data_9C17
# 
_entry.id   9C17 
# 
_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   9C17         pdb_00009c17 10.2210/pdb9c17/pdb 
WWPDB D_1000284502 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-23 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9C17 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9C16 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              wadie.bahou@stonybrookmedicine.edu 
_pdbx_contact_author.name_first         Wadie 
_pdbx_contact_author.name_last          Bahou 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6527-8503 
# 
_audit_author.name               'Kreitler, D.F.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0003-4758-7913 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                3480 
_citation.page_last                 3480 
_citation.title                     
'Small molecule BLVRB redox inhibitor promotes megakaryocytopoiesis and stress thrombopoiesis in vivo.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-58497-9 
_citation.pdbx_database_id_PubMed   40216753 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Nesbitt, N.M.'      1  0000-0001-5549-0383 
primary 'Araldi, G.L.'       2  ?                   
primary 'Pennacchia, L.'     3  0000-0002-4248-0482 
primary 'Marchenko, N.'      4  ?                   
primary 'Assar, Z.'          5  0000-0001-6008-6203 
primary 'Muzzarelli, K.M.'   6  0000-0003-1488-0750 
primary 'Thekke Veedu, R.R.' 7  0000-0003-3553-980X 
primary 'Medel-Lacruz, B.'   8  0000-0003-2831-7731 
primary 'Lee, E.'            9  ?                   
primary 'Eisenmesser, E.Z.'  10 ?                   
primary 'Kreitler, D.F.'     11 0000-0003-4758-7913 
primary 'Bahou, W.F.'        12 0000-0001-6527-8503 
# 
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 'Flavin reductase (NADPH)'                                                  22550.777 1   
1.5.1.30,1.3.1.-,2.6.99.- ? ? ? 
2 non-polymer syn 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'                          743.405   1   ? ? ? ? 
3 non-polymer syn '4-[(4R,7P)-7-(2-chlorophenyl)imidazo[5,1-b][1,3]thiazol-5-yl]benzoic acid' 354.810   1   ? ? ? ? 
4 water       nat water                                                                       18.015    210 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;FR,Biliverdin reductase B,BVR-B,Biliverdin-IX beta-reductase,Green heme-binding protein,GHBP,NADPH-dependent diaphorase,NADPH-flavin reductase,FLR,S-nitroso-CoA-assisted nitrosyltransferase,SNO-CoA-assisted nitrosyltransferase
;
# 
_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       
;GSRTMAVKKIAIFGATGQTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPRPAHVVVGDVLQAADVDKTVAGQDAVIVLLG
TRNDLSPTTVMSEGARNIVAAMKAHGVDKVVACTSAFLLWDPTKVPPRLQAVTDDHIRMHKVLRESGLKYVAVMPPHIGD
QPLTGAYTVTLDGRGPSRVISKHDLGHFMLRCLTTDEYDGHSTYPSHQYQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSRTMAVKKIAIFGATGQTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPRPAHVVVGDVLQAADVDKTVAGQDAVIVLLG
TRNDLSPTTVMSEGARNIVAAMKAHGVDKVVACTSAFLLWDPTKVPPRLQAVTDDHIRMHKVLRESGLKYVAVMPPHIGD
QPLTGAYTVTLDGRGPSRVISKHDLGHFMLRCLTTDEYDGHSTYPSHQYQ
;
_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 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'                          NAP   
3 '4-[(4R,7P)-7-(2-chlorophenyl)imidazo[5,1-b][1,3]thiazol-5-yl]benzoic acid' A1ATJ 
4 water                                                                       HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   ARG n 
1 4   THR n 
1 5   MET n 
1 6   ALA n 
1 7   VAL n 
1 8   LYS n 
1 9   LYS n 
1 10  ILE n 
1 11  ALA n 
1 12  ILE n 
1 13  PHE n 
1 14  GLY n 
1 15  ALA n 
1 16  THR n 
1 17  GLY n 
1 18  GLN n 
1 19  THR n 
1 20  GLY n 
1 21  LEU n 
1 22  THR n 
1 23  THR n 
1 24  LEU n 
1 25  ALA n 
1 26  GLN n 
1 27  ALA n 
1 28  VAL n 
1 29  GLN n 
1 30  ALA n 
1 31  GLY n 
1 32  TYR n 
1 33  GLU n 
1 34  VAL n 
1 35  THR n 
1 36  VAL n 
1 37  LEU n 
1 38  VAL n 
1 39  ARG n 
1 40  ASP n 
1 41  SER n 
1 42  SER n 
1 43  ARG n 
1 44  LEU n 
1 45  PRO n 
1 46  SER n 
1 47  GLU n 
1 48  GLY n 
1 49  PRO n 
1 50  ARG n 
1 51  PRO n 
1 52  ALA n 
1 53  HIS n 
1 54  VAL n 
1 55  VAL n 
1 56  VAL n 
1 57  GLY n 
1 58  ASP n 
1 59  VAL n 
1 60  LEU n 
1 61  GLN n 
1 62  ALA n 
1 63  ALA n 
1 64  ASP n 
1 65  VAL n 
1 66  ASP n 
1 67  LYS n 
1 68  THR n 
1 69  VAL n 
1 70  ALA n 
1 71  GLY n 
1 72  GLN n 
1 73  ASP n 
1 74  ALA n 
1 75  VAL n 
1 76  ILE n 
1 77  VAL n 
1 78  LEU n 
1 79  LEU n 
1 80  GLY n 
1 81  THR n 
1 82  ARG n 
1 83  ASN n 
1 84  ASP n 
1 85  LEU n 
1 86  SER n 
1 87  PRO n 
1 88  THR n 
1 89  THR n 
1 90  VAL n 
1 91  MET n 
1 92  SER n 
1 93  GLU n 
1 94  GLY n 
1 95  ALA n 
1 96  ARG n 
1 97  ASN n 
1 98  ILE n 
1 99  VAL n 
1 100 ALA n 
1 101 ALA n 
1 102 MET n 
1 103 LYS n 
1 104 ALA n 
1 105 HIS n 
1 106 GLY n 
1 107 VAL n 
1 108 ASP n 
1 109 LYS n 
1 110 VAL n 
1 111 VAL n 
1 112 ALA n 
1 113 CYS n 
1 114 THR n 
1 115 SER n 
1 116 ALA n 
1 117 PHE n 
1 118 LEU n 
1 119 LEU n 
1 120 TRP n 
1 121 ASP n 
1 122 PRO n 
1 123 THR n 
1 124 LYS n 
1 125 VAL n 
1 126 PRO n 
1 127 PRO n 
1 128 ARG n 
1 129 LEU n 
1 130 GLN n 
1 131 ALA n 
1 132 VAL n 
1 133 THR n 
1 134 ASP n 
1 135 ASP n 
1 136 HIS n 
1 137 ILE n 
1 138 ARG n 
1 139 MET n 
1 140 HIS n 
1 141 LYS n 
1 142 VAL n 
1 143 LEU n 
1 144 ARG n 
1 145 GLU n 
1 146 SER n 
1 147 GLY n 
1 148 LEU n 
1 149 LYS n 
1 150 TYR n 
1 151 VAL n 
1 152 ALA n 
1 153 VAL n 
1 154 MET n 
1 155 PRO n 
1 156 PRO n 
1 157 HIS n 
1 158 ILE n 
1 159 GLY n 
1 160 ASP n 
1 161 GLN n 
1 162 PRO n 
1 163 LEU n 
1 164 THR n 
1 165 GLY n 
1 166 ALA n 
1 167 TYR n 
1 168 THR n 
1 169 VAL n 
1 170 THR n 
1 171 LEU n 
1 172 ASP n 
1 173 GLY n 
1 174 ARG n 
1 175 GLY n 
1 176 PRO n 
1 177 SER n 
1 178 ARG n 
1 179 VAL n 
1 180 ILE n 
1 181 SER n 
1 182 LYS n 
1 183 HIS n 
1 184 ASP n 
1 185 LEU n 
1 186 GLY n 
1 187 HIS n 
1 188 PHE n 
1 189 MET n 
1 190 LEU n 
1 191 ARG n 
1 192 CYS n 
1 193 LEU n 
1 194 THR n 
1 195 THR n 
1 196 ASP n 
1 197 GLU n 
1 198 TYR n 
1 199 ASP n 
1 200 GLY n 
1 201 HIS n 
1 202 SER n 
1 203 THR n 
1 204 TYR n 
1 205 PRO n 
1 206 SER n 
1 207 HIS n 
1 208 GLN n 
1 209 TYR n 
1 210 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   210 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'BLVRB, FLR, SCAN' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_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                   GST 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pGEX 
_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 
A1ATJ non-polymer         . '4-[(4R,7P)-7-(2-chlorophenyl)imidazo[5,1-b][1,3]thiazol-5-yl]benzoic acid' ? 'C18 H11 Cl N2 O2 S' 
354.810 
ALA   'L-peptide linking' y ALANINE                                                                     ? 'C3 H7 N O2'         
89.093  
ARG   'L-peptide linking' y ARGININE                                                                    ? 'C6 H15 N4 O2 1'     
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                  ? 'C4 H8 N2 O3'        
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                             ? 'C4 H7 N O4'         
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                    ? 'C3 H7 N O2 S'       
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                   ? 'C5 H10 N2 O3'       
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                             ? 'C5 H9 N O4'         
147.129 
GLY   'peptide linking'   y GLYCINE                                                                     ? 'C2 H5 N O2'         
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                   ? 'C6 H10 N3 O2 1'     
156.162 
HOH   non-polymer         . WATER                                                                       ? 'H2 O'               
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                  ? 'C6 H13 N O2'        
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                     ? 'C6 H13 N O2'        
131.173 
LYS   'L-peptide linking' y LYSINE                                                                      ? 'C6 H15 N2 O2 1'     
147.195 
MET   'L-peptide linking' y METHIONINE                                                                  ? 'C5 H11 N O2 S'      
149.211 
NAP   non-polymer         . 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'                          
;2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
;
'C21 H28 N7 O17 P3'  743.405 
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   GLY 1   -3  ?   ?   ?   A . n 
A 1 2   SER 2   -2  ?   ?   ?   A . n 
A 1 3   ARG 3   -1  ?   ?   ?   A . n 
A 1 4   THR 4   0   ?   ?   ?   A . n 
A 1 5   MET 5   1   ?   ?   ?   A . n 
A 1 6   ALA 6   2   2   ALA ALA A . n 
A 1 7   VAL 7   3   3   VAL VAL A . n 
A 1 8   LYS 8   4   4   LYS LYS A . n 
A 1 9   LYS 9   5   5   LYS LYS A . n 
A 1 10  ILE 10  6   6   ILE ILE A . n 
A 1 11  ALA 11  7   7   ALA ALA A . n 
A 1 12  ILE 12  8   8   ILE ILE A . n 
A 1 13  PHE 13  9   9   PHE PHE A . n 
A 1 14  GLY 14  10  10  GLY GLY A . n 
A 1 15  ALA 15  11  11  ALA ALA A . n 
A 1 16  THR 16  12  12  THR THR A . n 
A 1 17  GLY 17  13  13  GLY GLY A . n 
A 1 18  GLN 18  14  14  GLN GLN A . n 
A 1 19  THR 19  15  15  THR THR A . n 
A 1 20  GLY 20  16  16  GLY GLY A . n 
A 1 21  LEU 21  17  17  LEU LEU A . n 
A 1 22  THR 22  18  18  THR THR A . n 
A 1 23  THR 23  19  19  THR THR A . n 
A 1 24  LEU 24  20  20  LEU LEU A . n 
A 1 25  ALA 25  21  21  ALA ALA A . n 
A 1 26  GLN 26  22  22  GLN GLN A . n 
A 1 27  ALA 27  23  23  ALA ALA A . n 
A 1 28  VAL 28  24  24  VAL VAL A . n 
A 1 29  GLN 29  25  25  GLN GLN A . n 
A 1 30  ALA 30  26  26  ALA ALA A . n 
A 1 31  GLY 31  27  27  GLY GLY A . n 
A 1 32  TYR 32  28  28  TYR TYR A . n 
A 1 33  GLU 33  29  29  GLU GLU A . n 
A 1 34  VAL 34  30  30  VAL VAL A . n 
A 1 35  THR 35  31  31  THR THR A . n 
A 1 36  VAL 36  32  32  VAL VAL A . n 
A 1 37  LEU 37  33  33  LEU LEU A . n 
A 1 38  VAL 38  34  34  VAL VAL A . n 
A 1 39  ARG 39  35  35  ARG ARG A . n 
A 1 40  ASP 40  36  36  ASP ASP A . n 
A 1 41  SER 41  37  37  SER SER A . n 
A 1 42  SER 42  38  38  SER SER A . n 
A 1 43  ARG 43  39  39  ARG ARG A . n 
A 1 44  LEU 44  40  40  LEU LEU A . n 
A 1 45  PRO 45  41  41  PRO PRO A . n 
A 1 46  SER 46  42  42  SER SER A . n 
A 1 47  GLU 47  43  43  GLU GLU A . n 
A 1 48  GLY 48  44  44  GLY GLY A . n 
A 1 49  PRO 49  45  45  PRO PRO A . n 
A 1 50  ARG 50  46  46  ARG ARG A . n 
A 1 51  PRO 51  47  47  PRO PRO A . n 
A 1 52  ALA 52  48  48  ALA ALA A . n 
A 1 53  HIS 53  49  49  HIS HIS A . n 
A 1 54  VAL 54  50  50  VAL VAL A . n 
A 1 55  VAL 55  51  51  VAL VAL A . n 
A 1 56  VAL 56  52  52  VAL VAL A . n 
A 1 57  GLY 57  53  53  GLY GLY A . n 
A 1 58  ASP 58  54  54  ASP ASP A . n 
A 1 59  VAL 59  55  55  VAL VAL A . n 
A 1 60  LEU 60  56  56  LEU LEU A . n 
A 1 61  GLN 61  57  57  GLN GLN A . n 
A 1 62  ALA 62  58  58  ALA ALA A . n 
A 1 63  ALA 63  59  59  ALA ALA A . n 
A 1 64  ASP 64  60  60  ASP ASP A . n 
A 1 65  VAL 65  61  61  VAL VAL A . n 
A 1 66  ASP 66  62  62  ASP ASP A . n 
A 1 67  LYS 67  63  63  LYS LYS A . n 
A 1 68  THR 68  64  64  THR THR A . n 
A 1 69  VAL 69  65  65  VAL VAL A . n 
A 1 70  ALA 70  66  66  ALA ALA A . n 
A 1 71  GLY 71  67  67  GLY GLY A . n 
A 1 72  GLN 72  68  68  GLN GLN A . n 
A 1 73  ASP 73  69  69  ASP ASP A . n 
A 1 74  ALA 74  70  70  ALA ALA A . n 
A 1 75  VAL 75  71  71  VAL VAL A . n 
A 1 76  ILE 76  72  72  ILE ILE A . n 
A 1 77  VAL 77  73  73  VAL VAL A . n 
A 1 78  LEU 78  74  74  LEU LEU A . n 
A 1 79  LEU 79  75  75  LEU LEU A . n 
A 1 80  GLY 80  76  76  GLY GLY A . n 
A 1 81  THR 81  77  77  THR THR A . n 
A 1 82  ARG 82  78  78  ARG ARG A . n 
A 1 83  ASN 83  79  79  ASN ASN A . n 
A 1 84  ASP 84  80  80  ASP ASP A . n 
A 1 85  LEU 85  81  81  LEU LEU A . n 
A 1 86  SER 86  82  82  SER SER A . n 
A 1 87  PRO 87  83  83  PRO PRO A . n 
A 1 88  THR 88  84  84  THR THR A . n 
A 1 89  THR 89  85  85  THR THR A . n 
A 1 90  VAL 90  86  86  VAL VAL A . n 
A 1 91  MET 91  87  87  MET MET A . n 
A 1 92  SER 92  88  88  SER SER A . n 
A 1 93  GLU 93  89  89  GLU GLU A . n 
A 1 94  GLY 94  90  90  GLY GLY A . n 
A 1 95  ALA 95  91  91  ALA ALA A . n 
A 1 96  ARG 96  92  92  ARG ARG A . n 
A 1 97  ASN 97  93  93  ASN ASN A . n 
A 1 98  ILE 98  94  94  ILE ILE A . n 
A 1 99  VAL 99  95  95  VAL VAL A . n 
A 1 100 ALA 100 96  96  ALA ALA A . n 
A 1 101 ALA 101 97  97  ALA ALA A . n 
A 1 102 MET 102 98  98  MET MET A . n 
A 1 103 LYS 103 99  99  LYS LYS A . n 
A 1 104 ALA 104 100 100 ALA ALA A . n 
A 1 105 HIS 105 101 101 HIS HIS A . n 
A 1 106 GLY 106 102 102 GLY GLY A . n 
A 1 107 VAL 107 103 103 VAL VAL A . n 
A 1 108 ASP 108 104 104 ASP ASP A . n 
A 1 109 LYS 109 105 105 LYS LYS A . n 
A 1 110 VAL 110 106 106 VAL VAL A . n 
A 1 111 VAL 111 107 107 VAL VAL A . n 
A 1 112 ALA 112 108 108 ALA ALA A . n 
A 1 113 CYS 113 109 109 CYS CYS A . n 
A 1 114 THR 114 110 110 THR THR A . n 
A 1 115 SER 115 111 111 SER SER A . n 
A 1 116 ALA 116 112 112 ALA ALA A . n 
A 1 117 PHE 117 113 113 PHE PHE A . n 
A 1 118 LEU 118 114 114 LEU LEU A . n 
A 1 119 LEU 119 115 115 LEU LEU A . n 
A 1 120 TRP 120 116 116 TRP TRP A . n 
A 1 121 ASP 121 117 117 ASP ASP A . n 
A 1 122 PRO 122 118 118 PRO PRO A . n 
A 1 123 THR 123 119 119 THR THR A . n 
A 1 124 LYS 124 120 120 LYS LYS A . n 
A 1 125 VAL 125 121 121 VAL VAL A . n 
A 1 126 PRO 126 122 122 PRO PRO A . n 
A 1 127 PRO 127 123 123 PRO PRO A . n 
A 1 128 ARG 128 124 124 ARG ARG A . n 
A 1 129 LEU 129 125 125 LEU LEU A . n 
A 1 130 GLN 130 126 126 GLN GLN A . n 
A 1 131 ALA 131 127 127 ALA ALA A . n 
A 1 132 VAL 132 128 128 VAL VAL A . n 
A 1 133 THR 133 129 129 THR THR A . n 
A 1 134 ASP 134 130 130 ASP ASP A . n 
A 1 135 ASP 135 131 131 ASP ASP A . n 
A 1 136 HIS 136 132 132 HIS HIS A . n 
A 1 137 ILE 137 133 133 ILE ILE A . n 
A 1 138 ARG 138 134 134 ARG ARG A . n 
A 1 139 MET 139 135 135 MET MET A . n 
A 1 140 HIS 140 136 136 HIS HIS A . n 
A 1 141 LYS 141 137 137 LYS LYS A . n 
A 1 142 VAL 142 138 138 VAL VAL A . n 
A 1 143 LEU 143 139 139 LEU LEU A . n 
A 1 144 ARG 144 140 140 ARG ARG A . n 
A 1 145 GLU 145 141 141 GLU GLU A . n 
A 1 146 SER 146 142 142 SER SER A . n 
A 1 147 GLY 147 143 143 GLY GLY A . n 
A 1 148 LEU 148 144 144 LEU LEU A . n 
A 1 149 LYS 149 145 145 LYS LYS A . n 
A 1 150 TYR 150 146 146 TYR TYR A . n 
A 1 151 VAL 151 147 147 VAL VAL A . n 
A 1 152 ALA 152 148 148 ALA ALA A . n 
A 1 153 VAL 153 149 149 VAL VAL A . n 
A 1 154 MET 154 150 150 MET MET A . n 
A 1 155 PRO 155 151 151 PRO PRO A . n 
A 1 156 PRO 156 152 152 PRO PRO A . n 
A 1 157 HIS 157 153 153 HIS HIS A . n 
A 1 158 ILE 158 154 154 ILE ILE A . n 
A 1 159 GLY 159 155 155 GLY GLY A . n 
A 1 160 ASP 160 156 156 ASP ASP A . n 
A 1 161 GLN 161 157 157 GLN GLN A . n 
A 1 162 PRO 162 158 158 PRO PRO A . n 
A 1 163 LEU 163 159 159 LEU LEU A . n 
A 1 164 THR 164 160 160 THR THR A . n 
A 1 165 GLY 165 161 161 GLY GLY A . n 
A 1 166 ALA 166 162 162 ALA ALA A . n 
A 1 167 TYR 167 163 163 TYR TYR A . n 
A 1 168 THR 168 164 164 THR THR A . n 
A 1 169 VAL 169 165 165 VAL VAL A . n 
A 1 170 THR 170 166 166 THR THR A . n 
A 1 171 LEU 171 167 167 LEU LEU A . n 
A 1 172 ASP 172 168 168 ASP ASP A . n 
A 1 173 GLY 173 169 169 GLY GLY A . n 
A 1 174 ARG 174 170 170 ARG ARG A . n 
A 1 175 GLY 175 171 171 GLY GLY A . n 
A 1 176 PRO 176 172 172 PRO PRO A . n 
A 1 177 SER 177 173 173 SER SER A . n 
A 1 178 ARG 178 174 174 ARG ARG A . n 
A 1 179 VAL 179 175 175 VAL VAL A . n 
A 1 180 ILE 180 176 176 ILE ILE A . n 
A 1 181 SER 181 177 177 SER SER A . n 
A 1 182 LYS 182 178 178 LYS LYS A . n 
A 1 183 HIS 183 179 179 HIS HIS A . n 
A 1 184 ASP 184 180 180 ASP ASP A . n 
A 1 185 LEU 185 181 181 LEU LEU A . n 
A 1 186 GLY 186 182 182 GLY GLY A . n 
A 1 187 HIS 187 183 183 HIS HIS A . n 
A 1 188 PHE 188 184 184 PHE PHE A . n 
A 1 189 MET 189 185 185 MET MET A . n 
A 1 190 LEU 190 186 186 LEU LEU A . n 
A 1 191 ARG 191 187 187 ARG ARG A . n 
A 1 192 CYS 192 188 188 CYS CYS A . n 
A 1 193 LEU 193 189 189 LEU LEU A . n 
A 1 194 THR 194 190 190 THR THR A . n 
A 1 195 THR 195 191 191 THR THR A . n 
A 1 196 ASP 196 192 192 ASP ASP A . n 
A 1 197 GLU 197 193 193 GLU GLU A . n 
A 1 198 TYR 198 194 194 TYR TYR A . n 
A 1 199 ASP 199 195 195 ASP ASP A . n 
A 1 200 GLY 200 196 196 GLY GLY A . n 
A 1 201 HIS 201 197 197 HIS HIS A . n 
A 1 202 SER 202 198 198 SER SER A . n 
A 1 203 THR 203 199 199 THR THR A . n 
A 1 204 TYR 204 200 200 TYR TYR A . n 
A 1 205 PRO 205 201 201 PRO PRO A . n 
A 1 206 SER 206 202 202 SER SER A . n 
A 1 207 HIS 207 203 203 HIS HIS A . n 
A 1 208 GLN 208 204 204 GLN GLN A . n 
A 1 209 TYR 209 205 205 TYR TYR A . n 
A 1 210 GLN 210 206 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1ATJ ? ? A1ATJ ? ? 'SUBJECT OF INVESTIGATION' ? 
2 NAP   ? ? NAP   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 NAP   1   301 303 NAP   NAP A . 
C 3 A1ATJ 1   302 304 A1ATJ LIG A . 
D 4 HOH   1   401 25  HOH   HOH A . 
D 4 HOH   2   402 158 HOH   HOH A . 
D 4 HOH   3   403 99  HOH   HOH A . 
D 4 HOH   4   404 26  HOH   HOH A . 
D 4 HOH   5   405 32  HOH   HOH A . 
D 4 HOH   6   406 54  HOH   HOH A . 
D 4 HOH   7   407 39  HOH   HOH A . 
D 4 HOH   8   408 155 HOH   HOH A . 
D 4 HOH   9   409 34  HOH   HOH A . 
D 4 HOH   10  410 29  HOH   HOH A . 
D 4 HOH   11  411 150 HOH   HOH A . 
D 4 HOH   12  412 80  HOH   HOH A . 
D 4 HOH   13  413 136 HOH   HOH A . 
D 4 HOH   14  414 169 HOH   HOH A . 
D 4 HOH   15  415 22  HOH   HOH A . 
D 4 HOH   16  416 63  HOH   HOH A . 
D 4 HOH   17  417 27  HOH   HOH A . 
D 4 HOH   18  418 68  HOH   HOH A . 
D 4 HOH   19  419 145 HOH   HOH A . 
D 4 HOH   20  420 14  HOH   HOH A . 
D 4 HOH   21  421 21  HOH   HOH A . 
D 4 HOH   22  422 84  HOH   HOH A . 
D 4 HOH   23  423 67  HOH   HOH A . 
D 4 HOH   24  424 138 HOH   HOH A . 
D 4 HOH   25  425 24  HOH   HOH A . 
D 4 HOH   26  426 139 HOH   HOH A . 
D 4 HOH   27  427 6   HOH   HOH A . 
D 4 HOH   28  428 43  HOH   HOH A . 
D 4 HOH   29  429 8   HOH   HOH A . 
D 4 HOH   30  430 49  HOH   HOH A . 
D 4 HOH   31  431 217 HOH   HOH A . 
D 4 HOH   32  432 13  HOH   HOH A . 
D 4 HOH   33  433 82  HOH   HOH A . 
D 4 HOH   34  434 101 HOH   HOH A . 
D 4 HOH   35  435 31  HOH   HOH A . 
D 4 HOH   36  436 107 HOH   HOH A . 
D 4 HOH   37  437 212 HOH   HOH A . 
D 4 HOH   38  438 113 HOH   HOH A . 
D 4 HOH   39  439 12  HOH   HOH A . 
D 4 HOH   40  440 17  HOH   HOH A . 
D 4 HOH   41  441 45  HOH   HOH A . 
D 4 HOH   42  442 40  HOH   HOH A . 
D 4 HOH   43  443 3   HOH   HOH A . 
D 4 HOH   44  444 37  HOH   HOH A . 
D 4 HOH   45  445 9   HOH   HOH A . 
D 4 HOH   46  446 20  HOH   HOH A . 
D 4 HOH   47  447 36  HOH   HOH A . 
D 4 HOH   48  448 15  HOH   HOH A . 
D 4 HOH   49  449 210 HOH   HOH A . 
D 4 HOH   50  450 117 HOH   HOH A . 
D 4 HOH   51  451 148 HOH   HOH A . 
D 4 HOH   52  452 2   HOH   HOH A . 
D 4 HOH   53  453 209 HOH   HOH A . 
D 4 HOH   54  454 18  HOH   HOH A . 
D 4 HOH   55  455 30  HOH   HOH A . 
D 4 HOH   56  456 172 HOH   HOH A . 
D 4 HOH   57  457 47  HOH   HOH A . 
D 4 HOH   58  458 16  HOH   HOH A . 
D 4 HOH   59  459 115 HOH   HOH A . 
D 4 HOH   60  460 83  HOH   HOH A . 
D 4 HOH   61  461 57  HOH   HOH A . 
D 4 HOH   62  462 182 HOH   HOH A . 
D 4 HOH   63  463 11  HOH   HOH A . 
D 4 HOH   64  464 35  HOH   HOH A . 
D 4 HOH   65  465 5   HOH   HOH A . 
D 4 HOH   66  466 152 HOH   HOH A . 
D 4 HOH   67  467 10  HOH   HOH A . 
D 4 HOH   68  468 52  HOH   HOH A . 
D 4 HOH   69  469 151 HOH   HOH A . 
D 4 HOH   70  470 41  HOH   HOH A . 
D 4 HOH   71  471 154 HOH   HOH A . 
D 4 HOH   72  472 185 HOH   HOH A . 
D 4 HOH   73  473 4   HOH   HOH A . 
D 4 HOH   74  474 110 HOH   HOH A . 
D 4 HOH   75  475 94  HOH   HOH A . 
D 4 HOH   76  476 7   HOH   HOH A . 
D 4 HOH   77  477 116 HOH   HOH A . 
D 4 HOH   78  478 167 HOH   HOH A . 
D 4 HOH   79  479 23  HOH   HOH A . 
D 4 HOH   80  480 105 HOH   HOH A . 
D 4 HOH   81  481 176 HOH   HOH A . 
D 4 HOH   82  482 1   HOH   HOH A . 
D 4 HOH   83  483 66  HOH   HOH A . 
D 4 HOH   84  484 75  HOH   HOH A . 
D 4 HOH   85  485 159 HOH   HOH A . 
D 4 HOH   86  486 58  HOH   HOH A . 
D 4 HOH   87  487 97  HOH   HOH A . 
D 4 HOH   88  488 126 HOH   HOH A . 
D 4 HOH   89  489 72  HOH   HOH A . 
D 4 HOH   90  490 59  HOH   HOH A . 
D 4 HOH   91  491 53  HOH   HOH A . 
D 4 HOH   92  492 62  HOH   HOH A . 
D 4 HOH   93  493 61  HOH   HOH A . 
D 4 HOH   94  494 118 HOH   HOH A . 
D 4 HOH   95  495 124 HOH   HOH A . 
D 4 HOH   96  496 85  HOH   HOH A . 
D 4 HOH   97  497 143 HOH   HOH A . 
D 4 HOH   98  498 19  HOH   HOH A . 
D 4 HOH   99  499 149 HOH   HOH A . 
D 4 HOH   100 500 103 HOH   HOH A . 
D 4 HOH   101 501 55  HOH   HOH A . 
D 4 HOH   102 502 51  HOH   HOH A . 
D 4 HOH   103 503 161 HOH   HOH A . 
D 4 HOH   104 504 78  HOH   HOH A . 
D 4 HOH   105 505 86  HOH   HOH A . 
D 4 HOH   106 506 73  HOH   HOH A . 
D 4 HOH   107 507 137 HOH   HOH A . 
D 4 HOH   108 508 33  HOH   HOH A . 
D 4 HOH   109 509 165 HOH   HOH A . 
D 4 HOH   110 510 46  HOH   HOH A . 
D 4 HOH   111 511 168 HOH   HOH A . 
D 4 HOH   112 512 71  HOH   HOH A . 
D 4 HOH   113 513 109 HOH   HOH A . 
D 4 HOH   114 514 91  HOH   HOH A . 
D 4 HOH   115 515 48  HOH   HOH A . 
D 4 HOH   116 516 87  HOH   HOH A . 
D 4 HOH   117 517 70  HOH   HOH A . 
D 4 HOH   118 518 193 HOH   HOH A . 
D 4 HOH   119 519 160 HOH   HOH A . 
D 4 HOH   120 520 76  HOH   HOH A . 
D 4 HOH   121 521 123 HOH   HOH A . 
D 4 HOH   122 522 77  HOH   HOH A . 
D 4 HOH   123 523 164 HOH   HOH A . 
D 4 HOH   124 524 120 HOH   HOH A . 
D 4 HOH   125 525 140 HOH   HOH A . 
D 4 HOH   126 526 191 HOH   HOH A . 
D 4 HOH   127 527 205 HOH   HOH A . 
D 4 HOH   128 528 106 HOH   HOH A . 
D 4 HOH   129 529 38  HOH   HOH A . 
D 4 HOH   130 530 81  HOH   HOH A . 
D 4 HOH   131 531 114 HOH   HOH A . 
D 4 HOH   132 532 69  HOH   HOH A . 
D 4 HOH   133 533 74  HOH   HOH A . 
D 4 HOH   134 534 79  HOH   HOH A . 
D 4 HOH   135 535 199 HOH   HOH A . 
D 4 HOH   136 536 196 HOH   HOH A . 
D 4 HOH   137 537 56  HOH   HOH A . 
D 4 HOH   138 538 102 HOH   HOH A . 
D 4 HOH   139 539 112 HOH   HOH A . 
D 4 HOH   140 540 179 HOH   HOH A . 
D 4 HOH   141 541 119 HOH   HOH A . 
D 4 HOH   142 542 64  HOH   HOH A . 
D 4 HOH   143 543 88  HOH   HOH A . 
D 4 HOH   144 544 188 HOH   HOH A . 
D 4 HOH   145 545 183 HOH   HOH A . 
D 4 HOH   146 546 89  HOH   HOH A . 
D 4 HOH   147 547 200 HOH   HOH A . 
D 4 HOH   148 548 50  HOH   HOH A . 
D 4 HOH   149 549 192 HOH   HOH A . 
D 4 HOH   150 550 60  HOH   HOH A . 
D 4 HOH   151 551 111 HOH   HOH A . 
D 4 HOH   152 552 195 HOH   HOH A . 
D 4 HOH   153 553 44  HOH   HOH A . 
D 4 HOH   154 554 178 HOH   HOH A . 
D 4 HOH   155 555 42  HOH   HOH A . 
D 4 HOH   156 556 28  HOH   HOH A . 
D 4 HOH   157 557 127 HOH   HOH A . 
D 4 HOH   158 558 218 HOH   HOH A . 
D 4 HOH   159 559 132 HOH   HOH A . 
D 4 HOH   160 560 162 HOH   HOH A . 
D 4 HOH   161 561 125 HOH   HOH A . 
D 4 HOH   162 562 180 HOH   HOH A . 
D 4 HOH   163 563 130 HOH   HOH A . 
D 4 HOH   164 564 90  HOH   HOH A . 
D 4 HOH   165 565 187 HOH   HOH A . 
D 4 HOH   166 566 197 HOH   HOH A . 
D 4 HOH   167 567 129 HOH   HOH A . 
D 4 HOH   168 568 201 HOH   HOH A . 
D 4 HOH   169 569 219 HOH   HOH A . 
D 4 HOH   170 570 177 HOH   HOH A . 
D 4 HOH   171 571 93  HOH   HOH A . 
D 4 HOH   172 572 174 HOH   HOH A . 
D 4 HOH   173 573 146 HOH   HOH A . 
D 4 HOH   174 574 208 HOH   HOH A . 
D 4 HOH   175 575 144 HOH   HOH A . 
D 4 HOH   176 576 157 HOH   HOH A . 
D 4 HOH   177 577 135 HOH   HOH A . 
D 4 HOH   178 578 175 HOH   HOH A . 
D 4 HOH   179 579 211 HOH   HOH A . 
D 4 HOH   180 580 181 HOH   HOH A . 
D 4 HOH   181 581 190 HOH   HOH A . 
D 4 HOH   182 582 186 HOH   HOH A . 
D 4 HOH   183 583 65  HOH   HOH A . 
D 4 HOH   184 584 156 HOH   HOH A . 
D 4 HOH   185 585 95  HOH   HOH A . 
D 4 HOH   186 586 203 HOH   HOH A . 
D 4 HOH   187 587 170 HOH   HOH A . 
D 4 HOH   188 588 171 HOH   HOH A . 
D 4 HOH   189 589 184 HOH   HOH A . 
D 4 HOH   190 590 131 HOH   HOH A . 
D 4 HOH   191 591 134 HOH   HOH A . 
D 4 HOH   192 592 108 HOH   HOH A . 
D 4 HOH   193 593 153 HOH   HOH A . 
D 4 HOH   194 594 198 HOH   HOH A . 
D 4 HOH   195 595 215 HOH   HOH A . 
D 4 HOH   196 596 163 HOH   HOH A . 
D 4 HOH   197 597 216 HOH   HOH A . 
D 4 HOH   198 598 166 HOH   HOH A . 
D 4 HOH   199 599 206 HOH   HOH A . 
D 4 HOH   200 600 98  HOH   HOH A . 
D 4 HOH   201 601 104 HOH   HOH A . 
D 4 HOH   202 602 122 HOH   HOH A . 
D 4 HOH   203 603 202 HOH   HOH A . 
D 4 HOH   204 604 142 HOH   HOH A . 
D 4 HOH   205 605 96  HOH   HOH A . 
D 4 HOH   206 606 204 HOH   HOH A . 
D 4 HOH   207 607 173 HOH   HOH A . 
D 4 HOH   208 608 214 HOH   HOH A . 
D 4 HOH   209 609 100 HOH   HOH A . 
D 4 HOH   210 610 207 HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A LYS 4 ? CG ? A LYS 8 CG 
2 1 Y 1 A LYS 4 ? CD ? A LYS 8 CD 
3 1 Y 1 A LYS 4 ? CE ? A LYS 8 CE 
4 1 Y 1 A LYS 4 ? NZ ? A LYS 8 NZ 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   108.090 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9C17 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     76.024 
_cell.length_a_esd                 ? 
_cell.length_b                     42.137 
_cell.length_b_esd                 ? 
_cell.length_c                     66.150 
_cell.length_c_esd                 ? 
_cell.volume                       201431.902 
_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                         9C17 
_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                   9C17 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.23 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.92 
_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              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M MES pH 6.5, 12% (w/v) PEG20000, 25% (v/v) MPD, 1 mM NADP+' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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                      'KB bimorph' 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-04-02 
_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                    'Si(111) DCM' 
_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   0.9201 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSLS-II BEAMLINE 17-ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9201 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-1 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          16.60 
_reflns.entry_id                                       9C17 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.63 
_reflns.d_resolution_low                               33.89 
_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                                     24724 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.4 
_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                                0.201 
_reflns.pdbx_Rpim_I_all                                0.101 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.991 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.173 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.63 
_reflns_shell.d_res_low                                     1.66 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1200 
_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                               4.0 
_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                               1.766 
_reflns_shell.pdbx_Rpim_I_all                               0.872 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.346 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.6 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.529 
_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                               19.00 
_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                                 9C17 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.63 
_refine.ls_d_res_low                             33.89 
_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                     24623 
_refine.ls_number_reflns_R_free                  1219 
_refine.ls_number_reflns_R_work                  23404 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.15 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1797 
_refine.ls_R_factor_R_free                       0.1996 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1787 
_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                      9C16 
_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                 21.6166 
_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                            0.2180 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.63 
_refine_hist.d_res_low                        33.89 
_refine_hist.number_atoms_solvent             210 
_refine_hist.number_atoms_total               1813 
_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        1531 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         72 
_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' ? 0.0069  ? 1686 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9987  ? 2318 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0596  ? 270  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0072  ? 293  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.7114 ? 604  ? 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' 1.63 1.70  . . 120 2514 96.63 . . . . 0.2751 . . . . . . . . . . . 0.3195 
'X-RAY DIFFRACTION' 1.70 1.78  . . 131 2570 99.05 . . . . 0.2526 . . . . . . . . . . . 0.3094 
'X-RAY DIFFRACTION' 1.78 1.87  . . 151 2573 99.56 . . . . 0.2240 . . . . . . . . . . . 0.2582 
'X-RAY DIFFRACTION' 1.87 1.99  . . 143 2595 99.31 . . . . 0.2051 . . . . . . . . . . . 0.2295 
'X-RAY DIFFRACTION' 1.99 2.14  . . 120 2610 99.49 . . . . 0.1859 . . . . . . . . . . . 0.2021 
'X-RAY DIFFRACTION' 2.14 2.36  . . 114 2630 99.71 . . . . 0.1642 . . . . . . . . . . . 0.1967 
'X-RAY DIFFRACTION' 2.36 2.70  . . 158 2595 99.49 . . . . 0.1706 . . . . . . . . . . . 0.2186 
'X-RAY DIFFRACTION' 2.70 3.40  . . 119 2648 99.60 . . . . 0.1562 . . . . . . . . . . . 0.1710 
'X-RAY DIFFRACTION' 3.40 33.89 . . 163 2669 99.44 . . . . 0.1600 . . . . . . . . . . . 0.1602 
# 
_struct.entry_id                     9C17 
_struct.title                        'Human biliverdin IX beta reductase in complex with NADP and BCT001028' 
_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        9C17 
_struct_keywords.text            'NADP binding, heme degradation, thrombopoiesis, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    BLVRB_HUMAN 
_struct_ref.pdbx_db_accession          P30043 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAVKKIAIFGATGQTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPRPAHVVVGDVLQAADVDKTVAGQDAVIVLLGTRND
LSPTTVMSEGARNIVAAMKAHGVDKVVACTSAFLLWDPTKVPPRLQAVTDDHIRMHKVLRESGLKYVAVMPPHIGDQPLT
GAYTVTLDGRGPSRVISKHDLGHFMLRCLTTDEYDGHSTYPSHQYQ
;
_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              9C17 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 5 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 210 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P30043 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  206 
_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       206 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9C17 GLY A 1 ? UNP P30043 ? ? 'expression tag' -3 1 
1 9C17 SER A 2 ? UNP P30043 ? ? 'expression tag' -2 2 
1 9C17 ARG A 3 ? UNP P30043 ? ? 'expression tag' -1 3 
1 9C17 THR A 4 ? UNP P30043 ? ? 'expression tag' 0  4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 17  ? ALA A 30  ? GLY A 13  ALA A 26  1 ? 14 
HELX_P HELX_P2 AA2 ASP A 40  ? LEU A 44  ? ASP A 36  LEU A 40  5 ? 5  
HELX_P HELX_P3 AA3 GLN A 61  ? ALA A 70  ? GLN A 57  ALA A 66  1 ? 10 
HELX_P HELX_P4 AA4 THR A 89  ? GLY A 106 ? THR A 85  GLY A 102 1 ? 18 
HELX_P HELX_P5 AA5 SER A 115 ? TRP A 120 ? SER A 111 TRP A 116 5 ? 6  
HELX_P HELX_P6 AA6 ASP A 121 ? VAL A 125 ? ASP A 117 VAL A 121 5 ? 5  
HELX_P HELX_P7 AA7 PRO A 126 ? ARG A 128 ? PRO A 122 ARG A 124 5 ? 3  
HELX_P HELX_P8 AA8 LEU A 129 ? SER A 146 ? LEU A 125 SER A 142 1 ? 18 
HELX_P HELX_P9 AA9 LYS A 182 ? CYS A 192 ? LYS A 178 CYS A 188 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 HIS A 53  ? VAL A 56  ? HIS A 49  VAL A 52  
AA1 2 GLU A 33  ? VAL A 38  ? GLU A 29  VAL A 34  
AA1 3 LYS A 9   ? PHE A 13  ? LYS A 5   PHE A 9   
AA1 4 ALA A 74  ? VAL A 77  ? ALA A 70  VAL A 73  
AA1 5 LYS A 109 ? CYS A 113 ? LYS A 105 CYS A 109 
AA1 6 LYS A 149 ? VAL A 153 ? LYS A 145 VAL A 149 
AA1 7 SER A 202 ? SER A 206 ? SER A 198 SER A 202 
AA1 8 THR A 168 ? LEU A 171 ? THR A 164 LEU A 167 
AA2 1 HIS A 157 ? GLY A 159 ? HIS A 153 GLY A 155 
AA2 2 VAL A 179 ? SER A 181 ? VAL A 175 SER A 177 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 55  ? O VAL A 51  N VAL A 36  ? N VAL A 32  
AA1 2 3 O THR A 35  ? O THR A 31  N ILE A 10  ? N ILE A 6   
AA1 3 4 N ALA A 11  ? N ALA A 7   O ILE A 76  ? O ILE A 72  
AA1 4 5 N VAL A 75  ? N VAL A 71  O VAL A 111 ? O VAL A 107 
AA1 5 6 N VAL A 110 ? N VAL A 106 O LYS A 149 ? O LYS A 145 
AA1 6 7 N ALA A 152 ? N ALA A 148 O THR A 203 ? O THR A 199 
AA1 7 8 O SER A 206 ? O SER A 202 N THR A 168 ? N THR A 164 
AA2 1 2 N GLY A 159 ? N GLY A 155 O ILE A 180 ? O ILE A 176 
# 
_pdbx_entry_details.entry_id                   9C17 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 78  ? ? 54.07   -122.98 
2 1 THR A 110 ? ? -119.94 -104.73 
3 1 PRO A 152 ? ? -77.82  -150.69 
# 
_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     410 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   D 
_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_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 609 ? 5.82 . 
2 1 O ? A HOH 610 ? 6.56 . 
