data_9MRB
# 
_entry.id   9MRB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9MRB         pdb_00009mrb 10.2210/pdb9mrb/pdb 
WWPDB D_1000291578 ?            ?                   
# 
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 2025-02-19 ? 
2 'Structure model' 1 1 2025-04-02 ? 
3 'Structure model' 1 2 2025-04-30 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' '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 
3 3 'Structure model' citation        
4 3 '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.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
12 3 'Structure model' '_citation.journal_volume'          
13 3 'Structure model' '_citation_author.name'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9MRB 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-07 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              dabaker@uw.edu 
_pdbx_contact_author.name_first         David 
_pdbx_contact_author.name_last          Baker 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7896-6217 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Pellock, S.J.' 1 ? 
'Lauko, A.'     2 ? 
'Bera, A.'      3 ? 
'Baker, D.'     4 ? 
# 
_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            Science 
_citation.journal_id_ASTM           SCIEAS 
_citation.journal_id_CSD            0038 
_citation.journal_id_ISSN           1095-9203 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            388 
_citation.language                  ? 
_citation.page_first                eadu2454 
_citation.page_last                 eadu2454 
_citation.title                     'Computational design of serine hydrolases.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1126/science.adu2454 
_citation.pdbx_database_id_PubMed   39946508 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lauko, A.'         1  0000-0001-5903-3518 
primary 'Pellock, S.J.'     2  0000-0002-7557-7985 
primary 'Sumida, K.H.'      3  0000-0003-2773-9676 
primary 'Anishchenko, I.'   4  0000-0003-3645-2044 
primary 'Juergens, D.'      5  0000-0001-6425-8391 
primary 'Ahern, W.'         6  0009-0006-1247-8847 
primary 'Jeung, J.'         7  0009-0004-8604-908X 
primary 'Shida, A.F.'       8  0000-0003-4140-6085 
primary 'Hunt, A.'          9  0000-0001-9620-593X 
primary 'Kalvet, I.'        10 0000-0002-6610-2857 
primary 'Norn, C.'          11 0000-0002-1450-4651 
primary 'Humphreys, I.R.'   12 ?                   
primary 'Jamieson, C.'      13 ?                   
primary 'Krishna, R.'       14 0009-0003-6387-9622 
primary 'Kipnis, Y.'        15 0000-0002-3057-4916 
primary 'Kang, A.'          16 0000-0001-5487-0499 
primary 'Brackenbrough, E.' 17 0009-0004-1476-0219 
primary 'Bera, A.K.'        18 0000-0001-9473-2912 
primary 'Sankaran, B.'      19 0000-0002-3266-8131 
primary 'Houk, K.N.'        20 0000-0002-8387-5261 
primary 'Baker, D.'         21 0000-0001-7896-6217 
# 
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 dad_t1                 17939.246 1  ? ? ? ? 
2 non-polymer nat 'TETRAETHYLENE GLYCOL' 194.226   1  ? ? ? ? 
3 water       nat water                  18.015    37 ? ? ? ? 
# 
_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       
;MTEEEKAQAVEDFHKYHTALVVRLAGVPPHERYERLDRWITEQLIYGDESKRDEWIDALAEAAGIFKEALERNITTPEEF
NAFLKEKGKRAVDLVATLTNAYIAVLEGDPEAIARFLGISLEEVQEIIDAARKAVKEGRGASIGIYTKLRELEERRAA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTEEEKAQAVEDFHKYHTALVVRLAGVPPHERYERLDRWITEQLIYGDESKRDEWIDALAEAAGIFKEALERNITTPEEF
NAFLKEKGKRAVDLVATLTNAYIAVLEGDPEAIARFLGISLEEVQEIIDAARKAVKEGRGASIGIYTKLRELEERRAA
;
_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 'TETRAETHYLENE GLYCOL' PG4 
3 water                  HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   THR n 
1 3   GLU n 
1 4   GLU n 
1 5   GLU n 
1 6   LYS n 
1 7   ALA n 
1 8   GLN n 
1 9   ALA n 
1 10  VAL n 
1 11  GLU n 
1 12  ASP n 
1 13  PHE n 
1 14  HIS n 
1 15  LYS n 
1 16  TYR n 
1 17  HIS n 
1 18  THR n 
1 19  ALA n 
1 20  LEU n 
1 21  VAL n 
1 22  VAL n 
1 23  ARG n 
1 24  LEU n 
1 25  ALA n 
1 26  GLY n 
1 27  VAL n 
1 28  PRO n 
1 29  PRO n 
1 30  HIS n 
1 31  GLU n 
1 32  ARG n 
1 33  TYR n 
1 34  GLU n 
1 35  ARG n 
1 36  LEU n 
1 37  ASP n 
1 38  ARG n 
1 39  TRP n 
1 40  ILE n 
1 41  THR n 
1 42  GLU n 
1 43  GLN n 
1 44  LEU n 
1 45  ILE n 
1 46  TYR n 
1 47  GLY n 
1 48  ASP n 
1 49  GLU n 
1 50  SER n 
1 51  LYS n 
1 52  ARG n 
1 53  ASP n 
1 54  GLU n 
1 55  TRP n 
1 56  ILE n 
1 57  ASP n 
1 58  ALA n 
1 59  LEU n 
1 60  ALA n 
1 61  GLU n 
1 62  ALA n 
1 63  ALA n 
1 64  GLY n 
1 65  ILE n 
1 66  PHE n 
1 67  LYS n 
1 68  GLU n 
1 69  ALA n 
1 70  LEU n 
1 71  GLU n 
1 72  ARG n 
1 73  ASN n 
1 74  ILE n 
1 75  THR n 
1 76  THR n 
1 77  PRO n 
1 78  GLU n 
1 79  GLU n 
1 80  PHE n 
1 81  ASN n 
1 82  ALA n 
1 83  PHE n 
1 84  LEU n 
1 85  LYS n 
1 86  GLU n 
1 87  LYS n 
1 88  GLY n 
1 89  LYS n 
1 90  ARG n 
1 91  ALA n 
1 92  VAL n 
1 93  ASP n 
1 94  LEU n 
1 95  VAL n 
1 96  ALA n 
1 97  THR n 
1 98  LEU n 
1 99  THR n 
1 100 ASN n 
1 101 ALA n 
1 102 TYR n 
1 103 ILE n 
1 104 ALA n 
1 105 VAL n 
1 106 LEU n 
1 107 GLU n 
1 108 GLY n 
1 109 ASP n 
1 110 PRO n 
1 111 GLU n 
1 112 ALA n 
1 113 ILE n 
1 114 ALA n 
1 115 ARG n 
1 116 PHE n 
1 117 LEU n 
1 118 GLY n 
1 119 ILE n 
1 120 SER n 
1 121 LEU n 
1 122 GLU n 
1 123 GLU n 
1 124 VAL n 
1 125 GLN n 
1 126 GLU n 
1 127 ILE n 
1 128 ILE n 
1 129 ASP n 
1 130 ALA n 
1 131 ALA n 
1 132 ARG n 
1 133 LYS n 
1 134 ALA n 
1 135 VAL n 
1 136 LYS n 
1 137 GLU n 
1 138 GLY n 
1 139 ARG n 
1 140 GLY n 
1 141 ALA n 
1 142 SER n 
1 143 ILE n 
1 144 GLY n 
1 145 ILE n 
1 146 TYR n 
1 147 THR n 
1 148 LYS n 
1 149 LEU n 
1 150 ARG n 
1 151 GLU n 
1 152 LEU n 
1 153 GLU n 
1 154 GLU n 
1 155 ARG n 
1 156 ARG n 
1 157 ALA n 
1 158 ALA 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                   158 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'synthetic construct' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     32630 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE               ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE             ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ? 'C4 H7 N O4'     133.103 
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 
PG4 non-polymer         . 'TETRAETHYLENE GLYCOL' ? 'C8 H18 O5'      194.226 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   THR 2   2   ?   ?   ?   A . n 
A 1 3   GLU 3   3   ?   ?   ?   A . n 
A 1 4   GLU 4   4   ?   ?   ?   A . n 
A 1 5   GLU 5   5   ?   ?   ?   A . n 
A 1 6   LYS 6   6   ?   ?   ?   A . n 
A 1 7   ALA 7   7   ?   ?   ?   A . n 
A 1 8   GLN 8   8   ?   ?   ?   A . n 
A 1 9   ALA 9   9   9   ALA ALA A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  ASP 12  12  12  ASP ASP A . n 
A 1 13  PHE 13  13  13  PHE PHE A . n 
A 1 14  HIS 14  14  14  HIS HIS A . n 
A 1 15  LYS 15  15  15  LYS LYS A . n 
A 1 16  TYR 16  16  16  TYR TYR A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  THR 18  18  18  THR THR A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  VAL 22  22  22  VAL VAL A . n 
A 1 23  ARG 23  23  23  ARG ARG A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  VAL 27  27  27  VAL VAL A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  HIS 30  30  30  HIS HIS A . n 
A 1 31  GLU 31  31  31  GLU GLU A . n 
A 1 32  ARG 32  32  32  ARG ARG A . n 
A 1 33  TYR 33  33  33  TYR TYR A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  ASP 37  37  37  ASP ASP A . n 
A 1 38  ARG 38  38  38  ARG ARG A . n 
A 1 39  TRP 39  39  39  TRP TRP A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  THR 41  41  41  THR THR A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  GLN 43  43  43  GLN GLN A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  ILE 45  45  45  ILE ILE A . n 
A 1 46  TYR 46  46  46  TYR TYR A . n 
A 1 47  GLY 47  47  ?   ?   ?   A . n 
A 1 48  ASP 48  48  ?   ?   ?   A . n 
A 1 49  GLU 49  49  ?   ?   ?   A . n 
A 1 50  SER 50  50  ?   ?   ?   A . n 
A 1 51  LYS 51  51  ?   ?   ?   A . n 
A 1 52  ARG 52  52  52  ARG ARG A . n 
A 1 53  ASP 53  53  53  ASP ASP A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  TRP 55  55  55  TRP TRP A . n 
A 1 56  ILE 56  56  56  ILE ILE A . n 
A 1 57  ASP 57  57  57  ASP ASP A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  ALA 62  62  62  ALA ALA A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  GLU 68  68  68  GLU GLU A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  ARG 72  72  72  ARG ARG A . n 
A 1 73  ASN 73  73  73  ASN ASN A . n 
A 1 74  ILE 74  74  74  ILE ILE A . n 
A 1 75  THR 75  75  75  THR THR A . n 
A 1 76  THR 76  76  76  THR THR A . n 
A 1 77  PRO 77  77  77  PRO PRO A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  GLU 79  79  79  GLU GLU A . n 
A 1 80  PHE 80  80  80  PHE PHE A . n 
A 1 81  ASN 81  81  81  ASN ASN A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  PHE 83  83  83  PHE PHE A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  LYS 85  85  85  LYS LYS A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  ASP 93  93  93  ASP ASP A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  THR 97  97  97  THR THR A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 ASN 100 100 100 ASN ASN A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 TYR 102 102 102 TYR TYR A . n 
A 1 103 ILE 103 103 103 ILE ILE A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 VAL 105 105 105 VAL VAL A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 GLU 107 107 107 GLU GLU A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 PRO 110 110 110 PRO PRO A . n 
A 1 111 GLU 111 111 111 GLU GLU A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 GLY 118 118 118 GLY GLY A . n 
A 1 119 ILE 119 119 119 ILE ILE A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 GLU 122 122 122 GLU GLU A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 GLN 125 125 125 GLN GLN A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 ILE 127 127 127 ILE ILE A . n 
A 1 128 ILE 128 128 128 ILE ILE A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 ARG 132 132 132 ARG ARG A . n 
A 1 133 LYS 133 133 133 LYS LYS A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ARG 139 139 139 ARG ARG A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ILE 143 143 143 ILE ILE A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 TYR 146 146 146 TYR TYR A . n 
A 1 147 THR 147 147 147 THR THR A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 ARG 150 150 150 ARG ARG A . n 
A 1 151 GLU 151 151 151 GLU GLU A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 GLU 153 153 153 GLU GLU A . n 
A 1 154 GLU 154 154 154 GLU GLU A . n 
A 1 155 ARG 155 155 ?   ?   ?   A . n 
A 1 156 ARG 156 156 ?   ?   ?   A . n 
A 1 157 ALA 157 157 ?   ?   ?   A . n 
A 1 158 ALA 158 158 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 PG4 1  301 301 PG4 PG4 A . 
C 3 HOH 1  401 8   HOH HOH A . 
C 3 HOH 2  402 35  HOH HOH A . 
C 3 HOH 3  403 110 HOH HOH A . 
C 3 HOH 4  404 24  HOH HOH A . 
C 3 HOH 5  405 7   HOH HOH A . 
C 3 HOH 6  406 105 HOH HOH A . 
C 3 HOH 7  407 91  HOH HOH A . 
C 3 HOH 8  408 100 HOH HOH A . 
C 3 HOH 9  409 82  HOH HOH A . 
C 3 HOH 10 410 42  HOH HOH A . 
C 3 HOH 11 411 99  HOH HOH A . 
C 3 HOH 12 412 104 HOH HOH A . 
C 3 HOH 13 413 3   HOH HOH A . 
C 3 HOH 14 414 4   HOH HOH A . 
C 3 HOH 15 415 67  HOH HOH A . 
C 3 HOH 16 416 93  HOH HOH A . 
C 3 HOH 17 417 28  HOH HOH A . 
C 3 HOH 18 418 89  HOH HOH A . 
C 3 HOH 19 419 47  HOH HOH A . 
C 3 HOH 20 420 20  HOH HOH A . 
C 3 HOH 21 421 45  HOH HOH A . 
C 3 HOH 22 422 101 HOH HOH A . 
C 3 HOH 23 423 112 HOH HOH A . 
C 3 HOH 24 424 109 HOH HOH A . 
C 3 HOH 25 425 77  HOH HOH A . 
C 3 HOH 26 426 106 HOH HOH A . 
C 3 HOH 27 427 97  HOH HOH A . 
C 3 HOH 28 428 83  HOH HOH A . 
C 3 HOH 29 429 59  HOH HOH A . 
C 3 HOH 30 430 116 HOH HOH A . 
C 3 HOH 31 431 115 HOH HOH A . 
C 3 HOH 32 432 113 HOH HOH A . 
C 3 HOH 33 433 56  HOH HOH A . 
C 3 HOH 34 434 102 HOH HOH A . 
C 3 HOH 35 435 107 HOH HOH A . 
C 3 HOH 36 436 111 HOH HOH A . 
C 3 HOH 37 437 98  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  ? ? ? 1.21_5207 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .         4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   97.226 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MRB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.424 
_cell.length_a_esd                 ? 
_cell.length_b                     56.721 
_cell.length_b_esd                 ? 
_cell.length_c                     51.595 
_cell.length_c_esd                 ? 
_cell.volume                       123168.614 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9MRB 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y' 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_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                   9MRB 
_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             1.72 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          28.34 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M Potassium chloride, 0.02M Tris pH7.0, 20% PEG4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-09-16 
_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   0.97934 
_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-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97934 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-2 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          28.66 
_reflns.entry_id                                       9MRB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.00 
_reflns.d_resolution_low                               51.19 
_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                                     8217 
_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                           98.77 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.04 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.09992 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.992 
_reflns.pdbx_CC_star                                   0.998 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1852 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.0 
_reflns_shell.d_res_low                                     2.13 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.92 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1357 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               4.4 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.7874 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.566 
_reflns_shell.pdbx_CC_star                                  0.85 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.62 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.494 
_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                               31.02 
_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                                 9MRB 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.00 
_refine.ls_d_res_low                             51.19 
_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                     8173 
_refine.ls_number_reflns_R_free                  818 
_refine.ls_number_reflns_R_work                  7355 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.77 
_refine.ls_percent_reflns_R_free                 10.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2171 
_refine.ls_R_factor_R_free                       0.2573 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2127 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.8149 
_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                            0.2112 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        51.19 
_refine_hist.number_atoms_solvent             37 
_refine_hist.number_atoms_total               1181 
_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        1131 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         13 
_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' ? 0.0018  ? 1162 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.3959  ? 1565 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0342  ? 175  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0041  ? 201  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.3099 ? 439  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.00 2.13  . . 136 1219 98.69 . . . . 0.2665 . . . . . . . . . . . 0.3125 
'X-RAY DIFFRACTION' 2.13 2.29  . . 133 1201 98.31 . . . . 0.2361 . . . . . . . . . . . 0.3178 
'X-RAY DIFFRACTION' 2.29 2.52  . . 137 1231 98.63 . . . . 0.2201 . . . . . . . . . . . 0.2798 
'X-RAY DIFFRACTION' 2.52 2.89  . . 136 1222 99.49 . . . . 0.2114 . . . . . . . . . . . 0.2511 
'X-RAY DIFFRACTION' 2.89 3.64  . . 136 1227 98.77 . . . . 0.2203 . . . . . . . . . . . 0.2410 
'X-RAY DIFFRACTION' 3.64 51.19 . . 140 1255 98.80 . . . . 0.1925 . . . . . . . . . . . 0.2389 
# 
_struct.entry_id                     9MRB 
_struct.title                        'The designed serine hydrolase known as dad_t1' 
_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        9MRB 
_struct_keywords.text            'enzyme, serine hydrolase, DE NOVO PROTEIN' 
_struct_keywords.pdbx_keywords   'DE NOVO PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9MRB 
_struct_ref.pdbx_db_accession          9MRB 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9MRB 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 158 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             9MRB 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  158 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       158 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_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                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ALA A 9   ? GLY A 26  ? ALA A 9   GLY A 26  1 ? 18 
HELX_P HELX_P2 AA2 HIS A 30  ? TYR A 46  ? HIS A 30  TYR A 46  1 ? 17 
HELX_P HELX_P3 AA3 ASP A 53  ? GLU A 71  ? ASP A 53  GLU A 71  1 ? 19 
HELX_P HELX_P4 AA4 THR A 76  ? GLY A 88  ? THR A 76  GLY A 88  1 ? 13 
HELX_P HELX_P5 AA5 GLY A 88  ? ASP A 109 ? GLY A 88  ASP A 109 1 ? 22 
