ILE A 59  ? 0.3288 0.3883 0.2800 -0.0596 0.0137  -0.0050 76  ILE A O   
455  C CB  . ILE A 59  ? 0.3221 0.3557 0.2667 -0.0598 0.0212  -0.0042 76  ILE A CB  
456  C CG1 . ILE A 59  ? 0.3300 0.3581 0.2740 -0.0633 0.0271  -0.0018 76  ILE A CG1 
457  C CG2 . ILE A 59  ? 0.3275 0.3637 0.2824 -0.0636 0.0181  -0.0094 76  ILE A CG2 
458  C CD1 . ILE A 59  ? 0.3489 0.3639 0.2977 -0.0674 0.0298  -0.0019 76  ILE A CD1 
459  N N   . HIS A 60  ? 0.2993 0.3533 0.2393 -0.0491 0.0152  -0.0015 77  HIS A N   
460  C CA  . HIS A 60  ? 0.2994 0.3624 0.2411 -0.0466 0.0139  -0.0008 77  HIS A CA  
461  C C   . HIS A 60  ? 0.3057 0.3846 0.2541 -0.0498 0.0133  0.0021  77  HIS A C   
462  O O   . HIS A 60  ? 0.3026 0.3857 0.2563 -0.0541 0.0126  0.0025  77  HIS A O   
463  C CB  . HIS A 60  ? 0.2971 0.3584 0.2306 -0.0368 0.0146  0.0004  77  HIS A CB  
464  C CG  . HIS A 60  ? 0.3228 0.3955 0.2566 -0.0327 0.0155  0.0024  77  HIS A CG  
465  N ND1 . HIS A 60  ? 0.3302 0.4219 0.2695 -0.0312 0.0175  0.0071  77  HIS A ND1 
466  C CD2 . HIS A 60  ? 0.3009 0.3692 0.2297 -0.0295 0.0151  0.0006  77  HIS A CD2 
467  C CE1 . HIS A 60  ? 0.3146 0.4136 0.2529 -0.0277 0.0201  0.0094  77  HIS A CE1 
468  N NE2 . HIS A 60  ? 0.3280 0.4120 0.2577 -0.0257 0.0186  0.0055  77  HIS A NE2 
469  N N   . GLU A 61  ? 0.2928 0.3795 0.2408 -0.0478 0.0128  0.0040  78  GLU A N   
470  C CA  . GLU A 61  ? 0.3225 0.4258 0.2796 -0.0516 0.0105  0.0057  78  GLU A CA  
471  C C   . GLU A 61  ? 0.3190 0.4192 0.2809 -0.0604 0.0079  0.0027  78  GLU A C   
472  O O   . GLU A 61  ? 0.3079 0.4147 0.2783 -0.0663 0.0064  0.0037  78  GLU A O   
473  C CB  . GLU A 61  ? 0.3018 0.4162 0.2581 -0.0461 0.0085  0.0072  78  GLU A CB  
474  C CG  . GLU A 61  ? 0.3607 0.4759 0.3107 -0.0353 0.0109  0.0096  78  GLU A CG  
475  C CD  . GLU A 61  ? 0.4046 0.5379 0.3638 -0.0332 0.0129  0.0127  78  GLU A CD  
476  O OE1 . GLU A 61  ? 0.4136 0.5683 0.3846 -0.0342 0.0112  0.0148  78  GLU A OE1 
477  O OE2 . GLU A 61  ? 0.3644 0.4910 0.3195 -0.0312 0.0164  0.0130  78  GLU A OE2 
478  N N   . GLN A 62  ? 0.2916 0.3813 0.2477 -0.0612 0.0078  -0.0005 79  GLN A N   
479  C CA  . GLN A 62  ? 0.2863 0.3724 0.2450 -0.0673 0.0054  -0.0044 79  GLN A CA  
480  C C   . GLN A 62  ? 0.3278 0.4079 0.2911 -0.0709 0.0058  -0.0054 79  GLN A C   
481  O O   . GLN A 62  ? 0.3224 0.4016 0.2901 -0.0758 0.0028  -0.0067 79  GLN A O   
482  C CB  . GLN A 62  ? 0.3112 0.3890 0.2619 -0.0656 0.0073  -0.0071 79  GLN A CB  
483  C CG  . GLN A 62  ? 0.3520 0.4263 0.3035 -0.0693 0.0050  -0.0122 79  GLN A CG  
484  C CD  . GLN A 62  ? 0.3492 0.4298 0.3017 -0.0716 -0.0018 -0.0146 79  GLN A CD  
485  O OE1 . GLN A 62  ? 0.4043 0.4915 0.3522 -0.0682 -0.0043 -0.0140 79  GLN A OE1 
486  N NE2 . GLN A 62  ? 0.3282 0.4059 0.2869 -0.0770 -0.0058 -0.0175 79  GLN A NE2 
487  N N   . ASP A 63  ? 0.3202 0.3941 0.2813 -0.0680 0.0084  -0.0052 80  ASP A N   
488  C CA  . ASP A 63  ? 0.2967 0.3651 0.2603 -0.0696 0.0074  -0.0065 80  ASP A CA  
489  C C   . ASP A 63  ? 0.3340 0.4074 0.2995 -0.0707 0.0070  -0.0019 80  ASP A C   
490  O O   . ASP A 63  ? 0.3110 0.3793 0.2778 -0.0734 0.0054  -0.0016 80  ASP A O   
491  C CB  . ASP A 63  ? 0.2986 0.3601 0.2601 -0.0661 0.0085  -0.0087 80  ASP A CB  
492  C CG  . ASP A 63  ? 0.3560 0.4131 0.3208 -0.0679 0.0097  -0.0129 80  ASP A CG  
493  O OD1 . ASP A 63  ? 0.3910 0.4465 0.3534 -0.0674 0.0129  -0.0121 80  ASP A OD1 
494  O OD2 . ASP A 63  ? 0.3844 0.4400 0.3538 -0.0694 0.0081  -0.0164 80  ASP A OD2 
495  N N   . LEU A 64  ? 0.3051 0.3888 0.2708 -0.0682 0.0091  0.0024  81  LEU A N   
496  C CA  . LEU A 64  ? 0.3161 0.4080 0.2857 -0.0699 0.0108  0.0083  81  LEU A CA  
497  C C   . LEU A 64  ? 0.3296 0.4258 0.3088 -0.0789 0.0082  0.0096  81  LEU A C   
498  O O   . LEU A 64  ? 0.3141 0.4099 0.2970 -0.0835 0.0093  0.0143  81  LEU A O   
499  C CB  . LEU A 64  ? 0.3475 0.4529 0.3168 -0.0637 0.0145  0.0124  81  LEU A CB  
500  C CG  . LEU A 64  ? 0.4024 0.5057 0.3624 -0.0554 0.0183  0.0146  81  LEU A CG  
501  C CD1 . LEU A 64  ? 0.3768 0.4822 0.3372 -0.0579 0.0215  0.0207  81  LEU A CD1 
502  C CD2 . LEU A 64  ? 0.4003 0.4870 0.3505 -0.0509 0.0156  0.0084  81  LEU A CD2 
503  N N   . GLU A 65  ? 0.3121 0.4107 0.2942 -0.0815 0.0043  0.0054  82  GLU A N   
504  C CA  . GLU A 65  ? 0.3043 0.4027 0.2940 -0.0900 -0.0007 0.0037  82  GLU A CA  
505  C C   . GLU A 65  ? 0.3205 0.4012 0.3066 -0.0929 -0.0027 0.0009  82  GLU A C   
506  O O   . GLU A 65  ? 0.3433 0.4190 0.3345 -0.0998 -0.0045 0.0034  82  GLU A O   
507  C CB  . GLU A 65  ? 0.3677 0.4702 0.3565 -0.0894 -0.0057 -0.0019 82  GLU A CB  
508  C CG  . GLU A 65  ? 0.3780 0.4992 0.3720 -0.0864 -0.0060 0.0007  82  GLU A CG  
509  C CD  . GLU A 65  ? 0.4575 0.5946 0.4680 -0.0938 -0.0070 0.0053  82  GLU A CD  
510  O OE1 . GLU A 65  ? 0.4710 0.6253 0.4877 -0.0899 -0.0030 0.0105  82  GLU A OE1 
511  O OE2 . GLU A 65  ? 0.4349 0.5677 0.4531 -0.1034 -0.0118 0.0035  82  GLU A OE2 
512  N N   . TRP A 66  ? 0.3281 0.3990 0.3062 -0.0877 -0.0023 -0.0040 83  TRP A N   
513  C CA  . TRP A 66  ? 0.3191 0.3753 0.2943 -0.0880 -0.0044 -0.0071 83  TRP A CA  
514  C C   . TRP A 66  ? 0.3131 0.3638 0.2870 -0.0877 -0.0027 -0.0013 83  TRP A C   
515  O O   . TRP A 66  ? 0.3176 0.3561 0.2905 -0.0903 -0.0053 -0.0007 83  TRP A O   
516  C CB  . TRP A 66  ? 0.3226 0.3747 0.2933 -0.0820 -0.0032 -0.0128 83  TRP A CB  
517  C CG  . TRP A 66  ? 0.3023 0.3559 0.2706 -0.0811 -0.0039 -0.0182 83  TRP A CG  
518  C CD1 . TRP A 66  ? 0.3103 0.3621 0.2774 -0.0839 -0.0084 -0.0217 83  TRP A CD1 
519  C CD2 . TRP A 66  ? 0.3298 0.3856 0.2949 -0.0767 0.0003  -0.0204 83  TRP A CD2 
520  N NE1 . TRP A 66  ? 0.3416 0.3949 0.3020 -0.0796 -0.0070 -0.0262 83  TRP A NE1 
521  C CE2 . TRP A 66  ? 0.3362 0.3922 0.2961 -0.0757 -0.0007 -0.0244 83  TRP A CE2 
522  C CE3 . TRP A 66  ? 0.3370 0.3940 0.3035 -0.0739 0.0045  -0.0194 83  TRP A CE3 
523  C CZ2 . TRP A 66  ? 0.3725 0.4302 0.3272 -0.0717 0.0045  -0.0255 83  TRP A CZ2 
524  C CZ3 . TRP A 66  ? 0.3208 0.3790 0.2853 -0.0719 0.0090  -0.0208 83  TRP A CZ3 
525  C CH2 . TRP A 66  ? 0.3204 0.3793 0.2786 -0.0707 0.0100  -0.0229 83  TRP A CH2 
526  N N   . LEU A 67  ? 0.3110 0.3684 0.2823 -0.0832 0.0015  0.0028  84  LEU A N   
527  C CA  . LEU A 67  ? 0.2957 0.3478 0.2616 -0.0808 0.0034  0.0085  84  LEU A CA  
528  C C   . LEU A 67  ? 0.3217 0.3745 0.2923 -0.0883 0.0052  0.0166  84  LEU A C   
529  O O   . LEU A 67  ? 0.3281 0.3687 0.2936 -0.0889 0.0053  0.0212  84  LEU A O   
530  C CB  . LEU A 67  ? 0.3090 0.3686 0.2693 -0.0735 0.0072  0.0105  84  LEU A CB  
531  C CG  . LEU A 67  ? 0.3481 0.4003 0.2974 -0.0671 0.0080  0.0138  84  LEU A CG  
532  C CD1 . LEU A 67  ? 0.3497 0.3895 0.2955 -0.0634 0.0021  0.0069  84  LEU A CD1 
533  C CD2 . LEU A 67  ? 0.3535 0.4129 0.2959 -0.0592 0.0111  0.0145  84  LEU A CD2 
534  N N   . GLN A 68  ? 0.3315 0.3982 0.3126 -0.0944 0.0063  0.0188  85  GLN A N   
535  C CA  . GLN A 68  ? 0.3547 0.4240 0.3447 -0.1038 0.0083  0.0269  85  GLN A CA  
536  C C   . GLN A 68  ? 0.3354 0.3882 0.3287 -0.1121 0.0019  0.0237  85  GLN A C   
537  O O   . GLN A 68  ? 0.3865 0.4309 0.3832 -0.1197 0.0031  0.0309  85  GLN A O   