# 
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 GLY -3  ? A GLY 1   
2 1 Y 1 A SER -2  ? A SER 2   
3 1 Y 1 A ARG -1  ? A ARG 3   
4 1 Y 1 A THR 0   ? A THR 4   
5 1 Y 1 A MET 1   ? A MET 5   
6 1 Y 1 A GLN 206 ? A GLN 210 
# 
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 
A1ATJ C10  C  Y N 1   
A1ATJ C13  C  Y N 2   
A1ATJ C15  C  Y N 3   
A1ATJ C20  C  Y N 4   
A1ATJ C21  C  Y N 5   
A1ATJ C24  C  Y N 6   
A1ATJ C02  C  N N 7   
A1ATJ C04  C  Y N 8   
A1ATJ C05  C  Y N 9   
A1ATJ C06  C  Y N 10  
A1ATJ C07  C  Y N 11  
A1ATJ C08  C  Y N 12  
A1ATJ C11  C  Y N 13  
A1ATJ C12  C  Y N 14  
A1ATJ C14  C  Y N 15  
A1ATJ C16  C  Y N 16  
A1ATJ C18  C  Y N 17  
A1ATJ C23  C  Y N 18  
A1ATJ N09  N  Y N 19  
A1ATJ N22  N  Y N 20  
A1ATJ O01  O  N N 21  
A1ATJ O03  O  N N 22  
A1ATJ S19  S  Y N 23  
A1ATJ CL17 CL N N 24  
A1ATJ H131 H  N N 25  
A1ATJ H151 H  N N 26  
A1ATJ H201 H  N N 27  
A1ATJ H211 H  N N 28  
A1ATJ H241 H  N N 29  
A1ATJ H051 H  N N 30  
A1ATJ H061 H  N N 31  
A1ATJ H121 H  N N 32  
A1ATJ H141 H  N N 33  
A1ATJ H231 H  N N 34  
A1ATJ H1   H  N N 35  
ALA   N    N  N N 36  
ALA   CA   C  N S 37  
ALA   C    C  N N 38  
ALA   O    O  N N 39  
ALA   CB   C  N N 40  
ALA   OXT  O  N N 41  
ALA   H    H  N N 42  
ALA   H2   H  N N 43  
ALA   HA   H  N N 44  
ALA   HB1  H  N N 45  
ALA   HB2  H  N N 46  
ALA   HB3  H  N N 47  
ALA   HXT  H  N N 48  
ARG   N    N  N N 49  
ARG   CA   C  N S 50  
ARG   C    C  N N 51  
ARG   O    O  N N 52  
ARG   CB   C  N N 53  
ARG   CG   C  N N 54  
ARG   CD   C  N N 55  
ARG   NE   N  N N 56  
ARG   CZ   C  N N 57  
ARG   NH1  N  N N 58  
ARG   NH2  N  N N 59  
ARG   OXT  O  N N 60  
ARG   H    H  N N 61  
ARG   H2   H  N N 62  
ARG   HA   H  N N 63  
ARG   HB2  H  N N 64  
ARG   HB3  H  N N 65  
ARG   HG2  H  N N 66  
ARG   HG3  H  N N 67  
ARG   HD2  H  N N 68  
ARG   HD3  H  N N 69  
ARG   HE   H  N N 70  
ARG   HH11 H  N N 71  
ARG   HH12 H  N N 72  
ARG   HH21 H  N N 73  
ARG   HH22 H  N N 74  
ARG   HXT  H  N N 75  
ASN   N    N  N N 76  
ASN   CA   C  N S 77  
ASN   C    C  N N 78  
ASN   O    O  N N 79  
ASN   CB   C  N N 80  
ASN   CG   C  N N 81  
ASN   OD1  O  N N 82  
ASN   ND2  N  N N 83  
ASN   OXT  O  N N 84  
ASN   H    H  N N 85  
ASN   H2   H  N N 86  
ASN   HA   H  N N 87  
ASN   HB2  H  N N 88  
ASN   HB3  H  N N 89  
ASN   HD21 H  N N 90  
ASN   HD22 H  N N 91  
ASN   HXT  H  N N 92  
ASP   N    N  N N 93  
ASP   CA   C  N S 94  
ASP   C    C  N N 95  
ASP   O    O  N N 96  
ASP   CB   C  N N 97  
ASP   CG   C  N N 98  
ASP   OD1  O  N N 99  
ASP   OD2  O  N N 100 
ASP   OXT  O  N N 101 
ASP   H    H  N N 102 
ASP   H2   H  N N 103 
ASP   HA   H  N N 104 
ASP   HB2  H  N N 105 
ASP   HB3  H  N N 106 
ASP   HD2  H  N N 107 
ASP   HXT  H  N N 108 
CYS   N    N  N N 109 
CYS   CA   C  N R 110 
CYS   C    C  N N 111 
CYS   O    O  N N 112 
CYS   CB   C  N N 113 
CYS   SG   S  N N 114 
CYS   OXT  O  N N 115 
CYS   H    H  N N 116 
CYS   H2   H  N N 117 
CYS   HA   H  N N 118 
CYS   HB2  H  N N 119 
CYS   HB3  H  N N 120 
CYS   HG   H  N N 121 
CYS   HXT  H  N N 122 
GLN   N    N  N N 123 
GLN   CA   C  N S 124 
GLN   C    C  N N 125 
GLN   O    O  N N 126 
GLN   CB   C  N N 127 
GLN   CG   C  N N 128 
GLN   CD   C  N N 129 
GLN   OE1  O  N N 130 
GLN   NE2  N  N N 131 
GLN   OXT  O  N N 132 
GLN   H    H  N N 133 
GLN   H2   H  N N 134 
GLN   HA   H  N N 135 
GLN   HB2  H  N N 136 
GLN   HB3  H  N N 137 
GLN   HG2  H  N N 138 
GLN   HG3  H  N N 139 
GLN   HE21 H  N N 140 
GLN   HE22 H  N N 141 
GLN   HXT  H  N N 142 
GLU   N    N  N N 143 
GLU   CA   C  N S 144 
GLU   C    C  N N 145 
GLU   O    O  N N 146 
GLU   CB   C  N N 147 
GLU   CG   C  N N 148 
GLU   CD   C  N N 149 
GLU   OE1  O  N N 150 
GLU   OE2  O  N N 151 
GLU   OXT  O  N N 152 
GLU   H    H  N N 153 
GLU   H2   H  N N 154 
GLU   HA   H  N N 155 
GLU   HB2  H  N N 156 
GLU   HB3  H  N N 157 
GLU   HG2  H  N N 158 
GLU   HG3  H  N N 159 
GLU   HE2  H  N N 160 
GLU   HXT  H  N N 161 
GLY   N    N  N N 162 
GLY   CA   C  N N 163 
GLY   C    C  N N 164 
GLY   O    O  N N 165 
GLY   OXT  O  N N 166 
GLY   H    H  N N 167 
GLY   H2   H  N N 168 
GLY   HA2  H  N N 169 
GLY   HA3  H  N N 170 
GLY   HXT  H  N N 171 
HIS   N    N  N N 172 
HIS   CA   C  N S 173 
HIS   C    C  N N 174 
HIS   O    O  N N 175 
HIS   CB   C  N N 176 
HIS   CG   C  Y N 177 
HIS   ND1  N  Y N 178 
HIS   CD2  C  Y N 179 
HIS   CE1  C  Y N 180 
HIS   NE2  N  Y N 181 
HIS   OXT  O  N N 182 
HIS   H    H  N N 183 
HIS   H2   H  N N 184 
HIS   HA   H  N N 185 
HIS   HB2  H  N N 186 
HIS   HB3  H  N N 187 
HIS   HD1  H  N N 188 
HIS   HD2  H  N N 189 
HIS   HE1  H  N N 190 
HIS   HE2  H  N N 191 
HIS   HXT  H  N N 192 
HOH   O    O  N N 193 
HOH   H1   H  N N 194 
HOH   H2   H  N N 195 
ILE   N    N  N N 196 
ILE   CA   C  N S 197 
ILE   C    C  N N 198 
ILE   O    O  N N 199 
ILE   CB   C  N S 200 
ILE   CG1  C  N N 201 
ILE   CG2  C  N N 202 
ILE   CD1  C  N N 203 
ILE   OXT  O  N N 204 
ILE   H    H  N N 205 
ILE   H2   H  N N 206 
ILE   HA   H  N N 207 
ILE   HB   H  N N 208 
ILE   HG12 H  N N 209 
ILE   HG13 H  N N 210 
ILE   HG21 H  N N 211 
ILE   HG22 H  N N 212 
ILE   HG23 H  N N 213 
ILE   HD11 H  N N 214 
ILE   HD12 H  N N 215 
ILE   HD13 H  N N 216 
ILE   HXT  H  N N 217 
LEU   N    N  N N 218 
LEU   CA   C  N S 219 
LEU   C    C  N N 220 
LEU   O    O  N N 221 
LEU   CB   C  N N 222 
LEU   CG   C  N N 223 
LEU   CD1  C  N N 224 
LEU   CD2  C  N N 225 
LEU   OXT  O  N N 226 
LEU   H    H  N N 227 
LEU   H2   H  N N 228 
LEU   HA   H  N N 229 
LEU   HB2  H  N N 230 
LEU   HB3  H  N N 231 
LEU   HG   H  N N 232 
LEU   HD11 H  N N 233 
LEU   HD12 H  N N 234 
LEU   HD13 H  N N 235 
LEU   HD21 H  N N 236 
LEU   HD22 H  N N 237 
LEU   HD23 H  N N 238 
LEU   HXT  H  N N 239 
LYS   N    N  N N 240 
LYS   CA   C  N S 241 
LYS   C    C  N N 242 
LYS   O    O  N N 243 
LYS   CB   C  N N 244 
LYS   CG   C  N N 245 
LYS   CD   C  N N 246 
LYS   CE   C  N N 247 
LYS   NZ   N  N N 248 
LYS   OXT  O  N N 249 
LYS   H    H  N N 250 
LYS   H2   H  N N 251 
LYS   HA   H  N N 252 
LYS   HB2  H  N N 253 
LYS   HB3  H  N N 254 
LYS   HG2  H  N N 255 
LYS   HG3  H  N N 256 
LYS   HD2  H  N N 257 
LYS   HD3  H  N N 258 
LYS   HE2  H  N N 259 
LYS   HE3  H  N N 260 
LYS   HZ1  H  N N 261 
LYS   HZ2  H  N N 262 
LYS   HZ3  H  N N 263 
LYS   HXT  H  N N 264 
MET   N    N  N N 265 
MET   CA   C  N S 266 
MET   C    C  N N 267 
MET   O    O  N N 268 
MET   CB   C  N N 269 
MET   CG   C  N N 270 
MET   SD   S  N N 271 
MET   CE   C  N N 272 
MET   OXT  O  N N 273 
MET   H    H  N N 274 
MET   H2   H  N N 275 
MET   HA   H  N N 276 
MET   HB2  H  N N 277 
MET   HB3  H  N N 278 
MET   HG2  H  N N 279 
MET   HG3  H  N N 280 
MET   HE1  H  N N 281 
MET   HE2  H  N N 282 
MET   HE3  H  N N 283 
MET   HXT  H  N N 284 
NAP   PA   P  N R 285 
NAP   O1A  O  N N 286 
NAP   O2A  O  N N 287 
NAP   O5B  O  N N 288 
NAP   C5B  C  N N 289 
NAP   C4B  C  N R 290 
NAP   O4B  O  N N 291 
NAP   C3B  C  N R 292 
NAP   O3B  O  N N 293 
NAP   C2B  C  N R 294 
NAP   O2B  O  N N 295 
NAP   C1B  C  N R 296 
NAP   N9A  N  Y N 297 
NAP   C8A  C  Y N 298 
NAP   N7A  N  Y N 299 
NAP   C5A  C  Y N 300 
NAP   C6A  C  Y N 301 
NAP   N6A  N  N N 302 
NAP   N1A  N  Y N 303 
NAP   C2A  C  Y N 304 
NAP   N3A  N  Y N 305 
NAP   C4A  C  Y N 306 
NAP   O3   O  N N 307 
NAP   PN   P  N N 308 
NAP   O1N  O  N N 309 
NAP   O2N  O  N N 310 
NAP   O5D  O  N N 311 
NAP   C5D  C  N N 312 
NAP   C4D  C  N R 313 
NAP   O4D  O  N N 314 
NAP   C3D  C  N S 315 
NAP   O3D  O  N N 316 
NAP   C2D  C  N R 317 
NAP   O2D  O  N N 318 
NAP   C1D  C  N R 319 
NAP   N1N  N  Y N 320 
NAP   C2N  C  Y N 321 
NAP   C3N  C  Y N 322 
NAP   C7N  C  N N 323 
NAP   O7N  O  N N 324 
NAP   N7N  N  N N 325 
NAP   C4N  C  Y N 326 
NAP   C5N  C  Y N 327 
NAP   C6N  C  Y N 328 
NAP   P2B  P  N N 329 
NAP   O1X  O  N N 330 
NAP   O2X  O  N N 331 
NAP   O3X  O  N N 332 
NAP   HOA2 H  N N 333 
NAP   H51A H  N N 334 
NAP   H52A H  N N 335 
NAP   H4B  H  N N 336 
NAP   H3B  H  N N 337 
NAP   HO3A H  N N 338 
NAP   H2B  H  N N 339 
NAP   H1B  H  N N 340 
NAP   H8A  H  N N 341 
NAP   H61A H  N N 342 
NAP   H62A H  N N 343 
NAP   H2A  H  N N 344 
NAP   H51N H  N N 345 
NAP   H52N H  N N 346 
NAP   H4D  H  N N 347 
NAP   H3D  H  N N 348 
NAP   HO3N H  N N 349 
NAP   H2D  H  N N 350 
NAP   HO2N H  N N 351 
NAP   H1D  H  N N 352 
NAP   H2N  H  N N 353 
NAP   H71N H  N N 354 
NAP   H72N H  N N 355 
NAP   H4N  H  N N 356 
NAP   H5N  H  N N 357 
NAP   H6N  H  N N 358 
NAP   HOP2 H  N N 359 
NAP   HOP3 H  N N 360 
PHE   N    N  N N 361 
PHE   CA   C  N S 362 
PHE   C    C  N N 363 
PHE   O    O  N N 364 
PHE   CB   C  N N 365 
PHE   CG   C  Y N 366 
PHE   CD1  C  Y N 367 
PHE   CD2  C  Y N 368 
PHE   CE1  C  Y N 369 
PHE   CE2  C  Y N 370 
PHE   CZ   C  Y N 371 
PHE   OXT  O  N N 372 
PHE   H    H  N N 373 
PHE   H2   H  N N 374 
PHE   HA   H  N N 375 
PHE   HB2  H  N N 376 
PHE   HB3  H  N N 377 
PHE   HD1  H  N N 378 
PHE   HD2  H  N N 379 
PHE   HE1  H  N N 380 
PHE   HE2  H  N N 381 
PHE   HZ   H  N N 382 
PHE   HXT  H  N N 383 
PRO   N    N  N N 384 
PRO   CA   C  N S 385 
PRO   C    C  N N 386 
PRO   O    O  N N 387 
PRO   CB   C  N N 388 
PRO   CG   C  N N 389 
PRO   CD   C  N N 390 
PRO   OXT  O  N N 391 
PRO   H    H  N N 392 
PRO   HA   H  N N 393 
PRO   HB2  H  N N 394 
PRO   HB3  H  N N 395 
PRO   HG2  H  N N 396 
PRO   HG3  H  N N 397 
PRO   HD2  H  N N 398 
PRO   HD3  H  N N 399 
PRO   HXT  H  N N 400 
SER   N    N  N N 401 
SER   CA   C  N S 402 
SER   C    C  N N 403 
SER   O    O  N N 404 
SER   CB   C  N N 405 
SER   OG   O  N N 406 
SER   OXT  O  N N 407 
SER   H    H  N N 408 
SER   H2   H  N N 409 
SER   HA   H  N N 410 
SER   HB2  H  N N 411 
SER   HB3  H  N N 412 
SER   HG   H  N N 413 
SER   HXT  H  N N 414 
THR   N    N  N N 415 
THR   CA   C  N S 416 
THR   C    C  N N 417 
THR   O    O  N N 418 
THR   CB   C  N R 419 
THR   OG1  O  N N 420 
THR   CG2  C  N N 421 
THR   OXT  O  N N 422 
THR   H    H  N N 423 
THR   H2   H  N N 424 
THR   HA   H  N N 425 
THR   HB   H  N N 426 
THR   HG1  H  N N 427 
THR   HG21 H  N N 428 
THR   HG22 H  N N 429 
THR   HG23 H  N N 430 
THR   HXT  H  N N 431 
TRP   N    N  N N 432 
TRP   CA   C  N S 433 
TRP   C    C  N N 434 
TRP   O    O  N N 435 
TRP   CB   C  N N 436 
TRP   CG   C  Y N 437 
TRP   CD1  C  Y N 438 
TRP   CD2  C  Y N 439 
TRP   NE1  N  Y N 440 
TRP   CE2  C  Y N 441 
TRP   CE3  C  Y N 442 
TRP   CZ2  C  Y N 443 
TRP   CZ3  C  Y N 444 
TRP   CH2  C  Y N 445 
TRP   OXT  O  N N 446 
TRP   H    H  N N 447 
TRP   H2   H  N N 448 
TRP   HA   H  N N 449 
TRP   HB2  H  N N 450 
TRP   HB3  H  N N 451 
TRP   HD1  H  N N 452 
TRP   HE1  H  N N 453 
TRP   HE3  H  N N 454 
TRP   HZ2  H  N N 455 
TRP   HZ3  H  N N 456 
TRP   HH2  H  N N 457 
TRP   HXT  H  N N 458 
TYR   N    N  N N 459 
TYR   CA   C  N S 460 
TYR   C    C  N N 461 
TYR   O    O  N N 462 
TYR   CB   C  N N 463 
TYR   CG   C  Y N 464 
TYR   CD1  C  Y N 465 
TYR   CD2  C  Y N 466 
TYR   CE1  C  Y N 467 
TYR   CE2  C  Y N 468 
TYR   CZ   C  Y N 469 
TYR   OH   O  N N 470 
TYR   OXT  O  N N 471 
TYR   H    H  N N 472 
TYR   H2   H  N N 473 
TYR   HA   H  N N 474 
TYR   HB2  H  N N 475 
TYR   HB3  H  N N 476 
TYR   HD1  H  N N 477 
TYR   HD2  H  N N 478 
TYR   HE1  H  N N 479 
TYR   HE2  H  N N 480 
TYR   HH   H  N N 481 
TYR   HXT  H  N N 482 
VAL   N    N  N N 483 
VAL   CA   C  N S 484 
VAL   C    C  N N 485 
VAL   O    O  N N 486 
VAL   CB   C  N N 487 
VAL   CG1  C  N N 488 
VAL   CG2  C  N N 489 
VAL   OXT  O  N N 490 
VAL   H    H  N N 491 
VAL   H2   H  N N 492 
VAL   HA   H  N N 493 
VAL   HB   H  N N 494 
VAL   HG11 H  N N 495 
VAL   HG12 H  N N 496 
VAL   HG13 H  N N 497 
VAL   HG21 H  N N 498 
VAL   HG22 H  N N 499 
VAL   HG23 H  N N 500 
VAL   HXT  H  N N 501 
# 
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 
A1ATJ C02  O01  sing N N 1   
A1ATJ O03  C02  doub N N 2   
A1ATJ C04  C02  sing N N 3   
A1ATJ C05  C04  doub Y N 4   
A1ATJ C06  C05  sing Y N 5   
A1ATJ C07  C06  doub Y N 6   
A1ATJ N09  C08  doub Y N 7   
A1ATJ C10  N09  sing Y N 8   
A1ATJ C12  C11  doub Y N 9   
A1ATJ C13  C12  sing Y N 10  
A1ATJ C14  C13  doub Y N 11  
A1ATJ C15  C14  sing Y N 12  
A1ATJ C16  C15  doub Y N 13  
A1ATJ CL17 C16  sing N N 14  
A1ATJ C11  C10  sing N N 15  
A1ATJ C18  C10  doub Y N 16  
A1ATJ S19  C18  sing Y N 17  
A1ATJ C20  S19  sing Y N 18  
A1ATJ C21  C20  doub Y N 19  
A1ATJ N22  C21  sing Y N 20  
A1ATJ C08  C07  sing N N 21  
A1ATJ C23  C07  sing Y N 22  
A1ATJ C24  C23  doub Y N 23  
A1ATJ C04  C24  sing Y N 24  
A1ATJ C08  N22  sing Y N 25  
A1ATJ C11  C16  sing Y N 26  
A1ATJ C18  N22  sing Y N 27  
A1ATJ C13  H131 sing N N 28  
A1ATJ C15  H151 sing N N 29  
A1ATJ C20  H201 sing N N 30  
A1ATJ C21  H211 sing N N 31  
A1ATJ C24  H241 sing N N 32  
A1ATJ C05  H051 sing N N 33  
A1ATJ C06  H061 sing N N 34  
A1ATJ C12  H121 sing N N 35  
A1ATJ C14  H141 sing N N 36  
A1ATJ C23  H231 sing N N 37  
A1ATJ O01  H1   sing N N 38  
ALA   N    CA   sing N N 39  
ALA   N    H    sing N N 40  
ALA   N    H2   sing N N 41  
ALA   CA   C    sing N N 42  
ALA   CA   CB   sing N N 43  
ALA   CA   HA   sing N N 44  
ALA   C    O    doub N N 45  
ALA   C    OXT  sing N N 46  
ALA   CB   HB1  sing N N 47  
ALA   CB   HB2  sing N N 48  
ALA   CB   HB3  sing N N 49  
ALA   OXT  HXT  sing N N 50  
ARG   N    CA   sing N N 51  
ARG   N    H    sing N N 52  
ARG   N    H2   sing N N 53  
ARG   CA   C    sing N N 54  
ARG   CA   CB   sing N N 55  
ARG   CA   HA   sing N N 56  
ARG   C    O    doub N N 57  
ARG   C    OXT  sing N N 58  
ARG   CB   CG   sing N N 59  
ARG   CB   HB2  sing N N 60  
ARG   CB   HB3  sing N N 61  
ARG   CG   CD   sing N N 62  
ARG   CG   HG2  sing N N 63  
ARG   CG   HG3  sing N N 64  
ARG   CD   NE   sing N N 65  
ARG   CD   HD2  sing N N 66  
ARG   CD   HD3  sing N N 67  
ARG   NE   CZ   sing N N 68  
ARG   NE   HE   sing N N 69  
ARG   CZ   NH1  sing N N 70  
ARG   CZ   NH2  doub N N 71  
ARG   NH1  HH11 sing N N 72  
ARG   NH1  HH12 sing N N 73  
ARG   NH2  HH21 sing N N 74  
ARG   NH2  HH22 sing N N 75  
ARG   OXT  HXT  sing N N 76  
ASN   N    CA   sing N N 77  
ASN   N    H    sing N N 78  
ASN   N    H2   sing N N 79  
ASN   CA   C    sing N N 80  
ASN   CA   CB   sing N N 81  
ASN   CA   HA   sing N N 82  
ASN   C    O    doub N N 83  
ASN   C    OXT  sing N N 84  
ASN   CB   CG   sing N N 85  
ASN   CB   HB2  sing N N 86  
ASN   CB   HB3  sing N N 87  
ASN   CG   OD1  doub N N 88  
ASN   CG   ND2  sing N N 89  
ASN   ND2  HD21 sing N N 90  
ASN   ND2  HD22 sing N N 91  
ASN   OXT  HXT  sing N N 92  
ASP   N    CA   sing N N 93  
ASP   N    H    sing N N 94  
ASP   N    H2   sing N N 95  
ASP   CA   C    sing N N 96  
ASP   CA   CB   sing N N 97  
ASP   CA   HA   sing N N 98  
ASP   C    O    doub N N 99  
ASP   C    OXT  sing N N 100 
ASP   CB   CG   sing N N 101 
ASP   CB   HB2  sing N N 102 
ASP   CB   HB3  sing N N 103 
ASP   CG   OD1  doub N N 104 
ASP   CG   OD2  sing N N 105 
ASP   OD2  HD2  sing N N 106 
ASP   OXT  HXT  sing N N 107 
CYS   N    CA   sing N N 108 
CYS   N    H    sing N N 109 
CYS   N    H2   sing N N 110 
CYS   CA   C    sing N N 111 
CYS   CA   CB   sing N N 112 
CYS   CA   HA   sing N N 113 
CYS   C    O    doub N N 114 
CYS   C    OXT  sing N N 115 
CYS   CB   SG   sing N N 116 
CYS   CB   HB2  sing N N 117 
CYS   CB   HB3  sing N N 118 
CYS   SG   HG   sing N N 119 
CYS   OXT  HXT  sing N N 120 
GLN   N    CA   sing N N 121 
GLN   N    H    sing N N 122 
GLN   N    H2   sing N N 123 
GLN   CA   C    sing N N 124 
GLN   CA   CB   sing N N 125 
GLN   CA   HA   sing N N 126 
GLN   C    O    doub N N 127 
GLN   C    OXT  sing N N 128 
GLN   CB   CG   sing N N 129 
GLN   CB   HB2  sing N N 130 
GLN   CB   HB3  sing N N 131 
GLN   CG   CD   sing N N 132 
GLN   CG   HG2  sing N N 133 
GLN   CG   HG3  sing N N 134 
GLN   CD   OE1  doub N N 135 
GLN   CD   NE2  sing N N 136 
GLN   NE2  HE21 sing N N 137 
GLN   NE2  HE22 sing N N 138 
GLN   OXT  HXT  sing N N 139 
GLU   N    CA   sing N N 140 
GLU   N    H    sing N N 141 
GLU   N    H2   sing N N 142 
GLU   CA   C    sing N N 143 
GLU   CA   CB   sing N N 144 
GLU   CA   HA   sing N N 145 
GLU   C    O    doub N N 146 
GLU   C    OXT  sing N N 147 
GLU   CB   CG   sing N N 148 
GLU   CB   HB2  sing N N 149 
GLU   CB   HB3  sing N N 150 
GLU   CG   CD   sing N N 151 
GLU   CG   HG2  sing N N 152 
GLU   CG   HG3  sing N N 153 
GLU   CD   OE1  doub N N 154 
GLU   CD   OE2  sing N N 155 
GLU   OE2  HE2  sing N N 156 
GLU   OXT  HXT  sing N N 157 
GLY   N    CA   sing N N 158 
GLY   N    H    sing N N 159 
GLY   N    H2   sing N N 160 
GLY   CA   C    sing N N 161 
GLY   CA   HA2  sing N N 162 
GLY   CA   HA3  sing N N 163 
GLY   C    O    doub N N 164 
GLY   C    OXT  sing N N 165 
GLY   OXT  HXT  sing N N 166 
HIS   N    CA   sing N N 167 
HIS   N    H    sing N N 168 
HIS   N    H2   sing N N 169 
HIS   CA   C    sing N N 170 
HIS   CA   CB   sing N N 171 
HIS   CA   HA   sing N N 172 
HIS   C    O    doub N N 173 
HIS   C    OXT  sing N N 174 
HIS   CB   CG   sing N N 175 
HIS   CB   HB2  sing N N 176 
HIS   CB   HB3  sing N N 177 
HIS   CG   ND1  sing Y N 178 
HIS   CG   CD2  doub Y N 179 
HIS   ND1  CE1  doub Y N 180 
HIS   ND1  HD1  sing N N 181 
HIS   CD2  NE2  sing Y N 182 
HIS   CD2  HD2  sing N N 183 
HIS   CE1  NE2  sing Y N 184 
HIS   CE1  HE1  sing N N 185 
HIS   NE2  HE2  sing N N 186 
HIS   OXT  HXT  sing N N 187 
HOH   O    H1   sing N N 188 
HOH   O    H2   sing N N 189 
ILE   N    CA   sing N N 190 
ILE   N    H    sing N N 191 
ILE   N    H2   sing N N 192 
ILE   CA   C    sing N N 193 
ILE   CA   CB   sing N N 194 
ILE   CA   HA   sing N N 195 
ILE   C    O    doub N N 196 
ILE   C    OXT  sing N N 197 
ILE   CB   CG1  sing N N 198 
ILE   CB   CG2  sing N N 199 
ILE   CB   HB   sing N N 200 
ILE   CG1  CD1  sing N N 201 
ILE   CG1  HG12 sing N N 202 
ILE   CG1  HG13 sing N N 203 
ILE   CG2  HG21 sing N N 204 
ILE   CG2  HG22 sing N N 205 
ILE   CG2  HG23 sing N N 206 
ILE   CD1  HD11 sing N N 207 
ILE   CD1  HD12 sing N N 208 
ILE   CD1  HD13 sing N N 209 
ILE   OXT  HXT  sing N N 210 
LEU   N    CA   sing N N 211 
LEU   N    H    sing N N 212 
LEU   N    H2   sing N N 213 
LEU   CA   C    sing N N 214 
LEU   CA   CB   sing N N 215 
LEU   CA   HA   sing N N 216 
LEU   C    O    doub N N 217 
LEU   C    OXT  sing N N 218 
LEU   CB   CG   sing N N 219 
LEU   CB   HB2  sing N N 220 
LEU   CB   HB3  sing N N 221 
LEU   CG   CD1  sing N N 222 
LEU   CG   CD2  sing N N 223 
LEU   CG   HG   sing N N 224 
LEU   CD1  HD11 sing N N 225 
LEU   CD1  HD12 sing N N 226 
LEU   CD1  HD13 sing N N 227 
LEU   CD2  HD21 sing N N 228 
LEU   CD2  HD22 sing N N 229 
LEU   CD2  HD23 sing N N 230 
LEU   OXT  HXT  sing N N 231 
LYS   N    CA   sing N N 232 
LYS   N    H    sing N N 233 
LYS   N    H2   sing N N 234 
LYS   CA   C    sing N N 235 
LYS   CA   CB   sing N N 236 
LYS   CA   HA   sing N N 237 
LYS   C    O    doub N N 238 
LYS   C    OXT  sing N N 239 
LYS   CB   CG   sing N N 240 
LYS   CB   HB2  sing N N 241 
LYS   CB   HB3  sing N N 242 
LYS   CG   CD   sing N N 243 
LYS   CG   HG2  sing N N 244 
LYS   CG   HG3  sing N N 245 
LYS   CD   CE   sing N N 246 
LYS   CD   HD2  sing N N 247 
LYS   CD   HD3  sing N N 248 
LYS   CE   NZ   sing N N 249 
LYS   CE   HE2  sing N N 250 
LYS   CE   HE3  sing N N 251 
LYS   NZ   HZ1  sing N N 252 
LYS   NZ   HZ2  sing N N 253 
LYS   NZ   HZ3  sing N N 254 
LYS   OXT  HXT  sing N N 255 
MET   N    CA   sing N N 256 
MET   N    H    sing N N 257 
MET   N    H2   sing N N 258 
MET   CA   C    sing N N 259 
MET   CA   CB   sing N N 260 
MET   CA   HA   sing N N 261 
MET   C    O    doub N N 262 
MET   C    OXT  sing N N 263 
MET   CB   CG   sing N N 264 
MET   CB   HB2  sing N N 265 
MET   CB   HB3  sing N N 266 
MET   CG   SD   sing N N 267 
MET   CG   HG2  sing N N 268 
MET   CG   HG3  sing N N 269 
MET   SD   CE   sing N N 270 
MET   CE   HE1  sing N N 271 
MET   CE   HE2  sing N N 272 
MET   CE   HE3  sing N N 273 
MET   OXT  HXT  sing N N 274 
NAP   PA   O1A  doub N N 275 
NAP   PA   O2A  sing N N 276 
NAP   PA   O5B  sing N N 277 
NAP   PA   O3   sing N N 278 
NAP   O2A  HOA2 sing N N 279 
NAP   O5B  C5B  sing N N 280 
NAP   C5B  C4B  sing N N 281 
NAP   C5B  H51A sing N N 282 
NAP   C5B  H52A sing N N 283 
NAP   C4B  O4B  sing N N 284 
NAP   C4B  C3B  sing N N 285 
NAP   C4B  H4B  sing N N 286 
NAP   O4B  C1B  sing N N 287 
NAP   C3B  O3B  sing N N 288 
NAP   C3B  C2B  sing N N 289 
NAP   C3B  H3B  sing N N 290 
NAP   O3B  HO3A sing N N 291 
NAP   C2B  O2B  sing N N 292 
NAP   C2B  C1B  sing N N 293 
NAP   C2B  H2B  sing N N 294 
NAP   O2B  P2B  sing N N 295 
NAP   C1B  N9A  sing N N 296 
NAP   C1B  H1B  sing N N 297 
NAP   N9A  C8A  sing Y N 298 
NAP   N9A  C4A  sing Y N 299 
NAP   C8A  N7A  doub Y N 300 
NAP   C8A  H8A  sing N N 301 
NAP   N7A  C5A  sing Y N 302 
NAP   C5A  C6A  sing Y N 303 
NAP   C5A  C4A  doub Y N 304 
NAP   C6A  N6A  sing N N 305 
NAP   C6A  N1A  doub Y N 306 
NAP   N6A  H61A sing N N 307 
NAP   N6A  H62A sing N N 308 
NAP   N1A  C2A  sing Y N 309 
NAP   C2A  N3A  doub Y N 310 
NAP   C2A  H2A  sing N N 311 
NAP   N3A  C4A  sing Y N 312 
NAP   O3   PN   sing N N 313 
NAP   PN   O1N  doub N N 314 
NAP   PN   O2N  sing N N 315 
NAP   PN   O5D  sing N N 316 
NAP   O5D  C5D  sing N N 317 
NAP   C5D  C4D  sing N N 318 
NAP   C5D  H51N sing N N 319 
NAP   C5D  H52N sing N N 320 
NAP   C4D  O4D  sing N N 321 
NAP   C4D  C3D  sing N N 322 
NAP   C4D  H4D  sing N N 323 
NAP   O4D  C1D  sing N N 324 
NAP   C3D  O3D  sing N N 325 
NAP   C3D  C2D  sing N N 326 
NAP   C3D  H3D  sing N N 327 
NAP   O3D  HO3N sing N N 328 
NAP   C2D  O2D  sing N N 329 
NAP   C2D  C1D  sing N N 330 
NAP   C2D  H2D  sing N N 331 
NAP   O2D  HO2N sing N N 332 
NAP   C1D  N1N  sing N N 333 
NAP   C1D  H1D  sing N N 334 
NAP   N1N  C2N  sing Y N 335 
NAP   N1N  C6N  doub Y N 336 
NAP   C2N  C3N  doub Y N 337 
NAP   C2N  H2N  sing N N 338 
NAP   C3N  C7N  sing N N 339 
NAP   C3N  C4N  sing Y N 340 
NAP   C7N  O7N  doub N N 341 
NAP   C7N  N7N  sing N N 342 
NAP   N7N  H71N sing N N 343 
NAP   N7N  H72N sing N N 344 
NAP   C4N  C5N  doub Y N 345 
NAP   C4N  H4N  sing N N 346 
NAP   C5N  C6N  sing Y N 347 
NAP   C5N  H5N  sing N N 348 
NAP   C6N  H6N  sing N N 349 
NAP   P2B  O1X  doub N N 350 
NAP   P2B  O2X  sing N N 351 
NAP   P2B  O3X  sing N N 352 
NAP   O2X  HOP2 sing N N 353 
NAP   O3X  HOP3 sing N N 354 
PHE   N    CA   sing N N 355 
PHE   N    H    sing N N 356 
PHE   N    H2   sing N N 357 
PHE   CA   C    sing N N 358 
PHE   CA   CB   sing N N 359 
PHE   CA   HA   sing N N 360 
PHE   C    O    doub N N 361 
PHE   C    OXT  sing N N 362 
PHE   CB   CG   sing N N 363 
PHE   CB   HB2  sing N N 364 
PHE   CB   HB3  sing N N 365 
PHE   CG   CD1  doub Y N 366 
PHE   CG   CD2  sing Y N 367 
PHE   CD1  CE1  sing Y N 368 
PHE   CD1  HD1  sing N N 369 
PHE   CD2  CE2  doub Y N 370 
PHE   CD2  HD2  sing N N 371 
PHE   CE1  CZ   doub Y N 372 
PHE   CE1  HE1  sing N N 373 
PHE   CE2  CZ   sing Y N 374 
PHE   CE2  HE2  sing N N 375 
PHE   CZ   HZ   sing N N 376 
PHE   OXT  HXT  sing N N 377 
PRO   N    CA   sing N N 378 
PRO   N    CD   sing N N 379 
PRO   N    H    sing N N 380 
PRO   CA   C    sing N N 381 
PRO   CA   CB   sing N N 382 
PRO   CA   HA   sing N N 383 
PRO   C    O    doub N N 384 
PRO   C    OXT  sing N N 385 
PRO   CB   CG   sing N N 386 
PRO   CB   HB2  sing N N 387 
PRO   CB   HB3  sing N N 388 
PRO   CG   CD   sing N N 389 
PRO   CG   HG2  sing N N 390 
PRO   CG   HG3  sing N N 391 
PRO   CD   HD2  sing N N 392 
PRO   CD   HD3  sing N N 393 
PRO   OXT  HXT  sing N N 394 
SER   N    CA   sing N N 395 
SER   N    H    sing N N 396 
SER   N    H2   sing N N 397 
SER   CA   C    sing N N 398 
SER   CA   CB   sing N N 399 
SER   CA   HA   sing N N 400 
SER   C    O    doub N N 401 
SER   C    OXT  sing N N 402 
SER   CB   OG   sing N N 403 
SER   CB   HB2  sing N N 404 
SER   CB   HB3  sing N N 405 
SER   OG   HG   sing N N 406 
SER   OXT  HXT  sing N N 407 
THR   N    CA   sing N N 408 
THR   N    H    sing N N 409 
THR   N    H2   sing N N 410 
THR   CA   C    sing N N 411 
THR   CA   CB   sing N N 412 
THR   CA   HA   sing N N 413 
THR   C    O    doub N N 414 
THR   C    OXT  sing N N 415 
THR   CB   OG1  sing N N 416 
THR   CB   CG2  sing N N 417 
THR   CB   HB   sing N N 418 
THR   OG1  HG1  sing N N 419 
THR   CG2  HG21 sing N N 420 
THR   CG2  HG22 sing N N 421 
THR   CG2  HG23 sing N N 422 
THR   OXT  HXT  sing N N 423 
TRP   N    CA   sing N N 424 
TRP   N    H    sing N N 425 
TRP   N    H2   sing N N 426 
TRP   CA   C    sing N N 427 
TRP   CA   CB   sing N N 428 
TRP   CA   HA   sing N N 429 
TRP   C    O    doub N N 430 
TRP   C    OXT  sing N N 431 
TRP   CB   CG   sing N N 432 
TRP   CB   HB2  sing N N 433 
TRP   CB   HB3  sing N N 434 
TRP   CG   CD1  doub Y N 435 
TRP   CG   CD2  sing Y N 436 
TRP   CD1  NE1  sing Y N 437 
TRP   CD1  HD1  sing N N 438 
TRP   CD2  CE2  doub Y N 439 
TRP   CD2  CE3  sing Y N 440 
TRP   NE1  CE2  sing Y N 441 
TRP   NE1  HE1  sing N N 442 
TRP   CE2  CZ2  sing Y N 443 
TRP   CE3  CZ3  doub Y N 444 
TRP   CE3  HE3  sing N N 445 
TRP   CZ2  CH2  doub Y N 446 
TRP   CZ2  HZ2  sing N N 447 
TRP   CZ3  CH2  sing Y N 448 
TRP   CZ3  HZ3  sing N N 449 
TRP   CH2  HH2  sing N N 450 
TRP   OXT  HXT  sing N N 451 
TYR   N    CA   sing N N 452 
TYR   N    H    sing N N 453 
TYR   N    H2   sing N N 454 
TYR   CA   C    sing N N 455 
TYR   CA   CB   sing N N 456 
TYR   CA   HA   sing N N 457 
TYR   C    O    doub N N 458 
TYR   C    OXT  sing N N 459 
TYR   CB   CG   sing N N 460 
TYR   CB   HB2  sing N N 461 
TYR   CB   HB3  sing N N 462 
TYR   CG   CD1  doub Y N 463 
TYR   CG   CD2  sing Y N 464 
TYR   CD1  CE1  sing Y N 465 
TYR   CD1  HD1  sing N N 466 
TYR   CD2  CE2  doub Y N 467 
TYR   CD2  HD2  sing N N 468 
TYR   CE1  CZ   doub Y N 469 
TYR   CE1  HE1  sing N N 470 
TYR   CE2  CZ   sing Y N 471 
TYR   CE2  HE2  sing N N 472 
TYR   CZ   OH   sing N N 473 
TYR   OH   HH   sing N N 474 
TYR   OXT  HXT  sing N N 475 
VAL   N    CA   sing N N 476 
VAL   N    H    sing N N 477 
VAL   N    H2   sing N N 478 
VAL   CA   C    sing N N 479 
VAL   CA   CB   sing N N 480 
VAL   CA   HA   sing N N 481 
VAL   C    O    doub N N 482 
VAL   C    OXT  sing N N 483 
VAL   CB   CG1  sing N N 484 
VAL   CB   CG2  sing N N 485 
VAL   CB   HB   sing N N 486 
VAL   CG1  HG11 sing N N 487 
VAL   CG1  HG12 sing N N 488 
VAL   CG1  HG13 sing N N 489 
VAL   CG2  HG21 sing N N 490 
VAL   CG2  HG22 sing N N 491 
VAL   CG2  HG23 sing N N 492 
VAL   OXT  HXT  sing N N 493 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)' 'United States' HL153144 1 
'National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)' 'United States' HL150927 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          9C16 
# 
_pdbx_related_exp_data_set.data_reference       10.5281/zenodo.11406111 
_pdbx_related_exp_data_set.data_set_type        'diffraction image data' 
_pdbx_related_exp_data_set.details              ? 
_pdbx_related_exp_data_set.metadata_reference   ? 
_pdbx_related_exp_data_set.ordinal              1 
# 
_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                    9C17 
_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]   0.013154 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004297 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.023732 
_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]   0.015903 
_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.
;
? 