HELX_P HELX_P6 AA6 ASP A 109 ? GLY A 118 ? ASP A 109 GLY A 118 1 ? 10 
HELX_P HELX_P7 AA7 SER A 120 ? GLU A 137 ? SER A 120 GLU A 137 1 ? 18 
HELX_P HELX_P8 AA8 GLY A 140 ? GLU A 154 ? GLY A 140 GLU A 154 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_pdbx_entry_details.entry_id                   9MRB 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     423 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   C 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 -x,y,-z         
3 x+1/2,y+1/2,z   
4 -x+1/2,y+1/2,-z 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A THR 2   ? A THR 2   
3  1 Y 1 A GLU 3   ? A GLU 3   
4  1 Y 1 A GLU 4   ? A GLU 4   
5  1 Y 1 A GLU 5   ? A GLU 5   
6  1 Y 1 A LYS 6   ? A LYS 6   
7  1 Y 1 A ALA 7   ? A ALA 7   
8  1 Y 1 A GLN 8   ? A GLN 8   
9  1 Y 1 A GLY 47  ? A GLY 47  
10 1 Y 1 A ASP 48  ? A ASP 48  
11 1 Y 1 A GLU 49  ? A GLU 49  
12 1 Y 1 A SER 50  ? A SER 50  
13 1 Y 1 A LYS 51  ? A LYS 51  
14 1 Y 1 A ARG 155 ? A ARG 155 
15 1 Y 1 A ARG 156 ? A ARG 156 
16 1 Y 1 A ALA 157 ? A ALA 157 
17 1 Y 1 A ALA 158 ? A ALA 158 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HIS N    N N N 123 
HIS CA   C N S 124 
HIS C    C N N 125 
HIS O    O N N 126 
HIS CB   C N N 127 
HIS CG   C Y N 128 
HIS ND1  N Y N 129 
HIS CD2  C Y N 130 
HIS CE1  C Y N 131 
HIS NE2  N Y N 132 
HIS OXT  O N N 133 
HIS H    H N N 134 
HIS H2   H N N 135 
HIS HA   H N N 136 
HIS HB2  H N N 137 
HIS HB3  H N N 138 
HIS HD1  H N N 139 
HIS HD2  H N N 140 
HIS HE1  H N N 141 
HIS HE2  H N N 142 
HIS HXT  H N N 143 
HOH O    O N N 144 
HOH H1   H N N 145 
HOH H2   H N N 146 
ILE N    N N N 147 
ILE CA   C N S 148 
ILE C    C N N 149 
ILE O    O N N 150 
ILE CB   C N S 151 
ILE CG1  C N N 152 
ILE CG2  C N N 153 
ILE CD1  C N N 154 
ILE OXT  O N N 155 
ILE H    H N N 156 
ILE H2   H N N 157 
ILE HA   H N N 158 
ILE HB   H N N 159 
ILE HG12 H N N 160 
ILE HG13 H N N 161 
ILE HG21 H N N 162 
ILE HG22 H N N 163 
ILE HG23 H N N 164 
ILE HD11 H N N 165 
ILE HD12 H N N 166 
ILE HD13 H N N 167 
ILE HXT  H N N 168 
LEU N    N N N 169 
LEU CA   C N S 170 
LEU C    C N N 171 
LEU O    O N N 172 
LEU CB   C N N 173 
LEU CG   C N N 174 
LEU CD1  C N N 175 
LEU CD2  C N N 176 
LEU OXT  O N N 177 
LEU H    H N N 178 
LEU H2   H N N 179 
LEU HA   H N N 180 
LEU HB2  H N N 181 
LEU HB3  H N N 182 
LEU HG   H N N 183 
LEU HD11 H N N 184 
LEU HD12 H N N 185 
LEU HD13 H N N 186 
LEU HD21 H N N 187 
LEU HD22 H N N 188 
LEU HD23 H N N 189 
LEU HXT  H N N 190 
LYS N    N N N 191 
LYS CA   C N S 192 
LYS C    C N N 193 
LYS O    O N N 194 
LYS CB   C N N 195 
LYS CG   C N N 196 
LYS CD   C N N 197 
LYS CE   C N N 198 
LYS NZ   N N N 199 
LYS OXT  O N N 200 
LYS H    H N N 201 
LYS H2   H N N 202 
LYS HA   H N N 203 
LYS HB2  H N N 204 
LYS HB3  H N N 205 
LYS HG2  H N N 206 
LYS HG3  H N N 207 
LYS HD2  H N N 208 
LYS HD3  H N N 209 
LYS HE2  H N N 210 
LYS HE3  H N N 211 
LYS HZ1  H N N 212 
LYS HZ2  H N N 213 
LYS HZ3  H N N 214 
LYS HXT  H N N 215 
MET N    N N N 216 
MET CA   C N S 217 
MET C    C N N 218 
MET O    O N N 219 
MET CB   C N N 220 
MET CG   C N N 221 
MET SD   S N N 222 
MET CE   C N N 223 
MET OXT  O N N 224 
MET H    H N N 225 
MET H2   H N N 226 
MET HA   H N N 227 
MET HB2  H N N 228 
MET HB3  H N N 229 
MET HG2  H N N 230 
MET HG3  H N N 231 
MET HE1  H N N 232 
MET HE2  H N N 233 
MET HE3  H N N 234 
MET HXT  H N N 235 
PG4 O1   O N N 236 
PG4 C1   C N N 237 
PG4 C2   C N N 238 
PG4 O2   O N N 239 
PG4 C3   C N N 240 
PG4 C4   C N N 241 
PG4 O3   O N N 242 
PG4 C5   C N N 243 
PG4 C6   C N N 244 
PG4 O4   O N N 245 
PG4 C7   C N N 246 
PG4 C8   C N N 247 
PG4 O5   O N N 248 
PG4 HO1  H N N 249 
PG4 H11  H N N 250 
PG4 H12  H N N 251 
PG4 H21  H N N 252 
PG4 H22  H N N 253 
PG4 H31  H N N 254 
PG4 H32  H N N 255 
PG4 H41  H N N 256 
PG4 H42  H N N 257 
PG4 H51  H N N 258 
PG4 H52  H N N 259 
PG4 H61  H N N 260 
PG4 H62  H N N 261 
PG4 H71  H N N 262 
PG4 H72  H N N 263 
PG4 H81  H N N 264 
PG4 H82  H N N 265 
PG4 HO5  H N N 266 
PHE N    N N N 267 
PHE CA   C N S 268 
PHE C    C N N 269 
PHE O    O N N 270 
PHE CB   C N N 271 
PHE CG   C Y N 272 
PHE CD1  C Y N 273 
PHE CD2  C Y N 274 
PHE CE1  C Y N 275 
PHE CE2  C Y N 276 
PHE CZ   C Y N 277 
PHE OXT  O N N 278 
PHE H    H N N 279 
PHE H2   H N N 280 
PHE HA   H N N 281 
PHE HB2  H N N 282 
PHE HB3  H N N 283 
PHE HD1  H N N 284 
PHE HD2  H N N 285 
PHE HE1  H N N 286 
PHE HE2  H N N 287 
PHE HZ   H N N 288 
PHE HXT  H N N 289 
PRO N    N N N 290 
PRO CA   C N S 291 
PRO C    C N N 292 
PRO O    O N N 293 
PRO CB   C N N 294 
PRO CG   C N N 295 
PRO CD   C N N 296 
PRO OXT  O N N 297 
PRO H    H N N 298 
PRO HA   H N N 299 
PRO HB2  H N N 300 
PRO HB3  H N N 301 
PRO HG2  H N N 302 
PRO HG3  H N N 303 
PRO HD2  H N N 304 
PRO HD3  H N N 305 
PRO HXT  H N N 306 
SER N    N N N 307 
SER CA   C N S 308 
SER C    C N N 309 
SER O    O N N 310 
SER CB   C N N 311 
SER OG   O N N 312 
SER OXT  O N N 313 
SER H    H N N 314 
SER H2   H N N 315 
SER HA   H N N 316 
SER HB2  H N N 317 
SER HB3  H N N 318 
SER HG   H N N 319 
SER HXT  H N N 320 
THR N    N N N 321 
THR CA   C N S 322 
THR C    C N N 323 
THR O    O N N 324 
THR CB   C N R 325 
THR OG1  O N N 326 
THR CG2  C N N 327 
THR OXT  O N N 328 
THR H    H N N 329 
THR H2   H N N 330 
THR HA   H N N 331 
THR HB   H N N 332 
THR HG1  H N N 333 
THR HG21 H N N 334 
THR HG22 H N N 335 
THR HG23 H N N 336 
THR HXT  H N N 337 
TRP N    N N N 338 
TRP CA   C N S 339 
TRP C    C N N 340 
TRP O    O N N 341 
TRP CB   C N N 342 
TRP CG   C Y N 343 
TRP CD1  C Y N 344 
TRP CD2  C Y N 345 
TRP NE1  N Y N 346 
TRP CE2  C Y N 347 
TRP CE3  C Y N 348 
TRP CZ2  C Y N 349 
TRP CZ3  C Y N 350 
TRP CH2  C Y N 351 
TRP OXT  O N N 352 
TRP H    H N N 353 
TRP H2   H N N 354 
TRP HA   H N N 355 
TRP HB2  H N N 356 
TRP HB3  H N N 357 
TRP HD1  H N N 358 
TRP HE1  H N N 359 
TRP HE3  H N N 360 
TRP HZ2  H N N 361 
TRP HZ3  H N N 362 
TRP HH2  H N N 363 
TRP HXT  H N N 364 
TYR N    N N N 365 
TYR CA   C N S 366 
TYR C    C N N 367 
TYR O    O N N 368 
TYR CB   C N N 369 
TYR CG   C Y N 370 
TYR CD1  C Y N 371 
TYR CD2  C Y N 372 
TYR CE1  C Y N 373 
TYR CE2  C Y N 374 
TYR CZ   C Y N 375 
TYR OH   O N N 376 
TYR OXT  O N N 377 
TYR H    H N N 378 
TYR H2   H N N 379 
TYR HA   H N N 380 
TYR HB2  H N N 381 
TYR HB3  H N N 382 
TYR HD1  H N N 383 
TYR HD2  H N N 384 
TYR HE1  H N N 385 
TYR HE2  H N N 386 
TYR HH   H N N 387 
TYR HXT  H N N 388 
VAL N    N N N 389 
VAL CA   C N S 390 
VAL C    C N N 391 
VAL O    O N N 392 
VAL CB   C N N 393 
VAL CG1  C N N 394 
VAL CG2  C N N 395 
VAL OXT  O N N 396 
VAL H    H N N 397 
VAL H2   H N N 398 
VAL HA   H N N 399 
VAL HB   H N N 400 
VAL HG11 H N N 401 
VAL HG12 H N N 402 
VAL HG13 H N N 403 
VAL HG21 H N N 404 
VAL HG22 H N N 405 
VAL HG23 H N N 406 
VAL HXT  H N N 407 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PG4 O1  C1   sing N N 224 
PG4 O1  HO1  sing N N 225 
PG4 C1  C2   sing N N 226 
PG4 C1  H11  sing N N 227 
PG4 C1  H12  sing N N 228 
PG4 C2  O2   sing N N 229 
PG4 C2  H21  sing N N 230 
PG4 C2  H22  sing N N 231 
PG4 O2  C3   sing N N 232 
PG4 C3  C4   sing N N 233 
PG4 C3  H31  sing N N 234 
PG4 C3  H32  sing N N 235 
PG4 C4  O3   sing N N 236 
PG4 C4  H41  sing N N 237 
PG4 C4  H42  sing N N 238 
PG4 O3  C5   sing N N 239 
PG4 C5  C6   sing N N 240 
PG4 C5  H51  sing N N 241 
PG4 C5  H52  sing N N 242 
PG4 C6  O4   sing N N 243 
PG4 C6  H61  sing N N 244 
PG4 C6  H62  sing N N 245 
PG4 O4  C7   sing N N 246 
PG4 C7  C8   sing N N 247 
PG4 C7  H71  sing N N 248 
PG4 C7  H72  sing N N 249 
PG4 C8  O5   sing N N 250 
PG4 C8  H81  sing N N 251 
PG4 C8  H82  sing N N 252 
PG4 O5  HO5  sing N N 253 
PHE N   CA   sing N N 254 
PHE N   H    sing N N 255 
PHE N   H2   sing N N 256 
PHE CA  C    sing N N 257 
PHE CA  CB   sing N N 258 
PHE CA  HA   sing N N 259 
PHE C   O    doub N N 260 
PHE C   OXT  sing N N 261 
PHE CB  CG   sing N N 262 
PHE CB  HB2  sing N N 263 
PHE CB  HB3  sing N N 264 
PHE CG  CD1  doub Y N 265 
PHE CG  CD2  sing Y N 266 
PHE CD1 CE1  sing Y N 267 
PHE CD1 HD1  sing N N 268 
PHE CD2 CE2  doub Y N 269 
PHE CD2 HD2  sing N N 270 
PHE CE1 CZ   doub Y N 271 
PHE CE1 HE1  sing N N 272 
PHE CE2 CZ   sing Y N 273 
PHE CE2 HE2  sing N N 274 
PHE CZ  HZ   sing N N 275 
PHE OXT HXT  sing N N 276 
PRO N   CA   sing N N 277 
PRO N   CD   sing N N 278 
PRO N   H    sing N N 279 
PRO CA  C    sing N N 280 
PRO CA  CB   sing N N 281 
PRO CA  HA   sing N N 282 
PRO C   O    doub N N 283 
PRO C   OXT  sing N N 284 
PRO CB  CG   sing N N 285 
PRO CB  HB2  sing N N 286 
PRO CB  HB3  sing N N 287 
PRO CG  CD   sing N N 288 
PRO CG  HG2  sing N N 289 
PRO CG  HG3  sing N N 290 
PRO CD  HD2  sing N N 291 
PRO CD  HD3  sing N N 292 
PRO OXT HXT  sing N N 293 
SER N   CA   sing N N 294 
SER N   H    sing N N 295 
SER N   H2   sing N N 296 
SER CA  C    sing N N 297 
SER CA  CB   sing N N 298 
SER CA  HA   sing N N 299 
SER C   O    doub N N 300 
SER C   OXT  sing N N 301 
SER CB  OG   sing N N 302 
SER CB  HB2  sing N N 303 
SER CB  HB3  sing N N 304 
SER OG  HG   sing N N 305 
SER OXT HXT  sing N N 306 
THR N   CA   sing N N 307 
THR N   H    sing N N 308 
THR N   H2   sing N N 309 
THR CA  C    sing N N 310 
THR CA  CB   sing N N 311 
THR CA  HA   sing N N 312 
THR C   O    doub N N 313 
THR C   OXT  sing N N 314 
THR CB  OG1  sing N N 315 
THR CB  CG2  sing N N 316 
THR CB  HB   sing N N 317 
THR OG1 HG1  sing N N 318 
THR CG2 HG21 sing N N 319 
THR CG2 HG22 sing N N 320 
THR CG2 HG23 sing N N 321 
THR OXT HXT  sing N N 322 
TRP N   CA   sing N N 323 
TRP N   H    sing N N 324 
TRP N   H2   sing N N 325 
TRP CA  C    sing N N 326 
TRP CA  CB   sing N N 327 
TRP CA  HA   sing N N 328 
TRP C   O    doub N N 329 
TRP C   OXT  sing N N 330 
TRP CB  CG   sing N N 331 
TRP CB  HB2  sing N N 332 
TRP CB  HB3  sing N N 333 
TRP CG  CD1  doub Y N 334 
TRP CG  CD2  sing Y N 335 
TRP CD1 NE1  sing Y N 336 
TRP CD1 HD1  sing N N 337 
TRP CD2 CE2  doub Y N 338 
TRP CD2 CE3  sing Y N 339 
TRP NE1 CE2  sing Y N 340 
TRP NE1 HE1  sing N N 341 
TRP CE2 CZ2  sing Y N 342 
TRP CE3 CZ3  doub Y N 343 
TRP CE3 HE3  sing N N 344 
TRP CZ2 CH2  doub Y N 345 
TRP CZ2 HZ2  sing N N 346 
TRP CZ3 CH2  sing Y N 347 
TRP CZ3 HZ3  sing N N 348 
TRP CH2 HH2  sing N N 349 
TRP OXT HXT  sing N N 350 
TYR N   CA   sing N N 351 
TYR N   H    sing N N 352 
TYR N   H2   sing N N 353 
TYR CA  C    sing N N 354 
TYR CA  CB   sing N N 355 
TYR CA  HA   sing N N 356 
TYR C   O    doub N N 357 
TYR C   OXT  sing N N 358 
TYR CB  CG   sing N N 359 
TYR CB  HB2  sing N N 360 
TYR CB  HB3  sing N N 361 
TYR CG  CD1  doub Y N 362 
TYR CG  CD2  sing Y N 363 
TYR CD1 CE1  sing Y N 364 
TYR CD1 HD1  sing N N 365 
TYR CD2 CE2  doub Y N 366 
TYR CD2 HD2  sing N N 367 
TYR CE1 CZ   doub Y N 368 
TYR CE1 HE1  sing N N 369 
TYR CE2 CZ   sing Y N 370 
TYR CE2 HE2  sing N N 371 
TYR CZ  OH   sing N N 372 
TYR OH  HH   sing N N 373 
TYR OXT HXT  sing N N 374 
VAL N   CA   sing N N 375 
VAL N   H    sing N N 376 
VAL N   H2   sing N N 377 
VAL CA  C    sing N N 378 
VAL CA  CB   sing N N 379 
VAL CA  HA   sing N N 380 
VAL C   O    doub N N 381 
VAL C   OXT  sing N N 382 
VAL CB  CG1  sing N N 383 
VAL CB  CG2  sing N N 384 
VAL CB  HB   sing N N 385 
VAL CG1 HG11 sing N N 386 
VAL CG1 HG12 sing N N 387 
VAL CG1 HG13 sing N N 388 
VAL CG2 HG21 sing N N 389 
VAL CG2 HG22 sing N N 390 
VAL CG2 HG23 sing N N 391 
VAL OXT HXT  sing N N 392 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Howard Hughes Medical Institute (HHMI)'                                                   'United States' ? 1 
'Other private'                                                                            ?               ? 2 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' ? 3 
'Defense Advanced Research Projects Agency (DARPA)'                                        'United States' ? 4 
'Defense Threat Reduction Agency (DTRA)'                                                   'United States' ? 5 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 1 2 1' 
_space_group.name_Hall        'C 2y' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9MRB 
_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]   0.023572 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002989 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017630 
_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]   0.019537 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . ALA A 1 9   ? -4.13400  -8.52600  5.71000  1.000 36.87549 ? 9   ALA A N   1 
ATOM   2    C CA  . ALA A 1 9   ? -4.13100  -7.19600  6.30900  1.000 41.12533 ? 9   ALA A CA  1 
ATOM   3    C C   . ALA A 1 9   ? -2.97500  -7.04800  7.29200  1.000 42.71844 ? 9   ALA A C   1 
ATOM   4    O O   . ALA A 1 9   ? -2.37700  -5.97600  7.40200  1.000 40.23684 ? 9   ALA A O   1 
ATOM   5    C CB  . ALA A 1 9   ? -5.45500  -6.91900  7.00200  1.000 43.27440 ? 9   ALA A CB  1 
ATOM   6    N N   . VAL A 1 10  ? -2.67200  -8.13000  8.01300  1.000 39.41556 ? 10  VAL A N   1 
ATOM   7    C CA  . VAL A 1 10  ? -1.52700  -8.12300  8.92000  1.000 40.79450 ? 10  VAL A CA  1 
ATOM   8    C C   . VAL A 1 10  ? -0.24200  -7.91400  8.13300  1.000 43.44771 ? 10  VAL A C   1 
ATOM   9    O O   . VAL A 1 10  ? 0.60000   -7.07900  8.48500  1.000 41.12023 ? 10  VAL A O   1 
ATOM   10   C CB  . VAL A 1 10  ? -1.47900  -9.42600  9.73700  1.000 40.39128 ? 10  VAL A CB  1 
ATOM   11   C CG1 . VAL A 1 10  ? -0.16000  -9.53600  10.48900 1.000 46.20319 ? 10  VAL A CG1 1 
ATOM   12   C CG2 . VAL A 1 10  ? -2.65600  -9.49100  10.69000 1.000 43.33653 ? 10  VAL A CG2 1 
ATOM   13   N N   . GLU A 1 11  ? -0.07600  -8.68100  7.05400  1.000 47.15990 ? 11  GLU A N   1 
ATOM   14   C CA  . GLU A 1 11  ? 1.06400   -8.49900  6.16400  1.000 40.87898 ? 11  GLU A CA  1 
ATOM   15   C C   . GLU A 1 11  ? 1.05400   -7.11700  5.52300  1.000 41.05874 ? 11  GLU A C   1 
ATOM   16   O O   . GLU A 1 11  ? 2.11800   -6.52400  5.30800  1.000 40.23157 ? 11  GLU A O   1 
ATOM   17   C CB  . GLU A 1 11  ? 1.05300   -9.59800  5.09800  1.000 41.79675 ? 11  GLU A CB  1 
ATOM   18   C CG  . GLU A 1 11  ? 1.81500   -9.27800  3.82100  1.000 45.30066 ? 11  GLU A CG  1 
ATOM   19   C CD  . GLU A 1 11  ? 3.31000   -9.43200  3.98000  1.000 49.98073 ? 11  GLU A CD  1 
ATOM   20   O OE1 . GLU A 1 11  ? 3.73900   -10.09000 4.95200  1.000 57.34336 ? 11  GLU A OE1 1 
ATOM   21   O OE2 . GLU A 1 11  ? 4.06000   -8.89500  3.13400  1.000 52.02281 ? 11  GLU A OE2 1 
ATOM   22   N N   . ASP A 1 12  ? -0.13200  -6.58100  5.22700  1.000 36.10511 ? 12  ASP A N   1 
ATOM   23   C CA  . ASP A 1 12  ? -0.25100  -5.27800  4.58600  1.000 36.09043 ? 12  ASP A CA  1 
ATOM   24   C C   . ASP A 1 12  ? -0.01500  -4.11200  5.53400  1.000 34.26413 ? 12  ASP A C   1 
ATOM   25   O O   . ASP A 1 12  ? 0.14300   -2.98100  5.05900  1.000 31.68082 ? 12  ASP A O   1 
ATOM   26   C CB  . ASP A 1 12  ? -1.63400  -5.12600  3.94900  1.000 35.65025 ? 12  ASP A CB  1 
ATOM   27   C CG  . ASP A 1 12  ? -1.77900  -5.92500  2.67300  1.000 35.96257 ? 12  ASP A CG  1 
ATOM   28   O OD1 . ASP A 1 12  ? -0.77400  -6.51100  2.22100  1.000 32.69288 ? 12  ASP A OD1 1 
ATOM   29   O OD2 . ASP A 1 12  ? -2.90000  -5.96700  2.12400  1.000 36.64101 ? 12  ASP A OD2 1 
ATOM   30   N N   . PHE A 1 13  ? 0.00700   -4.34800  6.84800  1.000 31.39187 ? 13  PHE A N   1 
ATOM   31   C CA  . PHE A 1 13  ? 0.13300   -3.23800  7.78800  1.000 30.95937 ? 13  PHE A CA  1 
ATOM   32   C C   . PHE A 1 13  ? 1.43800   -2.48300  7.58000  1.000 28.51607 ? 13  PHE A C   1 
ATOM   33   O O   . PHE A 1 13  ? 1.44400   -1.25100  7.50000  1.000 28.21069 ? 13  PHE A O   1 
ATOM   34   C CB  . PHE A 1 13  ? 0.03300   -3.73100  9.23100  1.000 30.72419 ? 13  PHE A CB  1 
ATOM   35   C CG  . PHE A 1 13  ? 0.42200   -2.68700  10.24500 1.000 28.80771 ? 13  PHE A CG  1 
ATOM   36   C CD1 . PHE A 1 13  ? -0.46200  -1.67900  10.59700 1.000 23.17778 ? 13  PHE A CD1 1 
ATOM   37   C CD2 . PHE A 1 13  ? 1.67900   -2.70200  10.83000 1.000 24.92621 ? 13  PHE A CD2 1 
ATOM   38   C CE1 . PHE A 1 13  ? -0.10400  -0.71100  11.51900 1.000 27.17490 ? 13  PHE A CE1 1 
ATOM   39   C CE2 . PHE A 1 13  ? 2.04400   -1.73600  11.75100 1.000 28.57942 ? 13  PHE A CE2 1 
ATOM   40   C CZ  . PHE A 1 13  ? 1.15000   -0.74000  12.09800 1.000 25.87993 ? 13  PHE A CZ  1 
ATOM   41   N N   . HIS A 1 14  ? 2.55800   -3.20400  7.49300  1.000 27.95987 ? 14  HIS A N   1 
ATOM   42   C CA  . HIS A 1 14  ? 3.84600   -2.53000  7.37800  1.000 29.44982 ? 14  HIS A CA  1 
ATOM   43   C C   . HIS A 1 14  ? 4.02900   -1.85500  6.02300  1.000 28.83897 ? 14  HIS A C   1 
ATOM   44   O O   . HIS A 1 14  ? 4.83600   -0.92600  5.91400  1.000 28.58872 ? 14  HIS A O   1 
ATOM   45   C CB  . HIS A 1 14  ? 4.99100   -3.51400  7.64500  1.000 31.36850 ? 14  HIS A CB  1 
ATOM   46   C CG  . HIS A 1 14  ? 5.34300   -4.37300  6.47100  1.000 28.65734 ? 14  HIS A CG  1 
ATOM   47   N ND1 . HIS A 1 14  ? 4.66700   -5.53500  6.16800  1.000 34.11708 ? 14  HIS A ND1 1 
ATOM   48   C CD2 . HIS A 1 14  ? 6.30600   -4.24200  5.52900  1.000 35.38543 ? 14  HIS A CD2 1 
ATOM   49   C CE1 . HIS A 1 14  ? 5.19500   -6.08000  5.08600  1.000 41.64300 ? 14  HIS A CE1 1 
ATOM   50   N NE2 . HIS A 1 14  ? 6.19100   -5.31500  4.67900  1.000 41.18761 ? 14  HIS A NE2 1 
ATOM   51   N N   . LYS A 1 15  ? 3.29800   -2.28700  4.99400  1.000 30.57541 ? 15  LYS A N   1 
ATOM   52   C CA  . LYS A 1 15  ? 3.34600   -1.58600  3.71400  1.000 27.44760 ? 15  LYS A CA  1 
ATOM   53   C C   . LYS A 1 15  ? 2.66900   -0.22400  3.81200  1.000 24.91485 ? 15  LYS A C   1 
ATOM   54   O O   . LYS A 1 15  ? 3.23600   0.79400   3.40100  1.000 22.03882 ? 15  LYS A O   1 
ATOM   55   C CB  . LYS A 1 15  ? 2.68900   -2.43000  2.62200  1.000 33.79772 ? 15  LYS A CB  1 
ATOM   56   C CG  . LYS A 1 15  ? 3.32100   -3.79300  2.41100  1.000 34.50369 ? 15  LYS A CG  1 
ATOM   57   C CD  . LYS A 1 15  ? 2.47000   -4.63000  1.46800  1.000 35.96159 ? 15  LYS A CD  1 
ATOM   58   C CE  . LYS A 1 15  ? 2.93500   -6.07500  1.43600  1.000 43.75437 ? 15  LYS A CE  1 