538  C CB  . GLN A 68  ? 0.3461 0.4391 0.3503 -0.1081 0.0108  0.0301  85  GLN A CB  
539  C CG  . GLN A 68  ? 0.4084 0.5162 0.4085 -0.0992 0.0185  0.0354  85  GLN A CG  
540  C CD  . GLN A 68  ? 0.4226 0.5546 0.4341 -0.0981 0.0196  0.0353  85  GLN A CD  
541  O OE1 . GLN A 68  ? 0.4343 0.5841 0.4609 -0.1045 0.0233  0.0422  85  GLN A OE1 
542  N NE2 . GLN A 68  ? 0.3767 0.5099 0.3828 -0.0908 0.0161  0.0280  85  GLN A NE2 
543  N N   . GLN A 69  ? 0.3315 0.3785 0.3230 -0.1106 -0.0046 0.0133  86  GLN A N   
544  C CA  . GLN A 69  ? 0.3432 0.3717 0.3343 -0.1156 -0.0115 0.0082  86  GLN A CA  
545  C C   . GLN A 69  ? 0.3675 0.3746 0.3475 -0.1108 -0.0119 0.0092  86  GLN A C   
546  O O   . GLN A 69  ? 0.3974 0.3856 0.3763 -0.1155 -0.0164 0.0089  86  GLN A O   
547  C CB  . GLN A 69  ? 0.3685 0.3975 0.3568 -0.1119 -0.0169 -0.0033 86  GLN A CB  
548  C CG  . GLN A 69  ? 0.3818 0.4266 0.3786 -0.1164 -0.0201 -0.0061 86  GLN A CG  
549  C CD  . GLN A 69  ? 0.4406 0.4860 0.4289 -0.1089 -0.0228 -0.0156 86  GLN A CD  
550  O OE1 . GLN A 69  ? 0.4311 0.4619 0.4109 -0.1049 -0.0254 -0.0223 86  GLN A OE1 
551  N NE2 . GLN A 69  ? 0.4495 0.5117 0.4394 -0.1066 -0.0222 -0.0160 86  GLN A NE2 
552  N N   . ALA A 70  ? 0.4031 0.3502 0.3228 -0.1472 -0.0388 -0.0514 87  ALA A N   
553  C CA  . ALA A 70  ? 0.4387 0.3571 0.3523 -0.1340 -0.0288 -0.0521 87  ALA A CA  
554  C C   . ALA A 70  ? 0.4814 0.3723 0.3938 -0.1441 -0.0292 -0.0495 87  ALA A C   
555  O O   . ALA A 70  ? 0.4663 0.3728 0.3939 -0.1570 -0.0314 -0.0408 87  ALA A O   
556  C CB  . ALA A 70  ? 0.3943 0.3352 0.3266 -0.1173 -0.0211 -0.0428 87  ALA A CB  
557  N N   . ASP A 71  ? 0.4512 0.2988 0.3433 -0.1378 -0.0263 -0.0573 88  ASP A N   
558  C CA  . ASP A 71  ? 0.4861 0.2981 0.3721 -0.1421 -0.0258 -0.0523 88  ASP A CA  
559  C C   . ASP A 71  ? 0.4807 0.2980 0.3795 -0.1239 -0.0203 -0.0411 88  ASP A C   
560  O O   . ASP A 71  ? 0.5075 0.3111 0.4059 -0.1301 -0.0207 -0.0305 88  ASP A O   
561  C CB  . ASP A 71  ? 0.5622 0.3203 0.4192 -0.1395 -0.0261 -0.0654 88  ASP A CB  
562  C CG  . ASP A 71  ? 0.5942 0.3399 0.4340 -0.1617 -0.0338 -0.0774 88  ASP A CG  
563  O OD1 . ASP A 71  ? 0.6083 0.3539 0.4518 -0.1869 -0.0398 -0.0731 88  ASP A OD1 
564  O OD2 . ASP A 71  ? 0.5911 0.3310 0.4141 -0.1552 -0.0337 -0.0915 88  ASP A OD2 
565  N N   . VAL A 72  ? 0.4415 0.2773 0.3497 -0.1030 -0.0154 -0.0433 89  VAL A N   
566  C CA  . VAL A 72  ? 0.4207 0.2682 0.3438 -0.0862 -0.0125 -0.0343 89  VAL A CA  
567  C C   . VAL A 72  ? 0.4177 0.3087 0.3599 -0.0787 -0.0086 -0.0339 89  VAL A C   
568  O O   . VAL A 72  ? 0.4094 0.3088 0.3477 -0.0764 -0.0053 -0.0427 89  VAL A O   
569  C CB  . VAL A 72  ? 0.4540 0.2696 0.3691 -0.0653 -0.0109 -0.0391 89  VAL A CB  
570  C CG1 . VAL A 72  ? 0.4452 0.2800 0.3787 -0.0478 -0.0111 -0.0305 89  VAL A CG1 
571  C CG2 . VAL A 72  ? 0.5301 0.2917 0.4204 -0.0723 -0.0152 -0.0393 89  VAL A CG2 
572  N N   . VAL A 73  ? 0.3579 0.2728 0.3165 -0.0762 -0.0087 -0.0237 90  VAL A N   
573  C CA  . VAL A 73  ? 0.3478 0.2970 0.3236 -0.0687 -0.0052 -0.0225 90  VAL A CA  
574  C C   . VAL A 73  ? 0.3813 0.3320 0.3677 -0.0515 -0.0039 -0.0218 90  VAL A C   
575  O O   . VAL A 73  ? 0.3816 0.3227 0.3674 -0.0484 -0.0084 -0.0146 90  VAL A O   
576  C CB  . VAL A 73  ? 0.3101 0.2848 0.2965 -0.0781 -0.0072 -0.0138 90  VAL A CB  
577  C CG1 . VAL A 73  ? 0.3144 0.3159 0.3149 -0.0703 -0.0040 -0.0129 90  VAL A CG1 
578  C CG2 . VAL A 73  ? 0.3291 0.3082 0.3103 -0.0940 -0.0106 -0.0152 90  VAL A CG2 
579  N N   . VAL A 74  ? 0.3371 0.3012 0.3327 -0.0410 0.0020  -0.0290 91  VAL A N   
580  C CA  . VAL A 74  ? 0.3367 0.3116 0.3495 -0.0249 0.0026  -0.0302 91  VAL A CA  
581  C C   . VAL A 74  ? 0.3110 0.3202 0.3422 -0.0268 0.0065  -0.0287 91  VAL A C   
582  O O   . VAL A 74  ? 0.3002 0.3201 0.3303 -0.0319 0.0141  -0.0325 91  VAL A O   
583  C CB  . VAL A 74  ? 0.3410 0.3051 0.3536 -0.0104 0.0082  -0.0416 91  VAL A CB  
584  C CG1 . VAL A 74  ? 0.3536 0.3387 0.3917 0.0073  0.0078  -0.0435 91  VAL A CG1 
585  C CG2 . VAL A 74  ? 0.4004 0.3212 0.3899 -0.0089 0.0040  -0.0441 91  VAL A CG2 
586  N N   . ALA A 75  ? 0.2843 0.3072 0.3288 -0.0234 0.0010  -0.0233 92  ALA A N   
587  C CA  . ALA A 75  ? 0.2931 0.3430 0.3531 -0.0274 0.0036  -0.0224 92  ALA A CA  
588  C C   . ALA A 75  ? 0.3061 0.3751 0.3888 -0.0167 0.0006  -0.0257 92  ALA A C   
589  O O   . ALA A 75  ? 0.3229 0.3854 0.4061 -0.0076 -0.0091 -0.0230 92  ALA A O   
590  C CB  . ALA A 75  ? 0.2737 0.3249 0.3274 -0.0368 -0.0011 -0.0145 92  ALA A CB  
591  N N   . GLU A 76  ? 0.2588 0.3518 0.3596 -0.0186 0.0085  -0.0310 93  GLU A N   
592  C CA  . GLU A 76  ? 0.2315 0.3517 0.3600 -0.0128 0.0051  -0.0347 93  GLU A CA  
593  C C   . GLU A 76  ? 0.2548 0.3829 0.3843 -0.0251 0.0013  -0.0304 93  GLU A C   
594  O O   . GLU A 76  ? 0.2541 0.3842 0.3804 -0.0369 0.0099  -0.0298 93  GLU A O   
595  C CB  . GLU A 76  ? 0.2477 0.3916 0.3975 -0.0105 0.0182  -0.0439 93  GLU A CB  
596  C CG  . GLU A 76  ? 0.2240 0.3996 0.4089 0.0025  0.0147  -0.0512 93  GLU A CG  
597  C CD  . GLU A 76  ? 0.2684 0.4669 0.4729 -0.0029 0.0032  -0.0498 93  GLU A CD  
598  O OE1 . GLU A 76  ? 0.2561 0.4730 0.4822 0.0108  -0.0089 -0.0529 93  GLU A OE1 
599  O OE2 . GLU A 76  ? 0.2338 0.4288 0.4295 -0.0195 0.0043  -0.0457 93  GLU A OE2 
600  N N   . VAL A 77  ? 0.2480 0.3758 0.3771 -0.0218 -0.0118 -0.0273 94  VAL A N   
601  C CA  . VAL A 77  ? 0.2340 0.3599 0.3549 -0.0317 -0.0160 -0.0240 94  VAL A CA  
602  C C   . VAL A 77  ? 0.2418 0.3914 0.3840 -0.0342 -0.0229 -0.0293 94  VAL A C   
603  O O   . VAL A 77  ? 0.2474 0.3932 0.3809 -0.0388 -0.0307 -0.0285 94  VAL A O   
604  C CB  . VAL A 77  ? 0.2158 0.3205 0.3123 -0.0293 -0.0237 -0.0168 94  VAL A CB  
605  C CG1 . VAL A 77  ? 0.2465 0.3317 0.3254 -0.0321 -0.0168 -0.0123 94  VAL A CG1 
606  C CG2 . VAL A 77  ? 0.2730 0.3756 0.3692 -0.0168 -0.0361 -0.0154 94  VAL A CG2 
607  N N   . THR A 78  ? 0.2131 0.3890 0.3840 -0.0321 -0.0200 -0.0362 95  THR A N   
608  C CA  . THR A 78  ? 0.2104 0.4141 0.4064 -0.0372 -0.0278 -0.0425 95  THR A CA  
609  C C   . THR A 78  ? 0.2552 0.4574 0.4501 -0.0569 -0.0204 -0.0439 95  THR A C   
610  O O   . THR A 78  ? 0.2394 0.4430 0.4338 -0.0644 -0.0302 -0.0466 95  THR A O   
611  C CB  . THR A 78  ? 0.2217 0.4605 0.4545 -0.0292 -0.0256 -0.0502 95  THR A CB  
612  O OG1 . THR A 78  ? 0.2431 0.4757 0.4732 -0.0078 -0.0339 -0.0487 95  THR A OG1 
613  C CG2 . THR A 78  ? 0.2266 0.5005 0.4905 -0.0357 -0.0361 -0.0577 95  THR A CG2 
614  N N   . GLN A 79  ? 0.2126 0.4077 0.4030 -0.0652 -0.0040 -0.0420 96  GLN A N   
615  C CA  . GLN A 79  ? 0.1860 0.3717 0.3705 -0.0831 0.0036  -0.0413 96  GLN A CA  
616  C C   . GLN A 79  ? 0.2447 0.3961 0.3958 -0.0827 0.0013  -0.0345 96  GLN A C   
617  O O   . GLN A 79  ? 0.2238 0.3603 0.3574 -0.0757 0.0055  -0.0288 96  GLN A O   
618  C CB  . GLN A 79  ? 0.2307 0.4219 0.4206 -0.0918 0.0223  -0.0408 96  GLN A CB  
619  C CG  . GLN A 79  ? 0.2338 0.4125 0.4171 -0.1116 0.0300  -0.0389 96  GLN A CG  
620  C CD  . GLN A 79  ? 0.2657 0.4701 0.4790 -0.1261 0.0269  -0.0468 96  GLN A CD  
621  O OE1 . GLN A 79  ? 0.2701 0.5091 0.5138 -0.1208 0.0247  -0.0526 96  GLN A OE1 
