data_9H1W
# 
_entry.id   9H1W 
# 
_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   9H1W         pdb_00009h1w 10.2210/pdb9h1w/pdb 
WWPDB D_1292142074 ?            ?                   
# 
_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       2025-04-30 
_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             ? 
# 
loop_
_database_PDB_caveat.id 
_database_PDB_caveat.text 
1 'BOG A 303 HAS WRONG CHIRALITY AT ATOM C3' 
2 'BOG A 303 HAS WRONG CHIRALITY AT ATOM C4' 
3 'BOG A 304 HAS WRONG CHIRALITY AT ATOM C3' 
4 'BOG A 304 HAS WRONG CHIRALITY AT ATOM C4' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9H1W 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 8pwp unspecified 
PDB . 8pwj unspecified 
PDB . 8pwi unspecified 
PDB . 8pwg unspecified 
PDB . 8pwq unspecified 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
4 richard.neutze@gu.se Richard Neutze  ? 'principal investigator/group leader' 0000-0003-0986-6153 
5 gisela.branden@gu.se Gisela  Branden ? 'principal investigator/group leader' 0000-0001-5615-7187 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ortolani, G.' 1 0000-0001-6373-9919 
'Bosman, R.'   2 0000-0002-9939-602X 
'Branden, G.'  3 0000-0001-5615-7187 
'Neutze, R.'   4 0000-0003-0986-6153 
# 
_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                3460 
_citation.page_last                 3460 
_citation.title                     
'Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-58263-x 
_citation.pdbx_database_id_PubMed   40216733 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Bosman, R.'         1  ?                   
primary 'Ortolani, G.'       2  0000-0001-6373-9919 
primary 'Ghosh, S.'          3  ?                   
primary 'James, D.'          4  0000-0002-8348-6661 
primary 'Norder, P.'         5  0000-0002-7193-640X 
primary 'Hammarin, G.'       6  0000-0001-5037-6039 
primary 'Ulfarsdottir, T.B.' 7  ?                   
primary 'Ostojic, L.'        8  ?                   
primary 'Weinert, T.'        9  0000-0002-0339-3722 
primary 'Dworkowski, F.'     10 0000-0001-5004-8684 
primary 'Tomizaki, T.'       11 0000-0003-0011-0990 
primary 'Standfuss, J.'      12 0000-0001-8825-386X 
primary 'Branden, G.'        13 0000-0001-5615-7187 
primary 'Neutze, R.'         14 0000-0003-0986-6153 
# 
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 'Sensory rhodopsin-2'                                   26666.137 1  ? ? ? ? 
2 non-polymer syn RETINAL                                                 284.436   1  ? ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                                          35.453    1  ? ? ? ? 
4 non-polymer syn 'octyl beta-D-glucopyranoside'                          292.369   8  ? ? ? ? 
5 non-polymer syn '[(Z)-octadec-9-enyl] (2R)-2,3-bis(oxidanyl)propanoate' 356.540   6  ? ? ? ? 
6 water       nat water                                                   18.015    33 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Sensory rhodopsin II,SR-II' 
# 
_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       
;MVGLTTLFWLGAIGMLVGTLAFAWAGRDAGSGERRYYVTLVGISGIAAVAYVVMALGVGWVPVAERTVFAPRYIDWILTT
PLIVYFLGLLAGLDSREFGIVITLNTVVMLAGFAGAMVPGIERYALFGMGAVAFLGLVYYLVGPMTESASQRSSGIKSLY
VRLRNLTVILWAIYPFIWLLGPPGVALLTPTVDVALIVYLDLVTKVGFGFIALDAAATLRAEHGESLAGVDTDAPAVADE
NSHHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MVGLTTLFWLGAIGMLVGTLAFAWAGRDAGSGERRYYVTLVGISGIAAVAYVVMALGVGWVPVAERTVFAPRYIDWILTT
PLIVYFLGLLAGLDSREFGIVITLNTVVMLAGFAGAMVPGIERYALFGMGAVAFLGLVYYLVGPMTESASQRSSGIKSLY
VRLRNLTVILWAIYPFIWLLGPPGVALLTPTVDVALIVYLDLVTKVGFGFIALDAAATLRAEHGESLAGVDTDAPAVADE
NSHHHHHHH
;
_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 RETINAL                                                 RET 
3 'CHLORIDE ION'                                          CL  
4 'octyl beta-D-glucopyranoside'                          BOG 
5 '[(Z)-octadec-9-enyl] (2R)-2,3-bis(oxidanyl)propanoate' MPG 
6 water                                                   HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   VAL n 
1 3   GLY n 
1 4   LEU n 
1 5   THR n 
1 6   THR n 
1 7   LEU n 
1 8   PHE n 
1 9   TRP n 
1 10  LEU n 
1 11  GLY n 
1 12  ALA n 
1 13  ILE n 
1 14  GLY n 
1 15  MET n 
1 16  LEU n 
1 17  VAL n 
1 18  GLY n 
1 19  THR n 
1 20  LEU n 
1 21  ALA n 
1 22  PHE n 
1 23  ALA n 
1 24  TRP n 
1 25  ALA n 
1 26  GLY n 
1 27  ARG n 
1 28  ASP n 
1 29  ALA n 
1 30  GLY n 
1 31  SER n 
1 32  GLY n 
1 33  GLU n 
1 34  ARG n 
1 35  ARG n 
1 36  TYR n 
1 37  TYR n 
1 38  VAL n 
1 39  THR n 
1 40  LEU n 
1 41  VAL n 
1 42  GLY n 
1 43  ILE n 
1 44  SER n 
1 45  GLY n 
1 46  ILE n 
1 47  ALA n 
1 48  ALA n 
1 49  VAL n 
1 50  ALA n 
1 51  TYR n 
1 52  VAL n 
1 53  VAL n 
1 54  MET n 
1 55  ALA n 
1 56  LEU n 
1 57  GLY n 
1 58  VAL n 
1 59  GLY n 
1 60  TRP n 
1 61  VAL n 
1 62  PRO n 
1 63  VAL n 
1 64  ALA n 
1 65  GLU n 
1 66  ARG n 
1 67  THR n 
1 68  VAL n 
1 69  PHE n 
1 70  ALA n 
1 71  PRO n 
1 72  ARG n 
1 73  TYR n 
1 74  ILE n 
1 75  ASP n 
1 76  TRP n 
1 77  ILE n 
1 78  LEU n 
1 79  THR n 
1 80  THR n 
1 81  PRO n 
1 82  LEU n 
1 83  ILE n 
1 84  VAL n 
1 85  TYR n 
1 86  PHE n 
1 87  LEU n 
1 88  GLY n 
1 89  LEU n 
1 90  LEU n 
1 91  ALA n 
1 92  GLY n 
1 93  LEU n 
1 94  ASP n 
1 95  SER n 
1 96  ARG n 
1 97  GLU n 
1 98  PHE n 
1 99  GLY n 
1 100 ILE n 
1 101 VAL n 
1 102 ILE n 
1 103 THR n 
1 104 LEU n 
1 105 ASN n 
1 106 THR n 
1 107 VAL n 
1 108 VAL n 
1 109 MET n 
1 110 LEU n 
1 111 ALA n 
1 112 GLY n 
1 113 PHE n 
1 114 ALA n 
1 115 GLY n 
1 116 ALA n 
1 117 MET n 
1 118 VAL n 
1 119 PRO n 
1 120 GLY n 
1 121 ILE n 
1 122 GLU n 
1 123 ARG n 
1 124 TYR n 
1 125 ALA n 
1 126 LEU n 
1 127 PHE n 
1 128 GLY n 
1 129 MET n 
1 130 GLY n 
1 131 ALA n 
1 132 VAL n 
1 133 ALA n 
1 134 PHE n 
1 135 LEU n 
1 136 GLY n 
1 137 LEU n 
1 138 VAL n 
1 139 TYR n 
1 140 TYR n 
1 141 LEU n 
1 142 VAL n 
1 143 GLY n 
1 144 PRO n 
1 145 MET n 
1 146 THR n 
1 147 GLU n 
1 148 SER n 
1 149 ALA n 
1 150 SER n 
1 151 GLN n 
1 152 ARG n 
1 153 SER n 
1 154 SER n 
1 155 GLY n 
1 156 ILE n 
1 157 LYS n 
1 158 SER n 
1 159 LEU n 
1 160 TYR n 
1 161 VAL n 
1 162 ARG n 
1 163 LEU n 
1 164 ARG n 
1 165 ASN n 
1 166 LEU n 
1 167 THR n 
1 168 VAL n 
1 169 ILE n 
1 170 LEU n 
1 171 TRP n 
1 172 ALA n 
1 173 ILE n 
1 174 TYR n 
1 175 PRO n 
1 176 PHE n 
1 177 ILE n 
1 178 TRP n 
1 179 LEU n 
1 180 LEU n 
1 181 GLY n 
1 182 PRO n 
1 183 PRO n 
1 184 GLY n 
1 185 VAL n 
1 186 ALA n 
1 187 LEU n 
1 188 LEU n 
1 189 THR n 
1 190 PRO n 
1 191 THR n 
1 192 VAL n 
1 193 ASP n 
1 194 VAL n 
1 195 ALA n 
1 196 LEU n 
1 197 ILE n 
1 198 VAL n 
1 199 TYR n 
1 200 LEU n 
1 201 ASP n 
1 202 LEU n 
1 203 VAL n 
1 204 THR n 
1 205 LYS n 
1 206 VAL n 
1 207 GLY n 
1 208 PHE n 
1 209 GLY n 
1 210 PHE n 
1 211 ILE n 
1 212 ALA n 
1 213 LEU n 
1 214 ASP n 
1 215 ALA n 
1 216 ALA n 
1 217 ALA n 
1 218 THR n 
1 219 LEU n 
1 220 ARG n 
1 221 ALA n 
1 222 GLU n 
1 223 HIS n 
1 224 GLY n 
1 225 GLU n 
1 226 SER n 
1 227 LEU n 
1 228 ALA n 
1 229 GLY n 
1 230 VAL n 
1 231 ASP n 
1 232 THR n 
1 233 ASP n 
1 234 ALA n 
1 235 PRO n 
1 236 ALA n 
1 237 VAL n 
1 238 ALA n 
1 239 ASP n 
1 240 GLU n 
1 241 ASN n 
1 242 SER n 
1 243 HIS n 
1 244 HIS n 
1 245 HIS n 
1 246 HIS n 
1 247 HIS n 
1 248 HIS n 
1 249 HIS 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                   249 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'sop2, sopII' 
_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      'Natronomonas pharaonis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2257 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                 ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                                ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                              ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                         ? 'C4 H7 N O4'     133.103 
BOG D-saccharide        n 'octyl beta-D-glucopyranoside'                          
'Beta-Octylglucoside; octyl beta-D-glucoside; octyl D-glucoside; octyl glucoside' 'C14 H28 O6'     292.369 
CL  non-polymer         . 'CHLORIDE ION'                                          ? 'Cl -1'          35.453  
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 
MPG non-polymer         . '[(Z)-octadec-9-enyl] (2R)-2,3-bis(oxidanyl)propanoate' ? 'C21 H40 O4'     356.540 
PHE 'L-peptide linking' y PHENYLALANINE                                           ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                                 ? 'C5 H9 N O2'     115.130 
RET non-polymer         . RETINAL                                                 ? 'C20 H28 O'      284.436 
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 
# 
_pdbx_chem_comp_identifier.comp_id           BOG 
_pdbx_chem_comp_identifier.type              'IUPAC CARBOHYDRATE SYMBOL' 
_pdbx_chem_comp_identifier.program           PDB-CARE 
_pdbx_chem_comp_identifier.program_version   1.0 
_pdbx_chem_comp_identifier.identifier        b-octylglucoside 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   VAL 2   2   2   VAL VAL A . n 
A 1 3   GLY 3   3   3   GLY GLY A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   THR 6   6   6   THR THR A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   TRP 9   9   9   TRP TRP A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  ILE 13  13  13  ILE ILE A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  MET 15  15  15  MET MET A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  VAL 17  17  17  VAL VAL A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  PHE 22  22  22  PHE PHE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  TRP 24  24  24  TRP TRP A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  ASP 28  28  ?   ?   ?   A . n 
A 1 29  ALA 29  29  ?   ?   ?   A . n 
A 1 30  GLY 30  30  ?   ?   ?   A . n 
A 1 31  SER 31  31  ?   ?   ?   A . n 
A 1 32  GLY 32  32  ?   ?   ?   A . n 
A 1 33  GLU 33  33  ?   ?   ?   A . n 
A 1 34  ARG 34  34  ?   ?   ?   A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  TYR 36  36  36  TYR TYR A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  LEU 40  40  40  LEU LEU A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  GLY 42  42  42  GLY GLY A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  SER 44  44  44  SER SER A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  ALA 48  48  48  ALA ALA A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  VAL 52  52  52  VAL VAL A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  MET 54  54  54  MET MET A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  TRP 60  60  60  TRP TRP A . n 
A 1 61  VAL 61  61  61  VAL VAL A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  THR 67  67  67  THR THR A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  PHE 69  69  69  PHE PHE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  PRO 71  71  71  PRO PRO A . n 
A 1 72  ARG 72  72  72  ARG ARG A . n 
A 1 73  TYR 73  73  73  TYR TYR A . n 
A 1 74  ILE 74  74  74  ILE ILE A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  TRP 76  76  76  TRP TRP A . n 
A 1 77  ILE 77  77  77  ILE ILE A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  THR 80  80  80  THR THR A . n 
A 1 81  PRO 81  81  81  PRO PRO A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  ILE 83  83  83  ILE ILE A . n 
A 1 84  VAL 84  84  84  VAL VAL A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  PHE 86  86  86  PHE PHE A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  ASP 94  94  94  ASP ASP A . n 
A 1 95  SER 95  95  95  SER SER A . n 
A 1 96  ARG 96  96  96  ARG ARG A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 THR 103 103 103 THR THR A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 ASN 105 105 105 ASN ASN A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 VAL 108 108 108 VAL VAL A . n 
A 1 109 MET 109 109 109 MET MET A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 PHE 113 113 113 PHE PHE A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 GLY 115 115 115 GLY GLY A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 MET 117 117 117 MET MET A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 PRO 119 119 119 PRO PRO A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 ILE 121 121 121 ILE ILE A . n 
A 1 122 GLU 122 122 122 GLU GLU A . n 
A 1 123 ARG 123 123 123 ARG ARG A . n 
A 1 124 TYR 124 124 124 TYR TYR A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 PHE 127 127 127 PHE PHE A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 MET 129 129 129 MET MET A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 ALA 133 133 133 ALA ALA A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 TYR 139 139 139 TYR TYR A . n 
A 1 140 TYR 140 140 140 TYR TYR A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 PRO 144 144 144 PRO PRO A . n 
A 1 145 MET 145 145 145 MET MET A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 SER 148 148 148 SER SER A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 GLN 151 151 151 GLN GLN A . n 
A 1 152 ARG 152 152 152 ARG ARG A . n 
A 1 153 SER 153 153 153 SER SER A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 ILE 156 156 156 ILE ILE A . n 
A 1 157 LYS 157 157 157 LYS LYS A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 TYR 160 160 160 TYR TYR A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 ARG 162 162 162 ARG ARG A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 ASN 165 165 165 ASN ASN A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 THR 167 167 167 THR THR A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 TRP 171 171 171 TRP TRP A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 ILE 173 173 173 ILE ILE A . n 
A 1 174 TYR 174 174 174 TYR TYR A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 PHE 176 176 176 PHE PHE A . n 
A 1 177 ILE 177 177 177 ILE ILE A . n 
A 1 178 TRP 178 178 178 TRP TRP A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 GLY 181 181 181 GLY GLY A . n 
A 1 182 PRO 182 182 182 PRO PRO A . n 
A 1 183 PRO 183 183 183 PRO PRO A . n 
A 1 184 GLY 184 184 184 GLY GLY A . n 
A 1 185 VAL 185 185 185 VAL VAL A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 THR 189 189 189 THR THR A . n 
A 1 190 PRO 190 190 190 PRO PRO A . n 
A 1 191 THR 191 191 191 THR THR A . n 
A 1 192 VAL 192 192 192 VAL VAL A . n 
A 1 193 ASP 193 193 193 ASP ASP A . n 
A 1 194 VAL 194 194 194 VAL VAL A . n 
A 1 195 ALA 195 195 195 ALA ALA A . n 
A 1 196 LEU 196 196 196 LEU LEU A . n 
A 1 197 ILE 197 197 197 ILE ILE A . n 
A 1 198 VAL 198 198 198 VAL VAL A . n 
A 1 199 TYR 199 199 199 TYR TYR A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 ASP 201 201 201 ASP ASP A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 THR 204 204 204 THR THR A . n 
A 1 205 LYS 205 205 205 LYS LYS A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 GLY 207 207 207 GLY GLY A . n 
A 1 208 PHE 208 208 208 PHE PHE A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 PHE 210 210 210 PHE PHE A . n 
A 1 211 ILE 211 211 211 ILE ILE A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 LEU 213 213 213 LEU LEU A . n 
A 1 214 ASP 214 214 214 ASP ASP A . n 
A 1 215 ALA 215 215 215 ALA ALA A . n 
A 1 216 ALA 216 216 216 ALA ALA A . n 
A 1 217 ALA 217 217 217 ALA ALA A . n 
A 1 218 THR 218 218 218 THR THR A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 ARG 220 220 ?   ?   ?   A . n 
A 1 221 ALA 221 221 ?   ?   ?   A . n 
A 1 222 GLU 222 222 ?   ?   ?   A . n 
A 1 223 HIS 223 223 ?   ?   ?   A . n 
A 1 224 GLY 224 224 ?   ?   ?   A . n 
A 1 225 GLU 225 225 ?   ?   ?   A . n 
A 1 226 SER 226 226 ?   ?   ?   A . n 
A 1 227 LEU 227 227 ?   ?   ?   A . n 
A 1 228 ALA 228 228 ?   ?   ?   A . n 
A 1 229 GLY 229 229 ?   ?   ?   A . n 
A 1 230 VAL 230 230 ?   ?   ?   A . n 
A 1 231 ASP 231 231 ?   ?   ?   A . n 
A 1 232 THR 232 232 ?   ?   ?   A . n 
A 1 233 ASP 233 233 ?   ?   ?   A . n 
A 1 234 ALA 234 234 ?   ?   ?   A . n 
A 1 235 PRO 235 235 ?   ?   ?   A . n 
A 1 236 ALA 236 236 ?   ?   ?   A . n 
A 1 237 VAL 237 237 ?   ?   ?   A . n 
A 1 238 ALA 238 238 ?   ?   ?   A . n 
A 1 239 ASP 239 239 ?   ?   ?   A . n 
A 1 240 GLU 240 240 ?   ?   ?   A . n 
A 1 241 ASN 241 241 ?   ?   ?   A . n 
A 1 242 SER 242 242 ?   ?   ?   A . n 
A 1 243 HIS 243 243 ?   ?   ?   A . n 
A 1 244 HIS 244 244 ?   ?   ?   A . n 
A 1 245 HIS 245 245 ?   ?   ?   A . n 
A 1 246 HIS 246 246 ?   ?   ?   A . n 
A 1 247 HIS 247 247 ?   ?   ?   A . n 
A 1 248 HIS 248 248 ?   ?   ?   A . n 
A 1 249 HIS 249 249 ?   ?   ?   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 BOG ? ? BOG ? ? 'SUBJECT OF INVESTIGATION' ? 
2 CL  ? ? CL  ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MPG ? ? MPG ? ? 'SUBJECT OF INVESTIGATION' ? 
4 RET ? ? RET ? ? '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 RET 1  301 301 RET RET A . 
C 3 CL  1  302 302 CL  CL  A . 
D 4 BOG 1  303 303 BOG BOG A . 
E 4 BOG 1  304 304 BOG BOG A . 
F 4 BOG 1  305 305 BOG BOG A . 
G 5 MPG 1  306 306 MPG MPG A . 
H 4 BOG 1  307 307 BOG BOG A . 
I 4 BOG 1  308 308 BOG BOG A . 
J 5 MPG 1  309 309 MPG MPG A . 
K 5 MPG 1  310 310 MPG MPG A . 
L 5 MPG 1  311 311 MPG MPG A . 
M 5 MPG 1  312 312 MPG MPG A . 
N 4 BOG 1  313 313 BOG BOG A . 
O 5 MPG 1  314 314 MPG MPG A . 
P 4 BOG 1  315 315 BOG BOG A . 
Q 4 BOG 1  316 316 BOG BOG A . 
R 6 HOH 1  401 432 HOH HOH A . 
R 6 HOH 2  402 401 HOH HOH A . 
R 6 HOH 3  403 402 HOH HOH A . 
R 6 HOH 4  404 404 HOH HOH A . 
R 6 HOH 5  405 407 HOH HOH A . 
R 6 HOH 6  406 5   HOH HOH A . 
R 6 HOH 7  407 408 HOH HOH A . 
R 6 HOH 8  408 2   HOH HOH A . 
R 6 HOH 9  409 409 HOH HOH A . 
R 6 HOH 10 410 411 HOH HOH A . 
R 6 HOH 11 411 412 HOH HOH A . 
R 6 HOH 12 412 413 HOH HOH A . 
R 6 HOH 13 413 415 HOH HOH A . 
R 6 HOH 14 414 416 HOH HOH A . 
R 6 HOH 15 415 19  HOH HOH A . 
R 6 HOH 16 416 418 HOH HOH A . 
R 6 HOH 17 417 419 HOH HOH A . 
R 6 HOH 18 418 420 HOH HOH A . 
R 6 HOH 19 419 421 HOH HOH A . 
R 6 HOH 20 420 423 HOH HOH A . 
R 6 HOH 21 421 422 HOH HOH A . 
R 6 HOH 22 422 426 HOH HOH A . 
R 6 HOH 23 423 425 HOH HOH A . 
R 6 HOH 24 424 427 HOH HOH A . 
R 6 HOH 25 425 424 HOH HOH A . 
R 6 HOH 26 426 428 HOH HOH A . 
R 6 HOH 27 427 430 HOH HOH A . 
R 6 HOH 28 428 431 HOH HOH A . 
R 6 HOH 29 429 405 HOH HOH A . 
R 6 HOH 30 430 20  HOH HOH A . 
R 6 HOH 31 431 435 HOH HOH A . 
R 6 HOH 32 432 437 HOH HOH A . 
R 6 HOH 33 433 438 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 GLU 97  ? CG    ? A GLU 97 CG    
2  1 Y 1 A GLU 97  ? CD    ? A GLU 97 CD    
3  1 Y 1 A GLU 97  ? OE1   ? A GLU 97 OE1   
4  1 Y 1 A GLU 97  ? OE2   ? A GLU 97 OE2   
5  1 N 1 A MPG 311 ? C12   ? L MPG 1  C12   
6  1 N 1 A MPG 311 ? C13   ? L MPG 1  C13   
7  1 N 1 A MPG 311 ? C14   ? L MPG 1  C14   
8  1 N 1 A MPG 311 ? C15   ? L MPG 1  C15   
9  1 N 1 A MPG 311 ? C16   ? L MPG 1  C16   
10 1 N 1 A MPG 311 ? C17   ? L MPG 1  C17   
11 1 N 1 A MPG 311 ? C18   ? L MPG 1  C18   
12 1 N 1 A MPG 314 ? C14   ? O MPG 1  C14   
13 1 N 1 A MPG 314 ? C15   ? O MPG 1  C15   
14 1 N 1 A MPG 314 ? C16   ? O MPG 1  C16   
15 1 N 1 A MPG 314 ? C17   ? O MPG 1  C17   
16 1 N 1 A MPG 314 ? C18   ? O MPG 1  C18   
17 1 N 1 A BOG 315 ? "C5'" ? P BOG 1  "C5'" 
18 1 N 1 A BOG 315 ? "C6'" ? P BOG 1  "C6'" 
19 1 N 1 A BOG 315 ? "C7'" ? P BOG 1  "C7'" 
20 1 N 1 A BOG 315 ? "C8'" ? P BOG 1  "C8'" 
# 
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' ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9H1W 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     89.750 
_cell.length_a_esd                 ? 
_cell.length_b                     131.750 
_cell.length_b_esd                 ? 
_cell.length_c                     51.000 
_cell.length_c_esd                 ? 
_cell.volume                       603052.688 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9H1W 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            'C 2c 2' 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9H1W 
_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             2.83 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.49 
_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          'LIPIDIC CUBIC PHASE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'CaCl2 150 mM, Glycine 100 mM, 38% (v/v) PEG 400, pH 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            296 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     296 
_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   Y 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-11-11 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0000342 
_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                        'SLS BEAMLINE X06SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0000342 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          46.51 
_reflns.entry_id                                       9H1W 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.20 
_reflns.d_resolution_low                               44.88 
_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                                     4429 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                268.03 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          22.88 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.9941 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.20 
_reflns_shell.d_res_low                                     44.88 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4429 
_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                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.9941 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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                               54.28 
_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                                 9H1W 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.20 
_refine.ls_d_res_low                             44.88 
_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                     4429 
_refine.ls_number_reflns_R_free                  791 
_refine.ls_number_reflns_R_work                  14917 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.75 
_refine.ls_percent_reflns_R_free                 5.04 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2158 
_refine.ls_R_factor_R_free                       0.2185 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2157 
_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                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 23.6588 
_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                            0.2771 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.20 
_refine_hist.d_res_low                        44.88 
_refine_hist.number_atoms_solvent             33 
_refine_hist.number_atoms_total               1951 
_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        1603 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         315 
_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' ? 0.0079  ? 1952 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0988  ? 2613 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.5504  ? 323  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0039  ? 283  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 18.6618 ? 689  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.20 2.34  . . 130 2401 99.37 . . . . 0.3319 . . . . . . . . . . . 0.3159 
'X-RAY DIFFRACTION' 2.34 2.52  . . 133 2453 99.54 . . . . 0.2592 . . . . . . . . . . . 0.2555 
'X-RAY DIFFRACTION' 2.52 2.77  . . 117 2475 99.81 . . . . 0.2296 . . . . . . . . . . . 0.2219 
'X-RAY DIFFRACTION' 2.77 3.17  . . 136 2476 99.89 . . . . 0.2147 . . . . . . . . . . . 0.2192 
'X-RAY DIFFRACTION' 3.17 4.00  . . 139 2493 99.96 . . . . 0.1881 . . . . . . . . . . . 0.1951 
'X-RAY DIFFRACTION' 4.00 44.88 . . 136 2619 99.89 . . . . 0.2080 . . . . . . . . . . . 0.2129 
# 
_struct.entry_id                     9H1W 
_struct.title                        
'Grouped 150-240 ms dark structure of sensory rhodopsin-II solved by serial millisecond crystallography' 
_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        9H1W 
_struct_keywords.text            
;SRII, serial millisecond crystallography, sensory rhodopsin, sensory rhodopsin II, SMX, SSX, Time-resolved crystallography, TRX, SIGNALING PROTEIN
;
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 4 ? 
G N N 5 ? 
H N N 4 ? 
I N N 4 ? 
J N N 5 ? 
K N N 5 ? 
L N N 5 ? 
M N N 5 ? 
N N N 4 ? 
O N N 5 ? 
P N N 4 ? 
Q N N 4 ? 
R N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    BACS2_NATPH 
_struct_ref.pdbx_db_accession          P42196 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MVGLTTLFWLGAIGMLVGTLAFAWAGRDAGSGERRYYVTLVGISGIAAVAYVVMALGVGWVPVAERTVFAPRYIDWILTT
PLIVYFLGLLAGLDSREFGIVITLNTVVMLAGFAGAMVPGIERYALFGMGAVAFLGLVYYLVGPMTESASQRSSGIKSLY
VRLRNLTVILWAIYPFIWLLGPPGVALLTPTVDVALIVYLDLVTKVGFGFIALDAAATLRAEHGESLAGVDTDAPAVAD
;
_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              9H1W 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 239 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P42196 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  239 
_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       239 
# 
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 9H1W GLU A 240 ? UNP P42196 ? ? 'expression tag' 240 1  
1 9H1W ASN A 241 ? UNP P42196 ? ? 'expression tag' 241 2  
1 9H1W SER A 242 ? UNP P42196 ? ? 'expression tag' 242 3  
1 9H1W HIS A 243 ? UNP P42196 ? ? 'expression tag' 243 4  
1 9H1W HIS A 244 ? UNP P42196 ? ? 'expression tag' 244 5  
1 9H1W HIS A 245 ? UNP P42196 ? ? 'expression tag' 245 6  
1 9H1W HIS A 246 ? UNP P42196 ? ? 'expression tag' 246 7  
1 9H1W HIS A 247 ? UNP P42196 ? ? 'expression tag' 247 8  
1 9H1W HIS A 248 ? UNP P42196 ? ? 'expression tag' 248 9  
1 9H1W HIS A 249 ? UNP P42196 ? ? 'expression tag' 249 10 
# 
_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,E,F,G,H,I,J,K,L,M,N,O,P,Q,R 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'light scattering' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 3   ? GLY A 26  ? GLY A 3   GLY A 26  1 ? 24 
HELX_P HELX_P2 AA2 TYR A 36  ? LEU A 56  ? TYR A 36  LEU A 56  1 ? 21 
HELX_P HELX_P3 AA3 ALA A 70  ? GLY A 92  ? ALA A 70  GLY A 92  1 ? 23 
HELX_P HELX_P4 AA4 ASP A 94  ? MET A 117 ? ASP A 94  MET A 117 1 ? 24 
HELX_P HELX_P5 AA5 ILE A 121 ? GLY A 143 ? ILE A 121 GLY A 143 1 ? 23 
HELX_P HELX_P6 AA6 GLY A 143 ? SER A 150 ? GLY A 143 SER A 150 1 ? 8  
HELX_P HELX_P7 AA7 SER A 153 ? ALA A 172 ? SER A 153 ALA A 172 1 ? 20 
HELX_P HELX_P8 AA8 ILE A 173 ? GLY A 181 ? ILE A 173 GLY A 181 1 ? 9  
HELX_P HELX_P9 AA9 THR A 189 ? LEU A 219 ? THR A 189 LEU A 219 1 ? 31 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        one 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           LYS 
_struct_conn.ptnr1_label_seq_id            205 
_struct_conn.ptnr1_label_atom_id           NZ 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           RET 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C15 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            LYS 
_struct_conn.ptnr1_auth_seq_id             205 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            RET 
_struct_conn.ptnr2_auth_seq_id             301 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               1.392 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      RET 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     LYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      205 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       RET 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        301 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      LYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       205 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C15 
_pdbx_modification_feature.modified_residue_id_linking_atom   NZ 
_pdbx_modification_feature.modified_residue_id                LYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        RET 
_pdbx_modification_feature.type                               Retinoylation 
_pdbx_modification_feature.category                           Lipid/lipid-like 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   2 
_struct_sheet.details          ? 