ATOM   59   N NZ  . LYS A 1 15  ? 1.91000   -6.95900  0.81300  1.000 36.59301 ? 15  LYS A NZ  1 
ATOM   60   N N   . TYR A 1 16  ? 1.45100   -0.18700  4.35800  1.000 23.90197 ? 16  TYR A N   1 
ATOM   61   C CA  . TYR A 1 16  ? 0.72700   1.07500   4.48600  1.000 24.14857 ? 16  TYR A CA  1 
ATOM   62   C C   . TYR A 1 16  ? 1.33900   1.96100   5.56300  1.000 23.49666 ? 16  TYR A C   1 
ATOM   63   O O   . TYR A 1 16  ? 1.45100   3.17900   5.38300  1.000 20.30050 ? 16  TYR A O   1 
ATOM   64   C CB  . TYR A 1 16  ? -0.74300  0.80300   4.80000  1.000 21.37819 ? 16  TYR A CB  1 
ATOM   65   C CG  . TYR A 1 16  ? -1.50800  0.16400   3.66700  1.000 26.30872 ? 16  TYR A CG  1 
ATOM   66   C CD1 . TYR A 1 16  ? -1.42700  0.67200   2.37800  1.000 29.35906 ? 16  TYR A CD1 1 
ATOM   67   C CD2 . TYR A 1 16  ? -2.31000  -0.95000  3.88500  1.000 27.23787 ? 16  TYR A CD2 1 
ATOM   68   C CE1 . TYR A 1 16  ? -2.12500  0.09300   1.33700  1.000 32.30862 ? 16  TYR A CE1 1 
ATOM   69   C CE2 . TYR A 1 16  ? -3.01100  -1.53800  2.85000  1.000 31.27878 ? 16  TYR A CE2 1 
ATOM   70   C CZ  . TYR A 1 16  ? -2.91500  -1.01200  1.57700  1.000 31.99230 ? 16  TYR A CZ  1 
ATOM   71   O OH  . TYR A 1 16  ? -3.61100  -1.58800  0.53900  1.000 32.04185 ? 16  TYR A OH  1 
ATOM   72   N N   . HIS A 1 17  ? 1.72500   1.36600   6.69300  1.000 20.43026 ? 17  HIS A N   1 
ATOM   73   C CA  . HIS A 1 17  ? 2.29200   2.13500   7.79600  1.000 27.33162 ? 17  HIS A CA  1 
ATOM   74   C C   . HIS A 1 17  ? 3.59100   2.81700   7.38100  1.000 22.91889 ? 17  HIS A C   1 
ATOM   75   O O   . HIS A 1 17  ? 3.75600   4.02600   7.57300  1.000 21.58188 ? 17  HIS A O   1 
ATOM   76   C CB  . HIS A 1 17  ? 2.50900   1.22000   9.00300  1.000 24.92175 ? 17  HIS A CB  1 
ATOM   77   C CG  . HIS A 1 17  ? 3.24600   1.86700   10.13300 1.000 25.69477 ? 17  HIS A CG  1 
ATOM   78   N ND1 . HIS A 1 17  ? 4.56200   1.57900   10.41900 1.000 21.43350 ? 17  HIS A ND1 1 
ATOM   79   C CD2 . HIS A 1 17  ? 2.85300   2.78400   11.04800 1.000 23.67033 ? 17  HIS A CD2 1 
ATOM   80   C CE1 . HIS A 1 17  ? 4.95000   2.29200   11.46200 1.000 27.61314 ? 17  HIS A CE1 1 
ATOM   81   N NE2 . HIS A 1 17  ? 3.93200   3.03000   11.86300 1.000 23.59973 ? 17  HIS A NE2 1 
ATOM   82   N N   . THR A 1 18  ? 4.52200   2.05900   6.79300  1.000 22.15300 ? 18  THR A N   1 
ATOM   83   C CA  . THR A 1 18  ? 5.79000   2.64800   6.36400  1.000 25.53418 ? 18  THR A CA  1 
ATOM   84   C C   . THR A 1 18  ? 5.57500   3.71500   5.29900  1.000 23.88095 ? 18  THR A C   1 
ATOM   85   O O   . THR A 1 18  ? 6.23400   4.76100   5.31800  1.000 18.92075 ? 18  THR A O   1 
ATOM   86   C CB  . THR A 1 18  ? 6.73400   1.56900   5.83200  1.000 28.86539 ? 18  THR A CB  1 
ATOM   87   O OG1 . THR A 1 18  ? 7.12200   0.70100   6.90000  1.000 28.88792 ? 18  THR A OG1 1 
ATOM   88   C CG2 . THR A 1 18  ? 7.98300   2.20000   5.22700  1.000 26.16089 ? 18  THR A CG2 1 
ATOM   89   N N   . ALA A 1 19  ? 4.66300   3.46500   4.35700  1.000 23.34994 ? 19  ALA A N   1 
ATOM   90   C CA  . ALA A 1 19  ? 4.44400   4.41900   3.27600  1.000 20.80277 ? 19  ALA A CA  1 
ATOM   91   C C   . ALA A 1 19  ? 3.95100   5.75700   3.81100  1.000 22.45941 ? 19  ALA A C   1 
ATOM   92   O O   . ALA A 1 19  ? 4.38100   6.81700   3.34100  1.000 20.54875 ? 19  ALA A O   1 
ATOM   93   C CB  . ALA A 1 19  ? 3.45500   3.84800   2.26100  1.000 18.40218 ? 19  ALA A CB  1 
ATOM   94   N N   . LEU A 1 20  ? 3.04600   5.73300   4.79400  1.000 17.92463 ? 20  LEU A N   1 
ATOM   95   C CA  . LEU A 1 20  ? 2.57000   6.98500   5.37100  1.000 19.47017 ? 20  LEU A CA  1 
ATOM   96   C C   . LEU A 1 20  ? 3.66200   7.66400   6.18800  1.000 19.23384 ? 20  LEU A C   1 
ATOM   97   O O   . LEU A 1 20  ? 3.85000   8.88200   6.08900  1.000 16.57479 ? 20  LEU A O   1 
ATOM   98   C CB  . LEU A 1 20  ? 1.33300   6.74300   6.23500  1.000 22.19799 ? 20  LEU A CB  1 
ATOM   99   C CG  . LEU A 1 20  ? 0.68000   8.03700   6.73700  1.000 21.64119 ? 20  LEU A CG  1 
ATOM   100  C CD1 . LEU A 1 20  ? -0.02500  8.77100   5.59900  1.000 23.16406 ? 20  LEU A CD1 1 
ATOM   101  C CD2 . LEU A 1 20  ? -0.28100  7.75800   7.87900  1.000 21.52963 ? 20  LEU A CD2 1 
ATOM   102  N N   . VAL A 1 21  ? 4.39600   6.89400   6.99200  1.000 16.05341 ? 21  VAL A N   1 
ATOM   103  C CA  . VAL A 1 21  ? 5.43200   7.48000   7.84000  1.000 20.29269 ? 21  VAL A CA  1 
ATOM   104  C C   . VAL A 1 21  ? 6.52800   8.11700   6.99500  1.000 18.93338 ? 21  VAL A C   1 
ATOM   105  O O   . VAL A 1 21  ? 7.04300   9.19000   7.33100  1.000 21.16855 ? 21  VAL A O   1 
ATOM   106  C CB  . VAL A 1 21  ? 6.00200   6.42400   8.80300  1.000 19.68953 ? 21  VAL A CB  1 
ATOM   107  C CG1 . VAL A 1 21  ? 7.12100   7.02800   9.63700  1.000 17.33315 ? 21  VAL A CG1 1 
ATOM   108  C CG2 . VAL A 1 21  ? 4.91200   5.90000   9.71100  1.000 21.09073 ? 21  VAL A CG2 1 
ATOM   109  N N   . VAL A 1 22  ? 6.90500   7.47100   5.88800  1.000 18.71803 ? 22  VAL A N   1 
ATOM   110  C CA  . VAL A 1 22  ? 7.91000   8.05000   4.99900  1.000 21.48138 ? 22  VAL A CA  1 
ATOM   111  C C   . VAL A 1 22  ? 7.38800   9.33800   4.37000  1.000 23.73782 ? 22  VAL A C   1 
ATOM   112  O O   . VAL A 1 22  ? 8.12200   10.32600  4.24300  1.000 21.93044 ? 22  VAL A O   1 
ATOM   113  C CB  . VAL A 1 22  ? 8.34200   7.02500   3.93000  1.000 24.10626 ? 22  VAL A CB  1 
ATOM   114  C CG1 . VAL A 1 22  ? 9.17200   7.69600   2.84400  1.000 20.32251 ? 22  VAL A CG1 1 
ATOM   115  C CG2 . VAL A 1 22  ? 9.13300   5.88400   4.56600  1.000 20.10785 ? 22  VAL A CG2 1 
ATOM   116  N N   . ARG A 1 23  ? 6.11100   9.35300   3.97400  1.000 21.89290 ? 23  ARG A N   1 
ATOM   117  C CA  . ARG A 1 23  ? 5.52900   10.57100  3.41500  1.000 23.12311 ? 23  ARG A CA  1 
ATOM   118  C C   . ARG A 1 23  ? 5.52600   11.70300  4.43700  1.000 23.33843 ? 23  ARG A C   1 
ATOM   119  O O   . ARG A 1 23  ? 5.86500   12.84900  4.11500  1.000 23.33154 ? 23  ARG A O   1 
ATOM   120  C CB  . ARG A 1 23  ? 4.10900   10.30300  2.91000  1.000 17.93947 ? 23  ARG A CB  1 
ATOM   121  C CG  . ARG A 1 23  ? 3.31100   11.58800  2.67700  1.000 29.09503 ? 23  ARG A CG  1 
ATOM   122  C CD  . ARG A 1 23  ? 2.11900   11.40500  1.74600  1.000 29.12181 ? 23  ARG A CD  1 
ATOM   123  N NE  . ARG A 1 23  ? 0.99600   10.68700  2.33700  1.000 34.82077 ? 23  ARG A NE  1 
ATOM   124  C CZ  . ARG A 1 23  ? -0.27700  10.97800  2.10300  1.000 34.89556 ? 23  ARG A CZ  1 
ATOM   125  N NH1 . ARG A 1 23  ? -0.62200  11.99900  1.33600  1.000 33.19428 ? 23  ARG A NH1 1 
ATOM   126  N NH2 . ARG A 1 23  ? -1.22700  10.22300  2.64600  1.000 29.77857 ? 23  ARG A NH2 1 
ATOM   127  N N   . LEU A 1 24  ? 5.14500   11.40000  5.68100  1.000 18.29339 ? 24  LEU A N   1 
ATOM   128  C CA  . LEU A 1 24  ? 5.04300   12.43500  6.70300  1.000 20.78892 ? 24  LEU A CA  1 
ATOM   129  C C   . LEU A 1 24  ? 6.40600   12.83500  7.25200  1.000 24.75393 ? 24  LEU A C   1 
ATOM   130  O O   . LEU A 1 24  ? 6.58000   13.97700  7.69300  1.000 22.48546 ? 24  LEU A O   1 
ATOM   131  C CB  . LEU A 1 24  ? 4.13400   11.96500  7.84000  1.000 21.79158 ? 24  LEU A CB  1 
ATOM   132  C CG  . LEU A 1 24  ? 2.72900   11.49300  7.44800  1.000 27.41469 ? 24  LEU A CG  1 
ATOM   133  C CD1 . LEU A 1 24  ? 1.89800   11.16900  8.67800  1.000 20.78304 ? 24  LEU A CD1 1 
ATOM   134  C CD2 . LEU A 1 24  ? 2.01400   12.51100  6.56900  1.000 26.84676 ? 24  LEU A CD2 1 
ATOM   135  N N   . ALA A 1 25  ? 7.37800   11.92200  7.24100  1.000 20.00244 ? 25  ALA A N   1 
ATOM   136  C CA  . ALA A 1 25  ? 8.72800   12.27000  7.65700  1.000 23.43582 ? 25  ALA A CA  1 
ATOM   137  C C   . ALA A 1 25  ? 9.49400   13.00700  6.56900  1.000 27.17950 ? 25  ALA A C   1 
ATOM   138  O O   . ALA A 1 25  ? 10.47000  13.70000  6.87700  1.000 29.33122 ? 25  ALA A O   1 
ATOM   139  C CB  . ALA A 1 25  ? 9.50000   11.01500  8.07300  1.000 24.60003 ? 25  ALA A CB  1 
ATOM   140  N N   . GLY A 1 26  ? 9.07300   12.87700  5.31300  1.000 25.79313 ? 26  GLY A N   1 
ATOM   141  C CA  . GLY A 1 26  ? 9.73400   13.55600  4.22100  1.000 26.87131 ? 26  GLY A CA  1 
ATOM   142  C C   . GLY A 1 26  ? 11.06700  12.97400  3.81900  1.000 29.95249 ? 26  GLY A C   1 
ATOM   143  O O   . GLY A 1 26  ? 11.78500  13.59900  3.03400  1.000 34.20278 ? 26  GLY A O   1 
ATOM   144  N N   . VAL A 1 27  ? 11.42400  11.80000  4.33200  1.000 28.07849 ? 27  VAL A N   1 
ATOM   145  C CA  . VAL A 1 27  ? 12.68200  11.15100  3.97100  1.000 29.18742 ? 27  VAL A CA  1 
ATOM   146  C C   . VAL A 1 27  ? 12.51600  10.49400  2.60600  1.000 29.92393 ? 27  VAL A C   1 
ATOM   147  O O   . VAL A 1 27  ? 11.39600  10.10400  2.24200  1.000 33.66413 ? 27  VAL A O   1 
ATOM   148  C CB  . VAL A 1 27  ? 13.11400  10.12900  5.03600  1.000 32.87044 ? 27  VAL A CB  1 
ATOM   149  C CG1 . VAL A 1 27  ? 13.43000  10.83300  6.34800  1.000 29.84946 ? 27  VAL A CG1 1 
ATOM   150  C CG2 . VAL A 1 27  ? 12.03500  9.07500   5.24000  1.000 26.38213 ? 27  VAL A CG2 1 
ATOM   151  N N   . PRO A 1 28  ? 13.57900  10.36800  1.81700  1.000 32.51146 ? 28  PRO A N   1 
ATOM   152  C CA  . PRO A 1 28  ? 13.47200  9.67000   0.53300  1.000 32.12886 ? 28  PRO A CA  1 
ATOM   153  C C   . PRO A 1 28  ? 13.01000  8.23900   0.73400  1.000 31.00131 ? 28  PRO A C   1 
ATOM   154  O O   . PRO A 1 28  ? 13.36100  7.59900   1.73600  1.000 25.72648 ? 28  PRO A O   1 
ATOM   155  C CB  . PRO A 1 28  ? 14.90600  9.71800   -0.01700 1.000 31.20742 ? 28  PRO A CB  1 
ATOM   156  C CG  . PRO A 1 28  ? 15.52500  10.89500  0.64900  1.000 27.72354 ? 28  PRO A CG  1 
ATOM   157  C CD  . PRO A 1 28  ? 14.91700  10.95000  2.02100  1.000 27.57221 ? 28  PRO A CD  1 
ATOM   158  N N   . PRO A 1 29  ? 12.20100  7.71100   -0.18200 1.000 31.50287 ? 29  PRO A N   1 
ATOM   159  C CA  . PRO A 1 29  ? 11.80900  6.30100   -0.08600 1.000 34.94206 ? 29  PRO A CA  1 
ATOM   160  C C   . PRO A 1 29  ? 13.01800  5.39000   -0.22700 1.000 29.44671 ? 29  PRO A C   1 
ATOM   161  O O   . PRO A 1 29  ? 13.90600  5.62500   -1.05000 1.000 38.06494 ? 29  PRO A O   1 
ATOM   162  C CB  . PRO A 1 29  ? 10.82600  6.12400   -1.24800 1.000 33.83341 ? 29  PRO A CB  1 
ATOM   163  C CG  . PRO A 1 29  ? 11.13100  7.24900   -2.18600 1.000 36.34080 ? 29  PRO A CG  1 
ATOM   164  C CD  . PRO A 1 29  ? 11.56300  8.39000   -1.32200 1.000 35.93579 ? 29  PRO A CD  1 
ATOM   165  N N   . HIS A 1 30  ? 13.05000  4.34600   0.59600  1.000 31.01280 ? 30  HIS A N   1 
ATOM   166  C CA  . HIS A 1 30  ? 14.16300  3.40800   0.59500  1.000 32.99515 ? 30  HIS A CA  1 
ATOM   167  C C   . HIS A 1 30  ? 13.70700  2.12000   1.26100  1.000 31.60221 ? 30  HIS A C   1 
ATOM   168  O O   . HIS A 1 30  ? 12.92300  2.15300   2.21200  1.000 29.88485 ? 30  HIS A O   1 
ATOM   169  C CB  . HIS A 1 30  ? 15.38400  3.99100   1.31600  1.000 31.12173 ? 30  HIS A CB  1 
ATOM   170  C CG  . HIS A 1 30  ? 16.66000  3.26300   1.03100  1.000 38.96277 ? 30  HIS A CG  1 
ATOM   171  N ND1 . HIS A 1 30  ? 17.19600  2.33300   1.89500  1.000 38.69813 ? 30  HIS A ND1 1 
ATOM   172  C CD2 . HIS A 1 30  ? 17.50800  3.32800   -0.02300 1.000 37.46555 ? 30  HIS A CD2 1 
ATOM   173  C CE1 . HIS A 1 30  ? 18.32000  1.85800   1.38700  1.000 42.71342 ? 30  HIS A CE1 1 
ATOM   174  N NE2 . HIS A 1 30  ? 18.53100  2.44500   0.22300  1.000 42.92004 ? 30  HIS A NE2 1 
ATOM   175  N N   . GLU A 1 31  ? 14.20800  0.98900   0.75900  1.000 32.83059 ? 31  GLU A N   1 
ATOM   176  C CA  . GLU A 1 31  ? 13.73300  -0.31100  1.21500  1.000 31.37160 ? 31  GLU A CA  1 
ATOM   177  C C   . GLU A 1 31  ? 14.11200  -0.61700  2.65900  1.000 33.00699 ? 31  GLU A C   1 
ATOM   178  O O   . GLU A 1 31  ? 13.56500  -1.56500  3.23600  1.000 29.67027 ? 31  GLU A O   1 
ATOM   179  C CB  . GLU A 1 31  ? 14.26400  -1.41100  0.29500  1.000 38.10507 ? 31  GLU A CB  1 
ATOM   180  C CG  . GLU A 1 31  ? 13.37700  -2.64000  0.26000  1.000 43.34916 ? 31  GLU A CG  1 
ATOM   181  C CD  . GLU A 1 31  ? 11.92900  -2.29200  -0.04100 1.000 47.74494 ? 31  GLU A CD  1 
ATOM   182  O OE1 . GLU A 1 31  ? 11.63600  -1.88000  -1.18400 1.000 51.35082 ? 31  GLU A OE1 1 
ATOM   183  O OE2 . GLU A 1 31  ? 11.08400  -2.41700  0.87200  1.000 44.53028 ? 31  GLU A OE2 1 
ATOM   184  N N   . ARG A 1 32  ? 15.02200  0.15400   3.25900  1.000 27.91792 ? 32  ARG A N   1 
ATOM   185  C CA  . ARG A 1 32  ? 15.43600  -0.12900  4.62800  1.000 32.37977 ? 32  ARG A CA  1 
ATOM   186  C C   . ARG A 1 32  ? 14.30300  0.09700   5.62200  1.000 28.05561 ? 32  ARG A C   1 
ATOM   187  O O   . ARG A 1 32  ? 14.25200  -0.57000  6.66100  1.000 22.70814 ? 32  ARG A O   1 
ATOM   188  C CB  . ARG A 1 32  ? 16.65000  0.72600   5.00300  1.000 27.03923 ? 32  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 32  ? 16.34300  2.21000   5.16300  1.000 30.82694 ? 32  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 32  ? 17.50900  2.96400   5.78400  1.000 34.24073 ? 32  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 32  ? 18.60800  3.16200   4.84600  1.000 40.32133 ? 32  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 32  ? 18.80300  4.27200   4.14700  1.000 44.51011 ? 32  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 32  ? 17.99000  5.31000   4.25600  1.000 40.85993 ? 32  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 32  ? 19.84300  4.34300   3.32100  1.000 49.33054 ? 32  ARG A NH2 1 
ATOM   195  N N   . TYR A 1 33  ? 13.38300  1.01600   5.32100  1.000 24.65218 ? 33  TYR A N   1 
ATOM   196  C CA  . TYR A 1 33  ? 12.34400  1.35900   6.28700  1.000 26.76957 ? 33  TYR A CA  1 
ATOM   197  C C   . TYR A 1 33  ? 11.28600  0.26600   6.36700  1.000 26.58777 ? 33  TYR A C   1 
ATOM   198  O O   . TYR A 1 33  ? 10.86100  -0.12200  7.46200  1.000 25.02398 ? 33  TYR A O   1 
ATOM   199  C CB  . TYR A 1 33  ? 11.71900  2.70500   5.92300  1.000 24.82398 ? 33  TYR A CB  1 
ATOM   200  C CG  . TYR A 1 33  ? 12.73900  3.81100   5.79500  1.000 26.82899 ? 33  TYR A CG  1 
ATOM   201  C CD1 . TYR A 1 33  ? 13.50900  4.19700   6.88400  1.000 28.12107 ? 33  TYR A CD1 1 
ATOM   202  C CD2 . TYR A 1 33  ? 12.93700  4.46600   4.58600  1.000 27.96198 ? 33  TYR A CD2 1 
ATOM   203  C CE1 . TYR A 1 33  ? 14.44900  5.20600   6.77500  1.000 28.85869 ? 33  TYR A CE1 1 
ATOM   204  C CE2 . TYR A 1 33  ? 13.87200  5.47600   4.46700  1.000 25.11235 ? 33  TYR A CE2 1 
ATOM   205  C CZ  . TYR A 1 33  ? 14.62400  5.84100   5.56400  1.000 32.12194 ? 33  TYR A CZ  1 
ATOM   206  O OH  . TYR A 1 33  ? 15.55600  6.84400   5.45500  1.000 31.51643 ? 33  TYR A OH  1 
ATOM   207  N N   . GLU A 1 34  ? 10.84600  -0.24200  5.21300  1.000 25.77369 ? 34  GLU A N   1 
ATOM   208  C CA  . GLU A 1 34  ? 9.90500   -1.35700  5.20200  1.000 27.34170 ? 34  GLU A CA  1 
ATOM   209  C C   . GLU A 1 34  ? 10.52200  -2.59800  5.83100  1.000 25.06376 ? 34  GLU A C   1 
ATOM   210  O O   . GLU A 1 34  ? 9.83600   -3.36200  6.52000  1.000 22.14958 ? 34  GLU A O   1 
ATOM   211  C CB  . GLU A 1 34  ? 9.45400   -1.65400  3.77100  1.000 26.95655 ? 34  GLU A CB  1 
ATOM   212  C CG  . GLU A 1 34  ? 8.41400   -0.69100  3.21600  1.000 36.13525 ? 34  GLU A CG  1 
ATOM   213  C CD  . GLU A 1 34  ? 9.02000   0.45200   2.41700  1.000 39.01009 ? 34  GLU A CD  1 
ATOM   214  O OE1 . GLU A 1 34  ? 10.14400  0.88500   2.74300  1.000 32.77320 ? 34  GLU A OE1 1 
ATOM   215  O OE2 . GLU A 1 34  ? 8.36800   0.91300   1.45400  1.000 34.59529 ? 34  GLU A OE2 1 
ATOM   216  N N   . ARG A 1 35  ? 11.82100  -2.81000  5.60700  1.000 26.00539 ? 35  ARG A N   1 
ATOM   217  C CA  . ARG A 1 35  ? 12.50300  -3.96400  6.18500  1.000 27.64836 ? 35  ARG A CA  1 
ATOM   218  C C   . ARG A 1 35  ? 12.52100  -3.88800  7.70700  1.000 27.08389 ? 35  ARG A C   1 
ATOM   219  O O   . ARG A 1 35  ? 12.20800  -4.86700  8.39400  1.000 22.94314 ? 35  ARG A O   1 
ATOM   220  C CB  . ARG A 1 35  ? 13.92300  -4.05300  5.62800  1.000 32.70150 ? 35  ARG A CB  1 
ATOM   221  C CG  . ARG A 1 35  ? 14.82600  -5.02000  6.36500  1.000 32.89105 ? 35  ARG A CG  1 
ATOM   222  C CD  . ARG A 1 35  ? 16.18200  -5.09900  5.68700  1.000 36.62767 ? 35  ARG A CD  1 
ATOM   223  N NE  . ARG A 1 35  ? 17.15500  -5.82900  6.48900  1.000 31.74918 ? 35  ARG A NE  1 
ATOM   224  C CZ  . ARG A 1 35  ? 17.97300  -5.26400  7.36600  1.000 38.17559 ? 35  ARG A CZ  1 
ATOM   225  N NH1 . ARG A 1 35  ? 17.95000  -3.96000  7.59200  1.000 34.87206 ? 35  ARG A NH1 1 
ATOM   226  N NH2 . ARG A 1 35  ? 18.83600  -6.02500  8.03100  1.000 30.86792 ? 35  ARG A NH2 1 
ATOM   227  N N   . LEU A 1 36  ? 12.88800  -2.72700  8.25400  1.000 25.66782 ? 36  LEU A N   1 
ATOM   228  C CA  . LEU A 1 36  ? 12.86800  -2.56100  9.70300  1.000 23.69450 ? 36  LEU A CA  1 
ATOM   229  C C   . LEU A 1 36  ? 11.44700  -2.64300  10.24500 1.000 24.30643 ? 36  LEU A C   1 
ATOM   230  O O   . LEU A 1 36  ? 11.21300  -3.22200  11.31300 1.000 20.51452 ? 36  LEU A O   1 
ATOM   231  C CB  . LEU A 1 36  ? 13.51300  -1.22800  10.08900 1.000 23.14442 ? 36  LEU A CB  1 
ATOM   232  C CG  . LEU A 1 36  ? 13.52500  -0.91800  11.58700 1.000 22.05481 ? 36  LEU A CG  1 
ATOM   233  C CD1 . LEU A 1 36  ? 14.27700  -2.00300  12.34300 1.000 25.40572 ? 36  LEU A CD1 1 
ATOM   234  C CD2 . LEU A 1 36  ? 14.13600  0.45000   11.85700 1.000 24.96538 ? 36  LEU A CD2 1 
ATOM   235  N N   . ASP A 1 37  ? 10.48100  -2.08200  9.51300  1.000 22.75798 ? 37  ASP A N   1 
ATOM   236  C CA  . ASP A 1 37  ? 9.10400   -2.07300  9.99100  1.000 27.70816 ? 37  ASP A CA  1 
ATOM   237  C C   . ASP A 1 37  ? 8.55300   -3.48700  10.12700 1.000 28.42798 ? 37  ASP A C   1 
ATOM   238  O O   . ASP A 1 37  ? 7.86000   -3.79700  11.10300 1.000 24.08421 ? 37  ASP A O   1 
ATOM   239  C CB  . ASP A 1 37  ? 8.22300   -1.25100  9.05400  1.000 28.02726 ? 37  ASP A CB  1 
ATOM   240  C CG  . ASP A 1 37  ? 6.96800   -0.74900  9.73500  1.000 29.79988 ? 37  ASP A CG  1 
ATOM   241  O OD1 . ASP A 1 37  ? 6.98700   -0.62000  10.97400 1.000 27.52731 ? 37  ASP A OD1 1 
ATOM   242  O OD2 . ASP A 1 37  ? 5.96300   -0.49500  9.03900  1.000 30.29927 ? 37  ASP A OD2 1 
ATOM   243  N N   . ARG A 1 38  ? 8.83800   -4.35500  9.15500  1.000 28.35828 ? 38  ARG A N   1 
ATOM   244  C CA  . ARG A 1 38  ? 8.40400   -5.74300  9.27500  1.000 31.10589 ? 38  ARG A CA  1 
ATOM   245  C C   . ARG A 1 38  ? 9.08800   -6.42800  10.45000 1.000 29.47011 ? 38  ARG A C   1 