622  N NE2 . GLN A 79  ? 0.3011 0.4828 0.5016 -0.1399 0.0237  -0.0460 96  GLN A NE2 
623  N N   . PRO A 80  ? 0.2023 0.3416 0.3446 -0.0893 -0.0055 -0.0360 97  PRO A N   
624  C CA  . PRO A 80  ? 0.2070 0.3178 0.3208 -0.0855 -0.0063 -0.0308 97  PRO A CA  
625  C C   . PRO A 80  ? 0.2470 0.3401 0.3473 -0.0890 0.0053  -0.0243 97  PRO A C   
626  O O   . PRO A 80  ? 0.2557 0.3466 0.3601 -0.1006 0.0137  -0.0240 97  PRO A O   
627  C CB  . PRO A 80  ? 0.2559 0.3571 0.3641 -0.0922 -0.0141 -0.0366 97  PRO A CB  
628  C CG  . PRO A 80  ? 0.2512 0.3787 0.3836 -0.0975 -0.0227 -0.0445 97  PRO A CG  
629  C CD  . PRO A 80  ? 0.2252 0.3778 0.3833 -0.0991 -0.0141 -0.0441 97  PRO A CD  
630  N N   . SER A 81  ? 0.2437 0.3242 0.3266 -0.0799 0.0051  -0.0187 98  SER A N   
631  C CA  . SER A 81  ? 0.2450 0.3116 0.3139 -0.0801 0.0124  -0.0121 98  SER A CA  
632  C C   . SER A 81  ? 0.2341 0.2903 0.2883 -0.0708 0.0081  -0.0081 98  SER A C   
633  O O   . SER A 81  ? 0.2166 0.2815 0.2720 -0.0645 0.0043  -0.0082 98  SER A O   
634  C CB  . SER A 81  ? 0.2530 0.3305 0.3258 -0.0792 0.0187  -0.0110 98  SER A CB  
635  O OG  . SER A 81  ? 0.2571 0.3212 0.3112 -0.0776 0.0220  -0.0048 98  SER A OG  
636  N N   . LEU A 82  ? 0.2283 0.2660 0.2691 -0.0698 0.0093  -0.0042 99  LEU A N   
637  C CA  . LEU A 82  ? 0.2223 0.2568 0.2546 -0.0593 0.0057  -0.0010 99  LEU A CA  
638  C C   . LEU A 82  ? 0.2530 0.2984 0.2846 -0.0568 0.0055  0.0029  99  LEU A C   
639  O O   . LEU A 82  ? 0.2374 0.2938 0.2719 -0.0518 0.0024  0.0030  99  LEU A O   
640  C CB  . LEU A 82  ? 0.2496 0.2607 0.2682 -0.0559 0.0058  0.0027  99  LEU A CB  
641  C CG  . LEU A 82  ? 0.2637 0.2555 0.2781 -0.0577 0.0053  -0.0025 99  LEU A CG  
642  C CD1 . LEU A 82  ? 0.2919 0.2532 0.2889 -0.0536 0.0055  0.0034  99  LEU A CD1 
643  C CD2 . LEU A 82  ? 0.2896 0.2888 0.3062 -0.0487 0.0019  -0.0091 99  LEU A CD2 
644  N N   . GLY A 83  ? 0.2207 0.2625 0.2465 -0.0619 0.0095  0.0058  100 GLY A N   
645  C CA  . GLY A 83  ? 0.2542 0.3023 0.2748 -0.0605 0.0081  0.0078  100 GLY A CA  
646  C C   . GLY A 83  ? 0.2326 0.2936 0.2630 -0.0608 0.0073  0.0034  100 GLY A C   
647  O O   . GLY A 83  ? 0.2376 0.3037 0.2664 -0.0595 0.0034  0.0041  100 GLY A O   
648  N N   . VAL A 84  ? 0.2181 0.2838 0.2588 -0.0630 0.0104  -0.0009 101 VAL A N   
649  C CA  . VAL A 84  ? 0.2474 0.3195 0.2947 -0.0606 0.0082  -0.0040 101 VAL A CA  
650  C C   . VAL A 84  ? 0.2347 0.3085 0.2817 -0.0578 0.0026  -0.0021 101 VAL A C   
651  O O   . VAL A 84  ? 0.2223 0.2954 0.2660 -0.0581 0.0006  -0.0009 101 VAL A O   
652  C CB  . VAL A 84  ? 0.2277 0.3080 0.2893 -0.0602 0.0101  -0.0089 101 VAL A CB  
653  C CG1 . VAL A 84  ? 0.2496 0.3317 0.3153 -0.0541 0.0050  -0.0105 101 VAL A CG1 
654  C CG2 . VAL A 84  ? 0.2381 0.3215 0.3016 -0.0636 0.0193  -0.0115 101 VAL A CG2 
655  N N   . GLY A 85  ? 0.2223 0.2966 0.2708 -0.0564 0.0011  -0.0024 102 GLY A N   
656  C CA  . GLY A 85  ? 0.2023 0.2793 0.2475 -0.0538 -0.0013 -0.0012 102 GLY A CA  
657  C C   . GLY A 85  ? 0.2218 0.3041 0.2652 -0.0536 -0.0006 0.0021  102 GLY A C   
658  O O   . GLY A 85  ? 0.2210 0.3089 0.2639 -0.0556 -0.0005 0.0039  102 GLY A O   
659  N N   . TYR A 86  ? 0.2283 0.3093 0.2706 -0.0518 -0.0007 0.0034  103 TYR A N   
660  C CA  . TYR A 86  ? 0.2142 0.3056 0.2586 -0.0501 -0.0030 0.0060  103 TYR A CA  
661  C C   . TYR A 86  ? 0.2180 0.3134 0.2618 -0.0574 -0.0049 0.0064  103 TYR A C   
662  O O   . TYR A 86  ? 0.2199 0.3285 0.2696 -0.0609 -0.0062 0.0072  103 TYR A O   
663  C CB  . TYR A 86  ? 0.2097 0.2943 0.2487 -0.0448 -0.0055 0.0085  103 TYR A CB  
664  C CG  . TYR A 86  ? 0.2201 0.3187 0.2629 -0.0407 -0.0113 0.0110  103 TYR A CG  
665  C CD1 . TYR A 86  ? 0.2068 0.3196 0.2603 -0.0313 -0.0123 0.0105  103 TYR A CD1 
666  C CD2 . TYR A 86  ? 0.2281 0.3282 0.2646 -0.0454 -0.0165 0.0126  103 TYR A CD2 
667  C CE1 . TYR A 86  ? 0.2021 0.3352 0.2653 -0.0264 -0.0191 0.0121  103 TYR A CE1 
668  C CE2 . TYR A 86  ? 0.2349 0.3521 0.2769 -0.0420 -0.0250 0.0142  103 TYR A CE2 
669  C CZ  . TYR A 86  ? 0.2134 0.3493 0.2713 -0.0322 -0.0268 0.0142  103 TYR A CZ  
670  O OH  . TYR A 86  ? 0.2045 0.3645 0.2740 -0.0277 -0.0364 0.0151  103 TYR A OH  
671  N N   . GLU A 87  ? 0.2137 0.2980 0.2506 -0.0607 -0.0042 0.0049  104 GLU A N   
672  C CA  . GLU A 87  ? 0.2061 0.2873 0.2385 -0.0671 -0.0058 0.0032  104 GLU A CA  
673  C C   . GLU A 87  ? 0.2285 0.3082 0.2637 -0.0710 -0.0052 0.0035  104 GLU A C   
674  O O   . GLU A 87  ? 0.2418 0.3227 0.2760 -0.0788 -0.0072 0.0038  104 GLU A O   
675  C CB  . GLU A 87  ? 0.2468 0.3155 0.2706 -0.0671 -0.0025 -0.0002 104 GLU A CB  
676  C CG  . GLU A 87  ? 0.2455 0.3121 0.2586 -0.0666 -0.0028 0.0011  104 GLU A CG  
677  C CD  . GLU A 87  ? 0.2778 0.3353 0.2827 -0.0668 0.0049  -0.0016 104 GLU A CD  
678  O OE1 . GLU A 87  ? 0.2882 0.3465 0.3028 -0.0653 0.0103  -0.0049 104 GLU A OE1 
679  O OE2 . GLU A 87  ? 0.3212 0.3727 0.3098 -0.0684 0.0056  -0.0002 104 GLU A OE2 
680  N N   . LEU A 88  ? 0.2296 0.3052 0.2662 -0.0668 -0.0031 0.0039  105 LEU A N   
681  C CA  . LEU A 88  ? 0.2186 0.2882 0.2515 -0.0695 -0.0031 0.0064  105 LEU A CA  
682  C C   . LEU A 88  ? 0.2521 0.3350 0.2877 -0.0745 -0.0009 0.0098  105 LEU A C   
683  O O   . LEU A 88  ? 0.2475 0.3263 0.2786 -0.0832 0.0003  0.0128  105 LEU A O   
684  C CB  . LEU A 88  ? 0.2413 0.3053 0.2730 -0.0625 -0.0042 0.0061  105 LEU A CB  
685  C CG  . LEU A 88  ? 0.2460 0.3021 0.2803 -0.0573 -0.0055 0.0022  105 LEU A CG  
686  C CD1 . LEU A 88  ? 0.2314 0.2920 0.2718 -0.0505 -0.0087 0.0005  105 LEU A CD1 
687  C CD2 . LEU A 88  ? 0.2831 0.3210 0.3085 -0.0581 -0.0072 0.0028  105 LEU A CD2 
688  N N   . GLY A 89  ? 0.2184 0.3165 0.2612 -0.0693 0.0007  0.0090  106 GLY A N   
689  C CA  . GLY A 89  ? 0.2014 0.3181 0.2508 -0.0719 0.0048  0.0106  106 GLY A CA  
690  C C   . GLY A 89  ? 0.1959 0.3275 0.2552 -0.0810 0.0031  0.0111  106 GLY A C   
691  O O   . GLY A 89  ? 0.2110 0.3541 0.2748 -0.0909 0.0073  0.0132  106 GLY A O   
692  N N   . ARG A 90  ? 0.2081 0.3405 0.2699 -0.0791 -0.0034 0.0091  107 ARG A N   
693  C CA  . ARG A 90  ? 0.2049 0.3515 0.2746 -0.0887 -0.0084 0.0082  107 ARG A CA  
694  C C   . ARG A 90  ? 0.2135 0.3426 0.2736 -0.1032 -0.0082 0.0081  107 ARG A C   
695  O O   . ARG A 90  ? 0.2471 0.3882 0.3148 -0.1171 -0.0090 0.0080  107 ARG A O   
696  C CB  . ARG A 90  ? 0.1870 0.3314 0.2525 -0.0830 -0.0167 0.0064  107 ARG A CB  
697  C CG  . ARG A 90  ? 0.2078 0.3641 0.2799 -0.0683 -0.0189 0.0078  107 ARG A CG  
698  C CD  . ARG A 90  ? 0.1909 0.3806 0.2852 -0.0645 -0.0192 0.0078  107 ARG A CD  
699  N NE  . ARG A 90  ? 0.2007 0.4140 0.3077 -0.0744 -0.0272 0.0064  107 ARG A NE  
700  C CZ  . ARG A 90  ? 0.1928 0.4194 0.3040 -0.0683 -0.0394 0.0063  107 ARG A CZ  
701  N NH1 . ARG A 90  ? 0.2263 0.4383 0.3252 -0.0528 -0.0439 0.0091  107 ARG A NH1 
702  N NH2 . ARG A 90  ? 0.2506 0.5042 0.3768 -0.0789 -0.0482 0.0037  107 ARG A NH2 
703  N N   . ALA A 91  ? 0.2177 0.3181 0.2621 -0.1003 -0.0076 0.0075  108 ALA A N   
704  C CA  . ALA A 91  ? 0.2453 0.3217 0.2775 -0.1110 -0.0082 0.0069  108 ALA A CA  
705  C C   . ALA A 91  ? 0.2679 0.3408 0.2979 -0.1207 -0.0027 0.0128  108 ALA A C   