# 
_struct_sheet_order.sheet_id     AA1 
_struct_sheet_order.range_id_1   1 
_struct_sheet_order.range_id_2   2 
_struct_sheet_order.offset       ? 
_struct_sheet_order.sense        anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TRP A 60 ? VAL A 63 ? TRP A 60 VAL A 63 
AA1 2 ARG A 66 ? PHE A 69 ? ARG A 66 PHE A 69 
# 
_pdbx_struct_sheet_hbond.sheet_id                AA1 
_pdbx_struct_sheet_hbond.range_id_1              1 
_pdbx_struct_sheet_hbond.range_id_2              2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id   N 
_pdbx_struct_sheet_hbond.range_1_label_comp_id   VAL 
_pdbx_struct_sheet_hbond.range_1_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_1_label_seq_id    61 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id    N 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id    VAL 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id     61 
_pdbx_struct_sheet_hbond.range_2_label_atom_id   O 
_pdbx_struct_sheet_hbond.range_2_label_comp_id   VAL 
_pdbx_struct_sheet_hbond.range_2_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_2_label_seq_id    68 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id    O 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id    VAL 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id     68 
# 
_pdbx_entry_details.entry_id                   9H1W 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 NH2 A ARG 96 ? ? O  A HOH 401 ? ? 0.82 
2 1 CZ  A ARG 96 ? ? O  A HOH 401 ? ? 0.90 
3 1 NE  A ARG 96 ? ? O  A HOH 401 ? ? 1.86 
4 1 NH1 A ARG 96 ? ? O  A HOH 401 ? ? 1.89 
5 1 O   A ALA 91 ? ? OG A SER 148 ? ? 2.18 
# 
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 ALA A 64  ? ? 57.19  -105.49 
2 1 ALA A 186 ? ? 22.05  42.94   
3 1 LEU A 187 ? ? -68.52 -76.41  
# 
loop_
_pdbx_validate_chiral.id 
_pdbx_validate_chiral.PDB_model_num 
_pdbx_validate_chiral.auth_atom_id 
_pdbx_validate_chiral.label_alt_id 
_pdbx_validate_chiral.auth_asym_id 
_pdbx_validate_chiral.auth_comp_id 
_pdbx_validate_chiral.auth_seq_id 
_pdbx_validate_chiral.PDB_ins_code 
_pdbx_validate_chiral.details 
_pdbx_validate_chiral.omega 
1 1 C3 ? A BOG 303 ? 'WRONG HAND' . 
2 1 C4 ? A BOG 303 ? 'WRONG HAND' . 
3 1 C3 ? A BOG 304 ? 'WRONG HAND' . 
4 1 C4 ? A BOG 304 ? 'WRONG HAND' . 
# 
_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     404 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   R 
_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,y,-z+1/2         
4 -x,-y,z+1/2         
5 x+1/2,y+1/2,z       
6 x+1/2,-y+1/2,-z     
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
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 ASP 28  ? A ASP 28  
2  1 Y 1 A ALA 29  ? A ALA 29  
3  1 Y 1 A GLY 30  ? A GLY 30  
4  1 Y 1 A SER 31  ? A SER 31  
5  1 Y 1 A GLY 32  ? A GLY 32  
6  1 Y 1 A GLU 33  ? A GLU 33  
7  1 Y 1 A ARG 34  ? A ARG 34  
8  1 Y 1 A ARG 220 ? A ARG 220 
9  1 Y 1 A ALA 221 ? A ALA 221 
10 1 Y 1 A GLU 222 ? A GLU 222 
11 1 Y 1 A HIS 223 ? A HIS 223 
12 1 Y 1 A GLY 224 ? A GLY 224 
13 1 Y 1 A GLU 225 ? A GLU 225 
14 1 Y 1 A SER 226 ? A SER 226 
15 1 Y 1 A LEU 227 ? A LEU 227 
16 1 Y 1 A ALA 228 ? A ALA 228 
17 1 Y 1 A GLY 229 ? A GLY 229 
18 1 Y 1 A VAL 230 ? A VAL 230 
19 1 Y 1 A ASP 231 ? A ASP 231 
20 1 Y 1 A THR 232 ? A THR 232 
21 1 Y 1 A ASP 233 ? A ASP 233 
22 1 Y 1 A ALA 234 ? A ALA 234 
23 1 Y 1 A PRO 235 ? A PRO 235 
24 1 Y 1 A ALA 236 ? A ALA 236 
25 1 Y 1 A VAL 237 ? A VAL 237 
26 1 Y 1 A ALA 238 ? A ALA 238 
27 1 Y 1 A ASP 239 ? A ASP 239 
28 1 Y 1 A GLU 240 ? A GLU 240 
29 1 Y 1 A ASN 241 ? A ASN 241 
30 1 Y 1 A SER 242 ? A SER 242 
31 1 Y 1 A HIS 243 ? A HIS 243 
32 1 Y 1 A HIS 244 ? A HIS 244 
33 1 Y 1 A HIS 245 ? A HIS 245 
34 1 Y 1 A HIS 246 ? A HIS 246 
35 1 Y 1 A HIS 247 ? A HIS 247 
36 1 Y 1 A HIS 248 ? A HIS 248 
37 1 Y 1 A HIS 249 ? A HIS 249 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
BOG C1     C  N R 74  
BOG O1     O  N N 75  
BOG C2     C  N R 76  
BOG O2     O  N N 77  
BOG C3     C  N S 78  
BOG O3     O  N N 79  
BOG C4     C  N S 80  
BOG O4     O  N N 81  
BOG C5     C  N R 82  
BOG O5     O  N N 83  
BOG C6     C  N N 84  
BOG O6     O  N N 85  
BOG "C1'"  C  N N 86  
BOG "C2'"  C  N N 87  
BOG "C3'"  C  N N 88  
BOG "C4'"  C  N N 89  
BOG "C5'"  C  N N 90  
BOG "C6'"  C  N N 91  
BOG "C7'"  C  N N 92  
BOG "C8'"  C  N N 93  
BOG H1     H  N N 94  
BOG H2     H  N N 95  
BOG HO2    H  N N 96  
BOG H3     H  N N 97  
BOG HO3    H  N N 98  
BOG H4     H  N N 99  
BOG HO4    H  N N 100 
BOG H5     H  N N 101 
BOG H61    H  N N 102 
BOG H62    H  N N 103 
BOG HO6    H  N N 104 
BOG "H1'1" H  N N 105 
BOG "H1'2" H  N N 106 
BOG "H2'1" H  N N 107 
BOG "H2'2" H  N N 108 
BOG "H3'1" H  N N 109 
BOG "H3'2" H  N N 110 
BOG "H4'1" H  N N 111 
BOG "H4'2" H  N N 112 
BOG "H5'1" H  N N 113 
BOG "H5'2" H  N N 114 
BOG "H6'1" H  N N 115 
BOG "H6'2" H  N N 116 
BOG "H7'1" H  N N 117 
BOG "H7'2" H  N N 118 
BOG "H8'1" H  N N 119 
BOG "H8'2" H  N N 120 
BOG "H8'3" H  N N 121 
CL  CL     CL 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 
MPG C2     C  N N 285 
MPG C3     C  N N 286 
MPG C4     C  N N 287 
MPG C5     C  N N 288 
MPG C6     C  N N 289 
MPG C7     C  N N 290 
MPG C8     C  N N 291 
MPG C9     C  N N 292 
MPG C10    C  N N 293 
MPG C11    C  N N 294 
MPG C12    C  N N 295 
MPG C13    C  N N 296 
MPG C14    C  N N 297 
MPG C15    C  N N 298 
MPG C16    C  N N 299 
MPG C17    C  N N 300 
MPG C18    C  N N 301 
MPG O1     O  N N 302 
MPG C1     C  N N 303 
MPG CXD    C  N R 304 
MPG O2     O  N N 305 
MPG C21    C  N N 306 
MPG O3     O  N N 307 
MPG O4     O  N N 308 
MPG CX3    C  N N 309 
MPG H21C   H  N N 310 
MPG H22C   H  N N 311 
MPG H31C   H  N N 312 
MPG H32C   H  N N 313 
MPG H41C   H  N N 314 
MPG H42C   H  N N 315 
MPG H51C   H  N N 316 
MPG H52C   H  N N 317 
MPG H61C   H  N N 318 
MPG H62C   H  N N 319 
MPG H71C   H  N N 320 
MPG H72C   H  N N 321 
MPG H81C   H  N N 322 
MPG H82C   H  N N 323 
MPG H9     H  N N 324 
MPG H10    H  N N 325 
MPG H111   H  N N 326 
MPG H112   H  N N 327 
MPG H121   H  N N 328 
MPG H122   H  N N 329 
MPG H131   H  N N 330 
MPG H132   H  N N 331 
MPG H141   H  N N 332 
MPG H142   H  N N 333 
MPG H151   H  N N 334 
MPG H152   H  N N 335 
MPG H161   H  N N 336 
MPG H162   H  N N 337 
MPG H171   H  N N 338 
MPG H172   H  N N 339 
MPG H181   H  N N 340 
MPG H182   H  N N 341 
MPG H183   H  N N 342 
MPG HX31   H  N N 343 
MPG HX32   H  N N 344 
MPG HXD    H  N N 345 
MPG H2     H  N N 346 
MPG H211   H  N N 347 
MPG H212   H  N N 348 
MPG H3     H  N N 349 
PHE N      N  N N 350 
PHE CA     C  N S 351 
PHE C      C  N N 352 
PHE O      O  N N 353 
PHE CB     C  N N 354 
PHE CG     C  Y N 355 
PHE CD1    C  Y N 356 
PHE CD2    C  Y N 357 
PHE CE1    C  Y N 358 
PHE CE2    C  Y N 359 
PHE CZ     C  Y N 360 
PHE OXT    O  N N 361 
PHE H      H  N N 362 
PHE H2     H  N N 363 
PHE HA     H  N N 364 
PHE HB2    H  N N 365 
PHE HB3    H  N N 366 
PHE HD1    H  N N 367 
PHE HD2    H  N N 368 
PHE HE1    H  N N 369 
PHE HE2    H  N N 370 
PHE HZ     H  N N 371 
PHE HXT    H  N N 372 
PRO N      N  N N 373 
PRO CA     C  N S 374 
PRO C      C  N N 375 
PRO O      O  N N 376 
PRO CB     C  N N 377 
PRO CG     C  N N 378 
PRO CD     C  N N 379 
PRO OXT    O  N N 380 
PRO H      H  N N 381 
PRO HA     H  N N 382 
PRO HB2    H  N N 383 
PRO HB3    H  N N 384 
PRO HG2    H  N N 385 
PRO HG3    H  N N 386 
PRO HD2    H  N N 387 
PRO HD3    H  N N 388 
PRO HXT    H  N N 389 
RET C1     C  N N 390 
RET C2     C  N N 391 
RET C3     C  N N 392 
RET C4     C  N N 393 
RET C5     C  N N 394 
RET C6     C  N N 395 
RET C7     C  N N 396 
RET C8     C  N N 397 
RET C9     C  N N 398 
RET C10    C  N N 399 
RET C11    C  N N 400 
RET C12    C  N N 401 
RET C13    C  N N 402 
RET C14    C  N N 403 
RET C15    C  N N 404 
RET O1     O  N N 405 
RET C16    C  N N 406 
RET C17    C  N N 407 
RET C18    C  N N 408 
RET C19    C  N N 409 
RET C20    C  N N 410 
RET H21    H  N N 411 
RET H22    H  N N 412 
RET H31    H  N N 413 
RET H32    H  N N 414 
RET H41    H  N N 415 
RET H42    H  N N 416 
RET H7     H  N N 417 
RET H8     H  N N 418 
RET H10    H  N N 419 
RET H11    H  N N 420 
RET H12    H  N N 421 
RET H14    H  N N 422 
RET H15    H  N N 423 
RET H161   H  N N 424 
RET H162   H  N N 425 
RET H163   H  N N 426 
RET H171   H  N N 427 
RET H172   H  N N 428 
RET H173   H  N N 429 
RET H181   H  N N 430 
RET H182   H  N N 431 
RET H183   H  N N 432 
RET H191   H  N N 433 
RET H192   H  N N 434 
RET H193   H  N N 435 
RET H201   H  N N 436 
RET H202   H  N N 437 
RET H203   H  N N 438 
SER N      N  N N 439 
SER CA     C  N S 440 
SER C      C  N N 441 
SER O      O  N N 442 
SER CB     C  N N 443 
SER OG     O  N N 444 
SER OXT    O  N N 445 
SER H      H  N N 446 
SER H2     H  N N 447 
SER HA     H  N N 448 
SER HB2    H  N N 449 
SER HB3    H  N N 450 
SER HG     H  N N 451 
SER HXT    H  N N 452 
THR N      N  N N 453 
THR CA     C  N S 454 
THR C      C  N N 455 
THR O      O  N N 456 
THR CB     C  N R 457 
THR OG1    O  N N 458 
THR CG2    C  N N 459 
THR OXT    O  N N 460 
THR H      H  N N 461 
THR H2     H  N N 462 
THR HA     H  N N 463 
THR HB     H  N N 464 
THR HG1    H  N N 465 
THR HG21   H  N N 466 
THR HG22   H  N N 467 
THR HG23   H  N N 468 
THR HXT    H  N N 469 
TRP N      N  N N 470 
TRP CA     C  N S 471 
TRP C      C  N N 472 
TRP O      O  N N 473 
TRP CB     C  N N 474 
TRP CG     C  Y N 475 
TRP CD1    C  Y N 476 
TRP CD2    C  Y N 477 
TRP NE1    N  Y N 478 
TRP CE2    C  Y N 479 
TRP CE3    C  Y N 480 
TRP CZ2    C  Y N 481 
TRP CZ3    C  Y N 482 
TRP CH2    C  Y N 483 
TRP OXT    O  N N 484 
TRP H      H  N N 485 
TRP H2     H  N N 486 
TRP HA     H  N N 487 
TRP HB2    H  N N 488 
TRP HB3    H  N N 489 
TRP HD1    H  N N 490 
TRP HE1    H  N N 491 
TRP HE3    H  N N 492 
TRP HZ2    H  N N 493 
TRP HZ3    H  N N 494 
TRP HH2    H  N N 495 
TRP HXT    H  N N 496 
TYR N      N  N N 497 
TYR CA     C  N S 498 
TYR C      C  N N 499 
TYR O      O  N N 500 
TYR CB     C  N N 501 
TYR CG     C  Y N 502 
TYR CD1    C  Y N 503 
TYR CD2    C  Y N 504 
TYR CE1    C  Y N 505 
TYR CE2    C  Y N 506 
TYR CZ     C  Y N 507 
TYR OH     O  N N 508 
TYR OXT    O  N N 509 
TYR H      H  N N 510 
TYR H2     H  N N 511 
TYR HA     H  N N 512 
TYR HB2    H  N N 513 
TYR HB3    H  N N 514 
TYR HD1    H  N N 515 
TYR HD2    H  N N 516 
TYR HE1    H  N N 517 
TYR HE2    H  N N 518 
TYR HH     H  N N 519 
TYR HXT    H  N N 520 
VAL N      N  N N 521 
VAL CA     C  N S 522 
VAL C      C  N N 523 
VAL O      O  N N 524 
VAL CB     C  N N 525 
VAL CG1    C  N N 526 
VAL CG2    C  N N 527 
VAL OXT    O  N N 528 
VAL H      H  N N 529 
VAL H2     H  N N 530 
VAL HA     H  N N 531 
VAL HB     H  N N 532 
VAL HG11   H  N N 533 
VAL HG12   H  N N 534 
VAL HG13   H  N N 535 
VAL HG21   H  N N 536 
VAL HG22   H  N N 537 
VAL HG23   H  N N 538 
VAL HXT    H  N N 539 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
BOG C1    O1     sing N N 70  
BOG C1    C2     sing N N 71  
BOG C1    O5     sing N N 72  
BOG C1    H1     sing N N 73  
BOG O1    "C1'"  sing N N 74  
BOG C2    O2     sing N N 75  
BOG C2    C3     sing N N 76  
BOG C2    H2     sing N N 77  
BOG O2    HO2    sing N N 78  
BOG C3    O3     sing N N 79  
BOG C3    C4     sing N N 80  
BOG C3    H3     sing N N 81  
BOG O3    HO3    sing N N 82  
BOG C4    O4     sing N N 83  
BOG C4    C5     sing N N 84  
BOG C4    H4     sing N N 85  
BOG O4    HO4    sing N N 86  
BOG C5    O5     sing N N 87  
BOG C5    C6     sing N N 88  
BOG C5    H5     sing N N 89  
BOG C6    O6     sing N N 90  
BOG C6    H61    sing N N 91  
BOG C6    H62    sing N N 92  
BOG O6    HO6    sing N N 93  
BOG "C1'" "C2'"  sing N N 94  
BOG "C1'" "H1'1" sing N N 95  
BOG "C1'" "H1'2" sing N N 96  
BOG "C2'" "C3'"  sing N N 97  
BOG "C2'" "H2'1" sing N N 98  
BOG "C2'" "H2'2" sing N N 99  
BOG "C3'" "C4'"  sing N N 100 
BOG "C3'" "H3'1" sing N N 101 
BOG "C3'" "H3'2" sing N N 102 
BOG "C4'" "C5'"  sing N N 103 
BOG "C4'" "H4'1" sing N N 104 
BOG "C4'" "H4'2" sing N N 105 
BOG "C5'" "C6'"  sing N N 106 
BOG "C5'" "H5'1" sing N N 107 
BOG "C5'" "H5'2" sing N N 108 
BOG "C6'" "C7'"  sing N N 109 
BOG "C6'" "H6'1" sing N N 110 
BOG "C6'" "H6'2" sing N N 111 
BOG "C7'" "C8'"  sing N N 112 
BOG "C7'" "H7'1" sing N N 113 
BOG "C7'" "H7'2" sing N N 114 
BOG "C8'" "H8'1" sing N N 115 
BOG "C8'" "H8'2" sing N N 116 
BOG "C8'" "H8'3" sing N N 117 
GLN N     CA     sing N N 118 
GLN N     H      sing N N 119 
GLN N     H2     sing N N 120 
GLN CA    C      sing N N 121 
GLN CA    CB     sing N N 122 
GLN CA    HA     sing N N 123 
GLN C     O      doub N N 124 
GLN C     OXT    sing N N 125 
GLN CB    CG     sing N N 126 
GLN CB    HB2    sing N N 127 
GLN CB    HB3    sing N N 128 
GLN CG    CD     sing N N 129 
GLN CG    HG2    sing N N 130 
GLN CG    HG3    sing N N 131 
GLN CD    OE1    doub N N 132 
GLN CD    NE2    sing N N 133 
GLN NE2   HE21   sing N N 134 
GLN NE2   HE22   sing N N 135 
GLN OXT   HXT    sing N N 136 
GLU N     CA     sing N N 137 
GLU N     H      sing N N 138 
GLU N     H2     sing N N 139 
GLU CA    C      sing N N 140 
GLU CA    CB     sing N N 141 
GLU CA    HA     sing N N 142 
GLU C     O      doub N N 143 
GLU C     OXT    sing N N 144 
GLU CB    CG     sing N N 145 
GLU CB    HB2    sing N N 146 
GLU CB    HB3    sing N N 147 
GLU CG    CD     sing N N 148 
GLU CG    HG2    sing N N 149 
GLU CG    HG3    sing N N 150 
GLU CD    OE1    doub N N 151 
GLU CD    OE2    sing N N 152 
GLU OE2   HE2    sing N N 153 
GLU OXT   HXT    sing N N 154 
GLY N     CA     sing N N 155 
GLY N     H      sing N N 156 
GLY N     H2     sing N N 157 
GLY CA    C      sing N N 158 
GLY CA    HA2    sing N N 159 
GLY CA    HA3    sing N N 160 
GLY C     O      doub N N 161 
GLY C     OXT    sing N N 162 
GLY OXT   HXT    sing N N 163 
HIS N     CA     sing N N 164 
HIS N     H      sing N N 165 
HIS N     H2     sing N N 166 
HIS CA    C      sing N N 167 
HIS CA    CB     sing N N 168 
HIS CA    HA     sing N N 169 
HIS C     O      doub N N 170 
HIS C     OXT    sing N N 171 
HIS CB    CG     sing N N 172 
HIS CB    HB2    sing N N 173 
HIS CB    HB3    sing N N 174 
HIS CG    ND1    sing Y N 175 
HIS CG    CD2    doub Y N 176 
HIS ND1   CE1    doub Y N 177 
HIS ND1   HD1    sing N N 178 
HIS CD2   NE2    sing Y N 179 
HIS CD2   HD2    sing N N 180 
HIS CE1   NE2    sing Y N 181 
HIS CE1   HE1    sing N N 182 
HIS NE2   HE2    sing N N 183 
HIS OXT   HXT    sing N N 184 
HOH O     H1     sing N N 185 
HOH O     H2     sing N N 186 
ILE N     CA     sing N N 187 
ILE N     H      sing N N 188 
ILE N     H2     sing N N 189 
ILE CA    C      sing N N 190 
ILE CA    CB     sing N N 191 
ILE CA    HA     sing N N 192 
ILE C     O      doub N N 193 
ILE C     OXT    sing N N 194 
ILE CB    CG1    sing N N 195 
ILE CB    CG2    sing N N 196 
ILE CB    HB     sing N N 197 
ILE CG1   CD1    sing N N 198 
ILE CG1   HG12   sing N N 199 
ILE CG1   HG13   sing N N 200 
ILE CG2   HG21   sing N N 201 
ILE CG2   HG22   sing N N 202 
ILE CG2   HG23   sing N N 203 
ILE CD1   HD11   sing N N 204 
ILE CD1   HD12   sing N N 205 
ILE CD1   HD13   sing N N 206 
ILE OXT   HXT    sing N N 207 
LEU N     CA     sing N N 208 
LEU N     H      sing N N 209 
LEU N     H2     sing N N 210 
LEU CA    C      sing N N 211 
LEU CA    CB     sing N N 212 
LEU CA    HA     sing N N 213 
LEU C     O      doub N N 214 
LEU C     OXT    sing N N 215 
LEU CB    CG     sing N N 216 
LEU CB    HB2    sing N N 217 
LEU CB    HB3    sing N N 218 
LEU CG    CD1    sing N N 219 
LEU CG    CD2    sing N N 220 
LEU CG    HG     sing N N 221 
LEU CD1   HD11   sing N N 222 
LEU CD1   HD12   sing N N 223 
LEU CD1   HD13   sing N N 224 
LEU CD2   HD21   sing N N 225 
LEU CD2   HD22   sing N N 226 
LEU CD2   HD23   sing N N 227 
LEU OXT   HXT    sing N N 228 
LYS N     CA     sing N N 229 
LYS N     H      sing N N 230 
LYS N     H2     sing N N 231 
LYS CA    C      sing N N 232 
LYS CA    CB     sing N N 233 
LYS CA    HA     sing N N 234 
LYS C     O      doub N N 235 
LYS C     OXT    sing N N 236 
LYS CB    CG     sing N N 237 
LYS CB    HB2    sing N N 238 
LYS CB    HB3    sing N N 239 
LYS CG    CD     sing N N 240 
LYS CG    HG2    sing N N 241 
LYS CG    HG3    sing N N 242 
LYS CD    CE     sing N N 243 
LYS CD    HD2    sing N N 244 
LYS CD    HD3    sing N N 245 
LYS CE    NZ     sing N N 246 
LYS CE    HE2    sing N N 247 
LYS CE    HE3    sing N N 248 
LYS NZ    HZ1    sing N N 249 
LYS NZ    HZ2    sing N N 250 
LYS NZ    HZ3    sing N N 251 
LYS OXT   HXT    sing N N 252 
MET N     CA     sing N N 253 
MET N     H      sing N N 254 
MET N     H2     sing N N 255 
MET CA    C      sing N N 256 
MET CA    CB     sing N N 257 
MET CA    HA     sing N N 258 
MET C     O      doub N N 259 
MET C     OXT    sing N N 260 
MET CB    CG     sing N N 261 
MET CB    HB2    sing N N 262 
MET CB    HB3    sing N N 263 
MET CG    SD     sing N N 264 
MET CG    HG2    sing N N 265 
MET CG    HG3    sing N N 266 
MET SD    CE     sing N N 267 
MET CE    HE1    sing N N 268 
MET CE    HE2    sing N N 269 
MET CE    HE3    sing N N 270 
MET OXT   HXT    sing N N 271 
MPG C2    C3     sing N N 272 
MPG C2    C1     sing N N 273 
MPG C3    C4     sing N N 274 
MPG C4    C5     sing N N 275 
MPG C5    C6     sing N N 276 
MPG C6    C7     sing N N 277 
MPG C7    C8     sing N N 278 
MPG C8    C9     sing N N 279 
MPG C9    C10    doub N Z 280 
MPG C10   C11    sing N N 281 
MPG C11   C12    sing N N 282 
MPG C12   C13    sing N N 283 
MPG C13   C14    sing N N 284 
MPG C14   C15    sing N N 285 
MPG C15   C16    sing N N 286 
MPG C16   C17    sing N N 287 
MPG C17   C18    sing N N 288 
MPG O1    C1     sing N N 289 
MPG O1    CX3    sing N N 290 
MPG CXD   O2     sing N N 291 
MPG CXD   C21    sing N N 292 
MPG CXD   CX3    sing N N 293 
MPG C21   O3     sing N N 294 
MPG C2    H21C   sing N N 295 
MPG C2    H22C   sing N N 296 
MPG C3    H31C   sing N N 297 
MPG C3    H32C   sing N N 298 
MPG CX3   O4     doub N N 299 
MPG C4    H41C   sing N N 300 
MPG C4    H42C   sing N N 301 
MPG C5    H51C   sing N N 302 
MPG C5    H52C   sing N N 303 
MPG C6    H61C   sing N N 304 
MPG C6    H62C   sing N N 305 
MPG C7    H71C   sing N N 306 
MPG C7    H72C   sing N N 307 
MPG C8    H81C   sing N N 308 
MPG C8    H82C   sing N N 309 
MPG C9    H9     sing N N 310 
MPG C10   H10    sing N N 311 
MPG C11   H111   sing N N 312 
MPG C11   H112   sing N N 313 
MPG C12   H121   sing N N 314 
MPG C12   H122   sing N N 315 
MPG C13   H131   sing N N 316 
MPG C13   H132   sing N N 317 
MPG C14   H141   sing N N 318 
MPG C14   H142   sing N N 319 
MPG C15   H151   sing N N 320 
MPG C15   H152   sing N N 321 
MPG C16   H161   sing N N 322 
MPG C16   H162   sing N N 323 
MPG C17   H171   sing N N 324 
MPG C17   H172   sing N N 325 
MPG C18   H181   sing N N 326 
MPG C18   H182   sing N N 327 
MPG C18   H183   sing N N 328 
MPG C1    HX31   sing N N 329 
MPG C1    HX32   sing N N 330 
MPG CXD   HXD    sing N N 331 
MPG O2    H2     sing N N 332 
MPG C21   H211   sing N N 333 
MPG C21   H212   sing N N 334 
MPG O3    H3     sing N N 335 
PHE N     CA     sing N N 336 
PHE N     H      sing N N 337 
PHE N     H2     sing N N 338 
PHE CA    C      sing N N 339 
PHE CA    CB     sing N N 340 
PHE CA    HA     sing N N 341 
PHE C     O      doub N N 342 
PHE C     OXT    sing N N 343 
PHE CB    CG     sing N N 344 
PHE CB    HB2    sing N N 345 
PHE CB    HB3    sing N N 346 
PHE CG    CD1    doub Y N 347 
PHE CG    CD2    sing Y N 348 
PHE CD1   CE1    sing Y N 349 
PHE CD1   HD1    sing N N 350 
PHE CD2   CE2    doub Y N 351 
PHE CD2   HD2    sing N N 352 
PHE CE1   CZ     doub Y N 353 
PHE CE1   HE1    sing N N 354 
PHE CE2   CZ     sing Y N 355 
PHE CE2   HE2    sing N N 356 
PHE CZ    HZ     sing N N 357 
PHE OXT   HXT    sing N N 358 
PRO N     CA     sing N N 359 
PRO N     CD     sing N N 360 
PRO N     H      sing N N 361 
PRO CA    C      sing N N 362 
PRO CA    CB     sing N N 363 
PRO CA    HA     sing N N 364 
PRO C     O      doub N N 365 
PRO C     OXT    sing N N 366 
PRO CB    CG     sing N N 367 
PRO CB    HB2    sing N N 368 
PRO CB    HB3    sing N N 369 
PRO CG    CD     sing N N 370 
PRO CG    HG2    sing N N 371 
PRO CG    HG3    sing N N 372 
PRO CD    HD2    sing N N 373 
PRO CD    HD3    sing N N 374 
PRO OXT   HXT    sing N N 375 
RET C1    C2     sing N N 376 
RET C1    C6     sing N N 377 
RET C1    C16    sing N N 378 
RET C1    C17    sing N N 379 
RET C2    C3     sing N N 380 
RET C2    H21    sing N N 381 
RET C2    H22    sing N N 382 
RET C3    C4     sing N N 383 
RET C3    H31    sing N N 384 
RET C3    H32    sing N N 385 
RET C4    C5     sing N N 386 
RET C4    H41    sing N N 387 
RET C4    H42    sing N N 388 
RET C5    C6     doub N N 389 
RET C5    C18    sing N N 390 
RET C6    C7     sing N N 391 
RET C7    C8     doub N E 392 
RET C7    H7     sing N N 393 
RET C8    C9     sing N N 394 
RET C8    H8     sing N N 395 
RET C9    C10    doub N E 396 
RET C9    C19    sing N N 397 
RET C10   C11    sing N N 398 
RET C10   H10    sing N N 399 
RET C11   C12    doub N E 400 
RET C11   H11    sing N N 401 
RET C12   C13    sing N N 402 
RET C12   H12    sing N N 403 
RET C13   C14    doub N E 404 
RET C13   C20    sing N N 405 
RET C14   C15    sing N N 406 
RET C14   H14    sing N N 407 
RET C15   O1     doub N N 408 
RET C15   H15    sing N N 409 
RET C16   H161   sing N N 410 
RET C16   H162   sing N N 411 
RET C16   H163   sing N N 412 
RET C17   H171   sing N N 413 
RET C17   H172   sing N N 414 
RET C17   H173   sing N N 415 
RET C18   H181   sing N N 416 
RET C18   H182   sing N N 417 
RET C18   H183   sing N N 418 
RET C19   H191   sing N N 419 
RET C19   H192   sing N N 420 
RET C19   H193   sing N N 421 
RET C20   H201   sing N N 422 
RET C20   H202   sing N N 423 
RET C20   H203   sing N N 424 
SER N     CA     sing N N 425 
SER N     H      sing N N 426 
SER N     H2     sing N N 427 
SER CA    C      sing N N 428 
SER CA    CB     sing N N 429 
SER CA    HA     sing N N 430 
SER C     O      doub N N 431 
SER C     OXT    sing N N 432 
SER CB    OG     sing N N 433 
SER CB    HB2    sing N N 434 
SER CB    HB3    sing N N 435 
SER OG    HG     sing N N 436 
SER OXT   HXT    sing N N 437 
THR N     CA     sing N N 438 
THR N     H      sing N N 439 
THR N     H2     sing N N 440 
THR CA    C      sing N N 441 
THR CA    CB     sing N N 442 
THR CA    HA     sing N N 443 
THR C     O      doub N N 444 
THR C     OXT    sing N N 445 
THR CB    OG1    sing N N 446 
THR CB    CG2    sing N N 447 
THR CB    HB     sing N N 448 
THR OG1   HG1    sing N N 449 
THR CG2   HG21   sing N N 450 
THR CG2   HG22   sing N N 451 
THR CG2   HG23   sing N N 452 
THR OXT   HXT    sing N N 453 
TRP N     CA     sing N N 454 
TRP N     H      sing N N 455 
TRP N     H2     sing N N 456 
TRP CA    C      sing N N 457 
TRP CA    CB     sing N N 458 
TRP CA    HA     sing N N 459 
TRP C     O      doub N N 460 
TRP C     OXT    sing N N 461 
TRP CB    CG     sing N N 462 
TRP CB    HB2    sing N N 463 
TRP CB    HB3    sing N N 464 
TRP CG    CD1    doub Y N 465 
TRP CG    CD2    sing Y N 466 
TRP CD1   NE1    sing Y N 467 
TRP CD1   HD1    sing N N 468 
TRP CD2   CE2    doub Y N 469 
TRP CD2   CE3    sing Y N 470 
TRP NE1   CE2    sing Y N 471 
TRP NE1   HE1    sing N N 472 
TRP CE2   CZ2    sing Y N 473 
TRP CE3   CZ3    doub Y N 474 
TRP CE3   HE3    sing N N 475 
TRP CZ2   CH2    doub Y N 476 
TRP CZ2   HZ2    sing N N 477 
TRP CZ3   CH2    sing Y N 478 
TRP CZ3   HZ3    sing N N 479 
TRP CH2   HH2    sing N N 480 
TRP OXT   HXT    sing N N 481 
TYR N     CA     sing N N 482 
TYR N     H      sing N N 483 
TYR N     H2     sing N N 484 
TYR CA    C      sing N N 485 
TYR CA    CB     sing N N 486 
TYR CA    HA     sing N N 487 
TYR C     O      doub N N 488 
TYR C     OXT    sing N N 489 
TYR CB    CG     sing N N 490 
TYR CB    HB2    sing N N 491 
TYR CB    HB3    sing N N 492 
TYR CG    CD1    doub Y N 493 
TYR CG    CD2    sing Y N 494 
TYR CD1   CE1    sing Y N 495 
TYR CD1   HD1    sing N N 496 
TYR CD2   CE2    doub Y N 497 
TYR CD2   HD2    sing N N 498 
TYR CE1   CZ     doub Y N 499 
TYR CE1   HE1    sing N N 500 
TYR CE2   CZ     sing Y N 501 
TYR CE2   HE2    sing N N 502 
TYR CZ    OH     sing N N 503 
TYR OH    HH     sing N N 504 
TYR OXT   HXT    sing N N 505 
VAL N     CA     sing N N 506 
VAL N     H      sing N N 507 
VAL N     H2     sing N N 508 
VAL CA    C      sing N N 509 
VAL CA    CB     sing N N 510 
VAL CA    HA     sing N N 511 
VAL C     O      doub N N 512 
VAL C     OXT    sing N N 513 
VAL CB    CG1    sing N N 514 
VAL CB    CG2    sing N N 515 
VAL CB    HB     sing N N 516 
VAL CG1   HG11   sing N N 517 
VAL CG1   HG12   sing N N 518 
VAL CG1   HG13   sing N N 519 
VAL CG2   HG21   sing N N 520 
VAL CG2   HG22   sing N N 521 
VAL CG2   HG23   sing N N 522 
VAL OXT   HXT    sing N N 523 
# 
_pdbx_audit_support.funding_organization   'H2020 Marie Curie Actions of the European Commission' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           637295 
_pdbx_audit_support.ordinal                1 
# 
_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   1h68 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   ? 