CL  ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 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.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P   ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . ALA   A 1 6   ? 17.94200 -14.22800 26.60900 1.000 39.44000 ?  2   ALA   A N    1 
ATOM   2    C  CA   . ALA   A 1 6   ? 18.28000 -12.85300 26.27000 1.000 40.92000 ?  2   ALA   A CA   1 
ATOM   3    C  C    . ALA   A 1 6   ? 18.23600 -12.63800 24.75900 1.000 39.06000 ?  2   ALA   A C    1 
ATOM   4    O  O    . ALA   A 1 6   ? 18.15600 -13.58400 23.97300 1.000 37.23000 ?  2   ALA   A O    1 
ATOM   5    C  CB   . ALA   A 1 6   ? 19.66100 -12.48100 26.82600 1.000 33.52000 ?  2   ALA   A CB   1 
ATOM   6    N  N    . VAL   A 1 7   ? 18.28900 -11.38100 24.36100 1.000 35.54000 ?  3   VAL   A N    1 
ATOM   7    C  CA   . VAL   A 1 7   ? 18.24000 -11.00400 22.95600 1.000 28.53000 ?  3   VAL   A CA   1 
ATOM   8    C  C    . VAL   A 1 7   ? 19.65300 -11.06100 22.39000 1.000 28.31000 ?  3   VAL   A C    1 
ATOM   9    O  O    . VAL   A 1 7   ? 20.57200 -10.44000 22.93400 1.000 28.40000 ?  3   VAL   A O    1 
ATOM   10   C  CB   . VAL   A 1 7   ? 17.62700 -9.60400  22.79700 1.000 26.37000 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  . VAL   A 1 7   ? 17.83900 -9.08400  21.37900 1.000 24.27000 ?  3   VAL   A CG1  1 
ATOM   12   C  CG2  . VAL   A 1 7   ? 16.14500 -9.64400  23.13300 1.000 31.27000 ?  3   VAL   A CG2  1 
ATOM   13   N  N    . LYS   A 1 8   ? 19.83500 -11.81600 21.30600 1.000 25.55000 ?  4   LYS   A N    1 
ATOM   14   C  CA   . LYS   A 1 8   ? 21.15500 -11.98900 20.70800 1.000 24.26000 ?  4   LYS   A CA   1 
ATOM   15   C  C    . LYS   A 1 8   ? 21.21400 -11.53300 19.25900 1.000 21.19000 ?  4   LYS   A C    1 
ATOM   16   O  O    . LYS   A 1 8   ? 22.16000 -10.83400 18.87300 1.000 19.71000 ?  4   LYS   A O    1 
ATOM   17   C  CB   . LYS   A 1 8   ? 21.59000 -13.46300 20.80700 1.000 26.93000 ?  4   LYS   A CB   1 
ATOM   18   N  N    . LYS   A 1 9   ? 20.23400 -11.92400 18.44500 1.000 19.82000 ?  5   LYS   A N    1 
ATOM   19   C  CA   . LYS   A 1 9   ? 20.17400 -11.55800 17.04000 1.000 16.41000 ?  5   LYS   A CA   1 
ATOM   20   C  C    . LYS   A 1 9   ? 19.13200 -10.46600 16.84300 1.000 18.43000 ?  5   LYS   A C    1 
ATOM   21   O  O    . LYS   A 1 9   ? 17.97500 -10.62100 17.25300 1.000 16.57000 ?  5   LYS   A O    1 
ATOM   22   C  CB   . LYS   A 1 9   ? 19.84300 -12.77400 16.17600 1.000 18.74000 ?  5   LYS   A CB   1 
ATOM   23   C  CG   . LYS   A 1 9   ? 20.90300 -13.86400 16.24700 1.000 23.67000 ?  5   LYS   A CG   1 
ATOM   24   C  CD   . LYS   A 1 9   ? 20.47700 -15.10800 15.47800 1.000 31.89000 ?  5   LYS   A CD   1 
ATOM   25   C  CE   . LYS   A 1 9   ? 21.38800 -16.28300 15.80900 1.000 42.57000 ?  5   LYS   A CE   1 
ATOM   26   N  NZ   . LYS   A 1 9   ? 20.92700 -17.56100 15.19900 1.000 44.90000 ?  5   LYS   A NZ   1 
ATOM   27   N  N    . ILE   A 1 10  ? 19.54000 -9.35600  16.23300 1.000 16.01000 ?  6   ILE   A N    1 
ATOM   28   C  CA   . ILE   A 1 10  ? 18.61500 -8.26000  15.97900 1.000 13.41000 ?  6   ILE   A CA   1 
ATOM   29   C  C    . ILE   A 1 10  ? 18.73700 -7.81100  14.53300 1.000 14.38000 ?  6   ILE   A C    1 
ATOM   30   O  O    . ILE   A 1 10  ? 19.80900 -7.89400  13.92200 1.000 16.80000 ?  6   ILE   A O    1 
ATOM   31   C  CB   . ILE   A 1 10  ? 18.83800 -7.05900  16.92900 1.000 16.73000 ?  6   ILE   A CB   1 
ATOM   32   C  CG1  . ILE   A 1 10  ? 20.20900 -6.42200  16.72600 1.000 13.85000 ?  6   ILE   A CG1  1 
ATOM   33   C  CG2  . ILE   A 1 10  ? 18.67700 -7.48300  18.37300 1.000 17.12000 ?  6   ILE   A CG2  1 
ATOM   34   C  CD1  . ILE   A 1 10  ? 20.42100 -5.12300  17.54600 1.000 14.80000 ?  6   ILE   A CD1  1 
ATOM   35   N  N    . ALA   A 1 11  ? 17.61000 -7.36800  13.97800 1.000 12.99000 ?  7   ALA   A N    1 
ATOM   36   C  CA   . ALA   A 1 11  ? 17.58300 -6.62600  12.72500 1.000 12.51000 ?  7   ALA   A CA   1 
ATOM   37   C  C    . ALA   A 1 11  ? 17.42100 -5.14500  13.04000 1.000 12.27000 ?  7   ALA   A C    1 
ATOM   38   O  O    . ALA   A 1 11  ? 16.65400 -4.77800  13.92900 1.000 14.84000 ?  7   ALA   A O    1 
ATOM   39   C  CB   . ALA   A 1 11  ? 16.43600 -7.09900  11.82500 1.000 15.19000 ?  7   ALA   A CB   1 
ATOM   40   N  N    . ILE   A 1 12  ? 18.16500 -4.29700  12.32800 1.000 13.07000 ?  8   ILE   A N    1 
ATOM   41   C  CA   . ILE   A 1 12  ? 18.03100 -2.84400  12.45200 1.000 13.21000 ?  8   ILE   A CA   1 
ATOM   42   C  C    . ILE   A 1 12  ? 17.61000 -2.30400  11.09500 1.000 15.26000 ?  8   ILE   A C    1 
ATOM   43   O  O    . ILE   A 1 12  ? 18.29600 -2.53800  10.09400 1.000 14.52000 ?  8   ILE   A O    1 
ATOM   44   C  CB   . ILE   A 1 12  ? 19.33500 -2.16900  12.90700 1.000 12.58000 ?  8   ILE   A CB   1 
ATOM   45   C  CG1  . ILE   A 1 12  ? 19.80800 -2.72200  14.25100 1.000 13.14000 ?  8   ILE   A CG1  1 
ATOM   46   C  CG2  . ILE   A 1 12  ? 19.15100 -0.64400  12.99100 1.000 11.69000 ?  8   ILE   A CG2  1 
ATOM   47   C  CD1  . ILE   A 1 12  ? 21.16500 -2.17200  14.67200 1.000 12.56000 ?  8   ILE   A CD1  1 
ATOM   48   N  N    . PHE   A 1 13  ? 16.48400 -1.59900  11.05900 1.000 12.52000 ?  9   PHE   A N    1 
ATOM   49   C  CA   . PHE   A 1 13  ? 16.06300 -0.85400  9.88000  1.000 11.18000 ?  9   PHE   A CA   1 
ATOM   50   C  C    . PHE   A 1 13  ? 16.43900 0.61800   10.05300 1.000 14.45000 ?  9   PHE   A C    1 
ATOM   51   O  O    . PHE   A 1 13  ? 16.26400 1.19800   11.13000 1.000 13.77000 ?  9   PHE   A O    1 
ATOM   52   C  CB   . PHE   A 1 13  ? 14.55200 -1.01400  9.65200  1.000 12.12000 ?  9   PHE   A CB   1 
ATOM   53   C  CG   . PHE   A 1 13  ? 14.14500 -2.43200  9.30900  1.000 13.57000 ?  9   PHE   A CG   1 
ATOM   54   C  CD1  . PHE   A 1 13  ? 13.87100 -3.34900  10.31200 1.000 12.08000 ?  9   PHE   A CD1  1 
ATOM   55   C  CD2  . PHE   A 1 13  ? 14.09500 -2.85500  7.98700  1.000 13.11000 ?  9   PHE   A CD2  1 
ATOM   56   C  CE1  . PHE   A 1 13  ? 13.51100 -4.65000  10.00000 1.000 13.81000 ?  9   PHE   A CE1  1 
ATOM   57   C  CE2  . PHE   A 1 13  ? 13.74300 -4.15700  7.67500  1.000 13.81000 ?  9   PHE   A CE2  1 
ATOM   58   C  CZ   . PHE   A 1 13  ? 13.45700 -5.05000  8.68000  1.000 13.67000 ?  9   PHE   A CZ   1 
ATOM   59   N  N    . GLY   A 1 14  ? 16.96600 1.22400   8.99200  1.000 12.09000 ?  10  GLY   A N    1 
ATOM   60   C  CA   . GLY   A 1 14  ? 17.47200 2.57200   9.13700  1.000 14.48000 ?  10  GLY   A CA   1 
ATOM   61   C  C    . GLY   A 1 14  ? 18.86700 2.64200   9.71600  1.000 13.45000 ?  10  GLY   A C    1 
ATOM   62   O  O    . GLY   A 1 14  ? 19.24800 3.67700   10.25900 1.000 13.00000 ?  10  GLY   A O    1 
ATOM   63   N  N    . ALA   A 1 15  ? 19.65700 1.57400   9.58300  1.000 13.12000 ?  11  ALA   A N    1 
ATOM   64   C  CA   . ALA   A 1 15  ? 20.99400 1.54000   10.16900 1.000 14.66000 ?  11  ALA   A CA   1 
ATOM   65   C  C    . ALA   A 1 15  ? 21.95500 2.53700   9.52900  1.000 13.47000 ?  11  ALA   A C    1 
ATOM   66   O  O    . ALA   A 1 15  ? 22.96100 2.88200   10.15100 1.000 14.90000 ?  11  ALA   A O    1 
ATOM   67   C  CB   . ALA   A 1 15  ? 21.57600 0.12900   10.06600 1.000 15.92000 ?  11  ALA   A CB   1 
ATOM   68   N  N    . THR   A 1 16  ? 21.68600 3.01800   8.31300  1.000 14.30000 ?  12  THR   A N    1 
ATOM   69   C  CA   . THR   A 1 16  ? 22.62000 3.95700   7.70200  1.000 14.52000 ?  12  THR   A CA   1 
ATOM   70   C  C    . THR   A 1 16  ? 22.30400 5.41500   8.01600  1.000 12.41000 ?  12  THR   A C    1 
ATOM   71   O  O    . THR   A 1 16  ? 23.04300 6.30200   7.57100  1.000 13.32000 ?  12  THR   A O    1 
ATOM   72   C  CB   . THR   A 1 16  ? 22.66100 3.76800   6.18200  1.000 17.32000 ?  12  THR   A CB   1 
ATOM   73   O  OG1  . THR   A 1 16  ? 21.33500 3.86600   5.65800  1.000 17.42000 ?  12  THR   A OG1  1 
ATOM   74   C  CG2  . THR   A 1 16  ? 23.25300 2.40800   5.83400  1.000 17.71000 ?  12  THR   A CG2  1 
ATOM   75   N  N    . GLY   A 1 17  ? 21.25000 5.68700   8.78300  1.000 13.19000 ?  13  GLY   A N    1 
ATOM   76   C  CA   . GLY   A 1 17  ? 20.83500 7.04900   9.06500  1.000 14.44000 ?  13  GLY   A CA   1 
ATOM   77   C  C    . GLY   A 1 17  ? 21.58200 7.65100   10.23900 1.000 15.90000 ?  13  GLY   A C    1 
ATOM   78   O  O    . GLY   A 1 17  ? 22.51000 7.06400   10.79600 1.000 15.26000 ?  13  GLY   A O    1 
ATOM   79   N  N    . GLN   A 1 18  ? 21.16400 8.86900   10.61300 1.000 14.49000 ?  14  GLN   A N    1 
ATOM   80   C  CA   . GLN   A 1 18  ? 21.85000 9.60000   11.67600 1.000 16.14000 ?  14  GLN   A CA   1 
ATOM   81   C  C    . GLN   A 1 18  ? 21.90700 8.78900   12.97100 1.000 15.30000 ?  14  GLN   A C    1 
ATOM   82   O  O    . GLN   A 1 18  ? 22.98900 8.56800   13.53700 1.000 12.89000 ?  14  GLN   A O    1 
ATOM   83   C  CB   . GLN   A 1 18  ? 21.15400 10.94700  11.90000 1.000 16.21000 ?  14  GLN   A CB   1 
ATOM   84   C  CG   . GLN   A 1 18  ? 21.62000 11.70400  13.12900 1.000 18.40000 ?  14  GLN   A CG   1 
ATOM   85   C  CD   . GLN   A 1 18  ? 20.92700 13.04900  13.31200 1.000 18.67000 ?  14  GLN   A CD   1 
ATOM   86   O  OE1  . GLN   A 1 18  ? 21.57600 14.03100  13.66600 1.000 21.43000 ?  14  GLN   A OE1  1 
ATOM   87   N  NE2  . GLN   A 1 18  ? 19.60100 13.09500  13.10000 1.000 16.50000 ?  14  GLN   A NE2  1 
ATOM   88   N  N    . THR   A 1 19  ? 20.75000 8.34700   13.46700 1.000 11.66000 ?  15  THR   A N    1 
ATOM   89   C  CA   . THR   A 1 19  ? 20.73000 7.53100   14.67900 1.000 12.38000 ?  15  THR   A CA   1 
ATOM   90   C  C    . THR   A 1 19  ? 21.13000 6.09600   14.39000 1.000 14.09000 ?  15  THR   A C    1 
ATOM   91   O  O    . THR   A 1 19  ? 21.77600 5.45200   15.22300 1.000 12.54000 ?  15  THR   A O    1 
ATOM   92   C  CB   . THR   A 1 19  ? 19.33800 7.56800   15.32100 1.000 13.67000 ?  15  THR   A CB   1 
ATOM   93   O  OG1  . THR   A 1 19  ? 18.91700 8.92500   15.43900 1.000 12.28000 ?  15  THR   A OG1  1 
ATOM   94   C  CG2  . THR   A 1 19  ? 19.34700 6.94700   16.72500 1.000 11.48000 ?  15  THR   A CG2  1 
ATOM   95   N  N    . GLY   A 1 20  ? 20.76600 5.58800   13.21500 1.000 11.41000 ?  16  GLY   A N    1 
ATOM   96   C  CA   . GLY   A 1 20  ? 21.06000 4.20000   12.90000 1.000 13.46000 ?  16  GLY   A CA   1 
ATOM   97   C  C    . GLY   A 1 20  ? 22.54000 3.86200   12.97000 1.000 13.17000 ?  16  GLY   A C    1 
ATOM   98   O  O    . GLY   A 1 20  ? 22.91600 2.79000   13.44500 1.000 13.51000 ?  16  GLY   A O    1 
ATOM   99   N  N    . LEU   A 1 21  ? 23.39400 4.75900   12.48200 1.000 12.93000 ?  17  LEU   A N    1 
ATOM   100  C  CA   . LEU   A 1 21  ? 24.81900 4.44200   12.39000 1.000 15.06000 ?  17  LEU   A CA   1 
ATOM   101  C  C    . LEU   A 1 21  ? 25.42600 4.22800   13.76700 1.000 13.19000 ?  17  LEU   A C    1 
ATOM   102  O  O    . LEU   A 1 21  ? 26.18000 3.26500   13.97600 1.000 16.14000 ?  17  LEU   A O    1 
ATOM   103  C  CB   . LEU   A 1 21  ? 25.55100 5.55200   11.65300 1.000 14.73000 ?  17  LEU   A CB   1 
ATOM   104  C  CG   . LEU   A 1 21  ? 25.42400 5.52200   10.13800 1.000 14.19000 ?  17  LEU   A CG   1 
ATOM   105  C  CD1  . LEU   A 1 21  ? 26.03600 6.80700   9.57200  1.000 15.11000 ?  17  LEU   A CD1  1 
ATOM   106  C  CD2  . LEU   A 1 21  ? 26.11100 4.29000   9.52000  1.000 15.45000 ?  17  LEU   A CD2  1 
ATOM   107  N  N    . THR   A 1 22  ? 25.08600 5.09300   14.72300 1.000 14.55000 ?  18  THR   A N    1 
ATOM   108  C  CA   . THR   A 1 22  ? 25.60100 4.92000   16.07500 1.000 13.17000 ?  18  THR   A CA   1 
ATOM   109  C  C    . THR   A 1 22  ? 24.90300 3.78000   16.80800 1.000 13.23000 ?  18  THR   A C    1 
ATOM   110  O  O    . THR   A 1 22  ? 25.54200 3.08500   17.60300 1.000 13.90000 ?  18  THR   A O    1 
ATOM   111  C  CB   . THR   A 1 22  ? 25.49800 6.24000   16.86300 1.000 15.69000 ?  18  THR   A CB   1 
ATOM   112  O  OG1  . THR   A 1 22  ? 26.02500 6.06300   18.18500 1.000 13.91000 ?  18  THR   A OG1  1 
ATOM   113  C  CG2  . THR   A 1 22  ? 24.06800 6.74700   16.95100 1.000 15.24000 ?  18  THR   A CG2  1 
ATOM   114  N  N    . THR   A 1 23  ? 23.61200 3.55200   16.54900 1.000 13.44000 ?  19  THR   A N    1 
ATOM   115  C  CA   . THR   A 1 23  ? 22.95100 2.36900   17.09300 1.000 12.51000 ?  19  THR   A CA   1 
ATOM   116  C  C    . THR   A 1 23  ? 23.63000 1.09600   16.60800 1.000 14.45000 ?  19  THR   A C    1 
ATOM   117  O  O    . THR   A 1 23  ? 23.84300 0.14900   17.38000 1.000 12.21000 ?  19  THR   A O    1 
ATOM   118  C  CB   . THR   A 1 23  ? 21.47400 2.37000   16.69400 1.000 15.61000 ?  19  THR   A CB   1 
ATOM   119  O  OG1  . THR   A 1 23  ? 20.85900 3.57800   17.16600 1.000 11.05000 ?  19  THR   A OG1  1 
ATOM   120  C  CG2  . THR   A 1 23  ? 20.74700 1.16000   17.29700 1.000 13.45000 ?  19  THR   A CG2  1 
ATOM   121  N  N    . LEU   A 1 24  ? 23.97100 1.05800   15.32400 1.000 13.40000 ?  20  LEU   A N    1 
ATOM   122  C  CA   . LEU   A 1 24  ? 24.66700 -0.09300  14.76300 1.000 14.63000 ?  20  LEU   A CA   1 
ATOM   123  C  C    . LEU   A 1 24  ? 26.00500 -0.31500  15.45600 1.000 15.87000 ?  20  LEU   A C    1 
ATOM   124  O  O    . LEU   A 1 24  ? 26.33500 -1.44300  15.85500 1.000 14.59000 ?  20  LEU   A O    1 
ATOM   125  C  CB   . LEU   A 1 24  ? 24.85200 0.12700   13.26300 1.000 13.32000 ?  20  LEU   A CB   1 
ATOM   126  C  CG   . LEU   A 1 24  ? 25.81900 -0.77500  12.50500 1.000 17.79000 ?  20  LEU   A CG   1 
ATOM   127  C  CD1  . LEU   A 1 24  ? 25.38100 -2.21500  12.60700 1.000 14.16000 ?  20  LEU   A CD1  1 
ATOM   128  C  CD2  . LEU   A 1 24  ? 25.88200 -0.31700  11.04200 1.000 17.56000 ?  20  LEU   A CD2  1 
ATOM   129  N  N    . ALA   A 1 25  ? 26.79300 0.75900   15.60100 1.000 14.67000 ?  21  ALA   A N    1 
ATOM   130  C  CA   . ALA   A 1 25  ? 28.10900 0.64200   16.22700 1.000 13.03000 ?  21  ALA   A CA   1 
ATOM   131  C  C    . ALA   A 1 25  ? 27.99000 0.18100   17.67500 1.000 18.73000 ?  21  ALA   A C    1 
ATOM   132  O  O    . ALA   A 1 25  ? 28.72800 -0.71200  18.11400 1.000 17.48000 ?  21  ALA   A O    1 
ATOM   133  C  CB   . ALA   A 1 25  ? 28.85200 1.97500   16.14800 1.000 15.18000 ?  21  ALA   A CB   1 
ATOM   134  N  N    . GLN   A 1 26  ? 27.04600 0.75600   18.42800 1.000 15.61000 ?  22  GLN   A N    1 
ATOM   135  C  CA   . GLN   A 1 26  ? 26.87500 0.34100   19.82300 1.000 13.15000 ?  22  GLN   A CA   1 
ATOM   136  C  C    . GLN   A 1 26  ? 26.36500 -1.09300  19.93700 1.000 17.61000 ?  22  GLN   A C    1 
ATOM   137  O  O    . GLN   A 1 26  ? 26.71900 -1.80800  20.88400 1.000 17.14000 ?  22  GLN   A O    1 
ATOM   138  C  CB   . GLN   A 1 26  ? 25.92800 1.30400   20.53900 1.000 16.07000 ?  22  GLN   A CB   1 
ATOM   139  C  CG   . GLN   A 1 26  ? 26.44700 2.73000   20.62100 1.000 16.36000 ?  22  GLN   A CG   1 
ATOM   140  C  CD   . GLN   A 1 26  ? 25.48300 3.65600   21.34000 1.000 16.08000 ?  22  GLN   A CD   1 
ATOM   141  O  OE1  . GLN   A 1 26  ? 25.13700 3.42300   22.50200 1.000 17.38000 ?  22  GLN   A OE1  1 
ATOM   142  N  NE2  . GLN   A 1 26  ? 25.02900 4.70000   20.64900 1.000 14.43000 ?  22  GLN   A NE2  1 
ATOM   143  N  N    . ALA   A 1 27  ? 25.53100 -1.53300  19.00000 1.000 14.09000 ?  23  ALA   A N    1 
ATOM   144  C  CA   . ALA   A 1 27  ? 25.01400 -2.89400  19.06100 1.000 15.52000 ?  23  ALA   A CA   1 
ATOM   145  C  C    . ALA   A 1 27  ? 26.13000 -3.90900  18.86300 1.000 18.60000 ?  23  ALA   A C    1 
ATOM   146  O  O    . ALA   A 1 27  ? 26.20800 -4.91300  19.58300 1.000 16.87000 ?  23  ALA   A O    1 
ATOM   147  C  CB   . ALA   A 1 27  ? 23.92700 -3.08200  18.00600 1.000 14.79000 ?  23  ALA   A CB   1 
ATOM   148  N  N    . VAL   A 1 28  ? 26.99000 -3.66300  17.87800 1.000 16.01000 ?  24  VAL   A N    1 
ATOM   149  C  CA   . VAL   A 1 28  ? 28.13700 -4.53100  17.63000 1.000 18.91000 ?  24  VAL   A CA   1 
ATOM   150  C  C    . VAL   A 1 28  ? 29.09600 -4.50300  18.81300 1.000 18.68000 ?  24  VAL   A C    1 
ATOM   151  O  O    . VAL   A 1 28  ? 29.58100 -5.55000  19.25700 1.000 20.07000 ?  24  VAL   A O    1 
ATOM   152  C  CB   . VAL   A 1 28  ? 28.82100 -4.11400  16.31500 1.000 20.00000 ?  24  VAL   A CB   1 
ATOM   153  C  CG1  . VAL   A 1 28  ? 30.14400 -4.84400  16.13500 1.000 20.49000 ?  24  VAL   A CG1  1 
ATOM   154  C  CG2  . VAL   A 1 28  ? 27.88400 -4.37400  15.13700 1.000 16.30000 ?  24  VAL   A CG2  1 
ATOM   155  N  N    . GLN   A 1 29  ? 29.36100 -3.31500  19.36100 1.000 16.31000 ?  25  GLN   A N    1 
ATOM   156  C  CA   . GLN   A 1 29  ? 30.19100 -3.21000  20.56500 1.000 19.20000 ?  25  GLN   A CA   1 
ATOM   157  C  C    . GLN   A 1 29  ? 29.64900 -4.06300  21.70500 1.000 23.01000 ?  25  GLN   A C    1 
ATOM   158  O  O    . GLN   A 1 29  ? 30.42300 -4.63500  22.48800 1.000 20.21000 ?  25  GLN   A O    1 
ATOM   159  C  CB   . GLN   A 1 29  ? 30.26500 -1.76300  21.03800 1.000 20.27000 ?  25  GLN   A CB   1 
ATOM   160  C  CG   . GLN   A 1 29  ? 31.18000 -0.85400  20.28500 1.000 23.58000 ?  25  GLN   A CG   1 
ATOM   161  C  CD   . GLN   A 1 29  ? 31.19100 0.53100   20.89900 1.000 28.36000 ?  25  GLN   A CD   1 
ATOM   162  O  OE1  . GLN   A 1 29  ? 30.13900 1.16600   21.04700 1.000 28.39000 ?  25  GLN   A OE1  1 
ATOM   163  N  NE2  . GLN   A 1 29  ? 32.37400 0.99800   21.29400 1.000 26.06000 ?  25  GLN   A NE2  1 
ATOM   164  N  N    . ALA   A 1 30  ? 28.32400 -4.11500  21.85400 1.000 18.66000 ?  26  ALA   A N    1 
ATOM   165  C  CA   . ALA   A 1 30  ? 27.71300 -4.84500  22.95600 1.000 19.93000 ?  26  ALA   A CA   1 
ATOM   166  C  C    . ALA   A 1 30  ? 27.64300 -6.34300  22.70800 1.000 19.84000 ?  26  ALA   A C    1 
ATOM   167  O  O    . ALA   A 1 30  ? 27.27400 -7.08800  23.62200 1.000 23.15000 ?  26  ALA   A O    1 
ATOM   168  C  CB   . ALA   A 1 30  ? 26.30400 -4.30900  23.24200 1.000 18.75000 ?  26  ALA   A CB   1 
ATOM   169  N  N    . GLY   A 1 31  ? 27.97200 -6.80500  21.50800 1.000 17.40000 ?  27  GLY   A N    1 
ATOM   170  C  CA   . GLY   A 1 31  ? 27.99700 -8.22300  21.22500 1.000 18.04000 ?  27  GLY   A CA   1 
ATOM   171  C  C    . GLY   A 1 31  ? 26.79000 -8.76800  20.50000 1.000 18.23000 ?  27  GLY   A C    1 
ATOM   172  O  O    . GLY   A 1 31  ? 26.65700 -9.99100  20.39300 1.000 21.61000 ?  27  GLY   A O    1 
ATOM   173  N  N    . TYR   A 1 32  ? 25.90200 -7.91300  20.00500 1.000 15.58000 ?  28  TYR   A N    1 
ATOM   174  C  CA   . TYR   A 1 32  ? 24.76900 -8.41300  19.25000 1.000 16.61000 ?  28  TYR   A CA   1 
ATOM   175  C  C    . TYR   A 1 32  ? 25.22100 -8.92300  17.89200 1.000 15.03000 ?  28  TYR   A C    1 
ATOM   176  O  O    . TYR   A 1 32  ? 26.18000 -8.42000  17.30400 1.000 19.75000 ?  28  TYR   A O    1 
ATOM   177  C  CB   . TYR   A 1 32  ? 23.71400 -7.31900  19.06700 1.000 16.32000 ?  28  TYR   A CB   1 
ATOM   178  C  CG   . TYR   A 1 32  ? 22.96300 -6.96600  20.33700 1.000 19.35000 ?  28  TYR   A CG   1 
ATOM   179  C  CD1  . TYR   A 1 32  ? 21.86800 -7.71900  20.75500 1.000 20.35000 ?  28  TYR   A CD1  1 
ATOM   180  C  CD2  . TYR   A 1 32  ? 23.34400 -5.87800  21.10600 1.000 18.22000 ?  28  TYR   A CD2  1 
ATOM   181  C  CE1  . TYR   A 1 32  ? 21.18000 -7.39700  21.91400 1.000 21.82000 ?  28  TYR   A CE1  1 
ATOM   182  C  CE2  . TYR   A 1 32  ? 22.66700 -5.55300  22.26300 1.000 18.07000 ?  28  TYR   A CE2  1 
ATOM   183  C  CZ   . TYR   A 1 32  ? 21.59100 -6.30900  22.66100 1.000 22.95000 ?  28  TYR   A CZ   1 
ATOM   184  O  OH   . TYR   A 1 32  ? 20.93500 -5.95000  23.81900 1.000 24.36000 ?  28  TYR   A OH   1 
ATOM   185  N  N    . GLU   A 1 33  ? 24.51800 -9.93300  17.39500 1.000 16.06000 ?  29  GLU   A N    1 
ATOM   186  C  CA   . GLU   A 1 33  ? 24.64700 -10.36100 16.00600 1.000 17.42000 ?  29  GLU   A CA   1 
ATOM   187  C  C    . GLU   A 1 33  ? 23.62200 -9.55700  15.21600 1.000 16.98000 ?  29  GLU   A C    1 
ATOM   188  O  O    . GLU   A 1 33  ? 22.41100 -9.79000  15.33900 1.000 16.82000 ?  29  GLU   A O    1 
ATOM   189  C  CB   . GLU   A 1 33  ? 24.42500 -11.86500 15.87400 1.000 16.40000 ?  29  GLU   A CB   1 
ATOM   190  C  CG   . GLU   A 1 33  ? 24.55800 -12.40200 14.45400 1.000 17.87000 ?  29  GLU   A CG   1 
ATOM   191  C  CD   . GLU   A 1 33  ? 24.35500 -13.91100 14.37300 1.000 25.79000 ?  29  GLU   A CD   1 
ATOM   192  O  OE1  . GLU   A 1 33  ? 24.37000 -14.58200 15.42900 1.000 26.41000 ?  29  GLU   A OE1  1 
ATOM   193  O  OE2  . GLU   A 1 33  ? 24.17500 -14.42800 13.24900 1.000 26.62000 ?  29  GLU   A OE2  1 
ATOM   194  N  N    . VAL   A 1 34  ? 24.10300 -8.57700  14.45300 1.000 17.31000 ?  30  VAL   A N    1 
ATOM   195  C  CA   . VAL   A 1 34  ? 23.25500 -7.55800  13.84100 1.000 15.42000 ?  30  VAL   A CA   1 
ATOM   196  C  C    . VAL   A 1 34  ? 23.08100 -7.84800  12.35800 1.000 16.49000 ?  30  VAL   A C    1 
ATOM   197  O  O    . VAL   A 1 34  ? 24.06200 -8.05100  11.63000 1.000 17.96000 ?  30  VAL   A O    1 
ATOM   198  C  CB   . VAL   A 1 34  ? 23.84100 -6.15000  14.04100 1.000 16.49000 ?  30  VAL   A CB   1 
ATOM   199  C  CG1  . VAL   A 1 34  ? 22.94500 -5.09800  13.37300 1.000 14.67000 ?  30  VAL   A CG1  1 
ATOM   200  C  CG2  . VAL   A 1 34  ? 24.05600 -5.85500  15.54500 1.000 15.93000 ?  30  VAL   A CG2  1 
ATOM   201  N  N    . THR   A 1 35  ? 21.83300 -7.82900  11.91100 1.000 12.96000 ?  31  THR   A N    1 
ATOM   202  C  CA   . THR   A 1 35  ? 21.46500 -7.84100  10.50400 1.000 16.45000 ?  31  THR   A CA   1 
ATOM   203  C  C    . THR   A 1 35  ? 20.86100 -6.49000  10.13400 1.000 14.86000 ?  31  THR   A C    1 
ATOM   204  O  O    . THR   A 1 35  ? 20.05100 -5.94100  10.89100 1.000 15.33000 ?  31  THR   A O    1 
ATOM   205  C  CB   . THR   A 1 35  ? 20.45600 -8.95100  10.22400 1.000 16.64000 ?  31  THR   A CB   1 
ATOM   206  O  OG1  . THR   A 1 35  ? 21.03300 -10.22100 10.56300 1.000 15.91000 ?  31  THR   A OG1  1 
ATOM   207  C  CG2  . THR   A 1 35  ? 20.02000 -8.95100  8.76500  1.000 15.99000 ?  31  THR   A CG2  1 
ATOM   208  N  N    . VAL   A 1 36  ? 21.24200 -5.95600  8.97200  1.000 13.47000 ?  32  VAL   A N    1 
ATOM   209  C  CA   . VAL   A 1 36  ? 20.74800 -4.65800  8.52400  1.000 11.53000 ?  32  VAL   A CA   1 
ATOM   210  C  C    . VAL   A 1 36  ? 20.12300 -4.82000  7.14600  1.000 15.02000 ?  32  VAL   A C    1 
ATOM   211  O  O    . VAL   A 1 36  ? 20.55300 -5.65800  6.34600  1.000 14.64000 ?  32  VAL   A O    1 
ATOM   212  C  CB   . VAL   A 1 36  ? 21.85100 -3.58200  8.48900  1.000 12.31000 ?  32  VAL   A CB   1 
ATOM   213  C  CG1  . VAL   A 1 36  ? 22.38000 -3.32600  9.89600  1.000 16.45000 ?  32  VAL   A CG1  1 
ATOM   214  C  CG2  . VAL   A 1 36  ? 22.99300 -3.97800  7.52800  1.000 13.12000 ?  32  VAL   A CG2  1 
ATOM   215  N  N    . LEU   A 1 37  ? 19.07700 -4.02900  6.89000  1.000 14.36000 ?  33  LEU   A N    1 
ATOM   216  C  CA   . LEU   A 1 37  ? 18.51900 -3.81900  5.55500  1.000 11.19000 ?  33  LEU   A CA   1 
ATOM   217  C  C    . LEU   A 1 37  ? 18.88600 -2.41100  5.11800  1.000 14.49000 ?  33  LEU   A C    1 
ATOM   218  O  O    . LEU   A 1 37  ? 18.49600 -1.44300  5.77300  1.000 12.57000 ?  33  LEU   A O    1 
ATOM   219  C  CB   . LEU   A 1 37  ? 16.99700 -4.00500  5.54100  1.000 12.16000 ?  33  LEU   A CB   1 
ATOM   220  C  CG   . LEU   A 1 37  ? 16.35500 -3.64500  4.18400  1.000 14.24000 ?  33  LEU   A CG   1 
ATOM   221  C  CD1  . LEU   A 1 37  ? 16.86600 -4.58500  3.09600  1.000 16.48000 ?  33  LEU   A CD1  1 
ATOM   222  C  CD2  . LEU   A 1 37  ? 14.82900 -3.65700  4.23600  1.000 15.81000 ?  33  LEU   A CD2  1 
ATOM   223  N  N    . VAL   A 1 38  ? 19.67000 -2.29300  4.03500  1.000 14.34000 ?  34  VAL   A N    1 
ATOM   224  C  CA   . VAL   A 1 38  ? 20.12000 -0.99500  3.55000  1.000 15.65000 ?  34  VAL   A CA   1 
ATOM   225  C  C    . VAL   A 1 38  ? 19.81200 -0.88800  2.06200  1.000 16.02000 ?  34  VAL   A C    1 
ATOM   226  O  O    . VAL   A 1 38  ? 19.84500 -1.87900  1.32800  1.000 18.77000 ?  34  VAL   A O    1 
ATOM   227  C  CB   . VAL   A 1 38  ? 21.62900 -0.77400  3.81900  1.000 12.95000 ?  34  VAL   A CB   1 
ATOM   228  C  CG1  . VAL   A 1 38  ? 21.91100 -0.84400  5.31300  1.000 14.09000 ?  34  VAL   A CG1  1 
ATOM   229  C  CG2  . VAL   A 1 38  ? 22.47100 -1.80700  3.07400  1.000 14.94000 ?  34  VAL   A CG2  1 
ATOM   230  N  N    . ARG   A 1 39  ? 19.50200 0.32500   1.61000  1.000 13.78000 ?  35  ARG   A N    1 
ATOM   231  C  CA   . ARG   A 1 39  ? 19.27300 0.49900   0.17600  1.000 15.25000 ?  35  ARG   A CA   1 
ATOM   232  C  C    . ARG   A 1 39  ? 20.57400 0.43800   -0.61800 1.000 19.36000 ?  35  ARG   A C    1 
ATOM   233  O  O    . ARG   A 1 39  ? 20.55500 0.09800   -1.80900 1.000 18.51000 ?  35  ARG   A O    1 
ATOM   234  C  CB   . ARG   A 1 39  ? 18.54600 1.82100   -0.08200 1.000 15.06000 ?  35  ARG   A CB   1 
ATOM   235  C  CG   . ARG   A 1 39  ? 17.14600 1.83300   0.55500  1.000 16.24000 ?  35  ARG   A CG   1 
ATOM   236  C  CD   . ARG   A 1 39  ? 16.31400 3.03400   0.10700  1.000 17.63000 ?  35  ARG   A CD   1 
ATOM   237  N  NE   . ARG   A 1 39  ? 16.72000 4.27900   0.74900  1.000 15.26000 ?  35  ARG   A NE   1 
ATOM   238  C  CZ   . ARG   A 1 39  ? 16.07400 5.42700   0.59300  1.000 17.71000 ?  35  ARG   A CZ   1 
ATOM   239  N  NH1  . ARG   A 1 39  ? 14.99600 5.51200   -0.17600 1.000 18.69000 ?  35  ARG   A NH1  1 
ATOM   240  N  NH2  . ARG   A 1 39  ? 16.51800 6.51500   1.21900  1.000 16.61000 ?  35  ARG   A NH2  1 
ATOM   241  N  N    . ASP   A 1 40  ? 21.70300 0.72400   0.02100  1.000 19.18000 ?  36  ASP   A N    1 
ATOM   242  C  CA   . ASP   A 1 40  ? 22.99300 0.75200   -0.65900 1.000 19.76000 ?  36  ASP   A CA   1 
ATOM   243  C  C    . ASP   A 1 40  ? 24.06400 0.45500   0.37800  1.000 21.54000 ?  36  ASP   A C    1 
ATOM   244  O  O    . ASP   A 1 40  ? 24.21600 1.22200   1.33500  1.000 21.47000 ?  36  ASP   A O    1 
ATOM   245  C  CB   . ASP   A 1 40  ? 23.21700 2.12000   -1.30100 1.000 24.87000 ?  36  ASP   A CB   1 
ATOM   246  C  CG   . ASP   A 1 40  ? 24.41500 2.14700   -2.23100 1.000 31.03000 ?  36  ASP   A CG   1 
ATOM   247  O  OD1  . ASP   A 1 40  ? 25.24800 1.21500   -2.17200 1.000 30.11000 ?  36  ASP   A OD1  1 
ATOM   248  O  OD2  . ASP   A 1 40  ? 24.50900 3.10600   -3.02900 1.000 27.93000 ?  36  ASP   A OD2  1 
ATOM   249  N  N    . SER   A 1 41  ? 24.79600 -0.65100  0.20100  1.000 22.48000 ?  37  SER   A N    1 
ATOM   250  C  CA   . SER   A 1 41  ? 25.83800 -0.99300  1.16600  1.000 23.46000 ?  37  SER   A CA   1 
ATOM   251  C  C    . SER   A 1 41  ? 26.96100 0.03800   1.18700  1.000 24.27000 ?  37  SER   A C    1 
ATOM   252  O  O    . SER   A 1 41  ? 27.72000 0.09000   2.16100  1.000 21.69000 ?  37  SER   A O    1 
ATOM   253  C  CB   . SER   A 1 41  ? 26.39900 -2.39400  0.88400  1.000 23.66000 ?  37  SER   A CB   1 
ATOM   254  O  OG   . SER   A 1 41  ? 26.69700 -2.56900  -0.49100 1.000 29.92000 ?  37  SER   A OG   1 
ATOM   255  N  N    . SER   A 1 42  ? 27.05600 0.88500   0.15900  1.000 21.85000 ?  38  SER   A N    1 
ATOM   256  C  CA   . SER   A 1 42  ? 28.02800 1.97100   0.16500  1.000 26.26000 ?  38  SER   A CA   1 
ATOM   257  C  C    . SER   A 1 42  ? 27.79800 2.95500   1.30200  1.000 23.87000 ?  38  SER   A C    1 
ATOM   258  O  O    . SER   A 1 42  ? 28.70500 3.72400   1.63200  1.000 22.27000 ?  38  SER   A O    1 
ATOM   259  C  CB   . SER   A 1 42  ? 27.98300 2.71900   -1.16800 1.000 27.95000 ?  38  SER   A CB   1 
ATOM   260  O  OG   . SER   A 1 42  ? 27.96800 1.79700   -2.24600 1.000 38.04000 ?  38  SER   A OG   1 
ATOM   261  N  N    . ARG   A 1 43  ? 26.61600 2.96600   1.91100  1.000 18.57000 ?  39  ARG   A N    1 
ATOM   262  C  CA   . ARG   A 1 43  ? 26.38800 3.90300   2.99900  1.000 19.73000 ?  39  ARG   A CA   1 
ATOM   263  C  C    . ARG   A 1 43  ? 26.63300 3.28200   4.36800  1.000 18.96000 ?  39  ARG   A C    1 
ATOM   264  O  O    . ARG   A 1 43  ? 26.41800 3.94900   5.38200  1.000 20.62000 ?  39  ARG   A O    1 
ATOM   265  C  CB   . ARG   A 1 43  ? 24.97800 4.49600   2.90000  1.000 22.79000 ?  39  ARG   A CB   1 
ATOM   266  C  CG   . ARG   A 1 43  ? 24.88600 5.54700   1.78400  1.000 25.80000 ?  39  ARG   A CG   1 
ATOM   267  C  CD   . ARG   A 1 43  ? 23.64600 6.44200   1.87900  1.000 26.76000 ?  39  ARG   A CD   1 
ATOM   268  N  NE   . ARG   A 1 43  ? 22.41900 5.77300   1.46700  1.000 24.30000 ?  39  ARG   A NE   1 
ATOM   269  C  CZ   . ARG   A 1 43  ? 22.06600 5.55500   0.20700  1.000 22.96000 ?  39  ARG   A CZ   1 
ATOM   270  N  NH1  . ARG   A 1 43  ? 22.86300 5.87400   -0.79800 1.000 24.55000 ?  39  ARG   A NH1  1 
ATOM   271  N  NH2  . ARG   A 1 43  ? 20.87700 5.01400   -0.05200 1.000 18.00000 ?  39  ARG   A NH2  1 
ATOM   272  N  N    . LEU   A 1 44  ? 27.10900 2.04300   4.41600  1.000 18.21000 ?  40  LEU   A N    1 
ATOM   273  C  CA   . LEU   A 1 44  ? 27.57800 1.42300   5.64900  1.000 18.63000 ?  40  LEU   A CA   1 
ATOM   274  C  C    . LEU   A 1 44  ? 29.05900 1.71800   5.87200  1.000 21.15000 ?  40  LEU   A C    1 
ATOM   275  O  O    . LEU   A 1 44  ? 29.81400 1.87700   4.90900  1.000 21.35000 ?  40  LEU   A O    1 
ATOM   276  C  CB   . LEU   A 1 44  ? 27.37300 -0.08600  5.60000  1.000 18.85000 ?  40  LEU   A CB   1 
ATOM   277  C  CG   . LEU   A 1 44  ? 25.93700 -0.56500  5.80200  1.000 18.31000 ?  40  LEU   A CG   1 
ATOM   278  C  CD1  . LEU   A 1 44  ? 25.83900 -2.05100  5.51800  1.000 19.94000 ?  40  LEU   A CD1  1 
ATOM   279  C  CD2  . LEU   A 1 44  ? 25.49800 -0.24000  7.23500  1.000 16.44000 ?  40  LEU   A CD2  1 
ATOM   280  N  N    . PRO   A 1 45  ? 29.49700 1.77000   7.13300  1.000 24.03000 ?  41  PRO   A N    1 
ATOM   281  C  CA   . PRO   A 1 45  ? 30.92600 1.97900   7.41100  1.000 27.10000 ?  41  PRO   A CA   1 
ATOM   282  C  C    . PRO   A 1 45  ? 31.77600 0.86100   6.83000  1.000 22.71000 ?  41  PRO   A C    1 
ATOM   283  O  O    . PRO   A 1 45  ? 31.37800 -0.30500  6.81700  1.000 21.87000 ?  41  PRO   A O    1 
ATOM   284  C  CB   . PRO   A 1 45  ? 30.99400 1.98600   8.94300  1.000 25.39000 ?  41  PRO   A CB   1 
ATOM   285  C  CG   . PRO   A 1 45  ? 29.77300 1.22300   9.38100  1.000 26.05000 ?  41  PRO   A CG   1 
ATOM   286  C  CD   . PRO   A 1 45  ? 28.71700 1.59400   8.37200  1.000 24.95000 ?  41  PRO   A CD   1 
ATOM   287  N  N    . SER   A 1 46  ? 32.96500 1.22300   6.35800  1.000 20.68000 ?  42  SER   A N    1 
ATOM   288  C  CA   . SER   A 1 46  ? 33.87900 0.23700   5.80300  1.000 26.94000 ?  42  SER   A CA   1 
ATOM   289  C  C    . SER   A 1 46  ? 34.88500 -0.26500  6.83000  1.000 23.96000 ?  42  SER   A C    1 
ATOM   290  O  O    . SER   A 1 46  ? 35.46600 -1.33600  6.63500  1.000 27.08000 ?  42  SER   A O    1 
ATOM   291  C  CB   . SER   A 1 46  ? 34.61000 0.81900   4.58700  1.000 27.61000 ?  42  SER   A CB   1 
ATOM   292  O  OG   . SER   A 1 46  ? 35.06300 2.13300   4.86100  1.000 38.05000 ?  42  SER   A OG   1 
ATOM   293  N  N    . GLU   A 1 47  ? 35.07800 0.46100   7.92600  1.000 21.29000 ?  43  GLU   A N    1 
ATOM   294  C  CA   . GLU   A 1 47  ? 35.90700 0.00300   9.02900  1.000 23.72000 ?  43  GLU   A CA   1 
ATOM   295  C  C    . GLU   A 1 47  ? 35.16400 0.22500   10.34500 1.000 21.33000 ?  43  GLU   A C    1 
ATOM   296  O  O    . GLU   A 1 47  ? 34.09500 0.84100   10.38700 1.000 24.29000 ?  43  GLU   A O    1 
ATOM   297  C  CB   . GLU   A 1 47  ? 37.26700 0.71700   9.04300  1.000 22.42000 ?  43  GLU   A CB   1 
ATOM   298  C  CG   . GLU   A 1 47  ? 38.18400 0.33700   7.87600  1.000 24.19000 ?  43  GLU   A CG   1 
ATOM   299  C  CD   . GLU   A 1 47  ? 37.95600 1.18400   6.62900  1.000 32.21000 ?  43  GLU   A CD   1 
ATOM   300  O  OE1  . GLU   A 1 47  ? 37.35800 2.27800   6.75000  1.000 31.63000 ?  43  GLU   A OE1  1 
ATOM   301  O  OE2  . GLU   A 1 47  ? 38.38500 0.75400   5.53000  1.000 31.72000 ?  43  GLU   A OE2  1 
ATOM   302  N  N    . GLY   A 1 48  ? 35.74800 -0.27400  11.43300 1.000 19.24000 ?  44  GLY   A N    1 
ATOM   303  C  CA   . GLY   A 1 48  ? 35.11000 -0.19000  12.72700 1.000 24.83000 ?  44  GLY   A CA   1 
ATOM   304  C  C    . GLY   A 1 48  ? 34.04200 -1.25500  12.89300 1.000 22.33000 ?  44  GLY   A C    1 
ATOM   305  O  O    . GLY   A 1 48  ? 34.01600 -2.25000  12.16200 1.000 22.67000 ?  44  GLY   A O    1 
ATOM   306  N  N    . PRO   A 1 49  ? 33.14500 -1.06900  13.86200 1.000 18.87000 ?  45  PRO   A N    1 
ATOM   307  C  CA   . PRO   A 1 49  ? 32.06500 -2.05000  14.07100 1.000 21.93000 ?  45  PRO   A CA   1 