706  O O   . ALA A 91  ? 0.2714 0.3332 0.2963 -0.1362 -0.0029 0.0135  108 ALA A O   
707  C CB  . ALA A 91  ? 0.2758 0.3253 0.2948 -0.1015 -0.0084 0.0044  108 ALA A CB  
708  N N   . VAL A 92  ? 0.2596 0.3386 0.2897 -0.1133 0.0026  0.0170  109 VAL A N   
709  C CA  . VAL A 92  ? 0.2578 0.3336 0.2807 -0.1232 0.0096  0.0237  109 VAL A CA  
710  C C   . VAL A 92  ? 0.2794 0.3846 0.3192 -0.1386 0.0143  0.0239  109 VAL A C   
711  O O   . VAL A 92  ? 0.2842 0.3818 0.3184 -0.1566 0.0190  0.0282  109 VAL A O   
712  C CB  . VAL A 92  ? 0.2471 0.3266 0.2641 -0.1116 0.0140  0.0263  109 VAL A CB  
713  C CG1 . VAL A 92  ? 0.3258 0.4116 0.3355 -0.1224 0.0243  0.0328  109 VAL A CG1 
714  C CG2 . VAL A 92  ? 0.3179 0.3695 0.3192 -0.1005 0.0081  0.0271  109 VAL A CG2 
715  N N   . ALA A 93  ? 0.2384 0.3783 0.3000 -0.1320 0.0130  0.0194  110 ALA A N   
716  C CA  . ALA A 93  ? 0.2635 0.4405 0.3483 -0.1442 0.0164  0.0184  110 ALA A CA  
717  C C   . ALA A 93  ? 0.2638 0.4374 0.3522 -0.1613 0.0086  0.0155  110 ALA A C   
718  O O   . ALA A 93  ? 0.2853 0.4742 0.3857 -0.1722 0.0117  0.0151  110 ALA A O   
719  C CB  . ALA A 93  ? 0.2607 0.4729 0.3674 -0.1279 0.0145  0.0142  110 ALA A CB  
720  N N   . PHE A 94  ? 0.2592 0.4065 0.3338 -0.1585 -0.0014 0.0118  111 PHE A N   
721  C CA  . PHE A 94  ? 0.3000 0.4323 0.3687 -0.1739 -0.0092 0.0072  111 PHE A CA  
722  C C   . PHE A 94  ? 0.3435 0.4334 0.3896 -0.1875 -0.0049 0.0107  111 PHE A C   
723  O O   . PHE A 94  ? 0.3624 0.4305 0.3987 -0.1987 -0.0107 0.0058  111 PHE A O   
724  C CB  . PHE A 94  ? 0.2935 0.4120 0.3512 -0.1641 -0.0197 0.0007  111 PHE A CB  
725  C CG  . PHE A 94  ? 0.2808 0.4340 0.3549 -0.1542 -0.0279 -0.0022 111 PHE A CG  
726  C CD1 . PHE A 94  ? 0.3322 0.5235 0.4304 -0.1604 -0.0325 -0.0037 111 PHE A CD1 
727  C CD2 . PHE A 94  ? 0.3034 0.4472 0.3669 -0.1358 -0.0308 -0.0030 111 PHE A CD2 
728  C CE1 . PHE A 94  ? 0.2999 0.5214 0.4117 -0.1491 -0.0427 -0.0055 111 PHE A CE1 
729  C CE2 . PHE A 94  ? 0.3101 0.4778 0.3823 -0.1259 -0.0393 -0.0037 111 PHE A CE2 
730  C CZ  . PHE A 94  ? 0.2793 0.4855 0.3752 -0.1315 -0.0464 -0.0047 111 PHE A CZ  
731  N N   . ASN A 95  ? 0.3416 0.4158 0.3757 -0.1850 0.0041  0.0188  112 ASN A N   
732  C CA  . ASN A 95  ? 0.4121 0.4408 0.4199 -0.1948 0.0077  0.0252  112 ASN A CA  
733  C C   . ASN A 95  ? 0.4391 0.4235 0.4260 -0.1867 -0.0006 0.0200  112 ASN A C   
734  O O   . ASN A 95  ? 0.4799 0.4271 0.4494 -0.2003 -0.0026 0.0195  112 ASN A O   
735  C CB  . ASN A 95  ? 0.4315 0.4610 0.4418 -0.2142 0.0127  0.0274  112 ASN A CB  
736  C CG  . ASN A 95  ? 0.5627 0.5397 0.5416 -0.2240 0.0167  0.0360  112 ASN A CG  
737  O OD1 . ASN A 95  ? 0.5924 0.5402 0.5489 -0.2158 0.0179  0.0436  112 ASN A OD1 
738  N ND2 . ASN A 95  ? 0.6242 0.5880 0.6002 -0.2415 0.0178  0.0355  112 ASN A ND2 
739  N N   . LYS A 96  ? 0.3827 0.3704 0.3711 -0.1643 -0.0044 0.0156  113 LYS A N   
740  C CA  . LYS A 96  ? 0.4148 0.3686 0.3874 -0.1537 -0.0098 0.0089  113 LYS A CA  
741  C C   . LYS A 96  ? 0.4696 0.3874 0.4238 -0.1410 -0.0087 0.0146  113 LYS A C   
742  O O   . LYS A 96  ? 0.4493 0.3751 0.4041 -0.1331 -0.0059 0.0225  113 LYS A O   
743  C CB  . LYS A 96  ? 0.3711 0.3466 0.3540 -0.1372 -0.0124 0.0020  113 LYS A CB  
744  C CG  . LYS A 96  ? 0.3302 0.3333 0.3246 -0.1459 -0.0171 -0.0038 113 LYS A CG  
745  C CD  . LYS A 96  ? 0.4017 0.3808 0.3820 -0.1607 -0.0228 -0.0119 113 LYS A CD  
746  C CE  . LYS A 96  ? 0.3598 0.3684 0.3501 -0.1693 -0.0309 -0.0179 113 LYS A CE  
747  N NZ  . LYS A 96  ? 0.3825 0.3661 0.3560 -0.1853 -0.0380 -0.0277 113 LYS A NZ  
748  N N   . ARG A 97  ? 0.4337 0.3105 0.3700 -0.1382 -0.0123 0.0098  114 ARG A N   
749  C CA  . ARG A 97  ? 0.4514 0.2980 0.3749 -0.1179 -0.0143 0.0116  114 ARG A CA  
750  C C   . ARG A 97  ? 0.4517 0.3277 0.3925 -0.0967 -0.0144 0.0067  114 ARG A C   
751  O O   . ARG A 97  ? 0.4251 0.3158 0.3741 -0.0937 -0.0136 -0.0032 114 ARG A O   
752  C CB  . ARG A 97  ? 0.5387 0.3380 0.4422 -0.1169 -0.0174 0.0038  114 ARG A CB  
753  C CG  . ARG A 97  ? 0.6110 0.3713 0.4990 -0.0963 -0.0207 0.0066  114 ARG A CG  
754  C CD  . ARG A 97  ? 0.6410 0.3469 0.5052 -0.0983 -0.0230 -0.0010 114 ARG A CD  
755  N NE  . ARG A 97  ? 0.7212 0.4017 0.5797 -0.0691 -0.0261 -0.0049 114 ARG A NE  
756  C CZ  . ARG A 97  ? 0.8036 0.4332 0.6413 -0.0610 -0.0281 -0.0131 114 ARG A CZ  
757  N NH1 . ARG A 97  ? 0.7729 0.3670 0.5902 -0.0823 -0.0279 -0.0189 114 ARG A NH1 
758  N NH2 . ARG A 97  ? 0.8001 0.4153 0.6389 -0.0302 -0.0309 -0.0169 114 ARG A NH2 
759  N N   . ILE A 98  ? 0.4181 0.3013 0.3621 -0.0835 -0.0155 0.0135  115 ILE A N   
760  C CA  . ILE A 98  ? 0.3586 0.2738 0.3217 -0.0684 -0.0154 0.0096  115 ILE A CA  
761  C C   . ILE A 98  ? 0.4200 0.3230 0.3818 -0.0485 -0.0208 0.0109  115 ILE A C   
762  O O   . ILE A 98  ? 0.3988 0.2827 0.3459 -0.0463 -0.0255 0.0204  115 ILE A O   
763  C CB  . ILE A 98  ? 0.3586 0.3070 0.3326 -0.0743 -0.0129 0.0148  115 ILE A CB  
764  C CG1 . ILE A 98  ? 0.3432 0.3117 0.3253 -0.0893 -0.0091 0.0122  115 ILE A CG1 
765  C CG2 . ILE A 98  ? 0.3172 0.2894 0.3065 -0.0600 -0.0142 0.0119  115 ILE A CG2 
766  C CD1 . ILE A 98  ? 0.3593 0.3546 0.3495 -0.0951 -0.0055 0.0177  115 ILE A CD1 
767  N N   . LEU A 99  ? 0.3678 0.2844 0.3451 -0.0341 -0.0203 0.0017  116 LEU A N   
768  C CA  . LEU A 99  ? 0.4131 0.3334 0.3999 -0.0138 -0.0261 0.0009  116 LEU A CA  
769  C C   . LEU A 99  ? 0.3720 0.3347 0.3846 -0.0104 -0.0238 -0.0040 116 LEU A C   
770  O O   . LEU A 99  ? 0.3484 0.3273 0.3724 -0.0127 -0.0159 -0.0121 116 LEU A O   
771  C CB  . LEU A 99  ? 0.4385 0.3362 0.4237 0.0017  -0.0263 -0.0074 116 LEU A CB  
772  C CG  . LEU A 99  ? 0.4257 0.3370 0.4293 0.0256  -0.0327 -0.0103 116 LEU A CG  
773  C CD1 . LEU A 99  ? 0.4662 0.3593 0.4564 0.0339  -0.0460 0.0018  116 LEU A CD1 
774  C CD2 . LEU A 99  ? 0.4598 0.3566 0.4672 0.0429  -0.0291 -0.0221 116 LEU A CD2 
775  N N   . CYS A 100 ? 0.3467 0.3243 0.3652 -0.0061 -0.0306 0.0009  117 CYS A N   
776  C CA  . CYS A 100 ? 0.3454 0.3591 0.3881 -0.0036 -0.0303 -0.0042 117 CYS A CA  
777  C C   . CYS A 100 ? 0.3854 0.4103 0.4454 0.0147  -0.0388 -0.0081 117 CYS A C   
778  O O   . CYS A 100 ? 0.3707 0.3766 0.4191 0.0262  -0.0497 -0.0025 117 CYS A O   
779  C CB  . CYS A 100 ? 0.3279 0.3529 0.3658 -0.0131 -0.0328 0.0011  117 CYS A CB  
780  S SG  . CYS A 100 ? 0.3139 0.3357 0.3394 -0.0311 -0.0234 0.0047  117 CYS A SG  
781  N N   . LEU A 101 ? 0.3215 0.3784 0.4097 0.0173  -0.0339 -0.0172 118 LEU A N   
782  C CA  . LEU A 101 ? 0.3110 0.3906 0.4256 0.0342  -0.0407 -0.0233 118 LEU A CA  
783  C C   . LEU A 101 ? 0.2997 0.4165 0.4377 0.0265  -0.0433 -0.0266 118 LEU A C   
784  O O   . LEU A 101 ? 0.2817 0.4124 0.4269 0.0120  -0.0320 -0.0299 118 LEU A O   
785  C CB  . LEU A 101 ? 0.3281 0.4146 0.4586 0.0437  -0.0294 -0.0336 118 LEU A CB  
786  C CG  . LEU A 101 ? 0.3349 0.3796 0.4395 0.0495  -0.0261 -0.0332 118 LEU A CG  
787  C CD1 . LEU A 101 ? 0.3971 0.4487 0.5105 0.0524  -0.0102 -0.0453 118 LEU A CD1 
788  C CD2 . LEU A 101 ? 0.4075 0.4278 0.5043 0.0700  -0.0402 -0.0292 118 LEU A CD2 
789  N N   . PHE A 102 ? 0.2970 0.4263 0.4433 0.0355  -0.0595 -0.0255 119 PHE A N   