_pdbx_serial_crystallography_sample_delivery.method        injection 
# 
_space_group.name_H-M_alt     'C 2 2 21' 
_space_group.name_Hall        'C 2c 2' 
_space_group.IT_number        20 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9H1W 
_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]   0.011142 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007590 
_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]   0.019608 
_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.
;
? 
H  ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . MET A 1 1   ? 36.43100 16.11900 -15.10700 1.000 174.28000 ? 1   MET A N     1 
ATOM   2    C  CA    . MET A 1 1   ? 37.15900 17.12800 -15.92900 1.000 163.81000 ? 1   MET A CA    1 
ATOM   3    C  C     . MET A 1 1   ? 37.52400 18.34400 -15.08500 1.000 142.22000 ? 1   MET A C     1 
ATOM   4    O  O     . MET A 1 1   ? 38.55600 18.97800 -15.30900 1.000 133.77000 ? 1   MET A O     1 
ATOM   5    C  CB    . MET A 1 1   ? 36.31100 17.55600 -17.12800 1.000 163.38000 ? 1   MET A CB    1 
ATOM   6    C  CG    . MET A 1 1   ? 37.00000 18.54700 -18.05600 1.000 163.62000 ? 1   MET A CG    1 
ATOM   7    S  SD    . MET A 1 1   ? 35.90600 19.16400 -19.35300 1.000 165.15000 ? 1   MET A SD    1 
ATOM   8    C  CE    . MET A 1 1   ? 36.39600 18.13600 -20.73600 1.000 139.62000 ? 1   MET A CE    1 
ATOM   9    N  N     . VAL A 1 2   ? 36.67300 18.66500 -14.11400 1.000 125.50000 ? 2   VAL A N     1 
ATOM   10   C  CA    . VAL A 1 2   ? 36.86000 19.81900 -13.24000 1.000 110.73000 ? 2   VAL A CA    1 
ATOM   11   C  C     . VAL A 1 2   ? 36.66200 19.34700 -11.80400 1.000 102.08000 ? 2   VAL A C     1 
ATOM   12   O  O     . VAL A 1 2   ? 35.53600 19.04000 -11.39200 1.000 100.77000 ? 2   VAL A O     1 
ATOM   13   C  CB    . VAL A 1 2   ? 35.90100 20.97000 -13.58700 1.000 98.68000  ? 2   VAL A CB    1 
ATOM   14   C  CG1   . VAL A 1 2   ? 34.44800 20.57100 -13.35200 1.000 98.53000  ? 2   VAL A CG1   1 
ATOM   15   C  CG2   . VAL A 1 2   ? 36.25700 22.21900 -12.79100 1.000 88.96000  ? 2   VAL A CG2   1 
ATOM   16   N  N     . GLY A 1 3   ? 37.75700 19.27500 -11.04400 1.000 89.68000  ? 3   GLY A N     1 
ATOM   17   C  CA    . GLY A 1 3   ? 37.69000 18.82100 -9.67300  1.000 62.93000  ? 3   GLY A CA    1 
ATOM   18   C  C     . GLY A 1 3   ? 37.58200 19.96500 -8.68400  1.000 52.44000  ? 3   GLY A C     1 
ATOM   19   O  O     . GLY A 1 3   ? 37.78800 21.13100 -9.01600  1.000 45.60000  ? 3   GLY A O     1 
ATOM   20   N  N     . LEU A 1 4   ? 37.24800 19.60600 -7.44400  1.000 50.47000  ? 4   LEU A N     1 
ATOM   21   C  CA    . LEU A 1 4   ? 37.14500 20.60500 -6.38600  1.000 45.32000  ? 4   LEU A CA    1 
ATOM   22   C  C     . LEU A 1 4   ? 38.43400 21.40900 -6.27300  1.000 41.30000  ? 4   LEU A C     1 
ATOM   23   O  O     . LEU A 1 4   ? 38.40400 22.64000 -6.16700  1.000 37.78000  ? 4   LEU A O     1 
ATOM   24   C  CB    . LEU A 1 4   ? 36.82300 19.93000 -5.05400  1.000 44.48000  ? 4   LEU A CB    1 
ATOM   25   C  CG    . LEU A 1 4   ? 35.46900 19.23600 -4.91700  1.000 46.75000  ? 4   LEU A CG    1 
ATOM   26   C  CD1   . LEU A 1 4   ? 35.34200 18.61900 -3.52700  1.000 54.79000  ? 4   LEU A CD1   1 
ATOM   27   C  CD2   . LEU A 1 4   ? 34.33100 20.20000 -5.18300  1.000 48.51000  ? 4   LEU A CD2   1 
ATOM   28   N  N     . THR A 1 5   ? 39.58200 20.72400 -6.29500  1.000 42.15000  ? 5   THR A N     1 
ATOM   29   C  CA    . THR A 1 5   ? 40.85400 21.41500 -6.11200  1.000 41.00000  ? 5   THR A CA    1 
ATOM   30   C  C     . THR A 1 5   ? 41.08800 22.43300 -7.22100  1.000 36.32000  ? 5   THR A C     1 
ATOM   31   O  O     . THR A 1 5   ? 41.60300 23.52800 -6.96800  1.000 39.09000  ? 5   THR A O     1 
ATOM   32   C  CB    . THR A 1 5   ? 42.00900 20.41300 -6.06100  1.000 47.85000  ? 5   THR A CB    1 
ATOM   33   O  OG1   . THR A 1 5   ? 41.77400 19.35000 -6.99100  1.000 51.17000  ? 5   THR A OG1   1 
ATOM   34   C  CG2   . THR A 1 5   ? 42.15800 19.84100 -4.65900  1.000 47.52000  ? 5   THR A CG2   1 
ATOM   35   N  N     . THR A 1 6   ? 40.72100 22.09000 -8.45800  1.000 34.94000  ? 6   THR A N     1 
ATOM   36   C  CA    . THR A 1 6   ? 40.85700 23.04900 -9.55000  1.000 34.08000  ? 6   THR A CA    1 
ATOM   37   C  C     . THR A 1 6   ? 40.04800 24.30800 -9.26800  1.000 30.05000  ? 6   THR A C     1 
ATOM   38   O  O     . THR A 1 6   ? 40.52600 25.42800 -9.48600  1.000 32.41000  ? 6   THR A O     1 
ATOM   39   C  CB    . THR A 1 6   ? 40.41100 22.42600 -10.87200 1.000 42.35000  ? 6   THR A CB    1 
ATOM   40   O  OG1   . THR A 1 6   ? 41.05600 21.16200 -11.06100 1.000 48.39000  ? 6   THR A OG1   1 
ATOM   41   C  CG2   . THR A 1 6   ? 40.75200 23.35000 -12.03300 1.000 44.22000  ? 6   THR A CG2   1 
ATOM   42   N  N     . LEU A 1 7   ? 38.81700 24.14200 -8.78200  1.000 34.83000  ? 7   LEU A N     1 
ATOM   43   C  CA    . LEU A 1 7   ? 37.98100 25.29700 -8.47800  1.000 34.98000  ? 7   LEU A CA    1 
ATOM   44   C  C     . LEU A 1 7   ? 38.58900 26.13700 -7.36300  1.000 29.09000  ? 7   LEU A C     1 
ATOM   45   O  O     . LEU A 1 7   ? 38.58400 27.37100 -7.43100  1.000 27.10000  ? 7   LEU A O     1 
ATOM   46   C  CB    . LEU A 1 7   ? 36.57600 24.83100 -8.10400  1.000 36.90000  ? 7   LEU A CB    1 
ATOM   47   C  CG    . LEU A 1 7   ? 35.80800 24.21300 -9.27400  1.000 37.12000  ? 7   LEU A CG    1 
ATOM   48   C  CD1   . LEU A 1 7   ? 34.48700 23.61500 -8.82500  1.000 38.82000  ? 7   LEU A CD1   1 
ATOM   49   C  CD2   . LEU A 1 7   ? 35.58400 25.25900 -10.36200 1.000 34.65000  ? 7   LEU A CD2   1 
ATOM   50   N  N     . PHE A 1 8   ? 39.13500 25.48600 -6.33400  1.000 31.89000  ? 8   PHE A N     1 
ATOM   51   C  CA    . PHE A 1 8   ? 39.76500 26.23300 -5.25000  1.000 31.66000  ? 8   PHE A CA    1 
ATOM   52   C  C     . PHE A 1 8   ? 40.97400 27.01600 -5.75700  1.000 33.34000  ? 8   PHE A C     1 
ATOM   53   O  O     . PHE A 1 8   ? 41.16600 28.18000 -5.38400  1.000 32.36000  ? 8   PHE A O     1 
ATOM   54   C  CB    . PHE A 1 8   ? 40.15700 25.28400 -4.11500  1.000 32.03000  ? 8   PHE A CB    1 
ATOM   55   C  CG    . PHE A 1 8   ? 38.97700 24.75100 -3.33100  1.000 33.93000  ? 8   PHE A CG    1 
ATOM   56   C  CD1   . PHE A 1 8   ? 37.90500 25.57000 -3.01100  1.000 30.34000  ? 8   PHE A CD1   1 
ATOM   57   C  CD2   . PHE A 1 8   ? 38.94100 23.42900 -2.91800  1.000 35.86000  ? 8   PHE A CD2   1 
ATOM   58   C  CE1   . PHE A 1 8   ? 36.82200 25.08400 -2.30100  1.000 33.84000  ? 8   PHE A CE1   1 
ATOM   59   C  CE2   . PHE A 1 8   ? 37.86000 22.93600 -2.20300  1.000 36.54000  ? 8   PHE A CE2   1 
ATOM   60   C  CZ    . PHE A 1 8   ? 36.80000 23.76400 -1.89700  1.000 31.65000  ? 8   PHE A CZ    1 
ATOM   61   N  N     . TRP A 1 9   ? 41.79300 26.40900 -6.62100  1.000 38.22000  ? 9   TRP A N     1 
ATOM   62   C  CA    . TRP A 1 9   ? 42.94200 27.13300 -7.16300  1.000 35.79000  ? 9   TRP A CA    1 
ATOM   63   C  C     . TRP A 1 9   ? 42.49100 28.35200 -7.96300  1.000 33.62000  ? 9   TRP A C     1 
ATOM   64   O  O     . TRP A 1 9   ? 43.12100 29.41400 -7.89800  1.000 28.75000  ? 9   TRP A O     1 
ATOM   65   C  CB    . TRP A 1 9   ? 43.79900 26.20500 -8.02900  1.000 41.74000  ? 9   TRP A CB    1 
ATOM   66   C  CG    . TRP A 1 9   ? 44.72000 25.33100 -7.22700  1.000 48.89000  ? 9   TRP A CG    1 
ATOM   67   C  CD1   . TRP A 1 9   ? 44.68900 23.97000 -7.14200  1.000 49.07000  ? 9   TRP A CD1   1 
ATOM   68   C  CD2   . TRP A 1 9   ? 45.80300 25.75900 -6.38700  1.000 51.20000  ? 9   TRP A CD2   1 
ATOM   69   N  NE1   . TRP A 1 9   ? 45.68300 23.52400 -6.30500  1.000 57.13000  ? 9   TRP A NE1   1 
ATOM   70   C  CE2   . TRP A 1 9   ? 46.38200 24.60100 -5.83000  1.000 60.15000  ? 9   TRP A CE2   1 
ATOM   71   C  CE3   . TRP A 1 9   ? 46.33900 27.00700 -6.05600  1.000 51.94000  ? 9   TRP A CE3   1 
ATOM   72   C  CZ2   . TRP A 1 9   ? 47.46800 24.65500 -4.95700  1.000 58.50000  ? 9   TRP A CZ2   1 
ATOM   73   C  CZ3   . TRP A 1 9   ? 47.42000 27.05600 -5.18900  1.000 54.80000  ? 9   TRP A CZ3   1 
ATOM   74   C  CH2   . TRP A 1 9   ? 47.97200 25.88900 -4.65200  1.000 58.05000  ? 9   TRP A CH2   1 
ATOM   75   N  N     . LEU A 1 10  ? 41.39500 28.21600 -8.71400  1.000 32.51000  ? 10  LEU A N     1 
ATOM   76   C  CA    . LEU A 1 10  ? 40.87200 29.34300 -9.47500  1.000 30.09000  ? 10  LEU A CA    1 
ATOM   77   C  C     . LEU A 1 10  ? 40.49600 30.49500 -8.55200  1.000 27.68000  ? 10  LEU A C     1 
ATOM   78   O  O     . LEU A 1 10  ? 40.80500 31.66000 -8.83100  1.000 26.86000  ? 10  LEU A O     1 
ATOM   79   C  CB    . LEU A 1 10  ? 39.65400 28.90600 -10.29000 1.000 34.34000  ? 10  LEU A CB    1 
ATOM   80   C  CG    . LEU A 1 10  ? 39.92600 27.94600 -11.44800 1.000 43.58000  ? 10  LEU A CG    1 
ATOM   81   C  CD1   . LEU A 1 10  ? 38.62700 27.46400 -12.07600 1.000 42.14000  ? 10  LEU A CD1   1 
ATOM   82   C  CD2   . LEU A 1 10  ? 40.80700 28.63300 -12.47800 1.000 53.19000  ? 10  LEU A CD2   1 
ATOM   83   N  N     . GLY A 1 11  ? 39.79700 30.19000 -7.45800  1.000 26.29000  ? 11  GLY A N     1 
ATOM   84   C  CA    . GLY A 1 11  ? 39.48700 31.22200 -6.48700  1.000 26.05000  ? 11  GLY A CA    1 
ATOM   85   C  C     . GLY A 1 11  ? 40.74000 31.83800 -5.90100  1.000 24.73000  ? 11  GLY A C     1 
ATOM   86   O  O     . GLY A 1 11  ? 40.83500 33.05800 -5.75400  1.000 25.49000  ? 11  GLY A O     1 
ATOM   87   N  N     . ALA A 1 12  ? 41.72300 30.99900 -5.56900  1.000 25.29000  ? 12  ALA A N     1 
ATOM   88   C  CA    . ALA A 1 12  ? 42.98900 31.50500 -5.05300  1.000 28.98000  ? 12  ALA A CA    1 
ATOM   89   C  C     . ALA A 1 12  ? 43.61200 32.50400 -6.02100  1.000 26.91000  ? 12  ALA A C     1 
ATOM   90   O  O     . ALA A 1 12  ? 43.99900 33.61000 -5.62600  1.000 29.41000  ? 12  ALA A O     1 
ATOM   91   C  CB    . ALA A 1 12  ? 43.94700 30.34100 -4.78900  1.000 31.87000  ? 12  ALA A CB    1 
ATOM   92   N  N     . ILE A 1 13  ? 43.70700 32.13500 -7.30100  1.000 31.55000  ? 13  ILE A N     1 
ATOM   93   C  CA    . ILE A 1 13  ? 44.33500 33.01300 -8.28500  1.000 30.95000  ? 13  ILE A CA    1 
ATOM   94   C  C     . ILE A 1 13  ? 43.55600 34.31700 -8.40100  1.000 29.00000  ? 13  ILE A C     1 
ATOM   95   O  O     . ILE A 1 13  ? 44.13600 35.40800 -8.43300  1.000 28.36000  ? 13  ILE A O     1 
ATOM   96   C  CB    . ILE A 1 13  ? 44.43900 32.31500 -9.65100  1.000 35.79000  ? 13  ILE A CB    1 
ATOM   97   C  CG1   . ILE A 1 13  ? 45.43300 31.15800 -9.60200  1.000 38.87000  ? 13  ILE A CG1   1 
ATOM   98   C  CG2   . ILE A 1 13  ? 44.84500 33.32100 -10.72300 1.000 38.65000  ? 13  ILE A CG2   1 
ATOM   99   C  CD1   . ILE A 1 13  ? 45.21400 30.14200 -10.71300 1.000 43.11000  ? 13  ILE A CD1   1 
ATOM   100  N  N     . GLY A 1 14  ? 42.22900 34.21600 -8.49200  1.000 29.79000  ? 14  GLY A N     1 
ATOM   101  C  CA    . GLY A 1 14  ? 41.41500 35.41300 -8.59200  1.000 25.81000  ? 14  GLY A CA    1 
ATOM   102  C  C     . GLY A 1 14  ? 41.61000 36.34500 -7.41400  1.000 27.52000  ? 14  GLY A C     1 
ATOM   103  O  O     . GLY A 1 14  ? 41.72300 37.56100 -7.58200  1.000 26.58000  ? 14  GLY A O     1 
ATOM   104  N  N     . MET A 1 15  ? 41.65400 35.79200 -6.20300  1.000 26.88000  ? 15  MET A N     1 
ATOM   105  C  CA    . MET A 1 15  ? 41.86800 36.63000 -5.02800  1.000 29.20000  ? 15  MET A CA    1 
ATOM   106  C  C     . MET A 1 15  ? 43.27300 37.22300 -5.02900  1.000 30.96000  ? 15  MET A C     1 
ATOM   107  O  O     . MET A 1 15  ? 43.46000 38.39100 -4.67100  1.000 27.98000  ? 15  MET A O     1 
ATOM   108  C  CB    . MET A 1 15  ? 41.60300 35.82200 -3.76100  1.000 27.61000  ? 15  MET A CB    1 
ATOM   109  C  CG    . MET A 1 15  ? 40.17100 35.28800 -3.66500  1.000 26.05000  ? 15  MET A CG    1 
ATOM   110  S  SD    . MET A 1 15  ? 38.93300 36.60600 -3.67700  1.000 20.89000  ? 15  MET A SD    1 
ATOM   111  C  CE    . MET A 1 15  ? 37.45400 35.71100 -3.20300  1.000 24.26000  ? 15  MET A CE    1 
ATOM   112  N  N     . LEU A 1 16  ? 44.27000 36.44300 -5.45100  1.000 29.33000  ? 16  LEU A N     1 
ATOM   113  C  CA    . LEU A 1 16  ? 45.63500 36.95400 -5.51400  1.000 34.24000  ? 16  LEU A CA    1 
ATOM   114  C  C     . LEU A 1 16  ? 45.72300 38.16800 -6.43100  1.000 33.19000  ? 16  LEU A C     1 
ATOM   115  O  O     . LEU A 1 16  ? 46.28300 39.20600 -6.05700  1.000 32.50000  ? 16  LEU A O     1 
ATOM   116  C  CB    . LEU A 1 16  ? 46.58400 35.85500 -5.98900  1.000 47.57000  ? 16  LEU A CB    1 
ATOM   117  C  CG    . LEU A 1 16  ? 47.48000 35.23800 -4.91600  1.000 65.87000  ? 16  LEU A CG    1 
ATOM   118  C  CD1   . LEU A 1 16  ? 48.36800 34.14100 -5.49200  1.000 66.87000  ? 16  LEU A CD1   1 
ATOM   119  C  CD2   . LEU A 1 16  ? 48.32900 36.31700 -4.25400  1.000 77.46000  ? 16  LEU A CD2   1 
ATOM   120  N  N     . VAL A 1 17  ? 45.16600 38.05700 -7.64100  1.000 33.79000  ? 17  VAL A N     1 
ATOM   121  C  CA    . VAL A 1 17  ? 45.22300 39.16500 -8.59200  1.000 38.59000  ? 17  VAL A CA    1 
ATOM   122  C  C     . VAL A 1 17  ? 44.55200 40.39800 -8.00500  1.000 37.73000  ? 17  VAL A C     1 
ATOM   123  O  O     . VAL A 1 17  ? 45.07400 41.51600 -8.09500  1.000 35.85000  ? 17  VAL A O     1 
ATOM   124  C  CB    . VAL A 1 17  ? 44.57500 38.75800 -9.92700  1.000 38.92000  ? 17  VAL A CB    1 
ATOM   125  C  CG1   . VAL A 1 17  ? 44.40800 39.97200 -10.82700 1.000 36.19000  ? 17  VAL A CG1   1 
ATOM   126  C  CG2   . VAL A 1 17  ? 45.40400 37.68200 -10.61500 1.000 38.96000  ? 17  VAL A CG2   1 
ATOM   127  N  N     . GLY A 1 18  ? 43.37500 40.21700 -7.40700  1.000 35.68000  ? 18  GLY A N     1 
ATOM   128  C  CA    . GLY A 1 18  ? 42.73000 41.33300 -6.73900  1.000 32.86000  ? 18  GLY A CA    1 
ATOM   129  C  C     . GLY A 1 18  ? 43.61600 41.94400 -5.67300  1.000 34.27000  ? 18  GLY A C     1 
ATOM   130  O  O     . GLY A 1 18  ? 43.76700 43.16600 -5.59600  1.000 32.27000  ? 18  GLY A O     1 
ATOM   131  N  N     . THR A 1 19  ? 44.23400 41.09500 -4.84700  1.000 40.43000  ? 19  THR A N     1 
ATOM   132  C  CA    . THR A 1 19  ? 45.07000 41.58800 -3.75800  1.000 41.99000  ? 19  THR A CA    1 
ATOM   133  C  C     . THR A 1 19  ? 46.19000 42.48000 -4.28000  1.000 40.97000  ? 19  THR A C     1 
ATOM   134  O  O     . THR A 1 19  ? 46.38000 43.60500 -3.80300  1.000 40.09000  ? 19  THR A O     1 
ATOM   135  C  CB    . THR A 1 19  ? 45.64900 40.41000 -2.96900  1.000 41.96000  ? 19  THR A CB    1 
ATOM   136  O  OG1   . THR A 1 19  ? 44.58700 39.65200 -2.37700  1.000 42.47000  ? 19  THR A OG1   1 
ATOM   137  C  CG2   . THR A 1 19  ? 46.59000 40.91000 -1.88400  1.000 38.54000  ? 19  THR A CG2   1 
ATOM   138  N  N     . LEU A 1 20  ? 46.95200 41.98700 -5.25600  1.000 41.50000  ? 20  LEU A N     1 
ATOM   139  C  CA    . LEU A 1 20  ? 48.05600 42.77500 -5.79400  1.000 43.35000  ? 20  LEU A CA    1 
ATOM   140  C  C     . LEU A 1 20  ? 47.55100 44.06700 -6.42400  1.000 43.76000  ? 20  LEU A C     1 
ATOM   141  O  O     . LEU A 1 20  ? 48.17200 45.12500 -6.27000  1.000 48.65000  ? 20  LEU A O     1 
ATOM   142  C  CB    . LEU A 1 20  ? 48.83700 41.95100 -6.81700  1.000 47.71000  ? 20  LEU A CB    1 
ATOM   143  C  CG    . LEU A 1 20  ? 49.42400 40.64300 -6.28200  1.000 52.00000  ? 20  LEU A CG    1 
ATOM   144  C  CD1   . LEU A 1 20  ? 50.13100 39.87900 -7.38700  1.000 51.05000  ? 20  LEU A CD1   1 
ATOM   145  C  CD2   . LEU A 1 20  ? 50.37000 40.91400 -5.12000  1.000 56.75000  ? 20  LEU A CD2   1 
ATOM   146  N  N     . ALA A 1 21  ? 46.42500 44.00100 -7.13700  1.000 43.21000  ? 21  ALA A N     1 
ATOM   147  C  CA    . ALA A 1 21  ? 45.87600 45.20400 -7.75400  1.000 43.21000  ? 21  ALA A CA    1 
ATOM   148  C  C     . ALA A 1 21  ? 45.53600 46.25200 -6.70200  1.000 44.21000  ? 21  ALA A C     1 
ATOM   149  O  O     . ALA A 1 21  ? 45.85600 47.43600 -6.86200  1.000 44.62000  ? 21  ALA A O     1 
ATOM   150  C  CB    . ALA A 1 21  ? 44.63800 44.84700 -8.58000  1.000 38.03000  ? 21  ALA A CB    1 
ATOM   151  N  N     . PHE A 1 22  ? 44.88800 45.83500 -5.61200  1.000 45.86000  ? 22  PHE A N     1 
ATOM   152  C  CA    . PHE A 1 22  ? 44.51200 46.79500 -4.58000  1.000 44.22000  ? 22  PHE A CA    1 
ATOM   153  C  C     . PHE A 1 22  ? 45.74500 47.35300 -3.87600  1.000 47.45000  ? 22  PHE A C     1 
ATOM   154  O  O     . PHE A 1 22  ? 45.82100 48.55800 -3.60700  1.000 49.69000  ? 22  PHE A O     1 
ATOM   155  C  CB    . PHE A 1 22  ? 43.55500 46.15200 -3.57100  1.000 40.66000  ? 22  PHE A CB    1 
ATOM   156  C  CG    . PHE A 1 22  ? 42.33500 45.52700 -4.20000  1.000 38.14000  ? 22  PHE A CG    1 
ATOM   157  C  CD1   . PHE A 1 22  ? 41.67400 46.15900 -5.24000  1.000 36.19000  ? 22  PHE A CD1   1 
ATOM   158  C  CD2   . PHE A 1 22  ? 41.85400 44.30800 -3.75000  1.000 36.05000  ? 22  PHE A CD2   1 
ATOM   159  C  CE1   . PHE A 1 22  ? 40.55900 45.58400 -5.82600  1.000 39.28000  ? 22  PHE A CE1   1 
ATOM   160  C  CE2   . PHE A 1 22  ? 40.73900 43.72600 -4.33200  1.000 36.49000  ? 22  PHE A CE2   1 
ATOM   161  C  CZ    . PHE A 1 22  ? 40.09200 44.36400 -5.37200  1.000 36.70000  ? 22  PHE A CZ    1 
ATOM   162  N  N     . ALA A 1 23  ? 46.72900 46.49800 -3.57900  1.000 52.78000  ? 23  ALA A N     1 
ATOM   163  C  CA    . ALA A 1 23  ? 47.93700 46.97100 -2.91100  1.000 58.75000  ? 23  ALA A CA    1 
ATOM   164  C  C     . ALA A 1 23  ? 48.66100 48.00900 -3.75800  1.000 64.25000  ? 23  ALA A C     1 
ATOM   165  O  O     . ALA A 1 23  ? 49.13600 49.02600 -3.23800  1.000 68.25000  ? 23  ALA A O     1 
ATOM   166  C  CB    . ALA A 1 23  ? 48.86400 45.79600 -2.60100  1.000 66.69000  ? 23  ALA A CB    1 
ATOM   167  N  N     . TRP A 1 24  ? 48.75500 47.77000 -5.06500  1.000 61.51000  ? 24  TRP A N     1 
ATOM   168  C  CA    . TRP A 1 24  ? 49.41000 48.73100 -5.94200  1.000 71.71000  ? 24  TRP A CA    1 
ATOM   169  C  C     . TRP A 1 24  ? 48.68700 50.07100 -5.91900  1.000 73.05000  ? 24  TRP A C     1 
ATOM   170  O  O     . TRP A 1 24  ? 49.30100 51.11900 -5.68000  1.000 81.70000  ? 24  TRP A O     1 
ATOM   171  C  CB    . TRP A 1 24  ? 49.48100 48.18400 -7.36900  1.000 77.06000  ? 24  TRP A CB    1 
ATOM   172  C  CG    . TRP A 1 24  ? 50.53000 48.87000 -8.17000  1.000 87.53000  ? 24  TRP A CG    1 
ATOM   173  C  CD1   . TRP A 1 24  ? 50.34700 49.86900 -9.08000  1.000 89.33000  ? 24  TRP A CD1   1 
ATOM   174  C  CD2   . TRP A 1 24  ? 51.93800 48.62700 -8.11600  1.000 91.90000  ? 24  TRP A CD2   1 
ATOM   175  N  NE1   . TRP A 1 24  ? 51.55700 50.26000 -9.60100  1.000 90.13000  ? 24  TRP A NE1   1 
ATOM   176  C  CE2   . TRP A 1 24  ? 52.54900 49.50800 -9.03000  1.000 96.37000  ? 24  TRP A CE2   1 