ATOM   246  O O   . ARG A 1 38  ? 8.45900   -7.20200  11.18000 1.000 31.74113 ? 38  ARG A O   1 
ATOM   247  C CB  . ARG A 1 38  ? 8.68800   -6.50700  7.98400  1.000 32.93366 ? 38  ARG A CB  1 
ATOM   248  C CG  . ARG A 1 38  ? 8.31200   -7.97600  8.08000  1.000 39.69771 ? 38  ARG A CG  1 
ATOM   249  C CD  . ARG A 1 38  ? 8.93200   -8.79800  6.96600  1.000 45.71487 ? 38  ARG A CD  1 
ATOM   250  N NE  . ARG A 1 38  ? 8.34600   -8.49000  5.66900  1.000 45.83469 ? 38  ARG A NE  1 
ATOM   251  C CZ  . ARG A 1 38  ? 7.17900   -8.95700  5.24700  1.000 49.30607 ? 38  ARG A CZ  1 
ATOM   252  N NH1 . ARG A 1 38  ? 6.42800   -9.73500  6.01000  1.000 42.73613 ? 38  ARG A NH1 1 
ATOM   253  N NH2 . ARG A 1 38  ? 6.75500   -8.63300  4.02900  1.000 48.45866 ? 38  ARG A NH2 1 
ATOM   254  N N   . TRP A 1 39  ? 10.37900  -6.15100  10.64600 1.000 27.63098 ? 39  TRP A N   1 
ATOM   255  C CA  . TRP A 1 39  ? 11.10200  -6.73200  11.77000 1.000 27.37747 ? 39  TRP A CA  1 
ATOM   256  C C   . TRP A 1 39  ? 10.47900  -6.31900  13.09800 1.000 28.19603 ? 39  TRP A C   1 
ATOM   257  O O   . TRP A 1 39  ? 10.37200  -7.13300  14.02100 1.000 27.40001 ? 39  TRP A O   1 
ATOM   258  C CB  . TRP A 1 39  ? 12.57400  -6.32000  11.71100 1.000 24.75083 ? 39  TRP A CB  1 
ATOM   259  C CG  . TRP A 1 39  ? 13.42600  -6.93100  12.78800 1.000 28.17497 ? 39  TRP A CG  1 
ATOM   260  C CD1 . TRP A 1 39  ? 14.19000  -8.06000  12.69000 1.000 27.34749 ? 39  TRP A CD1 1 
ATOM   261  C CD2 . TRP A 1 39  ? 13.60700  -6.43900  14.12100 1.000 30.05492 ? 39  TRP A CD2 1 
ATOM   262  N NE1 . TRP A 1 39  ? 14.83200  -8.30200  13.88100 1.000 29.95473 ? 39  TRP A NE1 1 
ATOM   263  C CE2 . TRP A 1 39  ? 14.49000  -7.32300  14.77600 1.000 33.88587 ? 39  TRP A CE2 1 
ATOM   264  C CE3 . TRP A 1 39  ? 13.10700  -5.33900  14.82500 1.000 29.03784 ? 39  TRP A CE3 1 
ATOM   265  C CZ2 . TRP A 1 39  ? 14.88200  -7.14000  16.09900 1.000 33.12105 ? 39  TRP A CZ2 1 
ATOM   266  C CZ3 . TRP A 1 39  ? 13.49600  -5.15900  16.13700 1.000 26.25623 ? 39  TRP A CZ3 1 
ATOM   267  C CH2 . TRP A 1 39  ? 14.37400  -6.05800  16.76200 1.000 35.66112 ? 39  TRP A CH2 1 
ATOM   268  N N   . ILE A 1 40  ? 10.05000  -5.05900  13.20800 1.000 29.90338 ? 40  ILE A N   1 
ATOM   269  C CA  . ILE A 1 40  ? 9.46400   -4.57400  14.45400 1.000 27.39493 ? 40  ILE A CA  1 
ATOM   270  C C   . ILE A 1 40  ? 8.13100   -5.26300  14.72400 1.000 28.28803 ? 40  ILE A C   1 
ATOM   271  O O   . ILE A 1 40  ? 7.87000   -5.72800  15.84100 1.000 28.73719 ? 40  ILE A O   1 
ATOM   272  C CB  . ILE A 1 40  ? 9.31200   -3.04200  14.41400 1.000 26.46073 ? 40  ILE A CB  1 
ATOM   273  C CG1 . ILE A 1 40  ? 10.68600  -2.36800  14.42800 1.000 27.32802 ? 40  ILE A CG1 1 
ATOM   274  C CG2 . ILE A 1 40  ? 8.46200   -2.55900  15.57900 1.000 21.95244 ? 40  ILE A CG2 1 
ATOM   275  C CD1 . ILE A 1 40  ? 10.63000  -0.85900  14.29200 1.000 25.49593 ? 40  ILE A CD1 1 
ATOM   276  N N   . THR A 1 41  ? 7.26600   -5.33700  13.70800 1.000 27.29477 ? 41  THR A N   1 
ATOM   277  C CA  . THR A 1 41  ? 5.95700   -5.95800  13.89800 1.000 30.06016 ? 41  THR A CA  1 
ATOM   278  C C   . THR A 1 41  ? 6.08100   -7.43400  14.24600 1.000 31.42155 ? 41  THR A C   1 
ATOM   279  O O   . THR A 1 41  ? 5.26000   -7.96500  15.00200 1.000 33.60004 ? 41  THR A O   1 
ATOM   280  C CB  . THR A 1 41  ? 5.09600   -5.78900  12.64600 1.000 25.58139 ? 41  THR A CB  1 
ATOM   281  O OG1 . THR A 1 41  ? 5.69200   -6.49900  11.55300 1.000 36.37213 ? 41  THR A OG1 1 
ATOM   282  C CG2 . THR A 1 41  ? 4.96200   -4.31600  12.28000 1.000 35.05289 ? 41  THR A CG2 1 
ATOM   283  N N   . GLU A 1 42  ? 7.09600   -8.11200  13.70700 1.000 31.30430 ? 42  GLU A N   1 
ATOM   284  C CA  . GLU A 1 42  ? 7.29300   -9.51900  14.03500 1.000 35.25297 ? 42  GLU A CA  1 
ATOM   285  C C   . GLU A 1 42  ? 7.81700   -9.69400  15.45500 1.000 37.18912 ? 42  GLU A C   1 
ATOM   286  O O   . GLU A 1 42  ? 7.51600   -10.70100 16.10500 1.000 34.69921 ? 42  GLU A O   1 
ATOM   287  C CB  . GLU A 1 42  ? 8.23800   -10.16400 13.02200 1.000 31.85582 ? 42  GLU A CB  1 
ATOM   288  C CG  . GLU A 1 42  ? 7.64200   -10.28900 11.62400 1.000 40.85681 ? 42  GLU A CG  1 
ATOM   289  C CD  . GLU A 1 42  ? 8.64900   -10.77300 10.59600 1.000 44.25908 ? 42  GLU A CD  1 
ATOM   290  O OE1 . GLU A 1 42  ? 9.83800   -10.92300 10.94900 1.000 44.26892 ? 42  GLU A OE1 1 
ATOM   291  O OE2 . GLU A 1 42  ? 8.25100   -11.00100 9.43400  1.000 45.31066 ? 42  GLU A OE2 1 
ATOM   292  N N   . GLN A 1 43  ? 8.59300   -8.72900  15.95600 1.000 33.82567 ? 43  GLN A N   1 
ATOM   293  C CA  . GLN A 1 43  ? 9.00400   -8.76800  17.35600 1.000 34.70805 ? 43  GLN A CA  1 
ATOM   294  C C   . GLN A 1 43  ? 7.80100   -8.63100  18.27700 1.000 38.51426 ? 43  GLN A C   1 
ATOM   295  O O   . GLN A 1 43  ? 7.75900   -9.24100  19.35200 1.000 36.30771 ? 43  GLN A O   1 
ATOM   296  C CB  . GLN A 1 43  ? 10.01900  -7.66100  17.64400 1.000 32.00660 ? 43  GLN A CB  1 
ATOM   297  C CG  . GLN A 1 43  ? 11.34000  -7.81700  16.92200 1.000 32.88758 ? 43  GLN A CG  1 
ATOM   298  C CD  . GLN A 1 43  ? 12.11200  -9.03900  17.36200 1.000 35.40378 ? 43  GLN A CD  1 
ATOM   299  O OE1 . GLN A 1 43  ? 11.96600  -9.51300  18.49000 1.000 33.94338 ? 43  GLN A OE1 1 
ATOM   300  N NE2 . GLN A 1 43  ? 12.94200  -9.56100  16.46800 1.000 43.37896 ? 43  GLN A NE2 1 
ATOM   301  N N   . LEU A 1 44  ? 6.81700   -7.82400  17.87300 1.000 40.64993 ? 44  LEU A N   1 
ATOM   302  C CA  . LEU A 1 44  ? 5.60300   -7.66700  18.66700 1.000 42.50033 ? 44  LEU A CA  1 
ATOM   303  C C   . LEU A 1 44  ? 4.89500   -9.00100  18.85400 1.000 45.08226 ? 44  LEU A C   1 
ATOM   304  O O   . LEU A 1 44  ? 4.53100   -9.37400  19.97600 1.000 47.10811 ? 44  LEU A O   1 
ATOM   305  C CB  . LEU A 1 44  ? 4.67100   -6.65500  18.00200 1.000 43.92631 ? 44  LEU A CB  1 
ATOM   306  C CG  . LEU A 1 44  ? 4.74200   -5.21800  18.51500 1.000 44.30041 ? 44  LEU A CG  1 
ATOM   307  C CD1 . LEU A 1 44  ? 3.77000   -4.32800  17.75500 1.000 32.50519 ? 44  LEU A CD1 1 
ATOM   308  C CD2 . LEU A 1 44  ? 4.45200   -5.18600  20.00700 1.000 42.90242 ? 44  LEU A CD2 1 
ATOM   309  N N   . ILE A 1 45  ? 4.69700   -9.73800  17.76000 1.000 42.26597 ? 45  ILE A N   1 
ATOM   310  C CA  . ILE A 1 45  ? 4.01100   -11.02600 17.83400 1.000 48.42337 ? 45  ILE A CA  1 
ATOM   311  C C   . ILE A 1 45  ? 4.80100   -11.99400 18.70600 1.000 48.28980 ? 45  ILE A C   1 
ATOM   312  O O   . ILE A 1 45  ? 4.30400   -12.49300 19.72300 1.000 50.39170 ? 45  ILE A O   1 
ATOM   313  C CB  . ILE A 1 45  ? 3.78500   -11.59200 16.42200 1.000 49.16835 ? 45  ILE A CB  1 
ATOM   314  C CG1 . ILE A 1 45  ? 3.11700   -10.53800 15.53600 1.000 45.44104 ? 45  ILE A CG1 1 
ATOM   315  C CG2 . ILE A 1 45  ? 2.94200   -12.85600 16.48700 1.000 47.73840 ? 45  ILE A CG2 1 
ATOM   316  C CD1 . ILE A 1 45  ? 3.15900   -10.86500 14.06100 1.000 47.07533 ? 45  ILE A CD1 1 
ATOM   317  N N   . TYR A 1 46  ? 6.04400   -12.26700 18.32400 1.000 44.52309 ? 46  TYR A N   1 
ATOM   318  C CA  . TYR A 1 46  ? 6.92200   -13.10000 19.13400 1.000 42.20392 ? 46  TYR A CA  1 
ATOM   319  C C   . TYR A 1 46  ? 7.36700   -12.33100 20.37300 1.000 42.14312 ? 46  TYR A C   1 
ATOM   320  O O   . TYR A 1 46  ? 6.71100   -12.37500 21.41200 1.000 42.33774 ? 46  TYR A O   1 
ATOM   321  C CB  . TYR A 1 46  ? 8.13800   -13.55600 18.32400 1.000 36.14082 ? 46  TYR A CB  1 
ATOM   322  C CG  . TYR A 1 46  ? 9.01700   -14.56300 19.03700 1.000 36.94251 ? 46  TYR A CG  1 
ATOM   323  C CD1 . TYR A 1 46  ? 9.97200   -14.15400 19.96100 1.000 43.52608 ? 46  TYR A CD1 1 
ATOM   324  C CD2 . TYR A 1 46  ? 8.89900   -15.92100 18.77700 1.000 39.11614 ? 46  TYR A CD2 1 
ATOM   325  C CE1 . TYR A 1 46  ? 10.77700  -15.07100 20.61200 1.000 43.63515 ? 46  TYR A CE1 1 
ATOM   326  C CE2 . TYR A 1 46  ? 9.70200   -16.84500 19.42100 1.000 37.31099 ? 46  TYR A CE2 1 
ATOM   327  C CZ  . TYR A 1 46  ? 10.63800  -16.41500 20.33700 1.000 40.23378 ? 46  TYR A CZ  1 
ATOM   328  O OH  . TYR A 1 46  ? 11.43900  -17.33100 20.98200 1.000 44.48400 ? 46  TYR A OH  1 
ATOM   329  N N   . ARG A 1 52  ? 1.01200   -12.82900 20.13600 1.000 47.13403 ? 52  ARG A N   1 
ATOM   330  C CA  . ARG A 1 52  ? -0.29800  -12.47900 20.67100 1.000 46.47988 ? 52  ARG A CA  1 
ATOM   331  C C   . ARG A 1 52  ? -1.27700  -12.15500 19.54900 1.000 41.94954 ? 52  ARG A C   1 
ATOM   332  O O   . ARG A 1 52  ? -0.99600  -11.31700 18.69200 1.000 42.58378 ? 52  ARG A O   1 
ATOM   333  C CB  . ARG A 1 52  ? -0.18900  -11.29400 21.63400 1.000 40.51741 ? 52  ARG A CB  1 
ATOM   334  C CG  . ARG A 1 52  ? -1.51200  -10.88900 22.26300 1.000 43.16060 ? 52  ARG A CG  1 
ATOM   335  C CD  . ARG A 1 52  ? -1.32900  -10.42100 23.70000 1.000 43.03461 ? 52  ARG A CD  1 
ATOM   336  N NE  . ARG A 1 52  ? -1.04600  -8.99400  23.80000 1.000 50.23791 ? 52  ARG A NE  1 
ATOM   337  C CZ  . ARG A 1 52  ? -0.79800  -8.36100  24.93900 1.000 53.75198 ? 52  ARG A CZ  1 
ATOM   338  N NH1 . ARG A 1 52  ? -0.76400  -9.00600  26.09400 1.000 53.81189 ? 52  ARG A NH1 1 
ATOM   339  N NH2 . ARG A 1 52  ? -0.58000  -7.04900  24.91900 1.000 53.82269 ? 52  ARG A NH2 1 
ATOM   340  N N   . ASP A 1 53  ? -2.43100  -12.82800 19.56000 1.000 44.01272 ? 53  ASP A N   1 
ATOM   341  C CA  . ASP A 1 53  ? -3.44900  -12.58100 18.54500 1.000 43.35936 ? 53  ASP A CA  1 
ATOM   342  C C   . ASP A 1 53  ? -4.08500  -11.20600 18.68400 1.000 44.55989 ? 53  ASP A C   1 
ATOM   343  O O   . ASP A 1 53  ? -4.69500  -10.71900 17.72600 1.000 44.67292 ? 53  ASP A O   1 
ATOM   344  C CB  . ASP A 1 53  ? -4.53100  -13.65900 18.61100 1.000 44.59512 ? 53  ASP A CB  1 
ATOM   345  C CG  . ASP A 1 53  ? -3.98300  -15.04900 18.37200 1.000 41.65441 ? 53  ASP A CG  1 
ATOM   346  O OD1 . ASP A 1 53  ? -3.26000  -15.24300 17.37100 1.000 40.80845 ? 53  ASP A OD1 1 
ATOM   347  O OD2 . ASP A 1 53  ? -4.27000  -15.94600 19.19200 1.000 38.05690 ? 53  ASP A OD2 1 
ATOM   348  N N   . GLU A 1 54  ? -3.96700  -10.57400 19.85300 1.000 44.75837 ? 54  GLU A N   1 
ATOM   349  C CA  . GLU A 1 54  ? -4.49200  -9.22300  20.01100 1.000 48.40777 ? 54  GLU A CA  1 
ATOM   350  C C   . GLU A 1 54  ? -3.68000  -8.22300  19.19800 1.000 45.89300 ? 54  GLU A C   1 
ATOM   351  O O   . GLU A 1 54  ? -4.23600  -7.26500  18.64700 1.000 41.71519 ? 54  GLU A O   1 
ATOM   352  C CB  . GLU A 1 54  ? -4.51200  -8.83600  21.48900 1.000 50.59160 ? 54  GLU A CB  1 
ATOM   353  C CG  . GLU A 1 54  ? -5.22100  -7.52000  21.79000 1.000 54.37200 ? 54  GLU A CG  1 
ATOM   354  C CD  . GLU A 1 54  ? -6.73700  -7.64600  21.82900 1.000 58.45604 ? 54  GLU A CD  1 
ATOM   355  O OE1 . GLU A 1 54  ? -7.30300  -8.46500  21.07300 1.000 57.91570 ? 54  GLU A OE1 1 
ATOM   356  O OE2 . GLU A 1 54  ? -7.36700  -6.92100  22.62700 1.000 62.27066 ? 54  GLU A OE2 1 
ATOM   357  N N   . TRP A 1 55  ? -2.36300  -8.42800  19.11100 1.000 43.59121 ? 55  TRP A N   1 
ATOM   358  C CA  . TRP A 1 55  ? -1.54400  -7.58400  18.24700 1.000 41.16001 ? 55  TRP A CA  1 
ATOM   359  C C   . TRP A 1 55  ? -1.83600  -7.85900  16.77900 1.000 41.26773 ? 55  TRP A C   1 
ATOM   360  O O   . TRP A 1 55  ? -1.84400  -6.93400  15.96000 1.000 35.41069 ? 55  TRP A O   1 
ATOM   361  C CB  . TRP A 1 55  ? -0.06000  -7.79200  18.54800 1.000 42.67830 ? 55  TRP A CB  1 
ATOM   362  C CG  . TRP A 1 55  ? 0.36900   -7.23400  19.87100 1.000 43.52357 ? 55  TRP A CG  1 
ATOM   363  C CD1 . TRP A 1 55  ? 0.88800   -7.92800  20.92400 1.000 48.54903 ? 55  TRP A CD1 1 
ATOM   364  C CD2 . TRP A 1 55  ? 0.30700   -5.86300  20.28500 1.000 42.34344 ? 55  TRP A CD2 1 
ATOM   365  N NE1 . TRP A 1 55  ? 1.15800   -7.07400  21.96700 1.000 46.93764 ? 55  TRP A NE1 1 
ATOM   366  C CE2 . TRP A 1 55  ? 0.80900   -5.80100  21.59900 1.000 42.30494 ? 55  TRP A CE2 1 
ATOM   367  C CE3 . TRP A 1 55  ? -0.12300  -4.68200  19.67000 1.000 43.73641 ? 55  TRP A CE3 1 
ATOM   368  C CZ2 . TRP A 1 55  ? 0.89300   -4.60700  22.31000 1.000 44.43414 ? 55  TRP A CZ2 1 
ATOM   369  C CZ3 . TRP A 1 55  ? -0.03900  -3.49700  20.37800 1.000 40.16622 ? 55  TRP A CZ3 1 
ATOM   370  C CH2 . TRP A 1 55  ? 0.46500   -3.46900  21.68400 1.000 43.14082 ? 55  TRP A CH2 1 
ATOM   371  N N   . ILE A 1 56  ? -2.07500  -9.12600  16.42800 1.000 39.70992 ? 56  ILE A N   1 
ATOM   372  C CA  . ILE A 1 56  ? -2.47100  -9.46200  15.06100 1.000 39.53465 ? 56  ILE A CA  1 
ATOM   373  C C   . ILE A 1 56  ? -3.74800  -8.72100  14.68600 1.000 39.29610 ? 56  ILE A C   1 
ATOM   374  O O   . ILE A 1 56  ? -3.83400  -8.09300  13.62400 1.000 39.22958 ? 56  ILE A O   1 
ATOM   375  C CB  . ILE A 1 56  ? -2.63600  -10.98500 14.90800 1.000 38.13003 ? 56  ILE A CB  1 
ATOM   376  C CG1 . ILE A 1 56  ? -1.27000  -11.66200 14.77400 1.000 39.69773 ? 56  ILE A CG1 1 
ATOM   377  C CG2 . ILE A 1 56  ? -3.53100  -11.31700 13.72300 1.000 39.92104 ? 56  ILE A CG2 1 
ATOM   378  C CD1 . ILE A 1 56  ? -1.35300  -13.16000 14.56600 1.000 41.83753 ? 56  ILE A CD1 1 
ATOM   379  N N   . ASP A 1 57  ? -4.75600  -8.77500  15.56200 1.000 38.32041 ? 57  ASP A N   1 
ATOM   380  C CA  . ASP A 1 57  ? -6.00000  -8.05400  15.31200 1.000 38.42635 ? 57  ASP A CA  1 
ATOM   381  C C   . ASP A 1 57  ? -5.76600  -6.54900  15.25200 1.000 36.61159 ? 57  ASP A C   1 
ATOM   382  O O   . ASP A 1 57  ? -6.40300  -5.84600  14.45900 1.000 32.25497 ? 57  ASP A O   1 
ATOM   383  C CB  . ASP A 1 57  ? -7.02700  -8.39500  16.39300 1.000 41.25741 ? 57  ASP A CB  1 
ATOM   384  C CG  . ASP A 1 57  ? -7.93700  -9.54200  15.99500 1.000 47.42318 ? 57  ASP A CG  1 
ATOM   385  O OD1 . ASP A 1 57  ? -7.44400  -10.51400 15.38400 1.000 48.81552 ? 57  ASP A OD1 1 
ATOM   386  O OD2 . ASP A 1 57  ? -9.14600  -9.47600  16.30200 1.000 53.90360 ? 57  ASP A OD2 1 
ATOM   387  N N   . ALA A 1 58  ? -4.85200  -6.03800  16.08000 1.000 36.24039 ? 58  ALA A N   1 
ATOM   388  C CA  . ALA A 1 58  ? -4.59700  -4.60100  16.09900 1.000 38.44718 ? 58  ALA A CA  1 
ATOM   389  C C   . ALA A 1 58  ? -3.89600  -4.14400  14.82600 1.000 30.21721 ? 58  ALA A C   1 
ATOM   390  O O   . ALA A 1 58  ? -4.18100  -3.05600  14.31300 1.000 31.83474 ? 58  ALA A O   1 
ATOM   391  C CB  . ALA A 1 58  ? -3.77200  -4.22900  17.33200 1.000 33.16869 ? 58  ALA A CB  1 
ATOM   392  N N   . LEU A 1 59  ? -2.97000  -4.95400  14.30800 1.000 29.97038 ? 59  LEU A N   1 
ATOM   393  C CA  . LEU A 1 59  ? -2.27300  -4.59000  13.07800 1.000 31.53483 ? 59  LEU A CA  1 
ATOM   394  C C   . LEU A 1 59  ? -3.20300  -4.67000  11.87500 1.000 31.09020 ? 59  LEU A C   1 
ATOM   395  O O   . LEU A 1 59  ? -3.13700  -3.82400  10.97500 1.000 26.62826 ? 59  LEU A O   1 
ATOM   396  C CB  . LEU A 1 59  ? -1.05700  -5.49300  12.87300 1.000 27.77737 ? 59  LEU A CB  1 
ATOM   397  C CG  . LEU A 1 59  ? 0.04700   -5.42300  13.93000 1.000 35.14631 ? 59  LEU A CG  1 
ATOM   398  C CD1 . LEU A 1 59  ? 1.15800   -6.41700  13.61700 1.000 35.09103 ? 59  LEU A CD1 1 
ATOM   399  C CD2 . LEU A 1 59  ? 0.59900   -4.01000  14.04300 1.000 30.62491 ? 59  LEU A CD2 1 
ATOM   400  N N   . ALA A 1 60  ? -4.07000  -5.68300  11.83700 1.000 30.40960 ? 60  ALA A N   1 
ATOM   401  C CA  . ALA A 1 60  ? -5.03900  -5.78200  10.75200 1.000 33.37583 ? 60  ALA A CA  1 
ATOM   402  C C   . ALA A 1 60  ? -5.98300  -4.58600  10.75800 1.000 28.44859 ? 60  ALA A C   1 
ATOM   403  O O   . ALA A 1 60  ? -6.26800  -3.99800  9.70900  1.000 27.89492 ? 60  ALA A O   1 
ATOM   404  C CB  . ALA A 1 60  ? -5.82000  -7.09100  10.86400 1.000 38.78000 ? 60  ALA A CB  1 
ATOM   405  N N   . GLU A 1 61  ? -6.46700  -4.20300  11.94200 1.000 30.80168 ? 61  GLU A N   1 
ATOM   406  C CA  . GLU A 1 61  ? -7.38000  -3.06900  12.03300 1.000 33.32537 ? 61  GLU A CA  1 
ATOM   407  C C   . GLU A 1 61  ? -6.66600  -1.75700  11.73300 1.000 27.51523 ? 61  GLU A C   1 
ATOM   408  O O   . GLU A 1 61  ? -7.23700  -0.86500  11.09600 1.000 28.40173 ? 61  GLU A O   1 
ATOM   409  C CB  . GLU A 1 61  ? -8.02300  -3.02600  13.41800 1.000 32.64013 ? 61  GLU A CB  1 
ATOM   410  C CG  . GLU A 1 61  ? -9.05900  -1.92800  13.58200 1.000 37.90382 ? 61  GLU A CG  1 
ATOM   411  C CD  . GLU A 1 61  ? -9.57800  -1.81800  15.00200 1.000 35.73800 ? 61  GLU A CD  1 
ATOM   412  O OE1 . GLU A 1 61  ? -9.27700  -2.71300  15.81900 1.000 35.93467 ? 61  GLU A OE1 1 
ATOM   413  O OE2 . GLU A 1 61  ? -10.28300 -0.83200  15.30100 1.000 39.85443 ? 61  GLU A OE2 1 
ATOM   414  N N   . ALA A 1 62  ? -5.41700  -1.62000  12.18300 1.000 30.04506 ? 62  ALA A N   1 
ATOM   415  C CA  . ALA A 1 62  ? -4.67000  -0.39700  11.91200 1.000 28.88969 ? 62  ALA A CA  1 
ATOM   416  C C   . ALA A 1 62  ? -4.27000  -0.29100  10.44800 1.000 27.15238 ? 62  ALA A C   1 
ATOM   417  O O   . ALA A 1 62  ? -4.09200  0.82100   9.93600  1.000 21.09425 ? 62  ALA A O   1 
ATOM   418  C CB  . ALA A 1 62  ? -3.42800  -0.32900  12.79700 1.000 23.39803 ? 62  ALA A CB  1 
ATOM   419  N N   . ALA A 1 63  ? -4.12200  -1.42800  9.76300  1.000 26.26359 ? 63  ALA A N   1 
ATOM   420  C CA  . ALA A 1 63  ? -3.68100  -1.40700  8.37300  1.000 25.95260 ? 63  ALA A CA  1 
ATOM   421  C C   . ALA A 1 63  ? -4.65500  -0.63200  7.49600  1.000 26.90866 ? 63  ALA A C   1 
ATOM   422  O O   . ALA A 1 63  ? -4.23800  0.11200   6.60000  1.000 26.81866 ? 63  ALA A O   1 
ATOM   423  C CB  . ALA A 1 63  ? -3.50900  -2.83400  7.85400  1.000 29.69948 ? 63  ALA A CB  1 
ATOM   424  N N   . GLY A 1 64  ? -5.95700  -0.78800  7.74300  1.000 23.49916 ? 64  GLY A N   1 
ATOM   425  C CA  . GLY A 1 64  ? -6.93800  -0.01800  7.00000  1.000 26.64385 ? 64  GLY A CA  1 
ATOM   426  C C   . GLY A 1 64  ? -6.94500  1.44900   7.37300  1.000 24.20728 ? 64  GLY A C   1 
ATOM   427  O O   . GLY A 1 64  ? -7.26700  2.30200   6.54200  1.000 28.25306 ? 64  GLY A O   1 
ATOM   428  N N   . ILE A 1 65  ? -6.58900  1.76500   8.62000  1.000 28.04252 ? 65  ILE A N   1 
ATOM   429  C CA  . ILE A 1 65  ? -6.51000  3.15900   9.04400  1.000 25.97501 ? 65  ILE A CA  1 
ATOM   430  C C   . ILE A 1 65  ? -5.39400  3.88000   8.29900  1.000 27.23550 ? 65  ILE A C   1 
ATOM   431  O O   . ILE A 1 65  ? -5.56800  5.01500   7.83900  1.000 23.38284 ? 65  ILE A O   1 
ATOM   432  C CB  . ILE A 1 65  ? -6.32200  3.23800   10.57000 1.000 28.71929 ? 65  ILE A CB  1 