790  C CA  . PHE A 102 ? 0.2756 0.4359 0.4401 0.0264  -0.0654 -0.0293 119 PHE A CA  
791  C C   . PHE A 102 ? 0.2967 0.4929 0.4967 0.0409  -0.0776 -0.0365 119 PHE A C   
792  O O   . PHE A 102 ? 0.3105 0.4983 0.5073 0.0611  -0.0914 -0.0335 119 PHE A O   
793  C CB  . PHE A 102 ? 0.2908 0.4325 0.4253 0.0194  -0.0759 -0.0216 119 PHE A CB  
794  C CG  . PHE A 102 ? 0.2992 0.4663 0.4468 0.0098  -0.0837 -0.0273 119 PHE A CG  
795  C CD1 . PHE A 102 ? 0.2750 0.4505 0.4295 -0.0081 -0.0720 -0.0319 119 PHE A CD1 
796  C CD2 . PHE A 102 ? 0.3061 0.4852 0.4563 0.0186  -0.1043 -0.0281 119 PHE A CD2 
797  C CE1 . PHE A 102 ? 0.2639 0.4567 0.4280 -0.0186 -0.0793 -0.0382 119 PHE A CE1 
798  C CE2 . PHE A 102 ? 0.2844 0.4854 0.4451 0.0078  -0.1130 -0.0352 119 PHE A CE2 
799  C CZ  . PHE A 102 ? 0.2787 0.4853 0.4464 -0.0115 -0.1000 -0.0408 119 PHE A CZ  
800  N N   . ARG A 103 ? 0.2721 0.5082 0.5061 0.0304  -0.0737 -0.0457 120 ARG A N   
801  C CA  . ARG A 103 ? 0.2939 0.5747 0.5701 0.0419  -0.0849 -0.0542 120 ARG A CA  
802  C C   . ARG A 103 ? 0.3140 0.6117 0.5938 0.0339  -0.1045 -0.0556 120 ARG A C   
803  O O   . ARG A 103 ? 0.2517 0.5628 0.5396 0.0119  -0.0989 -0.0604 120 ARG A O   
804  C CB  . ARG A 103 ? 0.2570 0.5767 0.5734 0.0338  -0.0661 -0.0649 120 ARG A CB  
805  C CG  . ARG A 103 ? 0.2772 0.5820 0.5883 0.0424  -0.0466 -0.0660 120 ARG A CG  
806  C CD  . ARG A 103 ? 0.2874 0.6370 0.6406 0.0396  -0.0285 -0.0776 120 ARG A CD  
807  N NE  . ARG A 103 ? 0.2905 0.6679 0.6626 0.0131  -0.0207 -0.0809 120 ARG A NE  
808  C CZ  . ARG A 103 ? 0.2310 0.5874 0.5802 -0.0095 -0.0052 -0.0768 120 ARG A CZ  
809  N NH1 . ARG A 103 ? 0.2359 0.5472 0.5433 -0.0098 0.0019  -0.0692 120 ARG A NH1 
810  N NH2 . ARG A 103 ? 0.2425 0.6198 0.6080 -0.0324 0.0021  -0.0791 120 ARG A NH2 
811  N N   . PRO A 104 ? 0.3140 0.6083 0.5845 0.0507  -0.1283 -0.0518 121 PRO A N   
812  C CA  . PRO A 104 ? 0.3416 0.6538 0.6136 0.0432  -0.1492 -0.0550 121 PRO A CA  
813  C C   . PRO A 104 ? 0.3525 0.7175 0.6735 0.0326  -0.1500 -0.0668 121 PRO A C   
814  O O   . PRO A 104 ? 0.3173 0.6870 0.6326 0.0154  -0.1578 -0.0691 121 PRO A O   
815  C CB  . PRO A 104 ? 0.3301 0.6285 0.5828 0.0684  -0.1742 -0.0473 121 PRO A CB  
816  C CG  . PRO A 104 ? 0.3784 0.6300 0.5986 0.0799  -0.1630 -0.0362 121 PRO A CG  
817  C CD  . PRO A 104 ? 0.3612 0.6240 0.6080 0.0753  -0.1376 -0.0426 121 PRO A CD  
818  N N   . GLN A 105 ? 0.3002 0.6944 0.6592 0.0402  -0.1374 -0.0711 122 GLN A N   
819  C CA  . GLN A 105 ? 0.3296 0.7645 0.7258 0.0269  -0.1333 -0.0772 122 GLN A CA  
820  C C   . GLN A 105 ? 0.3236 0.7555 0.7189 -0.0047 -0.1147 -0.0801 122 GLN A C   
821  O O   . GLN A 105 ? 0.3298 0.7881 0.7496 -0.0211 -0.1129 -0.0841 122 GLN A O   
822  C CB  . GLN A 105 ? 0.3748 0.8415 0.8097 0.0446  -0.1231 -0.0812 122 GLN A CB  
823  C CG  . GLN A 105 ? 0.4221 0.9368 0.9003 0.0341  -0.1208 -0.0869 122 GLN A CG  
824  C CD  . GLN A 105 ? 0.5273 1.0746 1.0429 0.0562  -0.1128 -0.0911 122 GLN A CD  
825  O OE1 . GLN A 105 ? 0.5867 1.1162 1.0929 0.0814  -0.1109 -0.0900 122 GLN A OE1 
826  N NE2 . GLN A 105 ? 0.4547 1.0488 1.0126 0.0474  -0.1084 -0.0964 122 GLN A NE2 
827  N N   . SER A 106 ? 0.3125 0.7105 0.6786 -0.0136 -0.1025 -0.0774 123 SER A N   
828  C CA  . SER A 106 ? 0.3114 0.6946 0.6660 -0.0415 -0.0886 -0.0779 123 SER A CA  
829  C C   . SER A 106 ? 0.3332 0.7100 0.6751 -0.0562 -0.1052 -0.0798 123 SER A C   
830  O O   . SER A 106 ? 0.3469 0.7146 0.6857 -0.0791 -0.0962 -0.0816 123 SER A O   
831  C CB  . SER A 106 ? 0.3371 0.6843 0.6603 -0.0441 -0.0766 -0.0739 123 SER A CB  
832  O OG  . SER A 106 ? 0.3146 0.6305 0.6004 -0.0376 -0.0921 -0.0689 123 SER A OG  
833  N N   . GLY A 107 ? 0.3265 0.7036 0.6569 -0.0434 -0.1296 -0.0794 124 GLY A N   
834  C CA  . GLY A 107 ? 0.3218 0.6870 0.6311 -0.0562 -0.1458 -0.0823 124 GLY A CA  
835  C C   . GLY A 107 ? 0.3364 0.6593 0.6017 -0.0638 -0.1435 -0.0817 124 GLY A C   
836  O O   . GLY A 107 ? 0.3833 0.6920 0.6253 -0.0728 -0.1566 -0.0856 124 GLY A O   
837  N N   . ARG A 108 ? 0.3215 0.6250 0.5747 -0.0607 -0.1273 -0.0778 125 ARG A N   
838  C CA  . ARG A 108 ? 0.3549 0.6152 0.5634 -0.0648 -0.1217 -0.0737 125 ARG A CA  
839  C C   . ARG A 108 ? 0.3350 0.5722 0.5070 -0.0458 -0.1329 -0.0647 125 ARG A C   
840  O O   . ARG A 108 ? 0.2891 0.5366 0.4690 -0.0278 -0.1413 -0.0597 125 ARG A O   
841  C CB  . ARG A 108 ? 0.3613 0.6004 0.5630 -0.0690 -0.0963 -0.0670 125 ARG A CB  
842  C CG  . ARG A 108 ? 0.3981 0.6478 0.6237 -0.0888 -0.0809 -0.0721 125 ARG A CG  
843  C CD  . ARG A 108 ? 0.3673 0.6032 0.5882 -0.0862 -0.0591 -0.0639 125 ARG A CD  
844  N NE  . ARG A 108 ? 0.4017 0.6496 0.6442 -0.1036 -0.0431 -0.0668 125 ARG A NE  
845  C CZ  . ARG A 108 ? 0.4052 0.6324 0.6365 -0.1222 -0.0365 -0.0675 125 ARG A CZ  
846  N NH1 . ARG A 108 ? 0.4363 0.6322 0.6380 -0.1252 -0.0434 -0.0683 125 ARG A NH1 
847  N NH2 . ARG A 108 ? 0.4323 0.6625 0.6755 -0.1347 -0.0217 -0.0651 125 ARG A NH2 
848  N N   . VAL A 109 ? 0.3608 0.5646 0.4910 -0.0498 -0.1320 -0.0626 126 VAL A N   
849  C CA  . VAL A 109 ? 0.3351 0.5104 0.4250 -0.0365 -0.1337 -0.0518 126 VAL A CA  
850  C C   . VAL A 109 ? 0.3168 0.4685 0.3941 -0.0381 -0.1109 -0.0441 126 VAL A C   
851  O O   . VAL A 109 ? 0.2980 0.4382 0.3697 -0.0495 -0.0989 -0.0476 126 VAL A O   
852  C CB  . VAL A 109 ? 0.3611 0.5190 0.4119 -0.0390 -0.1461 -0.0553 126 VAL A CB  
853  C CG1 . VAL A 109 ? 0.3821 0.5132 0.3916 -0.0266 -0.1460 -0.0425 126 VAL A CG1 
854  C CG2 . VAL A 109 ? 0.3940 0.5780 0.4583 -0.0398 -0.1716 -0.0650 126 VAL A CG2 
855  N N   . LEU A 110 ? 0.2784 0.4215 0.3511 -0.0265 -0.1062 -0.0338 127 LEU A N   
856  C CA  . LEU A 110 ? 0.2995 0.4248 0.3641 -0.0289 -0.0870 -0.0273 127 LEU A CA  
857  C C   . LEU A 110 ? 0.2969 0.3992 0.3272 -0.0335 -0.0804 -0.0244 127 LEU A C   
858  O O   . LEU A 110 ? 0.3441 0.4354 0.3461 -0.0298 -0.0888 -0.0219 127 LEU A O   
859  C CB  . LEU A 110 ? 0.2648 0.3817 0.3278 -0.0170 -0.0855 -0.0183 127 LEU A CB  
860  C CG  . LEU A 110 ? 0.2760 0.3735 0.3268 -0.0204 -0.0689 -0.0115 127 LEU A CG  
861  C CD1 . LEU A 110 ? 0.2411 0.3494 0.3142 -0.0288 -0.0553 -0.0166 127 LEU A CD1 
862  C CD2 . LEU A 110 ? 0.2944 0.3773 0.3386 -0.0100 -0.0704 -0.0039 127 LEU A CD2 
863  N N   . SER A 111 ? 0.2558 0.3520 0.2883 -0.0407 -0.0652 -0.0251 128 SER A N   
864  C CA  . SER A 111 ? 0.2838 0.3637 0.2921 -0.0427 -0.0552 -0.0227 128 SER A CA  
865  C C   . SER A 111 ? 0.3081 0.3759 0.2882 -0.0375 -0.0563 -0.0143 128 SER A C   
866  O O   . SER A 111 ? 0.3024 0.3661 0.2828 -0.0335 -0.0564 -0.0059 128 SER A O   
867  C CB  . SER A 111 ? 0.2634 0.3417 0.2826 -0.0454 -0.0408 -0.0194 128 SER A CB  
868  O OG  . SER A 111 ? 0.2881 0.3575 0.2909 -0.0455 -0.0316 -0.0180 128 SER A OG  
869  N N   . ALA A 112 ? 0.2890 0.3479 0.2420 -0.0383 -0.0554 -0.0164 129 ALA A N   
870  C CA  . ALA A 112 ? 0.2956 0.3420 0.2182 -0.0361 -0.0524 -0.0072 129 ALA A CA  
871  C C   . ALA A 112 ? 0.3299 0.3751 0.2565 -0.0396 -0.0360 0.0001  129 ALA A C   
872  O O   . ALA A 112 ? 0.3403 0.3753 0.2494 -0.0410 -0.0325 0.0103  129 ALA A O   
873  C CB  . ALA A 112 ? 0.3220 0.3606 0.2119 -0.0365 -0.0528 -0.0128 129 ALA A CB  