ATOM   308  C  C    . PRO   A 1 49  ? 31.12900 -2.12400  12.87100 1.000 20.84000 ?  45  PRO   A C    1 
ATOM   309  O  O    . PRO   A 1 49  ? 30.56800 -1.11800  12.43800 1.000 26.69000 ?  45  PRO   A O    1 
ATOM   310  C  CB   . PRO   A 1 49  ? 31.33100 -1.52600  15.31400 1.000 20.97000 ?  45  PRO   A CB   1 
ATOM   311  C  CG   . PRO   A 1 49  ? 32.17700 -0.46600  15.88900 1.000 25.37000 ?  45  PRO   A CG   1 
ATOM   312  C  CD   . PRO   A 1 49  ? 33.14000 0.01700   14.85600 1.000 18.46000 ?  45  PRO   A CD   1 
ATOM   313  N  N    . ARG   A 1 50  ? 30.95300 -3.33300  12.34900 1.000 20.65000 ?  46  ARG   A N    1 
ATOM   314  C  CA   . ARG   A 1 50  ? 30.13300 -3.59200  11.17500 1.000 21.61000 ?  46  ARG   A CA   1 
ATOM   315  C  C    . ARG   A 1 50  ? 29.15100 -4.72400  11.43800 1.000 17.80000 ?  46  ARG   A C    1 
ATOM   316  O  O    . ARG   A 1 50  ? 29.41400 -5.60800  12.26100 1.000 19.64000 ?  46  ARG   A O    1 
ATOM   317  C  CB   . ARG   A 1 50  ? 31.01400 -3.94700  9.96800  1.000 21.68000 ?  46  ARG   A CB   1 
ATOM   318  C  CG   . ARG   A 1 50  ? 31.68200 -2.73700  9.34100  1.000 23.08000 ?  46  ARG   A CG   1 
ATOM   319  C  CD   . ARG   A 1 50  ? 32.95300 -3.13100  8.62700  1.000 21.45000 ?  46  ARG   A CD   1 
ATOM   320  N  NE   . ARG   A 1 50  ? 33.99000 -3.45000  9.59800  1.000 21.19000 ?  46  ARG   A NE   1 
ATOM   321  C  CZ   . ARG   A 1 50  ? 35.03300 -4.22400  9.34800  1.000 19.42000 ?  46  ARG   A CZ   1 
ATOM   322  N  NH1  . ARG   A 1 50  ? 35.22700 -4.74600  8.14900  1.000 17.36000 ?  46  ARG   A NH1  1 
ATOM   323  N  NH2  . ARG   A 1 50  ? 35.88300 -4.50300  10.33400 1.000 16.30000 ?  46  ARG   A NH2  1 
ATOM   324  N  N    . PRO   A 1 51  ? 28.01400 -4.73100  10.74200 1.000 18.49000 ?  47  PRO   A N    1 
ATOM   325  C  CA   . PRO   A 1 51  ? 27.00100 -5.75700  11.00900 1.000 16.20000 ?  47  PRO   A CA   1 
ATOM   326  C  C    . PRO   A 1 51  ? 27.48400 -7.13900  10.60700 1.000 18.93000 ?  47  PRO   A C    1 
ATOM   327  O  O    . PRO   A 1 51  ? 28.33500 -7.29600  9.72700  1.000 18.29000 ?  47  PRO   A O    1 
ATOM   328  C  CB   . PRO   A 1 51  ? 25.80800 -5.31300  10.15000 1.000 18.07000 ?  47  PRO   A CB   1 
ATOM   329  C  CG   . PRO   A 1 51  ? 26.41500 -4.51400  9.04400  1.000 16.85000 ?  47  PRO   A CG   1 
ATOM   330  C  CD   . PRO   A 1 51  ? 27.63200 -3.84100  9.62600  1.000 18.94000 ?  47  PRO   A CD   1 
ATOM   331  N  N    . ALA   A 1 52  ? 26.92800 -8.15200  11.27200 1.000 17.15000 ?  48  ALA   A N    1 
ATOM   332  C  CA   . ALA   A 1 52  ? 27.23000 -9.52700  10.88900 1.000 18.23000 ?  48  ALA   A CA   1 
ATOM   333  C  C    . ALA   A 1 52  ? 26.58000 -9.89700  9.55900  1.000 21.10000 ?  48  ALA   A C    1 
ATOM   334  O  O    . ALA   A 1 52  ? 27.14100 -10.68900 8.79000  1.000 23.08000 ?  48  ALA   A O    1 
ATOM   335  C  CB   . ALA   A 1 52  ? 26.78300 -10.48700 11.99500 1.000 19.79000 ?  48  ALA   A CB   1 
ATOM   336  N  N    . HIS   A 1 53  ? 25.41200 -9.33400  9.25900  1.000 16.17000 ?  49  HIS   A N    1 
ATOM   337  C  CA   . HIS   A 1 53  ? 24.68300 -9.68300  8.04800  1.000 16.59000 ?  49  HIS   A CA   1 
ATOM   338  C  C    . HIS   A 1 53  ? 24.13900 -8.42500  7.39700  1.000 18.70000 ?  49  HIS   A C    1 
ATOM   339  O  O    . HIS   A 1 53  ? 23.59100 -7.55600  8.08000  1.000 18.21000 ?  49  HIS   A O    1 
ATOM   340  C  CB   . HIS   A 1 53  ? 23.53200 -10.64800 8.35200  1.000 16.83000 ?  49  HIS   A CB   1 
ATOM   341  C  CG   . HIS   A 1 53  ? 23.94600 -11.81900 9.18400  1.000 22.35000 ?  49  HIS   A CG   1 
ATOM   342  N  ND1  . HIS   A 1 53  ? 24.73700 -12.83600 8.69400  1.000 24.21000 ?  49  HIS   A ND1  1 
ATOM   343  C  CD2  . HIS   A 1 53  ? 23.68400 -12.13300 10.47500 1.000 22.82000 ?  49  HIS   A CD2  1 
ATOM   344  C  CE1  . HIS   A 1 53  ? 24.94300 -13.72800 9.64700  1.000 27.77000 ?  49  HIS   A CE1  1 
ATOM   345  N  NE2  . HIS   A 1 53  ? 24.31500 -13.32600 10.73800 1.000 22.57000 ?  49  HIS   A NE2  1 
ATOM   346  N  N    . VAL   A 1 54  ? 24.29000 -8.33800  6.07700  1.000 16.82000 ?  50  VAL   A N    1 
ATOM   347  C  CA   . VAL   A 1 54  ? 23.83300 -7.19600  5.29400  1.000 17.62000 ?  50  VAL   A CA   1 
ATOM   348  C  C    . VAL   A 1 54  ? 22.86100 -7.70000  4.24000  1.000 17.65000 ?  50  VAL   A C    1 
ATOM   349  O  O    . VAL   A 1 54  ? 23.21300 -8.56200  3.42400  1.000 20.62000 ?  50  VAL   A O    1 
ATOM   350  C  CB   . VAL   A 1 54  ? 24.99900 -6.45400  4.62400  1.000 17.32000 ?  50  VAL   A CB   1 
ATOM   351  C  CG1  . VAL   A 1 54  ? 24.46100 -5.40200  3.65900  1.000 18.19000 ?  50  VAL   A CG1  1 
ATOM   352  C  CG2  . VAL   A 1 54  ? 25.91700 -5.84000  5.66800  1.000 21.13000 ?  50  VAL   A CG2  1 
ATOM   353  N  N    . VAL   A 1 55  ? 21.64700 -7.16300  4.25300  1.000 15.14000 ?  51  VAL   A N    1 
ATOM   354  C  CA   . VAL   A 1 55  ? 20.68400 -7.35800  3.18200  1.000 14.10000 ?  51  VAL   A CA   1 
ATOM   355  C  C    . VAL   A 1 55  ? 20.58400 -6.03400  2.45100  1.000 15.66000 ?  51  VAL   A C    1 
ATOM   356  O  O    . VAL   A 1 55  ? 20.32200 -5.00100  3.07800  1.000 13.82000 ?  51  VAL   A O    1 
ATOM   357  C  CB   . VAL   A 1 55  ? 19.30800 -7.78400  3.71600  1.000 13.40000 ?  51  VAL   A CB   1 
ATOM   358  C  CG1  . VAL   A 1 55  ? 18.34000 -7.94700  2.56900  1.000 15.98000 ?  51  VAL   A CG1  1 
ATOM   359  C  CG2  . VAL   A 1 55  ? 19.43500 -9.05500  4.56000  1.000 16.94000 ?  51  VAL   A CG2  1 
ATOM   360  N  N    . VAL   A 1 56  ? 20.80600 -6.03900  1.14000  1.000 16.21000 ?  52  VAL   A N    1 
ATOM   361  C  CA   . VAL   A 1 56  ? 20.61900 -4.82800  0.34400  1.000 15.94000 ?  52  VAL   A CA   1 
ATOM   362  C  C    . VAL   A 1 56  ? 19.25300 -4.89500  -0.32900 1.000 18.55000 ?  52  VAL   A C    1 
ATOM   363  O  O    . VAL   A 1 56  ? 18.94800 -5.84200  -1.06100 1.000 18.17000 ?  52  VAL   A O    1 
ATOM   364  C  CB   . VAL   A 1 56  ? 21.74900 -4.62500  -0.67800 1.000 14.38000 ?  52  VAL   A CB   1 
ATOM   365  C  CG1  . VAL   A 1 56  ? 21.53900 -3.28600  -1.40000 1.000 15.71000 ?  52  VAL   A CG1  1 
ATOM   366  C  CG2  . VAL   A 1 56  ? 23.07100 -4.62100  0.03500  1.000 15.22000 ?  52  VAL   A CG2  1 
ATOM   367  N  N    . GLY   A 1 57  ? 18.42500 -3.89000  -0.07200 1.000 16.72000 ?  53  GLY   A N    1 
ATOM   368  C  CA   . GLY   A 1 57  ? 17.07600 -3.88800  -0.59800 1.000 16.24000 ?  53  GLY   A CA   1 
ATOM   369  C  C    . GLY   A 1 57  ? 16.30700 -2.72500  -0.01200 1.000 19.12000 ?  53  GLY   A C    1 
ATOM   370  O  O    . GLY   A 1 57  ? 16.89800 -1.79500  0.54100  1.000 21.40000 ?  53  GLY   A O    1 
ATOM   371  N  N    . ASP   A 1 58  ? 14.98300 -2.80900  -0.10900 1.000 14.35000 ?  54  ASP   A N    1 
ATOM   372  C  CA   . ASP   A 1 58  ? 14.11500 -1.68600  0.21300  1.000 16.31000 ?  54  ASP   A CA   1 
ATOM   373  C  C    . ASP   A 1 58  ? 13.06000 -2.13100  1.21500  1.000 14.47000 ?  54  ASP   A C    1 
ATOM   374  O  O    . ASP   A 1 58  ? 12.50700 -3.23000  1.10400  1.000 15.48000 ?  54  ASP   A O    1 
ATOM   375  C  CB   . ASP   A 1 58  ? 13.46600 -1.13200  -1.06800 1.000 17.12000 ?  54  ASP   A CB   1 
ATOM   376  C  CG   . ASP   A 1 58  ? 13.01200 0.29500   -0.91700 1.000 19.10000 ?  54  ASP   A CG   1 
ATOM   377  O  OD1  . ASP   A 1 58  ? 12.00400 0.52500   -0.20300 1.000 16.68000 ?  54  ASP   A OD1  1 
ATOM   378  O  OD2  . ASP   A 1 58  ? 13.67600 1.18200   -1.50200 1.000 17.93000 ?  54  ASP   A OD2  1 
ATOM   379  N  N    . VAL   A 1 59  ? 12.79500 -1.28100  2.21200  1.000 11.44000 ?  55  VAL   A N    1 
ATOM   380  C  CA   . VAL   A 1 59  ? 11.80300 -1.64400  3.21400  1.000 12.18000 ?  55  VAL   A CA   1 
ATOM   381  C  C    . VAL   A 1 59  ? 10.41800 -1.71700  2.59700  1.000 14.43000 ?  55  VAL   A C    1 
ATOM   382  O  O    . VAL   A 1 59  ? 9.50000  -2.27100  3.21400  1.000 14.79000 ?  55  VAL   A O    1 
ATOM   383  C  CB   . VAL   A 1 59  ? 11.82700 -0.64700  4.40200  1.000 13.01000 ?  55  VAL   A CB   1 
ATOM   384  C  CG1  . VAL   A 1 59  ? 11.10100 0.67200   4.04200  1.000 15.22000 ?  55  VAL   A CG1  1 
ATOM   385  C  CG2  . VAL   A 1 59  ? 11.22500 -1.29100  5.65400  1.000 14.52000 ?  55  VAL   A CG2  1 
ATOM   386  N  N    . LEU   A 1 60  ? 10.23900 -1.14700  1.39400  1.000 14.62000 ?  56  LEU   A N    1 
ATOM   387  C  CA   . LEU   A 1 60  ? 8.96900  -1.19200  0.67000  1.000 14.98000 ?  56  LEU   A CA   1 
ATOM   388  C  C    . LEU   A 1 60  ? 8.78100  -2.48900  -0.10900 1.000 19.56000 ?  56  LEU   A C    1 
ATOM   389  O  O    . LEU   A 1 60  ? 7.69800  -2.71200  -0.66600 1.000 19.77000 ?  56  LEU   A O    1 
ATOM   390  C  CB   . LEU   A 1 60  ? 8.85500  0.00500   -0.28500 1.000 15.79000 ?  56  LEU   A CB   1 
ATOM   391  C  CG   . LEU   A 1 60  ? 8.83900  1.37100   0.40700  1.000 19.90000 ?  56  LEU   A CG   1 
ATOM   392  C  CD1  . LEU   A 1 60  ? 8.78800  2.51700   -0.59000 1.000 19.29000 ?  56  LEU   A CD1  1 
ATOM   393  C  CD2  . LEU   A 1 60  ? 7.66400  1.43700   1.37800  1.000 17.86000 ?  56  LEU   A CD2  1 
ATOM   394  N  N    . GLN   A 1 61  ? 9.80000  -3.33900  -0.15700 1.000 15.97000 ?  57  GLN   A N    1 
ATOM   395  C  CA   . GLN   A 1 61  ? 9.72400  -4.64600  -0.80000 1.000 18.19000 ?  57  GLN   A CA   1 
ATOM   396  C  C    . GLN   A 1 61  ? 9.56400  -5.69200  0.29200  1.000 18.74000 ?  57  GLN   A C    1 
ATOM   397  O  O    . GLN   A 1 61  ? 10.50100 -5.93600  1.06100  1.000 19.25000 ?  57  GLN   A O    1 
ATOM   398  C  CB   . GLN   A 1 61  ? 10.97700 -4.92200  -1.62700 1.000 21.48000 ?  57  GLN   A CB   1 
ATOM   399  C  CG   . GLN   A 1 61  ? 11.11800 -4.07000  -2.85900 1.000 25.64000 ?  57  GLN   A CG   1 
ATOM   400  C  CD   . GLN   A 1 61  ? 10.13300 -4.47500  -3.93500 1.000 34.40000 ?  57  GLN   A CD   1 
ATOM   401  O  OE1  . GLN   A 1 61  ? 9.54700  -5.56100  -3.87600 1.000 36.01000 ?  57  GLN   A OE1  1 
ATOM   402  N  NE2  . GLN   A 1 61  ? 9.94400  -3.60500  -4.92500 1.000 42.35000 ?  57  GLN   A NE2  1 
ATOM   403  N  N    . ALA   A 1 62  ? 8.38400  -6.31700  0.35300  1.000 21.30000 ?  58  ALA   A N    1 
ATOM   404  C  CA   . ALA   A 1 62  ? 8.11300  -7.29000  1.40800  1.000 21.13000 ?  58  ALA   A CA   1 
ATOM   405  C  C    . ALA   A 1 62  ? 9.11700  -8.44000  1.40500  1.000 19.90000 ?  58  ALA   A C    1 
ATOM   406  O  O    . ALA   A 1 62  ? 9.47400  -8.95600  2.47400  1.000 17.43000 ?  58  ALA   A O    1 
ATOM   407  C  CB   . ALA   A 1 62  ? 6.68200  -7.81700  1.27800  1.000 21.28000 ?  58  ALA   A CB   1 
ATOM   408  N  N    . ALA   A 1 63  ? 9.60100  -8.85500  0.23100  1.000 21.58000 ?  59  ALA   A N    1 
ATOM   409  C  CA   . ALA   A 1 63  ? 10.57700 -9.93800  0.21100  1.000 21.19000 ?  59  ALA   A CA   1 
ATOM   410  C  C    . ALA   A 1 63  ? 11.87700 -9.52500  0.89800  1.000 20.34000 ?  59  ALA   A C    1 
ATOM   411  O  O    . ALA   A 1 63  ? 12.51700 -10.34100 1.57200  1.000 19.74000 ?  59  ALA   A O    1 
ATOM   412  C  CB   . ALA   A 1 63  ? 10.84400 -10.38500 -1.22700 1.000 24.42000 ?  59  ALA   A CB   1 
ATOM   413  N  N    . ASP   A 1 64  ? 12.27600 -8.25700  0.74600  1.000 17.25000 ?  60  ASP   A N    1 
ATOM   414  C  CA   . ASP   A 1 64  ? 13.50500 -7.77800  1.37500  1.000 18.47000 ?  60  ASP   A CA   1 
ATOM   415  C  C    . ASP   A 1 64  ? 13.35600 -7.69700  2.88700  1.000 16.20000 ?  60  ASP   A C    1 
ATOM   416  O  O    . ASP   A 1 64  ? 14.29900 -8.00100  3.62900  1.000 15.82000 ?  60  ASP   A O    1 
ATOM   417  C  CB   . ASP   A 1 64  ? 13.88600 -6.40200  0.82700  1.000 14.05000 ?  60  ASP   A CB   1 
ATOM   418  C  CG   . ASP   A 1 64  ? 14.25600 -6.44200  -0.64100 1.000 19.19000 ?  60  ASP   A CG   1 
ATOM   419  O  OD1  . ASP   A 1 64  ? 14.56300 -7.55500  -1.12100 1.000 23.32000 ?  60  ASP   A OD1  1 
ATOM   420  O  OD2  . ASP   A 1 64  ? 14.25500 -5.37100  -1.29700 1.000 20.02000 ?  60  ASP   A OD2  1 
ATOM   421  N  N    . VAL   A 1 65  ? 12.19100 -7.25600  3.35500  1.000 16.47000 ?  61  VAL   A N    1 
ATOM   422  C  CA   . VAL   A 1 65  ? 11.94700 -7.17300  4.79000  1.000 14.06000 ?  61  VAL   A CA   1 
ATOM   423  C  C    . VAL   A 1 65  ? 11.87700 -8.56500  5.39300  1.000 17.30000 ?  61  VAL   A C    1 
ATOM   424  O  O    . VAL   A 1 65  ? 12.40900 -8.82000  6.47600  1.000 15.60000 ?  61  VAL   A O    1 
ATOM   425  C  CB   . VAL   A 1 65  ? 10.65700 -6.37600  5.06000  1.000 15.86000 ?  61  VAL   A CB   1 
ATOM   426  C  CG1  . VAL   A 1 65  ? 10.29100 -6.42400  6.54000  1.000 14.98000 ?  61  VAL   A CG1  1 
ATOM   427  C  CG2  . VAL   A 1 65  ? 10.81900 -4.93000  4.59600  1.000 14.38000 ?  61  VAL   A CG2  1 
ATOM   428  N  N    . ASP   A 1 66  ? 11.24300 -9.49200  4.68200  1.000 14.44000 ?  62  ASP   A N    1 
ATOM   429  C  CA   . ASP   A 1 66  ? 11.07800 -10.85000 5.18800  1.000 17.92000 ?  62  ASP   A CA   1 
ATOM   430  C  C    . ASP   A 1 66  ? 12.42800 -11.51600 5.43300  1.000 18.23000 ?  62  ASP   A C    1 
ATOM   431  O  O    . ASP   A 1 66  ? 12.64800 -12.12800 6.48400  1.000 17.74000 ?  62  ASP   A O    1 
ATOM   432  C  CB   . ASP   A 1 66  ? 10.22200 -11.65100 4.20600  1.000 16.97000 ?  62  ASP   A CB   1 
ATOM   433  C  CG   . ASP   A 1 66  ? 9.73300  -12.95900 4.78500  1.000 26.32000 ?  62  ASP   A CG   1 
ATOM   434  O  OD1  . ASP   A 1 66  ? 10.48900 -13.95200 4.73100  1.000 26.85000 ?  62  ASP   A OD1  1 
ATOM   435  O  OD2  . ASP   A 1 66  ? 8.59100  -12.99100 5.29800  1.000 28.96000 ?  62  ASP   A OD2  1 
ATOM   436  N  N    . LYS   A 1 67  ? 13.35900 -11.38700 4.48700  1.000 16.47000 ?  63  LYS   A N    1 
ATOM   437  C  CA   . LYS   A 1 67  ? 14.65400 -12.03300 4.66700  1.000 19.23000 ?  63  LYS   A CA   1 
ATOM   438  C  C    . LYS   A 1 67  ? 15.51500 -11.32900 5.70900  1.000 17.56000 ?  63  LYS   A C    1 
ATOM   439  O  O    . LYS   A 1 67  ? 16.44800 -11.94800 6.23400  1.000 21.12000 ?  63  LYS   A O    1 
ATOM   440  C  CB   . LYS   A 1 67  ? 15.40000 -12.12500 3.32900  1.000 23.94000 ?  63  LYS   A CB   1 
ATOM   441  C  CG   . LYS   A 1 67  ? 15.84500 -10.80700 2.77500  1.000 22.39000 ?  63  LYS   A CG   1 
ATOM   442  C  CD   . LYS   A 1 67  ? 16.67400 -10.97900 1.49400  1.000 28.26000 ?  63  LYS   A CD   1 
ATOM   443  C  CE   . LYS   A 1 67  ? 15.81900 -11.43900 0.33300  1.000 29.66000 ?  63  LYS   A CE   1 
ATOM   444  N  NZ   . LYS   A 1 67  ? 16.52900 -11.21700 -0.97300 1.000 26.48000 ?  63  LYS   A NZ   1 
ATOM   445  N  N    . THR   A 1 68  ? 15.21200 -10.06200 6.02800  1.000 15.26000 ?  64  THR   A N    1 
ATOM   446  C  CA   . THR   A 1 68  ? 15.91400 -9.33200  7.08000  1.000 13.16000 ?  64  THR   A CA   1 
ATOM   447  C  C    . THR   A 1 68  ? 15.42300 -9.75100  8.46000  1.000 15.66000 ?  64  THR   A C    1 
ATOM   448  O  O    . THR   A 1 68  ? 16.22300 -9.90800  9.39000  1.000 15.37000 ?  64  THR   A O    1 
ATOM   449  C  CB   . THR   A 1 68  ? 15.72800 -7.82000  6.89000  1.000 16.73000 ?  64  THR   A CB   1 
ATOM   450  O  OG1  . THR   A 1 68  ? 16.18000 -7.43900  5.58600  1.000 15.76000 ?  64  THR   A OG1  1 
ATOM   451  C  CG2  . THR   A 1 68  ? 16.51700 -7.01600  7.93800  1.000 15.36000 ?  64  THR   A CG2  1 
ATOM   452  N  N    . VAL   A 1 69  ? 14.11300 -9.95800  8.59300  1.000 13.27000 ?  65  VAL   A N    1 
ATOM   453  C  CA   . VAL   A 1 69  ? 13.51600 -10.28200 9.88900  1.000 13.11000 ?  65  VAL   A CA   1 
ATOM   454  C  C    . VAL   A 1 69  ? 13.66400 -11.76100 10.24400 1.000 17.55000 ?  65  VAL   A C    1 
ATOM   455  O  O    . VAL   A 1 69  ? 13.63900 -12.11900 11.43100 1.000 16.91000 ?  65  VAL   A O    1 
ATOM   456  C  CB   . VAL   A 1 69  ? 12.03300 -9.85800  9.86600  1.000 12.93000 ?  65  VAL   A CB   1 
ATOM   457  C  CG1  . VAL   A 1 69  ? 11.25400 -10.38600 11.09600 1.000 17.25000 ?  65  VAL   A CG1  1 
ATOM   458  C  CG2  . VAL   A 1 69  ? 11.90200 -8.33400  9.78800  1.000 13.28000 ?  65  VAL   A CG2  1 
ATOM   459  N  N    . ALA   A 1 70  ? 13.81800 -12.63000 9.25100  1.000 16.51000 ?  66  ALA   A N    1 
ATOM   460  C  CA   . ALA   A 1 70  ? 13.90100 -14.06300 9.51400  1.000 16.74000 ?  66  ALA   A CA   1 
ATOM   461  C  C    . ALA   A 1 70  ? 15.04400 -14.36600 10.48000 1.000 15.90000 ?  66  ALA   A C    1 
ATOM   462  O  O    . ALA   A 1 70  ? 16.16300 -13.87700 10.31100 1.000 19.41000 ?  66  ALA   A O    1 
ATOM   463  C  CB   . ALA   A 1 70  ? 14.09800 -14.82500 8.20000  1.000 19.36000 ?  66  ALA   A CB   1 
ATOM   464  N  N    . GLY   A 1 71  ? 14.74700 -15.15900 11.50800 1.000 15.81000 ?  67  GLY   A N    1 
ATOM   465  C  CA   . GLY   A 1 71  ? 15.74700 -15.62200 12.44300 1.000 22.10000 ?  67  GLY   A CA   1 
ATOM   466  C  C    . GLY   A 1 71  ? 16.11500 -14.67400 13.56600 1.000 16.73000 ?  67  GLY   A C    1 
ATOM   467  O  O    . GLY   A 1 71  ? 16.95800 -15.03700 14.39200 1.000 19.68000 ?  67  GLY   A O    1 
ATOM   468  N  N    . GLN   A 1 72  ? 15.51200 -13.48500 13.64600 1.000 16.58000 ?  68  GLN   A N    1 
ATOM   469  C  CA   . GLN   A 1 72  ? 15.92500 -12.51600 14.65400 1.000 15.21000 ?  68  GLN   A CA   1 
ATOM   470  C  C    . GLN   A 1 72  ? 15.20500 -12.74000 15.98200 1.000 15.31000 ?  68  GLN   A C    1 
ATOM   471  O  O    . GLN   A 1 72  ? 14.12600 -13.33500 16.04000 1.000 19.77000 ?  68  GLN   A O    1 
ATOM   472  C  CB   . GLN   A 1 72  ? 15.66200 -11.08200 14.17700 1.000 15.24000 ?  68  GLN   A CB   1 
ATOM   473  C  CG   . GLN   A 1 72  ? 16.17000 -10.79500 12.76900 1.000 13.41000 ?  68  GLN   A CG   1 
ATOM   474  C  CD   . GLN   A 1 72  ? 17.66500 -10.92400 12.65100 1.000 18.30000 ?  68  GLN   A CD   1 
ATOM   475  O  OE1  . GLN   A 1 72  ? 18.38200 -10.96200 13.65300 1.000 18.54000 ?  68  GLN   A OE1  1 
ATOM   476  N  NE2  . GLN   A 1 72  ? 18.15300 -10.98000 11.41500 1.000 18.23000 ?  68  GLN   A NE2  1 
ATOM   477  N  N    . ASP   A 1 73  ? 15.81400 -12.22000 17.05500 1.000 15.57000 ?  69  ASP   A N    1 
ATOM   478  C  CA   . ASP   A 1 73  ? 15.15800 -12.15700 18.35900 1.000 16.42000 ?  69  ASP   A CA   1 
ATOM   479  C  C    . ASP   A 1 73  ? 14.36400 -10.86900 18.56400 1.000 18.52000 ?  69  ASP   A C    1 
ATOM   480  O  O    . ASP   A 1 73  ? 13.38100 -10.86900 19.31000 1.000 16.02000 ?  69  ASP   A O    1 
ATOM   481  C  CB   . ASP   A 1 73  ? 16.18900 -12.29400 19.48200 1.000 17.78000 ?  69  ASP   A CB   1 
ATOM   482  C  CG   . ASP   A 1 73  ? 16.93400 -13.61200 19.42100 1.000 25.29000 ?  69  ASP   A CG   1 
ATOM   483  O  OD1  . ASP   A 1 73  ? 16.28800 -14.62700 19.09500 1.000 26.37000 ?  69  ASP   A OD1  1 
ATOM   484  O  OD2  . ASP   A 1 73  ? 18.15600 -13.63000 19.68000 1.000 25.20000 ?  69  ASP   A OD2  1 
ATOM   485  N  N    . ALA   A 1 74  ? 14.76000 -9.77700  17.91200 1.000 18.08000 ?  70  ALA   A N    1 
ATOM   486  C  CA   . ALA   A 1 74  ? 14.09600 -8.48900  18.08100 1.000 13.62000 ?  70  ALA   A CA   1 
ATOM   487  C  C    . ALA   A 1 74  ? 14.44100 -7.61400  16.88500 1.000 13.39000 ?  70  ALA   A C    1 
ATOM   488  O  O    . ALA   A 1 74  ? 15.35600 -7.91500  16.11200 1.000 14.54000 ?  70  ALA   A O    1 
ATOM   489  C  CB   . ALA   A 1 74  ? 14.50100 -7.81100  19.39800 1.000 15.51000 ?  70  ALA   A CB   1 
ATOM   490  N  N    . VAL   A 1 75  ? 13.69800 -6.51200  16.75500 1.000 14.28000 ?  71  VAL   A N    1 
ATOM   491  C  CA   . VAL   A 1 75  ? 13.82000 -5.58900  15.63000 1.000 11.85000 ?  71  VAL   A CA   1 
ATOM   492  C  C    . VAL   A 1 75  ? 13.90100 -4.15900  16.15200 1.000 11.04000 ?  71  VAL   A C    1 
ATOM   493  O  O    . VAL   A 1 75  ? 13.14200 -3.77100  17.04500 1.000 12.59000 ?  71  VAL   A O    1 
ATOM   494  C  CB   . VAL   A 1 75  ? 12.62400 -5.73100  14.66100 1.000 13.61000 ?  71  VAL   A CB   1 
ATOM   495  C  CG1  . VAL   A 1 75  ? 12.69700 -4.68900  13.54600 1.000 14.83000 ?  71  VAL   A CG1  1 
ATOM   496  C  CG2  . VAL   A 1 75  ? 12.56600 -7.14600  14.07800 1.000 12.80000 ?  71  VAL   A CG2  1 
ATOM   497  N  N    A ILE   A 1 76  ? 14.83100 -3.39100  15.59800 0.300 11.55000 ?  72  ILE   A N    1 
ATOM   498  N  N    B ILE   A 1 76  ? 14.80500 -3.36700  15.57900 0.700 11.51000 ?  72  ILE   A N    1 
ATOM   499  C  CA   A ILE   A 1 76  ? 14.91800 -1.95500  15.81600 0.300 11.39000 ?  72  ILE   A CA   1 
ATOM   500  C  CA   B ILE   A 1 76  ? 14.90300 -1.94000  15.86400 0.700 11.33000 ?  72  ILE   A CA   1 
ATOM   501  C  C    A ILE   A 1 76  ? 14.44300 -1.27300  14.54300 0.300 12.80000 ?  72  ILE   A C    1 
ATOM   502  C  C    B ILE   A 1 76  ? 14.57300 -1.18000  14.58700 0.700 12.98000 ?  72  ILE   A C    1 
ATOM   503  O  O    A ILE   A 1 76  ? 14.75100 -1.72700  13.43400 0.300 12.04000 ?  72  ILE   A O    1 
ATOM   504  O  O    B ILE   A 1 76  ? 15.15000 -1.46300  13.52900 0.700 12.42000 ?  72  ILE   A O    1 
ATOM   505  C  CB   A ILE   A 1 76  ? 16.35800 -1.53200  16.17300 0.300 12.36000 ?  72  ILE   A CB   1 
ATOM   506  C  CB   B ILE   A 1 76  ? 16.30300 -1.55400  16.37900 0.700 12.37000 ?  72  ILE   A CB   1 
ATOM   507  C  CG1  A ILE   A 1 76  ? 16.83400 -2.28500  17.41700 0.300 13.63000 ?  72  ILE   A CG1  1 
ATOM   508  C  CG1  B ILE   A 1 76  ? 16.46400 -1.94700  17.85100 0.700 13.39000 ?  72  ILE   A CG1  1 
ATOM   509  C  CG2  A ILE   A 1 76  ? 16.46000 -0.02300  16.37800 0.300 12.81000 ?  72  ILE   A CG2  1 
ATOM   510  C  CG2  B ILE   A 1 76  ? 16.58800 -0.05900  16.16500 0.700 12.81000 ?  72  ILE   A CG2  1 
ATOM   511  C  CD1  A ILE   A 1 76  ? 16.10200 -1.89900  18.67900 0.300 13.21000 ?  72  ILE   A CD1  1 
ATOM   512  C  CD1  B ILE   A 1 76  ? 17.86700 -1.67600  18.39400 0.700 13.63000 ?  72  ILE   A CD1  1 
ATOM   513  N  N    . VAL   A 1 77  ? 13.67900 -0.19700  14.69400 1.000 9.84000  ?  73  VAL   A N    1 
ATOM   514  C  CA   . VAL   A 1 77  ? 13.22100 0.59700   13.55400 1.000 9.89000  ?  73  VAL   A CA   1 
ATOM   515  C  C    . VAL   A 1 77  ? 13.67000 2.03700   13.75000 1.000 12.31000 ?  73  VAL   A C    1 
ATOM   516  O  O    . VAL   A 1 77  ? 13.23000 2.71200   14.69500 1.000 11.93000 ?  73  VAL   A O    1 
ATOM   517  C  CB   . VAL   A 1 77  ? 11.69600 0.51000   13.36100 1.000 9.77000  ?  73  VAL   A CB   1 
ATOM   518  C  CG1  . VAL   A 1 77  ? 11.28200 1.24700   12.07700 1.000 10.81000 ?  73  VAL   A CG1  1 
ATOM   519  C  CG2  . VAL   A 1 77  ? 11.25100 -0.94500  13.27800 1.000 12.78000 ?  73  VAL   A CG2  1 
ATOM   520  N  N    . LEU   A 1 78  ? 14.52900 2.50700   12.84800 1.000 11.34000 ?  74  LEU   A N    1 
ATOM   521  C  CA   . LEU   A 1 78  ? 15.06500 3.86900   12.80700 1.000 12.44000 ?  74  LEU   A CA   1 
ATOM   522  C  C    . LEU   A 1 78  ? 14.92700 4.43100   11.39700 1.000 11.54000 ?  74  LEU   A C    1 
ATOM   523  O  O    . LEU   A 1 78  ? 15.78200 5.18100   10.91200 1.000 13.73000 ?  74  LEU   A O    1 
ATOM   524  C  CB   . LEU   A 1 78  ? 16.52000 3.91200   13.28300 1.000 12.35000 ?  74  LEU   A CB   1 
ATOM   525  C  CG   . LEU   A 1 78  ? 16.68500 3.81300   14.80700 1.000 14.07000 ?  74  LEU   A CG   1 
ATOM   526  C  CD1  . LEU   A 1 78  ? 18.14200 3.47700   15.20300 1.000 14.11000 ?  74  LEU   A CD1  1 
ATOM   527  C  CD2  . LEU   A 1 78  ? 16.22500 5.12200   15.45400 1.000 14.99000 ?  74  LEU   A CD2  1 
ATOM   528  N  N    . LEU   A 1 79  ? 13.83300 4.06700   10.73600 1.000 12.22000 ?  75  LEU   A N    1 
ATOM   529  C  CA   . LEU   A 1 79  ? 13.49200 4.60700   9.42800  1.000 13.87000 ?  75  LEU   A CA   1 
ATOM   530  C  C    . LEU   A 1 79  ? 13.19100 6.09900   9.51400  1.000 11.07000 ?  75  LEU   A C    1 
ATOM   531  O  O    . LEU   A 1 79  ? 12.77100 6.61100   10.55300 1.000 13.69000 ?  75  LEU   A O    1 
ATOM   532  C  CB   . LEU   A 1 79  ? 12.28700 3.86900   8.85300  1.000 12.94000 ?  75  LEU   A CB   1 
ATOM   533  C  CG   . LEU   A 1 79  ? 12.49000 2.38700   8.54200  1.000 14.11000 ?  75  LEU   A CG   1 
ATOM   534  C  CD1  . LEU   A 1 79  ? 11.14500 1.75800   8.21600  1.000 12.86000 ?  75  LEU   A CD1  1 
ATOM   535  C  CD2  . LEU   A 1 79  ? 13.47300 2.24000   7.37300  1.000 15.12000 ?  75  LEU   A CD2  1 
ATOM   536  N  N    . GLY   A 1 80  ? 13.41000 6.79200   8.40200  1.000 10.77000 ?  76  GLY   A N    1 
ATOM   537  C  CA   . GLY   A 1 80  ? 13.22100 8.23000   8.35300  1.000 11.49000 ?  76  GLY   A CA   1 
ATOM   538  C  C    . GLY   A 1 80  ? 13.38100 8.69700   6.92500  1.000 13.11000 ?  76  GLY   A C    1 
ATOM   539  O  O    . GLY   A 1 80  ? 13.60400 7.90000   6.01200  1.000 15.28000 ?  76  GLY   A O    1 
ATOM   540  N  N    . THR   A 1 81  ? 13.28600 10.01500  6.74200  1.000 10.85000 ?  77  THR   A N    1 
ATOM   541  C  CA   . THR   A 1 81  ? 13.27100 10.62200  5.41400  1.000 13.09000 ?  77  THR   A CA   1 
ATOM   542  C  C    . THR   A 1 81  ? 14.46700 11.53300  5.19400  1.000 13.77000 ?  77  THR   A C    1 
ATOM   543  O  O    . THR   A 1 81  ? 14.45900 12.33700  4.25100  1.000 16.32000 ?  77  THR   A O    1 
ATOM   544  C  CB   . THR   A 1 81  ? 11.97300 11.40300  5.20700  1.000 16.13000 ?  77  THR   A CB   1 
ATOM   545  O  OG1  . THR   A 1 81  ? 11.90600 12.46500  6.16500  1.000 16.61000 ?  77  THR   A OG1  1 
ATOM   546  C  CG2  . THR   A 1 81  ? 10.79200 10.50200  5.41400  1.000 17.38000 ?  77  THR   A CG2  1 
ATOM   547  N  N    . ARG   A 1 82  ? 15.47500 11.42300  6.06600  1.000 13.97000 ?  78  ARG   A N    1 
ATOM   548  C  CA   . ARG   A 1 82  ? 16.64600 12.33400  6.04400  1.000 15.34000 ?  78  ARG   A CA   1 
ATOM   549  C  C    . ARG   A 1 82  ? 16.13700 13.78800  6.10600  1.000 16.76000 ?  78  ARG   A C    1 
ATOM   550  O  O    . ARG   A 1 82  ? 15.43700 14.12300  7.06900  1.000 22.30000 ?  78  ARG   A O    1 
ATOM   551  C  CB   . ARG   A 1 82  ? 17.59200 11.95000  4.90000  1.000 16.96000 ?  78  ARG   A CB   1 
ATOM   552  C  CG   . ARG   A 1 82  ? 18.22200 10.57600  5.07500  1.000 17.92000 ?  78  ARG   A CG   1 
ATOM   553  C  CD   . ARG   A 1 82  ? 19.41700 10.36400  4.17100  1.000 17.70000 ?  78  ARG   A CD   1 
ATOM   554  N  NE   . ARG   A 1 82  ? 20.05200 9.08000   4.40300  1.000 15.01000 ?  78  ARG   A NE   1 
ATOM   555  C  CZ   . ARG   A 1 82  ? 21.03700 8.87100   5.26600  1.000 18.37000 ?  78  ARG   A CZ   1 
ATOM   556  N  NH1  . ARG   A 1 82  ? 21.51500 9.86600   5.99200  1.000 16.58000 ?  78  ARG   A NH1  1 
ATOM   557  N  NH2  . ARG   A 1 82  ? 21.54800 7.66300   5.39800  1.000 14.01000 ?  78  ARG   A NH2  1 
ATOM   558  N  N    . ASN   A 1 83  ? 16.49000 14.61100  5.13700  1.000 17.44000 ?  79  ASN   A N    1 
ATOM   559  C  CA   . ASN   A 1 83  ? 16.05100 16.01300  5.27500  1.000 16.64000 ?  79  ASN   A CA   1 
ATOM   560  C  C    . ASN   A 1 83  ? 14.78100 16.27400  4.44900  1.000 14.42000 ?  79  ASN   A C    1 
ATOM   561  O  O    . ASN   A 1 83  ? 14.39200 17.41700  4.35500  1.000 15.55000 ?  79  ASN   A O    1 
ATOM   562  C  CB   . ASN   A 1 83  ? 17.19000 16.96700  4.93600  1.000 24.30000 ?  79  ASN   A CB   1 
ATOM   563  C  CG   . ASN   A 1 83  ? 18.11600 17.14600  6.12100  1.000 38.19000 ?  79  ASN   A CG   1 
ATOM   564  O  OD1  . ASN   A 1 83  ? 17.73000 17.72400  7.13400  1.000 36.38000 ?  79  ASN   A OD1  1 
ATOM   565  N  ND2  . ASN   A 1 83  ? 19.31800 16.61100  6.02300  1.000 33.09000 ?  79  ASN   A ND2  1 
ATOM   566  N  N    . ASP   A 1 84  ? 14.17600 15.22500  3.90800  1.000 11.51000 ?  80  ASP   A N    1 
ATOM   567  C  CA   . ASP   A 1 84  ? 13.02300 15.43800  3.04200  1.000 14.25000 ?  80  ASP   A CA   1 
ATOM   568  C  C    . ASP   A 1 84  ? 11.75500 15.52200  3.88600  1.000 16.37000 ?  80  ASP   A C    1 
ATOM   569  O  O    . ASP   A 1 84  ? 11.37500 14.54700  4.53800  1.000 15.60000 ?  80  ASP   A O    1 
ATOM   570  C  CB   . ASP   A 1 84  ? 12.91200 14.30500  2.02300  1.000 15.80000 ?  80  ASP   A CB   1 
ATOM   571  C  CG   . ASP   A 1 84  ? 11.84200 14.56100  0.97500  1.000 19.31000 ?  80  ASP   A CG   1 
ATOM   572  O  OD1  . ASP   A 1 84  ? 11.14000 15.58900  1.05800  1.000 19.09000 ?  80  ASP   A OD1  1 
ATOM   573  O  OD2  . ASP   A 1 84  ? 11.71000 13.73300  0.05000  1.000 23.13000 ?  80  ASP   A OD2  1 
ATOM   574  N  N    . LEU   A 1 85  ? 11.09400 16.67300  3.86300  1.000 14.29000 ?  81  LEU   A N    1 
ATOM   575  C  CA   . LEU   A 1 85  ? 9.90500  16.86700  4.68200  1.000 13.89000 ?  81  LEU   A CA   1 
ATOM   576  C  C    . LEU   A 1 85  ? 8.61100  16.75900  3.88400  1.000 16.62000 ?  81  LEU   A C    1 
ATOM   577  O  O    . LEU   A 1 85  ? 7.54400  17.10300  4.40500  1.000 15.66000 ?  81  LEU   A O    1 
ATOM   578  C  CB   . LEU   A 1 85  ? 9.98100  18.21600  5.39100  1.000 18.32000 ?  81  LEU   A CB   1 
ATOM   579  C  CG   . LEU   A 1 85  ? 11.18100 18.36500  6.33600  1.000 20.29000 ?  81  LEU   A CG   1 
ATOM   580  C  CD1  . LEU   A 1 85  ? 11.14600 19.73000  7.00900  1.000 22.97000 ?  81  LEU   A CD1  1 
ATOM   581  C  CD2  . LEU   A 1 85  ? 11.19600 17.25700  7.38200  1.000 20.47000 ?  81  LEU   A CD2  1 
ATOM   582  N  N    . SER   A 1 86  ? 8.68300  16.25100  2.65400  1.000 14.54000 ?  82  SER   A N    1 
ATOM   583  C  CA   . SER   A 1 86  ? 7.51300  16.05500  1.81000  1.000 15.13000 ?  82  SER   A CA   1 
ATOM   584  C  C    . SER   A 1 86  ? 6.57100  14.99600  2.38600  1.000 16.47000 ?  82  SER   A C    1 
ATOM   585  O  O    . SER   A 1 86  ? 6.97900  14.15200  3.18500  1.000 16.77000 ?  82  SER   A O    1 
ATOM   586  C  CB   . SER   A 1 86  ? 7.95600  15.61900  0.41100  1.000 17.59000 ?  82  SER   A CB   1 
ATOM   587  O  OG   . SER   A 1 86  ? 8.80300  16.59100  -0.17100 1.000 26.47000 ?  82  SER   A OG   1 
ATOM   588  N  N    . PRO   A 1 87  ? 5.30700  14.99700  1.95500  1.000 18.71000 ?  83  PRO   A N    1 
ATOM   589  C  CA   . PRO   A 1 87  ? 4.40900  13.89200  2.30800  1.000 18.04000 ?  83  PRO   A CA   1 
ATOM   590  C  C    . PRO   A 1 87  ? 5.02500  12.54800  1.94300  1.000 17.38000 ?  83  PRO   A C    1 
ATOM   591  O  O    . PRO   A 1 87  ? 5.74500  12.41500  0.94500  1.000 17.81000 ?  83  PRO   A O    1 
ATOM   592  C  CB   . PRO   A 1 87  ? 3.15000  14.18300  1.48100  1.000 16.96000 ?  83  PRO   A CB   1 
ATOM   593  C  CG   . PRO   A 1 87  ? 3.16500  15.67200  1.32600  1.000 19.88000 ?  83  PRO   A CG   1 
ATOM   594  C  CD   . PRO   A 1 87  ? 4.61700  16.04800  1.18600  1.000 19.98000 ?  83  PRO   A CD   1 
ATOM   595  N  N    . THR   A 1 88  ? 4.76500  11.55100  2.78000  1.000 17.22000 ?  84  THR   A N    1 
ATOM   596  C  CA   . THR   A 1 88  ? 5.40900  10.25900  2.58900  1.000 15.88000 ?  84  THR   A CA   1 
ATOM   597  C  C    . THR   A 1 88  ? 4.58000  9.19100   3.27400  1.000 13.82000 ?  84  THR   A C    1 
ATOM   598  O  O    . THR   A 1 88  ? 3.86800  9.46500   4.24600  1.000 13.02000 ?  84  THR   A O    1 
ATOM   599  C  CB   . THR   A 1 88  ? 6.84300  10.24200  3.14700  1.000 16.37000 ?  84  THR   A CB   1 
ATOM   600  O  OG1  . THR   A 1 88  ? 7.45600  8.97700   2.86100  1.000 16.83000 ?  84  THR   A OG1  1 
ATOM   601  C  CG2  . THR   A 1 88  ? 6.83200  10.46100  4.65700  1.000 18.03000 ?  84  THR   A CG2  1 
ATOM   602  N  N    . THR   A 1 89  ? 4.68900  7.96400   2.76000  1.000 14.21000 ?  85  THR   A N    1 
ATOM   603  C  CA   . THR   A 1 89  ? 4.18100  6.79500   3.46400  1.000 14.44000 ?  85  THR   A CA   1 
ATOM   604  C  C    . THR   A 1 89  ? 5.26300  5.73100   3.62100  1.000 15.99000 ?  85  THR   A C    1 
ATOM   605  O  O    . THR   A 1 89  ? 4.94400  4.57200   3.89900  1.000 16.48000 ?  85  THR   A O    1 
ATOM   606  C  CB   . THR   A 1 89  ? 2.96200  6.20900   2.74700  1.000 16.23000 ?  85  THR   A CB   1 
ATOM   607  O  OG1  . THR   A 1 89  ? 3.31700  5.89900   1.38900  1.000 19.89000 ?  85  THR   A OG1  1 
ATOM   608  C  CG2  . THR   A 1 89  ? 1.78600  7.21200   2.76100  1.000 18.59000 ?  85  THR   A CG2  1 
ATOM   609  N  N    . VAL   A 1 90  ? 6.53900  6.09900   3.46500  1.000 15.58000 ?  86  VAL   A N    1 
ATOM   610  C  CA   . VAL   A 1 90  ? 7.59400  5.08700   3.48900  1.000 16.87000 ?  86  VAL   A CA   1 
ATOM   611  C  C    . VAL   A 1 90  ? 7.67600  4.43100   4.86000  1.000 14.59000 ?  86  VAL   A C    1 
ATOM   612  O  O    . VAL   A 1 90  ? 7.85500  3.21200   4.97300  1.000 16.55000 ?  86  VAL   A O    1 
ATOM   613  C  CB   . VAL   A 1 90  ? 8.95600  5.68200   3.06700  1.000 19.46000 ?  86  VAL   A CB   1 
ATOM   614  C  CG1  . VAL   A 1 90  ? 9.38300  6.82500   3.98600  1.000 22.29000 ?  86  VAL   A CG1  1 
ATOM   615  C  CG2  . VAL   A 1 90  ? 10.02000 4.60800   3.09400  1.000 17.26000 ?  86  VAL   A CG2  1 
ATOM   616  N  N    . MET   A 1 91  ? 7.52400  5.22100   5.92600  1.000 12.48000 ?  87  MET   A N    1 