ATOM   433  C CG1 . ILE A 1 65  ? -7.60200  2.80100   11.28600 1.000 31.52220 ? 65  ILE A CG1 1 
ATOM   434  C CG2 . ILE A 1 65  ? -5.90900  4.64100   10.99400 1.000 25.89312 ? 65  ILE A CG2 1 
ATOM   435  C CD1 . ILE A 1 65  ? -7.37900  2.34900   12.71000 1.000 29.80539 ? 65  ILE A CD1 1 
ATOM   436  N N   . PHE A 1 66  ? -4.23300  3.23500   8.16000  1.000 25.19436 ? 66  PHE A N   1 
ATOM   437  C CA  . PHE A 1 66  ? -3.13100  3.85900   7.43600  1.000 24.26933 ? 66  PHE A CA  1 
ATOM   438  C C   . PHE A 1 66  ? -3.37700  3.84400   5.93300  1.000 21.38355 ? 66  PHE A C   1 
ATOM   439  O O   . PHE A 1 66  ? -2.93400  4.75200   5.22000  1.000 18.65191 ? 66  PHE A O   1 
ATOM   440  C CB  . PHE A 1 66  ? -1.81400  3.16200   7.77200  1.000 22.03781 ? 66  PHE A CB  1 
ATOM   441  C CG  . PHE A 1 66  ? -1.31300  3.45800   9.15600  1.000 25.45056 ? 66  PHE A CG  1 
ATOM   442  C CD1 . PHE A 1 66  ? -0.50800  4.56000   9.39600  1.000 23.04337 ? 66  PHE A CD1 1 
ATOM   443  C CD2 . PHE A 1 66  ? -1.65200  2.63800   10.22000 1.000 25.44755 ? 66  PHE A CD2 1 
ATOM   444  C CE1 . PHE A 1 66  ? -0.04700  4.83600   10.67400 1.000 26.63010 ? 66  PHE A CE1 1 
ATOM   445  C CE2 . PHE A 1 66  ? -1.19700  2.90900   11.49600 1.000 23.60125 ? 66  PHE A CE2 1 
ATOM   446  C CZ  . PHE A 1 66  ? -0.39500  4.00900   11.72300 1.000 25.27684 ? 66  PHE A CZ  1 
ATOM   447  N N   . LYS A 1 67  ? -4.06900  2.81800   5.43100  1.000 22.16303 ? 67  LYS A N   1 
ATOM   448  C CA  . LYS A 1 67  ? -4.43200  2.79900   4.01700  1.000 29.21907 ? 67  LYS A CA  1 
ATOM   449  C C   . LYS A 1 67  ? -5.29900  4.00000   3.66500  1.000 21.08345 ? 67  LYS A C   1 
ATOM   450  O O   . LYS A 1 67  ? -5.05700  4.68200   2.66200  1.000 23.07157 ? 67  LYS A O   1 
ATOM   451  C CB  . LYS A 1 67  ? -5.15200  1.49600   3.66600  1.000 28.60100 ? 67  LYS A CB  1 
ATOM   452  C CG  . LYS A 1 67  ? -5.95200  1.57500   2.36900  1.000 32.60480 ? 67  LYS A CG  1 
ATOM   453  C CD  . LYS A 1 67  ? -6.11700  0.21500   1.70100  1.000 35.39080 ? 67  LYS A CD  1 
ATOM   454  C CE  . LYS A 1 67  ? -7.08600  -0.68100  2.45200  1.000 39.33100 ? 67  LYS A CE  1 
ATOM   455  N NZ  . LYS A 1 67  ? -7.37100  -1.92300  1.67900  1.000 41.90908 ? 67  LYS A NZ  1 
ATOM   456  N N   . GLU A 1 68  ? -6.31100  4.28200   4.48800  1.000 22.90868 ? 68  GLU A N   1 
ATOM   457  C CA  . GLU A 1 68  ? -7.18900  5.41600   4.21300  1.000 24.05394 ? 68  GLU A CA  1 
ATOM   458  C C   . GLU A 1 68  ? -6.44800  6.73700   4.35800  1.000 27.05034 ? 68  GLU A C   1 
ATOM   459  O O   . GLU A 1 68  ? -6.71300  7.68800   3.61300  1.000 24.72322 ? 68  GLU A O   1 
ATOM   460  C CB  . GLU A 1 68  ? -8.40400  5.37700   5.13600  1.000 28.99929 ? 68  GLU A CB  1 
ATOM   461  C CG  . GLU A 1 68  ? -9.30300  4.17700   4.90800  1.000 40.09091 ? 68  GLU A CG  1 
ATOM   462  C CD  . GLU A 1 68  ? -10.49500 4.15900   5.84000  1.000 49.47662 ? 68  GLU A CD  1 
ATOM   463  O OE1 . GLU A 1 68  ? -11.13800 5.21900   6.01200  1.000 48.97372 ? 68  GLU A OE1 1 
ATOM   464  O OE2 . GLU A 1 68  ? -10.78600 3.08400   6.41000  1.000 41.56267 ? 68  GLU A OE2 1 
ATOM   465  N N   . ALA A 1 69  ? -5.51900  6.81900   5.31600  1.000 20.37288 ? 69  ALA A N   1 
ATOM   466  C CA  . ALA A 1 69  ? -4.71400  8.02600   5.45500  1.000 19.45790 ? 69  ALA A CA  1 
ATOM   467  C C   . ALA A 1 69  ? -3.86100  8.26100   4.21500  1.000 20.97178 ? 69  ALA A C   1 
ATOM   468  O O   . ALA A 1 69  ? -3.69700  9.40300   3.77400  1.000 22.47502 ? 69  ALA A O   1 
ATOM   469  C CB  . ALA A 1 69  ? -3.83600  7.93600   6.70400  1.000 22.16970 ? 69  ALA A CB  1 
ATOM   470  N N   . LEU A 1 70  ? -3.32100  7.18600   3.63100  1.000 16.90100 ? 70  LEU A N   1 
ATOM   471  C CA  . LEU A 1 70  ? -2.54200  7.31300   2.40300  1.000 22.03865 ? 70  LEU A CA  1 
ATOM   472  C C   . LEU A 1 70  ? -3.38900  7.82200   1.24600  1.000 22.15112 ? 70  LEU A C   1 
ATOM   473  O O   . LEU A 1 70  ? -2.87600  8.51300   0.35800  1.000 25.29077 ? 70  LEU A O   1 
ATOM   474  C CB  . LEU A 1 70  ? -1.91800  5.96900   2.03000  1.000 25.01977 ? 70  LEU A CB  1 
ATOM   475  C CG  . LEU A 1 70  ? -0.61600  5.55800   2.71000  1.000 26.55927 ? 70  LEU A CG  1 
ATOM   476  C CD1 . LEU A 1 70  ? -0.20900  4.17300   2.23100  1.000 28.25294 ? 70  LEU A CD1 1 
ATOM   477  C CD2 . LEU A 1 70  ? 0.47600   6.57300   2.41300  1.000 27.80111 ? 70  LEU A CD2 1 
ATOM   478  N N   . GLU A 1 71  ? -4.67500  7.48800   1.23200  1.000 25.86494 ? 71  GLU A N   1 
ATOM   479  C CA  . GLU A 1 71  ? -5.56900  7.87300   0.14900  1.000 23.23583 ? 71  GLU A CA  1 
ATOM   480  C C   . GLU A 1 71  ? -6.18200  9.25200   0.35200  1.000 26.31496 ? 71  GLU A C   1 
ATOM   481  O O   . GLU A 1 71  ? -6.92100  9.72300   -0.52000 1.000 31.81127 ? 71  GLU A O   1 
ATOM   482  C CB  . GLU A 1 71  ? -6.67000  6.82100   -0.00900 1.000 25.17585 ? 71  GLU A CB  1 
ATOM   483  C CG  . GLU A 1 71  ? -6.11600  5.42400   -0.23500 1.000 24.01072 ? 71  GLU A CG  1 
ATOM   484  C CD  . GLU A 1 71  ? -7.18800  4.35700   -0.27100 1.000 34.27455 ? 71  GLU A CD  1 
ATOM   485  O OE1 . GLU A 1 71  ? -8.37300  4.70500   -0.11300 1.000 33.55313 ? 71  GLU A OE1 1 
ATOM   486  O OE2 . GLU A 1 71  ? -6.84500  3.17100   -0.45800 1.000 38.26569 ? 71  GLU A OE2 1 
ATOM   487  N N   . ARG A 1 72  ? -5.89200  9.90700   1.47100  1.000 26.73152 ? 72  ARG A N   1 
ATOM   488  C CA  . ARG A 1 72  ? -6.32900  11.26700  1.73600  1.000 29.33178 ? 72  ARG A CA  1 
ATOM   489  C C   . ARG A 1 72  ? -5.13700  12.21300  1.67000  1.000 28.87344 ? 72  ARG A C   1 
ATOM   490  O O   . ARG A 1 72  ? -3.97700  11.79000  1.68000  1.000 33.23338 ? 72  ARG A O   1 
ATOM   491  C CB  . ARG A 1 72  ? -7.01700  11.36600  3.10300  1.000 29.29446 ? 72  ARG A CB  1 
ATOM   492  C CG  . ARG A 1 72  ? -8.35900  10.65000  3.17200  1.000 35.71982 ? 72  ARG A CG  1 
ATOM   493  C CD  . ARG A 1 72  ? -9.00600  10.81300  4.54400  1.000 36.12439 ? 72  ARG A CD  1 
ATOM   494  N NE  . ARG A 1 72  ? -10.46100 10.75200  4.47300  1.000 46.95423 ? 72  ARG A NE  1 
ATOM   495  C CZ  . ARG A 1 72  ? -11.18800 9.68000   4.75900  1.000 51.03187 ? 72  ARG A CZ  1 
ATOM   496  N NH1 . ARG A 1 72  ? -10.62700 8.55100   5.16200  1.000 47.47765 ? 72  ARG A NH1 1 
ATOM   497  N NH2 . ARG A 1 72  ? -12.51100 9.74200   4.63800  1.000 50.06634 ? 72  ARG A NH2 1 
ATOM   498  N N   . ASN A 1 73  ? -5.43400  13.51100  1.59600  1.000 32.53163 ? 73  ASN A N   1 
ATOM   499  C CA  . ASN A 1 73  ? -4.39700  14.53900  1.48800  1.000 36.51472 ? 73  ASN A CA  1 
ATOM   500  C C   . ASN A 1 73  ? -3.84800  14.85100  2.88200  1.000 35.53883 ? 73  ASN A C   1 
ATOM   501  O O   . ASN A 1 73  ? -4.01600  15.93900  3.43600  1.000 37.95672 ? 73  ASN A O   1 
ATOM   502  C CB  . ASN A 1 73  ? -4.94700  15.78200  0.80300  1.000 41.35561 ? 73  ASN A CB  1 
ATOM   503  C CG  . ASN A 1 73  ? -3.87400  16.81900  0.52600  1.000 39.99843 ? 73  ASN A CG  1 
ATOM   504  O OD1 . ASN A 1 73  ? -2.70100  16.48700  0.35900  1.000 36.03132 ? 73  ASN A OD1 1 
ATOM   505  N ND2 . ASN A 1 73  ? -4.27500  18.08400  0.47500  1.000 42.21771 ? 73  ASN A ND2 1 
ATOM   506  N N   . ILE A 1 74  ? -3.17900  13.85300  3.45100  1.000 27.49673 ? 74  ILE A N   1 
ATOM   507  C CA  . ILE A 1 74  ? -2.57600  13.93800  4.77600  1.000 27.91394 ? 74  ILE A CA  1 
ATOM   508  C C   . ILE A 1 74  ? -1.06900  14.01100  4.58300  1.000 24.73764 ? 74  ILE A C   1 
ATOM   509  O O   . ILE A 1 74  ? -0.43300  13.02200  4.19900  1.000 21.69086 ? 74  ILE A O   1 
ATOM   510  C CB  . ILE A 1 74  ? -2.97100  12.74600  5.65800  1.000 24.35618 ? 74  ILE A CB  1 
ATOM   511  C CG1 . ILE A 1 74  ? -4.48400  12.72900  5.87600  1.000 27.46092 ? 74  ILE A CG1 1 
ATOM   512  C CG2 . ILE A 1 74  ? -2.23800  12.80300  6.98800  1.000 23.64885 ? 74  ILE A CG2 1 
ATOM   513  C CD1 . ILE A 1 74  ? -4.99200  11.47500  6.54000  1.000 25.26494 ? 74  ILE A CD1 1 
ATOM   514  N N   . THR A 1 75  ? -0.49100  15.18200  4.85000  1.000 21.22608 ? 75  THR A N   1 
ATOM   515  C CA  . THR A 1 75  ? 0.90800   15.43900  4.54900  1.000 25.15983 ? 75  THR A CA  1 
ATOM   516  C C   . THR A 1 75  ? 1.75700   15.78300  5.76500  1.000 23.11061 ? 75  THR A C   1 
ATOM   517  O O   . THR A 1 75  ? 2.98100   15.87700  5.62800  1.000 25.91721 ? 75  THR A O   1 
ATOM   518  C CB  . THR A 1 75  ? 1.03100   16.58300  3.52900  1.000 30.88967 ? 75  THR A CB  1 
ATOM   519  O OG1 . THR A 1 75  ? 0.78300   17.83100  4.18600  1.000 32.81709 ? 75  THR A OG1 1 
ATOM   520  C CG2 . THR A 1 75  ? 0.01500   16.40800  2.40900  1.000 28.29125 ? 75  THR A CG2 1 
ATOM   521  N N   . THR A 1 76  ? 1.15900   15.98100  6.93200  1.000 21.15940 ? 76  THR A N   1 
ATOM   522  C CA  . THR A 1 76  ? 1.87300   16.29200  8.16000  1.000 26.76192 ? 76  THR A CA  1 
ATOM   523  C C   . THR A 1 76  ? 1.40000   15.36000  9.26300  1.000 20.98143 ? 76  THR A C   1 
ATOM   524  O O   . THR A 1 76  ? 0.32500   14.76100  9.15900  1.000 20.86495 ? 76  THR A O   1 
ATOM   525  C CB  . THR A 1 76  ? 1.65100   17.75200  8.58700  1.000 22.49873 ? 76  THR A CB  1 
ATOM   526  O OG1 . THR A 1 76  ? 0.29800   17.92100  9.02400  1.000 28.47852 ? 76  THR A OG1 1 
ATOM   527  C CG2 . THR A 1 76  ? 1.93100   18.70700  7.43400  1.000 24.04172 ? 76  THR A CG2 1 
ATOM   528  N N   . PRO A 1 77  ? 2.18700   15.20500  10.33500 1.000 22.15054 ? 77  PRO A N   1 
ATOM   529  C CA  . PRO A 1 77  ? 1.73400   14.35200  11.44700 1.000 23.10788 ? 77  PRO A CA  1 
ATOM   530  C C   . PRO A 1 77  ? 0.46900   14.85000  12.12500 1.000 24.96430 ? 77  PRO A C   1 
ATOM   531  O O   . PRO A 1 77  ? -0.33400  14.03200  12.59000 1.000 20.13344 ? 77  PRO A O   1 
ATOM   532  C CB  . PRO A 1 77  ? 2.92900   14.36600  12.41000 1.000 28.47333 ? 77  PRO A CB  1 
ATOM   533  C CG  . PRO A 1 77  ? 4.10400   14.70500  11.55700 1.000 24.09383 ? 77  PRO A CG  1 
ATOM   534  C CD  . PRO A 1 77  ? 3.58800   15.63100  10.50000 1.000 24.65413 ? 77  PRO A CD  1 
ATOM   535  N N   . GLU A 1 78  ? 0.26400   16.16700  12.20700 1.000 23.82454 ? 78  GLU A N   1 
ATOM   536  C CA  . GLU A 1 78  ? -0.93500  16.68100  12.85900 1.000 24.51598 ? 78  GLU A CA  1 
ATOM   537  C C   . GLU A 1 78  ? -2.15800  16.57300  11.95900 1.000 20.16229 ? 78  GLU A C   1 
ATOM   538  O O   . GLU A 1 78  ? -3.28300  16.47100  12.46100 1.000 20.59080 ? 78  GLU A O   1 
ATOM   539  C CB  . GLU A 1 78  ? -0.72600  18.13100  13.30000 1.000 26.74102 ? 78  GLU A CB  1 
ATOM   540  C CG  . GLU A 1 78  ? -1.77400  18.63300  14.29000 1.000 27.05086 ? 78  GLU A CG  1 
ATOM   541  C CD  . GLU A 1 78  ? -1.78700  17.84100  15.59000 1.000 29.47244 ? 78  GLU A CD  1 
ATOM   542  O OE1 . GLU A 1 78  ? -0.72600  17.30900  15.98600 1.000 26.81725 ? 78  GLU A OE1 1 
ATOM   543  O OE2 . GLU A 1 78  ? -2.86100  17.74800  16.22100 1.000 34.45895 ? 78  GLU A OE2 1 
ATOM   544  N N   . GLU A 1 79  ? -1.96500  16.60000  10.63700 1.000 19.27747 ? 79  GLU A N   1 
ATOM   545  C CA  . GLU A 1 79  ? -3.06300  16.27100  9.73600  1.000 19.79257 ? 79  GLU A CA  1 
ATOM   546  C C   . GLU A 1 79  ? -3.45600  14.80500  9.86700  1.000 21.84941 ? 79  GLU A C   1 
ATOM   547  O O   . GLU A 1 79  ? -4.61200  14.44500  9.61900  1.000 25.16266 ? 79  GLU A O   1 
ATOM   548  C CB  . GLU A 1 79  ? -2.68200  16.60200  8.29200  1.000 24.64967 ? 79  GLU A CB  1 
ATOM   549  C CG  . GLU A 1 79  ? -2.71400  18.09500  7.97300  1.000 26.91723 ? 79  GLU A CG  1 
ATOM   550  C CD  . GLU A 1 79  ? -2.25500  18.40500  6.56000  1.000 30.40976 ? 79  GLU A CD  1 
ATOM   551  O OE1 . GLU A 1 79  ? -1.80900  17.47700  5.85500  1.000 25.35569 ? 79  GLU A OE1 1 
ATOM   552  O OE2 . GLU A 1 79  ? -2.33900  19.58100  6.15200  1.000 31.49910 ? 79  GLU A OE2 1 
ATOM   553  N N   . PHE A 1 80  ? -2.51000  13.95000  10.26200 1.000 20.48837 ? 80  PHE A N   1 
ATOM   554  C CA  . PHE A 1 80  ? -2.84700  12.56300  10.55600 1.000 24.12579 ? 80  PHE A CA  1 
ATOM   555  C C   . PHE A 1 80  ? -3.60100  12.45400  11.87400 1.000 23.50179 ? 80  PHE A C   1 
ATOM   556  O O   . PHE A 1 80  ? -4.56700  11.69100  11.97700 1.000 22.69690 ? 80  PHE A O   1 
ATOM   557  C CB  . PHE A 1 80  ? -1.58000  11.70700  10.58400 1.000 22.94397 ? 80  PHE A CB  1 
ATOM   558  C CG  . PHE A 1 80  ? -1.84100  10.25400  10.86000 1.000 20.71144 ? 80  PHE A CG  1 
ATOM   559  C CD1 . PHE A 1 80  ? -2.60700  9.50000   9.98700  1.000 22.18547 ? 80  PHE A CD1 1 
ATOM   560  C CD2 . PHE A 1 80  ? -1.32200  9.64300   11.99000 1.000 24.55905 ? 80  PHE A CD2 1 
ATOM   561  C CE1 . PHE A 1 80  ? -2.85400  8.16200   10.23600 1.000 24.93189 ? 80  PHE A CE1 1 
ATOM   562  C CE2 . PHE A 1 80  ? -1.56300  8.30500   12.24300 1.000 20.44741 ? 80  PHE A CE2 1 
ATOM   563  C CZ  . PHE A 1 80  ? -2.32900  7.56400   11.36400 1.000 23.52320 ? 80  PHE A CZ  1 
ATOM   564  N N   . ASN A 1 81  ? -3.17800  13.21200  12.89000 1.000 20.81618 ? 81  ASN A N   1 
ATOM   565  C CA  . ASN A 1 81  ? -3.88300  13.19600  14.16900 1.000 23.41424 ? 81  ASN A CA  1 
ATOM   566  C C   . ASN A 1 81  ? -5.30700  13.71300  14.02000 1.000 27.62514 ? 81  ASN A C   1 
ATOM   567  O O   . ASN A 1 81  ? -6.24300  13.14400  14.59400 1.000 25.84840 ? 81  ASN A O   1 
ATOM   568  C CB  . ASN A 1 81  ? -3.12000  14.02100  15.20600 1.000 24.24410 ? 81  ASN A CB  1 
ATOM   569  C CG  . ASN A 1 81  ? -1.78800  13.40100  15.57800 1.000 29.34807 ? 81  ASN A CG  1 
ATOM   570  O OD1 . ASN A 1 81  ? -1.63000  12.17900  15.55900 1.000 29.90070 ? 81  ASN A OD1 1 
ATOM   571  N ND2 . ASN A 1 81  ? -0.82000  14.24300  15.91700 1.000 23.06501 ? 81  ASN A ND2 1 
ATOM   572  N N   . ALA A 1 82  ? -5.49200  14.79400  13.25500 1.000 21.34515 ? 82  ALA A N   1 
ATOM   573  C CA  . ALA A 1 82  ? -6.84000  15.28300  12.98000 1.000 26.73786 ? 82  ALA A CA  1 
ATOM   574  C C   . ALA A 1 82  ? -7.66800  14.22900  12.25900 1.000 25.05220 ? 82  ALA A C   1 
ATOM   575  O O   . ALA A 1 82  ? -8.87100  14.09300  12.50900 1.000 24.42424 ? 82  ALA A O   1 
ATOM   576  C CB  . ALA A 1 82  ? -6.77400  16.56800  12.15500 1.000 21.53907 ? 82  ALA A CB  1 
ATOM   577  N N   . PHE A 1 83  ? -7.03600  13.47300  11.35800 1.000 22.25156 ? 83  PHE A N   1 
ATOM   578  C CA  . PHE A 1 83  ? -7.72800  12.38500  10.67500 1.000 26.87742 ? 83  PHE A CA  1 
ATOM   579  C C   . PHE A 1 83  ? -8.14500  11.29200  11.65300 1.000 26.37888 ? 83  PHE A C   1 
ATOM   580  O O   . PHE A 1 83  ? -9.26800  10.78000  11.58000 1.000 25.92821 ? 83  PHE A O   1 
ATOM   581  C CB  . PHE A 1 83  ? -6.83000  11.81500  9.57600  1.000 24.25667 ? 83  PHE A CB  1 
ATOM   582  C CG  . PHE A 1 83  ? -7.19400  10.42300  9.15100  1.000 27.49307 ? 83  PHE A CG  1 
ATOM   583  C CD1 . PHE A 1 83  ? -8.24500  10.20500  8.27700  1.000 33.26897 ? 83  PHE A CD1 1 
ATOM   584  C CD2 . PHE A 1 83  ? -6.47700  9.33100   9.61600  1.000 26.13567 ? 83  PHE A CD2 1 
ATOM   585  C CE1 . PHE A 1 83  ? -8.58100  8.92500   7.87900  1.000 32.08373 ? 83  PHE A CE1 1 
ATOM   586  C CE2 . PHE A 1 83  ? -6.80800  8.04800   9.22000  1.000 28.15536 ? 83  PHE A CE2 1 
ATOM   587  C CZ  . PHE A 1 83  ? -7.86300  7.84600   8.35000  1.000 31.61018 ? 83  PHE A CZ  1 
ATOM   588  N N   . LEU A 1 84  ? -7.24900  10.91600  12.57100 1.000 22.15212 ? 84  LEU A N   1 
ATOM   589  C CA  . LEU A 1 84  ? -7.57300  9.88600   13.55500 1.000 26.19764 ? 84  LEU A CA  1 
ATOM   590  C C   . LEU A 1 84  ? -8.75000  10.30500  14.42400 1.000 27.25527 ? 84  LEU A C   1 
ATOM   591  O O   . LEU A 1 84  ? -9.60100  9.47900   14.77300 1.000 24.51638 ? 84  LEU A O   1 
ATOM   592  C CB  . LEU A 1 84  ? -6.35200  9.58800   14.43100 1.000 25.88780 ? 84  LEU A CB  1 
ATOM   593  C CG  . LEU A 1 84  ? -5.14300  8.90000   13.79600 1.000 22.78728 ? 84  LEU A CG  1 
ATOM   594  C CD1 . LEU A 1 84  ? -3.99400  8.83600   14.78500 1.000 19.92103 ? 84  LEU A CD1 1 
ATOM   595  C CD2 . LEU A 1 84  ? -5.51400  7.50400   13.31900 1.000 20.02104 ? 84  LEU A CD2 1 
ATOM   596  N N   . LYS A 1 85  ? -8.80900  11.58400  14.79700 1.000 25.56639 ? 85  LYS A N   1 
ATOM   597  C CA  . LYS A 1 85  ? -9.90300  12.04500  15.64000 1.000 31.53852 ? 85  LYS A CA  1 
ATOM   598  C C   . LYS A 1 85  ? -11.21400 12.10200  14.86600 1.000 29.51705 ? 85  LYS A C   1 
ATOM   599  O O   . LYS A 1 85  ? -12.28600 11.91700  15.45100 1.000 29.49385 ? 85  LYS A O   1 
ATOM   600  C CB  . LYS A 1 85  ? -9.54900  13.40100  16.24900 1.000 28.08572 ? 85  LYS A CB  1 
ATOM   601  C CG  . LYS A 1 85  ? -8.26100  13.35600  17.07100 1.000 35.99087 ? 85  LYS A CG  1 
ATOM   602  C CD  . LYS A 1 85  ? -8.18000  14.49100  18.07600 1.000 42.66889 ? 85  LYS A CD  1 
ATOM   603  C CE  . LYS A 1 85  ? -8.00900  15.82600  17.38300 1.000 40.94381 ? 85  LYS A CE  1 
ATOM   604  N NZ  . LYS A 1 85  ? -6.79600  15.87400  16.51400 1.000 36.05600 ? 85  LYS A NZ  1 
ATOM   605  N N   . GLU A 1 86  ? -11.15100 12.33900  13.55600 1.000 25.90091 ? 86  GLU A N   1 
ATOM   606  C CA  . GLU A 1 86  ? -12.34300 12.18700  12.73000 1.000 31.28248 ? 86  GLU A CA  1 
ATOM   607  C C   . GLU A 1 86  ? -12.77900 10.72800  12.67900 1.000 29.12817 ? 86  GLU A C   1 
ATOM   608  O O   . GLU A 1 86  ? -13.98000 10.42900  12.69000 1.000 34.19702 ? 86  GLU A O   1 
ATOM   609  C CB  . GLU A 1 86  ? -12.07900 12.72400  11.32400 1.000 32.95544 ? 86  GLU A CB  1 
ATOM   610  C CG  . GLU A 1 86  ? -13.28100 13.39600  10.68500 1.000 44.61895 ? 86  GLU A CG  1 
ATOM   611  C CD  . GLU A 1 86  ? -13.14400 13.53400  9.18100  1.000 53.36468 ? 86  GLU A CD  1 
ATOM   612  O OE1 . GLU A 1 86  ? -12.75600 12.54600  8.52100  1.000 49.59227 ? 86  GLU A OE1 1 
ATOM   613  O OE2 . GLU A 1 86  ? -13.42400 14.63300  8.66000  1.000 51.76508 ? 86  GLU A OE2 1 
ATOM   614  N N   . LYS A 1 87  ? -11.81300 9.80600   12.64000 1.000 33.48078 ? 87  LYS A N   1 
ATOM   615  C CA  . LYS A 1 87  ? -12.13300 8.38300   12.64800 1.000 30.03278 ? 87  LYS A CA  1 
ATOM   616  C C   . LYS A 1 87  ? -12.79200 7.96200   13.95400 1.000 29.61133 ? 87  LYS A C   1 
ATOM   617  O O   . LYS A 1 87  ? -13.61400 7.03900   13.96800 1.000 33.78956 ? 87  LYS A O   1 
ATOM   618  C CB  . LYS A 1 87  ? -10.86700 7.56400   12.40200 1.000 34.17159 ? 87  LYS A CB  1 
ATOM   619  C CG  . LYS A 1 87  ? -10.66400 7.17200   10.95300 1.000 37.30416 ? 87  LYS A CG  1 