ATOM   177  C  CE3   . TRP A 1 24  ? 52.74200 47.74600 -7.38500  1.000 92.51000  ? 24  TRP A CE3   1 
ATOM   178  C  CZ2   . TRP A 1 24  ? 53.92700 49.54200 -9.22400  1.000 97.09000  ? 24  TRP A CZ2   1 
ATOM   179  C  CZ3   . TRP A 1 24  ? 54.11000 47.77400 -7.58900  1.000 100.02000 ? 24  TRP A CZ3   1 
ATOM   180  C  CH2   . TRP A 1 24  ? 54.68900 48.66400 -8.50000  1.000 100.94000 ? 24  TRP A CH2   1 
ATOM   181  N  N     . ALA A 1 25  ? 47.37200 50.06000 -6.15800  1.000 64.31000  ? 25  ALA A N     1 
ATOM   182  C  CA    . ALA A 1 25  ? 46.61300 51.30200 -6.18900  1.000 61.89000  ? 25  ALA A CA    1 
ATOM   183  C  C     . ALA A 1 25  ? 46.72900 52.08500 -4.88900  1.000 65.69000  ? 25  ALA A C     1 
ATOM   184  O  O     . ALA A 1 25  ? 46.44800 53.28700 -4.87600  1.000 68.01000  ? 25  ALA A O     1 
ATOM   185  C  CB    . ALA A 1 25  ? 45.14100 51.01100 -6.48700  1.000 61.24000  ? 25  ALA A CB    1 
ATOM   186  N  N     . GLY A 1 26  ? 47.13500 51.43600 -3.80100  1.000 67.29000  ? 26  GLY A N     1 
ATOM   187  C  CA    . GLY A 1 26  ? 47.35300 52.09600 -2.53600  1.000 77.09000  ? 26  GLY A CA    1 
ATOM   188  C  C     . GLY A 1 26  ? 48.79600 52.44700 -2.24500  1.000 88.87000  ? 26  GLY A C     1 
ATOM   189  O  O     . GLY A 1 26  ? 49.09500 52.86200 -1.12000  1.000 93.12000  ? 26  GLY A O     1 
ATOM   190  N  N     . ARG A 1 27  ? 49.69600 52.29000 -3.21800  1.000 98.50000  ? 27  ARG A N     1 
ATOM   191  C  CA    . ARG A 1 27  ? 51.11900 52.55800 -3.04200  1.000 113.71000 ? 27  ARG A CA    1 
ATOM   192  C  C     . ARG A 1 27  ? 51.35900 53.77300 -2.15700  1.000 125.83000 ? 27  ARG A C     1 
ATOM   193  O  O     . ARG A 1 27  ? 51.79400 53.64300 -1.00900  1.000 126.59000 ? 27  ARG A O     1 
ATOM   194  C  CB    . ARG A 1 27  ? 51.78700 52.77600 -4.40200  1.000 120.08000 ? 27  ARG A CB    1 
ATOM   195  C  CG    . ARG A 1 27  ? 52.21100 51.50700 -5.10600  1.000 147.46000 ? 27  ARG A CG    1 
ATOM   196  C  CD    . ARG A 1 27  ? 52.15800 51.64900 -6.62600  1.000 168.33000 ? 27  ARG A CD    1 
ATOM   197  N  NE    . ARG A 1 27  ? 52.14600 53.03400 -7.09600  1.000 178.52000 ? 27  ARG A NE    1 
ATOM   198  C  CZ    . ARG A 1 27  ? 53.20200 53.84300 -7.08400  1.000 184.00000 ? 27  ARG A CZ    1 
ATOM   199  N  NH1   . ARG A 1 27  ? 54.36800 53.41300 -6.61900  1.000 188.22000 ? 27  ARG A NH1   1 
ATOM   200  N  NH2   . ARG A 1 27  ? 53.08900 55.08500 -7.53500  1.000 165.38000 ? 27  ARG A NH2   1 
ATOM   201  N  N     . ARG A 1 35  ? 43.14400 53.92300 4.33900   1.000 76.61000  ? 35  ARG A N     1 
ATOM   202  C  CA    . ARG A 1 35  ? 42.29100 52.98100 5.05600   1.000 73.81000  ? 35  ARG A CA    1 
ATOM   203  C  C     . ARG A 1 35  ? 41.51700 52.08800 4.09500   1.000 58.69000  ? 35  ARG A C     1 
ATOM   204  O  O     . ARG A 1 35  ? 41.47000 50.86400 4.26600   1.000 49.96000  ? 35  ARG A O     1 
ATOM   205  C  CB    . ARG A 1 35  ? 41.31800 53.74000 5.95900   1.000 73.20000  ? 35  ARG A CB    1 
ATOM   206  C  CG    . ARG A 1 35  ? 41.92400 54.30100 7.23000   1.000 79.46000  ? 35  ARG A CG    1 
ATOM   207  C  CD    . ARG A 1 35  ? 40.88700 55.10000 8.01800   1.000 88.92000  ? 35  ARG A CD    1 
ATOM   208  N  NE    . ARG A 1 35  ? 39.94800 55.80300 7.14500   1.000 101.15000 ? 35  ARG A NE    1 
ATOM   209  C  CZ    . ARG A 1 35  ? 39.78900 57.12200 7.11600   1.000 102.33000 ? 35  ARG A CZ    1 
ATOM   210  N  NH1   . ARG A 1 35  ? 40.51100 57.89700 7.91500   1.000 103.02000 ? 35  ARG A NH1   1 
ATOM   211  N  NH2   . ARG A 1 35  ? 38.90700 57.66800 6.28900   1.000 101.93000 ? 35  ARG A NH2   1 
ATOM   212  N  N     . TYR A 1 36  ? 40.88500 52.68900 3.08700   1.000 54.89000  ? 36  TYR A N     1 
ATOM   213  C  CA    . TYR A 1 36  ? 40.08000 51.91200 2.15200   1.000 53.49000  ? 36  TYR A CA    1 
ATOM   214  C  C     . TYR A 1 36  ? 40.93100 50.87400 1.43100   1.000 52.46000  ? 36  TYR A C     1 
ATOM   215  O  O     . TYR A 1 36  ? 40.57200 49.69200 1.37300   1.000 49.40000  ? 36  TYR A O     1 
ATOM   216  C  CB    . TYR A 1 36  ? 39.40400 52.84600 1.14800   1.000 53.06000  ? 36  TYR A CB    1 
ATOM   217  C  CG    . TYR A 1 36  ? 38.52000 53.89700 1.78100   1.000 51.97000  ? 36  TYR A CG    1 
ATOM   218  C  CD1   . TYR A 1 36  ? 37.18000 53.64200 2.03500   1.000 49.85000  ? 36  TYR A CD1   1 
ATOM   219  C  CD2   . TYR A 1 36  ? 39.02300 55.14600 2.12200   1.000 57.09000  ? 36  TYR A CD2   1 
ATOM   220  C  CE1   . TYR A 1 36  ? 36.36500 54.59700 2.61100   1.000 55.69000  ? 36  TYR A CE1   1 
ATOM   221  C  CE2   . TYR A 1 36  ? 38.21600 56.10900 2.69900   1.000 60.90000  ? 36  TYR A CE2   1 
ATOM   222  C  CZ    . TYR A 1 36  ? 36.88700 55.82900 2.94100   1.000 59.74000  ? 36  TYR A CZ    1 
ATOM   223  O  OH    . TYR A 1 36  ? 36.07200 56.77800 3.51500   1.000 61.05000  ? 36  TYR A OH    1 
ATOM   224  N  N     . TYR A 1 37  ? 42.07300 51.29800 0.88400   1.000 53.45000  ? 37  TYR A N     1 
ATOM   225  C  CA    . TYR A 1 37  ? 42.91000 50.37800 0.12100   1.000 52.85000  ? 37  TYR A CA    1 
ATOM   226  C  C     . TYR A 1 37  ? 43.44900 49.25800 1.00400   1.000 47.08000  ? 37  TYR A C     1 
ATOM   227  O  O     . TYR A 1 37  ? 43.58200 48.11500 0.55600   1.000 48.33000  ? 37  TYR A O     1 
ATOM   228  C  CB    . TYR A 1 37  ? 44.06000 51.13800 -0.53900  1.000 53.75000  ? 37  TYR A CB    1 
ATOM   229  C  CG    . TYR A 1 37  ? 43.63000 52.05400 -1.66200  1.000 60.11000  ? 37  TYR A CG    1 
ATOM   230  C  CD1   . TYR A 1 37  ? 43.45900 51.57200 -2.95300  1.000 60.12000  ? 37  TYR A CD1   1 
ATOM   231  C  CD2   . TYR A 1 37  ? 43.40100 53.40500 -1.43300  1.000 60.66000  ? 37  TYR A CD2   1 
ATOM   232  C  CE1   . TYR A 1 37  ? 43.06700 52.40900 -3.98200  1.000 56.23000  ? 37  TYR A CE1   1 
ATOM   233  C  CE2   . TYR A 1 37  ? 43.00900 54.24700 -2.45600  1.000 56.93000  ? 37  TYR A CE2   1 
ATOM   234  C  CZ    . TYR A 1 37  ? 42.84400 53.74300 -3.72700  1.000 57.33000  ? 37  TYR A CZ    1 
ATOM   235  O  OH    . TYR A 1 37  ? 42.45600 54.58000 -4.74600  1.000 64.67000  ? 37  TYR A OH    1 
ATOM   236  N  N     . VAL A 1 38  ? 43.77000 49.56800 2.26100   1.000 49.11000  ? 38  VAL A N     1 
ATOM   237  C  CA    . VAL A 1 38  ? 44.27700 48.53500 3.16000   1.000 49.67000  ? 38  VAL A CA    1 
ATOM   238  C  C     . VAL A 1 38  ? 43.17500 47.53800 3.50200   1.000 44.12000  ? 38  VAL A C     1 
ATOM   239  O  O     . VAL A 1 38  ? 43.43300 46.33800 3.66500   1.000 41.10000  ? 38  VAL A O     1 
ATOM   240  C  CB    . VAL A 1 38  ? 44.87200 49.17600 4.42700   1.000 58.49000  ? 38  VAL A CB    1 
ATOM   241  C  CG1   . VAL A 1 38  ? 45.17700 48.10700 5.47200   1.000 55.50000  ? 38  VAL A CG1   1 
ATOM   242  C  CG2   . VAL A 1 38  ? 46.12500 49.96700 4.07900   1.000 69.66000  ? 38  VAL A CG2   1 
ATOM   243  N  N     . THR A 1 39  ? 41.93500 48.01300 3.62000   1.000 40.82000  ? 39  THR A N     1 
ATOM   244  C  CA    . THR A 1 39  ? 40.82400 47.10700 3.89200   1.000 41.07000  ? 39  THR A CA    1 
ATOM   245  C  C     . THR A 1 39  ? 40.59700 46.15400 2.72500   1.000 38.24000  ? 39  THR A C     1 
ATOM   246  O  O     . THR A 1 39  ? 40.37600 44.95500 2.93000   1.000 33.19000  ? 39  THR A O     1 
ATOM   247  C  CB    . THR A 1 39  ? 39.55500 47.90400 4.18800   1.000 43.26000  ? 39  THR A CB    1 
ATOM   248  O  OG1   . THR A 1 39  ? 39.81700 48.85400 5.22900   1.000 48.48000  ? 39  THR A OG1   1 
ATOM   249  C  CG2   . THR A 1 39  ? 38.42100 46.97800 4.62200   1.000 40.15000  ? 39  THR A CG2   1 
ATOM   250  N  N     . LEU A 1 40  ? 40.66200 46.66400 1.49300   1.000 43.16000  ? 40  LEU A N     1 
ATOM   251  C  CA    . LEU A 1 40  ? 40.44900 45.79600 0.34200   1.000 37.98000  ? 40  LEU A CA    1 
ATOM   252  C  C     . LEU A 1 40  ? 41.55500 44.76000 0.20700   1.000 39.00000  ? 40  LEU A C     1 
ATOM   253  O  O     . LEU A 1 40  ? 41.29200 43.63000 -0.22400  1.000 38.43000  ? 40  LEU A O     1 
ATOM   254  C  CB    . LEU A 1 40  ? 40.34400 46.64300 -0.92800  1.000 38.70000  ? 40  LEU A CB    1 
ATOM   255  C  CG    . LEU A 1 40  ? 39.05900 47.47400 -0.97000  1.000 40.50000  ? 40  LEU A CG    1 
ATOM   256  C  CD1   . LEU A 1 40  ? 39.16800 48.56700 -2.01300  1.000 43.96000  ? 40  LEU A CD1   1 
ATOM   257  C  CD2   . LEU A 1 40  ? 37.85100 46.58100 -1.23100  1.000 38.60000  ? 40  LEU A CD2   1 
ATOM   258  N  N     . VAL A 1 41  ? 42.79300 45.10800 0.56900   1.000 41.34000  ? 41  VAL A N     1 
ATOM   259  C  CA    . VAL A 1 41  ? 43.85300 44.10500 0.57200   1.000 43.19000  ? 41  VAL A CA    1 
ATOM   260  C  C     . VAL A 1 41  ? 43.52700 43.00600 1.57300   1.000 37.44000  ? 41  VAL A C     1 
ATOM   261  O  O     . VAL A 1 41  ? 43.72700 41.81600 1.30100   1.000 33.75000  ? 41  VAL A O     1 
ATOM   262  C  CB    . VAL A 1 41  ? 45.21800 44.75400 0.87100   1.000 48.93000  ? 41  VAL A CB    1 
ATOM   263  C  CG1   . VAL A 1 41  ? 46.27200 43.68000 1.10200   1.000 52.84000  ? 41  VAL A CG1   1 
ATOM   264  C  CG2   . VAL A 1 41  ? 45.62500 45.67300 -0.27200  1.000 47.86000  ? 41  VAL A CG2   1 
ATOM   265  N  N     . GLY A 1 42  ? 43.01000 43.38200 2.74300   1.000 35.99000  ? 42  GLY A N     1 
ATOM   266  C  CA    . GLY A 1 42  ? 42.64700 42.38100 3.73300   1.000 32.40000  ? 42  GLY A CA    1 
ATOM   267  C  C     . GLY A 1 42  ? 41.50600 41.49600 3.27100   1.000 30.90000  ? 42  GLY A C     1 
ATOM   268  O  O     . GLY A 1 42  ? 41.53600 40.27800 3.46200   1.000 32.84000  ? 42  GLY A O     1 
ATOM   269  N  N     . ILE A 1 43  ? 40.49000 42.09300 2.64800   1.000 33.36000  ? 43  ILE A N     1 
ATOM   270  C  CA    . ILE A 1 43  ? 39.33600 41.32600 2.19000   1.000 33.88000  ? 43  ILE A CA    1 
ATOM   271  C  C     . ILE A 1 43  ? 39.77100 40.21600 1.23800   1.000 31.82000  ? 43  ILE A C     1 
ATOM   272  O  O     . ILE A 1 43  ? 39.44800 39.04000 1.44000   1.000 32.66000  ? 43  ILE A O     1 
ATOM   273  C  CB    . ILE A 1 43  ? 38.30400 42.26100 1.53400   1.000 28.75000  ? 43  ILE A CB    1 
ATOM   274  C  CG1   . ILE A 1 43  ? 37.62600 43.11800 2.60300   1.000 26.32000  ? 43  ILE A CG1   1 
ATOM   275  C  CG2   . ILE A 1 43  ? 37.27300 41.45500 0.75400   1.000 27.66000  ? 43  ILE A CG2   1 
ATOM   276  C  CD1   . ILE A 1 43  ? 37.03600 44.40500 2.06900   1.000 28.13000  ? 43  ILE A CD1   1 
ATOM   277  N  N     . SER A 1 44  ? 40.50800 40.57000 0.18500   1.000 24.85000  ? 44  SER A N     1 
ATOM   278  C  CA    . SER A 1 44  ? 40.89400 39.56400 -0.79700  1.000 28.02000  ? 44  SER A CA    1 
ATOM   279  C  C     . SER A 1 44  ? 42.13800 38.79700 -0.37000  1.000 28.83000  ? 44  SER A C     1 
ATOM   280  O  O     . SER A 1 44  ? 42.29400 37.62700 -0.73400  1.000 31.23000  ? 44  SER A O     1 
ATOM   281  C  CB    . SER A 1 44  ? 41.11500 40.21100 -2.16500  1.000 33.36000  ? 44  SER A CB    1 
ATOM   282  O  OG    . SER A 1 44  ? 41.94600 41.35300 -2.06600  1.000 38.61000  ? 44  SER A OG    1 
ATOM   283  N  N     . GLY A 1 45  ? 43.02500 39.42800 0.40000   1.000 32.44000  ? 45  GLY A N     1 
ATOM   284  C  CA    . GLY A 1 45  ? 44.20800 38.72600 0.87100   1.000 31.58000  ? 45  GLY A CA    1 
ATOM   285  C  C     . GLY A 1 45  ? 43.86500 37.55400 1.76900   1.000 31.69000  ? 45  GLY A C     1 
ATOM   286  O  O     . GLY A 1 45  ? 44.41200 36.45800 1.62300   1.000 32.19000  ? 45  GLY A O     1 
ATOM   287  N  N     . ILE A 1 46  ? 42.94700 37.76800 2.71300   1.000 33.25000  ? 46  ILE A N     1 
ATOM   288  C  CA    . ILE A 1 46  ? 42.53700 36.67900 3.59500   1.000 34.46000  ? 46  ILE A CA    1 
ATOM   289  C  C     . ILE A 1 46  ? 41.87100 35.56900 2.79000   1.000 31.32000  ? 46  ILE A C     1 
ATOM   290  O  O     . ILE A 1 46  ? 42.13800 34.38000 3.00400   1.000 32.04000  ? 46  ILE A O     1 
ATOM   291  C  CB    . ILE A 1 46  ? 41.61500 37.21200 4.70600   1.000 36.77000  ? 46  ILE A CB    1 
ATOM   292  C  CG1   . ILE A 1 46  ? 42.42100 38.07400 5.68100   1.000 39.26000  ? 46  ILE A CG1   1 
ATOM   293  C  CG2   . ILE A 1 46  ? 40.95100 36.05800 5.44600   1.000 29.61000  ? 46  ILE A CG2   1 
ATOM   294  C  CD1   . ILE A 1 46  ? 41.58200 39.00000 6.53900   1.000 36.98000  ? 46  ILE A CD1   1 
ATOM   295  N  N     . ALA A 1 47  ? 41.01200 35.93800 1.83800   1.000 30.82000  ? 47  ALA A N     1 
ATOM   296  C  CA    . ALA A 1 47  ? 40.34100 34.93000 1.02500   1.000 27.52000  ? 47  ALA A CA    1 
ATOM   297  C  C     . ALA A 1 47  ? 41.34400 34.14200 0.19100   1.000 26.78000  ? 47  ALA A C     1 
ATOM   298  O  O     . ALA A 1 47  ? 41.21100 32.92200 0.04000   1.000 24.82000  ? 47  ALA A O     1 
ATOM   299  C  CB    . ALA A 1 47  ? 39.29000 35.58500 0.13000   1.000 26.38000  ? 47  ALA A CB    1 
ATOM   300  N  N     . ALA A 1 48  ? 42.34900 34.81900 -0.36900  1.000 28.22000  ? 48  ALA A N     1 
ATOM   301  C  CA    . ALA A 1 48  ? 43.39600 34.11500 -1.10000  1.000 32.10000  ? 48  ALA A CA    1 
ATOM   302  C  C     . ALA A 1 48  ? 43.95600 32.96900 -0.26800  1.000 30.74000  ? 48  ALA A C     1 
ATOM   303  O  O     . ALA A 1 48  ? 44.03500 31.82500 -0.73000  1.000 31.20000  ? 48  ALA A O     1 
ATOM   304  C  CB    . ALA A 1 48  ? 44.50900 35.08400 -1.49500  1.000 33.30000  ? 48  ALA A CB    1 
ATOM   305  N  N     . VAL A 1 49  ? 44.32400 33.25800 0.98200   1.000 31.82000  ? 49  VAL A N     1 
ATOM   306  C  CA    . VAL A 1 49  ? 44.91900 32.24000 1.84400   1.000 35.75000  ? 49  VAL A CA    1 
ATOM   307  C  C     . VAL A 1 49  ? 43.93500 31.09800 2.07700   1.000 31.30000  ? 49  VAL A C     1 
ATOM   308  O  O     . VAL A 1 49  ? 44.29400 29.91900 1.97400   1.000 29.45000  ? 49  VAL A O     1 
ATOM   309  C  CB    . VAL A 1 49  ? 45.37900 32.86600 3.17200   1.000 39.30000  ? 49  VAL A CB    1 
ATOM   310  C  CG1   . VAL A 1 49  ? 45.77800 31.78300 4.16500   1.000 40.62000  ? 49  VAL A CG1   1 
ATOM   311  C  CG2   . VAL A 1 49  ? 46.53000 33.83100 2.92900   1.000 39.95000  ? 49  VAL A CG2   1 
ATOM   312  N  N     . ALA A 1 50  ? 42.68300 31.42500 2.39800   1.000 30.39000  ? 50  ALA A N     1 
ATOM   313  C  CA    . ALA A 1 50  ? 41.70500 30.37300 2.65300   1.000 30.41000  ? 50  ALA A CA    1 
ATOM   314  C  C     . ALA A 1 50  ? 41.56900 29.44700 1.45000   1.000 26.06000  ? 50  ALA A C     1 
ATOM   315  O  O     . ALA A 1 50  ? 41.47500 28.22400 1.60200   1.000 25.89000  ? 50  ALA A O     1 
ATOM   316  C  CB    . ALA A 1 50  ? 40.35000 30.97900 3.01900   1.000 35.32000  ? 50  ALA A CB    1 
ATOM   317  N  N     . TYR A 1 51  ? 41.57700 30.00800 0.24000   1.000 23.91000  ? 51  TYR A N     1 
ATOM   318  C  CA    . TYR A 1 51  ? 41.38600 29.17800 -0.94400  1.000 27.81000  ? 51  TYR A CA    1 
ATOM   319  C  C     . TYR A 1 51  ? 42.60500 28.30200 -1.21300  1.000 27.37000  ? 51  TYR A C     1 
ATOM   320  O  O     . TYR A 1 51  ? 42.46200 27.13500 -1.59300  1.000 34.37000  ? 51  TYR A O     1 
ATOM   321  C  CB    . TYR A 1 51  ? 41.05700 30.05300 -2.14800  1.000 31.40000  ? 51  TYR A CB    1 
ATOM   322  C  CG    . TYR A 1 51  ? 39.57000 30.24700 -2.31900  1.000 29.20000  ? 51  TYR A CG    1 
ATOM   323  C  CD1   . TYR A 1 51  ? 38.77600 29.22400 -2.81800  1.000 26.12000  ? 51  TYR A CD1   1 
ATOM   324  C  CD2   . TYR A 1 51  ? 38.95400 31.43700 -1.95500  1.000 25.72000  ? 51  TYR A CD2   1 
ATOM   325  C  CE1   . TYR A 1 51  ? 37.41700 29.38400 -2.96700  1.000 28.66000  ? 51  TYR A CE1   1 
ATOM   326  C  CE2   . TYR A 1 51  ? 37.59000 31.60700 -2.09900  1.000 26.33000  ? 51  TYR A CE2   1 
ATOM   327  C  CZ    . TYR A 1 51  ? 36.82700 30.57600 -2.60900  1.000 30.98000  ? 51  TYR A CZ    1 
ATOM   328  O  OH    . TYR A 1 51  ? 35.46700 30.72800 -2.75600  1.000 31.51000  ? 51  TYR A OH    1 
ATOM   329  N  N     . VAL A 1 52  ? 43.81200 28.83800 -1.01900  1.000 28.17000  ? 52  VAL A N     1 
ATOM   330  C  CA    . VAL A 1 52  ? 45.01000 28.01700 -1.17600  1.000 28.49000  ? 52  VAL A CA    1 
ATOM   331  C  C     . VAL A 1 52  ? 44.96100 26.83200 -0.21900  1.000 32.21000  ? 52  VAL A C     1 
ATOM   332  O  O     . VAL A 1 52  ? 45.11500 25.67300 -0.62500  1.000 34.35000  ? 52  VAL A O     1 
ATOM   333  C  CB    . VAL A 1 52  ? 46.27900 28.86100 -0.96100  1.000 31.43000  ? 52  VAL A CB    1 
ATOM   334  C  CG1   . VAL A 1 52  ? 47.51000 27.96800 -0.93600  1.000 35.66000  ? 52  VAL A CG1   1 
ATOM   335  C  CG2   . VAL A 1 52  ? 46.40400 29.92200 -2.04800  1.000 33.13000  ? 52  VAL A CG2   1 
ATOM   336  N  N     . VAL A 1 53  ? 44.74000 27.10700 1.06800   1.000 37.34000  ? 53  VAL A N     1 
ATOM   337  C  CA    . VAL A 1 53  ? 44.63400 26.03500 2.05600   1.000 35.87000  ? 53  VAL A CA    1 
ATOM   338  C  C     . VAL A 1 53  ? 43.65000 24.97500 1.57800   1.000 33.65000  ? 53  VAL A C     1 
ATOM   339  O  O     . VAL A 1 53  ? 43.93300 23.77100 1.62000   1.000 38.18000  ? 53  VAL A O     1 
ATOM   340  C  CB    . VAL A 1 53  ? 44.22300 26.60800 3.42600   1.000 38.95000  ? 53  VAL A CB    1 
ATOM   341  C  CG1   . VAL A 1 53  ? 43.88700 25.49200 4.39800   1.000 43.48000  ? 53  VAL A CG1   1 
ATOM   342  C  CG2   . VAL A 1 53  ? 45.33000 27.49200 3.97800   1.000 40.15000  ? 53  VAL A CG2   1 
ATOM   343  N  N     . MET A 1 54  ? 42.47900 25.41000 1.11500   1.000 33.80000  ? 54  MET A N     1 
ATOM   344  C  CA    . MET A 1 54  ? 41.48500 24.45600 0.63400   1.000 35.32000  ? 54  MET A CA    1 
ATOM   345  C  C     . MET A 1 54  ? 41.95900 23.76100 -0.63400  1.000 38.93000  ? 54  MET A C     1 
ATOM   346  O  O     . MET A 1 54  ? 41.72500 22.55900 -0.81200  1.000 33.29000  ? 54  MET A O     1 
ATOM   347  C  CB    . MET A 1 54  ? 40.15400 25.16500 0.39400   1.000 34.32000  ? 54  MET A CB    1 
ATOM   348  C  CG    . MET A 1 54  ? 39.41500 25.50400 1.68500   1.000 34.13000  ? 54  MET A CG    1 
ATOM   349  S  SD    . MET A 1 54  ? 37.70300 26.01500 1.42200   1.000 39.97000  ? 54  MET A SD    1 
ATOM   350  C  CE    . MET A 1 54  ? 37.92300 27.72800 0.97000   1.000 32.14000  ? 54  MET A CE    1 
ATOM   351  N  N     . ALA A 1 55  ? 42.62400 24.49500 -1.52900  1.000 34.43000  ? 55  ALA A N     1 
ATOM   352  C  CA    . ALA A 1 55  ? 43.16700 23.86600 -2.72900  1.000 35.56000  ? 55  ALA A CA    1 
ATOM   353  C  C     . ALA A 1 55  ? 44.12700 22.74100 -2.36300  1.000 42.57000  ? 55  ALA A C     1 
ATOM   354  O  O     . ALA A 1 55  ? 44.13100 21.68300 -3.00200  1.000 41.40000  ? 55  ALA A O     1 
ATOM   355  C  CB    . ALA A 1 55  ? 43.86800 24.90700 -3.60200  1.000 35.93000  ? 55  ALA A CB    1 
ATOM   356  N  N     . LEU A 1 56  ? 44.93500 22.94500 -1.32400  1.000 45.69000  ? 56  LEU A N     1 
ATOM   357  C  CA    . LEU A 1 56  ? 45.89000 21.93400 -0.88600  1.000 45.37000  ? 56  LEU A CA    1 