ATOM   617  C  CA   . MET   A 1 91  ? 7.70300  4.66800   7.26400  1.000 15.38000 ?  87  MET   A CA   1 
ATOM   618  C  C    . MET   A 1 91  ? 6.52800  3.78400   7.66500  1.000 13.11000 ?  87  MET   A C    1 
ATOM   619  O  O    . MET   A 1 91  ? 6.72800  2.71500   8.25400  1.000 15.26000 ?  87  MET   A O    1 
ATOM   620  C  CB   . MET   A 1 91  ? 7.90200  5.79500   8.27700  1.000 15.16000 ?  87  MET   A CB   1 
ATOM   621  C  CG   . MET   A 1 91  ? 9.18600  6.58600   8.02800  1.000 13.67000 ?  87  MET   A CG   1 
ATOM   622  S  SD   . MET   A 1 91  ? 9.44100  7.89700   9.25200  1.000 18.51000 ?  87  MET   A SD   1 
ATOM   623  C  CE   . MET   A 1 91  ? 8.27300  9.12600   8.67800  1.000 17.93000 ?  87  MET   A CE   1 
ATOM   624  N  N    . SER   A 1 92  ? 5.29800  4.20100   7.35000  1.000 11.51000 ?  88  SER   A N    1 
ATOM   625  C  CA   . SER   A 1 92  ? 4.13700  3.39600   7.72400  1.000 15.13000 ?  88  SER   A CA   1 
ATOM   626  C  C    . SER   A 1 92  ? 4.01700  2.14500   6.85200  1.000 16.03000 ?  88  SER   A C    1 
ATOM   627  O  O    . SER   A 1 92  ? 3.70300  1.05900   7.35900  1.000 15.37000 ?  88  SER   A O    1 
ATOM   628  C  CB   . SER   A 1 92  ? 2.86400  4.23800   7.64300  1.000 14.06000 ?  88  SER   A CB   1 
ATOM   629  O  OG   . SER   A 1 92  ? 2.63200  4.72600   6.33000  1.000 19.42000 ?  88  SER   A OG   1 
ATOM   630  N  N    . GLU   A 1 93  ? 4.26600  2.27600   5.54600  1.000 16.63000 ?  89  GLU   A N    1 
ATOM   631  C  CA   . GLU   A 1 93  ? 4.29100  1.10300   4.67600  1.000 17.79000 ?  89  GLU   A CA   1 
ATOM   632  C  C    . GLU   A 1 93  ? 5.44600  0.17400   5.03200  1.000 19.03000 ?  89  GLU   A C    1 
ATOM   633  O  O    . GLU   A 1 93  ? 5.28300  -1.05500  5.04100  1.000 15.41000 ?  89  GLU   A O    1 
ATOM   634  C  CB   . GLU   A 1 93  ? 4.37200  1.53800   3.21200  1.000 20.81000 ?  89  GLU   A CB   1 
ATOM   635  C  CG   . GLU   A 1 93  ? 3.10700  2.21600   2.72500  1.000 27.20000 ?  89  GLU   A CG   1 
ATOM   636  C  CD   . GLU   A 1 93  ? 1.89400  1.31000   2.84900  1.000 40.86000 ?  89  GLU   A CD   1 
ATOM   637  O  OE1  . GLU   A 1 93  ? 1.89500  0.23700   2.20800  1.000 48.59000 ?  89  GLU   A OE1  1 
ATOM   638  O  OE2  . GLU   A 1 93  ? 0.95100  1.65600   3.60100  1.000 39.89000 ?  89  GLU   A OE2  1 
ATOM   639  N  N    . GLY   A 1 94  ? 6.62000  0.73500   5.32200  1.000 16.34000 ?  90  GLY   A N    1 
ATOM   640  C  CA   . GLY   A 1 94  ? 7.71100  -0.09000  5.82200  1.000 14.87000 ?  90  GLY   A CA   1 
ATOM   641  C  C    . GLY   A 1 94  ? 7.33600  -0.81300  7.10200  1.000 16.66000 ?  90  GLY   A C    1 
ATOM   642  O  O    . GLY   A 1 94  ? 7.63500  -2.00000  7.26900  1.000 13.97000 ?  90  GLY   A O    1 
ATOM   643  N  N    . ALA   A 1 95  ? 6.65900  -0.11100  8.01500  1.000 11.94000 ?  91  ALA   A N    1 
ATOM   644  C  CA   . ALA   A 1 95  ? 6.22600  -0.74200  9.26000  1.000 13.83000 ?  91  ALA   A CA   1 
ATOM   645  C  C    . ALA   A 1 95  ? 5.23200  -1.87300  9.01000  1.000 15.71000 ?  91  ALA   A C    1 
ATOM   646  O  O    . ALA   A 1 95  ? 5.28800  -2.91400  9.68000  1.000 14.68000 ?  91  ALA   A O    1 
ATOM   647  C  CB   . ALA   A 1 95  ? 5.61400  0.30500   10.19400 1.000 14.64000 ?  91  ALA   A CB   1 
ATOM   648  N  N    . ARG   A 1 96  ? 4.30200  -1.68600  8.06800  1.000 12.96000 ?  92  ARG   A N    1 
ATOM   649  C  CA   . ARG   A 1 96  ? 3.39000  -2.77100  7.71400  1.000 16.30000 ?  92  ARG   A CA   1 
ATOM   650  C  C    . ARG   A 1 96  ? 4.15700  -4.01600  7.29300  1.000 15.10000 ?  92  ARG   A C    1 
ATOM   651  O  O    . ARG   A 1 96  ? 3.84400  -5.12700  7.72900  1.000 15.95000 ?  92  ARG   A O    1 
ATOM   652  C  CB   . ARG   A 1 96  ? 2.44000  -2.33100  6.59700  1.000 20.52000 ?  92  ARG   A CB   1 
ATOM   653  C  CG   . ARG   A 1 96  ? 1.26700  -1.49200  7.08300  1.000 27.84000 ?  92  ARG   A CG   1 
ATOM   654  C  CD   . ARG   A 1 96  ? 0.29800  -1.14600  5.95500  1.000 33.34000 ?  92  ARG   A CD   1 
ATOM   655  N  NE   . ARG   A 1 96  ? -0.11900 0.24800   6.05200  1.000 46.62000 ?  92  ARG   A NE   1 
ATOM   656  C  CZ   . ARG   A 1 96  ? -1.09600 0.68700   6.83700  1.000 50.69000 ?  92  ARG   A CZ   1 
ATOM   657  N  NH1  . ARG   A 1 96  ? -1.81900 -0.14500  7.57100  1.000 48.64000 ?  92  ARG   A NH1  1 
ATOM   658  N  NH2  . ARG   A 1 96  ? -1.35000 1.99300   6.89300  1.000 47.41000 ?  92  ARG   A NH2  1 
ATOM   659  N  N    . ASN   A 1 97  ? 5.16800  -3.84700  6.43200  1.000 14.09000 ?  93  ASN   A N    1 
ATOM   660  C  CA   . ASN   A 1 97  ? 5.95800  -4.99100  5.97600  1.000 17.58000 ?  93  ASN   A CA   1 
ATOM   661  C  C    . ASN   A 1 97  ? 6.73600  -5.62200  7.12400  1.000 11.86000 ?  93  ASN   A C    1 
ATOM   662  O  O    . ASN   A 1 97  ? 6.86100  -6.85100  7.19800  1.000 16.11000 ?  93  ASN   A O    1 
ATOM   663  C  CB   . ASN   A 1 97  ? 6.91500  -4.56100  4.86800  1.000 14.84000 ?  93  ASN   A CB   1 
ATOM   664  C  CG   . ASN   A 1 97  ? 6.19900  -4.28300  3.56000  1.000 15.73000 ?  93  ASN   A CG   1 
ATOM   665  O  OD1  . ASN   A 1 97  ? 5.12900  -4.83600  3.30000  1.000 20.11000 ?  93  ASN   A OD1  1 
ATOM   666  N  ND2  . ASN   A 1 97  ? 6.79300  -3.43600  2.72400  1.000 16.95000 ?  93  ASN   A ND2  1 
ATOM   667  N  N    . ILE   A 1 98  ? 7.26000  -4.80100  8.03300  1.000 13.42000 ?  94  ILE   A N    1 
ATOM   668  C  CA   . ILE   A 1 98  ? 8.00400  -5.33200  9.17100  1.000 11.73000 ?  94  ILE   A CA   1 
ATOM   669  C  C    . ILE   A 1 98  ? 7.07900  -6.13300  10.08000 1.000 13.08000 ?  94  ILE   A C    1 
ATOM   670  O  O    . ILE   A 1 98  ? 7.40100  -7.26000  10.47800 1.000 14.49000 ?  94  ILE   A O    1 
ATOM   671  C  CB   . ILE   A 1 98  ? 8.70100  -4.19300  9.94000  1.000 11.03000 ?  94  ILE   A CB   1 
ATOM   672  C  CG1  . ILE   A 1 98  ? 9.84200  -3.60700  9.11000  1.000 13.73000 ?  94  ILE   A CG1  1 
ATOM   673  C  CG2  . ILE   A 1 98  ? 9.20800  -4.69900  11.29000 1.000 12.73000 ?  94  ILE   A CG2  1 
ATOM   674  C  CD1  . ILE   A 1 98  ? 10.38200 -2.25500  9.64800  1.000 14.89000 ?  94  ILE   A CD1  1 
ATOM   675  N  N    . VAL   A 1 99  ? 5.90600  -5.57900  10.39900 1.000 12.97000 ?  95  VAL   A N    1 
ATOM   676  C  CA   . VAL   A 1 99  ? 4.96500  -6.30000  11.25500 1.000 13.51000 ?  95  VAL   A CA   1 
ATOM   677  C  C    . VAL   A 1 99  ? 4.59400  -7.63600  10.63000 1.000 13.99000 ?  95  VAL   A C    1 
ATOM   678  O  O    . VAL   A 1 99  ? 4.54800  -8.67000  11.30800 1.000 16.65000 ?  95  VAL   A O    1 
ATOM   679  C  CB   . VAL   A 1 99  ? 3.71200  -5.45100  11.52700 1.000 18.24000 ?  95  VAL   A CB   1 
ATOM   680  C  CG1  . VAL   A 1 99  ? 2.58800  -6.34900  12.04800 1.000 19.35000 ?  95  VAL   A CG1  1 
ATOM   681  C  CG2  . VAL   A 1 99  ? 4.03400  -4.37300  12.54000 1.000 15.94000 ?  95  VAL   A CG2  1 
ATOM   682  N  N    . ALA   A 1 100 ? 4.28700  -7.63100  9.33200  1.000 15.03000 ?  96  ALA   A N    1 
ATOM   683  C  CA   . ALA   A 1 100 ? 3.90100  -8.87500  8.67600  1.000 15.25000 ?  96  ALA   A CA   1 
ATOM   684  C  C    . ALA   A 1 100 ? 5.03200  -9.89200  8.74000  1.000 15.89000 ?  96  ALA   A C    1 
ATOM   685  O  O    . ALA   A 1 100 ? 4.80100  -11.07400 9.02600  1.000 18.02000 ?  96  ALA   A O    1 
ATOM   686  C  CB   . ALA   A 1 100 ? 3.49800  -8.60100  7.22300  1.000 19.47000 ?  96  ALA   A CB   1 
ATOM   687  N  N    . ALA   A 1 101 ? 6.26600  -9.44900  8.49000  1.000 12.36000 ?  97  ALA   A N    1 
ATOM   688  C  CA   . ALA   A 1 101 ? 7.39700  -10.37100 8.54900  1.000 15.57000 ?  97  ALA   A CA   1 
ATOM   689  C  C    . ALA   A 1 101 ? 7.62100  -10.89200 9.96900  1.000 18.23000 ?  97  ALA   A C    1 
ATOM   690  O  O    . ALA   A 1 101 ? 7.88000  -12.09000 10.16600 1.000 17.41000 ?  97  ALA   A O    1 
ATOM   691  C  CB   . ALA   A 1 101 ? 8.64900  -9.67500  8.01300  1.000 15.66000 ?  97  ALA   A CB   1 
ATOM   692  N  N    . MET   A 1 102 ? 7.53400  -10.01200 10.97500 1.000 13.93000 ?  98  MET   A N    1 
ATOM   693  C  CA   . MET   A 1 102 ? 7.69600  -10.47000 12.35400 1.000 14.05000 ?  98  MET   A CA   1 
ATOM   694  C  C    . MET   A 1 102 ? 6.63900  -11.50400 12.71400 1.000 18.02000 ?  98  MET   A C    1 
ATOM   695  O  O    . MET   A 1 102 ? 6.93400  -12.50000 13.38600 1.000 16.24000 ?  98  MET   A O    1 
ATOM   696  C  CB   . MET   A 1 102 ? 7.63200  -9.28500  13.31600 1.000 17.52000 ?  98  MET   A CB   1 
ATOM   697  C  CG   . MET   A 1 102 ? 8.82700  -8.36600  13.22500 1.000 13.25000 ?  98  MET   A CG   1 
ATOM   698  S  SD   . MET   A 1 102 ? 8.60600  -6.94000  14.32000 1.000 13.94000 ?  98  MET   A SD   1 
ATOM   699  C  CE   . MET   A 1 102 ? 8.75400  -7.71600  15.93300 1.000 15.47000 ?  98  MET   A CE   1 
ATOM   700  N  N    . LYS   A 1 103 ? 5.40100  -11.29200 12.27000 1.000 15.06000 ?  99  LYS   A N    1 
ATOM   701  C  CA   . LYS   A 1 103 ? 4.35900  -12.26300 12.57300 1.000 17.02000 ?  99  LYS   A CA   1 
ATOM   702  C  C    . LYS   A 1 103 ? 4.63900  -13.59500 11.89200 1.000 16.85000 ?  99  LYS   A C    1 
ATOM   703  O  O    . LYS   A 1 103 ? 4.54500  -14.65700 12.52200 1.000 19.25000 ?  99  LYS   A O    1 
ATOM   704  C  CB   . LYS   A 1 103 ? 3.00100  -11.70400 12.16200 1.000 16.98000 ?  99  LYS   A CB   1 
ATOM   705  C  CG   . LYS   A 1 103 ? 2.57200  -10.56600 13.07300 1.000 19.75000 ?  99  LYS   A CG   1 
ATOM   706  C  CD   . LYS   A 1 103 ? 1.10900  -10.22800 12.90800 1.000 24.83000 ?  99  LYS   A CD   1 
ATOM   707  C  CE   . LYS   A 1 103 ? 0.59900  -9.58400  14.18000 1.000 28.77000 ?  99  LYS   A CE   1 
ATOM   708  N  NZ   . LYS   A 1 103 ? -0.69600 -8.90000  13.97000 1.000 33.12000 ?  99  LYS   A NZ   1 
ATOM   709  N  N    . ALA   A 1 104 ? 5.02000  -13.55700 10.62000 1.000 15.51000 ?  100 ALA   A N    1 
ATOM   710  C  CA   . ALA   A 1 104 ? 5.29100  -14.79400 9.89500  1.000 15.93000 ?  100 ALA   A CA   1 
ATOM   711  C  C    . ALA   A 1 104 ? 6.40300  -15.60000 10.55500 1.000 16.18000 ?  100 ALA   A C    1 
ATOM   712  O  O    . ALA   A 1 104 ? 6.35800  -16.83700 10.57500 1.000 18.93000 ?  100 ALA   A O    1 
ATOM   713  C  CB   . ALA   A 1 104 ? 5.64600  -14.47600 8.44300  1.000 19.54000 ?  100 ALA   A CB   1 
ATOM   714  N  N    . HIS   A 1 105 ? 7.41200  -14.92100 11.09300 1.000 15.52000 ?  101 HIS   A N    1 
ATOM   715  C  CA   . HIS   A 1 105 ? 8.61100  -15.55900 11.62200 1.000 14.68000 ?  101 HIS   A CA   1 
ATOM   716  C  C    . HIS   A 1 105 ? 8.60400  -15.73900 13.13400 1.000 17.79000 ?  101 HIS   A C    1 
ATOM   717  O  O    . HIS   A 1 105 ? 9.57900  -16.26500 13.68800 1.000 18.51000 ?  101 HIS   A O    1 
ATOM   718  C  CB   . HIS   A 1 105 ? 9.83900  -14.74800 11.22700 1.000 16.49000 ?  101 HIS   A CB   1 
ATOM   719  C  CG   . HIS   A 1 105 ? 10.17700 -14.85900 9.78000  1.000 18.15000 ?  101 HIS   A CG   1 
ATOM   720  N  ND1  . HIS   A 1 105 ? 10.75300 -15.99200 9.24200  1.000 21.39000 ?  101 HIS   A ND1  1 
ATOM   721  C  CD2  . HIS   A 1 105 ? 10.02800 -13.98700 8.75600  1.000 17.51000 ?  101 HIS   A CD2  1 
ATOM   722  C  CE1  . HIS   A 1 105 ? 10.94200 -15.81300 7.94800  1.000 22.84000 ?  101 HIS   A CE1  1 
ATOM   723  N  NE2  . HIS   A 1 105 ? 10.52500 -14.60000 7.62900  1.000 21.87000 ?  101 HIS   A NE2  1 
ATOM   724  N  N    . GLY   A 1 106 ? 7.55700  -15.29400 13.81800 1.000 15.92000 ?  102 GLY   A N    1 
ATOM   725  C  CA   . GLY   A 1 106 ? 7.51500  -15.45600 15.25800 1.000 18.40000 ?  102 GLY   A CA   1 
ATOM   726  C  C    . GLY   A 1 106 ? 8.43900  -14.55600 16.05300 1.000 17.50000 ?  102 GLY   A C    1 
ATOM   727  O  O    . GLY   A 1 106 ? 8.78000  -14.89700 17.18400 1.000 20.48000 ?  102 GLY   A O    1 
ATOM   728  N  N    . VAL   A 1 107 ? 8.84900  -13.41200 15.49600 1.000 15.57000 ?  103 VAL   A N    1 
ATOM   729  C  CA   . VAL   A 1 107 ? 9.57800  -12.38100 16.23600 1.000 17.46000 ?  103 VAL   A CA   1 
ATOM   730  C  C    . VAL   A 1 107 ? 8.56700  -11.47700 16.93600 1.000 17.58000 ?  103 VAL   A C    1 
ATOM   731  O  O    . VAL   A 1 107 ? 7.62700  -10.98800 16.30200 1.000 14.92000 ?  103 VAL   A O    1 
ATOM   732  C  CB   . VAL   A 1 107 ? 10.48000 -11.56900 15.29100 1.000 17.24000 ?  103 VAL   A CB   1 
ATOM   733  C  CG1  . VAL   A 1 107 ? 11.37500 -10.59100 16.08300 1.000 14.27000 ?  103 VAL   A CG1  1 
ATOM   734  C  CG2  . VAL   A 1 107 ? 11.31800 -12.50600 14.43500 1.000 17.01000 ?  103 VAL   A CG2  1 
ATOM   735  N  N    . ASP   A 1 108 ? 8.74900  -11.24100 18.24500 1.000 17.26000 ?  104 ASP   A N    1 
ATOM   736  C  CA   . ASP   A 1 108 ? 7.70800  -10.54000 18.98700 1.000 18.18000 ?  104 ASP   A CA   1 
ATOM   737  C  C    . ASP   A 1 108 ? 8.10200  -9.17300  19.53900 1.000 21.27000 ?  104 ASP   A C    1 
ATOM   738  O  O    . ASP   A 1 108 ? 7.22400  -8.47100  20.04500 1.000 25.32000 ?  104 ASP   A O    1 
ATOM   739  C  CB   . ASP   A 1 108 ? 7.17500  -11.42200 20.13500 1.000 22.30000 ?  104 ASP   A CB   1 
ATOM   740  C  CG   . ASP   A 1 108 ? 8.18400  -11.64800 21.24900 1.000 33.03000 ?  104 ASP   A CG   1 
ATOM   741  O  OD1  . ASP   A 1 108 ? 9.33400  -11.15800 21.16900 1.000 35.56000 ?  104 ASP   A OD1  1 
ATOM   742  O  OD2  . ASP   A 1 108 ? 7.81300  -12.34200 22.22600 1.000 39.54000 ?  104 ASP   A OD2  1 
ATOM   743  N  N    . LYS   A 1 109 ? 9.36600  -8.75700  19.43200 1.000 14.88000 ?  105 LYS   A N    1 
ATOM   744  C  CA   . LYS   A 1 109 ? 9.85400  -7.54000  20.08400 1.000 14.62000 ?  105 LYS   A CA   1 
ATOM   745  C  C    . LYS   A 1 109 ? 10.29600 -6.53100  19.03100 1.000 14.72000 ?  105 LYS   A C    1 
ATOM   746  O  O    . LYS   A 1 109 ? 11.20600 -6.81700  18.24100 1.000 12.73000 ?  105 LYS   A O    1 
ATOM   747  C  CB   . LYS   A 1 109 ? 11.01300 -7.86300  21.02800 1.000 17.85000 ?  105 LYS   A CB   1 
ATOM   748  C  CG   . LYS   A 1 109 ? 11.65100 -6.65900  21.69100 1.000 16.49000 ?  105 LYS   A CG   1 
ATOM   749  C  CD   . LYS   A 1 109 ? 10.66100 -5.97900  22.62800 1.000 22.12000 ?  105 LYS   A CD   1 
ATOM   750  C  CE   . LYS   A 1 109 ? 11.36200 -5.08300  23.62200 1.000 21.63000 ?  105 LYS   A CE   1 
ATOM   751  N  NZ   . LYS   A 1 109 ? 11.34300 -5.64900  25.00900 1.000 20.12000 ?  105 LYS   A NZ   1 
ATOM   752  N  N    . VAL   A 1 110 ? 9.67000  -5.34800  19.03500 1.000 14.39000 ?  106 VAL   A N    1 
ATOM   753  C  CA   . VAL   A 1 110 ? 10.03500 -4.26700  18.12300 1.000 11.68000 ?  106 VAL   A CA   1 
ATOM   754  C  C    . VAL   A 1 110 ? 10.13900 -2.95500  18.89700 1.000 14.80000 ?  106 VAL   A C    1 
ATOM   755  O  O    . VAL   A 1 110 ? 9.23800  -2.59400  19.66300 1.000 13.39000 ?  106 VAL   A O    1 
ATOM   756  C  CB   . VAL   A 1 110 ? 9.05400  -4.13800  16.94200 1.000 14.32000 ?  106 VAL   A CB   1 
ATOM   757  C  CG1  . VAL   A 1 110 ? 7.60100  -4.02500  17.40200 1.000 14.60000 ?  106 VAL   A CG1  1 
ATOM   758  C  CG2  . VAL   A 1 110 ? 9.45700  -2.94800  16.04800 1.000 11.53000 ?  106 VAL   A CG2  1 
ATOM   759  N  N    . VAL   A 1 111 ? 11.25700 -2.26400  18.71300 1.000 12.01000 ?  107 VAL   A N    1 
ATOM   760  C  CA   . VAL   A 1 111 ? 11.53000 -0.95400  19.30400 1.000 10.43000 ?  107 VAL   A CA   1 
ATOM   761  C  C    . VAL   A 1 111 ? 11.62000 0.03000   18.15200 1.000 11.82000 ?  107 VAL   A C    1 
ATOM   762  O  O    . VAL   A 1 111 ? 12.51300 -0.08800  17.30700 1.000 12.95000 ?  107 VAL   A O    1 
ATOM   763  C  CB   . VAL   A 1 111 ? 12.84100 -0.95800  20.10300 1.000 10.97000 ?  107 VAL   A CB   1 
ATOM   764  C  CG1  . VAL   A 1 111 ? 13.06400 0.38600   20.77900 1.000 10.48000 ?  107 VAL   A CG1  1 
ATOM   765  C  CG2  . VAL   A 1 111 ? 12.85100 -2.08900  21.12600 1.000 14.59000 ?  107 VAL   A CG2  1 
ATOM   766  N  N    . ALA   A 1 112 ? 10.70400 0.98800   18.09500 1.000 10.65000 ?  108 ALA   A N    1 
ATOM   767  C  CA   . ALA   A 1 112 ? 10.55900 1.79800   16.89300 1.000 10.21000 ?  108 ALA   A CA   1 
ATOM   768  C  C    . ALA   A 1 112 ? 10.50600 3.27000   17.24500 1.000 12.33000 ?  108 ALA   A C    1 
ATOM   769  O  O    . ALA   A 1 112 ? 9.78100  3.67300   18.15700 1.000 10.90000 ?  108 ALA   A O    1 
ATOM   770  C  CB   . ALA   A 1 112 ? 9.29200  1.40900   16.10100 1.000 9.89000  ?  108 ALA   A CB   1 
ATOM   771  N  N    . CYS   A 1 113 ? 11.25400 4.06500   16.47900 1.000 9.94000  ?  109 CYS   A N    1 
ATOM   772  C  CA   . CYS   A 1 113 ? 11.37200 5.50000   16.69700 1.000 10.37000 ?  109 CYS   A CA   1 
ATOM   773  C  C    . CYS   A 1 113 ? 10.33700 6.25000   15.86300 1.000 13.70000 ?  109 CYS   A C    1 
ATOM   774  O  O    . CYS   A 1 113 ? 10.28500 6.08100   14.64000 1.000 15.72000 ?  109 CYS   A O    1 
ATOM   775  C  CB   . CYS   A 1 113 ? 12.79000 5.93800   16.32600 1.000 11.92000 ?  109 CYS   A CB   1 
ATOM   776  S  SG   . CYS   A 1 113 ? 13.10700 7.64200   16.74400 1.000 13.32000 ?  109 CYS   A SG   1 
ATOM   777  N  N    . THR   A 1 114 ? 9.56300  7.10800   16.53100 1.000 13.48000 ?  110 THR   A N    1 
ATOM   778  C  CA   . THR   A 1 114 ? 8.67700  8.03500   15.78800 1.000 13.61000 ?  110 THR   A CA   1 
ATOM   779  C  C    . THR   A 1 114 ? 9.13900  9.44200   16.19600 1.000 11.38000 ?  110 THR   A C    1 
ATOM   780  O  O    . THR   A 1 114 ? 10.21900 9.82400   15.79600 1.000 13.34000 ?  110 THR   A O    1 
ATOM   781  C  CB   . THR   A 1 114 ? 7.17900  7.77200   16.01900 1.000 12.26000 ?  110 THR   A CB   1 
ATOM   782  O  OG1  . THR   A 1 114 ? 6.92500  7.62400   17.41400 1.000 13.23000 ?  110 THR   A OG1  1 
ATOM   783  C  CG2  . THR   A 1 114 ? 6.67900  6.56400   15.25400 1.000 15.45000 ?  110 THR   A CG2  1 
ATOM   784  N  N    . SER   A 1 115 ? 8.36800  10.09800  17.04700 1.000 11.33000 ?  111 SER   A N    1 
ATOM   785  C  CA   . SER   A 1 115 ? 8.71900  11.46100  17.50000 1.000 12.57000 ?  111 SER   A CA   1 
ATOM   786  C  C    . SER   A 1 115 ? 7.84300  11.89500  18.67000 1.000 12.48000 ?  111 SER   A C    1 
ATOM   787  O  O    . SER   A 1 115 ? 6.72900  11.40900  18.79700 1.000 11.78000 ?  111 SER   A O    1 
ATOM   788  C  CB   . SER   A 1 115 ? 8.67900  12.50100  16.37100 1.000 17.75000 ?  111 SER   A CB   1 
ATOM   789  O  OG   . SER   A 1 115 ? 7.91100  13.63500  16.68900 1.000 15.93000 ?  111 SER   A OG   1 
ATOM   790  N  N    . ALA   A 1 116 ? 8.38900  12.82000  19.44800 1.000 12.11000 ?  112 ALA   A N    1 
ATOM   791  C  CA   . ALA   A 1 116 ? 7.64700  13.36900  20.59500 1.000 11.11000 ?  112 ALA   A CA   1 
ATOM   792  C  C    . ALA   A 1 116 ? 6.42500  14.16200  20.12100 1.000 13.26000 ?  112 ALA   A C    1 
ATOM   793  O  O    . ALA   A 1 116 ? 5.56300  14.40000  20.94100 1.000 13.84000 ?  112 ALA   A O    1 
ATOM   794  C  CB   . ALA   A 1 116 ? 8.55500  14.26700  21.35200 1.000 14.30000 ?  112 ALA   A CB   1 
ATOM   795  N  N    . PHE   A 1 117 ? 6.39700  14.59000  18.85700 1.000 12.62000 ?  113 PHE   A N    1 
ATOM   796  C  CA   . PHE   A 1 117 ? 5.18800  15.28000  18.41300 1.000 14.62000 ?  113 PHE   A CA   1 
ATOM   797  C  C    . PHE   A 1 117 ? 3.93500  14.42500  18.57100 1.000 17.24000 ?  113 PHE   A C    1 
ATOM   798  O  O    . PHE   A 1 117 ? 2.83400  14.97300  18.65800 1.000 14.31000 ?  113 PHE   A O    1 
ATOM   799  C  CB   . PHE   A 1 117 ? 5.32100  15.73200  16.94900 1.000 13.26000 ?  113 PHE   A CB   1 
ATOM   800  C  CG   . PHE   A 1 117 ? 6.29200  16.86100  16.74100 1.000 16.60000 ?  113 PHE   A CG   1 
ATOM   801  C  CD1  . PHE   A 1 117 ? 6.54200  17.79000  17.73900 1.000 17.02000 ?  113 PHE   A CD1  1 
ATOM   802  C  CD2  . PHE   A 1 117 ? 6.94800  17.00400  15.53600 1.000 18.38000 ?  113 PHE   A CD2  1 
ATOM   803  C  CE1  . PHE   A 1 117 ? 7.45000  18.83200  17.53000 1.000 17.37000 ?  113 PHE   A CE1  1 
ATOM   804  C  CE2  . PHE   A 1 117 ? 7.85500  18.03800  15.32800 1.000 17.13000 ?  113 PHE   A CE2  1 
ATOM   805  C  CZ   . PHE   A 1 117 ? 8.09800  18.95400  16.33000 1.000 14.92000 ?  113 PHE   A CZ   1 
ATOM   806  N  N    . LEU   A 1 118 ? 4.06200  13.09700  18.62200 1.000 11.67000 ?  114 LEU   A N    1 
ATOM   807  C  CA   . LEU   A 1 118 ? 2.87700  12.28400  18.85300 1.000 12.74000 ?  114 LEU   A CA   1 
ATOM   808  C  C    . LEU   A 1 118 ? 2.34100  12.45600  20.26700 1.000 16.21000 ?  114 LEU   A C    1 
ATOM   809  O  O    . LEU   A 1 118 ? 1.23000  12.00000  20.55600 1.000 19.42000 ?  114 LEU   A O    1 
ATOM   810  C  CB   . LEU   A 1 118 ? 3.18000  10.81000  18.56800 1.000 10.83000 ?  114 LEU   A CB   1 
ATOM   811  C  CG   . LEU   A 1 118 ? 3.01500  10.33700  17.12000 1.000 12.41000 ?  114 LEU   A CG   1 
ATOM   812  C  CD1  . LEU   A 1 118 ? 3.81400  11.21000  16.17400 1.000 15.33000 ?  114 LEU   A CD1  1 
ATOM   813  C  CD2  . LEU   A 1 118 ? 3.45000  8.87600   17.01000 1.000 13.81000 ?  114 LEU   A CD2  1 
ATOM   814  N  N    . LEU   A 1 119 ? 3.11200  13.09900  21.14300 1.000 14.65000 ?  115 LEU   A N    1 
ATOM   815  C  CA   . LEU   A 1 119 ? 2.69600  13.43200  22.50100 1.000 13.43000 ?  115 LEU   A CA   1 
ATOM   816  C  C    . LEU   A 1 119 ? 2.30200  14.89700  22.65800 1.000 15.67000 ?  115 LEU   A C    1 
ATOM   817  O  O    . LEU   A 1 119 ? 1.95200  15.30800  23.76700 1.000 19.49000 ?  115 LEU   A O    1 
ATOM   818  C  CB   . LEU   A 1 119 ? 3.83200  13.10800  23.48700 1.000 15.96000 ?  115 LEU   A CB   1 
ATOM   819  C  CG   . LEU   A 1 119 ? 4.32400  11.66100  23.46800 1.000 12.78000 ?  115 LEU   A CG   1 
ATOM   820  C  CD1  . LEU   A 1 119 ? 5.62900  11.55800  24.22500 1.000 16.69000 ?  115 LEU   A CD1  1 
ATOM   821  C  CD2  . LEU   A 1 119 ? 3.25000  10.75900  24.07600 1.000 18.01000 ?  115 LEU   A CD2  1 
ATOM   822  N  N    . TRP   A 1 120 ? 2.36300  15.65900  21.57600 1.000 15.73000 ?  116 TRP   A N    1 
ATOM   823  C  CA   . TRP   A 1 120 ? 2.06100  17.10500  21.64900 1.000 14.17000 ?  116 TRP   A CA   1 
ATOM   824  C  C    . TRP   A 1 120 ? 0.60100  17.45700  21.39000 1.000 18.64000 ?  116 TRP   A C    1 
ATOM   825  O  O    . TRP   A 1 120 ? -0.11000 16.64900  20.81400 1.000 18.09000 ?  116 TRP   A O    1 
ATOM   826  C  CB   . TRP   A 1 120 ? 2.86500  17.86300  20.59000 1.000 18.31000 ?  116 TRP   A CB   1 
ATOM   827  C  CG   . TRP   A 1 120 ? 4.28300  18.17900  20.93200 1.000 15.35000 ?  116 TRP   A CG   1 
ATOM   828  C  CD1  . TRP   A 1 120 ? 5.16200  17.42100  21.64400 1.000 16.07000 ?  116 TRP   A CD1  1 
ATOM   829  C  CD2  . TRP   A 1 120 ? 4.99000  19.36700  20.55100 1.000 15.69000 ?  116 TRP   A CD2  1 
ATOM   830  N  NE1  . TRP   A 1 120 ? 6.37000  18.05300  21.72700 1.000 18.04000 ?  116 TRP   A NE1  1 
ATOM   831  C  CE2  . TRP   A 1 120 ? 6.29400  19.25200  21.07100 1.000 19.65000 ?  116 TRP   A CE2  1 
ATOM   832  C  CE3  . TRP   A 1 120 ? 4.65000  20.50800  19.82200 1.000 19.12000 ?  116 TRP   A CE3  1 
ATOM   833  C  CZ2  . TRP   A 1 120 ? 7.25200  20.24400  20.88900 1.000 20.51000 ?  116 TRP   A CZ2  1 
ATOM   834  C  CZ3  . TRP   A 1 120 ? 5.59700  21.48900  19.64400 1.000 17.67000 ?  116 TRP   A CZ3  1 
ATOM   835  C  CH2  . TRP   A 1 120 ? 6.88200  21.35300  20.16600 1.000 18.09000 ?  116 TRP   A CH2  1 
ATOM   836  N  N    . ASP   A 1 121 ? 0.21000  18.64100  21.84900 1.000 17.94000 ?  117 ASP   A N    1 
ATOM   837  C  CA   . ASP   A 1 121 ? -1.08700 19.22000  21.46300 1.000 18.35000 ?  117 ASP   A CA   1 
ATOM   838  C  C    . ASP   A 1 121 ? -0.98700 19.40700  19.94900 1.000 17.60000 ?  117 ASP   A C    1 
ATOM   839  O  O    . ASP   A 1 121 ? -0.04800 20.05400  19.50600 1.000 20.21000 ?  117 ASP   A O    1 
ATOM   840  C  CB   . ASP   A 1 121 ? -1.23100 20.56300  22.17900 1.000 23.12000 ?  117 ASP   A CB   1 
ATOM   841  C  CG   . ASP   A 1 121 ? -2.41700 21.44300  21.82000 1.000 24.90000 ?  117 ASP   A CG   1 
ATOM   842  O  OD1  . ASP   A 1 121 ? -3.15900 21.11800  20.88500 1.000 21.96000 ?  117 ASP   A OD1  1 
ATOM   843  O  OD2  . ASP   A 1 121 ? -2.57800 22.46600  22.49900 1.000 26.31000 ?  117 ASP   A OD2  1 
ATOM   844  N  N    . PRO   A 1 122 ? -1.90100 18.83200  19.15500 1.000 17.60000 ?  118 PRO   A N    1 
ATOM   845  C  CA   . PRO   A 1 122 ? -1.80400 18.93000  17.70400 1.000 17.87000 ?  118 PRO   A CA   1 
ATOM   846  C  C    . PRO   A 1 122 ? -1.80600 20.36700  17.14700 1.000 20.14000 ?  118 PRO   A C    1 
ATOM   847  O  O    . PRO   A 1 122 ? -1.33700 20.56400  16.06100 1.000 18.01000 ?  118 PRO   A O    1 
ATOM   848  C  CB   . PRO   A 1 122 ? -3.03600 18.16700  17.20500 1.000 18.28000 ?  118 PRO   A CB   1 
ATOM   849  C  CG   . PRO   A 1 122 ? -3.96000 18.07900  18.39600 1.000 22.31000 ?  118 PRO   A CG   1 
ATOM   850  C  CD   . PRO   A 1 122 ? -3.04600 18.04300  19.59800 1.000 21.39000 ?  118 PRO   A CD   1 
ATOM   851  N  N    . THR   A 1 123 ? -2.35100 21.32300  17.90800 1.000 21.44000 ?  119 THR   A N    1 
ATOM   852  C  CA   . THR   A 1 123 ? -2.30000 22.69300  17.41900 1.000 18.37000 ?  119 THR   A CA   1 
ATOM   853  C  C    . THR   A 1 123 ? -0.90900 23.29300  17.52500 1.000 23.75000 ?  119 THR   A C    1 
ATOM   854  O  O    . THR   A 1 123 ? -0.68400 24.37300  16.97400 1.000 21.83000 ?  119 THR   A O    1 
ATOM   855  C  CB   . THR   A 1 123 ? -3.27600 23.60500  18.17500 1.000 23.84000 ?  119 THR   A CB   1 
ATOM   856  O  OG1  . THR   A 1 123 ? -2.86500 23.73200  19.54200 1.000 23.73000 ?  119 THR   A OG1  1 
ATOM   857  C  CG2  . THR   A 1 123 ? -4.67200 23.05200  18.11900 1.000 23.48000 ?  119 THR   A CG2  1 
ATOM   858  N  N    . LYS   A 1 124 ? 0.01600  22.63600  18.22500 1.000 18.60000 ?  120 LYS   A N    1 
ATOM   859  C  CA   . LYS   A 1 124 ? 1.34500  23.18400  18.45600 1.000 18.59000 ?  120 LYS   A CA   1 
ATOM   860  C  C    . LYS   A 1 124 ? 2.42200  22.55900  17.57500 1.000 15.94000 ?  120 LYS   A C    1 
ATOM   861  O  O    . LYS   A 1 124 ? 3.55900  23.05200  17.57600 1.000 18.68000 ?  120 LYS   A O    1 
ATOM   862  C  CB   . LYS   A 1 124 ? 1.73800  23.01600  19.92800 1.000 18.04000 ?  120 LYS   A CB   1 
ATOM   863  C  CG   . LYS   A 1 124 ? 0.76800  23.65300  20.91600 1.000 24.89000 ?  120 LYS   A CG   1 
ATOM   864  C  CD   . LYS   A 1 124 ? 0.70800  25.15100  20.73100 1.000 29.49000 ?  120 LYS   A CD   1 
ATOM   865  C  CE   . LYS   A 1 124 ? -0.38500 25.75400  21.60000 1.000 40.19000 ?  120 LYS   A CE   1 
ATOM   866  N  NZ   . LYS   A 1 124 ? -0.17900 25.46300  23.04800 1.000 46.64000 ?  120 LYS   A NZ   1 
ATOM   867  N  N    . VAL   A 1 125 ? 2.10300  21.50200  16.83800 1.000 16.10000 ?  121 VAL   A N    1 
ATOM   868  C  CA   . VAL   A 1 125 ? 3.09200  20.86300  15.95700 1.000 14.49000 ?  121 VAL   A CA   1 
ATOM   869  C  C    . VAL   A 1 125 ? 3.42700  21.81500  14.81200 1.000 15.95000 ?  121 VAL   A C    1 
ATOM   870  O  O    . VAL   A 1 125 ? 2.50700  22.30200  14.13300 1.000 16.54000 ?  121 VAL   A O    1 
ATOM   871  C  CB   . VAL   A 1 125 ? 2.55000  19.52900  15.42900 1.000 14.24000 ?  121 VAL   A CB   1 
ATOM   872  C  CG1  . VAL   A 1 125 ? 3.51000  18.89300  14.42400 1.000 15.02000 ?  121 VAL   A CG1  1 
ATOM   873  C  CG2  . VAL   A 1 125 ? 2.29700  18.56800  16.58500 1.000 14.58000 ?  121 VAL   A CG2  1 
ATOM   874  N  N    . PRO   A 1 126 ? 4.70000  22.11500  14.56200 1.000 16.92000 ?  122 PRO   A N    1 
ATOM   875  C  CA   . PRO   A 1 126 ? 5.05300  23.04100  13.46700 1.000 14.01000 ?  122 PRO   A CA   1 
ATOM   876  C  C    . PRO   A 1 126 ? 4.52100  22.54100  12.13600 1.000 12.32000 ?  122 PRO   A C    1 
ATOM   877  O  O    . PRO   A 1 126 ? 4.79000  21.39600  11.74400 1.000 13.10000 ?  122 PRO   A O    1 
ATOM   878  C  CB   . PRO   A 1 126 ? 6.59100  23.04600  13.48400 1.000 15.38000 ?  122 PRO   A CB   1 
ATOM   879  C  CG   . PRO   A 1 126 ? 6.94700  22.69100  14.89400 1.000 17.72000 ?  122 PRO   A CG   1 
ATOM   880  C  CD   . PRO   A 1 126 ? 5.87600  21.72100  15.35400 1.000 16.22000 ?  122 PRO   A CD   1 
ATOM   881  N  N    . PRO   A 1 127 ? 3.75500  23.36800  11.41800 1.000 12.89000 ?  123 PRO   A N    1 
ATOM   882  C  CA   . PRO   A 1 127 ? 3.21500  22.93300  10.12100 1.000 15.46000 ?  123 PRO   A CA   1 
ATOM   883  C  C    . PRO   A 1 127 ? 4.26200  22.37200  9.16800  1.000 14.34000 ?  123 PRO   A C    1 
ATOM   884  O  O    . PRO   A 1 127 ? 3.96200  21.42500  8.43100  1.000 15.69000 ?  123 PRO   A O    1 
ATOM   885  C  CB   . PRO   A 1 127 ? 2.56800  24.21900  9.57600  1.000 14.80000 ?  123 PRO   A CB   1 
ATOM   886  C  CG   . PRO   A 1 127 ? 2.14600  24.96000  10.80200 1.000 12.37000 ?  123 PRO   A CG   1 
ATOM   887  C  CD   . PRO   A 1 127 ? 3.25700  24.70600  11.80700 1.000 12.74000 ?  123 PRO   A CD   1 
ATOM   888  N  N    . ARG   A 1 128 ? 5.48900  22.90500  9.16600  1.000 13.16000 ?  124 ARG   A N    1 
ATOM   889  C  CA   . ARG   A 1 128 ? 6.49000  22.39800  8.22500  1.000 14.14000 ?  124 ARG   A CA   1 
ATOM   890  C  C    . ARG   A 1 128 ? 6.87500  20.95200  8.51500  1.000 15.40000 ?  124 ARG   A C    1 
ATOM   891  O  O    . ARG   A 1 128 ? 7.33300  20.24400  7.61100  1.000 17.04000 ?  124 ARG   A O    1 
ATOM   892  C  CB   . ARG   A 1 128 ? 7.72800  23.30200  8.25200  1.000 18.09000 ?  124 ARG   A CB   1 
ATOM   893  C  CG   . ARG   A 1 128 ? 8.79600  22.98800  7.21700  1.000 20.28000 ?  124 ARG   A CG   1 
ATOM   894  C  CD   . ARG   A 1 128 ? 8.27500  23.05900  5.77700  1.000 24.10000 ?  124 ARG   A CD   1 
ATOM   895  N  NE   . ARG   A 1 128 ? 7.51500  24.27400  5.51800  1.000 24.69000 ?  124 ARG   A NE   1 
ATOM   896  C  CZ   . ARG   A 1 128 ? 8.05700  25.43300  5.17000  1.000 29.39000 ?  124 ARG   A CZ   1 
ATOM   897  N  NH1  . ARG   A 1 128 ? 9.36500  25.55900  4.99100  1.000 27.84000 ?  124 ARG   A NH1  1 
ATOM   898  N  NH2  . ARG   A 1 128 ? 7.27000  26.49700  5.02200  1.000 27.85000 ?  124 ARG   A NH2  1 
ATOM   899  N  N    . LEU   A 1 129 ? 6.69100  20.48800  9.74500  1.000 13.20000 ?  125 LEU   A N    1 
ATOM   900  C  CA   . LEU   A 1 129 ? 6.99000  19.11200  10.10100 1.000 13.62000 ?  125 LEU   A CA   1 
ATOM   901  C  C    . LEU   A 1 129 ? 5.75000  18.22200  10.12200 1.000 12.22000 ?  125 LEU   A C    1 
ATOM   902  O  O    . LEU   A 1 129 ? 5.85500  17.05200  10.49400 1.000 13.45000 ?  125 LEU   A O    1 
ATOM   903  C  CB   . LEU   A 1 129 ? 7.69200  19.06900  11.45900 1.000 14.23000 ?  125 LEU   A CB   1 
ATOM   904  C  CG   . LEU   A 1 129 ? 9.01000  19.84900  11.51300 1.000 17.17000 ?  125 LEU   A CG   1 
ATOM   905  C  CD1  . LEU   A 1 129 ? 9.57200  19.86200  12.92200 1.000 18.16000 ?  125 LEU   A CD1  1 
ATOM   906  C  CD2  . LEU   A 1 129 ? 10.02100 19.25900  10.55300 1.000 19.25000 ?  125 LEU   A CD2  1 
ATOM   907  N  N    . GLN   A 1 130 ? 4.58300  18.73800  9.71900  1.000 11.77000 ?  126 GLN   A N    1 
ATOM   908  C  CA   . GLN   A 1 130 ? 3.34900  17.95600  9.84600  1.000 14.75000 ?  126 GLN   A CA   1 
ATOM   909  C  C    . GLN   A 1 130 ? 3.30300  16.77100  8.88200  1.000 12.34000 ?  126 GLN   A C    1 
ATOM   910  O  O    . GLN   A 1 130 ? 2.75900  15.72000  9.22400  1.000 11.80000 ?  126 GLN   A O    1 
ATOM   911  C  CB   . GLN   A 1 130 ? 2.12200  18.83800  9.61600  1.000 16.84000 ?  126 GLN   A CB   1 
ATOM   912  C  CG   . GLN   A 1 130 ? 0.82500  18.09200  9.88300  1.000 15.07000 ?  126 GLN   A CG   1 
ATOM   913  C  CD   . GLN   A 1 130 ? 0.61700  17.83800  11.35900 1.000 20.47000 ?  126 GLN   A CD   1 
ATOM   914  O  OE1  . GLN   A 1 130 ? 0.33300  18.77300  12.12100 1.000 22.30000 ?  126 GLN   A OE1  1 
ATOM   915  N  NE2  . GLN   A 1 130 ? 0.76000  16.57800  11.78200 1.000 13.63000 ?  126 GLN   A NE2  1 
ATOM   916  N  N    . ALA   A 1 131 ? 3.84500  16.91600  7.67200  1.000 11.66000 ?  127 ALA   A N    1 
ATOM   917  C  CA   . ALA   A 1 131 ? 3.72400  15.82400  6.70900  1.000 14.88000 ?  127 ALA   A CA   1 
ATOM   918  C  C    . ALA   A 1 131 ? 4.48400  14.59200  7.17600  1.000 14.85000 ?  127 ALA   A C    1 
ATOM   919  O  O    . ALA   A 1 131 ? 3.98100  13.45900  7.06900  1.000 15.17000 ?  127 ALA   A O    1 
ATOM   920  C  CB   . ALA   A 1 131 ? 4.21000  16.26200  5.32700  1.000 15.34000 ?  127 ALA   A CB   1 
ATOM   921  N  N    . VAL   A 1 132 ? 5.70000  14.78800  7.69200  1.000 14.27000 ?  128 VAL   A N    1 
ATOM   922  C  CA   . VAL   A 1 132 ? 6.43400  13.66500  8.26500  1.000 12.06000 ?  128 VAL   A CA   1 
ATOM   923  C  C    . VAL   A 1 132 ? 5.72400  13.14800  9.50500  1.000 9.31000  ?  128 VAL   A C    1 
ATOM   924  O  O    . VAL   A 1 132 ? 5.59600  11.93100  9.70500  1.000 12.13000 ?  128 VAL   A O    1 
ATOM   925  C  CB   . VAL   A 1 132 ? 7.88600  14.07600  8.56400  1.000 12.59000 ?  128 VAL   A CB   1 