874  N N   . MET A 113 ? 0.3139 0.3682 0.2627 -0.0420 -0.0271 -0.0043 130 MET A N   
875  C CA  . MET A 113 ? 0.3026 0.3604 0.2572 -0.0455 -0.0143 0.0014  130 MET A CA  
876  C C   . MET A 113 ? 0.3460 0.4008 0.3126 -0.0472 -0.0166 0.0082  130 MET A C   
877  O O   . MET A 113 ? 0.3380 0.3914 0.3033 -0.0525 -0.0090 0.0145  130 MET A O   
878  C CB  . MET A 113 ? 0.2944 0.3618 0.2655 -0.0449 -0.0065 -0.0048 130 MET A CB  
879  C CG  . MET A 113 ? 0.2990 0.3650 0.2548 -0.0413 -0.0018 -0.0126 130 MET A CG  
880  S SD  . MET A 113 ? 0.3292 0.3978 0.2598 -0.0422 0.0100  -0.0089 130 MET A SD  
881  C CE  . MET A 113 ? 0.3070 0.3967 0.2628 -0.0434 0.0237  -0.0060 130 MET A CE  
882  N N   . ILE A 114 ? 0.2824 0.3372 0.2616 -0.0431 -0.0264 0.0059  131 ILE A N   
883  C CA  . ILE A 114 ? 0.2791 0.3278 0.2664 -0.0416 -0.0288 0.0104  131 ILE A CA  
884  C C   . ILE A 114 ? 0.3081 0.3407 0.2767 -0.0360 -0.0383 0.0172  131 ILE A C   
885  O O   . ILE A 114 ? 0.3364 0.3517 0.2939 -0.0377 -0.0362 0.0250  131 ILE A O   
886  C CB  . ILE A 114 ? 0.2768 0.3371 0.2899 -0.0389 -0.0313 0.0035  131 ILE A CB  
887  C CG1 . ILE A 114 ? 0.2501 0.3193 0.2744 -0.0443 -0.0226 -0.0008 131 ILE A CG1 
888  C CG2 . ILE A 114 ? 0.2932 0.3465 0.3132 -0.0351 -0.0320 0.0058  131 ILE A CG2 
889  C CD1 . ILE A 114 ? 0.2396 0.3066 0.2607 -0.0489 -0.0140 0.0035  131 ILE A CD1 
890  N N   . ARG A 115 ? 0.3128 0.3481 0.2754 -0.0296 -0.0503 0.0147  132 ARG A N   
891  C CA  . ARG A 115 ? 0.3072 0.3251 0.2476 -0.0219 -0.0621 0.0226  132 ARG A CA  
892  C C   . ARG A 115 ? 0.3970 0.3933 0.3024 -0.0287 -0.0544 0.0335  132 ARG A C   
893  O O   . ARG A 115 ? 0.4173 0.3888 0.3040 -0.0269 -0.0571 0.0440  132 ARG A O   
894  C CB  . ARG A 115 ? 0.3570 0.3853 0.2945 -0.0152 -0.0781 0.0171  132 ARG A CB  
895  C CG  . ARG A 115 ? 0.4316 0.4440 0.3468 -0.0036 -0.0952 0.0253  132 ARG A CG  
896  C CD  . ARG A 115 ? 0.4538 0.4700 0.3947 0.0094  -0.1042 0.0251  132 ARG A CD  
897  N NE  . ARG A 115 ? 0.3991 0.4493 0.3769 0.0140  -0.1136 0.0127  132 ARG A NE  
898  C CZ  . ARG A 115 ? 0.4322 0.4970 0.4405 0.0260  -0.1199 0.0091  132 ARG A CZ  
899  N NH1 . ARG A 115 ? 0.4240 0.4676 0.4276 0.0372  -0.1196 0.0161  132 ARG A NH1 
900  N NH2 . ARG A 115 ? 0.3976 0.4986 0.4418 0.0268  -0.1266 -0.0026 132 ARG A NH2 
901  N N   . GLY A 116 ? 0.3520 0.3561 0.2474 -0.0368 -0.0437 0.0308  133 GLY A N   
902  C CA  . GLY A 116 ? 0.3782 0.3683 0.2421 -0.0448 -0.0332 0.0400  133 GLY A CA  
903  C C   . GLY A 116 ? 0.3658 0.3550 0.2385 -0.0562 -0.0183 0.0451  133 GLY A C   
904  O O   . GLY A 116 ? 0.4065 0.3847 0.2555 -0.0659 -0.0083 0.0540  133 GLY A O   
905  N N   . ALA A 117 ? 0.3503 0.3519 0.2551 -0.0570 -0.0163 0.0394  134 ALA A N   
906  C CA  . ALA A 117 ? 0.3762 0.3760 0.2895 -0.0682 -0.0064 0.0434  134 ALA A CA  
907  C C   . ALA A 117 ? 0.4330 0.4010 0.3314 -0.0697 -0.0117 0.0525  134 ALA A C   
908  O O   . ALA A 117 ? 0.4285 0.3863 0.3229 -0.0830 -0.0037 0.0578  134 ALA A O   
909  C CB  . ALA A 117 ? 0.3375 0.3574 0.2837 -0.0676 -0.0048 0.0343  134 ALA A CB  
910  N N   . ALA A 118 ? 0.4151 0.3669 0.3053 -0.0562 -0.0256 0.0540  135 ALA A N   
911  C CA  . ALA A 118 ? 0.4904 0.4083 0.3678 -0.0526 -0.0322 0.0613  135 ALA A CA  
912  C C   . ALA A 118 ? 0.5617 0.4469 0.4002 -0.0627 -0.0283 0.0761  135 ALA A C   
913  O O   . ALA A 118 ? 0.5557 0.4410 0.3698 -0.0649 -0.0265 0.0817  135 ALA A O   
914  C CB  . ALA A 118 ? 0.5137 0.4279 0.3959 -0.0321 -0.0492 0.0586  135 ALA A CB  
915  N N   . ASP A 119 ? 0.5639 0.4176 0.3932 -0.0700 -0.0263 0.0821  136 ASP A N   
916  C CA  . ASP A 119 ? 0.6506 0.4625 0.4395 -0.0804 -0.0236 0.0980  136 ASP A CA  
917  C C   . ASP A 119 ? 0.7016 0.4655 0.4726 -0.0673 -0.0368 0.1042  136 ASP A C   
918  O O   . ASP A 119 ? 0.7666 0.4846 0.5014 -0.0764 -0.0353 0.1184  136 ASP A O   
919  C CB  . ASP A 119 ? 0.6828 0.4973 0.4736 -0.1075 -0.0059 0.1005  136 ASP A CB  
920  C CG  . ASP A 119 ? 0.6561 0.4751 0.4758 -0.1130 -0.0049 0.0904  136 ASP A CG  
921  O OD1 . ASP A 119 ? 0.6708 0.4634 0.4904 -0.1003 -0.0154 0.0874  136 ASP A OD1 
922  O OD2 . ASP A 119 ? 0.6893 0.5392 0.5310 -0.1293 0.0061  0.0847  136 ASP A OD2 
923  N N   . GLY A 120 ? 0.6627 0.4354 0.4584 -0.0462 -0.0487 0.0939  137 GLY A N   
924  C CA  . GLY A 120 ? 0.7112 0.4431 0.4939 -0.0273 -0.0624 0.0977  137 GLY A CA  
925  C C   . GLY A 120 ? 0.7713 0.4658 0.5498 -0.0353 -0.0573 0.0967  137 GLY A C   
926  O O   . GLY A 120 ? 0.8227 0.4754 0.5868 -0.0184 -0.0678 0.0996  137 GLY A O   
927  N N   . SER A 121 ? 0.7469 0.4543 0.5370 -0.0595 -0.0428 0.0917  138 SER A N   
928  C CA  . SER A 121 ? 0.7390 0.4115 0.5240 -0.0712 -0.0386 0.0886  138 SER A CA  
929  C C   . SER A 121 ? 0.6838 0.3962 0.5042 -0.0808 -0.0309 0.0724  138 SER A C   
930  O O   . SER A 121 ? 0.7235 0.4421 0.5624 -0.0657 -0.0348 0.0596  138 SER A O   
931  C CB  A SER A 121 ? 0.8190 0.4544 0.5706 -0.0989 -0.0298 0.1031  138 SER A CB  
932  C CB  B SER A 121 ? 0.8197 0.4536 0.5707 -0.0985 -0.0301 0.1031  138 SER A CB  
933  O OG  A SER A 121 ? 0.7740 0.4532 0.5408 -0.1227 -0.0159 0.1024  138 SER A OG  
934  O OG  B SER A 121 ? 0.8353 0.4287 0.5785 -0.1104 -0.0284 0.0992  138 SER A OG  
935  N N   . ARG A 122 ? 0.6651 0.4059 0.4944 -0.1052 -0.0197 0.0730  139 ARG A N   
936  C CA  . ARG A 122 ? 0.6149 0.3924 0.4749 -0.1137 -0.0148 0.0591  139 ARG A CA  
937  C C   . ARG A 122 ? 0.5700 0.3971 0.4588 -0.0979 -0.0161 0.0505  139 ARG A C   
938  O O   . ARG A 122 ? 0.4861 0.3336 0.3956 -0.0953 -0.0158 0.0387  139 ARG A O   
939  C CB  . ARG A 122 ? 0.6278 0.4231 0.4921 -0.1431 -0.0041 0.0621  139 ARG A CB  
940  C CG  . ARG A 122 ? 0.5635 0.3830 0.4517 -0.1531 -0.0032 0.0489  139 ARG A CG  
941  C CD  . ARG A 122 ? 0.5979 0.4104 0.4825 -0.1842 0.0028  0.0514  139 ARG A CD  
942  N NE  . ARG A 122 ? 0.5732 0.4091 0.4789 -0.1935 0.0002  0.0381  139 ARG A NE  
943  C CZ  . ARG A 122 ? 0.5910 0.3940 0.4863 -0.1980 -0.0057 0.0292  139 ARG A CZ  
944  N NH1 . ARG A 122 ? 0.6283 0.3716 0.4941 -0.1941 -0.0087 0.0320  139 ARG A NH1 
945  N NH2 . ARG A 122 ? 0.6150 0.4429 0.5268 -0.2056 -0.0094 0.0169  139 ARG A NH2 
946  N N   . PHE A 123 ? 0.5222 0.3666 0.4097 -0.0890 -0.0175 0.0561  140 PHE A N   
947  C CA  . PHE A 123 ? 0.4797 0.3627 0.3911 -0.0741 -0.0202 0.0481  140 PHE A CA  
948  C C   . PHE A 123 ? 0.5242 0.3939 0.4265 -0.0532 -0.0316 0.0513  140 PHE A C   
949  O O   . PHE A 123 ? 0.5102 0.3687 0.3906 -0.0522 -0.0349 0.0614  140 PHE A O   
950  C CB  . PHE A 123 ? 0.4629 0.3820 0.3832 -0.0831 -0.0127 0.0488  140 PHE A CB  
951  C CG  . PHE A 123 ? 0.4049 0.3595 0.3497 -0.0723 -0.0142 0.0393  140 PHE A CG  
952  C CD1 . PHE A 123 ? 0.3905 0.3485 0.3396 -0.0556 -0.0229 0.0364  140 PHE A CD1 
953  C CD2 . PHE A 123 ? 0.3580 0.3416 0.3218 -0.0795 -0.0076 0.0335  140 PHE A CD2 
954  C CE1 . PHE A 123 ? 0.3630 0.3504 0.3336 -0.0499 -0.0232 0.0280  140 PHE A CE1 
955  C CE2 . PHE A 123 ? 0.3314 0.3397 0.3131 -0.0709 -0.0085 0.0262  140 PHE A CE2 
956  C CZ  . PHE A 123 ? 0.3368 0.3456 0.3213 -0.0579 -0.0154 0.0234  140 PHE A CZ  
957  N N   . GLN A 124 ? 0.4862 0.3587 0.4048 -0.0363 -0.0376 0.0425  141 GLN A N   
958  C CA  . GLN A 124 ? 0.5156 0.3796 0.4319 -0.0144 -0.0503 0.0442  141 GLN A CA  