ATOM   620  C CD  . LYS A 1 87  ? -11.69900 6.14300   10.53000 1.000 41.58061 ? 87  LYS A CD  1 
ATOM   621  C CE  . LYS A 1 87  ? -11.65000 5.89300   9.03500  1.000 44.10977 ? 87  LYS A CE  1 
ATOM   622  N NZ  . LYS A 1 87  ? -11.97100 7.13200   8.27900  1.000 52.86539 ? 87  LYS A NZ  1 
ATOM   623  N N   . GLY A 1 88  ? -12.45200 8.62200   15.05100 1.000 30.13414 ? 88  GLY A N   1 
ATOM   624  C CA  . GLY A 1 88  ? -13.02600 8.32000   16.34600 1.000 29.02331 ? 88  GLY A CA  1 
ATOM   625  C C   . GLY A 1 88  ? -11.96500 7.96900   17.37000 1.000 31.23538 ? 88  GLY A C   1 
ATOM   626  O O   . GLY A 1 88  ? -10.79600 7.74400   17.06000 1.000 28.04040 ? 88  GLY A O   1 
ATOM   627  N N   . LYS A 1 89  ? -12.41900 7.93000   18.62500 1.000 27.95753 ? 89  LYS A N   1 
ATOM   628  C CA  . LYS A 1 89  ? -11.51900 7.65800   19.73900 1.000 31.42517 ? 89  LYS A CA  1 
ATOM   629  C C   . LYS A 1 89  ? -10.89400 6.27200   19.63100 1.000 31.90626 ? 89  LYS A C   1 
ATOM   630  O O   . LYS A 1 89  ? -9.77300  6.06000   20.10600 1.000 26.14119 ? 89  LYS A O   1 
ATOM   631  C CB  . LYS A 1 89  ? -12.27600 7.81400   21.05700 1.000 30.12892 ? 89  LYS A CB  1 
ATOM   632  C CG  . LYS A 1 89  ? -11.42300 7.69200   22.30500 1.000 35.56731 ? 89  LYS A CG  1 
ATOM   633  C CD  . LYS A 1 89  ? -12.18300 8.19100   23.52400 1.000 40.58753 ? 89  LYS A CD  1 
ATOM   634  C CE  . LYS A 1 89  ? -12.05000 7.23300   24.69600 1.000 43.43103 ? 89  LYS A CE  1 
ATOM   635  N NZ  . LYS A 1 89  ? -10.63900 7.07400   25.13400 1.000 34.46515 ? 89  LYS A NZ  1 
ATOM   636  N N   . ARG A 1 90  ? -11.59400 5.32200   19.00500 1.000 27.54583 ? 90  ARG A N   1 
ATOM   637  C CA  . ARG A 1 90  ? -11.02300 3.99200   18.81800 1.000 27.38013 ? 90  ARG A CA  1 
ATOM   638  C C   . ARG A 1 90  ? -9.76200  4.04900   17.96700 1.000 28.30951 ? 90  ARG A C   1 
ATOM   639  O O   . ARG A 1 90  ? -8.75500  3.41000   18.29400 1.000 26.12478 ? 90  ARG A O   1 
ATOM   640  C CB  . ARG A 1 90  ? -12.05100 3.06100   18.17900 1.000 28.12627 ? 90  ARG A CB  1 
ATOM   641  C CG  . ARG A 1 90  ? -11.48300 1.71100   17.75900 1.000 28.59112 ? 90  ARG A CG  1 
ATOM   642  C CD  . ARG A 1 90  ? -10.96500 0.93500   18.95400 1.000 34.50818 ? 90  ARG A CD  1 
ATOM   643  N NE  . ARG A 1 90  ? -10.47100 -0.38500  18.58200 1.000 37.97514 ? 90  ARG A NE  1 
ATOM   644  C CZ  . ARG A 1 90  ? -9.88400  -1.22500  19.42300 1.000 42.84531 ? 90  ARG A CZ  1 
ATOM   645  N NH1 . ARG A 1 90  ? -9.68400  -0.90600  20.69200 1.000 47.25971 ? 90  ARG A NH1 1 
ATOM   646  N NH2 . ARG A 1 90  ? -9.48500  -2.41500  18.98100 1.000 41.49801 ? 90  ARG A NH2 1 
ATOM   647  N N   . ALA A 1 91  ? -9.79800  4.81000   16.87200 1.000 24.96809 ? 91  ALA A N   1 
ATOM   648  C CA  . ALA A 1 91  ? -8.62600  4.91600   16.01100 1.000 25.95498 ? 91  ALA A CA  1 
ATOM   649  C C   . ALA A 1 91  ? -7.49000  5.65100   16.71100 1.000 24.11666 ? 91  ALA A C   1 
ATOM   650  O O   . ALA A 1 91  ? -6.32400  5.25700   16.59300 1.000 22.19735 ? 91  ALA A O   1 
ATOM   651  C CB  . ALA A 1 91  ? -8.99500  5.61600   14.70500 1.000 26.37832 ? 91  ALA A CB  1 
ATOM   652  N N   . VAL A 1 92  ? -7.81400  6.72300   17.44000 1.000 25.50397 ? 92  VAL A N   1 
ATOM   653  C CA  . VAL A 1 92  ? -6.80100  7.46500   18.18800 1.000 26.40036 ? 92  VAL A CA  1 
ATOM   654  C C   . VAL A 1 92  ? -6.08100  6.53900   19.15900 1.000 24.84234 ? 92  VAL A C   1 
ATOM   655  O O   . VAL A 1 92  ? -4.84600  6.48700   19.20000 1.000 23.86826 ? 92  VAL A O   1 
ATOM   656  C CB  . VAL A 1 92  ? -7.44100  8.65600   18.92500 1.000 24.65362 ? 92  VAL A CB  1 
ATOM   657  C CG1 . VAL A 1 92  ? -6.43000  9.31600   19.85600 1.000 23.52248 ? 92  VAL A CG1 1 
ATOM   658  C CG2 . VAL A 1 92  ? -8.00000  9.66800   17.93200 1.000 26.96013 ? 92  VAL A CG2 1 
ATOM   659  N N   . ASP A 1 93  ? -6.85000  5.78600   19.94900 1.000 23.65499 ? 93  ASP A N   1 
ATOM   660  C CA  . ASP A 1 93  ? -6.25900  4.93900   20.98000 1.000 30.67463 ? 93  ASP A CA  1 
ATOM   661  C C   . ASP A 1 93  ? -5.54000  3.73400   20.38700 1.000 26.12853 ? 93  ASP A C   1 
ATOM   662  O O   . ASP A 1 93  ? -4.54500  3.27200   20.95600 1.000 26.69092 ? 93  ASP A O   1 
ATOM   663  C CB  . ASP A 1 93  ? -7.33900  4.48400   21.96300 1.000 29.66914 ? 93  ASP A CB  1 
ATOM   664  C CG  . ASP A 1 93  ? -7.88900  5.62900   22.79300 1.000 31.39916 ? 93  ASP A CG  1 
ATOM   665  O OD1 . ASP A 1 93  ? -7.34100  6.74900   22.70300 1.000 32.55558 ? 93  ASP A OD1 1 
ATOM   666  O OD2 . ASP A 1 93  ? -8.87000  5.41100   23.53500 1.000 34.23814 ? 93  ASP A OD2 1 
ATOM   667  N N   . LEU A 1 94  ? -6.02300  3.21000   19.25800 1.000 19.88312 ? 94  LEU A N   1 
ATOM   668  C CA  . LEU A 1 94  ? -5.36200  2.06600   18.63700 1.000 24.89174 ? 94  LEU A CA  1 
ATOM   669  C C   . LEU A 1 94  ? -3.97000  2.43600   18.13900 1.000 26.34248 ? 94  LEU A C   1 
ATOM   670  O O   . LEU A 1 94  ? -3.01500  1.67200   18.32300 1.000 23.96035 ? 94  LEU A O   1 
ATOM   671  C CB  . LEU A 1 94  ? -6.21600  1.52200   17.49300 1.000 25.88068 ? 94  LEU A CB  1 
ATOM   672  C CG  . LEU A 1 94  ? -5.61100  0.38900   16.65900 1.000 29.83789 ? 94  LEU A CG  1 
ATOM   673  C CD1 . LEU A 1 94  ? -5.20600  -0.78500  17.53800 1.000 30.03938 ? 94  LEU A CD1 1 
ATOM   674  C CD2 . LEU A 1 94  ? -6.58800  -0.06300  15.58800 1.000 30.28263 ? 94  LEU A CD2 1 
ATOM   675  N N   . VAL A 1 95  ? -3.83600  3.60600   17.51100 1.000 24.31627 ? 95  VAL A N   1 
ATOM   676  C CA  . VAL A 1 95  ? -2.52800  4.04700   17.03900 1.000 22.75554 ? 95  VAL A CA  1 
ATOM   677  C C   . VAL A 1 95  ? -1.61700  4.36800   18.21600 1.000 20.81507 ? 95  VAL A C   1 
ATOM   678  O O   . VAL A 1 95  ? -0.42100  4.05700   18.19100 1.000 16.37505 ? 95  VAL A O   1 
ATOM   679  C CB  . VAL A 1 95  ? -2.68100  5.24900   16.08800 1.000 20.57608 ? 95  VAL A CB  1 
ATOM   680  C CG1 . VAL A 1 95  ? -1.31900  5.77000   15.66000 1.000 19.68774 ? 95  VAL A CG1 1 
ATOM   681  C CG2 . VAL A 1 95  ? -3.50200  4.85700   14.87500 1.000 19.92108 ? 95  VAL A CG2 1 
ATOM   682  N N   . ALA A 1 96  ? -2.16400  4.98100   19.27000 1.000 24.15423 ? 96  ALA A N   1 
ATOM   683  C CA  . ALA A 1 96  ? -1.35900  5.28800   20.44800 1.000 23.81884 ? 96  ALA A CA  1 
ATOM   684  C C   . ALA A 1 96  ? -0.81600  4.01900   21.09300 1.000 24.93128 ? 96  ALA A C   1 
ATOM   685  O O   . ALA A 1 96  ? 0.31500   4.00000   21.59300 1.000 24.24064 ? 96  ALA A O   1 
ATOM   686  C CB  . ALA A 1 96  ? -2.18400  6.09100   21.45300 1.000 27.65701 ? 96  ALA A CB  1 
ATOM   687  N N   . THR A 1 97  ? -1.61000  2.94600   21.08900 1.000 23.18313 ? 97  THR A N   1 
ATOM   688  C CA  . THR A 1 97  ? -1.15700  1.67700   21.65100 1.000 27.61741 ? 97  THR A CA  1 
ATOM   689  C C   . THR A 1 97  ? -0.02000  1.08400   20.82600 1.000 28.78106 ? 97  THR A C   1 
ATOM   690  O O   . THR A 1 97  ? 0.98000   0.60900   21.37800 1.000 27.05364 ? 97  THR A O   1 
ATOM   691  C CB  . THR A 1 97  ? -2.32900  0.69800   21.73400 1.000 29.41397 ? 97  THR A CB  1 
ATOM   692  O OG1 . THR A 1 97  ? -3.32600  1.22100   22.62100 1.000 35.67160 ? 97  THR A OG1 1 
ATOM   693  C CG2 . THR A 1 97  ? -1.86300  -0.65900  22.24000 1.000 37.07952 ? 97  THR A CG2 1 
ATOM   694  N N   . LEU A 1 98  ? -0.16000  1.09500   19.49900 1.000 28.16477 ? 98  LEU A N   1 
ATOM   695  C CA  . LEU A 1 98  ? 0.90900   0.59100   18.64200 1.000 25.12733 ? 98  LEU A CA  1 
ATOM   696  C C   . LEU A 1 98  ? 2.15300   1.46300   18.74700 1.000 21.98097 ? 98  LEU A C   1 
ATOM   697  O O   . LEU A 1 98  ? 3.28000   0.95800   18.70000 1.000 21.57385 ? 98  LEU A O   1 
ATOM   698  C CB  . LEU A 1 98  ? 0.42100   0.52000   17.19800 1.000 24.19045 ? 98  LEU A CB  1 
ATOM   699  C CG  . LEU A 1 98  ? -0.74900  -0.43700  16.98300 1.000 33.07191 ? 98  LEU A CG  1 
ATOM   700  C CD1 . LEU A 1 98  ? -1.49400  -0.08200  15.71800 1.000 28.41315 ? 98  LEU A CD1 1 
ATOM   701  C CD2 . LEU A 1 98  ? -0.25100  -1.87300  16.92700 1.000 34.29095 ? 98  LEU A CD2 1 
ATOM   702  N N   . THR A 1 99  ? 1.96400   2.77600   18.88800 1.000 23.34674 ? 99  THR A N   1 
ATOM   703  C CA  . THR A 1 99  ? 3.08500   3.68700   19.08600 1.000 23.87114 ? 99  THR A CA  1 
ATOM   704  C C   . THR A 1 99  ? 3.91500   3.28100   20.29600 1.000 20.32001 ? 99  THR A C   1 
ATOM   705  O O   . THR A 1 99  ? 5.13800   3.12800   20.20700 1.000 24.09167 ? 99  THR A O   1 
ATOM   706  C CB  . THR A 1 99  ? 2.56400   5.11600   19.25100 1.000 25.27467 ? 99  THR A CB  1 
ATOM   707  O OG1 . THR A 1 99  ? 2.05800   5.59100   17.99900 1.000 25.13729 ? 99  THR A OG1 1 
ATOM   708  C CG2 . THR A 1 99  ? 3.66500   6.04100   19.74100 1.000 23.04457 ? 99  THR A CG2 1 
ATOM   709  N N   . ASN A 1 100 ? 3.25600   3.09100   21.44100 1.000 21.38838 ? 100 ASN A N   1 
ATOM   710  C CA  . ASN A 1 100 ? 3.97600   2.70100   22.64600 1.000 25.99085 ? 100 ASN A CA  1 
ATOM   711  C C   . ASN A 1 100 ? 4.52000   1.28400   22.54100 1.000 22.82076 ? 100 ASN A C   1 
ATOM   712  O O   . ASN A 1 100 ? 5.53000   0.96200   23.17600 1.000 20.66256 ? 100 ASN A O   1 
ATOM   713  C CB  . ASN A 1 100 ? 3.06700   2.85300   23.86200 1.000 28.42852 ? 100 ASN A CB  1 
ATOM   714  C CG  . ASN A 1 100 ? 2.67900   4.30300   24.11400 1.000 32.63823 ? 100 ASN A CG  1 
ATOM   715  O OD1 . ASN A 1 100 ? 3.44200   5.22000   23.81200 1.000 36.61733 ? 100 ASN A OD1 1 
ATOM   716  N ND2 . ASN A 1 100 ? 1.49100   4.51400   24.66600 1.000 37.61230 ? 100 ASN A ND2 1 
ATOM   717  N N   . ALA A 1 101 ? 3.87800   0.42900   21.74100 1.000 21.72319 ? 101 ALA A N   1 
ATOM   718  C CA  . ALA A 1 101 ? 4.41900   -0.90400  21.50200 1.000 25.30987 ? 101 ALA A CA  1 
ATOM   719  C C   . ALA A 1 101 ? 5.73200   -0.83300  20.73100 1.000 20.15399 ? 101 ALA A C   1 
ATOM   720  O O   . ALA A 1 101 ? 6.67400   -1.57200  21.03400 1.000 29.25745 ? 101 ALA A O   1 
ATOM   721  C CB  . ALA A 1 101 ? 3.39900   -1.75900  20.75200 1.000 29.09507 ? 101 ALA A CB  1 
ATOM   722  N N   . TYR A 1 102 ? 5.80800   0.04900   19.73000 1.000 18.78414 ? 102 TYR A N   1 
ATOM   723  C CA  . TYR A 1 102 ? 7.06300   0.26500   19.01800 1.000 22.94604 ? 102 TYR A CA  1 
ATOM   724  C C   . TYR A 1 102 ? 8.16000   0.73600   19.96300 1.000 25.10262 ? 102 TYR A C   1 
ATOM   725  O O   . TYR A 1 102 ? 9.32000   0.32400   19.83700 1.000 18.55428 ? 102 TYR A O   1 
ATOM   726  C CB  . TYR A 1 102 ? 6.86200   1.28200   17.89500 1.000 22.05003 ? 102 TYR A CB  1 
ATOM   727  C CG  . TYR A 1 102 ? 6.40000   0.69200   16.58200 1.000 23.25170 ? 102 TYR A CG  1 
ATOM   728  C CD1 . TYR A 1 102 ? 5.22400   -0.04200  16.49800 1.000 25.78278 ? 102 TYR A CD1 1 
ATOM   729  C CD2 . TYR A 1 102 ? 7.13500   0.88500   15.42000 1.000 26.46132 ? 102 TYR A CD2 1 
ATOM   730  C CE1 . TYR A 1 102 ? 4.79900   -0.57400  15.29500 1.000 27.21885 ? 102 TYR A CE1 1 
ATOM   731  C CE2 . TYR A 1 102 ? 6.71800   0.35700   14.21300 1.000 28.20469 ? 102 TYR A CE2 1 
ATOM   732  C CZ  . TYR A 1 102 ? 5.55000   -0.37300  14.15700 1.000 28.77882 ? 102 TYR A CZ  1 
ATOM   733  O OH  . TYR A 1 102 ? 5.12800   -0.90200  12.95900 1.000 26.81955 ? 102 TYR A OH  1 
ATOM   734  N N   . ILE A 1 103 ? 7.81500   1.61000   20.91000 1.000 25.31292 ? 103 ILE A N   1 
ATOM   735  C CA  . ILE A 1 103 ? 8.79800   2.09200   21.87600 1.000 22.31121 ? 103 ILE A CA  1 
ATOM   736  C C   . ILE A 1 103 ? 9.28700   0.94700   22.75400 1.000 23.15927 ? 103 ILE A C   1 
ATOM   737  O O   . ILE A 1 103 ? 10.48900  0.81400   23.01400 1.000 27.03325 ? 103 ILE A O   1 
ATOM   738  C CB  . ILE A 1 103 ? 8.20300   3.23700   22.71500 1.000 23.27526 ? 103 ILE A CB  1 
ATOM   739  C CG1 . ILE A 1 103 ? 7.93600   4.46300   21.83800 1.000 21.76117 ? 103 ILE A CG1 1 
ATOM   740  C CG2 . ILE A 1 103 ? 9.12800   3.59500   23.87000 1.000 23.37106 ? 103 ILE A CG2 1 
ATOM   741  C CD1 . ILE A 1 103 ? 9.19100   5.11000   21.30300 1.000 19.89937 ? 103 ILE A CD1 1 
ATOM   742  N N   . ALA A 1 104 ? 8.36700   0.09800   23.21800 1.000 23.91475 ? 104 ALA A N   1 
ATOM   743  C CA  . ALA A 1 104 ? 8.75600   -1.02400  24.06600 1.000 28.31886 ? 104 ALA A CA  1 
ATOM   744  C C   . ALA A 1 104 ? 9.65000   -2.00300  23.31500 1.000 30.84295 ? 104 ALA A C   1 
ATOM   745  O O   . ALA A 1 104 ? 10.59900  -2.55200  23.88800 1.000 27.72898 ? 104 ALA A O   1 
ATOM   746  C CB  . ALA A 1 104 ? 7.51200   -1.73400  24.60000 1.000 25.43691 ? 104 ALA A CB  1 
ATOM   747  N N   . VAL A 1 105 ? 9.36300   -2.23200  22.03000 1.000 27.48281 ? 105 VAL A N   1 
ATOM   748  C CA  . VAL A 1 105 ? 10.18700  -3.13200  21.22500 1.000 27.88169 ? 105 VAL A CA  1 
ATOM   749  C C   . VAL A 1 105 ? 11.60100  -2.58000  21.08400 1.000 29.57856 ? 105 VAL A C   1 
ATOM   750  O O   . VAL A 1 105 ? 12.58600  -3.32200  21.19200 1.000 27.53372 ? 105 VAL A O   1 
ATOM   751  C CB  . VAL A 1 105 ? 9.52700   -3.37300  19.85400 1.000 30.21671 ? 105 VAL A CB  1 
ATOM   752  C CG1 . VAL A 1 105 ? 10.51700  -3.99000  18.87900 1.000 29.16378 ? 105 VAL A CG1 1 
ATOM   753  C CG2 . VAL A 1 105 ? 8.30300   -4.26700  20.00500 1.000 27.08254 ? 105 VAL A CG2 1 
ATOM   754  N N   . LEU A 1 106 ? 11.72500  -1.27200  20.84600 1.000 25.36393 ? 106 LEU A N   1 
ATOM   755  C CA  . LEU A 1 106 ? 13.04600  -0.65500  20.77100 1.000 20.84155 ? 106 LEU A CA  1 
ATOM   756  C C   . LEU A 1 106 ? 13.77200  -0.75600  22.10700 1.000 28.48771 ? 106 LEU A C   1 
ATOM   757  O O   . LEU A 1 106 ? 14.92300  -1.20200  22.17100 1.000 26.78332 ? 106 LEU A O   1 
ATOM   758  C CB  . LEU A 1 106 ? 12.92700  0.80900   20.34200 1.000 25.89582 ? 106 LEU A CB  1 
ATOM   759  C CG  . LEU A 1 106 ? 12.36200  1.15200   18.96200 1.000 27.27273 ? 106 LEU A CG  1 
ATOM   760  C CD1 . LEU A 1 106 ? 12.42400  2.65300   18.74400 1.000 26.48811 ? 106 LEU A CD1 1 
ATOM   761  C CD2 . LEU A 1 106 ? 13.10100  0.42000   17.85700 1.000 24.44122 ? 106 LEU A CD2 1 
ATOM   762  N N   . GLU A 1 107 ? 13.10900  -0.34700  23.19100 1.000 28.46749 ? 107 GLU A N   1 
ATOM   763  C CA  . GLU A 1 107 ? 13.72700  -0.35700  24.51000 1.000 30.25143 ? 107 GLU A CA  1 
ATOM   764  C C   . GLU A 1 107 ? 13.86900  -1.75700  25.09100 1.000 30.99417 ? 107 GLU A C   1 
ATOM   765  O O   . GLU A 1 107 ? 14.44900  -1.90000  26.17200 1.000 35.33146 ? 107 GLU A O   1 
ATOM   766  C CB  . GLU A 1 107 ? 12.91400  0.51100   25.47300 1.000 29.29072 ? 107 GLU A CB  1 
ATOM   767  C CG  . GLU A 1 107 ? 12.75300  1.95600   25.02100 1.000 30.44643 ? 107 GLU A CG  1 
ATOM   768  C CD  . GLU A 1 107 ? 11.81700  2.74600   25.91900 1.000 31.49200 ? 107 GLU A CD  1 
ATOM   769  O OE1 . GLU A 1 107 ? 11.04400  2.12400   26.68000 1.000 28.88632 ? 107 GLU A OE1 1 
ATOM   770  O OE2 . GLU A 1 107 ? 11.85900  3.99300   25.86800 1.000 34.82472 ? 107 GLU A OE2 1 
ATOM   771  N N   . GLY A 1 108 ? 13.36400  -2.78300  24.41000 1.000 29.81259 ? 108 GLY A N   1 
ATOM   772  C CA  . GLY A 1 108 ? 13.35400  -4.12700  24.95300 1.000 32.99600 ? 108 GLY A CA  1 
ATOM   773  C C   . GLY A 1 108 ? 14.52000  -4.98200  24.50600 1.000 30.69118 ? 108 GLY A C   1 
ATOM   774  O O   . GLY A 1 108 ? 15.09500  -5.72100  25.30900 1.000 32.85082 ? 108 GLY A O   1 
ATOM   775  N N   . ASP A 1 109 ? 14.87100  -4.90300  23.22400 1.000 37.39237 ? 109 ASP A N   1 
ATOM   776  C CA  . ASP A 1 109 ? 16.00700  -5.64500  22.67200 1.000 36.93615 ? 109 ASP A CA  1 
ATOM   777  C C   . ASP A 1 109 ? 16.81600  -4.72900  21.76500 1.000 31.93151 ? 109 ASP A C   1 
ATOM   778  O O   . ASP A 1 109 ? 16.84800  -4.90500  20.54200 1.000 31.66896 ? 109 ASP A O   1 
ATOM   779  C CB  . ASP A 1 109 ? 15.53000  -6.88600  21.91500 1.000 38.01873 ? 109 ASP A CB  1 
ATOM   780  C CG  . ASP A 1 109 ? 16.52100  -8.03300  21.99400 1.000 41.36790 ? 109 ASP A CG  1 
ATOM   781  O OD1 . ASP A 1 109 ? 17.72400  -7.79900  21.75300 1.000 36.81517 ? 109 ASP A OD1 1 
ATOM   782  O OD2 . ASP A 1 109 ? 16.10100  -9.16400  22.31900 1.000 49.86514 ? 109 ASP A OD2 1 
ATOM   783  N N   . PRO A 1 110 ? 17.49100  -3.72600  22.33700 1.000 28.53809 ? 110 PRO A N   1 
ATOM   784  C CA  . PRO A 1 110 ? 18.36200  -2.87700  21.51000 1.000 25.91720 ? 110 PRO A CA  1 
ATOM   785  C C   . PRO A 1 110 ? 19.56600  -3.61400  20.95000 1.000 25.21312 ? 110 PRO A C   1 
ATOM   786  O O   . PRO A 1 110 ? 20.13900  -3.16000  19.95200 1.000 26.20876 ? 110 PRO A O   1 
ATOM   787  C CB  . PRO A 1 110 ? 18.78500  -1.76100  22.47500 1.000 32.68839 ? 110 PRO A CB  1 
ATOM   788  C CG  . PRO A 1 110 ? 18.64000  -2.35900  23.82700 1.000 29.14079 ? 110 PRO A CG  1 
ATOM   789  C CD  . PRO A 1 110 ? 17.47400  -3.29200  23.74500 1.000 32.46649 ? 110 PRO A CD  1 
ATOM   790  N N   . GLU A 1 111 ? 19.96400  -4.73500  21.55500 1.000 26.32787 ? 111 GLU A N   1 
ATOM   791  C CA  . GLU A 1 111 ? 21.09500  -5.49400  21.03200 1.000 31.58584 ? 111 GLU A CA  1 
ATOM   792  C C   . GLU A 1 111 ? 20.74300  -6.16400  19.70900 1.000 30.24098 ? 111 GLU A C   1 
ATOM   793  O O   . GLU A 1 111 ? 21.54800  -6.15900  18.77100 1.000 29.06030 ? 111 GLU A O   1 
ATOM   794  C CB  . GLU A 1 111 ? 21.54800  -6.53100  22.06000 1.000 38.48305 ? 111 GLU A CB  1 
ATOM   795  C CG  . GLU A 1 111 ? 23.05800  -6.65100  22.20000 1.000 40.88416 ? 111 GLU A CG  1 
ATOM   796  C CD  . GLU A 1 111 ? 23.46700  -7.61700  23.29600 1.000 46.08571 ? 111 GLU A CD  1 
ATOM   797  O OE1 . GLU A 1 111 ? 22.58200  -8.31100  23.83800 1.000 53.70857 ? 111 GLU A OE1 1 
ATOM   798  O OE2 . GLU A 1 111 ? 24.67300  -7.68000  23.61600 1.000 49.14370 ? 111 GLU A OE2 1 
ATOM   799  N N   . ALA A 1 112 ? 19.54200  -6.74000  19.61200 1.000 28.74264 ? 112 ALA A N   1 
ATOM   800  C CA  . ALA A 1 112 ? 19.12300  -7.37200  18.36400 1.000 29.00243 ? 112 ALA A CA  1 
ATOM   801  C C   . ALA A 1 112 ? 18.90200  -6.33700  17.26800 1.000 30.46937 ? 112 ALA A C   1 
ATOM   802  O O   . ALA A 1 112 ? 19.22200  -6.58700  16.10000 1.000 24.13350 ? 112 ALA A O   1 
ATOM   803  C CB  . ALA A 1 112 ? 17.85700  -8.19600  18.59000 1.000 26.82240 ? 112 ALA A CB  1 
ATOM   804  N N   . ILE A 1 113 ? 18.35300  -5.17200  17.62300 1.000 27.45307 ? 113 ILE A N   1 
ATOM   805  C CA  . ILE A 1 113 ? 18.16900  -4.10300  16.64400 1.000 23.25278 ? 113 ILE A CA  1 
ATOM   806  C C   . ILE A 1 113 ? 19.51100  -3.67100  16.07200 1.000 25.14998 ? 113 ILE A C   1 
ATOM   807  O O   . ILE A 1 113 ? 19.64300  -3.43100  14.86500 1.000 18.66075 ? 113 ILE A O   1 