ATOM   926  C  CG1  . VAL   A 1 132 ? 8.61500  12.97000  9.31800  1.000 12.85000 ?  128 VAL   A CG1  1 
ATOM   927  C  CG2  . VAL   A 1 132 ? 8.61500  14.38500  7.26500  1.000 15.39000 ?  128 VAL   A CG2  1 
ATOM   928  N  N    . THR   A 1 133 ? 5.24700  14.05800  10.36200 1.000 9.15000  ?  129 THR   A N    1 
ATOM   929  C  CA   . THR   A 1 133 ? 4.54800  13.62400  11.56900 1.000 12.56000 ?  129 THR   A CA   1 
ATOM   930  C  C    . THR   A 1 133 ? 3.32700  12.77600  11.22700 1.000 11.08000 ?  129 THR   A C    1 
ATOM   931  O  O    . THR   A 1 133 ? 3.03800  11.79200  11.91200 1.000 11.88000 ?  129 THR   A O    1 
ATOM   932  C  CB   . THR   A 1 133 ? 4.16300  14.84700  12.40000 1.000 10.96000 ?  129 THR   A CB   1 
ATOM   933  O  OG1  . THR   A 1 133 ? 5.36100  15.52500  12.78600 1.000 13.01000 ?  129 THR   A OG1  1 
ATOM   934  C  CG2  . THR   A 1 133 ? 3.39700  14.44500  13.65400 1.000 13.67000 ?  129 THR   A CG2  1 
ATOM   935  N  N    . ASP   A 1 134 ? 2.62300  13.12200  10.14500 1.000 12.22000 ?  130 ASP   A N    1 
ATOM   936  C  CA   . ASP   A 1 134 ? 1.46600  12.33600  9.72400  1.000 15.31000 ?  130 ASP   A CA   1 
ATOM   937  C  C    . ASP   A 1 134 ? 1.84900  10.88300  9.48600  1.000 12.78000 ?  130 ASP   A C    1 
ATOM   938  O  O    . ASP   A 1 134 ? 1.08700  9.96900   9.82100  1.000 12.09000 ?  130 ASP   A O    1 
ATOM   939  C  CB   . ASP   A 1 134 ? 0.85600  12.92400  8.44700  1.000 14.79000 ?  130 ASP   A CB   1 
ATOM   940  C  CG   . ASP   A 1 134 ? 0.00800  14.16100  8.70800  1.000 19.44000 ?  130 ASP   A CG   1 
ATOM   941  O  OD1  . ASP   A 1 134 ? -0.17500 14.56200  9.87300  1.000 17.52000 ?  130 ASP   A OD1  1 
ATOM   942  O  OD2  . ASP   A 1 134 ? -0.48300 14.75000  7.72700  1.000 19.34000 ?  130 ASP   A OD2  1 
ATOM   943  N  N    . ASP   A 1 135 ? 3.01900  10.64000  8.89700  1.000 11.24000 ?  131 ASP   A N    1 
ATOM   944  C  CA   . ASP   A 1 135 ? 3.37400  9.24600   8.67200  1.000 12.59000 ?  131 ASP   A CA   1 
ATOM   945  C  C    . ASP   A 1 135 ? 3.92200  8.58700   9.93000  1.000 12.19000 ?  131 ASP   A C    1 
ATOM   946  O  O    . ASP   A 1 135 ? 3.77400  7.37100   10.08600 1.000 11.73000 ?  131 ASP   A O    1 
ATOM   947  C  CB   . ASP   A 1 135 ? 4.36600  9.10100   7.51600  1.000 14.22000 ?  131 ASP   A CB   1 
ATOM   948  C  CG   . ASP   A 1 135 ? 4.27900  7.72800   6.87300  1.000 15.33000 ?  131 ASP   A CG   1 
ATOM   949  O  OD1  . ASP   A 1 135 ? 3.13300  7.28000   6.63300  1.000 11.98000 ?  131 ASP   A OD1  1 
ATOM   950  O  OD2  . ASP   A 1 135 ? 5.33500  7.10700   6.61700  1.000 15.54000 ?  131 ASP   A OD2  1 
ATOM   951  N  N    . HIS   A 1 136 ? 4.54600  9.35400   10.83500 1.000 13.81000 ?  132 HIS   A N    1 
ATOM   952  C  CA   . HIS   A 1 136 ? 4.84400  8.80400   12.16100 1.000 12.46000 ?  132 HIS   A CA   1 
ATOM   953  C  C    . HIS   A 1 136 ? 3.56800  8.32700   12.84600 1.000 13.77000 ?  132 HIS   A C    1 
ATOM   954  O  O    . HIS   A 1 136 ? 3.54800  7.25900   13.46600 1.000 13.07000 ?  132 HIS   A O    1 
ATOM   955  C  CB   . HIS   A 1 136 ? 5.53200  9.84600   13.05700 1.000 10.12000 ?  132 HIS   A CB   1 
ATOM   956  C  CG   . HIS   A 1 136 ? 6.97100  10.10200  12.72200 1.000 11.42000 ?  132 HIS   A CG   1 
ATOM   957  N  ND1  . HIS   A 1 136 ? 7.55100  11.34500  12.87800 1.000 12.23000 ?  132 HIS   A ND1  1 
ATOM   958  C  CD2  . HIS   A 1 136 ? 7.94800  9.28600   12.26000 1.000 11.75000 ?  132 HIS   A CD2  1 
ATOM   959  C  CE1  . HIS   A 1 136 ? 8.82200  11.28600  12.50800 1.000 11.92000 ?  132 HIS   A CE1  1 
ATOM   960  N  NE2  . HIS   A 1 136 ? 9.09000  10.04700  12.13800 1.000 10.51000 ?  132 HIS   A NE2  1 
ATOM   961  N  N    . ILE   A 1 137 ? 2.50200  9.12800   12.77300 1.000 12.91000 ?  133 ILE   A N    1 
ATOM   962  C  CA   . ILE   A 1 137 ? 1.21600  8.71200   13.34400 1.000 13.06000 ?  133 ILE   A CA   1 
ATOM   963  C  C    . ILE   A 1 137 ? 0.74900  7.41100   12.69800 1.000 12.12000 ?  133 ILE   A C    1 
ATOM   964  O  O    . ILE   A 1 137 ? 0.36200  6.45600   13.38300 1.000 12.19000 ?  133 ILE   A O    1 
ATOM   965  C  CB   . ILE   A 1 137 ? 0.17600  9.84000   13.18800 1.000 12.63000 ?  133 ILE   A CB   1 
ATOM   966  C  CG1  . ILE   A 1 137 ? 0.58200  11.03800  14.04200 1.000 13.83000 ?  133 ILE   A CG1  1 
ATOM   967  C  CG2  . ILE   A 1 137 ? -1.21000 9.38200   13.58500 1.000 13.21000 ?  133 ILE   A CG2  1 
ATOM   968  C  CD1  . ILE   A 1 137 ? -0.13400 12.31900  13.63200 1.000 17.46000 ?  133 ILE   A CD1  1 
ATOM   969  N  N    . ARG   A 1 138 ? 0.80200  7.34700   11.36800 1.000 13.32000 ?  134 ARG   A N    1 
ATOM   970  C  CA   . ARG   A 1 138 ? 0.38500  6.13800   10.66600 1.000 14.06000 ?  134 ARG   A CA   1 
ATOM   971  C  C    . ARG   A 1 138 ? 1.22200  4.93400   11.07700 1.000 15.37000 ?  134 ARG   A C    1 
ATOM   972  O  O    . ARG   A 1 138 ? 0.69000  3.83500   11.26600 1.000 12.73000 ?  134 ARG   A O    1 
ATOM   973  C  CB   . ARG   A 1 138 ? 0.46700  6.36800   9.15700  1.000 14.39000 ?  134 ARG   A CB   1 
ATOM   974  C  CG   . ARG   A 1 138 ? -0.67300 7.21400   8.62500  1.000 16.09000 ?  134 ARG   A CG   1 
ATOM   975  C  CD   . ARG   A 1 138 ? -0.64200 7.26100   7.10800  1.000 13.52000 ?  134 ARG   A CD   1 
ATOM   976  N  NE   . ARG   A 1 138 ? 0.47800  8.03000   6.58200  1.000 13.96000 ?  134 ARG   A NE   1 
ATOM   977  C  CZ   . ARG   A 1 138 ? 0.39900  9.31200   6.25000  1.000 13.55000 ?  134 ARG   A CZ   1 
ATOM   978  N  NH1  . ARG   A 1 138 ? -0.71300 10.01300  6.44800  1.000 15.90000 ?  134 ARG   A NH1  1 
ATOM   979  N  NH2  . ARG   A 1 138 ? 1.45400  9.90500   5.70600  1.000 15.28000 ?  134 ARG   A NH2  1 
ATOM   980  N  N    . MET   A 1 139 ? 2.53500  5.12500   11.22400 1.000 12.36000 ?  135 MET   A N    1 
ATOM   981  C  CA   . MET   A 1 139 ? 3.41800  4.01600   11.59000 1.000 12.17000 ?  135 MET   A CA   1 
ATOM   982  C  C    . MET   A 1 139 ? 3.14300  3.54800   13.00700 1.000 13.93000 ?  135 MET   A C    1 
ATOM   983  O  O    . MET   A 1 139 ? 3.10200  2.34200   13.28200 1.000 13.18000 ?  135 MET   A O    1 
ATOM   984  C  CB   . MET   A 1 139 ? 4.88100  4.45900   11.43600 1.000 13.33000 ?  135 MET   A CB   1 
ATOM   985  C  CG   . MET   A 1 139 ? 5.89400  3.57800   12.13000 1.000 13.56000 ?  135 MET   A CG   1 
ATOM   986  S  SD   . MET   A 1 139 ? 7.57000  4.29100   11.92400 1.000 25.55000 ?  135 MET   A SD   1 
ATOM   987  C  CE   . MET   A 1 139 ? 8.54000  3.20800   12.95900 1.000 27.56000 ?  135 MET   A CE   1 
ATOM   988  N  N    . HIS   A 1 140 ? 2.95900  4.49900   13.92000 1.000 11.14000 ?  136 HIS   A N    1 
ATOM   989  C  CA   . HIS   A 1 140 ? 2.66200  4.15600   15.30200 1.000 12.51000 ?  136 HIS   A CA   1 
ATOM   990  C  C    . HIS   A 1 140 ? 1.37300  3.35600   15.39300 1.000 15.56000 ?  136 HIS   A C    1 
ATOM   991  O  O    . HIS   A 1 140 ? 1.27300  2.40700   16.17800 1.000 16.78000 ?  136 HIS   A O    1 
ATOM   992  C  CB   . HIS   A 1 140 ? 2.56500  5.44400   16.11700 1.000 14.21000 ?  136 HIS   A CB   1 
ATOM   993  C  CG   . HIS   A 1 140 ? 2.18900  5.22200   17.54100 1.000 14.49000 ?  136 HIS   A CG   1 
ATOM   994  N  ND1  . HIS   A 1 140 ? 2.98700  4.52500   18.42100 1.000 15.40000 ?  136 HIS   A ND1  1 
ATOM   995  C  CD2  . HIS   A 1 140 ? 1.10400  5.62300   18.24900 1.000 18.09000 ?  136 HIS   A CD2  1 
ATOM   996  C  CE1  . HIS   A 1 140 ? 2.40200  4.48800   19.60600 1.000 18.25000 ?  136 HIS   A CE1  1 
ATOM   997  N  NE2  . HIS   A 1 140 ? 1.25900  5.14600   19.52900 1.000 20.91000 ?  136 HIS   A NE2  1 
ATOM   998  N  N    . LYS   A 1 141 ? 0.37900  3.72700   14.58700 1.000 12.73000 ?  137 LYS   A N    1 
ATOM   999  C  CA   . LYS   A 1 141 ? -0.89100 3.01100   14.56900 1.000 18.41000 ?  137 LYS   A CA   1 
ATOM   1000 C  C    . LYS   A 1 141 ? -0.69200 1.56600   14.12700 1.000 16.88000 ?  137 LYS   A C    1 
ATOM   1001 O  O    . LYS   A 1 141 ? -1.21600 0.63100   14.74900 1.000 17.64000 ?  137 LYS   A O    1 
ATOM   1002 C  CB   . LYS   A 1 141 ? -1.86200 3.73800   13.64200 1.000 18.52000 ?  137 LYS   A CB   1 
ATOM   1003 C  CG   . LYS   A 1 141 ? -3.23700 3.11600   13.55600 1.000 28.63000 ?  137 LYS   A CG   1 
ATOM   1004 C  CD   . LYS   A 1 141 ? -4.11000 3.87900   12.56900 1.000 32.58000 ?  137 LYS   A CD   1 
ATOM   1005 C  CE   . LYS   A 1 141 ? -5.44600 3.19000   12.36300 1.000 38.20000 ?  137 LYS   A CE   1 
ATOM   1006 N  NZ   . LYS   A 1 141 ? -6.15100 2.99000   13.65300 1.000 44.21000 ?  137 LYS   A NZ   1 
ATOM   1007 N  N    . VAL   A 1 142 ? 0.08600  1.36700   13.05800 1.000 17.36000 ?  138 VAL   A N    1 
ATOM   1008 C  CA   . VAL   A 1 142 ? 0.38900  0.01900   12.57500 1.000 15.51000 ?  138 VAL   A CA   1 
ATOM   1009 C  C    . VAL   A 1 142 ? 1.04600  -0.80500  13.67200 1.000 17.47000 ?  138 VAL   A C    1 
ATOM   1010 O  O    . VAL   A 1 142 ? 0.68800  -1.96800  13.90400 1.000 15.30000 ?  138 VAL   A O    1 
ATOM   1011 C  CB   . VAL   A 1 142 ? 1.28600  0.09300   11.32500 1.000 15.50000 ?  138 VAL   A CB   1 
ATOM   1012 C  CG1  . VAL   A 1 142 ? 1.92600  -1.27000  11.03800 1.000 15.03000 ?  138 VAL   A CG1  1 
ATOM   1013 C  CG2  . VAL   A 1 142 ? 0.48200  0.57100   10.11900 1.000 18.66000 ?  138 VAL   A CG2  1 
ATOM   1014 N  N    . LEU   A 1 143 ? 2.00400  -0.21400  14.38000 1.000 14.03000 ?  139 LEU   A N    1 
ATOM   1015 C  CA   . LEU   A 1 143 ? 2.73400  -0.98000  15.38500 1.000 12.14000 ?  139 LEU   A CA   1 
ATOM   1016 C  C    . LEU   A 1 143 ? 1.88900  -1.21100  16.63000 1.000 14.84000 ?  139 LEU   A C    1 
ATOM   1017 O  O    . LEU   A 1 143 ? 1.92600  -2.30100  17.22100 1.000 16.96000 ?  139 LEU   A O    1 
ATOM   1018 C  CB   . LEU   A 1 143 ? 4.04000  -0.26300  15.72800 1.000 12.21000 ?  139 LEU   A CB   1 
ATOM   1019 C  CG   . LEU   A 1 143 ? 5.01300  -0.19000  14.54400 1.000 15.11000 ?  139 LEU   A CG   1 
ATOM   1020 C  CD1  . LEU   A 1 143 ? 6.12300  0.83000   14.77500 1.000 12.76000 ?  139 LEU   A CD1  1 
ATOM   1021 C  CD2  . LEU   A 1 143 ? 5.61900  -1.56100  14.25300 1.000 18.88000 ?  139 LEU   A CD2  1 
ATOM   1022 N  N    . ARG   A 1 144 ? 1.13800  -0.19400  17.06200 1.000 14.24000 ?  140 ARG   A N    1 
ATOM   1023 C  CA   . ARG   A 1 144 ? 0.29300  -0.36900  18.24200 1.000 18.59000 ?  140 ARG   A CA   1 
ATOM   1024 C  C    . ARG   A 1 144 ? -0.78900 -1.42100  18.01200 1.000 20.43000 ?  140 ARG   A C    1 
ATOM   1025 O  O    . ARG   A 1 144 ? -1.13000 -2.17100  18.93400 1.000 23.86000 ?  140 ARG   A O    1 
ATOM   1026 C  CB   . ARG   A 1 144 ? -0.32700 0.97400   18.64600 1.000 23.29000 ?  140 ARG   A CB   1 
ATOM   1027 C  CG   . ARG   A 1 144 ? -1.25900 0.90500   19.85400 1.000 35.65000 ?  140 ARG   A CG   1 
ATOM   1028 C  CD   . ARG   A 1 144 ? -1.61000 2.29700   20.37200 1.000 39.09000 ?  140 ARG   A CD   1 
ATOM   1029 N  NE   . ARG   A 1 144 ? -1.78000 3.25700   19.28600 1.000 40.74000 ?  140 ARG   A NE   1 
ATOM   1030 C  CZ   . ARG   A 1 144 ? -2.89900 3.41900   18.59400 1.000 45.83000 ?  140 ARG   A CZ   1 
ATOM   1031 N  NH1  . ARG   A 1 144 ? -3.97300 2.68200   18.83500 1.000 51.35000 ?  140 ARG   A NH1  1 
ATOM   1032 N  NH2  . ARG   A 1 144 ? -2.94400 4.34400   17.63800 1.000 39.11000 ?  140 ARG   A NH2  1 
ATOM   1033 N  N    . GLU   A 1 145 ? -1.32100 -1.51100  16.79000 1.000 17.91000 ?  141 GLU   A N    1 
ATOM   1034 C  CA   . GLU   A 1 145 ? -2.38200 -2.46300  16.48600 1.000 21.95000 ?  141 GLU   A CA   1 
ATOM   1035 C  C    . GLU   A 1 145 ? -1.86100 -3.86300  16.18500 1.000 22.95000 ?  141 GLU   A C    1 
ATOM   1036 O  O    . GLU   A 1 145 ? -2.66200 -4.79600  16.08400 1.000 22.78000 ?  141 GLU   A O    1 
ATOM   1037 C  CB   . GLU   A 1 145 ? -3.21200 -1.94600  15.30700 1.000 21.81000 ?  141 GLU   A CB   1 
ATOM   1038 C  CG   . GLU   A 1 145 ? -3.95900 -0.67300  15.63800 1.000 25.52000 ?  141 GLU   A CG   1 
ATOM   1039 C  CD   . GLU   A 1 145 ? -4.74100 -0.11200  14.46800 1.000 36.02000 ?  141 GLU   A CD   1 
ATOM   1040 O  OE1  . GLU   A 1 145 ? -4.63600 -0.66100  13.35000 1.000 34.09000 ?  141 GLU   A OE1  1 
ATOM   1041 O  OE2  . GLU   A 1 145 ? -5.46600 0.88400   14.67700 1.000 42.36000 ?  141 GLU   A OE2  1 
ATOM   1042 N  N    . SER   A 1 146 ? -0.54500 -4.03300  16.05500 1.000 20.75000 ?  142 SER   A N    1 
ATOM   1043 C  CA   . SER   A 1 146 ? 0.01000  -5.32000  15.64900 1.000 18.68000 ?  142 SER   A CA   1 
ATOM   1044 C  C    . SER   A 1 146 ? -0.11200 -6.38300  16.73200 1.000 20.08000 ?  142 SER   A C    1 
ATOM   1045 O  O    . SER   A 1 146 ? -0.09600 -7.57400  16.41100 1.000 22.73000 ?  142 SER   A O    1 
ATOM   1046 C  CB   . SER   A 1 146 ? 1.48100  -5.16200  15.26200 1.000 18.10000 ?  142 SER   A CB   1 
ATOM   1047 O  OG   . SER   A 1 146 ? 2.27000  -4.87900  16.40400 1.000 17.20000 ?  142 SER   A OG   1 
ATOM   1048 N  N    . GLY   A 1 147 ? -0.22600 -5.99100  17.99700 1.000 17.44000 ?  143 GLY   A N    1 
ATOM   1049 C  CA   . GLY   A 1 147 ? -0.18800 -6.95500  19.07600 1.000 21.79000 ?  143 GLY   A CA   1 
ATOM   1050 C  C    . GLY   A 1 147 ? 1.19300  -7.45700  19.43700 1.000 21.01000 ?  143 GLY   A C    1 
ATOM   1051 O  O    . GLY   A 1 147 ? 1.31100  -8.33600  20.30000 1.000 24.51000 ?  143 GLY   A O    1 
ATOM   1052 N  N    . LEU   A 1 148 ? 2.24100  -6.94100  18.80200 1.000 18.96000 ?  144 LEU   A N    1 
ATOM   1053 C  CA   . LEU   A 1 148 ? 3.60800  -7.29700  19.14100 1.000 18.95000 ?  144 LEU   A CA   1 
ATOM   1054 C  C    . LEU   A 1 148 ? 4.04200  -6.57100  20.41000 1.000 18.75000 ?  144 LEU   A C    1 
ATOM   1055 O  O    . LEU   A 1 148 ? 3.41500  -5.60200  20.84700 1.000 19.51000 ?  144 LEU   A O    1 
ATOM   1056 C  CB   . LEU   A 1 148 ? 4.54000  -6.94100  17.98800 1.000 17.89000 ?  144 LEU   A CB   1 
ATOM   1057 C  CG   . LEU   A 1 148 ? 4.21900  -7.58100  16.64100 1.000 15.43000 ?  144 LEU   A CG   1 
ATOM   1058 C  CD1  . LEU   A 1 148 ? 4.94800  -6.84900  15.51600 1.000 16.89000 ?  144 LEU   A CD1  1 
ATOM   1059 C  CD2  . LEU   A 1 148 ? 4.59600  -9.05200  16.66200 1.000 21.33000 ?  144 LEU   A CD2  1 
ATOM   1060 N  N    . LYS   A 1 149 ? 5.14200  -7.03300  21.00700 1.000 17.58000 ?  145 LYS   A N    1 
ATOM   1061 C  CA   . LYS   A 1 149 ? 5.72700  -6.29100  22.12300 1.000 18.53000 ?  145 LYS   A CA   1 
ATOM   1062 C  C    . LYS   A 1 149 ? 6.42400  -5.07000  21.53900 1.000 17.59000 ?  145 LYS   A C    1 
ATOM   1063 O  O    . LYS   A 1 149 ? 7.53300  -5.16800  21.01300 1.000 17.10000 ?  145 LYS   A O    1 
ATOM   1064 C  CB   . LYS   A 1 149 ? 6.68900  -7.16200  22.92300 1.000 20.26000 ?  145 LYS   A CB   1 
ATOM   1065 C  CG   . LYS   A 1 149 ? 6.04700  -8.45600  23.39800 1.000 23.98000 ?  145 LYS   A CG   1 
ATOM   1066 C  CD   . LYS   A 1 149 ? 6.59900  -8.92500  24.72100 1.000 30.28000 ?  145 LYS   A CD   1 
ATOM   1067 C  CE   . LYS   A 1 149 ? 8.02100  -9.37600  24.61800 1.000 31.96000 ?  145 LYS   A CE   1 
ATOM   1068 N  NZ   . LYS   A 1 149 ? 8.35300  -10.27400 25.77100 1.000 28.83000 ?  145 LYS   A NZ   1 
ATOM   1069 N  N    . TYR   A 1 150 ? 5.77500  -3.91100  21.64800 1.000 14.75000 ?  146 TYR   A N    1 
ATOM   1070 C  CA   . TYR   A 1 150 ? 6.16400  -2.70300  20.92900 1.000 13.42000 ?  146 TYR   A CA   1 
ATOM   1071 C  C    . TYR   A 1 150 ? 6.55500  -1.62400  21.92800 1.000 13.37000 ?  146 TYR   A C    1 
ATOM   1072 O  O    . TYR   A 1 150 ? 5.73200  -1.22300  22.76100 1.000 12.15000 ?  146 TYR   A O    1 
ATOM   1073 C  CB   . TYR   A 1 150 ? 5.00700  -2.24000  20.03400 1.000 14.48000 ?  146 TYR   A CB   1 
ATOM   1074 C  CG   . TYR   A 1 150 ? 5.08200  -0.82200  19.49000 1.000 12.64000 ?  146 TYR   A CG   1 
ATOM   1075 C  CD1  . TYR   A 1 150 ? 6.26500  -0.31200  18.95200 1.000 11.42000 ?  146 TYR   A CD1  1 
ATOM   1076 C  CD2  . TYR   A 1 150 ? 3.94800  -0.01600  19.47300 1.000 13.98000 ?  146 TYR   A CD2  1 
ATOM   1077 C  CE1  . TYR   A 1 150 ? 6.31400  0.98700   18.45000 1.000 11.76000 ?  146 TYR   A CE1  1 
ATOM   1078 C  CE2  . TYR   A 1 150 ? 3.98100  1.27200   18.96800 1.000 12.22000 ?  146 TYR   A CE2  1 
ATOM   1079 C  CZ   . TYR   A 1 150 ? 5.16400  1.76500   18.45400 1.000 12.49000 ?  146 TYR   A CZ   1 
ATOM   1080 O  OH   . TYR   A 1 150 ? 5.18400  3.05200   17.96600 1.000 11.82000 ?  146 TYR   A OH   1 
ATOM   1081 N  N    . VAL   A 1 151 ? 7.80600  -1.15900  21.85400 1.000 10.05000 ?  147 VAL   A N    1 
ATOM   1082 C  CA   . VAL   A 1 151 ? 8.23400  0.03600   22.58600 1.000 10.81000 ?  147 VAL   A CA   1 
ATOM   1083 C  C    . VAL   A 1 151 ? 8.22100  1.20100   21.60700 1.000 13.36000 ?  147 VAL   A C    1 
ATOM   1084 O  O    . VAL   A 1 151 ? 8.93700  1.18400   20.59800 1.000 12.15000 ?  147 VAL   A O    1 
ATOM   1085 C  CB   . VAL   A 1 151 ? 9.62800  -0.11800  23.21900 1.000 11.53000 ?  147 VAL   A CB   1 
ATOM   1086 C  CG1  . VAL   A 1 151 ? 9.96200  1.13700   24.02100 1.000 12.67000 ?  147 VAL   A CG1  1 
ATOM   1087 C  CG2  . VAL   A 1 151 ? 9.72500  -1.35800  24.11100 1.000 12.48000 ?  147 VAL   A CG2  1 
ATOM   1088 N  N    . ALA   A 1 152 ? 7.39500  2.20000   21.90200 1.000 12.01000 ?  148 ALA   A N    1 
ATOM   1089 C  CA   . ALA   A 1 152 ? 7.22100  3.37600   21.05300 1.000 10.77000 ?  148 ALA   A CA   1 
ATOM   1090 C  C    . ALA   A 1 152 ? 8.18100  4.44000   21.56000 1.000 14.17000 ?  148 ALA   A C    1 
ATOM   1091 O  O    . ALA   A 1 152 ? 7.91600  5.10500   22.56700 1.000 14.44000 ?  148 ALA   A O    1 
ATOM   1092 C  CB   . ALA   A 1 152 ? 5.77400  3.86100   21.08300 1.000 13.70000 ?  148 ALA   A CB   1 
ATOM   1093 N  N    . VAL   A 1 153 ? 9.29500  4.61700   20.85700 1.000 12.29000 ?  149 VAL   A N    1 
ATOM   1094 C  CA   . VAL   A 1 153 ? 10.29500 5.60800   21.24500 1.000 12.56000 ?  149 VAL   A CA   1 
ATOM   1095 C  C    . VAL   A 1 153 ? 9.96800  6.91800   20.54000 1.000 14.96000 ?  149 VAL   A C    1 
ATOM   1096 O  O    . VAL   A 1 153 ? 9.85500  6.96100   19.31100 1.000 9.46000  ?  149 VAL   A O    1 
ATOM   1097 C  CB   . VAL   A 1 153 ? 11.71600 5.13000   20.92000 1.000 10.10000 ?  149 VAL   A CB   1 
ATOM   1098 C  CG1  . VAL   A 1 153 ? 12.74600 6.13600   21.45400 1.000 13.24000 ?  149 VAL   A CG1  1 
ATOM   1099 C  CG2  . VAL   A 1 153 ? 11.95600 3.76200   21.55800 1.000 10.71000 ?  149 VAL   A CG2  1 
ATOM   1100 N  N    . MET   A 1 154 ? 9.79300  7.98300   21.32100 1.000 10.76000 ?  150 MET   A N    1 
ATOM   1101 C  CA   . MET   A 1 154 ? 9.24000  9.24500   20.82700 1.000 11.15000 ?  150 MET   A CA   1 
ATOM   1102 C  C    . MET   A 1 154 ? 10.16700 10.38500  21.23000 1.000 13.77000 ?  150 MET   A C    1 
ATOM   1103 O  O    . MET   A 1 154 ? 9.88800  11.12100  22.18400 1.000 12.76000 ?  150 MET   A O    1 
ATOM   1104 C  CB   . MET   A 1 154 ? 7.81800  9.44500   21.36000 1.000 13.00000 ?  150 MET   A CB   1 
ATOM   1105 C  CG   . MET   A 1 154 ? 6.82700  8.43800   20.80400 1.000 11.95000 ?  150 MET   A CG   1 
ATOM   1106 S  SD   . MET   A 1 154 ? 5.12400  8.78500   21.30700 1.000 13.22000 ?  150 MET   A SD   1 
ATOM   1107 C  CE   . MET   A 1 154 ? 4.26600  7.46400   20.45900 1.000 14.30000 ?  150 MET   A CE   1 
ATOM   1108 N  N    . PRO   A 1 155 ? 11.27800 10.55900  20.52300 1.000 13.21000 ?  151 PRO   A N    1 
ATOM   1109 C  CA   . PRO   A 1 155 ? 12.30300 11.51300  20.96300 1.000 13.22000 ?  151 PRO   A CA   1 
ATOM   1110 C  C    . PRO   A 1 155 ? 11.96000 12.93500  20.56200 1.000 14.49000 ?  151 PRO   A C    1 
ATOM   1111 O  O    . PRO   A 1 155 ? 11.23400 13.16900  19.57700 1.000 10.05000 ?  151 PRO   A O    1 
ATOM   1112 C  CB   . PRO   A 1 155 ? 13.56600 11.03000  20.23300 1.000 13.14000 ?  151 PRO   A CB   1 
ATOM   1113 C  CG   . PRO   A 1 155 ? 13.00500 10.46300  18.95000 1.000 14.15000 ?  151 PRO   A CG   1 
ATOM   1114 C  CD   . PRO   A 1 155 ? 11.71900 9.77700   19.35500 1.000 9.33000  ?  151 PRO   A CD   1 
ATOM   1115 N  N    . PRO   A 1 156 ? 12.45400 13.91600  21.31700 1.000 12.86000 ?  152 PRO   A N    1 
ATOM   1116 C  CA   . PRO   A 1 156 ? 12.43000 15.30000  20.83500 1.000 10.71000 ?  152 PRO   A CA   1 
ATOM   1117 C  C    . PRO   A 1 156 ? 13.54400 15.51900  19.82400 1.000 14.59000 ?  152 PRO   A C    1 
ATOM   1118 O  O    . PRO   A 1 156 ? 13.92700 14.58800  19.11100 1.000 14.46000 ?  152 PRO   A O    1 
ATOM   1119 C  CB   . PRO   A 1 156 ? 12.64900 16.11500  22.11800 1.000 13.97000 ?  152 PRO   A CB   1 
ATOM   1120 C  CG   . PRO   A 1 156 ? 13.53000 15.23200  22.95500 1.000 12.96000 ?  152 PRO   A CG   1 
ATOM   1121 C  CD   . PRO   A 1 156 ? 13.07500 13.80600  22.65700 1.000 11.72000 ?  152 PRO   A CD   1 
ATOM   1122 N  N    . HIS   A 1 157 ? 14.05800 16.74000  19.73100 1.000 14.52000 ?  153 HIS   A N    1 
ATOM   1123 C  CA   . HIS   A 1 157 ? 15.10900 17.02700  18.75800 1.000 15.99000 ?  153 HIS   A CA   1 
ATOM   1124 C  C    . HIS   A 1 157 ? 16.31400 16.10700  18.94700 1.000 14.41000 ?  153 HIS   A C    1 
ATOM   1125 O  O    . HIS   A 1 157 ? 16.76800 15.87800  20.07300 1.000 14.07000 ?  153 HIS   A O    1 
ATOM   1126 C  CB   . HIS   A 1 157 ? 15.55200 18.48000  18.86500 1.000 14.12000 ?  153 HIS   A CB   1 
ATOM   1127 C  CG   . HIS   A 1 157 ? 16.66700 18.81500  17.92200 1.000 19.70000 ?  153 HIS   A CG   1 
ATOM   1128 N  ND1  . HIS   A 1 157 ? 16.47700 18.92300  16.56000 1.000 24.57000 ?  153 HIS   A ND1  1 
ATOM   1129 C  CD2  . HIS   A 1 157 ? 17.99000 19.00400  18.13600 1.000 25.68000 ?  153 HIS   A CD2  1 
ATOM   1130 C  CE1  . HIS   A 1 157 ? 17.63100 19.20000  15.97900 1.000 28.38000 ?  153 HIS   A CE1  1 
ATOM   1131 N  NE2  . HIS   A 1 157 ? 18.56600 19.25500  16.91200 1.000 28.93000 ?  153 HIS   A NE2  1 
ATOM   1132 N  N    . ILE   A 1 158 ? 16.82700 15.56500  17.84400 1.000 11.03000 ?  154 ILE   A N    1 
ATOM   1133 C  CA   . ILE   A 1 158 ? 17.96700 14.65000  17.88300 1.000 15.37000 ?  154 ILE   A CA   1 
ATOM   1134 C  C    . ILE   A 1 158 ? 19.23600 15.44900  17.61300 1.000 16.10000 ?  154 ILE   A C    1 
ATOM   1135 O  O    . ILE   A 1 158 ? 19.41500 15.98100  16.51400 1.000 16.19000 ?  154 ILE   A O    1 
ATOM   1136 C  CB   . ILE   A 1 158 ? 17.81300 13.50900  16.86200 1.000 13.73000 ?  154 ILE   A CB   1 
ATOM   1137 C  CG1  . ILE   A 1 158 ? 16.60300 12.63500  17.19200 1.000 12.31000 ?  154 ILE   A CG1  1 
ATOM   1138 C  CG2  . ILE   A 1 158 ? 19.08600 12.64600  16.81700 1.000 15.14000 ?  154 ILE   A CG2  1 
ATOM   1139 C  CD1  . ILE   A 1 158 ? 16.24800 11.66000  16.06700 1.000 12.42000 ?  154 ILE   A CD1  1 
ATOM   1140 N  N    . GLY   A 1 159 ? 20.12400 15.52600  18.60700 1.000 19.06000 ?  155 GLY   A N    1 
ATOM   1141 C  CA   . GLY   A 1 159 ? 21.34900 16.28800  18.49600 1.000 18.66000 ?  155 GLY   A CA   1 
ATOM   1142 C  C    . GLY   A 1 159 ? 22.58900 15.43100  18.26400 1.000 19.10000 ?  155 GLY   A C    1 
ATOM   1143 O  O    . GLY   A 1 159 ? 22.54800 14.20600  18.18500 1.000 19.38000 ?  155 GLY   A O    1 
ATOM   1144 N  N    . ASP   A 1 160 ? 23.73000 16.11200  18.14200 1.000 20.27000 ?  156 ASP   A N    1 
ATOM   1145 C  CA   . ASP   A 1 160 ? 24.99300 15.42200  17.91100 1.000 18.74000 ?  156 ASP   A CA   1 
ATOM   1146 C  C    . ASP   A 1 160 ? 25.91200 15.48600  19.13100 1.000 22.55000 ?  156 ASP   A C    1 
ATOM   1147 O  O    . ASP   A 1 160 ? 27.13200 15.31900  19.00200 1.000 22.02000 ?  156 ASP   A O    1 
ATOM   1148 C  CB   . ASP   A 1 160 ? 25.69000 15.96800  16.66000 1.000 25.82000 ?  156 ASP   A CB   1 
ATOM   1149 C  CG   . ASP   A 1 160 ? 25.92300 17.45900  16.71800 1.000 39.20000 ?  156 ASP   A CG   1 
ATOM   1150 O  OD1  . ASP   A 1 160 ? 25.48000 18.10200  17.69600 1.000 40.61000 ?  156 ASP   A OD1  1 
ATOM   1151 O  OD2  . ASP   A 1 160 ? 26.55600 17.98900  15.77900 1.000 48.39000 ?  156 ASP   A OD2  1 
ATOM   1152 N  N    . GLN   A 1 161 ? 25.34000 15.70700  20.31000 1.000 18.61000 ?  157 GLN   A N    1 
ATOM   1153 C  CA   . GLN   A 1 161 ? 26.09300 15.73100  21.55200 1.000 19.93000 ?  157 GLN   A CA   1 
ATOM   1154 C  C    . GLN   A 1 161 ? 26.62800 14.33700  21.85700 1.000 20.76000 ?  157 GLN   A C    1 
ATOM   1155 O  O    . GLN   A 1 161 ? 26.23800 13.35400  21.21900 1.000 19.61000 ?  157 GLN   A O    1 
ATOM   1156 C  CB   . GLN   A 1 161 ? 25.20700 16.24800  22.68600 1.000 20.61000 ?  157 GLN   A CB   1 
ATOM   1157 C  CG   . GLN   A 1 161 ? 24.62700 17.62500  22.42500 1.000 24.32000 ?  157 GLN   A CG   1 
ATOM   1158 C  CD   . GLN   A 1 161 ? 23.25500 17.54700  21.80000 1.000 26.86000 ?  157 GLN   A CD   1 
ATOM   1159 O  OE1  . GLN   A 1 161 ? 22.86900 16.51000  21.26000 1.000 23.57000 ?  157 GLN   A OE1  1 
ATOM   1160 N  NE2  . GLN   A 1 161 ? 22.50000 18.63600  21.88400 1.000 28.62000 ?  157 GLN   A NE2  1 
ATOM   1161 N  N    . PRO   A 1 162 ? 27.54300 14.20600  22.82000 1.000 20.77000 ?  158 PRO   A N    1 
ATOM   1162 C  CA   . PRO   A 1 162 ? 28.17400 12.90400  23.05600 1.000 18.65000 ?  158 PRO   A CA   1 
ATOM   1163 C  C    . PRO   A 1 162 ? 27.20200 11.89300  23.64200 1.000 19.19000 ?  158 PRO   A C    1 
ATOM   1164 O  O    . PRO   A 1 162 ? 26.09100 12.21000  24.08600 1.000 21.53000 ?  158 PRO   A O    1 
ATOM   1165 C  CB   . PRO   A 1 162 ? 29.30000 13.21800  24.04800 1.000 26.55000 ?  158 PRO   A CB   1 
ATOM   1166 C  CG   . PRO   A 1 162 ? 29.57600 14.67300  23.86000 1.000 29.05000 ?  158 PRO   A CG   1 
ATOM   1167 C  CD   . PRO   A 1 162 ? 28.23900 15.28200  23.55400 1.000 26.98000 ?  158 PRO   A CD   1 
ATOM   1168 N  N    . LEU   A 1 163 ? 27.63900 10.63800  23.58700 1.000 16.27000 ?  159 LEU   A N    1 
ATOM   1169 C  CA   . LEU   A 1 163 ? 27.02500 9.57900   24.37400 1.000 17.61000 ?  159 LEU   A CA   1 
ATOM   1170 C  C    . LEU   A 1 163 ? 27.25300 9.83900   25.85600 1.000 19.73000 ?  159 LEU   A C    1 
ATOM   1171 O  O    . LEU   A 1 163 ? 28.37900 10.13400  26.27100 1.000 20.06000 ?  159 LEU   A O    1 
ATOM   1172 C  CB   . LEU   A 1 163 ? 27.62700 8.23200   23.97900 1.000 15.38000 ?  159 LEU   A CB   1 
ATOM   1173 C  CG   . LEU   A 1 163 ? 27.17900 7.02200   24.79600 1.000 15.81000 ?  159 LEU   A CG   1 
ATOM   1174 C  CD1  . LEU   A 1 163 ? 25.72000 6.71800   24.48600 1.000 18.02000 ?  159 LEU   A CD1  1 
ATOM   1175 C  CD2  . LEU   A 1 163 ? 28.06100 5.82200   24.49100 1.000 16.72000 ?  159 LEU   A CD2  1 
ATOM   1176 N  N    . THR   A 1 164 ? 26.18900 9.73000   26.65800 1.000 17.46000 ?  160 THR   A N    1 
ATOM   1177 C  CA   . THR   A 1 164 ? 26.31000 9.92100   28.10100 1.000 17.31000 ?  160 THR   A CA   1 
ATOM   1178 C  C    . THR   A 1 164 ? 25.73400 8.74900   28.88300 1.000 19.19000 ?  160 THR   A C    1 
ATOM   1179 O  O    . THR   A 1 164 ? 26.17500 8.47800   30.00400 1.000 18.19000 ?  160 THR   A O    1 
ATOM   1180 C  CB   . THR   A 1 164 ? 25.60800 11.20000  28.57200 1.000 18.45000 ?  160 THR   A CB   1 
ATOM   1181 O  OG1  . THR   A 1 164 ? 24.18300 11.01900  28.52200 1.000 18.00000 ?  160 THR   A OG1  1 
ATOM   1182 C  CG2  . THR   A 1 164 ? 26.02800 12.41600  27.73300 1.000 19.08000 ?  160 THR   A CG2  1 
ATOM   1183 N  N    . GLY   A 1 165 ? 24.71200 8.08600   28.33700 1.000 16.55000 ?  161 GLY   A N    1 
ATOM   1184 C  CA   . GLY   A 1 165 ? 23.97700 7.08900   29.09700 1.000 17.71000 ?  161 GLY   A CA   1 
ATOM   1185 C  C    . GLY   A 1 165 ? 23.25800 7.64400   30.31500 1.000 15.62000 ?  161 GLY   A C    1 
ATOM   1186 O  O    . GLY   A 1 165 ? 22.75200 6.88000   31.14200 1.000 21.36000 ?  161 GLY   A O    1 
ATOM   1187 N  N    . ALA   A 1 166 ? 23.18400 8.97200   30.43200 1.000 14.39000 ?  162 ALA   A N    1 
ATOM   1188 C  CA   . ALA   A 1 166 ? 22.69600 9.63300   31.63900 1.000 21.59000 ?  162 ALA   A CA   1 
ATOM   1189 C  C    . ALA   A 1 166 ? 21.36600 10.34500  31.42900 1.000 18.81000 ?  162 ALA   A C    1 
ATOM   1190 O  O    . ALA   A 1 166 ? 20.91000 11.08200  32.31700 1.000 18.41000 ?  162 ALA   A O    1 
ATOM   1191 C  CB   . ALA   A 1 166 ? 23.74200 10.62300  32.15000 1.000 22.21000 ?  162 ALA   A CB   1 
ATOM   1192 N  N    . TYR   A 1 167 ? 20.73000 10.12600  30.28400 1.000 16.62000 ?  163 TYR   A N    1 
ATOM   1193 C  CA   . TYR   A 1 167 ? 19.47900 10.76900  29.92500 1.000 16.11000 ?  163 TYR   A CA   1 
ATOM   1194 C  C    . TYR   A 1 167 ? 18.32200 10.30600  30.82000 1.000 14.39000 ?  163 TYR   A C    1 
ATOM   1195 O  O    . TYR   A 1 167 ? 18.36600 9.25600   31.47200 1.000 15.41000 ?  163 TYR   A O    1 
ATOM   1196 C  CB   . TYR   A 1 167 ? 19.15700 10.46600  28.45600 1.000 13.76000 ?  163 TYR   A CB   1 
ATOM   1197 C  CG   . TYR   A 1 167 ? 19.24100 8.99300   28.14000 1.000 13.43000 ?  163 TYR   A CG   1 
ATOM   1198 C  CD1  . TYR   A 1 167 ? 18.14700 8.15200   28.32400 1.000 15.59000 ?  163 TYR   A CD1  1 
ATOM   1199 C  CD2  . TYR   A 1 167 ? 20.42600 8.43300   27.66500 1.000 11.45000 ?  163 TYR   A CD2  1 
ATOM   1200 C  CE1  . TYR   A 1 167 ? 18.23500 6.79700   28.04900 1.000 15.71000 ?  163 TYR   A CE1  1 
ATOM   1201 C  CE2  . TYR   A 1 167 ? 20.52200 7.08900   27.39000 1.000 14.12000 ?  163 TYR   A CE2  1 
ATOM   1202 C  CZ   . TYR   A 1 167 ? 19.42800 6.27400   27.59600 1.000 16.83000 ?  163 TYR   A CZ   1 
ATOM   1203 O  OH   . TYR   A 1 167 ? 19.52800 4.93700   27.31500 1.000 15.44000 ?  163 TYR   A OH   1 
ATOM   1204 N  N    . THR   A 1 168 ? 17.26100 11.09600  30.81300 1.000 13.73000 ?  164 THR   A N    1 
ATOM   1205 C  CA   . THR   A 1 168 ? 16.01800 10.76900  31.49600 1.000 13.94000 ?  164 THR   A CA   1 
ATOM   1206 C  C    . THR   A 1 168 ? 15.07300 10.04800  30.53500 1.000 15.19000 ?  164 THR   A C    1 
ATOM   1207 O  O    . THR   A 1 168 ? 15.01300 10.37800  29.34800 1.000 15.25000 ?  164 THR   A O    1 
ATOM   1208 C  CB   . THR   A 1 168 ? 15.38400 12.06100  32.01800 1.000 17.36000 ?  164 THR   A CB   1 
ATOM   1209 O  OG1  . THR   A 1 168 ? 16.26100 12.64600  32.99100 1.000 23.53000 ?  164 THR   A OG1  1 
ATOM   1210 C  CG2  . THR   A 1 168 ? 13.98800 11.82300  32.61400 1.000 16.95000 ?  164 THR   A CG2  1 
ATOM   1211 N  N    . VAL   A 1 169 ? 14.35800 9.04200   31.03900 1.000 14.60000 ?  165 VAL   A N    1 
ATOM   1212 C  CA   . VAL   A 1 169 ? 13.34600 8.33700   30.25700 1.000 14.68000 ?  165 VAL   A CA   1 
ATOM   1213 C  C    . VAL   A 1 169 ? 11.98800 8.64500   30.86900 1.000 14.60000 ?  165 VAL   A C    1 
ATOM   1214 O  O    . VAL   A 1 169 ? 11.69800 8.22800   31.99900 1.000 15.92000 ?  165 VAL   A O    1 
ATOM   1215 C  CB   . VAL   A 1 169 ? 13.59400 6.82500   30.20700 1.000 16.49000 ?  165 VAL   A CB   1 
ATOM   1216 C  CG1  . VAL   A 1 169 ? 12.47600 6.14300   29.41000 1.000 15.61000 ?  165 VAL   A CG1  1 
ATOM   1217 C  CG2  . VAL   A 1 169 ? 14.96800 6.54000   29.58200 1.000 14.83000 ?  165 VAL   A CG2  1 
ATOM   1218 N  N    . THR   A 1 170 ? 11.15300 9.37200   30.13500 1.000 14.57000 ?  166 THR   A N    1 
ATOM   1219 C  CA   . THR   A 1 170 ? 9.81500  9.73300   30.59800 1.000 12.89000 ?  166 THR   A CA   1 
ATOM   1220 C  C    . THR   A 1 170 ? 8.79600  8.81800   29.93400 1.000 15.65000 ?  166 THR   A C    1 
ATOM   1221 O  O    . THR   A 1 170 ? 8.84000  8.60400   28.71900 1.000 14.23000 ?  166 THR   A O    1 
ATOM   1222 C  CB   . THR   A 1 170 ? 9.50900  11.20200  30.29200 1.000 14.09000 ?  166 THR   A CB   1 
ATOM   1223 O  OG1  . THR   A 1 170 ? 10.48800 12.03600  30.94200 1.000 14.78000 ?  166 THR   A OG1  1 
ATOM   1224 C  CG2  . THR   A 1 170 ? 8.10500  11.57900  30.77700 1.000 16.27000 ?  166 THR   A CG2  1 
ATOM   1225 N  N    . LEU   A 1 171 ? 7.90300  8.25400   30.73200 1.000 12.72000 ?  167 LEU   A N    1 
ATOM   1226 C  CA   . LEU   A 1 171 ? 6.93000  7.29000   30.24500 1.000 15.97000 ?  167 LEU   A CA   1 
ATOM   1227 C  C    . LEU   A 1 171 ? 5.60100  7.97500   29.94400 1.000 16.64000 ?  167 LEU   A C    1 
ATOM   1228 O  O    . LEU   A 1 171 ? 5.05500  8.68700   30.79500 1.000 18.48000 ?  167 LEU   A O    1 
ATOM   1229 C  CB   . LEU   A 1 171 ? 6.72700  6.17500   31.27100 1.000 19.12000 ?  167 LEU   A CB   1 
ATOM   1230 C  CG   . LEU   A 1 171 ? 7.25900  4.79700   30.89800 1.000 28.18000 ?  167 LEU   A CG   1 
ATOM   1231 C  CD1  . LEU   A 1 171 ? 8.74000  4.87300   30.58300 1.000 24.49000 ?  167 LEU   A CD1  1 
ATOM   1232 C  CD2  . LEU   A 1 171 ? 6.98300  3.81900   32.03600 1.000 32.51000 ?  167 LEU   A CD2  1 
ATOM   1233 N  N    . ASP   A 1 172 ? 5.09000  7.75800   28.73200 1.000 13.50000 ?  168 ASP   A N    1 
ATOM   1234 C  CA   . ASP   A 1 172 ? 3.71000  8.10800   28.38200 1.000 14.73000 ?  168 ASP   A CA   1 
ATOM   1235 C  C    . ASP   A 1 172 ? 3.44000  9.60600   28.53800 1.000 18.62000 ?  168 ASP   A C    1 