ATOM   358  C  C     . LEU A 1 56  ? 45.23600 20.78200 -0.13800  1.000 47.31000  ? 56  LEU A C     1 
ATOM   359  O  O     . LEU A 1 56  ? 45.95300 19.88500 0.32300   1.000 50.67000  ? 56  LEU A O     1 
ATOM   360  C  CB    . LEU A 1 56  ? 46.95500 22.58000 0.00100   1.000 45.45000  ? 56  LEU A CB    1 
ATOM   361  C  CG    . LEU A 1 56  ? 47.88900 23.55900 -0.71200  1.000 56.61000  ? 56  LEU A CG    1 
ATOM   362  C  CD1   . LEU A 1 56  ? 48.73600 24.33600 0.28400   1.000 56.19000  ? 56  LEU A CD1   1 
ATOM   363  C  CD2   . LEU A 1 56  ? 48.76700 22.81500 -1.70700  1.000 64.93000  ? 56  LEU A CD2   1 
ATOM   364  N  N     . GLY A 1 57  ? 43.91300 20.77600 -0.00100  1.000 42.73000  ? 57  GLY A N     1 
ATOM   365  C  CA    . GLY A 1 57  ? 43.23100 19.70600 0.69300   1.000 36.83000  ? 57  GLY A CA    1 
ATOM   366  C  C     . GLY A 1 57  ? 43.19000 19.83900 2.19700   1.000 42.84000  ? 57  GLY A C     1 
ATOM   367  O  O     . GLY A 1 57  ? 42.85400 18.86500 2.88200   1.000 43.70000  ? 57  GLY A O     1 
ATOM   368  N  N     . VAL A 1 58  ? 43.51100 20.99900 2.73200   1.000 46.73000  ? 58  VAL A N     1 
ATOM   369  C  CA    . VAL A 1 58  ? 43.53200 21.20700 4.17300   1.000 51.96000  ? 58  VAL A CA    1 
ATOM   370  C  C     . VAL A 1 58  ? 42.18000 21.74700 4.61500   1.000 54.07000  ? 58  VAL A C     1 
ATOM   371  O  O     . VAL A 1 58  ? 41.57200 22.58200 3.93400   1.000 47.82000  ? 58  VAL A O     1 
ATOM   372  C  CB    . VAL A 1 58  ? 44.67700 22.15900 4.56800   1.000 63.52000  ? 58  VAL A CB    1 
ATOM   373  C  CG1   . VAL A 1 58  ? 44.52700 22.59400 6.01800   1.000 70.02000  ? 58  VAL A CG1   1 
ATOM   374  C  CG2   . VAL A 1 58  ? 46.02200 21.48600 4.33700   1.000 65.09000  ? 58  VAL A CG2   1 
ATOM   375  N  N     . GLY A 1 59  ? 41.69900 21.25300 5.75200   1.000 56.40000  ? 59  GLY A N     1 
ATOM   376  C  CA    . GLY A 1 59  ? 40.48100 21.77200 6.33500   1.000 52.90000  ? 59  GLY A CA    1 
ATOM   377  C  C     . GLY A 1 59  ? 39.19800 21.18500 5.79900   1.000 48.37000  ? 59  GLY A C     1 
ATOM   378  O  O     . GLY A 1 59  ? 38.13400 21.78000 5.99300   1.000 42.02000  ? 59  GLY A O     1 
ATOM   379  N  N     . TRP A 1 60  ? 39.25900 20.04100 5.12300   1.000 45.14000  ? 60  TRP A N     1 
ATOM   380  C  CA    . TRP A 1 60  ? 38.06100 19.37200 4.61800   1.000 44.35000  ? 60  TRP A CA    1 
ATOM   381  C  C     . TRP A 1 60  ? 37.54800 18.45600 5.72300   1.000 45.91000  ? 60  TRP A C     1 
ATOM   382  O  O     . TRP A 1 60  ? 38.05900 17.35000 5.91300   1.000 51.41000  ? 60  TRP A O     1 
ATOM   383  C  CB    . TRP A 1 60  ? 38.36400 18.57300 3.35600   1.000 40.11000  ? 60  TRP A CB    1 
ATOM   384  C  CG    . TRP A 1 60  ? 38.89900 19.34800 2.18700   1.000 40.12000  ? 60  TRP A CG    1 
ATOM   385  C  CD1   . TRP A 1 60  ? 39.57600 20.53500 2.21100   1.000 40.15000  ? 60  TRP A CD1   1 
ATOM   386  C  CD2   . TRP A 1 60  ? 38.81100 18.96500 0.81200   1.000 37.84000  ? 60  TRP A CD2   1 
ATOM   387  N  NE1   . TRP A 1 60  ? 39.91300 20.91200 0.93100   1.000 41.11000  ? 60  TRP A NE1   1 
ATOM   388  C  CE2   . TRP A 1 60  ? 39.45100 19.96500 0.05500   1.000 39.11000  ? 60  TRP A CE2   1 
ATOM   389  C  CE3   . TRP A 1 60  ? 38.25100 17.86900 0.14700   1.000 40.92000  ? 60  TRP A CE3   1 
ATOM   390  C  CZ2   . TRP A 1 60  ? 39.54400 19.90300 -1.33500  1.000 41.54000  ? 60  TRP A CZ2   1 
ATOM   391  C  CZ3   . TRP A 1 60  ? 38.34100 17.81100 -1.23200  1.000 41.45000  ? 60  TRP A CZ3   1 
ATOM   392  C  CH2   . TRP A 1 60  ? 38.98400 18.82200 -1.95700  1.000 42.10000  ? 60  TRP A CH2   1 
ATOM   393  N  N     . VAL A 1 61  ? 36.53000 18.90000 6.45200   1.000 48.26000  ? 61  VAL A N     1 
ATOM   394  C  CA    . VAL A 1 61  ? 36.05000 18.21500 7.64600   1.000 49.53000  ? 61  VAL A CA    1 
ATOM   395  C  C     . VAL A 1 61  ? 34.87000 17.33200 7.26300   1.000 48.49000  ? 61  VAL A C     1 
ATOM   396  O  O     . VAL A 1 61  ? 33.85300 17.86200 6.78200   1.000 42.08000  ? 61  VAL A O     1 
ATOM   397  C  CB    . VAL A 1 61  ? 35.65100 19.20900 8.74800   1.000 50.42000  ? 61  VAL A CB    1 
ATOM   398  C  CG1   . VAL A 1 61  ? 35.24600 18.46000 10.01400  1.000 53.47000  ? 61  VAL A CG1   1 
ATOM   399  C  CG2   . VAL A 1 61  ? 36.78300 20.18600 9.02900   1.000 48.28000  ? 61  VAL A CG2   1 
ATOM   400  N  N     . PRO A 1 62  ? 34.93200 16.01600 7.46900   1.000 51.16000  ? 62  PRO A N     1 
ATOM   401  C  CA    . PRO A 1 62  ? 33.74900 15.18000 7.24900   1.000 50.59000  ? 62  PRO A CA    1 
ATOM   402  C  C     . PRO A 1 62  ? 32.77400 15.33400 8.40400   1.000 50.04000  ? 62  PRO A C     1 
ATOM   403  O  O     . PRO A 1 62  ? 33.16500 15.35500 9.57300   1.000 51.40000  ? 62  PRO A O     1 
ATOM   404  C  CB    . PRO A 1 62  ? 34.32500 13.76300 7.18500   1.000 53.64000  ? 62  PRO A CB    1 
ATOM   405  C  CG    . PRO A 1 62  ? 35.47900 13.81600 8.14500   1.000 56.72000  ? 62  PRO A CG    1 
ATOM   406  C  CD    . PRO A 1 62  ? 36.04000 15.23600 8.06400   1.000 55.04000  ? 62  PRO A CD    1 
ATOM   407  N  N     . VAL A 1 63  ? 31.49400 15.45600 8.06700   1.000 51.10000  ? 63  VAL A N     1 
ATOM   408  C  CA    . VAL A 1 63  ? 30.44000 15.64800 9.05700   1.000 55.24000  ? 63  VAL A CA    1 
ATOM   409  C  C     . VAL A 1 63  ? 29.24400 14.82300 8.60500   1.000 57.47000  ? 63  VAL A C     1 
ATOM   410  O  O     . VAL A 1 63  ? 28.60000 15.15400 7.60100   1.000 49.92000  ? 63  VAL A O     1 
ATOM   411  C  CB    . VAL A 1 63  ? 30.05300 17.12500 9.22300   1.000 51.30000  ? 63  VAL A CB    1 
ATOM   412  C  CG1   . VAL A 1 63  ? 28.89500 17.26400 10.19800  1.000 51.39000  ? 63  VAL A CG1   1 
ATOM   413  C  CG2   . VAL A 1 63  ? 31.25400 17.93700 9.68900   1.000 48.97000  ? 63  VAL A CG2   1 
ATOM   414  N  N     . ALA A 1 64  ? 28.94700 13.75100 9.33800   1.000 63.04000  ? 64  ALA A N     1 
ATOM   415  C  CA    . ALA A 1 64  ? 27.87100 12.84300 8.95900   1.000 64.97000  ? 64  ALA A CA    1 
ATOM   416  C  C     . ALA A 1 64  ? 28.11700 12.30000 7.55800   1.000 71.63000  ? 64  ALA A C     1 
ATOM   417  O  O     . ALA A 1 64  ? 28.99500 11.45300 7.36000   1.000 72.37000  ? 64  ALA A O     1 
ATOM   418  C  CB    . ALA A 1 64  ? 26.51700 13.54800 9.04500   1.000 62.89000  ? 64  ALA A CB    1 
ATOM   419  N  N     . GLU A 1 65  ? 27.36400 12.79100 6.57500   1.000 72.51000  ? 65  GLU A N     1 
ATOM   420  C  CA    . GLU A 1 65  ? 27.43700 12.28200 5.21400   1.000 73.20000  ? 65  GLU A CA    1 
ATOM   421  C  C     . GLU A 1 65  ? 28.03300 13.27600 4.22900   1.000 67.51000  ? 65  GLU A C     1 
ATOM   422  O  O     . GLU A 1 65  ? 28.21400 12.92900 3.05600   1.000 69.97000  ? 65  GLU A O     1 
ATOM   423  C  CB    . GLU A 1 65  ? 26.03800 11.87800 4.73200   1.000 82.90000  ? 65  GLU A CB    1 
ATOM   424  C  CG    . GLU A 1 65  ? 25.42000 10.72100 5.49700   1.000 96.28000  ? 65  GLU A CG    1 
ATOM   425  C  CD    . GLU A 1 65  ? 26.38500 9.56800  5.69100   1.000 106.33000 ? 65  GLU A CD    1 
ATOM   426  O  OE1   . GLU A 1 65  ? 27.43000 9.77400  6.34400   1.000 111.27000 ? 65  GLU A OE1   1 
ATOM   427  O  OE2   . GLU A 1 65  ? 26.09900 8.45800  5.19200   1.000 110.12000 ? 65  GLU A OE2   1 
ATOM   428  N  N     . ARG A 1 66  ? 28.34400 14.49200 4.66300   1.000 58.93000  ? 66  ARG A N     1 
ATOM   429  C  CA    . ARG A 1 66  ? 28.80400 15.54600 3.77500   1.000 55.78000  ? 66  ARG A CA    1 
ATOM   430  C  C     . ARG A 1 66  ? 30.20200 16.00000 4.17300   1.000 50.37000  ? 66  ARG A C     1 
ATOM   431  O  O     . ARG A 1 66  ? 30.73600 15.61500 5.21700   1.000 52.15000  ? 66  ARG A O     1 
ATOM   432  C  CB    . ARG A 1 66  ? 27.84100 16.73700 3.79400   1.000 53.40000  ? 66  ARG A CB    1 
ATOM   433  C  CG    . ARG A 1 66  ? 27.62200 17.32400 5.17600   1.000 55.58000  ? 66  ARG A CG    1 
ATOM   434  C  CD    . ARG A 1 66  ? 26.18300 17.77500 5.36700   1.000 64.38000  ? 66  ARG A CD    1 
ATOM   435  N  NE    . ARG A 1 66  ? 25.92500 18.17900 6.74600   1.000 75.72000  ? 66  ARG A NE    1 
ATOM   436  C  CZ    . ARG A 1 66  ? 26.56000 19.17100 7.36200   1.000 83.83000  ? 66  ARG A CZ    1 
ATOM   437  N  NH1   . ARG A 1 66  ? 27.49200 19.86600 6.72300   1.000 88.27000  ? 66  ARG A NH1   1 
ATOM   438  N  NH2   . ARG A 1 66  ? 26.26100 19.46700 8.62000   1.000 85.05000  ? 66  ARG A NH2   1 
ATOM   439  N  N     . THR A 1 67  ? 30.78400 16.83500 3.32100   1.000 42.58000  ? 67  THR A N     1 
ATOM   440  C  CA    . THR A 1 67  ? 32.10100 17.41300 3.54400   1.000 43.53000  ? 67  THR A CA    1 
ATOM   441  C  C     . THR A 1 67  ? 31.95200 18.91500 3.74800   1.000 41.55000  ? 67  THR A C     1 
ATOM   442  O  O     . THR A 1 67  ? 31.31800 19.59700 2.93500   1.000 38.45000  ? 67  THR A O     1 
ATOM   443  C  CB    . THR A 1 67  ? 33.03500 17.11500 2.37000   1.000 44.96000  ? 67  THR A CB    1 
ATOM   444  O  OG1   . THR A 1 67  ? 33.08800 15.69900 2.15100   1.000 50.23000  ? 67  THR A OG1   1 
ATOM   445  C  CG2   . THR A 1 67  ? 34.43400 17.63100 2.65100   1.000 41.84000  ? 67  THR A CG2   1 
ATOM   446  N  N     . VAL A 1 68  ? 32.52500 19.41600 4.84000   1.000 42.89000  ? 68  VAL A N     1 
ATOM   447  C  CA    . VAL A 1 68  ? 32.45000 20.82100 5.22000   1.000 47.50000  ? 68  VAL A CA    1 
ATOM   448  C  C     . VAL A 1 68  ? 33.83300 21.43400 5.04700   1.000 44.34000  ? 68  VAL A C     1 
ATOM   449  O  O     . VAL A 1 68  ? 34.84200 20.82900 5.42900   1.000 47.03000  ? 68  VAL A O     1 
ATOM   450  C  CB    . VAL A 1 68  ? 31.95200 20.98200 6.66900   1.000 52.09000  ? 68  VAL A CB    1 
ATOM   451  C  CG1   . VAL A 1 68  ? 32.48400 22.27000 7.28000   1.000 53.44000  ? 68  VAL A CG1   1 
ATOM   452  C  CG2   . VAL A 1 68  ? 30.43200 20.94600 6.71900   1.000 55.99000  ? 68  VAL A CG2   1 
ATOM   453  N  N     . PHE A 1 69  ? 33.87700 22.64200 4.49300   1.000 38.63000  ? 69  PHE A N     1 
ATOM   454  C  CA    . PHE A 1 69  ? 35.13100 23.32500 4.18200   1.000 36.93000  ? 69  PHE A CA    1 
ATOM   455  C  C     . PHE A 1 69  ? 35.35300 24.41800 5.22100   1.000 34.33000  ? 69  PHE A C     1 
ATOM   456  O  O     . PHE A 1 69  ? 34.82000 25.52400 5.10000   1.000 37.23000  ? 69  PHE A O     1 
ATOM   457  C  CB    . PHE A 1 69  ? 35.09300 23.88300 2.76300   1.000 31.41000  ? 69  PHE A CB    1 
ATOM   458  C  CG    . PHE A 1 69  ? 34.86900 22.83200 1.72100   1.000 36.93000  ? 69  PHE A CG    1 
ATOM   459  C  CD1   . PHE A 1 69  ? 35.89500 21.98000 1.35100   1.000 34.99000  ? 69  PHE A CD1   1 
ATOM   460  C  CD2   . PHE A 1 69  ? 33.62900 22.68200 1.12400   1.000 35.59000  ? 69  PHE A CD2   1 
ATOM   461  C  CE1   . PHE A 1 69  ? 35.69500 21.00600 0.39600   1.000 32.07000  ? 69  PHE A CE1   1 
ATOM   462  C  CE2   . PHE A 1 69  ? 33.42100 21.70800 0.16700   1.000 35.66000  ? 69  PHE A CE2   1 
ATOM   463  C  CZ    . PHE A 1 69  ? 34.45700 20.86700 -0.19600  1.000 32.54000  ? 69  PHE A CZ    1 
ATOM   464  N  N     . ALA A 1 70  ? 36.15000 24.10500 6.23100   1.000 37.88000  ? 70  ALA A N     1 
ATOM   465  C  CA    . ALA A 1 70  ? 36.28900 24.97200 7.39000   1.000 37.79000  ? 70  ALA A CA    1 
ATOM   466  C  C     . ALA A 1 70  ? 36.98000 26.28700 7.05400   1.000 34.66000  ? 70  ALA A C     1 
ATOM   467  O  O     . ALA A 1 70  ? 36.59600 27.32900 7.59500   1.000 29.54000  ? 70  ALA A O     1 
ATOM   468  C  CB    . ALA A 1 70  ? 37.05500 24.24900 8.50300   1.000 40.43000  ? 70  ALA A CB    1 
ATOM   469  N  N     . PRO A 1 71  ? 38.00500 26.29800 6.19700   1.000 35.81000  ? 71  PRO A N     1 
ATOM   470  C  CA    . PRO A 1 71  ? 38.63900 27.58700 5.86700   1.000 34.15000  ? 71  PRO A CA    1 
ATOM   471  C  C     . PRO A 1 71  ? 37.66700 28.58900 5.26900   1.000 26.82000  ? 71  PRO A C     1 
ATOM   472  O  O     . PRO A 1 71  ? 37.82800 29.79700 5.47800   1.000 31.20000  ? 71  PRO A O     1 
ATOM   473  C  CB    . PRO A 1 71  ? 39.74500 27.18900 4.87900   1.000 35.72000  ? 71  PRO A CB    1 
ATOM   474  C  CG    . PRO A 1 71  ? 40.07700 25.76600 5.25400   1.000 35.38000  ? 71  PRO A CG    1 
ATOM   475  C  CD    . PRO A 1 71  ? 38.74300 25.15700 5.61900   1.000 33.96000  ? 71  PRO A CD    1 
ATOM   476  N  N     . ARG A 1 72  ? 36.65300 28.12000 4.54300   1.000 28.72000  ? 72  ARG A N     1 
ATOM   477  C  CA    . ARG A 1 72  ? 35.66000 29.02700 3.97800   1.000 28.73000  ? 72  ARG A CA    1 
ATOM   478  C  C     . ARG A 1 72  ? 35.00600 29.87900 5.05700   1.000 28.31000  ? 72  ARG A C     1 
ATOM   479  O  O     . ARG A 1 72  ? 34.80700 31.08400 4.87000   1.000 27.13000  ? 72  ARG A O     1 
ATOM   480  C  CB    . ARG A 1 72  ? 34.60500 28.22800 3.21500   1.000 29.34000  ? 72  ARG A CB    1 
ATOM   481  C  CG    . ARG A 1 72  ? 33.25600 28.91600 3.06800   1.000 27.05000  ? 72  ARG A CG    1 
ATOM   482  C  CD    . ARG A 1 72  ? 32.20500 27.95200 2.53700   1.000 25.04000  ? 72  ARG A CD    1 
ATOM   483  N  NE    . ARG A 1 72  ? 32.41300 27.64900 1.12300   1.000 21.96000  ? 72  ARG A NE    1 
ATOM   484  C  CZ    . ARG A 1 72  ? 31.79600 26.67500 0.46100   1.000 28.10000  ? 72  ARG A CZ    1 
ATOM   485  N  NH1   . ARG A 1 72  ? 30.92400 25.89000 1.07900   1.000 27.36000  ? 72  ARG A NH1   1 
ATOM   486  N  NH2   . ARG A 1 72  ? 32.05300 26.48300 -0.82600  1.000 30.06000  ? 72  ARG A NH2   1 
ATOM   487  N  N     . TYR A 1 73  ? 34.65000 29.27200 6.19000   1.000 30.74000  ? 73  TYR A N     1 
ATOM   488  C  CA    . TYR A 1 73  ? 33.91800 30.01600 7.20900   1.000 24.94000  ? 73  TYR A CA    1 
ATOM   489  C  C     . TYR A 1 73  ? 34.83800 30.93300 8.00900   1.000 26.00000  ? 73  TYR A C     1 
ATOM   490  O  O     . TYR A 1 73  ? 34.43800 32.04300 8.37700   1.000 27.66000  ? 73  TYR A O     1 
ATOM   491  C  CB    . TYR A 1 73  ? 33.16600 29.04600 8.11500   1.000 31.17000  ? 73  TYR A CB    1 
ATOM   492  C  CG    . TYR A 1 73  ? 32.08800 28.29000 7.36800   1.000 29.00000  ? 73  TYR A CG    1 
ATOM   493  C  CD1   . TYR A 1 73  ? 30.84000 28.85700 7.14600   1.000 30.33000  ? 73  TYR A CD1   1 
ATOM   494  C  CD2   . TYR A 1 73  ? 32.33100 27.02200 6.86000   1.000 29.65000  ? 73  TYR A CD2   1 
ATOM   495  C  CE1   . TYR A 1 73  ? 29.85800 28.17500 6.45500   1.000 29.81000  ? 73  TYR A CE1   1 
ATOM   496  C  CE2   . TYR A 1 73  ? 31.35500 26.33100 6.16700   1.000 28.72000  ? 73  TYR A CE2   1 
ATOM   497  C  CZ    . TYR A 1 73  ? 30.12100 26.91300 5.96600   1.000 29.68000  ? 73  TYR A CZ    1 
ATOM   498  O  OH    . TYR A 1 73  ? 29.14900 26.22600 5.27600   1.000 34.92000  ? 73  TYR A OH    1 
ATOM   499  N  N     . ILE A 1 74  ? 36.07300 30.51000 8.28000   1.000 30.19000  ? 74  ILE A N     1 
ATOM   500  C  CA    . ILE A 1 74  ? 37.02400 31.42700 8.90100   1.000 29.84000  ? 74  ILE A CA    1 
ATOM   501  C  C     . ILE A 1 74  ? 37.22100 32.64700 8.00900   1.000 29.16000  ? 74  ILE A C     1 
ATOM   502  O  O     . ILE A 1 74  ? 37.19700 33.79500 8.47200   1.000 33.59000  ? 74  ILE A O     1 
ATOM   503  C  CB    . ILE A 1 74  ? 38.35800 30.71800 9.18800   1.000 40.65000  ? 74  ILE A CB    1 
ATOM   504  C  CG1   . ILE A 1 74  ? 38.20800 29.73400 10.34900  1.000 50.40000  ? 74  ILE A CG1   1 
ATOM   505  C  CG2   . ILE A 1 74  ? 39.43500 31.74100 9.53600   1.000 44.64000  ? 74  ILE A CG2   1 
ATOM   506  C  CD1   . ILE A 1 74  ? 37.62500 28.40500 9.95500   1.000 55.31000  ? 74  ILE A CD1   1 
ATOM   507  N  N     . ASP A 1 75  ? 37.43600 32.41200 6.71300   1.000 29.80000  ? 75  ASP A N     1 
ATOM   508  C  CA    . ASP A 1 75  ? 37.46300 33.48900 5.72600   1.000 21.59000  ? 75  ASP A CA    1 
ATOM   509  C  C     . ASP A 1 75  ? 36.26300 34.41400 5.90300   1.000 19.53000  ? 75  ASP A C     1 
ATOM   510  O  O     . ASP A 1 75  ? 36.41600 35.62300 6.10800   1.000 21.77000  ? 75  ASP A O     1 
ATOM   511  C  CB    . ASP A 1 75  ? 37.50900 32.86000 4.32300   1.000 28.01000  ? 75  ASP A CB    1 
ATOM   512  C  CG    . ASP A 1 75  ? 37.15100 33.83100 3.19600   1.000 27.67000  ? 75  ASP A CG    1 
ATOM   513  O  OD1   . ASP A 1 75  ? 36.84400 35.01500 3.44600   1.000 27.60000  ? 75  ASP A OD1   1 
ATOM   514  O  OD2   . ASP A 1 75  ? 37.18400 33.38700 2.02800   1.000 28.57000  ? 75  ASP A OD2   1 
ATOM   515  N  N     . TRP A 1 76  ? 35.05400 33.85700 5.82900   1.000 23.42000  ? 76  TRP A N     1 
ATOM   516  C  CA    . TRP A 1 76  ? 33.86300 34.69500 5.86900   1.000 22.53000  ? 76  TRP A CA    1 
ATOM   517  C  C     . TRP A 1 76  ? 33.78700 35.49700 7.16600   1.000 25.38000  ? 76  TRP A C     1 
ATOM   518  O  O     . TRP A 1 76  ? 33.40300 36.67400 7.15500   1.000 25.40000  ? 76  TRP A O     1 
ATOM   519  C  CB    . TRP A 1 76  ? 32.61100 33.83300 5.69300   1.000 22.97000  ? 76  TRP A CB    1 
ATOM   520  C  CG    . TRP A 1 76  ? 32.42200 33.28700 4.29300   1.000 20.19000  ? 76  TRP A CG    1 
ATOM   521  C  CD1   . TRP A 1 76  ? 33.21700 33.51200 3.20700   1.000 21.77000  ? 76  TRP A CD1   1 
ATOM   522  C  CD2   . TRP A 1 76  ? 31.36500 32.42500 3.84300   1.000 20.42000  ? 76  TRP A CD2   1 
ATOM   523  N  NE1   . TRP A 1 76  ? 32.72000 32.84800 2.10800   1.000 22.74000  ? 76  TRP A NE1   1 
ATOM   524  C  CE2   . TRP A 1 76  ? 31.58500 32.17200 2.47300   1.000 19.69000  ? 76  TRP A CE2   1 
ATOM   525  C  CE3   . TRP A 1 76  ? 30.25600 31.84300 4.46600   1.000 21.12000  ? 76  TRP A CE3   1 
ATOM   526  C  CZ2   . TRP A 1 76  ? 30.73900 31.36500 1.71800   1.000 22.65000  ? 76  TRP A CZ2   1 
ATOM   527  C  CZ3   . TRP A 1 76  ? 29.41800 31.04200 3.71500   1.000 23.99000  ? 76  TRP A CZ3   1 
ATOM   528  C  CH2   . TRP A 1 76  ? 29.66400 30.81200 2.35400   1.000 21.94000  ? 76  TRP A CH2   1 
ATOM   529  N  N     . ILE A 1 77  ? 34.16100 34.88400 8.29200   1.000 20.44000  ? 77  ILE A N     1 
ATOM   530  C  CA    . ILE A 1 77  ? 34.03400 35.56500 9.57700   1.000 21.04000  ? 77  ILE A CA    1 
ATOM   531  C  C     . ILE A 1 77  ? 34.95300 36.78000 9.65000   1.000 19.40000  ? 77  ILE A C     1 
ATOM   532  O  O     . ILE A 1 77  ? 34.64900 37.75900 10.34100  1.000 24.90000  ? 77  ILE A O     1 
ATOM   533  C  CB    . ILE A 1 77  ? 34.32200 34.59200 10.73700  1.000 32.78000  ? 77  ILE A CB    1 
ATOM   534  C  CG1   . ILE A 1 77  ? 33.23000 33.52600 10.82700  1.000 33.94000  ? 77  ILE A CG1   1 
ATOM   535  C  CG2   . ILE A 1 77  ? 34.44400 35.35400 12.05200  1.000 37.92000  ? 77  ILE A CG2   1 
ATOM   536  C  CD1   . ILE A 1 77  ? 33.63700 32.30700 11.63800  1.000 37.48000  ? 77  ILE A CD1   1 
ATOM   537  N  N     . LEU A 1 78  ? 36.08800 36.73700 8.96000   1.000 23.02000  ? 78  LEU A N     1 