959  C C   . GLN A 124 ? 0.4526 0.3604 0.4012 -0.0038 -0.0528 0.0335  141 GLN A C   
960  O O   . GLN A 124 ? 0.4298 0.3595 0.4006 -0.0075 -0.0451 0.0236  141 GLN A O   
961  C CB  . GLN A 124 ? 0.5871 0.4141 0.4961 -0.0015 -0.0549 0.0424  141 GLN A CB  
962  C CG  . GLN A 124 ? 0.6538 0.4276 0.5242 -0.0021 -0.0606 0.0567  141 GLN A CG  
963  C CD  . GLN A 124 ? 0.7322 0.4620 0.5930 0.0117  -0.0649 0.0539  141 GLN A CD  
964  O OE1 . GLN A 124 ? 0.7686 0.4663 0.6152 -0.0026 -0.0579 0.0529  141 GLN A OE1 
965  N NE2 . GLN A 124 ? 0.7575 0.4832 0.6241 0.0400  -0.0776 0.0527  141 GLN A NE2 
966  N N   . VAL A 125 ? 0.4351 0.3548 0.3843 0.0076  -0.0640 0.0358  142 VAL A N   
967  C CA  . VAL A 125 ? 0.4350 0.3950 0.4160 0.0161  -0.0682 0.0255  142 VAL A CA  
968  C C   . VAL A 125 ? 0.4648 0.4240 0.4536 0.0391  -0.0838 0.0249  142 VAL A C   
969  O O   . VAL A 125 ? 0.4603 0.4036 0.4269 0.0469  -0.0974 0.0341  142 VAL A O   
970  C CB  . VAL A 125 ? 0.4324 0.4157 0.4124 0.0068  -0.0688 0.0255  142 VAL A CB  
971  C CG1 . VAL A 125 ? 0.3992 0.4206 0.4126 0.0123  -0.0732 0.0142  142 VAL A CG1 
972  C CG2 . VAL A 125 ? 0.4210 0.4062 0.3949 -0.0118 -0.0541 0.0262  142 VAL A CG2 
973  N N   . TRP A 126 ? 0.4135 0.3922 0.4336 0.0507  -0.0822 0.0140  143 TRP A N   
974  C CA  . TRP A 126 ? 0.4548 0.4410 0.4912 0.0755  -0.0964 0.0112  143 TRP A CA  
975  C C   . TRP A 126 ? 0.4559 0.4964 0.5338 0.0787  -0.0999 0.0000  143 TRP A C   
976  O O   . TRP A 126 ? 0.4218 0.4890 0.5248 0.0692  -0.0858 -0.0098 143 TRP A O   
977  C CB  . TRP A 126 ? 0.5048 0.4707 0.5465 0.0902  -0.0913 0.0059  143 TRP A CB  
978  C CG  . TRP A 126 ? 0.5249 0.4331 0.5268 0.0880  -0.0904 0.0158  143 TRP A CG  
979  C CD1 . TRP A 126 ? 0.5782 0.4543 0.5424 0.0744  -0.0931 0.0301  143 TRP A CD1 
980  C CD2 . TRP A 126 ? 0.5811 0.4538 0.5751 0.0992  -0.0863 0.0118  143 TRP A CD2 
981  N NE1 . TRP A 126 ? 0.6119 0.4348 0.5465 0.0733  -0.0904 0.0361  143 TRP A NE1 
982  C CE2 . TRP A 126 ? 0.6108 0.4279 0.5617 0.0890  -0.0874 0.0246  143 TRP A CE2 
983  C CE3 . TRP A 126 ? 0.6053 0.4869 0.6231 0.1161  -0.0803 -0.0024 143 TRP A CE3 
984  C CZ2 . TRP A 126 ? 0.6654 0.4317 0.5955 0.0940  -0.0845 0.0236  143 TRP A CZ2 
985  C CZ3 . TRP A 126 ? 0.6688 0.5002 0.6646 0.1240  -0.0771 -0.0045 143 TRP A CZ3 
986  C CH2 . TRP A 126 ? 0.6673 0.4397 0.6192 0.1124  -0.0801 0.0083  143 TRP A CH2 
987  N N   . ASP A 127 ? 0.4495 0.5050 0.5328 0.0912  -0.1194 0.0019  144 ASP A N   
988  C CA  . ASP A 127 ? 0.4313 0.5401 0.5601 0.0976  -0.1260 -0.0099 144 ASP A CA  
989  C C   . ASP A 127 ? 0.4427 0.5659 0.6037 0.1201  -0.1245 -0.0183 144 ASP A C   
990  O O   . ASP A 127 ? 0.4942 0.5827 0.6380 0.1396  -0.1302 -0.0131 144 ASP A O   
991  C CB  . ASP A 127 ? 0.4142 0.5368 0.5397 0.1051  -0.1506 -0.0067 144 ASP A CB  
992  C CG  . ASP A 127 ? 0.4449 0.5594 0.5411 0.0840  -0.1514 -0.0021 144 ASP A CG  
993  O OD1 . ASP A 127 ? 0.4102 0.5230 0.5030 0.0636  -0.1332 -0.0043 144 ASP A OD1 
994  O OD2 . ASP A 127 ? 0.5112 0.6223 0.5876 0.0895  -0.1715 0.0030  144 ASP A OD2 
995  N N   . TYR A 128 ? 0.4487 0.6221 0.6557 0.1176  -0.1160 -0.0317 145 TYR A N   
996  C CA  . TYR A 128 ? 0.4414 0.6371 0.6838 0.1397  -0.1118 -0.0420 145 TYR A CA  
997  C C   . TYR A 128 ? 0.4115 0.6749 0.7091 0.1345  -0.1079 -0.0554 145 TYR A C   
998  O O   . TYR A 128 ? 0.3497 0.6337 0.6536 0.1096  -0.1033 -0.0571 145 TYR A O   
999  C CB  . TYR A 128 ? 0.4435 0.6091 0.6714 0.1381  -0.0895 -0.0451 145 TYR A CB  
1000 C CG  . TYR A 128 ? 0.3959 0.5839 0.6364 0.1142  -0.0662 -0.0526 145 TYR A CG  
1001 C CD1 . TYR A 128 ? 0.3641 0.5405 0.5819 0.0874  -0.0608 -0.0462 145 TYR A CD1 
1002 C CD2 . TYR A 128 ? 0.4406 0.6603 0.7138 0.1197  -0.0492 -0.0658 145 TYR A CD2 
1003 C CE1 . TYR A 128 ? 0.3296 0.5213 0.5548 0.0676  -0.0416 -0.0512 145 TYR A CE1 
1004 C CE2 . TYR A 128 ? 0.3790 0.6146 0.6574 0.0973  -0.0279 -0.0707 145 TYR A CE2 
1005 C CZ  . TYR A 128 ? 0.3392 0.5587 0.5925 0.0717  -0.0255 -0.0626 145 TYR A CZ  
1006 O OH  . TYR A 128 ? 0.3126 0.5427 0.5669 0.0512  -0.0065 -0.0656 145 TYR A OH  
1007 N N   . GLU A 129 ? 0.4403 0.7375 0.7784 0.1587  -0.1099 -0.0653 146 GLU A N   
1008 C CA  . GLU A 129 ? 0.4640 0.8295 0.8605 0.1542  -0.1000 -0.0798 146 GLU A CA  
1009 C C   . GLU A 129 ? 0.4623 0.8300 0.8684 0.1547  -0.0703 -0.0892 146 GLU A C   
1010 O O   . GLU A 129 ? 0.4819 0.8066 0.8612 0.1706  -0.0643 -0.0878 146 GLU A O   
1011 C CB  . GLU A 129 ? 0.4746 0.8704 0.8981 0.1732  -0.1168 -0.0799 146 GLU A CB  
1012 C CG  . GLU A 129 ? 0.5793 0.9551 1.0015 0.2090  -0.1207 -0.0800 146 GLU A CG  
1013 C CD  . GLU A 129 ? 0.6215 1.0423 1.0890 0.2194  -0.1047 -0.0911 146 GLU A CD  
1014 O OE1 . GLU A 129 ? 0.6483 1.0568 1.1187 0.2500  -0.1086 -0.0920 146 GLU A OE1 
1015 O OE2 . GLU A 129 ? 0.6024 1.0669 1.0997 0.1966  -0.0871 -0.0981 146 GLU A OE2 
1016 N N   . GLU A 130 ? 0.4351 1.0173 0.8888 -0.0721 -0.0678 -0.1082 147 GLU A N   
1017 C CA  . GLU A 130 ? 0.4596 1.0387 0.9258 -0.0719 -0.0188 -0.0908 147 GLU A CA  
1018 C C   . GLU A 130 ? 0.4324 1.0648 0.9216 -0.0159 -0.0212 -0.0934 147 GLU A C   
1019 O O   . GLU A 130 ? 0.4429 1.0328 0.8963 0.0030  0.0061  -0.0788 147 GLU A O   
1020 C CB  . GLU A 130 ? 0.3865 1.0223 0.9225 -0.1279 0.0187  -0.0940 147 GLU A CB  
1021 C CG  . GLU A 130 ? 0.4454 1.0254 0.9507 -0.1414 0.0691  -0.0649 147 GLU A CG  
1022 C CD  . GLU A 130 ? 0.3766 1.0354 0.9500 -0.1753 0.1119  -0.0606 147 GLU A CD  
1023 O OE1 . GLU A 130 ? 0.3698 1.0766 0.9533 -0.1483 0.1348  -0.0552 147 GLU A OE1 
1024 O OE2 . GLU A 130 ? 0.4075 1.0601 1.0084 -0.2262 0.1223  -0.0597 147 GLU A OE2 
1025 N N   . GLY A 131 ? 0.3939 1.1191 0.9418 0.0140  -0.0555 -0.1148 148 GLY A N   
1026 C CA  . GLY A 131 ? 0.3800 1.1621 0.9621 0.0722  -0.0551 -0.1231 148 GLY A CA  
1027 C C   . GLY A 131 ? 0.4025 1.0809 0.9003 0.1266  -0.0701 -0.1099 148 GLY A C   
1028 O O   . GLY A 131 ? 0.4543 1.1506 0.9651 0.1708  -0.0572 -0.1172 148 GLY A O   
1029 N N   . GLU A 132 ? 0.4704 1.0398 0.8817 0.1217  -0.0939 -0.0932 149 GLU A N   
1030 C CA  . GLU A 132 ? 0.5152 0.9837 0.8476 0.1672  -0.1117 -0.0798 149 GLU A CA  
1031 C C   . GLU A 132 ? 0.5100 0.8735 0.7680 0.1437  -0.0788 -0.0612 149 GLU A C   
1032 O O   . GLU A 132 ? 0.5390 0.8040 0.7212 0.1606  -0.0925 -0.0476 149 GLU A O   
1033 C CB  . GLU A 132 ? 0.5832 1.0097 0.8664 0.1838  -0.1650 -0.0720 149 GLU A CB  
1034 C CG  . GLU A 132 ? 0.5905 1.0051 0.8498 0.1290  -0.1712 -0.0705 149 GLU A CG  
1035 C CD  . GLU A 132 ? 0.6935 1.0268 0.8608 0.1379  -0.2106 -0.0556 149 GLU A CD  
1036 O OE1 . GLU A 132 ? 0.7333 1.0672 0.8797 0.0990  -0.2212 -0.0617 149 GLU A OE1 
1037 O OE2 . GLU A 132 ? 0.8134 1.0788 0.9253 0.1823  -0.2296 -0.0384 149 GLU A OE2 
1038 N N   . VAL A 133 ? 0.5074 0.8916 0.7859 0.1050  -0.0362 -0.0586 150 VAL A N   
1039 C CA  . VAL A 133 ? 0.5351 0.8314 0.7487 0.0829  -0.0118 -0.0405 150 VAL A CA  
1040 C C   . VAL A 133 ? 0.5081 0.7593 0.6841 0.1175  -0.0040 -0.0414 150 VAL A C   
1041 O O   . VAL A 133 ? 0.5370 0.6997 0.6470 0.1139  -0.0057 -0.0298 150 VAL A O   
1042 C CB  . VAL A 133 ? 0.4673 0.7917 0.7082 0.0365  0.0265  -0.0324 150 VAL A CB  