ATOM   1236 O  O    . ASP   A 1 172 ? 2.34100  10.02900  28.90400 1.000 20.81000 ?  168 ASP   A O    1 
ATOM   1237 C  CB   . ASP   A 1 172 ? 2.72800  7.27300   29.21100 1.000 17.21000 ?  168 ASP   A CB   1 
ATOM   1238 C  CG   . ASP   A 1 172 ? 2.95700  5.78500   29.02700 1.000 21.20000 ?  168 ASP   A CG   1 
ATOM   1239 O  OD1  . ASP   A 1 172 ? 3.06900  5.35100   27.86000 1.000 18.84000 ?  168 ASP   A OD1  1 
ATOM   1240 O  OD2  . ASP   A 1 172 ? 3.06100  5.05500   30.03300 1.000 22.81000 ?  168 ASP   A OD2  1 
ATOM   1241 N  N    . GLY   A 1 173 ? 4.44100  10.41900  28.23400 1.000 15.75000 ?  169 GLY   A N    1 
ATOM   1242 C  CA   . GLY   A 1 173 ? 4.29000  11.86300  28.29800 1.000 15.45000 ?  169 GLY   A CA   1 
ATOM   1243 C  C    . GLY   A 1 173 ? 5.59900  12.53200  27.92700 1.000 17.05000 ?  169 GLY   A C    1 
ATOM   1244 O  O    . GLY   A 1 173 ? 6.61500  11.87000  27.69200 1.000 16.10000 ?  169 GLY   A O    1 
ATOM   1245 N  N    A ARG   A 1 174 ? 5.55900  13.86500  27.87500 0.520 16.67000 ?  170 ARG   A N    1 
ATOM   1246 N  N    B ARG   A 1 174 ? 5.54700  13.86500  27.89000 0.480 16.69000 ?  170 ARG   A N    1 
ATOM   1247 C  CA   A ARG   A 1 174 ? 6.73100  14.64700  27.51300 0.520 14.71000 ?  170 ARG   A CA   1 
ATOM   1248 C  CA   B ARG   A 1 174 ? 6.74200  14.64800  27.51800 0.480 14.71000 ?  170 ARG   A CA   1 
ATOM   1249 C  C    A ARG   A 1 174 ? 7.65800  14.82300  28.71200 0.520 15.43000 ?  170 ARG   A C    1 
ATOM   1250 C  C    B ARG   A 1 174 ? 7.67000  14.79200  28.71700 0.480 15.45000 ?  170 ARG   A C    1 
ATOM   1251 O  O    A ARG   A 1 174 ? 7.21800  14.91900  29.86000 0.520 15.34000 ?  170 ARG   A O    1 
ATOM   1252 O  O    B ARG   A 1 174 ? 7.19000  14.95800  29.83600 0.480 15.38000 ?  170 ARG   A O    1 
ATOM   1253 C  CB   A ARG   A 1 174 ? 6.30800  16.01400  26.96200 0.520 18.51000 ?  170 ARG   A CB   1 
ATOM   1254 C  CB   B ARG   A 1 174 ? 6.34300  16.03100  27.01100 0.480 18.49000 ?  170 ARG   A CB   1 
ATOM   1255 C  CG   A ARG   A 1 174 ? 5.24500  15.89400  25.85300 0.520 20.12000 ?  170 ARG   A CG   1 
ATOM   1256 C  CG   B ARG   A 1 174 ? 5.47900  16.00300  25.76000 0.480 20.25000 ?  170 ARG   A CG   1 
ATOM   1257 C  CD   A ARG   A 1 174 ? 4.57800  17.22700  25.48200 0.520 22.38000 ?  170 ARG   A CD   1 
ATOM   1258 C  CD   B ARG   A 1 174 ? 5.22300  17.41100  25.26700 0.480 22.38000 ?  170 ARG   A CD   1 
ATOM   1259 N  NE   A ARG   A 1 174 ? 3.91900  17.86500  26.62000 0.520 24.25000 ?  170 ARG   A NE   1 
ATOM   1260 N  NE   B ARG   A 1 174 ? 6.45900  18.09000  24.89600 0.480 24.25000 ?  170 ARG   A NE   1 
ATOM   1261 C  CZ   A ARG   A 1 174 ? 2.60600  17.92500  26.80200 0.520 32.95000 ?  170 ARG   A CZ   1 
ATOM   1262 C  CZ   B ARG   A 1 174 ? 6.92300  19.19200  25.47500 0.480 32.95000 ?  170 ARG   A CZ   1 
ATOM   1263 N  NH1  A ARG   A 1 174 ? 1.75700  17.36900  25.94600 0.520 26.72000 ?  170 ARG   A NH1  1 
ATOM   1264 N  NH1  B ARG   A 1 174 ? 6.26100  19.74400  26.47800 0.480 26.72000 ?  170 ARG   A NH1  1 
ATOM   1265 N  NH2  A ARG   A 1 174 ? 2.12900  18.57400  27.86100 0.520 37.04000 ?  170 ARG   A NH2  1 
ATOM   1266 N  NH2  B ARG   A 1 174 ? 8.05400  19.73200  25.05900 0.480 37.04000 ?  170 ARG   A NH2  1 
ATOM   1267 N  N    . GLY   A 1 175 ? 8.95900  14.85300  28.43800 1.000 14.06000 ?  171 GLY   A N    1 
ATOM   1268 C  CA   . GLY   A 1 175 ? 9.94600  14.98800  29.48600 1.000 14.40000 ?  171 GLY   A CA   1 
ATOM   1269 C  C    . GLY   A 1 175 ? 10.51500 16.39500  29.61500 1.000 13.18000 ?  171 GLY   A C    1 
ATOM   1270 O  O    . GLY   A 1 175 ? 10.14800 17.31000  28.87800 1.000 14.16000 ?  171 GLY   A O    1 
ATOM   1271 N  N    . PRO   A 1 176 ? 11.46800 16.57600  30.53700 1.000 13.78000 ?  172 PRO   A N    1 
ATOM   1272 C  CA   . PRO   A 1 176 ? 11.90100 17.93700  30.90600 1.000 16.97000 ?  172 PRO   A CA   1 
ATOM   1273 C  C    . PRO   A 1 176 ? 12.96200 18.56100  30.01300 1.000 19.68000 ?  172 PRO   A C    1 
ATOM   1274 O  O    . PRO   A 1 176 ? 13.30200 19.73200  30.23500 1.000 20.06000 ?  172 PRO   A O    1 
ATOM   1275 C  CB   . PRO   A 1 176 ? 12.44900 17.75100  32.32500 1.000 17.40000 ?  172 PRO   A CB   1 
ATOM   1276 C  CG   . PRO   A 1 176 ? 12.92800 16.32700  32.34500 1.000 19.12000 ?  172 PRO   A CG   1 
ATOM   1277 C  CD   . PRO   A 1 176 ? 11.97500 15.55300  31.46800 1.000 16.93000 ?  172 PRO   A CD   1 
ATOM   1278 N  N    . SER   A 1 177 ? 13.51300 17.83900  29.03600 1.000 14.18000 ?  173 SER   A N    1 
ATOM   1279 C  CA   . SER   A 1 177 ? 14.40600 18.45300  28.06700 1.000 15.34000 ?  173 SER   A CA   1 
ATOM   1280 C  C    . SER   A 1 177 ? 13.83800 18.25200  26.67000 1.000 16.64000 ?  173 SER   A C    1 
ATOM   1281 O  O    . SER   A 1 177 ? 13.05600 17.32900  26.42900 1.000 15.79000 ?  173 SER   A O    1 
ATOM   1282 C  CB   . SER   A 1 177 ? 15.81700 17.86800  28.15300 1.000 17.09000 ?  173 SER   A CB   1 
ATOM   1283 O  OG   . SER   A 1 177 ? 16.55900 18.19400  26.98700 1.000 20.47000 ?  173 SER   A OG   1 
ATOM   1284 N  N    . ARG   A 1 178 ? 14.22400 19.14000  25.75000 1.000 15.83000 ?  174 ARG   A N    1 
ATOM   1285 C  CA   . ARG   A 1 178 ? 13.75600 19.06300  24.37100 1.000 17.05000 ?  174 ARG   A CA   1 
ATOM   1286 C  C    . ARG   A 1 178 ? 14.83500 18.55400  23.41800 1.000 15.25000 ?  174 ARG   A C    1 
ATOM   1287 O  O    . ARG   A 1 178 ? 14.71600 18.73600  22.20500 1.000 14.58000 ?  174 ARG   A O    1 
ATOM   1288 C  CB   . ARG   A 1 178 ? 13.22500 20.42800  23.91300 1.000 21.54000 ?  174 ARG   A CB   1 
ATOM   1289 C  CG   . ARG   A 1 178 ? 11.95300 20.83600  24.67900 1.000 28.63000 ?  174 ARG   A CG   1 
ATOM   1290 C  CD   . ARG   A 1 178 ? 11.16900 21.94200  23.99000 1.000 41.60000 ?  174 ARG   A CD   1 
ATOM   1291 N  NE   . ARG   A 1 178 ? 10.86600 21.62200  22.59900 1.000 36.36000 ?  174 ARG   A NE   1 
ATOM   1292 C  CZ   . ARG   A 1 178 ? 10.27700 22.45700  21.75400 1.000 37.23000 ?  174 ARG   A CZ   1 
ATOM   1293 N  NH1  . ARG   A 1 178 ? 9.85800  23.65000  22.14300 1.000 42.45000 ?  174 ARG   A NH1  1 
ATOM   1294 N  NH2  . ARG   A 1 178 ? 10.11500 22.08900  20.48600 1.000 38.85000 ?  174 ARG   A NH2  1 
ATOM   1295 N  N    A VAL   A 1 179 ? 15.88500 17.91700  23.93800 0.530 13.45000 ?  175 VAL   A N    1 
ATOM   1296 N  N    B VAL   A 1 179 ? 15.98500 17.91700  23.93800 0.470 13.14000 ?  175 VAL   A N    1 
ATOM   1297 C  CA   A VAL   A 1 179 ? 16.92700 17.35000  23.08400 0.530 13.45000 ?  175 VAL   A CA   1 
ATOM   1298 C  CA   B VAL   A 1 179 ? 17.02700 17.35000  23.08400 0.470 13.26000 ?  175 VAL   A CA   1 
ATOM   1299 C  C    A VAL   A 1 179 ? 17.37900 15.99900  23.62400 0.530 14.49000 ?  175 VAL   A C    1 
ATOM   1300 C  C    B VAL   A 1 179 ? 17.47900 15.99900  23.62400 0.470 14.48000 ?  175 VAL   A C    1 
ATOM   1301 O  O    A VAL   A 1 179 ? 17.38500 15.75300  24.83600 0.530 14.30000 ?  175 VAL   A O    1 
ATOM   1302 O  O    B VAL   A 1 179 ? 17.48500 15.75300  24.83600 0.470 14.34000 ?  175 VAL   A O    1 
ATOM   1303 C  CB   A VAL   A 1 179 ? 18.12500 18.32300  22.93300 0.530 16.63000 ?  175 VAL   A CB   1 
ATOM   1304 C  CB   B VAL   A 1 179 ? 18.22500 18.32300  22.93300 0.470 16.65000 ?  175 VAL   A CB   1 
ATOM   1305 C  CG1  A VAL   A 1 179 ? 18.79500 18.57300  24.27100 0.530 19.53000 ?  175 VAL   A CG1  1 
ATOM   1306 C  CG1  B VAL   A 1 179 ? 19.35300 17.68000  22.14800 0.470 19.53000 ?  175 VAL   A CG1  1 
ATOM   1307 C  CG2  A VAL   A 1 179 ? 19.12700 17.78700  21.91800 0.530 20.72000 ?  175 VAL   A CG2  1 
ATOM   1308 C  CG2  B VAL   A 1 179 ? 17.78000 19.62300  22.27500 0.470 20.72000 ?  175 VAL   A CG2  1 
ATOM   1309 N  N    . ILE   A 1 180 ? 17.72200 15.10300  22.70100 1.000 11.39000 ?  176 ILE   A N    1 
ATOM   1310 C  CA   . ILE   A 1 180 ? 18.42000 13.85700  23.00100 1.000 11.32000 ?  176 ILE   A CA   1 
ATOM   1311 C  C    . ILE   A 1 180 ? 19.53200 13.70400  21.96800 1.000 12.95000 ?  176 ILE   A C    1 
ATOM   1312 O  O    . ILE   A 1 180 ? 19.31900 13.94900  20.77600 1.000 12.92000 ?  176 ILE   A O    1 
ATOM   1313 C  CB   . ILE   A 1 180 ? 17.45600 12.65000  22.97700 1.000 11.22000 ?  176 ILE   A CB   1 
ATOM   1314 C  CG1  . ILE   A 1 180 ? 18.10900 11.38500  23.54900 1.000 14.86000 ?  176 ILE   A CG1  1 
ATOM   1315 C  CG2  . ILE   A 1 180 ? 16.90500 12.39300  21.56000 1.000 10.50000 ?  176 ILE   A CG2  1 
ATOM   1316 C  CD1  . ILE   A 1 180 ? 18.50100 11.49500  25.02800 1.000 11.62000 ?  176 ILE   A CD1  1 
ATOM   1317 N  N    . SER   A 1 181 ? 20.72700 13.32200  22.41200 1.000 13.88000 ?  177 SER   A N    1 
ATOM   1318 C  CA   . SER   A 1 181 ? 21.76800 13.11200  21.42100 1.000 11.67000 ?  177 SER   A CA   1 
ATOM   1319 C  C    . SER   A 1 181 ? 21.47600 11.83700  20.65100 1.000 10.94000 ?  177 SER   A C    1 
ATOM   1320 O  O    . SER   A 1 181 ? 20.91400 10.87900  21.18500 1.000 13.76000 ?  177 SER   A O    1 
ATOM   1321 C  CB   . SER   A 1 181 ? 23.16200 13.05100  22.06100 1.000 15.64000 ?  177 SER   A CB   1 
ATOM   1322 O  OG   . SER   A 1 181 ? 23.40900 11.82300  22.71800 1.000 17.16000 ?  177 SER   A OG   1 
ATOM   1323 N  N    . LYS   A 1 182 ? 21.85800 11.83800  19.37300 1.000 10.81000 ?  178 LYS   A N    1 
ATOM   1324 C  CA   . LYS   A 1 182 ? 21.68700 10.64000  18.55900 1.000 14.98000 ?  178 LYS   A CA   1 
ATOM   1325 C  C    . LYS   A 1 182 ? 22.32800 9.42300   19.22000 1.000 13.61000 ?  178 LYS   A C    1 
ATOM   1326 O  O    . LYS   A 1 182 ? 21.78500 8.31800   19.15400 1.000 10.87000 ?  178 LYS   A O    1 
ATOM   1327 C  CB   . LYS   A 1 182 ? 22.26000 10.87000  17.15700 1.000 15.09000 ?  178 LYS   A CB   1 
ATOM   1328 C  CG   . LYS   A 1 182 ? 23.77500 11.13100  17.10800 1.000 15.01000 ?  178 LYS   A CG   1 
ATOM   1329 C  CD   . LYS   A 1 182 ? 24.19600 11.43500  15.68300 1.000 19.02000 ?  178 LYS   A CD   1 
ATOM   1330 C  CE   . LYS   A 1 182 ? 25.66500 11.80500  15.60100 1.000 17.39000 ?  178 LYS   A CE   1 
ATOM   1331 N  NZ   . LYS   A 1 182 ? 26.03000 12.17200  14.21100 1.000 18.33000 ?  178 LYS   A NZ   1 
ATOM   1332 N  N    . HIS   A 1 183 ? 23.47500 9.61200   19.88400 1.000 12.91000 ?  179 HIS   A N    1 
ATOM   1333 C  CA   . HIS   A 1 183 ? 24.14300 8.49400   20.54900 1.000 11.00000 ?  179 HIS   A CA   1 
ATOM   1334 C  C    . HIS   A 1 183 ? 23.34000 7.99100   21.73400 1.000 10.87000 ?  179 HIS   A C    1 
ATOM   1335 O  O    . HIS   A 1 183 ? 23.23200 6.77700   21.95200 1.000 13.05000 ?  179 HIS   A O    1 
ATOM   1336 C  CB   . HIS   A 1 183 ? 25.53500 8.92400   21.00100 1.000 12.28000 ?  179 HIS   A CB   1 
ATOM   1337 C  CG   . HIS   A 1 183 ? 26.38700 9.42400   19.88500 1.000 13.45000 ?  179 HIS   A CG   1 
ATOM   1338 N  ND1  . HIS   A 1 183 ? 26.83000 8.60600   18.86800 1.000 17.90000 ?  179 HIS   A ND1  1 
ATOM   1339 C  CD2  . HIS   A 1 183 ? 26.85100 10.66400  19.60400 1.000 14.81000 ?  179 HIS   A CD2  1 
ATOM   1340 C  CE1  . HIS   A 1 183 ? 27.55200 9.31800   18.02100 1.000 16.51000 ?  179 HIS   A CE1  1 
ATOM   1341 N  NE2  . HIS   A 1 183 ? 27.57600 10.57000  18.44100 1.000 14.34000 ?  179 HIS   A NE2  1 
ATOM   1342 N  N    . ASP   A 1 184 ? 22.81600 8.90600   22.53900 1.000 12.61000 ?  180 ASP   A N    1 
ATOM   1343 C  CA   . ASP   A 1 184 ? 21.95700 8.50000   23.64800 1.000 11.99000 ?  180 ASP   A CA   1 
ATOM   1344 C  C    . ASP   A 1 184 ? 20.65100 7.87100   23.16200 1.000 11.20000 ?  180 ASP   A C    1 
ATOM   1345 O  O    . ASP   A 1 184 ? 20.13800 6.93800   23.79400 1.000 10.34000 ?  180 ASP   A O    1 
ATOM   1346 C  CB   . ASP   A 1 184 ? 21.69800 9.70300   24.56000 1.000 12.78000 ?  180 ASP   A CB   1 
ATOM   1347 C  CG   . ASP   A 1 184 ? 22.85500 9.93500   25.55600 1.000 13.62000 ?  180 ASP   A CG   1 
ATOM   1348 O  OD1  . ASP   A 1 184 ? 23.59000 8.96900   25.80500 1.000 14.82000 ?  180 ASP   A OD1  1 
ATOM   1349 O  OD2  . ASP   A 1 184 ? 23.01900 11.05900  26.09400 1.000 16.61000 ?  180 ASP   A OD2  1 
ATOM   1350 N  N    . LEU   A 1 185 ? 20.07300 8.38000   22.06900 1.000 11.80000 ?  181 LEU   A N    1 
ATOM   1351 C  CA   . LEU   A 1 185 ? 18.87200 7.74200   21.53400 1.000 10.94000 ?  181 LEU   A CA   1 
ATOM   1352 C  C    . LEU   A 1 185 ? 19.17400 6.30900   21.11300 1.000 10.78000 ?  181 LEU   A C    1 
ATOM   1353 O  O    . LEU   A 1 185 ? 18.42000 5.38200   21.43900 1.000 10.90000 ?  181 LEU   A O    1 
ATOM   1354 C  CB   . LEU   A 1 185 ? 18.31000 8.55600   20.36400 1.000 13.69000 ?  181 LEU   A CB   1 
ATOM   1355 C  CG   . LEU   A 1 185 ? 17.06800 8.00400   19.64600 1.000 10.35000 ?  181 LEU   A CG   1 
ATOM   1356 C  CD1  . LEU   A 1 185 ? 15.91100 7.73600   20.61700 1.000 10.26000 ?  181 LEU   A CD1  1 
ATOM   1357 C  CD2  . LEU   A 1 185 ? 16.61100 8.98500   18.57400 1.000 10.13000 ?  181 LEU   A CD2  1 
ATOM   1358 N  N    . GLY   A 1 186 ? 20.30100 6.10000   20.43000 1.000 11.67000 ?  182 GLY   A N    1 
ATOM   1359 C  CA   . GLY   A 1 186 ? 20.66800 4.74500   20.04600 1.000 11.73000 ?  182 GLY   A CA   1 
ATOM   1360 C  C    . GLY   A 1 186 ? 20.90300 3.86100   21.25000 1.000 14.69000 ?  182 GLY   A C    1 
ATOM   1361 O  O    . GLY   A 1 186 ? 20.45300 2.71000   21.29100 1.000 13.06000 ?  182 GLY   A O    1 
ATOM   1362 N  N    . HIS   A 1 187 ? 21.61900 4.39100   22.24400 1.000 12.61000 ?  183 HIS   A N    1 
ATOM   1363 C  CA   . HIS   A 1 187 ? 21.80600 3.69400   23.51500 1.000 12.96000 ?  183 HIS   A CA   1 
ATOM   1364 C  C    . HIS   A 1 187 ? 20.47200 3.24200   24.09500 1.000 14.09000 ?  183 HIS   A C    1 
ATOM   1365 O  O    . HIS   A 1 187 ? 20.33500 2.11100   24.57400 1.000 10.93000 ?  183 HIS   A O    1 
ATOM   1366 C  CB   . HIS   A 1 187 ? 22.52800 4.63300   24.48300 1.000 14.16000 ?  183 HIS   A CB   1 
ATOM   1367 C  CG   . HIS   A 1 187 ? 22.90500 4.00400   25.79200 1.000 14.57000 ?  183 HIS   A CG   1 
ATOM   1368 N  ND1  . HIS   A 1 187 ? 22.04600 3.96000   26.87300 1.000 15.39000 ?  183 HIS   A ND1  1 
ATOM   1369 C  CD2  . HIS   A 1 187 ? 24.05900 3.42400   26.20200 1.000 19.95000 ?  183 HIS   A CD2  1 
ATOM   1370 C  CE1  . HIS   A 1 187 ? 22.65300 3.36200   27.88600 1.000 19.46000 ?  183 HIS   A CE1  1 
ATOM   1371 N  NE2  . HIS   A 1 187 ? 23.87400 3.02700   27.50500 1.000 17.90000 ?  183 HIS   A NE2  1 
ATOM   1372 N  N    . PHE   A 1 188 ? 19.46800 4.12700   24.06900 1.000 11.39000 ?  184 PHE   A N    1 
ATOM   1373 C  CA   . PHE   A 1 188 ? 18.19000 3.77800   24.67600 1.000 12.83000 ?  184 PHE   A CA   1 
ATOM   1374 C  C    . PHE   A 1 188 ? 17.46500 2.69000   23.88700 1.000 13.74000 ?  184 PHE   A C    1 
ATOM   1375 O  O    . PHE   A 1 188 ? 16.85400 1.79200   24.48100 1.000 13.35000 ?  184 PHE   A O    1 
ATOM   1376 C  CB   . PHE   A 1 188 ? 17.31000 5.01800   24.82400 1.000 9.44000  ?  184 PHE   A CB   1 
ATOM   1377 C  CG   . PHE   A 1 188 ? 15.96500 4.71200   25.41800 1.000 13.24000 ?  184 PHE   A CG   1 
ATOM   1378 C  CD1  . PHE   A 1 188 ? 15.87600 4.16000   26.68600 1.000 12.25000 ?  184 PHE   A CD1  1 
ATOM   1379 C  CD2  . PHE   A 1 188 ? 14.80500 4.93300   24.69900 1.000 13.67000 ?  184 PHE   A CD2  1 
ATOM   1380 C  CE1  . PHE   A 1 188 ? 14.64900 3.84100   27.23400 1.000 12.49000 ?  184 PHE   A CE1  1 
ATOM   1381 C  CE2  . PHE   A 1 188 ? 13.56800 4.62500   25.24300 1.000 14.76000 ?  184 PHE   A CE2  1 
ATOM   1382 C  CZ   . PHE   A 1 188 ? 13.49200 4.07400   26.50700 1.000 15.90000 ?  184 PHE   A CZ   1 
ATOM   1383 N  N    A MET   A 1 189 ? 17.50500 2.77700   22.54800 0.690 12.57000 ?  185 MET   A N    1 
ATOM   1384 N  N    B MET   A 1 189 ? 17.52500 2.72400   22.56000 0.310 12.54000 ?  185 MET   A N    1 
ATOM   1385 C  CA   A MET   A 1 189 ? 16.89300 1.75300   21.70400 0.690 13.72000 ?  185 MET   A CA   1 
ATOM   1386 C  CA   B MET   A 1 189 ? 16.79200 1.69900   21.83200 0.310 13.67000 ?  185 MET   A CA   1 
ATOM   1387 C  C    A MET   A 1 189 ? 17.40900 0.37300   22.08700 0.690 14.24000 ?  185 MET   A C    1 
ATOM   1388 C  C    B MET   A 1 189 ? 17.43100 0.32400   21.97600 0.310 14.17000 ?  185 MET   A C    1 
ATOM   1389 O  O    A MET   A 1 189 ? 16.63300 -0.57700  22.25000 0.690 13.78000 ?  185 MET   A O    1 
ATOM   1390 O  O    B MET   A 1 189 ? 16.72900 -0.68500  21.85700 0.310 14.49000 ?  185 MET   A O    1 
ATOM   1391 C  CB   A MET   A 1 189 ? 17.18100 2.02800   20.22000 0.690 12.93000 ?  185 MET   A CB   1 
ATOM   1392 C  CB   B MET   A 1 189 ? 16.65400 2.10900   20.37500 0.310 12.89000 ?  185 MET   A CB   1 
ATOM   1393 C  CG   A MET   A 1 189 ? 16.77700 3.40800   19.67100 0.690 14.60000 ?  185 MET   A CG   1 
ATOM   1394 C  CG   B MET   A 1 189 ? 15.98400 3.45700   20.25900 0.310 12.70000 ?  185 MET   A CG   1 
ATOM   1395 S  SD   A MET   A 1 189 ? 15.00000 3.72600   19.46200 0.690 14.54000 ?  185 MET   A SD   1 
ATOM   1396 S  SD   B MET   A 1 189 ? 15.67200 3.93800   18.56500 0.310 13.36000 ?  185 MET   A SD   1 
ATOM   1397 C  CE   A MET   A 1 189 ? 14.53000 2.53800   18.19500 0.690 13.60000 ?  185 MET   A CE   1 
ATOM   1398 C  CE   B MET   A 1 189 ? 14.27300 2.89300   18.14900 0.310 12.87000 ?  185 MET   A CE   1 
ATOM   1399 N  N    . LEU   A 1 190 ? 18.73300 0.26200   22.27100 1.000 12.17000 ?  186 LEU   A N    1 
ATOM   1400 C  CA   . LEU   A 1 190 ? 19.34200 -1.00500  22.64900 1.000 13.34000 ?  186 LEU   A CA   1 
ATOM   1401 C  C    . LEU   A 1 190 ? 18.98200 -1.40000  24.07800 1.000 14.97000 ?  186 LEU   A C    1 
ATOM   1402 O  O    . LEU   A 1 190 ? 18.79400 -2.59000  24.35900 1.000 15.64000 ?  186 LEU   A O    1 
ATOM   1403 C  CB   . LEU   A 1 190 ? 20.86100 -0.93100  22.48800 1.000 12.32000 ?  186 LEU   A CB   1 
ATOM   1404 C  CG   . LEU   A 1 190 ? 21.32700 -0.72400  21.04600 1.000 15.47000 ?  186 LEU   A CG   1 
ATOM   1405 C  CD1  . LEU   A 1 190 ? 22.81500 -0.46400  21.00700 1.000 17.23000 ?  186 LEU   A CD1  1 
ATOM   1406 C  CD2  . LEU   A 1 190 ? 20.96800 -1.92400  20.17700 1.000 17.22000 ?  186 LEU   A CD2  1 
ATOM   1407 N  N    . ARG   A 1 191 ? 18.89600 -0.42500  24.99200 1.000 14.42000 ?  187 ARG   A N    1 
ATOM   1408 C  CA   . ARG   A 1 191 ? 18.44100 -0.72700  26.35200 1.000 14.40000 ?  187 ARG   A CA   1 
ATOM   1409 C  C    . ARG   A 1 191 ? 17.07200 -1.40100  26.34800 1.000 16.07000 ?  187 ARG   A C    1 
ATOM   1410 O  O    . ARG   A 1 191 ? 16.81500 -2.30000  27.15700 1.000 16.83000 ?  187 ARG   A O    1 
ATOM   1411 C  CB   . ARG   A 1 191 ? 18.37900 0.55400   27.19500 1.000 13.62000 ?  187 ARG   A CB   1 
ATOM   1412 C  CG   . ARG   A 1 191 ? 17.81200 0.32800   28.59800 1.000 19.98000 ?  187 ARG   A CG   1 
ATOM   1413 C  CD   . ARG   A 1 191 ? 17.39900 1.62000   29.30000 1.000 29.17000 ?  187 ARG   A CD   1 
ATOM   1414 N  NE   . ARG   A 1 191 ? 18.54600 2.44200   29.66500 1.000 31.40000 ?  187 ARG   A NE   1 
ATOM   1415 C  CZ   . ARG   A 1 191 ? 18.48800 3.50100   30.46200 1.000 35.15000 ?  187 ARG   A CZ   1 
ATOM   1416 N  NH1  . ARG   A 1 191 ? 17.34700 3.89400   31.00800 1.000 37.03000 ?  187 ARG   A NH1  1 
ATOM   1417 N  NH2  . ARG   A 1 191 ? 19.60400 4.17900   30.72000 1.000 38.41000 ?  187 ARG   A NH2  1 
ATOM   1418 N  N    . CYS   A 1 192 ? 16.17600 -0.97100  25.45000 1.000 12.22000 ?  188 CYS   A N    1 
ATOM   1419 C  CA   . CYS   A 1 192 ? 14.84200 -1.54900  25.32700 1.000 13.80000 ?  188 CYS   A CA   1 
ATOM   1420 C  C    . CYS   A 1 192 ? 14.85600 -3.00600  24.89600 1.000 16.06000 ?  188 CYS   A C    1 
ATOM   1421 O  O    . CYS   A 1 192 ? 13.83000 -3.67100  25.03000 1.000 18.35000 ?  188 CYS   A O    1 
ATOM   1422 C  CB   . CYS   A 1 192 ? 14.01000 -0.73200  24.33500 1.000 15.50000 ?  188 CYS   A CB   1 
ATOM   1423 S  SG   . CYS   A 1 192 ? 13.59700 0.89500   24.95800 1.000 17.39000 ?  188 CYS   A SG   1 
ATOM   1424 N  N    . LEU   A 1 193 ? 15.98200 -3.50900  24.39000 1.000 14.35000 ?  189 LEU   A N    1 
ATOM   1425 C  CA   . LEU   A 1 193 ? 16.11900 -4.92900  24.08400 1.000 13.90000 ?  189 LEU   A CA   1 
ATOM   1426 C  C    . LEU   A 1 193 ? 16.38600 -5.77700  25.31600 1.000 18.58000 ?  189 LEU   A C    1 
ATOM   1427 O  O    . LEU   A 1 193 ? 16.19300 -6.99400  25.26200 1.000 20.98000 ?  189 LEU   A O    1 
ATOM   1428 C  CB   . LEU   A 1 193 ? 17.25900 -5.16800  23.09200 1.000 18.72000 ?  189 LEU   A CB   1 
ATOM   1429 C  CG   . LEU   A 1 193 ? 17.19700 -4.37700  21.78700 1.000 19.25000 ?  189 LEU   A CG   1 
ATOM   1430 C  CD1  . LEU   A 1 193 ? 18.48700 -4.59000  20.99400 1.000 15.89000 ?  189 LEU   A CD1  1 
ATOM   1431 C  CD2  . LEU   A 1 193 ? 15.98200 -4.79300  20.98400 1.000 17.54000 ?  189 LEU   A CD2  1 
ATOM   1432 N  N    . THR   A 1 194 ? 16.81900 -5.17300  26.41600 1.000 17.15000 ?  190 THR   A N    1 
ATOM   1433 C  CA   . THR   A 1 194 ? 17.23200 -5.92600  27.59100 1.000 18.77000 ?  190 THR   A CA   1 
ATOM   1434 C  C    . THR   A 1 194 ? 16.17000 -5.96500  28.67400 1.000 18.15000 ?  190 THR   A C    1 
ATOM   1435 O  O    . THR   A 1 194 ? 16.39200 -6.58600  29.71500 1.000 18.62000 ?  190 THR   A O    1 
ATOM   1436 C  CB   . THR   A 1 194 ? 18.51400 -5.33100  28.17700 1.000 21.07000 ?  190 THR   A CB   1 
ATOM   1437 O  OG1  . THR   A 1 194 ? 18.20000 -4.08900  28.81600 1.000 21.45000 ?  190 THR   A OG1  1 
ATOM   1438 C  CG2  . THR   A 1 194 ? 19.53300 -5.07900  27.08100 1.000 22.45000 ?  190 THR   A CG2  1 
ATOM   1439 N  N    . THR   A 1 195 ? 15.03400 -5.31100  28.45900 1.000 16.08000 ?  191 THR   A N    1 
ATOM   1440 C  CA   . THR   A 1 195 ? 13.98600 -5.25500  29.46200 1.000 17.30000 ?  191 THR   A CA   1 
ATOM   1441 C  C    . THR   A 1 195 ? 12.65100 -5.20500  28.74600 1.000 17.09000 ?  191 THR   A C    1 
ATOM   1442 O  O    . THR   A 1 195 ? 12.56500 -4.72400  27.61200 1.000 15.70000 ?  191 THR   A O    1 
ATOM   1443 C  CB   . THR   A 1 195 ? 14.15000 -4.03100  30.37300 1.000 17.84000 ?  191 THR   A CB   1 
ATOM   1444 O  OG1  . THR   A 1 195 ? 13.11300 -4.02800  31.35800 1.000 15.85000 ?  191 THR   A OG1  1 
ATOM   1445 C  CG2  . THR   A 1 195 ? 14.05000 -2.73800  29.55500 1.000 15.65000 ?  191 THR   A CG2  1 
ATOM   1446 N  N    . ASP   A 1 196 ? 11.61700 -5.73900  29.39600 1.000 13.06000 ?  192 ASP   A N    1 
ATOM   1447 C  CA   . ASP   A 1 196 ? 10.25400 -5.59400  28.90800 1.000 15.17000 ?  192 ASP   A CA   1 
ATOM   1448 C  C    . ASP   A 1 196 ? 9.49700  -4.46600  29.60300 1.000 13.23000 ?  192 ASP   A C    1 
ATOM   1449 O  O    . ASP   A 1 196 ? 8.31400  -4.26900  29.31300 1.000 14.27000 ?  192 ASP   A O    1 
ATOM   1450 C  CB   . ASP   A 1 196 ? 9.47900  -6.90800  29.07700 1.000 16.52000 ?  192 ASP   A CB   1 
ATOM   1451 C  CG   . ASP   A 1 196 ? 9.93900  -8.00000  28.11800 1.000 23.86000 ?  192 ASP   A CG   1 
ATOM   1452 O  OD1  . ASP   A 1 196 ? 10.82700 -7.74700  27.27500 1.000 24.04000 ?  192 ASP   A OD1  1 
ATOM   1453 O  OD2  . ASP   A 1 196 ? 9.39400  -9.12300  28.20900 1.000 24.29000 ?  192 ASP   A OD2  1 
ATOM   1454 N  N    . GLU   A 1 197 ? 10.14100 -3.73000  30.51400 1.000 13.63000 ?  193 GLU   A N    1 
ATOM   1455 C  CA   . GLU   A 1 197 ? 9.42100  -2.77100  31.34700 1.000 15.86000 ?  193 GLU   A CA   1 
ATOM   1456 C  C    . GLU   A 1 197 ? 8.83800  -1.61000  30.54600 1.000 16.32000 ?  193 GLU   A C    1 
ATOM   1457 O  O    . GLU   A 1 197 ? 7.96000  -0.90600  31.05500 1.000 15.30000 ?  193 GLU   A O    1 
ATOM   1458 C  CB   . GLU   A 1 197 ? 10.33900 -2.23200  32.44400 1.000 15.16000 ?  193 GLU   A CB   1 
ATOM   1459 C  CG   . GLU   A 1 197 ? 11.50200 -1.42400  31.92900 1.000 16.82000 ?  193 GLU   A CG   1 
ATOM   1460 C  CD   . GLU   A 1 197 ? 12.55200 -1.21400  32.99800 1.000 24.99000 ?  193 GLU   A CD   1 
ATOM   1461 O  OE1  . GLU   A 1 197 ? 12.35200 -0.33300  33.86000 1.000 29.18000 ?  193 GLU   A OE1  1 
ATOM   1462 O  OE2  . GLU   A 1 197 ? 13.55800 -1.95000  32.98200 1.000 26.04000 ?  193 GLU   A OE2  1 
ATOM   1463 N  N    . TYR   A 1 198 ? 9.29400  -1.39800  29.31000 1.000 15.14000 ?  194 TYR   A N    1 
ATOM   1464 C  CA   . TYR   A 1 198 ? 8.75700  -0.34000  28.46500 1.000 14.59000 ?  194 TYR   A CA   1 
ATOM   1465 C  C    . TYR   A 1 198 ? 7.75700  -0.83800  27.43000 1.000 11.81000 ?  194 TYR   A C    1 
ATOM   1466 O  O    . TYR   A 1 198 ? 7.20200  -0.01600  26.69100 1.000 13.03000 ?  194 TYR   A O    1 
ATOM   1467 C  CB   . TYR   A 1 198 ? 9.88900  0.39900   27.73800 1.000 14.85000 ?  194 TYR   A CB   1 
ATOM   1468 C  CG   . TYR   A 1 198 ? 10.99500 0.93100   28.62700 1.000 15.62000 ?  194 TYR   A CG   1 
ATOM   1469 C  CD1  . TYR   A 1 198 ? 10.74300 1.88100   29.60800 1.000 16.74000 ?  194 TYR   A CD1  1 
ATOM   1470 C  CD2  . TYR   A 1 198 ? 12.28800 0.49500   28.46700 1.000 15.92000 ?  194 TYR   A CD2  1 
ATOM   1471 C  CE1  . TYR   A 1 198 ? 11.77900 2.36900   30.41400 1.000 16.91000 ?  194 TYR   A CE1  1 
ATOM   1472 C  CE2  . TYR   A 1 198 ? 13.31300 0.96800   29.25800 1.000 20.49000 ?  194 TYR   A CE2  1 
ATOM   1473 C  CZ   . TYR   A 1 198 ? 13.05100 1.90700   30.22700 1.000 23.30000 ?  194 TYR   A CZ   1 
ATOM   1474 O  OH   . TYR   A 1 198 ? 14.09200 2.36600   30.99700 1.000 25.33000 ?  194 TYR   A OH   1 
ATOM   1475 N  N    . ASP   A 1 199 ? 7.52800  -2.14900  27.33900 1.000 12.51000 ?  195 ASP   A N    1 
ATOM   1476 C  CA   . ASP   A 1 199 ? 6.61600  -2.68900  26.33600 1.000 13.20000 ?  195 ASP   A CA   1 
ATOM   1477 C  C    . ASP   A 1 199 ? 5.22800  -2.09800  26.50000 1.000 17.58000 ?  195 ASP   A C    1 
ATOM   1478 O  O    . ASP   A 1 199 ? 4.68100  -2.09100  27.60300 1.000 14.97000 ?  195 ASP   A O    1 
ATOM   1479 C  CB   . ASP   A 1 199 ? 6.51700  -4.21200  26.45400 1.000 13.31000 ?  195 ASP   A CB   1 
ATOM   1480 C  CG   . ASP   A 1 199 ? 7.82800  -4.92400  26.15000 1.000 15.73000 ?  195 ASP   A CG   1 
ATOM   1481 O  OD1  . ASP   A 1 199 ? 8.81800  -4.26700  25.75700 1.000 15.76000 ?  195 ASP   A OD1  1 
ATOM   1482 O  OD2  . ASP   A 1 199 ? 7.85900  -6.16000  26.31300 1.000 16.11000 ?  195 ASP   A OD2  1 
ATOM   1483 N  N    . GLY   A 1 200 ? 4.64200  -1.63700  25.39100 1.000 12.69000 ?  196 GLY   A N    1 
ATOM   1484 C  CA   . GLY   A 1 200 ? 3.31000  -1.06600  25.40900 1.000 15.24000 ?  196 GLY   A CA   1 
ATOM   1485 C  C    . GLY   A 1 200 ? 3.23300  0.36400   25.89600 1.000 18.01000 ?  196 GLY   A C    1 
ATOM   1486 O  O    . GLY   A 1 200 ? 2.12700  0.92500   25.94900 1.000 16.15000 ?  196 GLY   A O    1 
ATOM   1487 N  N    . HIS   A 1 201 ? 4.36300  0.96400   26.25200 1.000 14.63000 ?  197 HIS   A N    1 
ATOM   1488 C  CA   . HIS   A 1 201 ? 4.46200  2.36000   26.64400 1.000 15.03000 ?  197 HIS   A CA   1 
ATOM   1489 C  C    . HIS   A 1 201 ? 5.03700  3.19900   25.51100 1.000 16.26000 ?  197 HIS   A C    1 
ATOM   1490 O  O    . HIS   A 1 201 ? 5.66700  2.69000   24.58000 1.000 12.32000 ?  197 HIS   A O    1 
ATOM   1491 C  CB   . HIS   A 1 201 ? 5.38600  2.53100   27.85800 1.000 14.55000 ?  197 HIS   A CB   1 
ATOM   1492 C  CG   . HIS   A 1 201 ? 4.88200  1.89300   29.11300 1.000 16.39000 ?  197 HIS   A CG   1 
ATOM   1493 N  ND1  . HIS   A 1 201 ? 4.04700  2.55100   29.99300 1.000 20.22000 ?  197 HIS   A ND1  1 
ATOM   1494 C  CD2  . HIS   A 1 201 ? 5.11600  0.67200   29.65500 1.000 18.71000 ?  197 HIS   A CD2  1 
ATOM   1495 C  CE1  . HIS   A 1 201 ? 3.77600  1.75600   31.01500 1.000 25.18000 ?  197 HIS   A CE1  1 
ATOM   1496 N  NE2  . HIS   A 1 201 ? 4.41700  0.61400   30.83700 1.000 21.07000 ?  197 HIS   A NE2  1 
ATOM   1497 N  N    A SER   A 1 202 ? 4.82300  4.50200   25.61400 0.540 15.65000 ?  198 SER   A N    1 
ATOM   1498 N  N    B SER   A 1 202 ? 4.81300  4.50400   25.60300 0.460 15.65000 ?  198 SER   A N    1 
ATOM   1499 C  CA   A SER   A 1 202 ? 5.60100  5.47000   24.86300 0.540 13.66000 ?  198 SER   A CA   1 
ATOM   1500 C  CA   B SER   A 1 202 ? 5.60400  5.46800   24.85600 0.460 13.69000 ?  198 SER   A CA   1 
ATOM   1501 C  C    A SER   A 1 202 ? 6.72000  5.97400   25.76100 0.540 15.41000 ?  198 SER   A C    1 
ATOM   1502 C  C    B SER   A 1 202 ? 6.72500  5.95600   25.76100 0.460 15.41000 ?  198 SER   A C    1 
ATOM   1503 O  O    A SER   A 1 202 ? 6.52800  6.15100   26.97100 0.540 15.27000 ?  198 SER   A O    1 
ATOM   1504 O  O    B SER   A 1 202 ? 6.53300  6.11700   26.97200 0.460 15.30000 ?  198 SER   A O    1 
ATOM   1505 C  CB   A SER   A 1 202 ? 4.72800  6.62500   24.37900 0.540 16.06000 ?  198 SER   A CB   1 
ATOM   1506 C  CB   B SER   A 1 202 ? 4.76400  6.65000   24.37400 0.460 16.05000 ?  198 SER   A CB   1 
ATOM   1507 O  OG   A SER   A 1 202 ? 3.64200  6.12100   23.61600 0.540 13.85000 ?  198 SER   A OG   1 
ATOM   1508 O  OG   B SER   A 1 202 ? 4.53400  7.56800   25.42300 0.460 15.09000 ?  198 SER   A OG   1 
ATOM   1509 N  N    . THR   A 1 203 ? 7.89600  6.17000   25.17400 1.000 13.33000 ?  199 THR   A N    1 
ATOM   1510 C  CA   . THR   A 1 203 ? 9.08400  6.55300   25.92200 1.000 13.91000 ?  199 THR   A CA   1 
ATOM   1511 C  C    . THR   A 1 203 ? 9.68400  7.80000   25.29400 1.000 12.62000 ?  199 THR   A C    1 
ATOM   1512 O  O    . THR   A 1 203 ? 9.83000  7.87800   24.06700 1.000 14.96000 ?  199 THR   A O    1 
ATOM   1513 C  CB   . THR   A 1 203 ? 10.11900 5.41600   25.96400 1.000 15.10000 ?  199 THR   A CB   1 
ATOM   1514 O  OG1  . THR   A 1 203 ? 10.46800 5.02700   24.63000 1.000 13.32000 ?  199 THR   A OG1  1 
ATOM   1515 C  CG2  . THR   A 1 203 ? 9.54700  4.19800   26.70900 1.000 12.24000 ?  199 THR   A CG2  1 
ATOM   1516 N  N    . TYR   A 1 204 ? 10.01200 8.76400   26.14200 1.000 11.38000 ?  200 TYR   A N    1 
ATOM   1517 C  CA   . TYR   A 1 204 ? 10.58300 10.05100  25.73500 1.000 10.35000 ?  200 TYR   A CA   1 
ATOM   1518 C  C    . TYR   A 1 204 ? 11.96100 10.16100  26.37200 1.000 12.58000 ?  200 TYR   A C    1 
ATOM   1519 O  O    . TYR   A 1 204 ? 12.06500 10.48700  27.57000 1.000 12.75000 ?  200 TYR   A O    1 
ATOM   1520 C  CB   . TYR   A 1 204 ? 9.66800  11.18900  26.19100 1.000 11.07000 ?  200 TYR   A CB   1 
ATOM   1521 C  CG   . TYR   A 1 204 ? 10.05900 12.62400  25.86700 1.000 10.27000 ?  200 TYR   A CG   1 
ATOM   1522 C  CD1  . TYR   A 1 204 ? 11.06600 13.29000  26.58500 1.000 12.74000 ?  200 TYR   A CD1  1 
ATOM   1523 C  CD2  . TYR   A 1 204 ? 9.35000  13.35000  24.92400 1.000 12.62000 ?  200 TYR   A CD2  1 
ATOM   1524 C  CE1  . TYR   A 1 204 ? 11.38100 14.62700  26.31900 1.000 11.15000 ?  200 TYR   A CE1  1 
ATOM   1525 C  CE2  . TYR   A 1 204 ? 9.65300  14.68100  24.65300 1.000 14.60000 ?  200 TYR   A CE2  1 
ATOM   1526 C  CZ   . TYR   A 1 204 ? 10.66300 15.31200  25.35200 1.000 14.59000 ?  200 TYR   A CZ   1 
ATOM   1527 O  OH   . TYR   A 1 204 ? 10.94600 16.63200  25.08000 1.000 15.84000 ?  200 TYR   A OH   1 
ATOM   1528 N  N    . PRO   A 1 205 ? 13.04200 9.87600   25.63600 1.000 11.28000 ?  201 PRO   A N    1 
ATOM   1529 C  CA   . PRO   A 1 205 ? 14.39500 10.06700  26.18600 1.000 11.13000 ?  201 PRO   A CA   1 
ATOM   1530 C  C    . PRO   A 1 205 ? 14.81800 11.51900  26.00300 1.000 12.06000 ?  201 PRO   A C    1 
ATOM   1531 O  O    . PRO   A 1 205 ? 14.66700 12.07500  24.91700 1.000 12.04000 ?  201 PRO   A O    1 
ATOM   1532 C  CB   . PRO   A 1 205 ? 15.26000 9.13900   25.32600 1.000 12.79000 ?  201 PRO   A CB   1 
ATOM   1533 C  CG   . PRO   A 1 205 ? 14.56600 9.19000   23.96400 1.000 13.11000 ?  201 PRO   A CG   1 
ATOM   1534 C  CD   . PRO   A 1 205 ? 13.06900 9.33700   24.26000 1.000 10.41000 ?  201 PRO   A CD   1 
ATOM   1535 N  N    . SER   A 1 206 ? 15.36100 12.13500  27.05000 1.000 13.10000 ?  202 SER   A N    1 
ATOM   1536 C  CA   . SER   A 1 206 ? 15.85100 13.50200  26.89500 1.000 12.14000 ?  202 SER   A CA   1 
ATOM   1537 C  C    . SER   A 1 206 ? 16.95700 13.76900  27.91000 1.000 14.09000 ?  202 SER   A C    1 
ATOM   1538 O  O    . SER   A 1 206 ? 17.07800 13.07000  28.91600 1.000 16.01000 ?  202 SER   A O    1 
ATOM   1539 C  CB   . SER   A 1 206 ? 14.72000 14.53700  27.03900 1.000 14.64000 ?  202 SER   A CB   1 
ATOM   1540 O  OG   . SER   A 1 206 ? 14.28800 14.68800  28.38400 1.000 13.84000 ?  202 SER   A OG   1 
ATOM   1541 N  N    . HIS   A 1 207 ? 17.76700 14.77900  27.60800 1.000 14.71000 ?  203 HIS   A N    1 
ATOM   1542 C  CA   . HIS   A 1 207 ? 18.88200 15.12700  28.51700 1.000 18.97000 ?  203 HIS   A CA   1 
ATOM   1543 C  C    . HIS   A 1 207 ? 19.32500 16.58200  28.36100 1.000 20.46000 ?  203 HIS   A C    1 
ATOM   1544 O  O    . HIS   A 1 207 ? 19.02700 17.19600  27.35400 1.000 18.89000 ?  203 HIS   A O    1 