ATOM   538  C  CA    . LEU A 1 78  ? 37.03200 37.84200 9.00400   1.000 27.06000  ? 78  LEU A CA    1 
ATOM   539  C  C     . LEU A 1 78  ? 36.84400 38.83800 7.87000   1.000 31.98000  ? 78  LEU A C     1 
ATOM   540  O  O     . LEU A 1 78  ? 37.07300 40.03800 8.06500   1.000 32.42000  ? 78  LEU A O     1 
ATOM   541  C  CB    . LEU A 1 78  ? 38.46600 37.31100 8.95700   1.000 29.04000  ? 78  LEU A CB    1 
ATOM   542  C  CG    . LEU A 1 78  ? 38.87500 36.36700 10.08200  1.000 36.12000  ? 78  LEU A CG    1 
ATOM   543  C  CD1   . LEU A 1 78  ? 40.20100 35.71300 9.75600   1.000 32.35000  ? 78  LEU A CD1   1 
ATOM   544  C  CD2   . LEU A 1 78  ? 38.94700 37.13900 11.39300  1.000 43.38000  ? 78  LEU A CD2   1 
ATOM   545  N  N     . THR A 1 79  ? 36.43200 38.37700 6.68800   1.000 27.21000  ? 79  THR A N     1 
ATOM   546  C  CA    . THR A 1 79  ? 36.36200 39.27000 5.54200   1.000 20.76000  ? 79  THR A CA    1 
ATOM   547  C  C     . THR A 1 79  ? 35.03300 40.01500 5.46300   1.000 20.77000  ? 79  THR A C     1 
ATOM   548  O  O     . THR A 1 79  ? 35.01400 41.19000 5.07900   1.000 25.87000  ? 79  THR A O     1 
ATOM   549  C  CB    . THR A 1 79  ? 36.60200 38.50200 4.23600   1.000 26.94000  ? 79  THR A CB    1 
ATOM   550  O  OG1   . THR A 1 79  ? 35.60600 37.48500 4.07000   1.000 23.62000  ? 79  THR A OG1   1 
ATOM   551  C  CG2   . THR A 1 79  ? 37.98300 37.86200 4.23700   1.000 27.15000  ? 79  THR A CG2   1 
ATOM   552  N  N     . THR A 1 80  ? 33.91800 39.37800 5.81700   1.000 23.00000  ? 80  THR A N     1 
ATOM   553  C  CA    . THR A 1 80  ? 32.63700 40.07200 5.71100   1.000 22.74000  ? 80  THR A CA    1 
ATOM   554  C  C     . THR A 1 80  ? 32.52600 41.28100 6.63500   1.000 21.75000  ? 80  THR A C     1 
ATOM   555  O  O     . THR A 1 80  ? 31.94800 42.29700 6.19700   1.000 24.93000  ? 80  THR A O     1 
ATOM   556  C  CB    . THR A 1 80  ? 31.46400 39.10700 5.95300   1.000 22.80000  ? 80  THR A CB    1 
ATOM   557  O  OG1   . THR A 1 80  ? 31.60000 38.46300 7.22600   1.000 30.23000  ? 80  THR A OG1   1 
ATOM   558  C  CG2   . THR A 1 80  ? 31.39900 38.05800 4.84400   1.000 22.58000  ? 80  THR A CG2   1 
ATOM   559  N  N     . PRO A 1 81  ? 33.02200 41.27000 7.87600   1.000 23.93000  ? 81  PRO A N     1 
ATOM   560  C  CA    . PRO A 1 81  ? 32.98200 42.51300 8.66300   1.000 24.53000  ? 81  PRO A CA    1 
ATOM   561  C  C     . PRO A 1 81  ? 33.83000 43.61700 8.04900   1.000 26.77000  ? 81  PRO A C     1 
ATOM   562  O  O     . PRO A 1 81  ? 33.51900 44.80400 8.21200   1.000 25.84000  ? 81  PRO A O     1 
ATOM   563  C  CB    . PRO A 1 81  ? 33.50700 42.08400 10.04100  1.000 32.20000  ? 81  PRO A CB    1 
ATOM   564  C  CG    . PRO A 1 81  ? 34.29400 40.84300 9.79500   1.000 33.75000  ? 81  PRO A CG    1 
ATOM   565  C  CD    . PRO A 1 81  ? 33.62100 40.15200 8.62800   1.000 31.59000  ? 81  PRO A CD    1 
ATOM   566  N  N     . LEU A 1 82  ? 34.89600 43.25000 7.33800   1.000 27.96000  ? 82  LEU A N     1 
ATOM   567  C  CA    . LEU A 1 82  ? 35.70800 44.24300 6.64600   1.000 28.68000  ? 82  LEU A CA    1 
ATOM   568  C  C     . LEU A 1 82  ? 34.93600 44.87700 5.49400   1.000 28.48000  ? 82  LEU A C     1 
ATOM   569  O  O     . LEU A 1 82  ? 35.09300 46.07200 5.21800   1.000 26.52000  ? 82  LEU A O     1 
ATOM   570  C  CB    . LEU A 1 82  ? 36.99200 43.59300 6.13700   1.000 30.89000  ? 82  LEU A CB    1 
ATOM   571  C  CG    . LEU A 1 82  ? 38.02900 43.21700 7.19500   1.000 33.89000  ? 82  LEU A CG    1 
ATOM   572  C  CD1   . LEU A 1 82  ? 39.15800 42.41700 6.56200   1.000 32.38000  ? 82  LEU A CD1   1 
ATOM   573  C  CD2   . LEU A 1 82  ? 38.56200 44.46000 7.88100   1.000 36.48000  ? 82  LEU A CD2   1 
ATOM   574  N  N     . ILE A 1 83  ? 34.10300 44.09200 4.80800   1.000 27.60000  ? 83  ILE A N     1 
ATOM   575  C  CA    . ILE A 1 83  ? 33.24400 44.65700 3.77400   1.000 26.58000  ? 83  ILE A CA    1 
ATOM   576  C  C     . ILE A 1 83  ? 32.22800 45.60700 4.39300   1.000 24.92000  ? 83  ILE A C     1 
ATOM   577  O  O     . ILE A 1 83  ? 31.98000 46.70100 3.87200   1.000 26.48000  ? 83  ILE A O     1 
ATOM   578  C  CB    . ILE A 1 83  ? 32.55200 43.53500 2.97700   1.000 24.40000  ? 83  ILE A CB    1 
ATOM   579  C  CG1   . ILE A 1 83  ? 33.58400 42.70300 2.21300   1.000 22.99000  ? 83  ILE A CG1   1 
ATOM   580  C  CG2   . ILE A 1 83  ? 31.52300 44.12400 2.02200   1.000 26.55000  ? 83  ILE A CG2   1 
ATOM   581  C  CD1   . ILE A 1 83  ? 33.01200 41.46100 1.56400   1.000 19.18000  ? 83  ILE A CD1   1 
ATOM   582  N  N     . VAL A 1 84  ? 31.62000 45.20500 5.51200   1.000 27.37000  ? 84  VAL A N     1 
ATOM   583  C  CA    . VAL A 1 84  ? 30.67300 46.07900 6.19600   1.000 28.40000  ? 84  VAL A CA    1 
ATOM   584  C  C     . VAL A 1 84  ? 31.38100 47.32500 6.71600   1.000 28.81000  ? 84  VAL A C     1 
ATOM   585  O  O     . VAL A 1 84  ? 30.83800 48.43500 6.66900   1.000 31.74000  ? 84  VAL A O     1 
ATOM   586  C  CB    . VAL A 1 84  ? 29.96300 45.31100 7.32800   1.000 28.61000  ? 84  VAL A CB    1 
ATOM   587  C  CG1   . VAL A 1 84  ? 29.20100 46.27000 8.23400   1.000 31.06000  ? 84  VAL A CG1   1 
ATOM   588  C  CG2   . VAL A 1 84  ? 29.02300 44.26100 6.74300   1.000 27.22000  ? 84  VAL A CG2   1 
ATOM   589  N  N     . TYR A 1 85  ? 32.60600 47.16300 7.21500   1.000 30.22000  ? 85  TYR A N     1 
ATOM   590  C  CA    . TYR A 1 85  ? 33.39500 48.31800 7.63700   1.000 36.48000  ? 85  TYR A CA    1 
ATOM   591  C  C     . TYR A 1 85  ? 33.60800 49.28200 6.47300   1.000 39.04000  ? 85  TYR A C     1 
ATOM   592  O  O     . TYR A 1 85  ? 33.36400 50.48900 6.59800   1.000 35.29000  ? 85  TYR A O     1 
ATOM   593  C  CB    . TYR A 1 85  ? 34.72900 47.84400 8.22100   1.000 39.21000  ? 85  TYR A CB    1 
ATOM   594  C  CG    . TYR A 1 85  ? 35.66800 48.95700 8.62900   1.000 46.25000  ? 85  TYR A CG    1 
ATOM   595  C  CD1   . TYR A 1 85  ? 35.31400 49.87200 9.61200   1.000 50.79000  ? 85  TYR A CD1   1 
ATOM   596  C  CD2   . TYR A 1 85  ? 36.91700 49.08500 8.03500   1.000 51.94000  ? 85  TYR A CD2   1 
ATOM   597  C  CE1   . TYR A 1 85  ? 36.17500 50.89100 9.98500   1.000 52.36000  ? 85  TYR A CE1   1 
ATOM   598  C  CE2   . TYR A 1 85  ? 37.78300 50.09700 8.40200   1.000 56.65000  ? 85  TYR A CE2   1 
ATOM   599  C  CZ    . TYR A 1 85  ? 37.40800 50.99600 9.37700   1.000 56.48000  ? 85  TYR A CZ    1 
ATOM   600  O  OH    . TYR A 1 85  ? 38.26900 52.00300 9.74100   1.000 61.12000  ? 85  TYR A OH    1 
ATOM   601  N  N     . PHE A 1 86  ? 34.04600 48.76100 5.32400   1.000 37.54000  ? 86  PHE A N     1 
ATOM   602  C  CA    . PHE A 1 86  ? 34.24500 49.60300 4.14900   1.000 33.98000  ? 86  PHE A CA    1 
ATOM   603  C  C     . PHE A 1 86  ? 32.99000 50.40600 3.82800   1.000 32.78000  ? 86  PHE A C     1 
ATOM   604  O  O     . PHE A 1 86  ? 33.05200 51.62100 3.59900   1.000 32.18000  ? 86  PHE A O     1 
ATOM   605  C  CB    . PHE A 1 86  ? 34.65400 48.73300 2.95700   1.000 38.10000  ? 86  PHE A CB    1 
ATOM   606  C  CG    . PHE A 1 86  ? 35.07400 49.51000 1.74000   1.000 33.56000  ? 86  PHE A CG    1 
ATOM   607  C  CD1   . PHE A 1 86  ? 34.13500 50.14800 0.94500   1.000 35.14000  ? 86  PHE A CD1   1 
ATOM   608  C  CD2   . PHE A 1 86  ? 36.40900 49.59400 1.38400   1.000 39.44000  ? 86  PHE A CD2   1 
ATOM   609  C  CE1   . PHE A 1 86  ? 34.51800 50.85700 -0.17400  1.000 39.10000  ? 86  PHE A CE1   1 
ATOM   610  C  CE2   . PHE A 1 86  ? 36.79900 50.30400 0.26400   1.000 44.19000  ? 86  PHE A CE2   1 
ATOM   611  C  CZ    . PHE A 1 86  ? 35.85100 50.93500 -0.51700  1.000 43.02000  ? 86  PHE A CZ    1 
ATOM   612  N  N     . LEU A 1 87  ? 31.83200 49.74200 3.80900   1.000 32.23000  ? 87  LEU A N     1 
ATOM   613  C  CA    . LEU A 1 87  ? 30.58600 50.45000 3.53700   1.000 31.72000  ? 87  LEU A CA    1 
ATOM   614  C  C     . LEU A 1 87  ? 30.25200 51.44200 4.64200   1.000 40.07000  ? 87  LEU A C     1 
ATOM   615  O  O     . LEU A 1 87  ? 29.64800 52.48600 4.37300   1.000 38.77000  ? 87  LEU A O     1 
ATOM   616  C  CB    . LEU A 1 87  ? 29.44100 49.45300 3.37700   1.000 32.61000  ? 87  LEU A CB    1 
ATOM   617  C  CG    . LEU A 1 87  ? 29.51100 48.52300 2.16900   1.000 34.82000  ? 87  LEU A CG    1 
ATOM   618  C  CD1   . LEU A 1 87  ? 28.41600 47.47600 2.26600   1.000 37.87000  ? 87  LEU A CD1   1 
ATOM   619  C  CD2   . LEU A 1 87  ? 29.39200 49.32000 0.88300   1.000 34.61000  ? 87  LEU A CD2   1 
ATOM   620  N  N     . GLY A 1 88  ? 30.61800 51.12700 5.88400   1.000 41.22000  ? 88  GLY A N     1 
ATOM   621  C  CA    . GLY A 1 88  ? 30.34500 52.04200 6.97600   1.000 45.86000  ? 88  GLY A CA    1 
ATOM   622  C  C     . GLY A 1 88  ? 31.14800 53.32400 6.87300   1.000 44.62000  ? 88  GLY A C     1 
ATOM   623  O  O     . GLY A 1 88  ? 30.65300 54.40500 7.20500   1.000 40.38000  ? 88  GLY A O     1 
ATOM   624  N  N     . LEU A 1 89  ? 32.39700 53.22200 6.41100   1.000 43.36000  ? 89  LEU A N     1 
ATOM   625  C  CA    . LEU A 1 89  ? 33.19700 54.42300 6.20300   1.000 42.15000  ? 89  LEU A CA    1 
ATOM   626  C  C     . LEU A 1 89  ? 32.57500 55.30400 5.12700   1.000 46.64000  ? 89  LEU A C     1 
ATOM   627  O  O     . LEU A 1 89  ? 32.45400 56.52400 5.29800   1.000 46.56000  ? 89  LEU A O     1 
ATOM   628  C  CB    . LEU A 1 89  ? 34.62900 54.03800 5.81900   1.000 42.98000  ? 89  LEU A CB    1 
ATOM   629  C  CG    . LEU A 1 89  ? 35.50300 53.39400 6.90000   1.000 51.66000  ? 89  LEU A CG    1 
ATOM   630  C  CD1   . LEU A 1 89  ? 36.82100 52.93900 6.28100   1.000 53.35000  ? 89  LEU A CD1   1 
ATOM   631  C  CD2   . LEU A 1 89  ? 35.75400 54.34000 8.06200   1.000 57.81000  ? 89  LEU A CD2   1 
ATOM   632  N  N     . LEU A 1 90  ? 32.16700 54.70400 4.00500   1.000 43.56000  ? 90  LEU A N     1 
ATOM   633  C  CA    . LEU A 1 90  ? 31.53500 55.47800 2.94300   1.000 47.35000  ? 90  LEU A CA    1 
ATOM   634  C  C     . LEU A 1 90  ? 30.31400 56.22300 3.46400   1.000 44.08000  ? 90  LEU A C     1 
ATOM   635  O  O     . LEU A 1 90  ? 30.08800 57.38600 3.11000   1.000 43.87000  ? 90  LEU A O     1 
ATOM   636  C  CB    . LEU A 1 90  ? 31.12200 54.56500 1.79200   1.000 52.23000  ? 90  LEU A CB    1 
ATOM   637  C  CG    . LEU A 1 90  ? 32.12000 54.22200 0.69200   1.000 56.49000  ? 90  LEU A CG    1 
ATOM   638  C  CD1   . LEU A 1 90  ? 31.39500 53.37000 -0.35000  1.000 52.20000  ? 90  LEU A CD1   1 
ATOM   639  C  CD2   . LEU A 1 90  ? 32.71900 55.45600 0.06000   1.000 64.58000  ? 90  LEU A CD2   1 
ATOM   640  N  N     . ALA A 1 91  ? 29.50400 55.56400 4.29300   1.000 44.33000  ? 91  ALA A N     1 
ATOM   641  C  CA    . ALA A 1 91  ? 28.28000 56.16300 4.80700   1.000 45.76000  ? 91  ALA A CA    1 
ATOM   642  C  C     . ALA A 1 91  ? 28.53100 57.12100 5.96200   1.000 48.62000  ? 91  ALA A C     1 
ATOM   643  O  O     . ALA A 1 91  ? 27.62900 57.88600 6.31700   1.000 44.76000  ? 91  ALA A O     1 
ATOM   644  C  CB    . ALA A 1 91  ? 27.31100 55.06600 5.25200   1.000 44.07000  ? 91  ALA A CB    1 
ATOM   645  N  N     . GLY A 1 92  ? 29.72200 57.09800 6.55400   1.000 54.61000  ? 92  GLY A N     1 
ATOM   646  C  CA    . GLY A 1 92  ? 30.04100 57.99300 7.64800   1.000 56.51000  ? 92  GLY A CA    1 
ATOM   647  C  C     . GLY A 1 92  ? 29.34800 57.62800 8.94400   1.000 56.25000  ? 92  GLY A C     1 
ATOM   648  O  O     . GLY A 1 92  ? 28.72700 58.48000 9.58500   1.000 57.01000  ? 92  GLY A O     1 
ATOM   649  N  N     . LEU A 1 93  ? 29.44800 56.36600 9.34500   1.000 55.38000  ? 93  LEU A N     1 
ATOM   650  C  CA    . LEU A 1 93  ? 28.82700 55.92000 10.58100  1.000 59.16000  ? 93  LEU A CA    1 
ATOM   651  C  C     . LEU A 1 93  ? 29.65200 56.35800 11.78500  1.000 60.51000  ? 93  LEU A C     1 
ATOM   652  O  O     . LEU A 1 93  ? 30.88500 56.36700 11.74300  1.000 57.98000  ? 93  LEU A O     1 
ATOM   653  C  CB    . LEU A 1 93  ? 28.68500 54.40000 10.58900  1.000 53.67000  ? 93  LEU A CB    1 
ATOM   654  C  CG    . LEU A 1 93  ? 27.57500 53.78100 9.74200   1.000 51.64000  ? 93  LEU A CG    1 
ATOM   655  C  CD1   . LEU A 1 93  ? 27.59300 52.26600 9.93600   1.000 47.94000  ? 93  LEU A CD1   1 
ATOM   656  C  CD2   . LEU A 1 93  ? 26.22000 54.35500 10.09500  1.000 54.30000  ? 93  LEU A CD2   1 
ATOM   657  N  N     . ASP A 1 94  ? 28.96000 56.73200 12.85700  1.000 65.61000  ? 94  ASP A N     1 
ATOM   658  C  CA    . ASP A 1 94  ? 29.62700 56.92000 14.13500  1.000 72.67000  ? 94  ASP A CA    1 
ATOM   659  C  C     . ASP A 1 94  ? 30.01700 55.55900 14.70900  1.000 75.50000  ? 94  ASP A C     1 
ATOM   660  O  O     . ASP A 1 94  ? 29.41000 54.52800 14.40400  1.000 69.67000  ? 94  ASP A O     1 
ATOM   661  C  CB    . ASP A 1 94  ? 28.72600 57.67400 15.10800  1.000 77.97000  ? 94  ASP A CB    1 
ATOM   662  C  CG    . ASP A 1 94  ? 27.80600 56.75500 15.87600  1.000 86.83000  ? 94  ASP A CG    1 
ATOM   663  O  OD1   . ASP A 1 94  ? 28.07400 55.53600 15.89300  1.000 90.67000  ? 94  ASP A OD1   1 
ATOM   664  O  OD2   . ASP A 1 94  ? 26.81500 57.24700 16.45500  1.000 91.17000  ? 94  ASP A OD2   1 
ATOM   665  N  N     . SER A 1 95  ? 31.04500 55.56500 15.55900  1.000 79.72000  ? 95  SER A N     1 
ATOM   666  C  CA    . SER A 1 95  ? 31.61200 54.31100 16.04300  1.000 76.70000  ? 95  SER A CA    1 
ATOM   667  C  C     . SER A 1 95  ? 30.58500 53.42100 16.73300  1.000 72.60000  ? 95  SER A C     1 
ATOM   668  O  O     . SER A 1 95  ? 30.85200 52.23100 16.93500  1.000 72.35000  ? 95  SER A O     1 
ATOM   669  C  CB    . SER A 1 95  ? 32.76900 54.59700 17.00400  1.000 78.53000  ? 95  SER A CB    1 
ATOM   670  O  OG    . SER A 1 95  ? 33.44600 53.40300 17.35800  1.000 81.75000  ? 95  SER A OG    1 
ATOM   671  N  N     . ARG A 1 96  ? 29.42100 53.96200 17.09600  1.000 73.75000  ? 96  ARG A N     1 
ATOM   672  C  CA    . ARG A 1 96  ? 28.39500 53.15100 17.74600  1.000 75.18000  ? 96  ARG A CA    1 
ATOM   673  C  C     . ARG A 1 96  ? 27.55100 52.40300 16.72300  1.000 66.05000  ? 96  ARG A C     1 
ATOM   674  O  O     . ARG A 1 96  ? 27.19800 51.23900 16.94200  1.000 52.71000  ? 96  ARG A O     1 
ATOM   675  C  CB    . ARG A 1 96  ? 27.51800 54.04300 18.62300  1.000 81.10000  ? 96  ARG A CB    1 
ATOM   676  C  CG    . ARG A 1 96  ? 26.02600 53.77000 18.54200  1.000 83.93000  ? 96  ARG A CG    1 
ATOM   677  C  CD    . ARG A 1 96  ? 25.62100 52.71500 19.56700  1.000 96.10000  ? 96  ARG A CD    1 
ATOM   678  N  NE    . ARG A 1 96  ? 24.17000 52.54200 19.64800  1.000 110.01000 ? 96  ARG A NE    1 
ATOM   679  C  CZ    . ARG A 1 96  ? 23.52600 52.00700 20.68400  1.000 115.86000 ? 96  ARG A CZ    1 
ATOM   680  N  NH1   . ARG A 1 96  ? 24.19800 51.58200 21.74700  1.000 114.08000 ? 96  ARG A NH1   1 
ATOM   681  N  NH2   . ARG A 1 96  ? 22.20400 51.89400 20.65800  1.000 116.26000 ? 96  ARG A NH2   1 
ATOM   682  N  N     . GLU A 1 97  ? 27.20600 53.05400 15.61000  1.000 67.11000  ? 97  GLU A N     1 
ATOM   683  C  CA    . GLU A 1 97  ? 26.48600 52.35900 14.54900  1.000 57.74000  ? 97  GLU A CA    1 
ATOM   684  C  C     . GLU A 1 97  ? 27.31100 51.20100 14.00300  1.000 52.59000  ? 97  GLU A C     1 
ATOM   685  O  O     . GLU A 1 97  ? 26.77100 50.13200 13.69400  1.000 47.14000  ? 97  GLU A O     1 
ATOM   686  C  CB    . GLU A 1 97  ? 26.12700 53.33900 13.43200  1.000 55.01000  ? 97  GLU A CB    1 
ATOM   687  N  N     . PHE A 1 98  ? 28.62700 51.39800 13.88000  1.000 51.07000  ? 98  PHE A N     1 
ATOM   688  C  CA    . PHE A 1 98  ? 29.50500 50.30900 13.47000  1.000 51.57000  ? 98  PHE A CA    1 
ATOM   689  C  C     . PHE A 1 98  ? 29.28100 49.06900 14.32400  1.000 43.49000  ? 98  PHE A C     1 
ATOM   690  O  O     . PHE A 1 98  ? 29.20100 47.94900 13.80400  1.000 32.79000  ? 98  PHE A O     1 
ATOM   691  C  CB    . PHE A 1 98  ? 30.96900 50.75100 13.57100  1.000 55.52000  ? 98  PHE A CB    1 
ATOM   692  C  CG    . PHE A 1 98  ? 31.48700 51.44500 12.34700  1.000 58.18000  ? 98  PHE A CG    1 
ATOM   693  C  CD1   . PHE A 1 98  ? 31.64400 50.75900 11.15400  1.000 53.43000  ? 98  PHE A CD1   1 
ATOM   694  C  CD2   . PHE A 1 98  ? 31.83000 52.78700 12.39000  1.000 59.04000  ? 98  PHE A CD2   1 
ATOM   695  C  CE1   . PHE A 1 98  ? 32.12600 51.39600 10.03000  1.000 48.19000  ? 98  PHE A CE1   1 
ATOM   696  C  CE2   . PHE A 1 98  ? 32.31200 53.43000 11.26700  1.000 59.84000  ? 98  PHE A CE2   1 
ATOM   697  C  CZ    . PHE A 1 98  ? 32.45900 52.73400 10.08500  1.000 50.56000  ? 98  PHE A CZ    1 
ATOM   698  N  N     . GLY A 1 99  ? 29.17900 49.25200 15.64200  1.000 47.29000  ? 99  GLY A N     1 
ATOM   699  C  CA    . GLY A 1 99  ? 29.07800 48.10800 16.53200  1.000 40.97000  ? 99  GLY A CA    1 
ATOM   700  C  C     . GLY A 1 99  ? 27.85500 47.25700 16.25700  1.000 38.15000  ? 99  GLY A C     1 
ATOM   701  O  O     . GLY A 1 99  ? 27.92700 46.02500 16.27900  1.000 39.94000  ? 99  GLY A O     1 
ATOM   702  N  N     . ILE A 1 100 ? 26.71600 47.89800 15.99100  1.000 41.32000  ? 100 ILE A N     1 
ATOM   703  C  CA    . ILE A 1 100 ? 25.48900 47.15100 15.72600  1.000 41.80000  ? 100 ILE A CA    1 
ATOM   704  C  C     . ILE A 1 100 ? 25.65700 46.27500 14.49100  1.000 37.86000  ? 100 ILE A C     1 
ATOM   705  O  O     . ILE A 1 100 ? 25.45500 45.05500 14.53800  1.000 37.48000  ? 100 ILE A O     1 
ATOM   706  C  CB    . ILE A 1 100 ? 24.29800 48.11400 15.57300  1.000 45.93000  ? 100 ILE A CB    1 
ATOM   707  C  CG1   . ILE A 1 100 ? 24.25200 49.09600 16.74500  1.000 55.61000  ? 100 ILE A CG1   1 
ATOM   708  C  CG2   . ILE A 1 100 ? 22.99500 47.33000 15.47900  1.000 43.97000  ? 100 ILE A CG2   1 
ATOM   709  C  CD1   . ILE A 1 100 ? 22.88000 49.68800 16.99800  1.000 64.40000  ? 100 ILE A CD1   1 
ATOM   710  N  N     . VAL A 1 101 ? 26.03800 46.88100 13.36400  1.000 36.17000  ? 101 VAL A N     1 
ATOM   711  C  CA    . VAL A 1 101 ? 26.05100 46.12800 12.11300  1.000 35.24000  ? 101 VAL A CA    1 
ATOM   712  C  C     . VAL A 1 101 ? 27.12000 45.04300 12.14900  1.000 30.05000  ? 101 VAL A C     1 
ATOM   713  O  O     . VAL A 1 101 ? 26.89400 43.91700 11.69000  1.000 33.12000  ? 101 VAL A O     1 
ATOM   714  C  CB    . VAL A 1 101 ? 26.23100 47.06700 10.90500  1.000 39.82000  ? 101 VAL A CB    1 
ATOM   715  C  CG1   . VAL A 1 101 ? 25.08200 48.06300 10.83400  1.000 42.14000  ? 101 VAL A CG1   1 
ATOM   716  C  CG2   . VAL A 1 101 ? 27.57300 47.78400 10.95700  1.000 40.72000  ? 101 VAL A CG2   1 
ATOM   717  N  N     . ILE A 1 102 ? 28.29700 45.35000 12.70100  1.000 29.71000  ? 102 ILE A N     1 
ATOM   718  C  CA    . ILE A 1 102 ? 29.34100 44.33400 12.77600  1.000 27.47000  ? 102 ILE A CA    1 