ATOM   808  C CB  . ILE A 1 113 ? 17.42500  -2.91700  17.28300 1.000 23.07493 ? 113 ILE A CB  1 
ATOM   809  C CG1 . ILE A 1 113 ? 16.05900  -3.36500  17.79600 1.000 25.67732 ? 113 ILE A CG1 1 
ATOM   810  C CG2 . ILE A 1 113 ? 17.27800  -1.77800  16.28300 1.000 27.20932 ? 113 ILE A CG2 1 
ATOM   811  C CD1 . ILE A 1 113 ? 15.29800  -2.29600  18.52100 1.000 24.86773 ? 113 ILE A CD1 1 
ATOM   812  N N   . ALA A 1 114 ? 20.52800  -3.56500  16.93100 1.000 23.11473 ? 114 ALA A N   1 
ATOM   813  C CA  . ALA A 1 114 ? 21.85500  -3.17300  16.47300 1.000 23.41469 ? 114 ALA A CA  1 
ATOM   814  C C   . ALA A 1 114 ? 22.41100  -4.18300  15.47900 1.000 22.69894 ? 114 ALA A C   1 
ATOM   815  O O   . ALA A 1 114 ? 22.91000  -3.81200  14.41100 1.000 22.76381 ? 114 ALA A O   1 
ATOM   816  C CB  . ALA A 1 114 ? 22.79600  -3.01500  17.66900 1.000 21.97372 ? 114 ALA A CB  1 
ATOM   817  N N   . ARG A 1 115 ? 22.33400  -5.47200  15.81700 1.000 24.99620 ? 115 ARG A N   1 
ATOM   818  C CA  . ARG A 1 115 ? 22.82500  -6.49900  14.90400 1.000 25.84531 ? 115 ARG A CA  1 
ATOM   819  C C   . ARG A 1 115 ? 21.99600  -6.55900  13.62900 1.000 25.30224 ? 115 ARG A C   1 
ATOM   820  O O   . ARG A 1 115 ? 22.52500  -6.88600  12.56200 1.000 31.00501 ? 115 ARG A O   1 
ATOM   821  C CB  . ARG A 1 115 ? 22.83200  -7.86100  15.59700 1.000 29.65189 ? 115 ARG A CB  1 
ATOM   822  C CG  . ARG A 1 115 ? 23.83400  -7.97400  16.73500 1.000 32.26521 ? 115 ARG A CG  1 
ATOM   823  C CD  . ARG A 1 115 ? 23.96900  -9.41400  17.21000 1.000 35.63988 ? 115 ARG A CD  1 
ATOM   824  N NE  . ARG A 1 115 ? 22.81500  -9.86200  17.98000 1.000 41.58000 ? 115 ARG A NE  1 
ATOM   825  C CZ  . ARG A 1 115 ? 22.77600  -9.91800  19.30500 1.000 41.65016 ? 115 ARG A CZ  1 
ATOM   826  N NH1 . ARG A 1 115 ? 23.81300  -9.55600  20.04300 1.000 40.83429 ? 115 ARG A NH1 1 
ATOM   827  N NH2 . ARG A 1 115 ? 21.66900  -10.35100 19.90400 1.000 41.12462 ? 115 ARG A NH2 1 
ATOM   828  N N   . PHE A 1 116 ? 20.70100  -6.24400  13.71600 1.000 24.38042 ? 116 PHE A N   1 
ATOM   829  C CA  . PHE A 1 116 ? 19.84900  -6.28900  12.53200 1.000 26.75043 ? 116 PHE A CA  1 
ATOM   830  C C   . PHE A 1 116 ? 20.16100  -5.14100  11.58000 1.000 25.72831 ? 116 PHE A C   1 
ATOM   831  O O   . PHE A 1 116 ? 20.22400  -5.33800  10.36100 1.000 26.98060 ? 116 PHE A O   1 
ATOM   832  C CB  . PHE A 1 116 ? 18.37700  -6.26700  12.94500 1.000 27.33193 ? 116 PHE A CB  1 
ATOM   833  C CG  . PHE A 1 116 ? 17.42200  -6.35300  11.79100 1.000 26.18135 ? 116 PHE A CG  1 
ATOM   834  C CD1 . PHE A 1 116 ? 17.24100  -7.54700  11.10900 1.000 28.86934 ? 116 PHE A CD1 1 
ATOM   835  C CD2 . PHE A 1 116 ? 16.69600  -5.24300  11.39300 1.000 25.78268 ? 116 PHE A CD2 1 
ATOM   836  C CE1 . PHE A 1 116 ? 16.35800  -7.62900  10.04600 1.000 28.97933 ? 116 PHE A CE1 1 
ATOM   837  C CE2 . PHE A 1 116 ? 15.81200  -5.31700  10.33100 1.000 29.42066 ? 116 PHE A CE2 1 
ATOM   838  C CZ  . PHE A 1 116 ? 15.64300  -6.51200  9.65800  1.000 30.66697 ? 116 PHE A CZ  1 
ATOM   839  N N   . LEU A 1 117 ? 20.36300  -3.93800  12.11200 1.000 21.94776 ? 117 LEU A N   1 
ATOM   840  C CA  . LEU A 1 117 ? 20.66400  -2.77300  11.29200 1.000 23.86913 ? 117 LEU A CA  1 
ATOM   841  C C   . LEU A 1 117 ? 22.15300  -2.59500  11.02400 1.000 25.84855 ? 117 LEU A C   1 
ATOM   842  O O   . LEU A 1 117 ? 22.52400  -1.69500  10.26400 1.000 31.57927 ? 117 LEU A O   1 
ATOM   843  C CB  . LEU A 1 117 ? 20.11100  -1.50700  11.95700 1.000 24.57926 ? 117 LEU A CB  1 
ATOM   844  C CG  . LEU A 1 117 ? 18.58700  -1.43700  12.05500 1.000 25.11255 ? 117 LEU A CG  1 
ATOM   845  C CD1 . LEU A 1 117 ? 18.15600  -0.28000  12.93900 1.000 25.66259 ? 117 LEU A CD1 1 
ATOM   846  C CD2 . LEU A 1 117 ? 17.97500  -1.31900  10.66800 1.000 17.89058 ? 117 LEU A CD2 1 
ATOM   847  N N   . GLY A 1 118 ? 23.00700  -3.42100  11.61900 1.000 30.03211 ? 118 GLY A N   1 
ATOM   848  C CA  . GLY A 1 118 ? 24.44000  -3.27200  11.43100 1.000 32.39227 ? 118 GLY A CA  1 
ATOM   849  C C   . GLY A 1 118 ? 25.00300  -1.99200  12.00900 1.000 31.79818 ? 118 GLY A C   1 
ATOM   850  O O   . GLY A 1 118 ? 25.85100  -1.35000  11.37600 1.000 33.49105 ? 118 GLY A O   1 
ATOM   851  N N   . ILE A 1 119 ? 24.54500  -1.59700  13.19700 1.000 29.98828 ? 119 ILE A N   1 
ATOM   852  C CA  . ILE A 1 119 ? 25.00000  -0.38500  13.86200 1.000 30.16517 ? 119 ILE A CA  1 
ATOM   853  C C   . ILE A 1 119 ? 25.35300  -0.73000  15.30300 1.000 26.93677 ? 119 ILE A C   1 
ATOM   854  O O   . ILE A 1 119 ? 25.07700  -1.82700  15.78900 1.000 28.36888 ? 119 ILE A O   1 
ATOM   855  C CB  . ILE A 1 119 ? 23.94700  0.74400   13.81700 1.000 30.12103 ? 119 ILE A CB  1 
ATOM   856  C CG1 . ILE A 1 119 ? 22.68400  0.32100   14.57100 1.000 26.59691 ? 119 ILE A CG1 1 
ATOM   857  C CG2 . ILE A 1 119 ? 23.61800  1.11700   12.37700 1.000 27.85217 ? 119 ILE A CG2 1 
ATOM   858  C CD1 . ILE A 1 119 ? 21.55900  1.33000   14.50500 1.000 21.93672 ? 119 ILE A CD1 1 
ATOM   859  N N   . SER A 1 120 ? 25.97000  0.22900   15.98600 1.000 28.08014 ? 120 SER A N   1 
ATOM   860  C CA  . SER A 1 120 ? 26.36400  0.02700   17.37000 1.000 31.72837 ? 120 SER A CA  1 
ATOM   861  C C   . SER A 1 120 ? 25.17200  0.22100   18.30300 1.000 27.20330 ? 120 SER A C   1 
ATOM   862  O O   . SER A 1 120 ? 24.12100  0.74500   17.92200 1.000 27.44866 ? 120 SER A O   1 
ATOM   863  C CB  . SER A 1 120 ? 27.49000  0.98500   17.75300 1.000 31.01202 ? 120 SER A CB  1 
ATOM   864  O OG  . SER A 1 120 ? 27.05400  2.33400   17.70600 1.000 29.46310 ? 120 SER A OG  1 
ATOM   865  N N   . LEU A 1 121 ? 25.35100  -0.21700  19.55300 1.000 25.52824 ? 121 LEU A N   1 
ATOM   866  C CA  . LEU A 1 121 ? 24.33800  0.02300   20.57500 1.000 28.02629 ? 121 LEU A CA  1 
ATOM   867  C C   . LEU A 1 121 ? 24.11900  1.51100   20.80200 1.000 25.88995 ? 121 LEU A C   1 
ATOM   868  O O   . LEU A 1 121 ? 22.99800  1.93400   21.10700 1.000 24.03566 ? 121 LEU A O   1 
ATOM   869  C CB  . LEU A 1 121 ? 24.73800  -0.65400  21.88700 1.000 30.25202 ? 121 LEU A CB  1 
ATOM   870  C CG  . LEU A 1 121 ? 24.15600  -2.03400  22.20200 1.000 34.52877 ? 121 LEU A CG  1 
ATOM   871  C CD1 . LEU A 1 121 ? 24.51100  -3.05000  21.13000 1.000 35.69952 ? 121 LEU A CD1 1 
ATOM   872  C CD2 . LEU A 1 121 ? 24.64300  -2.50400  23.56800 1.000 38.27079 ? 121 LEU A CD2 1 
ATOM   873  N N   . GLU A 1 122 ? 25.17500  2.31700   20.65700 1.000 27.74535 ? 122 GLU A N   1 
ATOM   874  C CA  . GLU A 1 122 ? 25.04100  3.75900   20.83200 1.000 29.01174 ? 122 GLU A CA  1 
ATOM   875  C C   . GLU A 1 122 ? 24.12700  4.36000   19.77300 1.000 26.86673 ? 122 GLU A C   1 
ATOM   876  O O   . GLU A 1 122 ? 23.32200  5.24900   20.06900 1.000 25.32398 ? 122 GLU A O   1 
ATOM   877  C CB  . GLU A 1 122 ? 26.41800  4.42200   20.79100 1.000 28.90227 ? 122 GLU A CB  1 
ATOM   878  C CG  . GLU A 1 122 ? 26.37000  5.93800   20.83300 1.000 37.69960 ? 122 GLU A CG  1 
ATOM   879  C CD  . GLU A 1 122 ? 25.71600  6.46300   22.09700 1.000 41.02132 ? 122 GLU A CD  1 
ATOM   880  O OE1 . GLU A 1 122 ? 26.21500  6.15000   23.19900 1.000 41.53755 ? 122 GLU A OE1 1 
ATOM   881  O OE2 . GLU A 1 122 ? 24.69500  7.17600   21.98900 1.000 40.74841 ? 122 GLU A OE2 1 
ATOM   882  N N   . GLU A 1 123 ? 24.23800  3.88600   18.53000 1.000 27.03660 ? 123 GLU A N   1 
ATOM   883  C CA  . GLU A 1 123 ? 23.37100  4.38900   17.47100 1.000 27.31094 ? 123 GLU A CA  1 
ATOM   884  C C   . GLU A 1 123 ? 21.93100  3.93100   17.65700 1.000 25.57211 ? 123 GLU A C   1 
ATOM   885  O O   . GLU A 1 123 ? 21.00100  4.63700   17.24900 1.000 26.11159 ? 123 GLU A O   1 
ATOM   886  C CB  . GLU A 1 123 ? 23.90700  3.95300   16.10900 1.000 30.49775 ? 123 GLU A CB  1 
ATOM   887  C CG  . GLU A 1 123 ? 25.16700  4.69800   15.69100 1.000 33.82876 ? 123 GLU A CG  1 
ATOM   888  C CD  . GLU A 1 123 ? 25.92500  3.98800   14.59100 1.000 38.05644 ? 123 GLU A CD  1 
ATOM   889  O OE1 . GLU A 1 123 ? 26.34800  2.83500   14.81400 1.000 35.31392 ? 123 GLU A OE1 1 
ATOM   890  O OE2 . GLU A 1 123 ? 26.09300  4.57800   13.50400 1.000 38.17029 ? 123 GLU A OE2 1 
ATOM   891  N N   . VAL A 1 124 ? 21.72400  2.76200   18.26700 1.000 23.19208 ? 124 VAL A N   1 
ATOM   892  C CA  . VAL A 1 124 ? 20.36900  2.33400   18.59700 1.000 21.97935 ? 124 VAL A CA  1 
ATOM   893  C C   . VAL A 1 124 ? 19.77200  3.24100   19.66500 1.000 21.65502 ? 124 VAL A C   1 
ATOM   894  O O   . VAL A 1 124 ? 18.58000  3.56900   19.62400 1.000 18.89114 ? 124 VAL A O   1 
ATOM   895  C CB  . VAL A 1 124 ? 20.36700  0.85700   19.03200 1.000 24.84851 ? 124 VAL A CB  1 
ATOM   896  C CG1 . VAL A 1 124 ? 19.01000  0.46300   19.58600 1.000 19.12971 ? 124 VAL A CG1 1 
ATOM   897  C CG2 . VAL A 1 124 ? 20.73700  -0.02900  17.85800 1.000 25.41110 ? 124 VAL A CG2 1 
ATOM   898  N N   . GLN A 1 125 ? 20.58500  3.66500   20.63500 1.000 17.88374 ? 125 GLN A N   1 
ATOM   899  C CA  . GLN A 1 125 ? 20.10400  4.62700   21.62200 1.000 24.05216 ? 125 GLN A CA  1 
ATOM   900  C C   . GLN A 1 125 ? 19.75300  5.96100   20.97900 1.000 22.93248 ? 125 GLN A C   1 
ATOM   901  O O   . GLN A 1 125 ? 18.85200  6.65700   21.45800 1.000 21.83589 ? 125 GLN A O   1 
ATOM   902  C CB  . GLN A 1 125 ? 21.14600  4.82500   22.72100 1.000 25.64247 ? 125 GLN A CB  1 
ATOM   903  C CG  . GLN A 1 125 ? 21.25000  3.65400   23.67200 1.000 24.81992 ? 125 GLN A CG  1 
ATOM   904  C CD  . GLN A 1 125 ? 20.01200  3.49300   24.52900 1.000 26.84828 ? 125 GLN A CD  1 
ATOM   905  O OE1 . GLN A 1 125 ? 19.35100  4.47200   24.87500 1.000 29.68216 ? 125 GLN A OE1 1 
ATOM   906  N NE2 . GLN A 1 125 ? 19.68700  2.25300   24.87200 1.000 30.07421 ? 125 GLN A NE2 1 
ATOM   907  N N   . GLU A 1 126 ? 20.45100  6.33700   19.90500 1.000 19.46442 ? 126 GLU A N   1 
ATOM   908  C CA  . GLU A 1 126 ? 20.07100  7.53800   19.17100 1.000 26.14148 ? 126 GLU A CA  1 
ATOM   909  C C   . GLU A 1 126 ? 18.70000  7.37100   18.52800 1.000 20.71614 ? 126 GLU A C   1 
ATOM   910  O O   . GLU A 1 126 ? 17.90500  8.31600   18.48800 1.000 19.53498 ? 126 GLU A O   1 
ATOM   911  C CB  . GLU A 1 126 ? 21.12700  7.87000   18.11600 1.000 29.02897 ? 126 GLU A CB  1 
ATOM   912  C CG  . GLU A 1 126 ? 22.38300  8.52700   18.66900 1.000 32.75312 ? 126 GLU A CG  1 
ATOM   913  C CD  . GLU A 1 126 ? 23.32200  8.99900   17.57400 1.000 40.60026 ? 126 GLU A CD  1 
ATOM   914  O OE1 . GLU A 1 126 ? 22.90700  9.85500   16.76500 1.000 46.96433 ? 126 GLU A OE1 1 
ATOM   915  O OE2 . GLU A 1 126 ? 24.47000  8.51000   17.51600 1.000 45.41866 ? 126 GLU A OE2 1 
ATOM   916  N N   . ILE A 1 127 ? 18.40100  6.17100   18.03000 1.000 20.81817 ? 127 ILE A N   1 
ATOM   917  C CA  . ILE A 1 127 ? 17.07800  5.91000   17.46700 1.000 21.05823 ? 127 ILE A CA  1 
ATOM   918  C C   . ILE A 1 127 ? 16.02000  5.92100   18.56400 1.000 21.35083 ? 127 ILE A C   1 
ATOM   919  O O   . ILE A 1 127 ? 14.91500  6.44100   18.37500 1.000 19.49324 ? 127 ILE A O   1 
ATOM   920  C CB  . ILE A 1 127 ? 17.08300  4.57700   16.69700 1.000 22.96786 ? 127 ILE A CB  1 
ATOM   921  C CG1 . ILE A 1 127 ? 18.08100  4.63500   15.53700 1.000 23.65343 ? 127 ILE A CG1 1 
ATOM   922  C CG2 . ILE A 1 127 ? 15.67900  4.23800   16.20400 1.000 21.29587 ? 127 ILE A CG2 1 
ATOM   923  C CD1 . ILE A 1 127 ? 18.25900  3.32000   14.81100 1.000 22.18879 ? 127 ILE A CD1 1 
ATOM   924  N N   . ILE A 1 128 ? 16.34400  5.34900   19.72700 1.000 21.98061 ? 128 ILE A N   1 
ATOM   925  C CA  . ILE A 1 128 ? 15.41400  5.34400   20.85400 1.000 17.02521 ? 128 ILE A CA  1 
ATOM   926  C C   . ILE A 1 128 ? 15.10100  6.76900   21.29500 1.000 22.56714 ? 128 ILE A C   1 
ATOM   927  O O   . ILE A 1 128 ? 13.95000  7.09900   21.60500 1.000 22.64248 ? 128 ILE A O   1 
ATOM   928  C CB  . ILE A 1 128 ? 15.98900  4.50300   22.00900 1.000 23.11890 ? 128 ILE A CB  1 
ATOM   929  C CG1 . ILE A 1 128 ? 16.05100  3.02500   21.61900 1.000 24.51783 ? 128 ILE A CG1 1 
ATOM   930  C CG2 . ILE A 1 128 ? 15.17100  4.68400   23.27700 1.000 23.67845 ? 128 ILE A CG2 1 
ATOM   931  C CD1 . ILE A 1 128 ? 16.67700  2.14600   22.68300 1.000 24.84948 ? 128 ILE A CD1 1 
ATOM   932  N N   . ASP A 1 129 ? 16.11800  7.63600   21.32700 1.000 24.24278 ? 129 ASP A N   1 
ATOM   933  C CA  . ASP A 1 129 ? 15.89600  9.01900   21.74000 1.000 27.76717 ? 129 ASP A CA  1 
ATOM   934  C C   . ASP A 1 129 ? 15.01800  9.76300   20.74200 1.000 23.89619 ? 129 ASP A C   1 
ATOM   935  O O   . ASP A 1 129 ? 14.11900  10.51200  21.14000 1.000 22.49888 ? 129 ASP A O   1 
ATOM   936  C CB  . ASP A 1 129 ? 17.23000  9.74300   21.91400 1.000 24.98725 ? 129 ASP A CB  1 
ATOM   937  C CG  . ASP A 1 129 ? 17.97400  9.30800   23.16200 1.000 29.92894 ? 129 ASP A CG  1 
ATOM   938  O OD1 . ASP A 1 129 ? 17.33400  8.75800   24.08500 1.000 31.33691 ? 129 ASP A OD1 1 
ATOM   939  O OD2 . ASP A 1 129 ? 19.20100  9.52700   23.22600 1.000 30.28298 ? 129 ASP A OD2 1 
ATOM   940  N N   . ALA A 1 130 ? 15.26800  9.57700   19.44400 1.000 20.00346 ? 130 ALA A N   1 
ATOM   941  C CA  . ALA A 1 130 ? 14.45000  10.24000  18.43500 1.000 27.51588 ? 130 ALA A CA  1 
ATOM   942  C C   . ALA A 1 130 ? 13.01200  9.73700   18.47200 1.000 23.20285 ? 130 ALA A C   1 
ATOM   943  O O   . ALA A 1 130 ? 12.06900  10.52400  18.32400 1.000 20.63090 ? 130 ALA A O   1 
ATOM   944  C CB  . ALA A 1 130 ? 15.05700  10.03600  17.04700 1.000 26.80290 ? 130 ALA A CB  1 
ATOM   945  N N   . ALA A 1 131 ? 12.82300  8.43100   18.67300 1.000 21.31624 ? 131 ALA A N   1 
ATOM   946  C CA  . ALA A 1 131 ? 11.47400  7.87700   18.72500 1.000 22.03035 ? 131 ALA A CA  1 
ATOM   947  C C   . ALA A 1 131 ? 10.70400  8.42100   19.92100 1.000 22.23714 ? 131 ALA A C   1 
ATOM   948  O O   . ALA A 1 131 ? 9.56000   8.87000   19.78600 1.000 19.13952 ? 131 ALA A O   1 
ATOM   949  C CB  . ALA A 1 131 ? 11.53500  6.34900   18.77000 1.000 19.46206 ? 131 ALA A CB  1 
ATOM   950  N N   . ARG A 1 132 ? 11.32200  8.39400   21.10600 1.000 19.28837 ? 132 ARG A N   1 
ATOM   951  C CA  . ARG A 1 132 ? 10.64700  8.88400   22.30500 1.000 22.96238 ? 132 ARG A CA  1 
ATOM   952  C C   . ARG A 1 132 ? 10.33600  10.37000  22.19200 1.000 22.97274 ? 132 ARG A C   1 
ATOM   953  O O   . ARG A 1 132 ? 9.27800   10.82500  22.64300 1.000 22.79826 ? 132 ARG A O   1 
ATOM   954  C CB  . ARG A 1 132 ? 11.50600  8.61500   23.54100 1.000 17.79435 ? 132 ARG A CB  1 
ATOM   955  C CG  . ARG A 1 132 ? 11.66000  7.14900   23.89300 1.000 20.44491 ? 132 ARG A CG  1 
ATOM   956  C CD  . ARG A 1 132 ? 12.85200  6.95100   24.81400 1.000 29.58725 ? 132 ARG A CD  1 
ATOM   957  N NE  . ARG A 1 132 ? 12.70500  7.67500   26.07100 1.000 31.55117 ? 132 ARG A NE  1 
ATOM   958  C CZ  . ARG A 1 132 ? 13.72100  8.11700   26.79900 1.000 35.84970 ? 132 ARG A CZ  1 
ATOM   959  N NH1 . ARG A 1 132 ? 14.97400  7.96400   26.40000 1.000 34.37495 ? 132 ARG A NH1 1 
ATOM   960  N NH2 . ARG A 1 132 ? 13.47500  8.73200   27.95200 1.000 38.43097 ? 132 ARG A NH2 1 
ATOM   961  N N   . LYS A 1 133 ? 11.25400  11.14100  21.60400 1.000 21.79666 ? 133 LYS A N   1 
ATOM   962  C CA  . LYS A 1 133 ? 11.00500  12.56300  21.39100 1.000 23.21404 ? 133 LYS A CA  1 
ATOM   963  C C   . LYS A 1 133 ? 9.84600   12.78000  20.42600 1.000 31.42753 ? 133 LYS A C   1 
ATOM   964  O O   . LYS A 1 133 ? 9.00400   13.66200  20.64000 1.000 26.65086 ? 133 LYS A O   1 
ATOM   965  C CB  . LYS A 1 133 ? 12.27300  13.24200  20.87100 1.000 25.00951 ? 133 LYS A CB  1 
ATOM   966  C CG  . LYS A 1 133 ? 12.05400  14.64200  20.32500 1.000 35.89138 ? 133 LYS A CG  1 
ATOM   967  C CD  . LYS A 1 133 ? 13.36300  15.26900  19.88000 1.000 38.29404 ? 133 LYS A CD  1 
ATOM   968  C CE  . LYS A 1 133 ? 13.13500  16.63500  19.25700 1.000 46.46337 ? 133 LYS A CE  1 
ATOM   969  N NZ  . LYS A 1 133 ? 12.28500  16.54800  18.03700 1.000 45.97253 ? 133 LYS A NZ  1 
ATOM   970  N N   . ALA A 1 134 ? 9.78400   11.98300  19.35800 1.000 27.54860 ? 134 ALA A N   1 
ATOM   971  C CA  . ALA A 1 134 ? 8.69700   12.12400  18.39800 1.000 29.42397 ? 134 ALA A CA  1 
ATOM   972  C C   . ALA A 1 134 ? 7.35200   11.76600  19.01700 1.000 27.55700 ? 134 ALA A C   1 
ATOM   973  O O   . ALA A 1 134 ? 6.32800   12.35600  18.65500 1.000 30.81354 ? 134 ALA A O   1 
ATOM   974  C CB  . ALA A 1 134 ? 8.96900   11.25700  17.17000 1.000 22.39637 ? 134 ALA A CB  1 
ATOM   975  N N   . VAL A 1 135 ? 7.33400   10.80900  19.94700 1.000 26.75376 ? 135 VAL A N   1 
ATOM   976  C CA  . VAL A 1 135 ? 6.08700   10.42600  20.60500 1.000 26.45453 ? 135 VAL A CA  1 
ATOM   977  C C   . VAL A 1 135 ? 5.57100   11.56900  21.46900 1.000 30.52162 ? 135 VAL A C   1 
ATOM   978  O O   . VAL A 1 135 ? 4.38800   11.92900  21.41200 1.000 31.74347 ? 135 VAL A O   1 
ATOM   979  C CB  . VAL A 1 135 ? 6.28500   9.14000   21.43200 1.000 31.09925 ? 135 VAL A CB  1 
ATOM   980  C CG1 . VAL A 1 135 ? 5.03700   8.83500   22.25300 1.000 29.66346 ? 135 VAL A CG1 1 
ATOM   981  C CG2 . VAL A 1 135 ? 6.61900   7.96400   20.52800 1.000 22.35360 ? 135 VAL A CG2 1 
ATOM   982  N N   . LYS A 1 136 ? 6.45400   12.16500  22.27500 1.000 29.89277 ? 136 LYS A N   1 
ATOM   983  C CA  . LYS A 1 136 ? 6.03200   13.23400  23.17200 1.000 29.71913 ? 136 LYS A CA  1 
ATOM   984  C C   . LYS A 1 136 ? 5.57500   14.47900  22.42100 1.000 32.59493 ? 136 LYS A C   1 
ATOM   985  O O   . LYS A 1 136 ? 4.82300   15.28400  22.98100 1.000 31.63699 ? 136 LYS A O   1 
ATOM   986  C CB  . LYS A 1 136 ? 7.16200   13.57800  24.14200 1.000 35.88820 ? 136 LYS A CB  1 
ATOM   987  C CG  . LYS A 1 136 ? 7.41800   12.49300  25.17700 1.000 35.02094 ? 136 LYS A CG  1 
ATOM   988  C CD  . LYS A 1 136 ? 8.36200   12.95800  26.27300 1.000 45.26953 ? 136 LYS A CD  1 
ATOM   989  C CE  . LYS A 1 136 ? 9.81500   12.76200  25.88000 1.000 43.33256 ? 136 LYS A CE  1 
ATOM   990  N NZ  . LYS A 1 136 ? 10.70700  12.91500  27.06300 1.000 46.75633 ? 136 LYS A NZ  1 
ATOM   991  N N   . GLU A 1 137 ? 6.00000   14.65600  21.17100 1.000 32.09240 ? 137 GLU A N   1 
ATOM   992  C CA  . GLU A 1 137 ? 5.53100   15.75800  20.34300 1.000 35.21247 ? 137 GLU A CA  1 
ATOM   993  C C   . GLU A 1 137 ? 4.38500   15.35300  19.41700 1.000 33.87988 ? 137 GLU A C   1 
ATOM   994  O O   . GLU A 1 137 ? 4.07100   16.09000  18.47600 1.000 35.32394 ? 137 GLU A O   1 