1043 C CG1 . VAL A 133 ? 0.4907 0.8653 0.7575 0.0437  0.0609  -0.0340 150 VAL A CG1 
1044 C CG2 . VAL A 133 ? 0.4396 0.6776 0.6217 0.0099  0.0364  -0.0138 150 VAL A CG2 
1045 N N   . GLU A 134 ? 0.4873 0.7996 0.7055 0.1505  0.0048  -0.0594 151 GLU A N   
1046 C CA  . GLU A 134 ? 0.5113 0.7746 0.6906 0.1833  0.0121  -0.0684 151 GLU A CA  
1047 C C   . GLU A 134 ? 0.5779 0.7501 0.7065 0.2177  -0.0242 -0.0661 151 GLU A C   
1048 O O   . GLU A 134 ? 0.6087 0.6903 0.6747 0.2172  -0.0213 -0.0620 151 GLU A O   
1049 C CB  . GLU A 134 ? 0.4970 0.8490 0.7328 0.2149  0.0324  -0.0943 151 GLU A CB  
1050 C CG  . GLU A 134 ? 0.4926 0.9156 0.7546 0.1790  0.0771  -0.0917 151 GLU A CG  
1051 C CD  . GLU A 134 ? 0.4671 0.9835 0.8022 0.1476  0.0845  -0.0872 151 GLU A CD  
1052 O OE1 . GLU A 134 ? 0.4416 0.9940 0.8212 0.1612  0.0531  -0.0956 151 GLU A OE1 
1053 O OE2 . GLU A 134 ? 0.4161 0.9688 0.7624 0.1078  0.1205  -0.0748 151 GLU A OE2 
1054 N N   . ALA A 135 ? 0.5788 0.7735 0.7320 0.2462  -0.0597 -0.0673 152 ALA A N   
1055 C CA  . ALA A 135 ? 0.6316 0.7308 0.7275 0.2811  -0.0962 -0.0571 152 ALA A CA  
1056 C C   . ALA A 135 ? 0.6782 0.6756 0.6917 0.2407  -0.0985 -0.0312 152 ALA A C   
1057 O O   . ALA A 135 ? 0.7298 0.6219 0.6776 0.2504  -0.1051 -0.0216 152 ALA A O   
1058 C CB  . ALA A 135 ? 0.6370 0.7909 0.7724 0.3177  -0.1391 -0.0583 152 ALA A CB  
1059 N N   . LEU A 136 ? 0.6421 0.6685 0.6601 0.1935  -0.0900 -0.0218 153 LEU A N   
1060 C CA  . LEU A 136 ? 0.6790 0.6231 0.6264 0.1571  -0.0872 -0.0017 153 LEU A CA  
1061 C C   . LEU A 136 ? 0.6927 0.5865 0.6106 0.1361  -0.0560 -0.0001 153 LEU A C   
1062 O O   . LEU A 136 ? 0.7514 0.5589 0.6065 0.1235  -0.0570 0.0127  153 LEU A O   
1063 C CB  . LEU A 136 ? 0.6604 0.6479 0.6246 0.1163  -0.0824 0.0005  153 LEU A CB  
1064 C CG  . LEU A 136 ? 0.7221 0.7408 0.6901 0.1255  -0.1205 -0.0008 153 LEU A CG  
1065 C CD1 . LEU A 136 ? 0.7090 0.7449 0.6764 0.0786  -0.1115 -0.0038 153 LEU A CD1 
1066 C CD2 . LEU A 136 ? 0.8166 0.7524 0.7072 0.1526  -0.1539 0.0175  153 LEU A CD2 
1067 N N   . LEU A 137 ? 0.6034 0.5542 0.5639 0.1289  -0.0284 -0.0122 154 LEU A N   
1068 C CA  . LEU A 137 ? 0.6670 0.5812 0.5987 0.1100  -0.0050 -0.0122 154 LEU A CA  
1069 C C   . LEU A 137 ? 0.7324 0.5776 0.6266 0.1368  -0.0131 -0.0235 154 LEU A C   
1070 O O   . LEU A 137 ? 0.7665 0.5448 0.6149 0.1158  -0.0076 -0.0199 154 LEU A O   
1071 C CB  . LEU A 137 ? 0.5943 0.5840 0.5680 0.0987  0.0235  -0.0189 154 LEU A CB  
1072 C CG  . LEU A 137 ? 0.5447 0.5742 0.5454 0.0649  0.0358  -0.0041 154 LEU A CG  
1073 C CD1 . LEU A 137 ? 0.5004 0.6142 0.5545 0.0617  0.0577  -0.0076 154 LEU A CD1 
1074 C CD2 . LEU A 137 ? 0.5623 0.5511 0.5310 0.0348  0.0475  0.0102  154 LEU A CD2 
1075 N N   . ASP A 138 ? 0.7205 0.5812 0.6378 0.1831  -0.0259 -0.0397 155 ASP A N   
1076 C CA  . ASP A 138 ? 0.7673 0.5438 0.6466 0.2141  -0.0357 -0.0524 155 ASP A CA  
1077 C C   . ASP A 138 ? 0.8808 0.5455 0.6934 0.2034  -0.0562 -0.0284 155 ASP A C   
1078 O O   . ASP A 138 ? 0.9510 0.5250 0.7142 0.1911  -0.0518 -0.0306 155 ASP A O   
1079 C CB  . ASP A 138 ? 0.7467 0.5591 0.6681 0.2750  -0.0497 -0.0724 155 ASP A CB  
1080 C CG  . ASP A 138 ? 0.7430 0.6553 0.7197 0.2865  -0.0211 -0.1015 155 ASP A CG  
1081 O OD1 . ASP A 138 ? 0.7234 0.6541 0.6884 0.2515  0.0066  -0.1059 155 ASP A OD1 
1082 O OD2 . ASP A 138 ? 0.7012 0.6776 0.7322 0.3325  -0.0266 -0.1196 155 ASP A OD2 
1083 N N   . ARG A 139 ? 0.8569 0.5280 0.6640 0.2035  -0.0776 -0.0059 156 ARG A N   
1084 C CA  . ARG A 139 ? 0.9439 0.5130 0.6774 0.1919  -0.0950 0.0218  156 ARG A CA  
1085 C C   . ARG A 139 ? 0.9079 0.4413 0.6040 0.1327  -0.0693 0.0319  156 ARG A C   
1086 O O   . ARG A 139 ? 1.0360 0.4704 0.6729 0.1156  -0.0676 0.0433  156 ARG A O   
1087 C CB  . ARG A 139 ? 0.9415 0.5444 0.6746 0.2031  -0.1237 0.0397  156 ARG A CB  
1088 C CG  . ARG A 139 ? 1.1149 0.6190 0.7613 0.1983  -0.1459 0.0726  156 ARG A CG  
1089 C CD  . ARG A 139 ? 1.1608 0.7208 0.8112 0.2138  -0.1793 0.0829  156 ARG A CD  
1090 N NE  . ARG A 139 ? 1.1194 0.7932 0.8619 0.2488  -0.1914 0.0576  156 ARG A NE  
1091 C CZ  . ARG A 139 ? 1.1002 0.8527 0.8747 0.2648  -0.2225 0.0553  156 ARG A CZ  
1092 N NH1 . ARG A 139 ? 1.1446 0.8725 0.8579 0.2532  -0.2490 0.0761  156 ARG A NH1 
1093 N NH2 . ARG A 139 ? 0.9901 0.8549 0.8598 0.2902  -0.2264 0.0294  156 ARG A NH2 
1094 N N   . TYR A 140 ? 0.8534 0.4666 0.5876 0.1009  -0.0481 0.0274  157 TYR A N   
1095 C CA  . TYR A 140 ? 0.8502 0.4468 0.5621 0.0513  -0.0248 0.0351  157 TYR A CA  
1096 C C   . TYR A 140 ? 0.8678 0.4306 0.5708 0.0366  -0.0098 0.0209  157 TYR A C   
1097 O O   . TYR A 140 ? 0.8962 0.4081 0.5637 0.0004  0.0007  0.0285  157 TYR A O   
1098 C CB  . TYR A 140 ? 0.7663 0.4510 0.5258 0.0309  -0.0081 0.0329  157 TYR A CB  
1099 C CG  . TYR A 140 ? 0.7533 0.4346 0.5025 -0.0110 0.0150  0.0388  157 TYR A CG  
1100 C CD1 . TYR A 140 ? 0.7599 0.4150 0.4740 -0.0342 0.0188  0.0523  157 TYR A CD1 
1101 C CD2 . TYR A 140 ? 0.7147 0.4283 0.4901 -0.0250 0.0327  0.0294  157 TYR A CD2 
1102 C CE1 . TYR A 140 ? 0.7786 0.4429 0.4935 -0.0685 0.0430  0.0539  157 TYR A CE1 
1103 C CE2 . TYR A 140 ? 0.7142 0.4383 0.4916 -0.0577 0.0507  0.0336  157 TYR A CE2 
1104 C CZ  . TYR A 140 ? 0.6952 0.3969 0.4476 -0.0783 0.0576  0.0447  157 TYR A CZ  
1105 O OH  . TYR A 140 ? 0.6907 0.4143 0.4547 -0.1070 0.0788  0.0452  157 TYR A OH  
1106 N N   . PHE A 141 ? 0.8575 0.4536 0.5918 0.0607  -0.0073 -0.0025 158 PHE A N   
1107 C CA  . PHE A 141 ? 0.8844 0.4591 0.6084 0.0451  0.0046  -0.0230 158 PHE A CA  
1108 C C   . PHE A 141 ? 1.0009 0.4754 0.6854 0.0663  -0.0074 -0.0372 158 PHE A C   
1109 O O   . PHE A 141 ? 1.0387 0.4930 0.7145 0.0584  -0.0001 -0.0641 158 PHE A O   
1110 C CB  . PHE A 141 ? 0.7877 0.4553 0.5556 0.0543  0.0180  -0.0422 158 PHE A CB  
1111 C CG  . PHE A 141 ? 0.7380 0.4796 0.5349 0.0262  0.0323  -0.0274 158 PHE A CG  
1112 C CD1 . PHE A 141 ? 0.7118 0.4565 0.5008 -0.0098 0.0413  -0.0259 158 PHE A CD1 
1113 C CD2 . PHE A 141 ? 0.6828 0.4896 0.5187 0.0361  0.0360  -0.0160 158 PHE A CD2 
1114 C CE1 . PHE A 141 ? 0.6400 0.4479 0.4585 -0.0266 0.0525  -0.0113 158 PHE A CE1 
1115 C CE2 . PHE A 141 ? 0.6387 0.4955 0.4984 0.0132  0.0495  -0.0015 158 PHE A CE2 
1116 C CZ  . PHE A 141 ? 0.5982 0.4535 0.4486 -0.0138 0.0572  0.0019  158 PHE A CZ  
1117 N N   . GLU A 142 ? 1.0523 0.4585 0.7086 0.0936  -0.0274 -0.0204 159 GLU A N   
1118 C CA  . GLU A 142 ? 1.1889 0.4794 0.8032 0.1182  -0.0401 -0.0291 159 GLU A CA  
1119 C C   . GLU A 142 ? 1.2751 0.4511 0.8232 0.0762  -0.0396 -0.0038 159 GLU A C   
1120 O O   . GLU A 142 ? 1.3527 0.5086 0.8924 0.0306  -0.0234 -0.0164 159 GLU A O   
1121 C CB  . GLU A 142 ? 1.2421 0.5239 0.8669 0.1845  -0.0660 -0.0243 159 GLU A CB  
1122 C CG  . GLU A 142 ? 1.2914 0.6086 0.9579 0.2359  -0.0644 -0.0642 159 GLU A CG  
1123 C CD  . GLU A 142 ? 1.2771 0.6274 0.9784 0.3032  -0.0895 -0.0607 159 GLU A CD  
1124 O OE1 . GLU A 142 ? 1.2597 0.6917 1.0181 0.3427  -0.0823 -0.0924 159 GLU A OE1 
1125 O OE2 . GLU A 142 ? 1.3306 0.6359 1.0034 0.3150  -0.1160 -0.0265 159 GLU A OE2 
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