ATOM   719  C  C     . ILE A 1 102 ? 28.93200 43.21300 13.72500  1.000 27.48000  ? 102 ILE A C     1 
ATOM   720  O  O     . ILE A 1 102 ? 29.30700 42.05100 13.52000  1.000 28.41000  ? 102 ILE A O     1 
ATOM   721  C  CB    . ILE A 1 102 ? 30.68300 44.96800 13.18400  1.000 34.23000  ? 102 ILE A CB    1 
ATOM   722  C  CG1   . ILE A 1 102 ? 31.31800 45.65500 11.97000  1.000 44.33000  ? 102 ILE A CG1   1 
ATOM   723  C  CG2   . ILE A 1 102 ? 31.63200 43.90900 13.73200  1.000 33.54000  ? 102 ILE A CG2   1 
ATOM   724  C  CD1   . ILE A 1 102 ? 32.07800 46.92200 12.29700  1.000 51.49000  ? 102 ILE A CD1   1 
ATOM   725  N  N     . THR A 1 103 ? 28.15800 43.52900 14.76300  1.000 24.55000  ? 103 THR A N     1 
ATOM   726  C  CA    . THR A 1 103 ? 27.65300 42.47900 15.64100  1.000 27.59000  ? 103 THR A CA    1 
ATOM   727  C  C     . THR A 1 103 ? 26.63600 41.61200 14.90900  1.000 25.31000  ? 103 THR A C     1 
ATOM   728  O  O     . THR A 1 103 ? 26.70900 40.37900 14.95200  1.000 30.39000  ? 103 THR A O     1 
ATOM   729  C  CB    . THR A 1 103 ? 27.03200 43.08500 16.90000  1.000 32.97000  ? 103 THR A CB    1 
ATOM   730  O  OG1   . THR A 1 103 ? 28.05300 43.68500 17.70500  1.000 33.05000  ? 103 THR A OG1   1 
ATOM   731  C  CG2   . THR A 1 103 ? 26.31400 42.00800 17.70800  1.000 34.71000  ? 103 THR A CG2   1 
ATOM   732  N  N     . LEU A 1 104 ? 25.67400 42.24500 14.23400  1.000 27.90000  ? 104 LEU A N     1 
ATOM   733  C  CA    . LEU A 1 104 ? 24.71300 41.49500 13.43300  1.000 23.58000  ? 104 LEU A CA    1 
ATOM   734  C  C     . LEU A 1 104 ? 25.41900 40.61300 12.41000  1.000 21.54000  ? 104 LEU A C     1 
ATOM   735  O  O     . LEU A 1 104 ? 25.05300 39.44700 12.22400  1.000 24.03000  ? 104 LEU A O     1 
ATOM   736  C  CB    . LEU A 1 104 ? 23.75700 42.45600 12.72800  1.000 27.56000  ? 104 LEU A CB    1 
ATOM   737  C  CG    . LEU A 1 104 ? 22.57300 43.02200 13.51100  1.000 32.23000  ? 104 LEU A CG    1 
ATOM   738  C  CD1   . LEU A 1 104 ? 21.75100 43.94500 12.62300  1.000 37.38000  ? 104 LEU A CD1   1 
ATOM   739  C  CD2   . LEU A 1 104 ? 21.70800 41.90200 14.06100  1.000 33.41000  ? 104 LEU A CD2   1 
ATOM   740  N  N     . ASN A 1 105 ? 26.43000 41.15600 11.73000  1.000 23.73000  ? 105 ASN A N     1 
ATOM   741  C  CA    . ASN A 1 105 ? 27.15200 40.37100 10.73500  1.000 25.06000  ? 105 ASN A CA    1 
ATOM   742  C  C     . ASN A 1 105 ? 27.76900 39.12600 11.36100  1.000 23.84000  ? 105 ASN A C     1 
ATOM   743  O  O     . ASN A 1 105 ? 27.64000 38.01800 10.82700  1.000 24.96000  ? 105 ASN A O     1 
ATOM   744  C  CB    . ASN A 1 105 ? 28.23300 41.22600 10.07600  1.000 28.57000  ? 105 ASN A CB    1 
ATOM   745  C  CG    . ASN A 1 105 ? 28.87200 40.54200 8.88300   1.000 27.58000  ? 105 ASN A CG    1 
ATOM   746  O  OD1   . ASN A 1 105 ? 28.36300 40.61100 7.76600   1.000 28.76000  ? 105 ASN A OD1   1 
ATOM   747  N  ND2   . ASN A 1 105 ? 29.98900 39.86800 9.11700   1.000 28.40000  ? 105 ASN A ND2   1 
ATOM   748  N  N     . THR A 1 106 ? 28.44200 39.29000 12.50100  1.000 26.06000  ? 106 THR A N     1 
ATOM   749  C  CA    . THR A 1 106 ? 29.13500 38.16700 13.12200  1.000 27.06000  ? 106 THR A CA    1 
ATOM   750  C  C     . THR A 1 106 ? 28.15800 37.06500 13.51800  1.000 23.82000  ? 106 THR A C     1 
ATOM   751  O  O     . THR A 1 106 ? 28.49200 35.87600 13.45300  1.000 24.52000  ? 106 THR A O     1 
ATOM   752  C  CB    . THR A 1 106 ? 29.92400 38.63900 14.34100  1.000 34.75000  ? 106 THR A CB    1 
ATOM   753  O  OG1   . THR A 1 106 ? 30.87900 39.62900 13.94400  1.000 31.49000  ? 106 THR A OG1   1 
ATOM   754  C  CG2   . THR A 1 106 ? 30.64700 37.46800 14.99700  1.000 38.48000  ? 106 THR A CG2   1 
ATOM   755  N  N     . VAL A 1 107 ? 26.95000 37.43800 13.94000  1.000 23.75000  ? 107 VAL A N     1 
ATOM   756  C  CA    . VAL A 1 107 ? 25.95200 36.42700 14.27500  1.000 24.26000  ? 107 VAL A CA    1 
ATOM   757  C  C     . VAL A 1 107 ? 25.62000 35.59100 13.04800  1.000 25.98000  ? 107 VAL A C     1 
ATOM   758  O  O     . VAL A 1 107 ? 25.50000 34.36300 13.13000  1.000 26.47000  ? 107 VAL A O     1 
ATOM   759  C  CB    . VAL A 1 107 ? 24.69200 37.08600 14.86100  1.000 29.20000  ? 107 VAL A CB    1 
ATOM   760  C  CG1   . VAL A 1 107 ? 23.63200 36.02900 15.13400  1.000 29.09000  ? 107 VAL A CG1   1 
ATOM   761  C  CG2   . VAL A 1 107 ? 25.03600 37.85000 16.13500  1.000 33.38000  ? 107 VAL A CG2   1 
ATOM   762  N  N     . VAL A 1 108 ? 25.46300 36.24200 11.89300  1.000 22.05000  ? 108 VAL A N     1 
ATOM   763  C  CA    . VAL A 1 108 ? 25.19200 35.51100 10.65800  1.000 20.44000  ? 108 VAL A CA    1 
ATOM   764  C  C     . VAL A 1 108 ? 26.30100 34.50300 10.39100  1.000 21.96000  ? 108 VAL A C     1 
ATOM   765  O  O     . VAL A 1 108 ? 26.04800 33.31100 10.17300  1.000 20.56000  ? 108 VAL A O     1 
ATOM   766  C  CB    . VAL A 1 108 ? 25.04000 36.48500 9.47600   1.000 21.39000  ? 108 VAL A CB    1 
ATOM   767  C  CG1   . VAL A 1 108 ? 24.84100 35.70700 8.17800   1.000 24.32000  ? 108 VAL A CG1   1 
ATOM   768  C  CG2   . VAL A 1 108 ? 23.90100 37.46400 9.71700   1.000 20.52000  ? 108 VAL A CG2   1 
ATOM   769  N  N     . MET A 1 109 ? 27.55000 34.97800 10.40800  1.000 18.73000  ? 109 MET A N     1 
ATOM   770  C  CA    . MET A 1 109 ? 28.67900 34.13600 10.03700  1.000 20.38000  ? 109 MET A CA    1 
ATOM   771  C  C     . MET A 1 109 ? 28.85200 32.98500 11.01900  1.000 22.87000  ? 109 MET A C     1 
ATOM   772  O  O     . MET A 1 109 ? 29.04400 31.82900 10.61900  1.000 25.93000  ? 109 MET A O     1 
ATOM   773  C  CB    . MET A 1 109 ? 29.94600 35.00300 9.99300   1.000 25.50000  ? 109 MET A CB    1 
ATOM   774  C  CG    . MET A 1 109 ? 29.95900 35.98800 8.84000   1.000 25.13000  ? 109 MET A CG    1 
ATOM   775  S  SD    . MET A 1 109 ? 29.41900 35.16800 7.32400   1.000 37.55000  ? 109 MET A SD    1 
ATOM   776  C  CE    . MET A 1 109 ? 28.09400 36.20500 6.77700   1.000 20.00000  ? 109 MET A CE    1 
ATOM   777  N  N     . LEU A 1 110 ? 28.78900 33.27400 12.32100  1.000 21.41000  ? 110 LEU A N     1 
ATOM   778  C  CA    . LEU A 1 110 ? 28.97300 32.23300 13.32500  1.000 25.66000  ? 110 LEU A CA    1 
ATOM   779  C  C     . LEU A 1 110 ? 27.86500 31.18900 13.24600  1.000 24.36000  ? 110 LEU A C     1 
ATOM   780  O  O     . LEU A 1 110 ? 28.12800 29.98600 13.34900  1.000 28.16000  ? 110 LEU A O     1 
ATOM   781  C  CB    . LEU A 1 110 ? 29.02300 32.85600 14.72000  1.000 30.58000  ? 110 LEU A CB    1 
ATOM   782  C  CG    . LEU A 1 110 ? 30.27000 33.67900 15.04100  1.000 34.99000  ? 110 LEU A CG    1 
ATOM   783  C  CD1   . LEU A 1 110 ? 30.23200 34.16000 16.48500  1.000 40.27000  ? 110 LEU A CD1   1 
ATOM   784  C  CD2   . LEU A 1 110 ? 31.53400 32.87400 14.77900  1.000 40.33000  ? 110 LEU A CD2   1 
ATOM   785  N  N     . ALA A 1 111 ? 26.61500 31.63000 13.07400  1.000 31.45000  ? 111 ALA A N     1 
ATOM   786  C  CA    . ALA A 1 111 ? 25.51100 30.68500 12.95700  1.000 27.97000  ? 111 ALA A CA    1 
ATOM   787  C  C     . ALA A 1 111 ? 25.70300 29.75800 11.76400  1.000 24.37000  ? 111 ALA A C     1 
ATOM   788  O  O     . ALA A 1 111 ? 25.43300 28.55400 11.85300  1.000 27.65000  ? 111 ALA A O     1 
ATOM   789  C  CB    . ALA A 1 111 ? 24.18600 31.43800 12.83500  1.000 31.62000  ? 111 ALA A CB    1 
ATOM   790  N  N     . GLY A 1 112 ? 26.16000 30.29900 10.63600  1.000 24.63000  ? 112 GLY A N     1 
ATOM   791  C  CA    . GLY A 1 112 ? 26.39700 29.45700 9.47700   1.000 26.14000  ? 112 GLY A CA    1 
ATOM   792  C  C     . GLY A 1 112 ? 27.52400 28.47200 9.71300   1.000 26.76000  ? 112 GLY A C     1 
ATOM   793  O  O     . GLY A 1 112 ? 27.42400 27.29800 9.34500   1.000 25.21000  ? 112 GLY A O     1 
ATOM   794  N  N     . PHE A 1 113 ? 28.60900 28.93600 10.33100  1.000 29.06000  ? 113 PHE A N     1 
ATOM   795  C  CA    . PHE A 1 113 ? 29.72600 28.05400 10.65600  1.000 32.89000  ? 113 PHE A CA    1 
ATOM   796  C  C     . PHE A 1 113 ? 29.27900 26.92900 11.58100  1.000 35.01000  ? 113 PHE A C     1 
ATOM   797  O  O     . PHE A 1 113 ? 29.60700 25.75800 11.36000  1.000 32.59000  ? 113 PHE A O     1 
ATOM   798  C  CB    . PHE A 1 113 ? 30.84500 28.87800 11.29500  1.000 34.55000  ? 113 PHE A CB    1 
ATOM   799  C  CG    . PHE A 1 113 ? 32.15000 28.14500 11.43200  1.000 35.89000  ? 113 PHE A CG    1 
ATOM   800  C  CD1   . PHE A 1 113 ? 32.38900 26.96700 10.74500  1.000 36.48000  ? 113 PHE A CD1   1 
ATOM   801  C  CD2   . PHE A 1 113 ? 33.14400 28.64900 12.25200  1.000 48.68000  ? 113 PHE A CD2   1 
ATOM   802  C  CE1   . PHE A 1 113 ? 33.59200 26.30600 10.87600  1.000 45.60000  ? 113 PHE A CE1   1 
ATOM   803  C  CE2   . PHE A 1 113 ? 34.34900 27.99200 12.38600  1.000 56.21000  ? 113 PHE A CE2   1 
ATOM   804  C  CZ    . PHE A 1 113 ? 34.57300 26.82000 11.69900  1.000 52.56000  ? 113 PHE A CZ    1 
ATOM   805  N  N     . ALA A 1 114 ? 28.52500 27.26800 12.62800  1.000 34.86000  ? 114 ALA A N     1 
ATOM   806  C  CA    . ALA A 1 114 ? 28.08500 26.25800 13.58100  1.000 34.94000  ? 114 ALA A CA    1 
ATOM   807  C  C     . ALA A 1 114 ? 27.11700 25.27500 12.93500  1.000 31.46000  ? 114 ALA A C     1 
ATOM   808  O  O     . ALA A 1 114 ? 27.23700 24.05900 13.12600  1.000 30.98000  ? 114 ALA A O     1 
ATOM   809  C  CB    . ALA A 1 114 ? 27.44000 26.92500 14.79300  1.000 33.64000  ? 114 ALA A CB    1 
ATOM   810  N  N     . GLY A 1 115 ? 26.15200 25.78200 12.16300  1.000 32.46000  ? 115 GLY A N     1 
ATOM   811  C  CA    . GLY A 1 115 ? 25.20100 24.89600 11.51100  1.000 32.69000  ? 115 GLY A CA    1 
ATOM   812  C  C     . GLY A 1 115 ? 25.86100 23.94300 10.53500  1.000 32.17000  ? 115 GLY A C     1 
ATOM   813  O  O     . GLY A 1 115 ? 25.46200 22.78300 10.41800  1.000 33.32000  ? 115 GLY A O     1 
ATOM   814  N  N     . ALA A 1 116 ? 26.88100 24.41500 9.81800   1.000 30.56000  ? 116 ALA A N     1 
ATOM   815  C  CA    . ALA A 1 116 ? 27.59600 23.52600 8.91000   1.000 37.92000  ? 116 ALA A CA    1 
ATOM   816  C  C     . ALA A 1 116 ? 28.28200 22.39600 9.66800   1.000 38.55000  ? 116 ALA A C     1 
ATOM   817  O  O     . ALA A 1 116 ? 28.36600 21.27000 9.16300   1.000 37.73000  ? 116 ALA A O     1 
ATOM   818  C  CB    . ALA A 1 116 ? 28.62000 24.31500 8.09200   1.000 38.56000  ? 116 ALA A CB    1 
ATOM   819  N  N     . MET A 1 117 ? 28.76000 22.66800 10.88000  1.000 39.30000  ? 117 MET A N     1 
ATOM   820  C  CA    . MET A 1 117 ? 29.54700 21.71200 11.64500  1.000 40.00000  ? 117 MET A CA    1 
ATOM   821  C  C     . MET A 1 117 ? 28.70500 20.79100 12.51900  1.000 42.68000  ? 117 MET A C     1 
ATOM   822  O  O     . MET A 1 117 ? 29.27000 19.94900 13.22500  1.000 41.14000  ? 117 MET A O     1 
ATOM   823  C  CB    . MET A 1 117 ? 30.55200 22.45400 12.53500  1.000 42.82000  ? 117 MET A CB    1 
ATOM   824  C  CG    . MET A 1 117 ? 31.67800 23.14600 11.78600  1.000 48.22000  ? 117 MET A CG    1 
ATOM   825  S  SD    . MET A 1 117 ? 32.83400 21.98400 11.03300  1.000 61.78000  ? 117 MET A SD    1 
ATOM   826  C  CE    . MET A 1 117 ? 33.63600 21.30700 12.48500  1.000 69.25000  ? 117 MET A CE    1 
ATOM   827  N  N     . VAL A 1 118 ? 27.38700 20.92200 12.49300  1.000 43.53000  ? 118 VAL A N     1 
ATOM   828  C  CA    . VAL A 1 118 ? 26.48800 20.12200 13.32800  1.000 41.50000  ? 118 VAL A CA    1 
ATOM   829  C  C     . VAL A 1 118 ? 25.82200 19.07900 12.45200  1.000 44.38000  ? 118 VAL A C     1 
ATOM   830  O  O     . VAL A 1 118 ? 25.21700 19.43700 11.42800  1.000 42.53000  ? 118 VAL A O     1 
ATOM   831  C  CB    . VAL A 1 118 ? 25.43400 21.00700 14.02100  1.000 44.42000  ? 118 VAL A CB    1 
ATOM   832  C  CG1   . VAL A 1 118 ? 24.25600 20.15900 14.48400  1.000 45.15000  ? 118 VAL A CG1   1 
ATOM   833  C  CG2   . VAL A 1 118 ? 26.05300 21.76500 15.18500  1.000 45.23000  ? 118 VAL A CG2   1 
ATOM   834  N  N     . PRO A 1 119 ? 25.87400 17.78500 12.80800  1.000 49.57000  ? 119 PRO A N     1 
ATOM   835  C  CA    . PRO A 1 119 ? 25.32400 16.76000 11.91200  1.000 51.77000  ? 119 PRO A CA    1 
ATOM   836  C  C     . PRO A 1 119 ? 23.80500 16.67100 11.92400  1.000 49.85000  ? 119 PRO A C     1 
ATOM   837  O  O     . PRO A 1 119 ? 23.19000 16.38100 10.89200  1.000 48.94000  ? 119 PRO A O     1 
ATOM   838  C  CB    . PRO A 1 119 ? 25.95300 15.45200 12.42200  1.000 55.20000  ? 119 PRO A CB    1 
ATOM   839  C  CG    . PRO A 1 119 ? 26.66200 15.77800 13.70800  1.000 54.98000  ? 119 PRO A CG    1 
ATOM   840  C  CD    . PRO A 1 119 ? 26.44500 17.21700 14.04500  1.000 53.98000  ? 119 PRO A CD    1 
ATOM   841  N  N     . GLY A 1 120 ? 23.18800 16.91600 13.07900  1.000 49.43000  ? 120 GLY A N     1 
ATOM   842  C  CA    . GLY A 1 120 ? 21.76200 16.73200 13.22900  1.000 51.86000  ? 120 GLY A CA    1 
ATOM   843  C  C     . GLY A 1 120 ? 20.94500 17.87800 12.66700  1.000 52.45000  ? 120 GLY A C     1 
ATOM   844  O  O     . GLY A 1 120 ? 21.45700 18.83900 12.09200  1.000 48.90000  ? 120 GLY A O     1 
ATOM   845  N  N     . ILE A 1 121 ? 19.62700 17.76800 12.85600  1.000 51.85000  ? 121 ILE A N     1 
ATOM   846  C  CA    . ILE A 1 121 ? 18.71000 18.76400 12.31700  1.000 54.71000  ? 121 ILE A CA    1 
ATOM   847  C  C     . ILE A 1 121 ? 18.78300 20.07600 13.08500  1.000 49.07000  ? 121 ILE A C     1 
ATOM   848  O  O     . ILE A 1 121 ? 18.29200 21.10100 12.59400  1.000 44.11000  ? 121 ILE A O     1 
ATOM   849  C  CB    . ILE A 1 121 ? 17.26900 18.23000 12.32500  1.000 67.63000  ? 121 ILE A CB    1 
ATOM   850  C  CG1   . ILE A 1 121 ? 17.02800 17.38300 13.57300  1.000 73.74000  ? 121 ILE A CG1   1 
ATOM   851  C  CG2   . ILE A 1 121 ? 16.99800 17.40200 11.08100  1.000 76.33000  ? 121 ILE A CG2   1 
ATOM   852  C  CD1   . ILE A 1 121 ? 17.02800 18.17100 14.85200  1.000 94.94000  ? 121 ILE A CD1   1 
ATOM   853  N  N     . GLU A 1 122 ? 19.37800 20.07700 14.28200  1.000 48.17000  ? 122 GLU A N     1 
ATOM   854  C  CA    . GLU A 1 122 ? 19.61700 21.33300 14.97500  1.000 44.13000  ? 122 GLU A CA    1 
ATOM   855  C  C     . GLU A 1 122 ? 20.34100 22.33700 14.08600  1.000 42.40000  ? 122 GLU A C     1 
ATOM   856  O  O     . GLU A 1 122 ? 20.29000 23.54200 14.35400  1.000 44.16000  ? 122 GLU A O     1 
ATOM   857  C  CB    . GLU A 1 122 ? 20.44800 21.11700 16.24500  1.000 48.02000  ? 122 GLU A CB    1 
ATOM   858  C  CG    . GLU A 1 122 ? 20.15800 19.82700 16.98700  1.000 54.65000  ? 122 GLU A CG    1 
ATOM   859  C  CD    . GLU A 1 122 ? 21.02800 18.68300 16.51100  1.000 64.26000  ? 122 GLU A CD    1 
ATOM   860  O  OE1   . GLU A 1 122 ? 22.26900 18.82800 16.52600  1.000 69.46000  ? 122 GLU A OE1   1 
ATOM   861  O  OE2   . GLU A 1 122 ? 20.46600 17.64200 16.11000  1.000 69.31000  ? 122 GLU A OE2   1 
ATOM   862  N  N     . ARG A 1 123 ? 21.02700 21.86200 13.04300  1.000 36.90000  ? 123 ARG A N     1 
ATOM   863  C  CA    . ARG A 1 123 ? 21.75600 22.76800 12.16200  1.000 37.80000  ? 123 ARG A CA    1 
ATOM   864  C  C     . ARG A 1 123 ? 20.81300 23.69900 11.41600  1.000 33.06000  ? 123 ARG A C     1 
ATOM   865  O  O     . ARG A 1 123 ? 21.19400 24.82600 11.08300  1.000 36.73000  ? 123 ARG A O     1 
ATOM   866  C  CB    . ARG A 1 123 ? 22.61100 21.96700 11.18000  1.000 40.10000  ? 123 ARG A CB    1 
ATOM   867  C  CG    . ARG A 1 123 ? 21.84900 21.30500 10.04100  1.000 42.24000  ? 123 ARG A CG    1 
ATOM   868  C  CD    . ARG A 1 123 ? 22.75500 20.32200 9.30300   1.000 48.82000  ? 123 ARG A CD    1 
ATOM   869  N  NE    . ARG A 1 123 ? 22.17500 19.84800 8.04900   1.000 52.04000  ? 123 ARG A NE    1 
ATOM   870  C  CZ    . ARG A 1 123 ? 21.26300 18.88400 7.96300   1.000 62.12000  ? 123 ARG A CZ    1 
ATOM   871  N  NH1   . ARG A 1 123 ? 20.81900 18.28800 9.06100   1.000 66.36000  ? 123 ARG A NH1   1 
ATOM   872  N  NH2   . ARG A 1 123 ? 20.79500 18.51700 6.77700   1.000 62.53000  ? 123 ARG A NH2   1 
ATOM   873  N  N     . TYR A 1 124 ? 19.58400 23.25600 11.14200  1.000 26.50000  ? 124 TYR A N     1 
ATOM   874  C  CA    . TYR A 1 124 ? 18.62100 24.15800 10.52100  1.000 32.85000  ? 124 TYR A CA    1 
ATOM   875  C  C     . TYR A 1 124 ? 18.14800 25.22200 11.50200  1.000 33.59000  ? 124 TYR A C     1 
ATOM   876  O  O     . TYR A 1 124 ? 17.76900 26.32300 11.08800  1.000 29.33000  ? 124 TYR A O     1 
ATOM   877  C  CB    . TYR A 1 124 ? 17.43100 23.37100 9.97600   1.000 38.78000  ? 124 TYR A CB    1 
ATOM   878  C  CG    . TYR A 1 124 ? 17.74700 22.55700 8.74200   1.000 44.62000  ? 124 TYR A CG    1 
ATOM   879  C  CD1   . TYR A 1 124 ? 18.05100 23.17200 7.53500   1.000 43.09000  ? 124 TYR A CD1   1 
ATOM   880  C  CD2   . TYR A 1 124 ? 17.73700 21.17200 8.78900   1.000 51.88000  ? 124 TYR A CD2   1 
ATOM   881  C  CE1   . TYR A 1 124 ? 18.33600 22.42600 6.40600   1.000 49.20000  ? 124 TYR A CE1   1 
ATOM   882  C  CE2   . TYR A 1 124 ? 18.02100 20.41700 7.66900   1.000 57.68000  ? 124 TYR A CE2   1 
ATOM   883  C  CZ    . TYR A 1 124 ? 18.32000 21.04800 6.48000   1.000 57.07000  ? 124 TYR A CZ    1 
ATOM   884  O  OH    . TYR A 1 124 ? 18.60300 20.29200 5.36600   1.000 62.21000  ? 124 TYR A OH    1 
ATOM   885  N  N     . ALA A 1 125 ? 18.15600 24.91300 12.80100  1.000 31.45000  ? 125 ALA A N     1 
ATOM   886  C  CA    . ALA A 1 125 ? 17.85300 25.92800 13.80300  1.000 30.44000  ? 125 ALA A CA    1 
ATOM   887  C  C     . ALA A 1 125 ? 18.93300 27.00200 13.83200  1.000 26.78000  ? 125 ALA A C     1 
ATOM   888  O  O     . ALA A 1 125 ? 18.63200 28.19100 13.99000  1.000 23.32000  ? 125 ALA A O     1 
ATOM   889  C  CB    . ALA A 1 125 ? 17.70200 25.28300 15.18000  1.000 33.46000  ? 125 ALA A CB    1 
ATOM   890  N  N     . LEU A 1 126 ? 20.19600 26.60300 13.68400  1.000 23.51000  ? 126 LEU A N     1 
ATOM   891  C  CA    . LEU A 1 126 ? 21.26900 27.58800 13.59700  1.000 25.04000  ? 126 LEU A CA    1 
ATOM   892  C  C     . LEU A 1 126 ? 21.15700 28.39700 12.31000  1.000 23.31000  ? 126 LEU A C     1 
ATOM   893  O  O     . LEU A 1 126 ? 21.36200 29.61600 12.31700  1.000 26.28000  ? 126 LEU A O     1 
ATOM   894  C  CB    . LEU A 1 126 ? 22.62500 26.89100 13.69200  1.000 30.42000  ? 126 LEU A CB    1 
ATOM   895  C  CG    . LEU A 1 126 ? 22.86800 26.22800 15.05100  1.000 32.64000  ? 126 LEU A CG    1 
ATOM   896  C  CD1   . LEU A 1 126 ? 23.96700 25.18000 14.98100  1.000 37.28000  ? 126 LEU A CD1   1 
ATOM   897  C  CD2   . LEU A 1 126 ? 23.19600 27.29100 16.09800  1.000 30.25000  ? 126 LEU A CD2   1 
ATOM   898  N  N     . PHE A 1 127 ? 20.81900 27.73900 11.20000  1.000 29.07000  ? 127 PHE A N     1 
ATOM   899  C  CA    . PHE A 1 127 ? 20.66400 28.45600 9.93900   1.000 25.75000  ? 127 PHE A CA    1 