ATOM   1545 C  CB   . HIS   A 1 207 ? 20.05100 14.17500  28.24400 1.000 15.62000 ?  203 HIS   A CB   1 
ATOM   1546 C  CG   . HIS   A 1 207 ? 21.08900 14.16000  29.29900 1.000 16.63000 ?  203 HIS   A CG   1 
ATOM   1547 N  ND1  . HIS   A 1 207 ? 20.77100 14.08300  30.62800 1.000 20.31000 ?  203 HIS   A ND1  1 
ATOM   1548 C  CD2  . HIS   A 1 207 ? 22.42700 14.24100  29.22400 1.000 20.56000 ?  203 HIS   A CD2  1 
ATOM   1549 C  CE1  . HIS   A 1 207 ? 21.87200 14.10900  31.33500 1.000 21.24000 ?  203 HIS   A CE1  1 
ATOM   1550 N  NE2  . HIS   A 1 207 ? 22.89000 14.20500  30.49800 1.000 21.06000 ?  203 HIS   A NE2  1 
ATOM   1551 N  N    . GLN   A 1 208 ? 20.03400 17.08100  29.37100 1.000 25.78000 ?  204 GLN   A N    1 
ATOM   1552 C  CA   . GLN   A 1 208 ? 20.65700 18.41600  29.24800 1.000 27.87000 ?  204 GLN   A CA   1 
ATOM   1553 C  C    . GLN   A 1 208 ? 22.15600 18.17300  29.02800 1.000 24.17000 ?  204 GLN   A C    1 
ATOM   1554 O  O    . GLN   A 1 208 ? 22.76600 17.49600  29.84300 1.000 26.17000 ?  204 GLN   A O    1 
ATOM   1555 C  CB   . GLN   A 1 208 ? 20.36700 19.30300  30.46200 1.000 31.53000 ?  204 GLN   A CB   1 
ATOM   1556 C  CG   . GLN   A 1 208 ? 18.90800 19.31100  30.88800 1.000 38.67000 ?  204 GLN   A CG   1 
ATOM   1557 C  CD   . GLN   A 1 208 ? 18.11300 20.45600  30.31100 1.000 59.99000 ?  204 GLN   A CD   1 
ATOM   1558 O  OE1  . GLN   A 1 208 ? 18.65500 21.36100  29.68200 1.000 69.08000 ?  204 GLN   A OE1  1 
ATOM   1559 N  NE2  . GLN   A 1 208 ? 16.80900 20.43000  30.53600 1.000 53.01000 ?  204 GLN   A NE2  1 
ATOM   1560 N  N    . TYR   A 1 209 ? 22.68600 18.68400  27.92900 1.000 23.67000 ?  205 TYR   A N    1 
ATOM   1561 C  CA   . TYR   A 1 209 ? 24.13000 18.53900  27.63200 1.000 25.31000 ?  205 TYR   A CA   1 
ATOM   1562 C  C    . TYR   A 1 209 ? 24.84700 19.85700  27.97300 1.000 27.83000 ?  205 TYR   A C    1 
ATOM   1563 O  O    . TYR   A 1 209 ? 25.98000 19.69900  28.43000 1.000 41.40000 ?  205 TYR   A O    1 
ATOM   1564 C  CB   . TYR   A 1 209 ? 24.31800 18.07800  26.18900 1.000 24.05000 ?  205 TYR   A CB   1 
ATOM   1565 C  CG   . TYR   A 1 209 ? 23.59200 16.78600  25.89000 1.000 23.07000 ?  205 TYR   A CG   1 
ATOM   1566 C  CD1  . TYR   A 1 209 ? 22.27500 16.77500  25.46100 1.000 18.98000 ?  205 TYR   A CD1  1 
ATOM   1567 C  CD2  . TYR   A 1 209 ? 24.21400 15.56500  26.07100 1.000 21.39000 ?  205 TYR   A CD2  1 
ATOM   1568 C  CE1  . TYR   A 1 209 ? 21.60300 15.59100  25.20600 1.000 15.72000 ?  205 TYR   A CE1  1 
ATOM   1569 C  CE2  . TYR   A 1 209 ? 23.56100 14.37300  25.81400 1.000 15.77000 ?  205 TYR   A CE2  1 
ATOM   1570 C  CZ   . TYR   A 1 209 ? 22.24700 14.38300  25.38700 1.000 17.89000 ?  205 TYR   A CZ   1 
ATOM   1571 O  OH   . TYR   A 1 209 ? 21.60400 13.20600  25.15100 1.000 13.96000 ?  205 TYR   A OH   1 
HETATM 1572 P  PA   . NAP   B 2 .   ? 17.55200 9.43500   9.15800  1.000 14.32000 ?  301 NAP   A PA   1 
HETATM 1573 O  O1A  . NAP   B 2 .   ? 16.57000 10.25600  8.42000  1.000 14.62000 ?  301 NAP   A O1A  1 
HETATM 1574 O  O2A  . NAP   B 2 .   ? 18.96400 10.17800  9.33400  1.000 15.96000 ?  301 NAP   A O2A  1 
HETATM 1575 O  O5B  . NAP   B 2 .   ? 17.89000 8.08500   8.34900  1.000 14.14000 ?  301 NAP   A O5B  1 
HETATM 1576 C  C5B  . NAP   B 2 .   ? 16.69700 7.47700   7.86400  1.000 13.86000 ?  301 NAP   A C5B  1 
HETATM 1577 C  C4B  . NAP   B 2 .   ? 17.00300 5.99700   7.60700  1.000 11.28000 ?  301 NAP   A C4B  1 
HETATM 1578 O  O4B  . NAP   B 2 .   ? 15.87800 5.37600   6.96600  1.000 12.46000 ?  301 NAP   A O4B  1 
HETATM 1579 C  C3B  . NAP   B 2 .   ? 18.21800 5.81200   6.67000  1.000 11.18000 ?  301 NAP   A C3B  1 
HETATM 1580 O  O3B  . NAP   B 2 .   ? 18.98500 4.67700   7.07100  1.000 12.08000 ?  301 NAP   A O3B  1 
HETATM 1581 C  C2B  . NAP   B 2 .   ? 17.56600 5.49500   5.30700  1.000 12.48000 ?  301 NAP   A C2B  1 
HETATM 1582 O  O2B  . NAP   B 2 .   ? 18.40500 4.64900   4.51200  1.000 13.67000 ?  301 NAP   A O2B  1 
HETATM 1583 C  C1B  . NAP   B 2 .   ? 16.39100 4.63800   5.83800  1.000 12.99000 ?  301 NAP   A C1B  1 
HETATM 1584 N  N9A  . NAP   B 2 .   ? 15.38200 4.47800   4.79500  1.000 11.05000 ?  301 NAP   A N9A  1 
HETATM 1585 C  C8A  . NAP   B 2 .   ? 14.57700 5.44700   4.27100  1.000 12.40000 ?  301 NAP   A C8A  1 
HETATM 1586 N  N7A  . NAP   B 2 .   ? 13.81500 4.93100   3.34900  1.000 11.59000 ?  301 NAP   A N7A  1 
HETATM 1587 C  C5A  . NAP   B 2 .   ? 14.08900 3.60800   3.22800  1.000 11.80000 ?  301 NAP   A C5A  1 
HETATM 1588 C  C6A  . NAP   B 2 .   ? 13.60200 2.56400   2.42600  1.000 14.20000 ?  301 NAP   A C6A  1 
HETATM 1589 N  N6A  . NAP   B 2 .   ? 12.60900 2.79500   1.49200  1.000 13.77000 ?  301 NAP   A N6A  1 
HETATM 1590 N  N1A  . NAP   B 2 .   ? 14.12000 1.35100   2.58600  1.000 15.63000 ?  301 NAP   A N1A  1 
HETATM 1591 C  C2A  . NAP   B 2 .   ? 15.07200 1.11700   3.47300  1.000 14.41000 ?  301 NAP   A C2A  1 
HETATM 1592 N  N3A  . NAP   B 2 .   ? 15.56100 2.06100   4.24700  1.000 12.24000 ?  301 NAP   A N3A  1 
HETATM 1593 C  C4A  . NAP   B 2 .   ? 15.10100 3.30400   4.15500  1.000 12.81000 ?  301 NAP   A C4A  1 
HETATM 1594 O  O3   . NAP   B 2 .   ? 16.91200 8.94000   10.55800 1.000 14.29000 ?  301 NAP   A O3   1 
HETATM 1595 P  PN   . NAP   B 2 .   ? 17.17300 9.82400   11.88500 1.000 15.64000 ?  301 NAP   A PN   1 
HETATM 1596 O  O1N  . NAP   B 2 .   ? 18.10200 9.03400   12.82800 1.000 15.56000 ?  301 NAP   A O1N  1 
HETATM 1597 O  O2N  . NAP   B 2 .   ? 17.73500 11.23200  11.59800 1.000 17.06000 ?  301 NAP   A O2N  1 
HETATM 1598 O  O5D  . NAP   B 2 .   ? 15.74100 10.02300  12.59000 1.000 13.70000 ?  301 NAP   A O5D  1 
HETATM 1599 C  C5D  . NAP   B 2 .   ? 15.15400 8.75000   12.85700 1.000 10.42000 ?  301 NAP   A C5D  1 
HETATM 1600 C  C4D  . NAP   B 2 .   ? 13.66700 8.99400   13.12500 1.000 14.23000 ?  301 NAP   A C4D  1 
HETATM 1601 O  O4D  . NAP   B 2 .   ? 13.52600 9.97700   14.18000 1.000 13.58000 ?  301 NAP   A O4D  1 
HETATM 1602 C  C3D  . NAP   B 2 .   ? 13.00400 9.59700   11.86600 1.000 11.95000 ?  301 NAP   A C3D  1 
HETATM 1603 O  O3D  . NAP   B 2 .   ? 11.75000 8.95500   11.62500 1.000 13.30000 ?  301 NAP   A O3D  1 
HETATM 1604 C  C2D  . NAP   B 2 .   ? 12.79800 11.08400  12.23000 1.000 13.40000 ?  301 NAP   A C2D  1 
HETATM 1605 O  O2D  . NAP   B 2 .   ? 11.64200 11.59300  11.56600 1.000 13.47000 ?  301 NAP   A O2D  1 
HETATM 1606 C  C1D  . NAP   B 2 .   ? 12.56700 10.96700  13.74800 1.000 13.14000 ?  301 NAP   A C1D  1 
HETATM 1607 N  N1N  . NAP   B 2 .   ? 12.82900 12.19700  14.50800 1.000 12.95000 ?  301 NAP   A N1N  1 
HETATM 1608 C  C2N  . NAP   B 2 .   ? 13.78400 13.03900  14.15400 1.000 11.15000 ?  301 NAP   A C2N  1 
HETATM 1609 C  C3N  . NAP   B 2 .   ? 14.02500 14.19100  14.91300 1.000 14.05000 ?  301 NAP   A C3N  1 
HETATM 1610 C  C7N  . NAP   B 2 .   ? 15.08300 15.15900  14.55500 1.000 18.03000 ?  301 NAP   A C7N  1 
HETATM 1611 O  O7N  . NAP   B 2 .   ? 15.37500 16.03900  15.34300 1.000 15.43000 ?  301 NAP   A O7N  1 
HETATM 1612 N  N7N  . NAP   B 2 .   ? 15.73100 15.06700  13.37900 1.000 15.16000 ?  301 NAP   A N7N  1 
HETATM 1613 C  C4N  . NAP   B 2 .   ? 13.24200 14.42900  16.05000 1.000 13.84000 ?  301 NAP   A C4N  1 
HETATM 1614 C  C5N  . NAP   B 2 .   ? 12.25900 13.51200  16.37900 1.000 13.76000 ?  301 NAP   A C5N  1 
HETATM 1615 C  C6N  . NAP   B 2 .   ? 12.08800 12.39800  15.58000 1.000 15.21000 ?  301 NAP   A C6N  1 
HETATM 1616 P  P2B  . NAP   B 2 .   ? 19.29000 5.41900   3.39300  1.000 15.94000 ?  301 NAP   A P2B  1 
HETATM 1617 O  O1X  . NAP   B 2 .   ? 20.69500 5.50100   3.85900  1.000 17.32000 ?  301 NAP   A O1X  1 
HETATM 1618 O  O2X  . NAP   B 2 .   ? 18.75000 6.89200   3.07400  1.000 14.72000 ?  301 NAP   A O2X  1 
HETATM 1619 O  O3X  . NAP   B 2 .   ? 19.22400 4.53200   2.05700  1.000 18.12000 ?  301 NAP   A O3X  1 
HETATM 1620 C  C10  . A1ATJ C 3 .   ? 12.40100 17.04400  12.43900 0.840 21.13000 ?  302 A1ATJ A C10  1 
HETATM 1621 C  C13  . A1ATJ C 3 .   ? 14.62300 19.25100  10.34700 0.840 21.61000 ?  302 A1ATJ A C13  1 
HETATM 1622 C  C15  . A1ATJ C 3 .   ? 14.65000 17.03100  9.37200  0.840 22.53000 ?  302 A1ATJ A C15  1 
HETATM 1623 C  C20  . A1ATJ C 3 .   ? 9.19900  14.82100  12.74800 0.840 18.95000 ?  302 A1ATJ A C20  1 
HETATM 1624 C  C21  . A1ATJ C 3 .   ? 9.58600  15.43800  13.93300 0.840 18.56000 ?  302 A1ATJ A C21  1 
HETATM 1625 C  C24  . A1ATJ C 3 .   ? 11.49500 18.77000  17.87800 0.840 20.47000 ?  302 A1ATJ A C24  1 
HETATM 1626 C  C02  . A1ATJ C 3 .   ? 10.48800 18.29600  20.16400 0.840 24.27000 ?  302 A1ATJ A C02  1 
HETATM 1627 C  C04  . A1ATJ C 3 .   ? 10.75400 17.91500  18.69400 0.840 18.94000 ?  302 A1ATJ A C04  1 
HETATM 1628 C  C05  . A1ATJ C 3 .   ? 10.26900 16.73400  18.13000 0.840 18.08000 ?  302 A1ATJ A C05  1 
HETATM 1629 C  C06  . A1ATJ C 3 .   ? 10.51700 16.41900  16.78100 0.840 17.51000 ?  302 A1ATJ A C06  1 
HETATM 1630 C  C07  . A1ATJ C 3 .   ? 11.28600 17.28100  15.98100 0.840 18.54000 ?  302 A1ATJ A C07  1 
HETATM 1631 C  C08  . A1ATJ C 3 .   ? 11.54900 17.02700  14.57900 0.840 16.22000 ?  302 A1ATJ A C08  1 
HETATM 1632 C  C11  . A1ATJ C 3 .   ? 13.31700 17.44900  11.39500 0.840 23.11000 ?  302 A1ATJ A C11  1 
HETATM 1633 C  C12  . A1ATJ C 3 .   ? 13.75900 18.79500  11.34100 0.840 25.32000 ?  302 A1ATJ A C12  1 
HETATM 1634 C  C14  . A1ATJ C 3 .   ? 15.06800 18.36400  9.36600  0.840 25.55000 ?  302 A1ATJ A C14  1 
HETATM 1635 C  C16  . A1ATJ C 3 .   ? 13.78600 16.60700  10.37400 0.840 20.02000 ?  302 A1ATJ A C16  1 
HETATM 1636 C  C18  . A1ATJ C 3 .   ? 11.27500 16.23000  12.42500 0.840 21.06000 ?  302 A1ATJ A C18  1 
HETATM 1637 C  C23  . A1ATJ C 3 .   ? 11.75700 18.47500  16.54000 0.840 21.52000 ?  302 A1ATJ A C23  1 
HETATM 1638 N  N09  . A1ATJ C 3 .   ? 12.52700 17.53100  13.76800 0.840 19.26000 ?  302 A1ATJ A N09  1 
HETATM 1639 N  N22  . A1ATJ C 3 .   ? 10.76000 16.20500  13.70800 0.840 18.94000 ?  302 A1ATJ A N22  1 
HETATM 1640 O  O01  . A1ATJ C 3 .   ? 9.67000  17.61900  20.82800 0.840 23.14000 ?  302 A1ATJ A O01  1 
HETATM 1641 O  O03  . A1ATJ C 3 .   ? 11.10200 19.29400  20.56700 0.840 22.50000 -1 302 A1ATJ A O03  1 
HETATM 1642 S  S19  . A1ATJ C 3 .   ? 10.25900 15.23400  11.43300 0.840 21.09000 ?  302 A1ATJ A S19  1 
HETATM 1643 CL CL17 . A1ATJ C 3 .   ? 13.27200 14.94100  10.36100 0.840 24.44000 ?  302 A1ATJ A CL17 1 
HETATM 1644 O  O    . HOH   D 4 .   ? 9.02600  17.82800  23.01400 1.000 23.79000 ?  401 HOH   A O    1 
HETATM 1645 O  O    . HOH   D 4 .   ? 21.11000 16.10200  12.63700 1.000 35.85000 ?  402 HOH   A O    1 
HETATM 1646 O  O    . HOH   D 4 .   ? 14.75000 19.05200  14.82500 1.000 29.86000 ?  403 HOH   A O    1 
HETATM 1647 O  O    . HOH   D 4 .   ? 13.40900 3.60600   -1.91200 1.000 21.54000 ?  404 HOH   A O    1 
HETATM 1648 O  O    . HOH   D 4 .   ? 18.535   -12.694   -0.957   1.000 21.27000 ?  405 HOH   A O    1 
HETATM 1649 O  O    . HOH   D 4 .   ? 21.52100 -3.69300  24.85900 1.000 26.19000 ?  406 HOH   A O    1 
HETATM 1650 O  O    . HOH   D 4 .   ? 24.11300 14.21100  13.42300 1.000 26.78000 ?  407 HOH   A O    1 
HETATM 1651 O  O    . HOH   D 4 .   ? -3.09800 -1.57300  11.51800 1.000 36.85000 ?  408 HOH   A O    1 
HETATM 1652 O  O    . HOH   D 4 .   ? 13.61400 12.32700  -0.92600 1.000 23.56000 ?  409 HOH   A O    1 
HETATM 1653 O  O    . HOH   D 4 .   ? 27.74186 9.95300   31.44010 0.50  28.03000 ?  410 HOH   A O    1 
HETATM 1654 O  O    . HOH   D 4 .   ? 19.45100 -15.83300 20.09700 1.000 36.99000 ?  411 HOH   A O    1 
HETATM 1655 O  O    . HOH   D 4 .   ? 15.06400 -4.85200  -3.70400 1.000 27.29000 ?  412 HOH   A O    1 
HETATM 1656 O  O    . HOH   D 4 .   ? 19.38200 12.65100  8.66400  1.000 23.68000 ?  413 HOH   A O    1 
HETATM 1657 O  O    . HOH   D 4 .   ? 12.74800 -14.93900 3.90400  1.000 33.99000 ?  414 HOH   A O    1 
HETATM 1658 O  O    . HOH   D 4 .   ? 16.42100 0.02000   6.33800  1.000 18.20000 ?  415 HOH   A O    1 
HETATM 1659 O  O    . HOH   D 4 .   ? 0.41800  3.85500   5.27000  1.000 30.01000 ?  416 HOH   A O    1 
HETATM 1660 O  O    . HOH   D 4 .   ? 19.30800 -0.90300  8.18900  1.000 20.74000 ?  417 HOH   A O    1 
HETATM 1661 O  O    . HOH   D 4 .   ? 13.43900 4.06400   32.86700 1.000 27.26000 ?  418 HOH   A O    1 
HETATM 1662 O  O    . HOH   D 4 .   ? 17.59000 -12.60000 8.53800  1.000 26.44000 ?  419 HOH   A O    1 
HETATM 1663 O  O    . HOH   D 4 .   ? 10.58100 11.91200  33.55300 1.000 15.10000 ?  420 HOH   A O    1 
HETATM 1664 O  O    . HOH   D 4 .   ? -0.94800 18.44600  14.37900 1.000 22.20000 ?  421 HOH   A O    1 
HETATM 1665 O  O    . HOH   D 4 .   ? 30.63400 1.47600   12.89800 1.000 28.56000 ?  422 HOH   A O    1 
HETATM 1666 O  O    . HOH   D 4 .   ? 5.58100  -12.63100 16.56700 1.000 23.07000 ?  423 HOH   A O    1 
HETATM 1667 O  O    . HOH   D 4 .   ? 31.16500 -2.48800  5.34900  1.000 36.36000 ?  424 HOH   A O    1 
HETATM 1668 O  O    . HOH   D 4 .   ? 14.92100 12.41900  9.02100  1.000 17.56000 ?  425 HOH   A O    1 
HETATM 1669 O  O    . HOH   D 4 .   ? 11.21700 -12.37100 19.54200 1.000 29.65000 ?  426 HOH   A O    1 
HETATM 1670 O  O    . HOH   D 4 .   ? 7.27900  5.13700   18.25600 1.000 15.29000 ?  427 HOH   A O    1 
HETATM 1671 O  O    . HOH   D 4 .   ? 28.74300 -8.09300  17.89300 1.000 24.55000 ?  428 HOH   A O    1 
HETATM 1672 O  O    . HOH   D 4 .   ? 5.82000  -7.17800  27.67700 1.000 19.55000 ?  429 HOH   A O    1 
HETATM 1673 O  O    . HOH   D 4 .   ? 25.38600 14.07900  31.42300 1.000 23.13000 ?  430 HOH   A O    1 
HETATM 1674 O  O    . HOH   D 4 .   ? 23.70300 19.53300  19.07600 1.000 41.52000 ?  431 HOH   A O    1 
HETATM 1675 O  O    . HOH   D 4 .   ? 21.08000 -10.97000 13.12400 1.000 16.16000 ?  432 HOH   A O    1 
HETATM 1676 O  O    . HOH   D 4 .   ? 32.61900 2.26500   12.09900 1.000 30.59000 ?  433 HOH   A O    1 
HETATM 1677 O  O    . HOH   D 4 .   ? 19.72000 6.96900   31.77900 1.000 28.55000 ?  434 HOH   A O    1 
HETATM 1678 O  O    . HOH   D 4 .   ? 18.66300 15.91400  13.94700 1.000 19.64000 ?  435 HOH   A O    1 
HETATM 1679 O  O    . HOH   D 4 .   ? 5.28700  -2.26100  0.41800  1.000 32.22000 ?  436 HOH   A O    1 
HETATM 1680 O  O    . HOH   D 4 .   ? 10.98700 -7.80200  -4.23200 1.000 41.03000 ?  437 HOH   A O    1 
HETATM 1681 O  O    . HOH   D 4 .   ? 20.56700 -7.44600  -2.49000 1.000 28.30000 ?  438 HOH   A O    1 
HETATM 1682 O  O    . HOH   D 4 .   ? 0.74200  21.43300  12.19600 1.000 18.52000 ?  439 HOH   A O    1 
HETATM 1683 O  O    . HOH   D 4 .   ? 6.84100  13.70900  14.11400 1.000 19.66000 ?  440 HOH   A O    1 
HETATM 1684 O  O    . HOH   D 4 .   ? 39.63200 -1.63400  5.38300  1.000 28.07000 ?  441 HOH   A O    1 
HETATM 1685 O  O    . HOH   D 4 .   ? 18.18500 14.30700  32.08500 1.000 25.36000 ?  442 HOH   A O    1 
HETATM 1686 O  O    . HOH   D 4 .   ? 2.57800  12.58100  4.92500  1.000 16.68000 ?  443 HOH   A O    1 
HETATM 1687 O  O    . HOH   D 4 .   ? 25.31300 6.35900   5.93800  1.000 21.33000 ?  444 HOH   A O    1 
HETATM 1688 O  O    . HOH   D 4 .   ? 10.81100 -2.70000  27.19100 1.000 14.40000 ?  445 HOH   A O    1 
HETATM 1689 O  O    . HOH   D 4 .   ? 29.52300 -7.93900  13.64800 1.000 19.14000 ?  446 HOH   A O    1 
HETATM 1690 O  O    . HOH   D 4 .   ? 26.70100 1.94200   24.15600 1.000 23.88000 ?  447 HOH   A O    1 
HETATM 1691 O  O    . HOH   D 4 .   ? 9.41800  12.97100  3.39800  1.000 18.08000 ?  448 HOH   A O    1 
HETATM 1692 O  O    . HOH   D 4 .   ? 17.73500 -9.46700  26.21200 1.000 35.90000 ?  449 HOH   A O    1 
HETATM 1693 O  O    . HOH   D 4 .   ? 3.74200  -15.14700 15.07800 1.000 30.73000 ?  450 HOH   A O    1 
HETATM 1694 O  O    . HOH   D 4 .   ? 7.59600  0.54200   33.34000 1.000 33.81000 ?  451 HOH   A O    1 
HETATM 1695 O  O    . HOH   D 4 .   ? 15.75800 13.11100  11.47400 1.000 15.56000 ?  452 HOH   A O    1 
HETATM 1696 O  O    . HOH   D 4 .   ? -2.90500 -7.31900  14.24700 1.000 34.90000 ?  453 HOH   A O    1 
HETATM 1697 O  O    . HOH   D 4 .   ? 5.16400  13.70100  31.20100 1.000 19.15000 ?  454 HOH   A O    1 
HETATM 1698 O  O    . HOH   D 4 .   ? 25.51300 9.43600   12.90300 1.000 18.55000 ?  455 HOH   A O    1 
HETATM 1699 O  O    . HOH   D 4 .   ? 18.44900 21.16000  26.95300 1.000 34.91000 ?  456 HOH   A O    1 
HETATM 1700 O  O    . HOH   D 4 .   ? 25.104   -1.945    -2.637   1.000 25.00000 ?  457 HOH   A O    1 
HETATM 1701 O  O    . HOH   D 4 .   ? 12.45400 11.71000  8.94600  1.000 15.60000 ?  458 HOH   A O    1 
HETATM 1702 O  O    . HOH   D 4 .   ? 29.95000 11.68000  27.92100 1.000 29.55000 ?  459 HOH   A O    1 
HETATM 1703 O  O    . HOH   D 4 .   ? 10.42500 19.65700  27.46500 1.000 31.53000 ?  460 HOH   A O    1 
HETATM 1704 O  O    . HOH   D 4 .   ? 28.18900 2.66200   12.18800 1.000 24.99000 ?  461 HOH   A O    1 
HETATM 1705 O  O    . HOH   D 4 .   ? 10.94300 -11.04300 23.40700 1.000 37.48000 ?  462 HOH   A O    1 
HETATM 1706 O  O    . HOH   D 4 .   ? 4.13600  19.58700  6.37700  1.000 16.22000 ?  463 HOH   A O    1 
HETATM 1707 O  O    . HOH   D 4 .   ? 18.65000 1.98000   3.84000  1.000 21.03000 ?  464 HOH   A O    1 
HETATM 1708 O  O    . HOH   D 4 .   ? 6.76400  17.49000  7.02800  1.000 15.72000 ?  465 HOH   A O    1 
HETATM 1709 O  O    . HOH   D 4 .   ? 33.38400 3.95800   6.47700  1.000 44.28000 ?  466 HOH   A O    1 
HETATM 1710 O  O    . HOH   D 4 .   ? 26.82400 -8.04300  14.53800 1.000 17.45000 ?  467 HOH   A O    1 
HETATM 1711 O  O    . HOH   D 4 .   ? -0.84300 -3.60100  12.25300 1.000 25.87000 ?  468 HOH   A O    1 
HETATM 1712 O  O    . HOH   D 4 .   ? 29.68900 2.73000   23.31000 1.000 33.80000 ?  469 HOH   A O    1 
HETATM 1713 O  O    . HOH   D 4 .   ? 1.61600  -3.77100  19.75600 1.000 23.27000 ?  470 HOH   A O    1 
HETATM 1714 O  O    . HOH   D 4 .   ? -0.36500 -0.06100  25.14700 1.000 34.01000 ?  471 HOH   A O    1 
HETATM 1715 O  O    . HOH   D 4 .   ? 28.78300 12.16900  14.72500 1.000 34.41000 ?  472 HOH   A O    1 
HETATM 1716 O  O    . HOH   D 4 .   ? 12.88900 12.49400  29.43000 1.000 12.66000 ?  473 HOH   A O    1 
HETATM 1717 O  O    . HOH   D 4 .   ? 3.94900  -7.32900  3.81100  1.000 30.96000 ?  474 HOH   A O    1 
HETATM 1718 O  O    . HOH   D 4 .   ? -0.51600 5.78200   21.61100 1.000 29.93000 ?  475 HOH   A O    1 
HETATM 1719 O  O    . HOH   D 4 .   ? 11.80600 4.80900   12.64900 1.000 15.42000 ?  476 HOH   A O    1 
HETATM 1720 O  O    . HOH   D 4 .   ? 21.22600 20.36700  26.21200 1.000 28.16000 ?  477 HOH   A O    1 
HETATM 1721 O  O    . HOH   D 4 .   ? 23.26500 4.13600   31.49000 1.000 34.24000 ?  478 HOH   A O    1 
HETATM 1722 O  O    . HOH   D 4 .   ? -1.04400 13.00500  5.58800  1.000 18.24000 ?  479 HOH   A O    1 
HETATM 1723 O  O    . HOH   D 4 .   ? 5.30100  4.15700   0.39900  1.000 29.01000 ?  480 HOH   A O    1 
HETATM 1724 O  O    . HOH   D 4 .   ? 12.52500 -13.07800 0.89300  1.000 23.10000 ?  481 HOH   A O    1 
HETATM 1725 O  O    . HOH   D 4 .   ? 18.67000 6.41600   11.50800 1.000 13.00000 ?  482 HOH   A O    1 
HETATM 1726 O  O    . HOH   D 4 .   ? 11.517   23.732    5.201    1.000 27.84000 ?  483 HOH   A O    1 
HETATM 1727 O  O    . HOH   D 4 .   ? 15.83900 0.65000   -3.25200 1.000 28.86000 ?  484 HOH   A O    1 
HETATM 1728 O  O    . HOH   D 4 .   ? 13.88900 -8.57700  -3.68000 1.000 38.70000 ?  485 HOH   A O    1 
HETATM 1729 O  O    . HOH   D 4 .   ? 23.75900 9.04100   7.78100  1.000 22.33000 ?  486 HOH   A O    1 
HETATM 1730 O  O    . HOH   D 4 .   ? 15.37600 -7.13600  32.31000 1.000 31.81000 ?  487 HOH   A O    1 
HETATM 1731 O  O    . HOH   D 4 .   ? 2.60600  3.54200   22.99300 1.000 28.67000 ?  488 HOH   A O    1 
HETATM 1732 O  O    . HOH   D 4 .   ? 8.70900  -8.34700  -2.42800 1.000 36.92000 ?  489 HOH   A O    1 
HETATM 1733 O  O    . HOH   D 4 .   ? 7.00500  -8.41100  4.81300  1.000 24.58000 ?  490 HOH   A O    1 
HETATM 1734 O  O    . HOH   D 4 .   ? 28.65900 13.11800  17.74900 1.000 31.70000 ?  491 HOH   A O    1 
HETATM 1735 O  O    . HOH   D 4 .   ? 2.32300  -12.19900 8.13200  1.000 29.63000 ?  492 HOH   A O    1 
HETATM 1736 O  O    . HOH   D 4 .   ? 19.49000 1.78100   6.33300  1.000 24.17000 ?  493 HOH   A O    1 
HETATM 1737 O  O    . HOH   D 4 .   ? 34.89000 3.31700   8.08700  1.000 38.15000 ?  494 HOH   A O    1 
HETATM 1738 O  O    . HOH   D 4 .   ? 10.04900 13.97100  -2.28400 1.000 35.24000 ?  495 HOH   A O    1 
HETATM 1739 O  O    . HOH   D 4 .   ? 17.46900 -8.52300  -1.37200 1.000 27.29000 ?  496 HOH   A O    1 
HETATM 1740 O  O    . HOH   D 4 .   ? 13.36400 -15.96900 15.15500 1.000 27.16000 ?  497 HOH   A O    1 
HETATM 1741 O  O    . HOH   D 4 .   ? 0.50600  14.82800  16.96300 1.000 21.86000 ?  498 HOH   A O    1 
HETATM 1742 O  O    . HOH   D 4 .   ? 29.71500 14.55400  20.03100 1.000 37.25000 ?  499 HOH   A O    1 
HETATM 1743 O  O    . HOH   D 4 .   ? 5.87700  19.43000  4.05500  1.000 28.28000 ?  500 HOH   A O    1 
HETATM 1744 O  O    . HOH   D 4 .   ? 1.13000  -5.81700  8.42200  1.000 22.44000 ?  501 HOH   A O    1 
HETATM 1745 O  O    . HOH   D 4 .   ? 15.89600 21.37600  26.48800 1.000 28.13000 ?  502 HOH   A O    1 
HETATM 1746 O  O    . HOH   D 4 .   ? 21.36500 19.87200  16.55500 1.000 42.74000 ?  503 HOH   A O    1 
HETATM 1747 O  O    . HOH   D 4 .   ? -3.05300 9.94800   8.14300  1.000 30.62000 ?  504 HOH   A O    1 
HETATM 1748 O  O    . HOH   D 4 .   ? -1.84600 3.50400   9.89200  1.000 25.87000 ?  505 HOH   A O    1 
HETATM 1749 O  O    . HOH   D 4 .   ? 14.384   -11.137   -2.931   1.000 30.01000 ?  506 HOH   A O    1 
HETATM 1750 O  O    . HOH   D 4 .   ? 6.29000  -11.21900 5.18900  1.000 28.34000 ?  507 HOH   A O    1 
HETATM 1751 O  O    . HOH   D 4 .   ? 3.93700  1.07000   22.81300 1.000 19.47000 ?  508 HOH   A O    1 
HETATM 1752 O  O    . HOH   D 4 .   ? 17.38100 -14.67800 5.83100  1.000 38.78000 ?  509 HOH   A O    1 
HETATM 1753 O  O    . HOH   D 4 .   ? 30.15700 10.35900  22.14200 1.000 27.18000 ?  510 HOH   A O    1 
HETATM 1754 O  O    . HOH   D 4 .   ? 19.84400 -8.28000  25.19300 1.000 36.31000 ?  511 HOH   A O    1 
HETATM 1755 O  O    . HOH   D 4 .   ? 2.64300  5.75100   32.83700 1.000 34.56000 ?  512 HOH   A O    1 
HETATM 1756 O  O    . HOH   D 4 .   ? 29.63400 -6.44800  7.24300  1.000 36.85000 ?  513 HOH   A O    1 
HETATM 1757 O  O    . HOH   D 4 .   ? 4.72900  11.22300  32.23100 1.000 30.57000 ?  514 HOH   A O    1 
HETATM 1758 O  O    . HOH   D 4 .   ? 3.28100  -3.59900  23.16500 1.000 25.28000 ?  515 HOH   A O    1 
HETATM 1759 O  O    . HOH   D 4 .   ? 5.62900  13.79700  -1.64700 1.000 36.99000 ?  516 HOH   A O    1 
HETATM 1760 O  O    . HOH   D 4 .   ? 6.88800  9.18100   26.53400 1.000 21.28000 ?  517 HOH   A O    1 
HETATM 1761 O  O    . HOH   D 4 .   ? -1.53500 -6.41700  12.63200 1.000 40.47000 ?  518 HOH   A O    1 
HETATM 1762 O  O    . HOH   D 4 .   ? 1.26200  6.59100   25.89200 1.000 29.40000 ?  519 HOH   A O    1 
HETATM 1763 O  O    . HOH   D 4 .   ? 12.67400 7.03400   1.62500  1.000 25.54000 ?  520 HOH   A O    1 
HETATM 1764 O  O    . HOH   D 4 .   ? 13.45500 -7.72400  24.42000 1.000 32.98000 ?  521 HOH   A O    1 
HETATM 1765 O  O    . HOH   D 4 .   ? 11.60000 9.56900   34.63400 1.000 26.28000 ?  522 HOH   A O    1 
HETATM 1766 O  O    . HOH   D 4 .   ? 17.14100 17.59800  12.76900 1.000 35.32000 ?  523 HOH   A O    1 
HETATM 1767 O  O    . HOH   D 4 .   ? 21.87600 -10.99600 2.39400  1.000 32.56000 ?  524 HOH   A O    1 
HETATM 1768 O  O    . HOH   D 4 .   ? 6.16800  -5.60600  -1.49700 1.000 33.01000 ?  525 HOH   A O    1 
HETATM 1769 O  O    . HOH   D 4 .   ? 0.691    12.392    29.638   1.000 37.09000 ?  526 HOH   A O    1 
HETATM 1770 O  O    . HOH   D 4 .   ? 8.03900  9.01000   33.60600 1.000 23.47000 ?  527 HOH   A O    1 
HETATM 1771 O  O    . HOH   D 4 .   ? 21.39400 2.53800   2.54900  1.000 24.31000 ?  528 HOH   A O    1 
HETATM 1772 O  O    . HOH   D 4 .   ? 14.82100 8.20300   33.87300 1.000 25.23000 ?  529 HOH   A O    1 
HETATM 1773 O  O    . HOH   D 4 .   ? 25.48700 -12.81000 5.79400  1.000 34.05000 ?  530 HOH   A O    1 
HETATM 1774 O  O    . HOH   D 4 .   ? 20.35000 -12.65500 8.95400  1.000 30.19000 ?  531 HOH   A O    1 
HETATM 1775 O  O    . HOH   D 4 .   ? 27.64000 -0.46700  23.40500 1.000 30.42000 ?  532 HOH   A O    1 
HETATM 1776 O  O    . HOH   D 4 .   ? 5.72900  7.96500   -0.06300 1.000 23.53000 ?  533 HOH   A O    1 
HETATM 1777 O  O    . HOH   D 4 .   ? 1.99500  -1.79100  28.93000 1.000 29.25000 ?  534 HOH   A O    1 
HETATM 1778 O  O    . HOH   D 4 .   ? 3.49400  -10.10600 21.39300 1.000 38.00000 ?  535 HOH   A O    1 
HETATM 1779 O  O    . HOH   D 4 .   ? -1.02000 6.78700   16.04300 1.000 30.37000 ?  536 HOH   A O    1 
HETATM 1780 O  O    . HOH   D 4 .   ? 3.01000  15.23700  28.78300 1.000 28.53000 ?  537 HOH   A O    1 
HETATM 1781 O  O    . HOH   D 4 .   ? 1.44500  13.89100  26.38500 1.000 27.41000 ?  538 HOH   A O    1 
HETATM 1782 O  O    . HOH   D 4 .   ? 20.88300 12.80100  6.33700  1.000 32.59000 ?  539 HOH   A O    1 
HETATM 1783 O  O    . HOH   D 4 .   ? 22.20100 0.12400   25.88200 1.000 30.37000 ?  540 HOH   A O    1 
HETATM 1784 O  O    . HOH   D 4 .   ? 11.84000 5.62200   33.52600 1.000 38.92000 ?  541 HOH   A O    1 
HETATM 1785 O  O    . HOH   D 4 .   ? 21.65200 -8.51400  -0.40700 1.000 25.05000 ?  542 HOH   A O    1 
HETATM 1786 O  O    . HOH   D 4 .   ? 16.03900 15.54100  30.72600 1.000 21.21000 ?  543 HOH   A O    1 
HETATM 1787 O  O    . HOH   D 4 .   ? 2.35200  -5.80500  4.10100  1.000 36.34000 ?  544 HOH   A O    1 
HETATM 1788 O  O    . HOH   D 4 .   ? 10.05000 1.66600   34.12600 1.000 34.49000 ?  545 HOH   A O    1 
HETATM 1789 O  O    . HOH   D 4 .   ? 16.04700 17.79900  31.93300 1.000 31.38000 ?  546 HOH   A O    1 
HETATM 1790 O  O    . HOH   D 4 .   ? 8.32400  11.38900  -0.39400 1.000 35.38000 ?  547 HOH   A O    1 
HETATM 1791 O  O    . HOH   D 4 .   ? -0.04800 15.89800  14.68500 1.000 21.80000 ?  548 HOH   A O    1 
HETATM 1792 O  O    . HOH   D 4 .   ? 4.59500  23.34300  5.07000  1.000 33.80000 ?  549 HOH   A O    1 
HETATM 1793 O  O    . HOH   D 4 .   ? 32.86000 -5.57100  13.32800 1.000 30.59000 ?  550 HOH   A O    1 
HETATM 1794 O  O    . HOH   D 4 .   ? 18.15800 -1.48200  -3.02800 1.000 29.35000 ?  551 HOH   A O    1 
HETATM 1795 O  O    . HOH   D 4 .   ? 21.64000 -14.69400 9.89900  1.000 40.18000 ?  552 HOH   A O    1 
HETATM 1796 O  O    . HOH   D 4 .   ? 2.32800  20.36000  23.42300 1.000 25.97000 ?  553 HOH   A O    1 
HETATM 1797 O  O    . HOH   D 4 .   ? 11.845   -18.788   10.199   1.000 37.33000 ?  554 HOH   A O    1 
HETATM 1798 O  O    . HOH   D 4 .   ? 25.97700 -10.64400 4.75000  1.000 28.83000 ?  555 HOH   A O    1 
HETATM 1799 O  O    . HOH   D 4 .   ? 11.49300 5.15400   -0.29200 1.000 21.14000 ?  556 HOH   A O    1 
HETATM 1800 O  O    . HOH   D 4 .   ? 14.846   22.121    28.685   1.000 32.95000 ?  557 HOH   A O    1 
HETATM 1801 O  O    . HOH   D 4 .   ? 37.63000 3.19300   3.28200  1.000 49.85000 ?  558 HOH   A O    1 
HETATM 1802 O  O    . HOH   D 4 .   ? -2.08500 10.64900  10.00600 1.000 29.23000 ?  559 HOH   A O    1 
HETATM 1803 O  O    . HOH   D 4 .   ? 21.03300 20.00000  19.30800 1.000 39.26000 ?  560 HOH   A O    1 
HETATM 1804 O  O    . HOH   D 4 .   ? 33.41400 -4.55900  5.42400  1.000 34.13000 ?  561 HOH   A O    1 
HETATM 1805 O  O    . HOH   D 4 .   ? 14.83700 9.36200   1.63800  1.000 34.25000 ?  562 HOH   A O    1 
HETATM 1806 O  O    . HOH   D 4 .   ? 35.43900 -5.14500  13.58100 1.000 29.71000 ?  563 HOH   A O    1 
HETATM 1807 O  O    . HOH   D 4 .   ? 18.22800 16.08700  10.03000 1.000 34.28000 ?  564 HOH   A O    1 
HETATM 1808 O  O    . HOH   D 4 .   ? 30.09000 4.24100   19.49900 1.000 34.27000 ?  565 HOH   A O    1 
HETATM 1809 O  O    . HOH   D 4 .   ? -3.35700 1.14800   10.38200 1.000 34.84000 ?  566 HOH   A O    1 
HETATM 1810 O  O    . HOH   D 4 .   ? 9.99900  11.03900  1.59400  1.000 32.44000 ?  567 HOH   A O    1 
HETATM 1811 O  O    . HOH   D 4 .   ? 25.98400 16.05600  30.17800 1.000 40.00000 ?  568 HOH   A O    1 
HETATM 1812 O  O    . HOH   D 4 .   ? 12.382   22.444    28.146   1.000 39.33000 ?  569 HOH   A O    1 
HETATM 1813 O  O    . HOH   D 4 .   ? 4.11000  25.23000  6.09000  1.000 30.43000 ?  570 HOH   A O    1 
HETATM 1814 O  O    . HOH   D 4 .   ? 16.99700 9.97200   0.43400  1.000 31.02000 ?  571 HOH   A O    1 
HETATM 1815 O  O    . HOH   D 4 .   ? 36.925   2.893     12.751   1.000 31.69000 ?  572 HOH   A O    1 
HETATM 1816 O  O    . HOH   D 4 .   ? 12.686   -18.919   7.890    1.000 36.08000 ?  573 HOH   A O    1 
HETATM 1817 O  O    . HOH   D 4 .   ? -3.25600 24.34300  14.19700 1.000 32.81000 ?  574 HOH   A O    1 
HETATM 1818 O  O    . HOH   D 4 .   ? 1.53100  0.49500   22.19300 1.000 34.13000 ?  575 HOH   A O    1 
HETATM 1819 O  O    . HOH   D 4 .   ? -1.10800 13.49500  17.85900 1.000 36.74000 ?  576 HOH   A O    1 
HETATM 1820 O  O    . HOH   D 4 .   ? 14.56100 4.41000   -3.86400 1.000 33.02000 ?  577 HOH   A O    1 
HETATM 1821 O  O    . HOH   D 4 .   ? 27.20400 4.87500   28.21300 1.000 33.00000 ?  578 HOH   A O    1 
HETATM 1822 O  O    . HOH   D 4 .   ? 27.701   6.545     -0.827   1.000 32.55000 ?  579 HOH   A O    1 
HETATM 1823 O  O    . HOH   D 4 .   ? 29.40800 6.55800   29.00200 1.000 35.08000 ?  580 HOH   A O    1 
HETATM 1824 O  O    . HOH   D 4 .   ? 15.54900 6.08500   33.70200 1.000 40.79000 ?  581 HOH   A O    1 
HETATM 1825 O  O    . HOH   D 4 .   ? 29.27700 -3.59800  6.55600  1.000 37.17000 ?  582 HOH   A O    1 
HETATM 1826 O  O    . HOH   D 4 .   ? 0.80900  14.38200  4.02300  1.000 24.63000 ?  583 HOH   A O    1 
HETATM 1827 O  O    . HOH   D 4 .   ? 18.56600 16.32700  33.00400 1.000 38.31000 ?  584 HOH   A O    1 
HETATM 1828 O  O    . HOH   D 4 .   ? 0.37400  -8.13900  9.44400  1.000 31.38000 ?  585 HOH   A O    1 
HETATM 1829 O  O    . HOH   D 4 .   ? 1.88500  -4.46800  25.76100 1.000 38.14000 ?  586 HOH   A O    1 
HETATM 1830 O  O    . HOH   D 4 .   ? 30.20000 -10.35000 12.08200 1.000 35.29000 ?  587 HOH   A O    1 
HETATM 1831 O  O    . HOH   D 4 .   ? 28.93600 -1.95400  25.20900 1.000 38.86000 ?  588 HOH   A O    1 
HETATM 1832 O  O    . HOH   D 4 .   ? 13.25700 -18.83400 12.31100 1.000 35.76000 ?  589 HOH   A O    1 
HETATM 1833 O  O    . HOH   D 4 .   ? 25.45500 8.30400   4.27600  1.000 32.86000 ?  590 HOH   A O    1 
HETATM 1834 O  O    . HOH   D 4 .   ? 27.96300 7.66200   6.29600  1.000 37.75000 ?  591 HOH   A O    1 
HETATM 1835 O  O    . HOH   D 4 .   ? 27.72900 8.25700   14.38500 1.000 35.05000 ?  592 HOH   A O    1 
HETATM 1836 O  O    . HOH   D 4 .   ? 1.61300  -1.98700  22.02800 1.000 27.72000 ?  593 HOH   A O    1 
HETATM 1837 O  O    . HOH   D 4 .   ? 1.64700  -14.68800 8.45800  1.000 36.35000 ?  594 HOH   A O    1 
HETATM 1838 O  O    . HOH   D 4 .   ? 24.93900 10.56600  9.91300  1.000 35.10000 ?  595 HOH   A O    1 
HETATM 1839 O  O    . HOH   D 4 .   ? 32.27400 11.91900  26.64600 1.000 40.06000 ?  596 HOH   A O    1 
HETATM 1840 O  O    . HOH   D 4 .   ? 20.77300 18.30000  12.62600 1.000 40.02000 ?  597 HOH   A O    1 
HETATM 1841 O  O    . HOH   D 4 .   ? 0.36700  -10.57300 8.27100  1.000 36.77000 ?  598 HOH   A O    1 
HETATM 1842 O  O    . HOH   D 4 .   ? 20.88200 -12.85900 6.02100  1.000 38.56000 ?  599 HOH   A O    1 
HETATM 1843 O  O    . HOH   D 4 .   ? -0.21800 -3.91100  9.70500  1.000 31.20000 ?  600 HOH   A O    1 
HETATM 1844 O  O    . HOH   D 4 .   ? 28.60600 12.40100  30.38100 1.000 32.16000 ?  601 HOH   A O    1 
HETATM 1845 O  O    . HOH   D 4 .   ? 3.18500  14.68500  -2.23900 1.000 39.54000 ?  602 HOH   A O    1 
HETATM 1846 O  O    . HOH   D 4 .   ? -1.17500 -1.89500  23.65000 1.000 46.58000 ?  603 HOH   A O    1 
HETATM 1847 O  O    . HOH   D 4 .   ? 13.94000 9.82200   36.02500 1.000 35.72000 ?  604 HOH   A O    1 
HETATM 1848 O  O    . HOH   D 4 .   ? 3.81600  19.56500  2.25100  1.000 34.55000 ?  605 HOH   A O    1 
HETATM 1849 O  O    . HOH   D 4 .   ? 29.73600 5.17600   11.08100 1.000 36.75000 ?  606 HOH   A O    1 
HETATM 1850 O  O    . HOH   D 4 .   ? -4.37500 8.65300   10.74400 1.000 42.10000 ?  607 HOH   A O    1 
HETATM 1851 O  O    . HOH   D 4 .   ? 9.50200  5.85200   -1.87500 1.000 39.50000 ?  608 HOH   A O    1 
HETATM 1852 O  O    . HOH   D 4 .   ? 0.51200  14.50900  -1.31500 1.000 31.46000 ?  609 HOH   A O    1 
HETATM 1853 O  O    . HOH   D 4 .   ? -3.17000 12.88900  15.77700 1.000 42.06000 ?  610 HOH   A O    1 
# 