ATOM   995  C CB  . GLU A 1 137 ? 6.69100   16.33700  19.52900 1.000 33.94837 ? 137 GLU A CB  1 
ATOM   996  C CG  . GLU A 1 137 ? 7.88700   16.76700  20.37300 1.000 38.04109 ? 137 GLU A CG  1 
ATOM   997  C CD  . GLU A 1 137 ? 8.91800   17.54100  19.57100 1.000 43.41689 ? 137 GLU A CD  1 
ATOM   998  O OE1 . GLU A 1 137 ? 8.56500   18.03700  18.48100 1.000 46.54849 ? 137 GLU A OE1 1 
ATOM   999  O OE2 . GLU A 1 137 ? 10.07600  17.65300  20.02500 1.000 46.61224 ? 137 GLU A OE2 1 
ATOM   1000 N N   . GLY A 1 138 ? 3.76500   14.19900  19.65800 1.000 32.27770 ? 138 GLY A N   1 
ATOM   1001 C CA  . GLY A 1 138 ? 2.56300   13.80200  18.94800 1.000 30.06694 ? 138 GLY A CA  1 
ATOM   1002 C C   . GLY A 1 138 ? 2.75800   13.29800  17.53600 1.000 28.92258 ? 138 GLY A C   1 
ATOM   1003 O O   . GLY A 1 138 ? 1.77200   13.18300  16.79900 1.000 30.86547 ? 138 GLY A O   1 
ATOM   1004 N N   . ARG A 1 139 ? 3.98600   12.98000  17.13500 1.000 25.48216 ? 139 ARG A N   1 
ATOM   1005 C CA  . ARG A 1 139 ? 4.27400   12.55500  15.77200 1.000 22.42835 ? 139 ARG A CA  1 
ATOM   1006 C C   . ARG A 1 139 ? 4.37300   11.04200  15.62300 1.000 24.32023 ? 139 ARG A C   1 
ATOM   1007 O O   . ARG A 1 139 ? 4.62400   10.55700  14.51400 1.000 24.86128 ? 139 ARG A O   1 
ATOM   1008 C CB  . ARG A 1 139 ? 5.57400   13.20500  15.28800 1.000 25.90255 ? 139 ARG A CB  1 
ATOM   1009 C CG  . ARG A 1 139 ? 5.75700   14.63200  15.78400 1.000 29.33484 ? 139 ARG A CG  1 
ATOM   1010 C CD  . ARG A 1 139 ? 6.84800   15.36500  15.02100 1.000 26.16257 ? 139 ARG A CD  1 
ATOM   1011 N NE  . ARG A 1 139 ? 8.13600   14.68200  15.07100 1.000 38.22487 ? 139 ARG A NE  1 
ATOM   1012 C CZ  . ARG A 1 139 ? 8.99500   14.77500  16.07800 1.000 42.45582 ? 139 ARG A CZ  1 
ATOM   1013 N NH1 . ARG A 1 139 ? 8.71100   15.47100  17.16700 1.000 45.08365 ? 139 ARG A NH1 1 
ATOM   1014 N NH2 . ARG A 1 139 ? 10.17000  14.15700  15.99000 1.000 41.65536 ? 139 ARG A NH2 1 
ATOM   1015 N N   . GLY A 1 140 ? 4.18000   10.28800  16.70000 1.000 23.71664 ? 140 GLY A N   1 
ATOM   1016 C CA  . GLY A 1 140 ? 4.35100   8.85300   16.66700 1.000 25.82693 ? 140 GLY A CA  1 
ATOM   1017 C C   . GLY A 1 140 ? 5.81300   8.44600   16.70100 1.000 24.89297 ? 140 GLY A C   1 
ATOM   1018 O O   . GLY A 1 140 ? 6.72700   9.24300   16.48900 1.000 26.15343 ? 140 GLY A O   1 
ATOM   1019 N N   . ALA A 1 141 ? 6.03200   7.15700   16.96100 1.000 23.36614 ? 141 ALA A N   1 
ATOM   1020 C CA  . ALA A 1 141 ? 7.38900   6.65500   17.14400 1.000 23.16165 ? 141 ALA A CA  1 
ATOM   1021 C C   . ALA A 1 141 ? 8.13400   6.51000   15.82100 1.000 23.12852 ? 141 ALA A C   1 
ATOM   1022 O O   . ALA A 1 141 ? 9.32200   6.84200   15.73800 1.000 20.68861 ? 141 ALA A O   1 
ATOM   1023 C CB  . ALA A 1 141 ? 7.35700   5.31300   17.87800 1.000 22.54712 ? 141 ALA A CB  1 
ATOM   1024 N N   . SER A 1 142 ? 7.45600   6.03100   14.77500 1.000 18.35198 ? 142 SER A N   1 
ATOM   1025 C CA  . SER A 1 142 ? 8.16100   5.62300   13.56300 1.000 22.88747 ? 142 SER A CA  1 
ATOM   1026 C C   . SER A 1 142 ? 8.70200   6.81000   12.77300 1.000 20.30063 ? 142 SER A C   1 
ATOM   1027 O O   . SER A 1 142 ? 9.67900   6.65700   12.03000 1.000 18.58755 ? 142 SER A O   1 
ATOM   1028 C CB  . SER A 1 142 ? 7.24300   4.77300   12.68500 1.000 22.44521 ? 142 SER A CB  1 
ATOM   1029 O OG  . SER A 1 142 ? 6.91500   3.56400   13.34500 1.000 24.09263 ? 142 SER A OG  1 
ATOM   1030 N N   . ILE A 1 143 ? 8.08900   7.98900   12.90000 1.000 21.57214 ? 143 ILE A N   1 
ATOM   1031 C CA  . ILE A 1 143 ? 8.65500   9.17200   12.25600 1.000 22.76444 ? 143 ILE A CA  1 
ATOM   1032 C C   . ILE A 1 143 ? 10.04000  9.46600   12.81700 1.000 18.36888 ? 143 ILE A C   1 
ATOM   1033 O O   . ILE A 1 143 ? 10.98200  9.75200   12.06900 1.000 19.06409 ? 143 ILE A O   1 
ATOM   1034 C CB  . ILE A 1 143 ? 7.71000   10.37800  12.40700 1.000 17.11183 ? 143 ILE A CB  1 
ATOM   1035 C CG1 . ILE A 1 143 ? 6.46900   10.19100  11.53300 1.000 23.48100 ? 143 ILE A CG1 1 
ATOM   1036 C CG2 . ILE A 1 143 ? 8.43000   11.67800  12.06000 1.000 19.97594 ? 143 ILE A CG2 1 
ATOM   1037 C CD1 . ILE A 1 143 ? 5.56400   11.39800  11.49400 1.000 24.44773 ? 143 ILE A CD1 1 
ATOM   1038 N N   . GLY A 1 144 ? 10.19300  9.38100   14.14000 1.000 20.07117 ? 144 GLY A N   1 
ATOM   1039 C CA  . GLY A 1 144 ? 11.50600  9.57800   14.73400 1.000 23.67683 ? 144 GLY A CA  1 
ATOM   1040 C C   . GLY A 1 144 ? 12.48900  8.48900   14.34800 1.000 23.08722 ? 144 GLY A C   1 
ATOM   1041 O O   . GLY A 1 144 ? 13.66500  8.76400   14.09100 1.000 22.68423 ? 144 GLY A O   1 
ATOM   1042 N N   . ILE A 1 145 ? 12.01900  7.24000   14.29400 1.000 19.15249 ? 145 ILE A N   1 
ATOM   1043 C CA  . ILE A 1 145 ? 12.88500  6.12400   13.92000 1.000 17.72136 ? 145 ILE A CA  1 
ATOM   1044 C C   . ILE A 1 145 ? 13.43400  6.32200   12.51300 1.000 19.80685 ? 145 ILE A C   1 
ATOM   1045 O O   . ILE A 1 145 ? 14.64400  6.22700   12.28100 1.000 17.85124 ? 145 ILE A O   1 
ATOM   1046 C CB  . ILE A 1 145 ? 12.12800  4.78800   14.03300 1.000 18.08967 ? 145 ILE A CB  1 
ATOM   1047 C CG1 . ILE A 1 145 ? 11.64100  4.55300   15.46200 1.000 20.66381 ? 145 ILE A CG1 1 
ATOM   1048 C CG2 . ILE A 1 145 ? 13.01600  3.63300   13.57400 1.000 18.90717 ? 145 ILE A CG2 1 
ATOM   1049 C CD1 . ILE A 1 145 ? 10.72700  3.34900   15.59600 1.000 22.18985 ? 145 ILE A CD1 1 
ATOM   1050 N N   . TYR A 1 146 ? 12.54900  6.59900   11.55100 1.000 19.89432 ? 146 TYR A N   1 
ATOM   1051 C CA  . TYR A 1 146 ? 12.97100  6.63900   10.15500 1.000 21.03560 ? 146 TYR A CA  1 
ATOM   1052 C C   . TYR A 1 146 ? 13.85600  7.84600   9.87300  1.000 21.26445 ? 146 TYR A C   1 
ATOM   1053 O O   . TYR A 1 146 ? 14.81400  7.74900   9.09800  1.000 23.26333 ? 146 TYR A O   1 
ATOM   1054 C CB  . TYR A 1 146 ? 11.75500  6.64500   9.22500  1.000 16.88291 ? 146 TYR A CB  1 
ATOM   1055 C CG  . TYR A 1 146 ? 10.94000  5.36600   9.21500  1.000 21.45039 ? 146 TYR A CG  1 
ATOM   1056 C CD1 . TYR A 1 146 ? 11.32900  4.25100   9.95300  1.000 23.69337 ? 146 TYR A CD1 1 
ATOM   1057 C CD2 . TYR A 1 146 ? 9.77800   5.27500   8.45900  1.000 23.52245 ? 146 TYR A CD2 1 
ATOM   1058 C CE1 . TYR A 1 146 ? 10.57800  3.08700   9.94100  1.000 24.93849 ? 146 TYR A CE1 1 
ATOM   1059 C CE2 . TYR A 1 146 ? 9.02000   4.11800   8.44100  1.000 26.87438 ? 146 TYR A CE2 1 
ATOM   1060 C CZ  . TYR A 1 146 ? 9.42400   3.02800   9.18200  1.000 30.12716 ? 146 TYR A CZ  1 
ATOM   1061 O OH  . TYR A 1 146 ? 8.67100   1.87800   9.16300  1.000 32.70573 ? 146 TYR A OH  1 
ATOM   1062 N N   . THR A 1 147 ? 13.54600  8.99400   10.47700 1.000 20.60186 ? 147 THR A N   1 
ATOM   1063 C CA  . THR A 1 147 ? 14.39100  10.17100  10.29100 1.000 24.27880 ? 147 THR A CA  1 
ATOM   1064 C C   . THR A 1 147 ? 15.78300  9.93400   10.86300 1.000 27.21286 ? 147 THR A C   1 
ATOM   1065 O O   . THR A 1 147 ? 16.79400  10.25700  10.22900 1.000 23.54274 ? 147 THR A O   1 
ATOM   1066 C CB  . THR A 1 147 ? 13.74500  11.39500  10.94100 1.000 26.82927 ? 147 THR A CB  1 
ATOM   1067 O OG1 . THR A 1 147 ? 13.40700  11.09300  12.30100 1.000 31.52898 ? 147 THR A OG1 1 
ATOM   1068 C CG2 . THR A 1 147 ? 12.48900  11.80000  10.18500 1.000 22.62157 ? 147 THR A CG2 1 
ATOM   1069 N N   . LYS A 1 148 ? 15.85400  9.36300   12.06600 1.000 25.61539 ? 148 LYS A N   1 
ATOM   1070 C CA  . LYS A 1 148 ? 17.15000  9.05300   12.66000 1.000 27.89812 ? 148 LYS A CA  1 
ATOM   1071 C C   . LYS A 1 148 ? 17.89300  8.00400   11.84400 1.000 28.27209 ? 148 LYS A C   1 
ATOM   1072 O O   . LYS A 1 148 ? 19.11200  8.10200   11.65400 1.000 30.88498 ? 148 LYS A O   1 
ATOM   1073 C CB  . LYS A 1 148 ? 16.96500  8.58200   14.10100 1.000 24.39527 ? 148 LYS A CB  1 
ATOM   1074 C CG  . LYS A 1 148 ? 18.24500  8.11300   14.77000 1.000 24.55040 ? 148 LYS A CG  1 
ATOM   1075 C CD  . LYS A 1 148 ? 19.29400  9.21000   14.78700 1.000 26.51387 ? 148 LYS A CD  1 
ATOM   1076 C CE  . LYS A 1 148 ? 18.84800  10.38700  15.63400 1.000 30.43272 ? 148 LYS A CE  1 
ATOM   1077 N NZ  . LYS A 1 148 ? 19.90700  11.42800  15.71800 1.000 42.29030 ? 148 LYS A NZ  1 
ATOM   1078 N N   . LEU A 1 149 ? 17.17600  6.99500   11.34700 1.000 25.21563 ? 149 LEU A N   1 
ATOM   1079 C CA  . LEU A 1 149 ? 17.81600  5.96300   10.53700 1.000 30.19634 ? 149 LEU A CA  1 
ATOM   1080 C C   . LEU A 1 149 ? 18.34900  6.54100   9.23300  1.000 33.48706 ? 149 LEU A C   1 
ATOM   1081 O O   . LEU A 1 149 ? 19.40400  6.11900   8.74500  1.000 35.63208 ? 149 LEU A O   1 
ATOM   1082 C CB  . LEU A 1 149 ? 16.83300  4.82600   10.25900 1.000 22.92486 ? 149 LEU A CB  1 
ATOM   1083 C CG  . LEU A 1 149 ? 17.41100  3.62400   9.51100  1.000 33.37931 ? 149 LEU A CG  1 
ATOM   1084 C CD1 . LEU A 1 149 ? 18.59600  3.05200   10.27700 1.000 38.44664 ? 149 LEU A CD1 1 
ATOM   1085 C CD2 . LEU A 1 149 ? 16.35100  2.56000   9.28900  1.000 36.21415 ? 149 LEU A CD2 1 
ATOM   1086 N N   . ARG A 1 150 ? 17.63100  7.50700   8.65400  1.000 30.80608 ? 150 ARG A N   1 
ATOM   1087 C CA  . ARG A 1 150 ? 18.12200  8.18300   7.45800  1.000 33.62185 ? 150 ARG A CA  1 
ATOM   1088 C C   . ARG A 1 150 ? 19.43600  8.89700   7.74300  1.000 38.23708 ? 150 ARG A C   1 
ATOM   1089 O O   . ARG A 1 150 ? 20.38100  8.81900   6.94900  1.000 38.78827 ? 150 ARG A O   1 
ATOM   1090 C CB  . ARG A 1 150 ? 17.06700  9.16800   6.95000  1.000 33.33904 ? 150 ARG A CB  1 
ATOM   1091 C CG  . ARG A 1 150 ? 17.30400  9.71800   5.54600  1.000 35.96018 ? 150 ARG A CG  1 
ATOM   1092 C CD  . ARG A 1 150 ? 18.04100  11.05000  5.57100  1.000 38.69988 ? 150 ARG A CD  1 
ATOM   1093 N NE  . ARG A 1 150 ? 17.70000  11.88300  4.42300  1.000 40.99848 ? 150 ARG A NE  1 
ATOM   1094 C CZ  . ARG A 1 150 ? 18.28100  11.79900  3.23400  1.000 44.45412 ? 150 ARG A CZ  1 
ATOM   1095 N NH1 . ARG A 1 150 ? 19.23900  10.92100  2.99200  1.000 49.95670 ? 150 ARG A NH1 1 
ATOM   1096 N NH2 . ARG A 1 150 ? 17.88900  12.61800  2.26200  1.000 41.59206 ? 150 ARG A NH2 1 
ATOM   1097 N N   . GLU A 1 151 ? 19.51600  9.58900   8.88100  1.000 38.80149 ? 151 GLU A N   1 
ATOM   1098 C CA  . GLU A 1 151 ? 20.73300  10.31700  9.22600  1.000 42.11534 ? 151 GLU A CA  1 
ATOM   1099 C C   . GLU A 1 151 ? 21.88700  9.36400   9.51500  1.000 40.98595 ? 151 GLU A C   1 
ATOM   1100 O O   . GLU A 1 151 ? 23.03300  9.64300   9.14700  1.000 40.56343 ? 151 GLU A O   1 
ATOM   1101 C CB  . GLU A 1 151 ? 20.47300  11.22400  10.42900 1.000 39.22633 ? 151 GLU A CB  1 
ATOM   1102 C CG  . GLU A 1 151 ? 19.31600  12.18900  10.23600 1.000 41.96519 ? 151 GLU A CG  1 
ATOM   1103 C CD  . GLU A 1 151 ? 18.80900  12.75600  11.54700 1.000 39.74471 ? 151 GLU A CD  1 
ATOM   1104 O OE1 . GLU A 1 151 ? 19.44600  12.50400  12.59200 1.000 46.92909 ? 151 GLU A OE1 1 
ATOM   1105 O OE2 . GLU A 1 151 ? 17.77000  13.44900  11.53200 1.000 46.11249 ? 151 GLU A OE2 1 
ATOM   1106 N N   . LEU A 1 152 ? 21.60200  8.23400   10.16600 1.000 38.02643 ? 152 LEU A N   1 
ATOM   1107 C CA  . LEU A 1 152 ? 22.66000  7.28800   10.51100 1.000 46.65502 ? 152 LEU A CA  1 
ATOM   1108 C C   . LEU A 1 152 ? 23.30900  6.70400   9.26100  1.000 50.42144 ? 152 LEU A C   1 
ATOM   1109 O O   . LEU A 1 152 ? 24.53800  6.62500   9.16400  1.000 52.98848 ? 152 LEU A O   1 
ATOM   1110 C CB  . LEU A 1 152 ? 22.10100  6.17200   11.39600 1.000 42.29598 ? 152 LEU A CB  1 
ATOM   1111 C CG  . LEU A 1 152 ? 21.81900  6.49800   12.86300 1.000 38.06590 ? 152 LEU A CG  1 
ATOM   1112 C CD1 . LEU A 1 152 ? 21.33700  5.25200   13.59200 1.000 32.89102 ? 152 LEU A CD1 1 
ATOM   1113 C CD2 . LEU A 1 152 ? 23.06100  7.06600   13.53300 1.000 37.87158 ? 152 LEU A CD2 1 
ATOM   1114 N N   . GLU A 1 153 ? 22.49300  6.28400   8.29300  1.000 49.80305 ? 153 GLU A N   1 
ATOM   1115 C CA  . GLU A 1 153 ? 23.01400  5.67500   7.07500  1.000 50.96678 ? 153 GLU A CA  1 
ATOM   1116 C C   . GLU A 1 153 ? 23.67000  6.68600   6.14400  1.000 52.58083 ? 153 GLU A C   1 
ATOM   1117 O O   . GLU A 1 153 ? 24.47600  6.29100   5.29500  1.000 52.39317 ? 153 GLU A O   1 
ATOM   1118 C CB  . GLU A 1 153 ? 21.89100  4.94200   6.33500  1.000 51.05306 ? 153 GLU A CB  1 
ATOM   1119 C CG  . GLU A 1 153 ? 21.14100  3.92200   7.18400  1.000 51.18498 ? 153 GLU A CG  1 
ATOM   1120 C CD  . GLU A 1 153 ? 21.71300  2.52000   7.07300  1.000 58.98396 ? 153 GLU A CD  1 
ATOM   1121 O OE1 . GLU A 1 153 ? 22.76500  2.35200   6.42100  1.000 58.64477 ? 153 GLU A OE1 1 
ATOM   1122 O OE2 . GLU A 1 153 ? 21.10200  1.58400   7.63400  1.000 60.75020 ? 153 GLU A OE2 1 
ATOM   1123 N N   . GLU A 1 154 ? 23.34500  7.96900   6.27900  1.000 47.31640 ? 154 GLU A N   1 
ATOM   1124 C CA  . GLU A 1 154 ? 23.97300  9.01600   5.48000  1.000 46.42493 ? 154 GLU A CA  1 
ATOM   1125 C C   . GLU A 1 154 ? 23.77800  10.38400  6.12700  1.000 49.32167 ? 154 GLU A C   1 
ATOM   1126 O O   . GLU A 1 154 ? 24.56300  11.30600  5.90400  1.000 56.56042 ? 154 GLU A O   1 
ATOM   1127 C CB  . GLU A 1 154 ? 23.41200  9.02700   4.05500  1.000 55.53929 ? 154 GLU A CB  1 
ATOM   1128 C CG  . GLU A 1 154 ? 21.91900  9.30100   3.97000  1.000 51.54291 ? 154 GLU A CG  1 
ATOM   1129 C CD  . GLU A 1 154 ? 21.10800  8.04600   3.71300  1.000 51.09699 ? 154 GLU A CD  1 
ATOM   1130 O OE1 . GLU A 1 154 ? 21.69700  6.94400   3.70500  1.000 55.40124 ? 154 GLU A OE1 1 
ATOM   1131 O OE2 . GLU A 1 154 ? 19.88100  8.16000   3.51300  1.000 49.81832 ? 154 GLU A OE2 1 
HETATM 1132 O O1  . PG4 B 2 .   ? -2.96300  -4.84400  23.78600 1.000 48.03187 ? 301 PG4 A O1  1 
HETATM 1133 C C1  . PG4 B 2 .   ? -3.34900  -4.55100  22.46400 1.000 47.90524 ? 301 PG4 A C1  1 
HETATM 1134 C C2  . PG4 B 2 .   ? -4.40700  -3.47800  22.47600 1.000 42.62424 ? 301 PG4 A C2  1 
HETATM 1135 O O2  . PG4 B 2 .   ? -4.98700  -3.36000  21.20300 1.000 46.86013 ? 301 PG4 A O2  1 
HETATM 1136 C C3  . PG4 B 2 .   ? -5.37100  -2.04300  20.90600 1.000 42.99107 ? 301 PG4 A C3  1 
HETATM 1137 C C4  . PG4 B 2 .   ? -6.53300  -1.64400  21.77600 1.000 45.69835 ? 301 PG4 A C4  1 
HETATM 1138 O O3  . PG4 B 2 .   ? -6.28300  -0.37800  22.32800 1.000 45.14494 ? 301 PG4 A O3  1 
HETATM 1139 C C5  . PG4 B 2 .   ? -7.40000  0.15200   22.99000 1.000 46.59797 ? 301 PG4 A C5  1 
HETATM 1140 C C6  . PG4 B 2 .   ? -6.98600  0.58700   24.37100 1.000 42.57156 ? 301 PG4 A C6  1 
HETATM 1141 O O4  . PG4 B 2 .   ? -6.13400  1.70100   24.29300 1.000 40.10026 ? 301 PG4 A O4  1 
HETATM 1142 C C7  . PG4 B 2 .   ? -5.84800  2.23300   25.56300 1.000 39.35397 ? 301 PG4 A C7  1 
HETATM 1143 C C8  . PG4 B 2 .   ? -5.02500  3.49200   25.45200 1.000 41.81208 ? 301 PG4 A C8  1 
HETATM 1144 O O5  . PG4 B 2 .   ? -4.76400  3.78600   24.09900 1.000 37.55728 ? 301 PG4 A O5  1 
HETATM 1145 O O   . HOH C 3 .   ? 5.25200   8.05800   13.61900 1.000 22.61473 ? 401 HOH A O   1 
HETATM 1146 O O   . HOH C 3 .   ? -9.65200  -0.31100  9.89600  1.000 29.83000 ? 402 HOH A O   1 
HETATM 1147 O O   . HOH C 3 .   ? 12.17900  -7.50400  7.58800  1.000 35.31944 ? 403 HOH A O   1 
HETATM 1148 O O   . HOH C 3 .   ? -10.40400 3.58100   -1.61400 1.000 31.23865 ? 404 HOH A O   1 
HETATM 1149 O O   . HOH C 3 .   ? -3.00000  8.47400   18.65400 1.000 21.63001 ? 405 HOH A O   1 
HETATM 1150 O O   . HOH C 3 .   ? -2.039    -17.584   18.995   1.000 36.68728 ? 406 HOH A O   1 
HETATM 1151 O O   . HOH C 3 .   ? 21.384    -7.681    9.417    1.000 32.64415 ? 407 HOH A O   1 
HETATM 1152 O O   . HOH C 3 .   ? 27.74800  1.78600   12.64600 1.000 43.58676 ? 408 HOH A O   1 
HETATM 1153 O O   . HOH C 3 .   ? 12.57700  12.78600  16.77900 1.000 35.62469 ? 409 HOH A O   1 
HETATM 1154 O O   . HOH C 3 .   ? 9.21200   11.34100  1.00100  1.000 27.93040 ? 410 HOH A O   1 
HETATM 1155 O O   . HOH C 3 .   ? 6.18900   2.07800   25.66000 1.000 26.70100 ? 411 HOH A O   1 
HETATM 1156 O O   . HOH C 3 .   ? -1.375    14.206    -0.584   1.000 41.73272 ? 412 HOH A O   1 
HETATM 1157 O O   . HOH C 3 .   ? 3.26200   -6.18400  8.56900  1.000 35.89104 ? 413 HOH A O   1 
HETATM 1158 O O   . HOH C 3 .   ? 0.25100   7.75800   17.97900 1.000 27.65821 ? 414 HOH A O   1 
HETATM 1159 O O   . HOH C 3 .   ? -3.40500  10.93800  17.37000 1.000 34.83496 ? 415 HOH A O   1 
HETATM 1160 O O   . HOH C 3 .   ? 1.39900   6.80400   22.61800 1.000 34.67873 ? 416 HOH A O   1 
HETATM 1161 O O   . HOH C 3 .   ? 4.67600   -8.43900  9.68000  1.000 40.64433 ? 417 HOH A O   1 
HETATM 1162 O O   . HOH C 3 .   ? -3.36600  18.75000  3.22500  1.000 38.86454 ? 418 HOH A O   1 
HETATM 1163 O O   . HOH C 3 .   ? 1.01100   11.27000  14.74000 1.000 25.79156 ? 419 HOH A O   1 
HETATM 1164 O O   . HOH C 3 .   ? 2.90500   10.49000  19.35900 1.000 29.86025 ? 420 HOH A O   1 
HETATM 1165 O O   . HOH C 3 .   ? 27.93000  -1.50800  20.03500 1.000 29.28966 ? 421 HOH A O   1 
HETATM 1166 O O   . HOH C 3 .   ? 2.41200   18.15000  12.28400 1.000 31.60279 ? 422 HOH A O   1 
HETATM 1167 O O   . HOH C 3 .   ? 0.00000   9.17400   0.00000  0.50  35.25602 ? 423 HOH A O   1 
HETATM 1168 O O   . HOH C 3 .   ? -14.33800 5.28900   17.74500 1.000 30.45368 ? 424 HOH A O   1 
HETATM 1169 O O   . HOH C 3 .   ? 12.08700  -6.25800  21.74600 1.000 32.21153 ? 425 HOH A O   1 
HETATM 1170 O O   . HOH C 3 .   ? 8.32500   0.89400   27.23100 1.000 28.95241 ? 426 HOH A O   1 
HETATM 1171 O O   . HOH C 3 .   ? 19.85100  -9.84400  22.46400 1.000 39.25651 ? 427 HOH A O   1 
HETATM 1172 O O   . HOH C 3 .   ? 10.27900  -6.64400  4.19800  1.000 38.81976 ? 428 HOH A O   1 
HETATM 1173 O O   . HOH C 3 .   ? 28.09300  1.40100   21.08500 1.000 31.21110 ? 429 HOH A O   1 
HETATM 1174 O O   . HOH C 3 .   ? 7.91500   9.27200   25.08600 1.000 37.53078 ? 430 HOH A O   1 
HETATM 1175 O O   . HOH C 3 .   ? 10.91800  14.65100  9.92300  1.000 35.06576 ? 431 HOH A O   1 
HETATM 1176 O O   . HOH C 3 .   ? -14.38000 4.29800   6.60700  1.000 60.65497 ? 432 HOH A O   1 
HETATM 1177 O O   . HOH C 3 .   ? -10.93400 2.19500   9.84800  1.000 42.20627 ? 433 HOH A O   1 
HETATM 1178 O O   . HOH C 3 .   ? 1.34300   8.33700   15.49800 1.000 32.07316 ? 434 HOH A O   1 
HETATM 1179 O O   . HOH C 3 .   ? 6.53400   -7.71600  22.89500 1.000 43.03902 ? 435 HOH A O   1 
HETATM 1180 O O   . HOH C 3 .   ? 2.58800   8.36600   11.63200 1.000 34.46588 ? 436 HOH A O   1 
HETATM 1181 O O   . HOH C 3 .   ? 0.71900   8.87600   20.50600 1.000 30.72493 ? 437 HOH A O   1 
# 