ATOM   900  C  C     . PHE A 1 127 ? 19.56900 29.51000 10.04100  1.000 19.04000  ? 127 PHE A C     1 
ATOM   901  O  O     . PHE A 1 127 ? 19.73900 30.64100 9.57200   1.000 23.84000  ? 127 PHE A O     1 
ATOM   902  C  CB    . PHE A 1 127 ? 20.35400 27.47300 8.81000   1.000 33.33000  ? 127 PHE A CB    1 
ATOM   903  C  CG    . PHE A 1 127 ? 19.90600 28.13300 7.53800   1.000 31.55000  ? 127 PHE A CG    1 
ATOM   904  C  CD1   . PHE A 1 127 ? 20.83300 28.61700 6.63400   1.000 28.62000  ? 127 PHE A CD1   1 
ATOM   905  C  CD2   . PHE A 1 127 ? 18.55900 28.27000 7.24900   1.000 32.59000  ? 127 PHE A CD2   1 
ATOM   906  C  CE1   . PHE A 1 127 ? 20.42700 29.22700 5.46200   1.000 33.14000  ? 127 PHE A CE1   1 
ATOM   907  C  CE2   . PHE A 1 127 ? 18.14600 28.87600 6.08300   1.000 35.85000  ? 127 PHE A CE2   1 
ATOM   908  C  CZ    . PHE A 1 127 ? 19.08200 29.35800 5.18600   1.000 36.78000  ? 127 PHE A CZ    1 
ATOM   909  N  N     . GLY A 1 128 ? 18.43300 29.15500 10.64300  1.000 25.63000  ? 128 GLY A N     1 
ATOM   910  C  CA    . GLY A 1 128 ? 17.35600 30.11800 10.78700  1.000 26.91000  ? 128 GLY A CA    1 
ATOM   911  C  C     . GLY A 1 128 ? 17.76700 31.34200 11.58100  1.000 27.48000  ? 128 GLY A C     1 
ATOM   912  O  O     . GLY A 1 128 ? 17.35800 32.46400 11.27000  1.000 29.69000  ? 128 GLY A O     1 
ATOM   913  N  N     . MET A 1 129 ? 18.58800 31.15100 12.61300  1.000 25.87000  ? 129 MET A N     1 
ATOM   914  C  CA    . MET A 1 129 ? 19.00900 32.29900 13.40500  1.000 26.48000  ? 129 MET A CA    1 
ATOM   915  C  C     . MET A 1 129 ? 19.89700 33.23200 12.59200  1.000 23.59000  ? 129 MET A C     1 
ATOM   916  O  O     . MET A 1 129 ? 19.77500 34.45900 12.69000  1.000 22.15000  ? 129 MET A O     1 
ATOM   917  C  CB    . MET A 1 129 ? 19.73400 31.85000 14.66800  1.000 31.36000  ? 129 MET A CB    1 
ATOM   918  C  CG    . MET A 1 129 ? 19.60900 32.89400 15.77000  1.000 45.85000  ? 129 MET A CG    1 
ATOM   919  S  SD    . MET A 1 129 ? 20.43000 32.47100 17.29300  1.000 52.76000  ? 129 MET A SD    1 
ATOM   920  C  CE    . MET A 1 129 ? 22.12700 32.38700 16.76000  1.000 50.79000  ? 129 MET A CE    1 
ATOM   921  N  N     . GLY A 1 130 ? 20.80200 32.67300 11.79100  1.000 18.80000  ? 130 GLY A N     1 
ATOM   922  C  CA    . GLY A 1 130 ? 21.56700 33.50500 10.87900  1.000 21.85000  ? 130 GLY A CA    1 
ATOM   923  C  C     . GLY A 1 130 ? 20.67900 34.25400 9.90400   1.000 21.25000  ? 130 GLY A C     1 
ATOM   924  O  O     . GLY A 1 130 ? 20.91100 35.42900 9.61300   1.000 22.79000  ? 130 GLY A O     1 
ATOM   925  N  N     . ALA A 1 131 ? 19.63700 33.58600 9.40300   1.000 22.24000  ? 131 ALA A N     1 
ATOM   926  C  CA    . ALA A 1 131 ? 18.71200 34.24800 8.49100   1.000 24.18000  ? 131 ALA A CA    1 
ATOM   927  C  C     . ALA A 1 131 ? 18.04100 35.44200 9.15800   1.000 23.70000  ? 131 ALA A C     1 
ATOM   928  O  O     . ALA A 1 131 ? 17.93000 36.51500 8.55500   1.000 26.54000  ? 131 ALA A O     1 
ATOM   929  C  CB    . ALA A 1 131 ? 17.65800 33.25500 7.99800   1.000 26.76000  ? 131 ALA A CB    1 
ATOM   930  N  N     . VAL A 1 132 ? 17.58900 35.27700 10.40300  1.000 25.07000  ? 132 VAL A N     1 
ATOM   931  C  CA    . VAL A 1 132 ? 16.91500 36.37500 11.08900  1.000 24.17000  ? 132 VAL A CA    1 
ATOM   932  C  C     . VAL A 1 132 ? 17.86300 37.55500 11.24800  1.000 21.02000  ? 132 VAL A C     1 
ATOM   933  O  O     . VAL A 1 132 ? 17.50000 38.70700 10.97800  1.000 22.43000  ? 132 VAL A O     1 
ATOM   934  C  CB    . VAL A 1 132 ? 16.36700 35.91000 12.45000  1.000 27.36000  ? 132 VAL A CB    1 
ATOM   935  C  CG1   . VAL A 1 132 ? 15.92000 37.11100 13.27000  1.000 34.28000  ? 132 VAL A CG1   1 
ATOM   936  C  CG2   . VAL A 1 132 ? 15.22400 34.93000 12.25700  1.000 30.43000  ? 132 VAL A CG2   1 
ATOM   937  N  N     . ALA A 1 133 ? 19.09400 37.28500 11.68800  1.000 23.69000  ? 133 ALA A N     1 
ATOM   938  C  CA    . ALA A 1 133 ? 20.07100 38.35200 11.86400  1.000 23.18000  ? 133 ALA A CA    1 
ATOM   939  C  C     . ALA A 1 133 ? 20.45000 38.98900 10.53600  1.000 24.76000  ? 133 ALA A C     1 
ATOM   940  O  O     . ALA A 1 133 ? 20.76700 40.18300 10.48900  1.000 23.94000  ? 133 ALA A O     1 
ATOM   941  C  CB    . ALA A 1 133 ? 21.32100 37.81300 12.55700  1.000 20.56000  ? 133 ALA A CB    1 
ATOM   942  N  N     . PHE A 1 134 ? 20.43300 38.21200 9.45400   1.000 24.05000  ? 134 PHE A N     1 
ATOM   943  C  CA    . PHE A 1 134 ? 20.74700 38.76900 8.14500   1.000 25.27000  ? 134 PHE A CA    1 
ATOM   944  C  C     . PHE A 1 134 ? 19.70200 39.79900 7.72700   1.000 22.21000  ? 134 PHE A C     1 
ATOM   945  O  O     . PHE A 1 134 ? 20.04200 40.84400 7.16100   1.000 25.58000  ? 134 PHE A O     1 
ATOM   946  C  CB    . PHE A 1 134 ? 20.85000 37.64400 7.11600   1.000 23.39000  ? 134 PHE A CB    1 
ATOM   947  C  CG    . PHE A 1 134 ? 21.19900 38.11500 5.74100   1.000 23.53000  ? 134 PHE A CG    1 
ATOM   948  C  CD1   . PHE A 1 134 ? 22.45600 38.62900 5.46600   1.000 20.07000  ? 134 PHE A CD1   1 
ATOM   949  C  CD2   . PHE A 1 134 ? 20.27000 38.04300 4.72100   1.000 25.53000  ? 134 PHE A CD2   1 
ATOM   950  C  CE1   . PHE A 1 134 ? 22.77600 39.06400 4.19800   1.000 23.82000  ? 134 PHE A CE1   1 
ATOM   951  C  CE2   . PHE A 1 134 ? 20.58300 38.47400 3.44900   1.000 26.01000  ? 134 PHE A CE2   1 
ATOM   952  C  CZ    . PHE A 1 134 ? 21.83800 38.98800 3.18600   1.000 25.33000  ? 134 PHE A CZ    1 
ATOM   953  N  N     . LEU A 1 135 ? 18.42700 39.52800 8.01100   1.000 22.34000  ? 135 LEU A N     1 
ATOM   954  C  CA    . LEU A 1 135 ? 17.38600 40.49800 7.68800   1.000 26.82000  ? 135 LEU A CA    1 
ATOM   955  C  C     . LEU A 1 135 ? 17.60900 41.80600 8.43500   1.000 29.24000  ? 135 LEU A C     1 
ATOM   956  O  O     . LEU A 1 135 ? 17.40100 42.89300 7.88100   1.000 29.83000  ? 135 LEU A O     1 
ATOM   957  C  CB    . LEU A 1 135 ? 16.01000 39.91900 8.01000   1.000 31.01000  ? 135 LEU A CB    1 
ATOM   958  C  CG    . LEU A 1 135 ? 15.59500 38.77200 7.08800   1.000 39.56000  ? 135 LEU A CG    1 
ATOM   959  C  CD1   . LEU A 1 135 ? 14.35200 38.07500 7.61100   1.000 41.64000  ? 135 LEU A CD1   1 
ATOM   960  C  CD2   . LEU A 1 135 ? 15.37200 39.27500 5.66700   1.000 42.78000  ? 135 LEU A CD2   1 
ATOM   961  N  N     . GLY A 1 136 ? 18.04400 41.72600 9.69200   1.000 31.59000  ? 136 GLY A N     1 
ATOM   962  C  CA    . GLY A 1 136 ? 18.37900 42.93800 10.41800  1.000 29.05000  ? 136 GLY A CA    1 
ATOM   963  C  C     . GLY A 1 136 ? 19.55000 43.67700 9.79900   1.000 27.38000  ? 136 GLY A C     1 
ATOM   964  O  O     . GLY A 1 136 ? 19.55900 44.91000 9.74000   1.000 27.48000  ? 136 GLY A O     1 
ATOM   965  N  N     . LEU A 1 137 ? 20.55200 42.93500 9.32400   1.000 27.19000  ? 137 LEU A N     1 
ATOM   966  C  CA    . LEU A 1 137 ? 21.68800 43.56500 8.66300   1.000 28.24000  ? 137 LEU A CA    1 
ATOM   967  C  C     . LEU A 1 137 ? 21.25500 44.27300 7.38500   1.000 26.95000  ? 137 LEU A C     1 
ATOM   968  O  O     . LEU A 1 137 ? 21.71700 45.38300 7.09200   1.000 25.07000  ? 137 LEU A O     1 
ATOM   969  C  CB    . LEU A 1 137 ? 22.75800 42.51700 8.35600   1.000 27.63000  ? 137 LEU A CB    1 
ATOM   970  C  CG    . LEU A 1 137 ? 24.02100 43.01000 7.64900   1.000 32.20000  ? 137 LEU A CG    1 
ATOM   971  C  CD1   . LEU A 1 137 ? 24.79100 43.95500 8.55100   1.000 37.15000  ? 137 LEU A CD1   1 
ATOM   972  C  CD2   . LEU A 1 137 ? 24.89500 41.83100 7.22900   1.000 33.26000  ? 137 LEU A CD2   1 
ATOM   973  N  N     . VAL A 1 138 ? 20.37400 43.64100 6.60600   1.000 30.90000  ? 138 VAL A N     1 
ATOM   974  C  CA    . VAL A 1 138 ? 19.88500 44.26800 5.38300   1.000 28.97000  ? 138 VAL A CA    1 
ATOM   975  C  C     . VAL A 1 138 ? 19.13600 45.55100 5.71300   1.000 29.61000  ? 138 VAL A C     1 
ATOM   976  O  O     . VAL A 1 138 ? 19.26700 46.56200 5.01300   1.000 33.04000  ? 138 VAL A O     1 
ATOM   977  C  CB    . VAL A 1 138 ? 18.99700 43.29000 4.59200   1.000 29.63000  ? 138 VAL A CB    1 
ATOM   978  C  CG1   . VAL A 1 138 ? 18.25700 44.02700 3.47800   1.000 31.89000  ? 138 VAL A CG1   1 
ATOM   979  C  CG2   . VAL A 1 138 ? 19.83100 42.15500 4.02700   1.000 25.55000  ? 138 VAL A CG2   1 
ATOM   980  N  N     . TYR A 1 139 ? 18.34200 45.53400 6.78800   1.000 33.11000  ? 139 TYR A N     1 
ATOM   981  C  CA    . TYR A 1 139 ? 17.63200 46.74500 7.17700   1.000 36.15000  ? 139 TYR A CA    1 
ATOM   982  C  C     . TYR A 1 139 ? 18.60400 47.89100 7.42900   1.000 39.81000  ? 139 TYR A C     1 
ATOM   983  O  O     . TYR A 1 139 ? 18.35100 49.03100 7.02500   1.000 40.66000  ? 139 TYR A O     1 
ATOM   984  C  CB    . TYR A 1 139 ? 16.78800 46.51100 8.42800   1.000 41.03000  ? 139 TYR A CB    1 
ATOM   985  C  CG    . TYR A 1 139 ? 16.30300 47.81500 9.04000   1.000 51.63000  ? 139 TYR A CG    1 
ATOM   986  C  CD1   . TYR A 1 139 ? 15.14800 48.43800 8.57900   1.000 54.05000  ? 139 TYR A CD1   1 
ATOM   987  C  CD2   . TYR A 1 139 ? 16.98700 48.40500 10.09500  1.000 58.41000  ? 139 TYR A CD2   1 
ATOM   988  C  CE1   . TYR A 1 139 ? 14.69700 49.61900 9.14700   1.000 60.94000  ? 139 TYR A CE1   1 
ATOM   989  C  CE2   . TYR A 1 139 ? 16.54500 49.58500 10.66600  1.000 63.68000  ? 139 TYR A CE2   1 
ATOM   990  C  CZ    . TYR A 1 139 ? 15.40000 50.18700 10.18900  1.000 68.36000  ? 139 TYR A CZ    1 
ATOM   991  O  OH    . TYR A 1 139 ? 14.95800 51.36100 10.75600  1.000 85.37000  ? 139 TYR A OH    1 
ATOM   992  N  N     . TYR A 1 140 ? 19.71700 47.61200 8.11000   1.000 37.56000  ? 140 TYR A N     1 
ATOM   993  C  CA    . TYR A 1 140 ? 20.64800 48.68800 8.43300   1.000 37.05000  ? 140 TYR A CA    1 
ATOM   994  C  C     . TYR A 1 140 ? 21.34700 49.20400 7.18400   1.000 41.54000  ? 140 TYR A C     1 
ATOM   995  O  O     . TYR A 1 140 ? 21.58400 50.41000 7.05700   1.000 34.66000  ? 140 TYR A O     1 
ATOM   996  C  CB    . TYR A 1 140 ? 21.65000 48.21100 9.47900   1.000 35.62000  ? 140 TYR A CB    1 
ATOM   997  C  CG    . TYR A 1 140 ? 21.13000 48.42200 10.88200  1.000 43.55000  ? 140 TYR A CG    1 
ATOM   998  C  CD1   . TYR A 1 140 ? 20.35600 47.45500 11.50800  1.000 46.67000  ? 140 TYR A CD1   1 
ATOM   999  C  CD2   . TYR A 1 140 ? 21.37800 49.60600 11.56500  1.000 46.22000  ? 140 TYR A CD2   1 
ATOM   1000 C  CE1   . TYR A 1 140 ? 19.86100 47.65000 12.78500  1.000 57.44000  ? 140 TYR A CE1   1 
ATOM   1001 C  CE2   . TYR A 1 140 ? 20.88700 49.81000 12.84200  1.000 54.77000  ? 140 TYR A CE2   1 
ATOM   1002 C  CZ    . TYR A 1 140 ? 20.12900 48.82900 13.44700  1.000 59.33000  ? 140 TYR A CZ    1 
ATOM   1003 O  OH    . TYR A 1 140 ? 19.63800 49.02400 14.71600  1.000 63.42000  ? 140 TYR A OH    1 
ATOM   1004 N  N     . LEU A 1 141 ? 21.65600 48.31800 6.23700   1.000 40.75000  ? 141 LEU A N     1 
ATOM   1005 C  CA    . LEU A 1 141 ? 22.29300 48.76100 5.00100   1.000 38.52000  ? 141 LEU A CA    1 
ATOM   1006 C  C     . LEU A 1 141 ? 21.35400 49.63800 4.18500   1.000 36.95000  ? 141 LEU A C     1 
ATOM   1007 O  O     . LEU A 1 141 ? 21.75300 50.69300 3.67600   1.000 35.23000  ? 141 LEU A O     1 
ATOM   1008 C  CB    . LEU A 1 141 ? 22.73400 47.54800 4.18400   1.000 37.25000  ? 141 LEU A CB    1 
ATOM   1009 C  CG    . LEU A 1 141 ? 23.95600 46.78800 4.69800   1.000 41.80000  ? 141 LEU A CG    1 
ATOM   1010 C  CD1   . LEU A 1 141 ? 23.99200 45.39700 4.08800   1.000 39.18000  ? 141 LEU A CD1   1 
ATOM   1011 C  CD2   . LEU A 1 141 ? 25.22000 47.56400 4.38000   1.000 49.74000  ? 141 LEU A CD2   1 
ATOM   1012 N  N     . VAL A 1 142 ? 20.09500 49.21800 4.05600   1.000 32.51000  ? 142 VAL A N     1 
ATOM   1013 C  CA    . VAL A 1 142 ? 19.14200 49.92300 3.20900   1.000 38.83000  ? 142 VAL A CA    1 
ATOM   1014 C  C     . VAL A 1 142 ? 18.54300 51.14400 3.89200   1.000 40.68000  ? 142 VAL A C     1 
ATOM   1015 O  O     . VAL A 1 142 ? 18.07200 52.06000 3.20300   1.000 42.12000  ? 142 VAL A O     1 
ATOM   1016 C  CB    . VAL A 1 142 ? 18.03600 48.94400 2.77400   1.000 36.97000  ? 142 VAL A CB    1 
ATOM   1017 C  CG1   . VAL A 1 142 ? 16.82700 49.68900 2.23200   1.000 49.17000  ? 142 VAL A CG1   1 
ATOM   1018 C  CG2   . VAL A 1 142 ? 18.57800 47.96000 1.74400   1.000 36.33000  ? 142 VAL A CG2   1 
ATOM   1019 N  N     . GLY A 1 143 ? 18.55200 51.19400 5.21900   1.000 39.37000  ? 143 GLY A N     1 
ATOM   1020 C  CA    . GLY A 1 143 ? 17.93200 52.27800 5.93900   1.000 43.67000  ? 143 GLY A CA    1 
ATOM   1021 C  C     . GLY A 1 143 ? 18.93100 53.20100 6.60500   1.000 42.71000  ? 143 GLY A C     1 
ATOM   1022 O  O     . GLY A 1 143 ? 19.47600 54.11800 5.98400   1.000 48.69000  ? 143 GLY A O     1 
ATOM   1023 N  N     . PRO A 1 144 ? 19.18500 52.97600 7.89800   1.000 43.17000  ? 144 PRO A N     1 
ATOM   1024 C  CA    . PRO A 1 144 ? 20.06400 53.89400 8.64300   1.000 44.16000  ? 144 PRO A CA    1 
ATOM   1025 C  C     . PRO A 1 144 ? 21.37200 54.23000 7.94500   1.000 45.77000  ? 144 PRO A C     1 
ATOM   1026 O  O     . PRO A 1 144 ? 21.78100 55.39800 7.95100   1.000 50.76000  ? 144 PRO A O     1 
ATOM   1027 C  CB    . PRO A 1 144 ? 20.30400 53.13800 9.95900   1.000 44.33000  ? 144 PRO A CB    1 
ATOM   1028 C  CG    . PRO A 1 144 ? 19.06500 52.31900 10.15400  1.000 42.12000  ? 144 PRO A CG    1 
ATOM   1029 C  CD    . PRO A 1 144 ? 18.55200 51.97100 8.77700   1.000 43.55000  ? 144 PRO A CD    1 
ATOM   1030 N  N     . MET A 1 145 ? 22.04900 53.24800 7.35100   1.000 42.66000  ? 145 MET A N     1 
ATOM   1031 C  CA    . MET A 1 145 ? 23.32500 53.53900 6.70000   1.000 39.90000  ? 145 MET A CA    1 
ATOM   1032 C  C     . MET A 1 145 ? 23.13000 54.35100 5.42800   1.000 40.36000  ? 145 MET A C     1 
ATOM   1033 O  O     . MET A 1 145 ? 24.01600 55.12300 5.04400   1.000 38.53000  ? 145 MET A O     1 
ATOM   1034 C  CB    . MET A 1 145 ? 24.06700 52.23400 6.40300   1.000 39.73000  ? 145 MET A CB    1 
ATOM   1035 C  CG    . MET A 1 145 ? 24.42500 51.45400 7.66000   1.000 41.42000  ? 145 MET A CG    1 
ATOM   1036 S  SD    . MET A 1 145 ? 25.36800 49.94300 7.36700   1.000 40.11000  ? 145 MET A SD    1 
ATOM   1037 C  CE    . MET A 1 145 ? 26.72000 50.57100 6.37400   1.000 38.97000  ? 145 MET A CE    1 
ATOM   1038 N  N     . THR A 1 146 ? 21.98000 54.20200 4.76700   1.000 39.58000  ? 146 THR A N     1 
ATOM   1039 C  CA    . THR A 1 146 ? 21.68600 55.01300 3.59000   1.000 43.48000  ? 146 THR A CA    1 
ATOM   1040 C  C     . THR A 1 146 ? 21.31100 56.43600 3.98300   1.000 45.51000  ? 146 THR A C     1 
ATOM   1041 O  O     . THR A 1 146 ? 21.75300 57.39400 3.33900   1.000 51.31000  ? 146 THR A O     1 
ATOM   1042 C  CB    . THR A 1 146 ? 20.56600 54.36600 2.77700   1.000 38.94000  ? 146 THR A CB    1 
ATOM   1043 O  OG1   . THR A 1 146 ? 20.97000 53.05300 2.36700   1.000 40.90000  ? 146 THR A OG1   1 
ATOM   1044 C  CG2   . THR A 1 146 ? 20.24400 55.20400 1.54500   1.000 36.62000  ? 146 THR A CG2   1 
ATOM   1045 N  N     . GLU A 1 147 ? 20.50100 56.59300 5.03400   1.000 53.95000  ? 147 GLU A N     1 
ATOM   1046 C  CA    . GLU A 1 147 ? 20.26400 57.91800 5.59800   1.000 57.64000  ? 147 GLU A CA    1 
ATOM   1047 C  C     . GLU A 1 147 ? 21.58700 58.62500 5.87000   1.000 55.06000  ? 147 GLU A C     1 
ATOM   1048 O  O     . GLU A 1 147 ? 21.77400 59.79200 5.50500   1.000 55.29000  ? 147 GLU A O     1 
ATOM   1049 C  CB    . GLU A 1 147 ? 19.45100 57.80800 6.89100   1.000 63.39000  ? 147 GLU A CB    1 
ATOM   1050 C  CG    . GLU A 1 147 ? 17.96100 57.54300 6.70800   1.000 81.90000  ? 147 GLU A CG    1 
ATOM   1051 C  CD    . GLU A 1 147 ? 17.09100 58.45100 7.57200   1.000 90.46000  ? 147 GLU A CD    1 
ATOM   1052 O  OE1   . GLU A 1 147 ? 16.94500 58.17500 8.78300   1.000 87.44000  ? 147 GLU A OE1   1 
ATOM   1053 O  OE2   . GLU A 1 147 ? 16.55100 59.44400 7.03800   1.000 97.81000  ? 147 GLU A OE2   1 
ATOM   1054 N  N     . SER A 1 148 ? 22.52600 57.91600 6.50200   1.000 48.85000  ? 148 SER A N     1 
ATOM   1055 C  CA    . SER A 1 148 ? 23.78800 58.52800 6.90100   1.000 43.48000  ? 148 SER A CA    1 
ATOM   1056 C  C     . SER A 1 148 ? 24.64300 58.87700 5.69100   1.000 49.02000  ? 148 SER A C     1 
ATOM   1057 O  O     . SER A 1 148 ? 25.21700 59.97100 5.62700   1.000 48.81000  ? 148 SER A O     1 
ATOM   1058 C  CB    . SER A 1 148 ? 24.53800 57.58400 7.84500   1.000 45.82000  ? 148 SER A CB    1 
ATOM   1059 O  OG    . SER A 1 148 ? 25.93900 57.69300 7.67900   1.000 47.47000  ? 148 SER A OG    1 
ATOM   1060 N  N     . ALA A 1 149 ? 24.74800 57.96300 4.72300   1.000 48.90000  ? 149 ALA A N     1 
ATOM   1061 C  CA    . ALA A 1 149 ? 25.51300 58.25100 3.51600   1.000 45.46000  ? 149 ALA A CA    1 
ATOM   1062 C  C     . ALA A 1 149 ? 24.97200 59.46600 2.77300   1.000 50.99000  ? 149 ALA A C     1 
ATOM   1063 O  O     . ALA A 1 149 ? 25.70700 60.08000 1.99100   1.000 50.07000  ? 149 ALA A O     1 
ATOM   1064 C  CB    . ALA A 1 149 ? 25.50900 57.03500 2.58600   1.000 44.27000  ? 149 ALA A CB    1 
ATOM   1065 N  N     . SER A 1 150 ? 23.70600 59.82200 3.00000   1.000 53.36000  ? 150 SER A N     1 
ATOM   1066 C  CA    . SER A 1 150 ? 23.11800 60.95200 2.29000   1.000 61.71000  ? 150 SER A CA    1 
ATOM   1067 C  C     . SER A 1 150 ? 23.82100 62.25700 2.63000   1.000 64.08000  ? 150 SER A C     1 
ATOM   1068 O  O     . SER A 1 150 ? 23.87600 63.16800 1.79500   1.000 67.63000  ? 150 SER A O     1 
ATOM   1069 C  CB    . SER A 1 150 ? 21.62800 61.05600 2.61900   1.000 65.76000  ? 150 SER A CB    1 
ATOM   1070 O  OG    . SER A 1 150 ? 21.39800 62.03400 3.61800   1.000 72.74000  ? 150 SER A OG    1 
ATOM   1071 N  N     . GLN A 1 151 ? 24.36600 62.37200 3.84200   1.000 68.80000  ? 151 GLN A N     1 
ATOM   1072 C  CA    . GLN A 1 151 ? 25.01000 63.61000 4.25900   1.000 73.86000  ? 151 GLN A CA    1 
ATOM   1073 C  C     . GLN A 1 151 ? 26.33300 63.86500 3.55200   1.000 63.05000  ? 151 GLN A C     1 
ATOM   1074 O  O     . GLN A 1 151 ? 26.94700 64.91100 3.79700   1.000 57.78000  ? 151 GLN A O     1 
ATOM   1075 C  CB    . GLN A 1 151 ? 25.25400 63.60500 5.77200   1.000 82.93000  ? 151 GLN A CB    1 
ATOM   1076 C  CG    . GLN A 1 151 ? 24.20900 62.86700 6.59400   1.000 92.23000  ? 151 GLN A CG    1 
ATOM   1077 C  CD    . GLN A 1 151 ? 22.87000 63.57300 6.61100   1.000 109.49000 ? 151 GLN A CD    1 
ATOM   1078 O  OE1   . GLN A 1 151 ? 22.63700 64.50400 5.84200   1.000 120.49000 ? 151 GLN A OE1   1 
ATOM   1079 N  NE2   . GLN A 1 151 ? 21.97800 63.12800 7.48900   1.000 120.99000 ? 151 GLN A NE2   1 
ATOM   1080 N  N     . ARG A 1 152 ? 26.80100 62.96000 2.70500   1.000 53.58000  ? 152 ARG A N     1 
ATOM   1081 C  CA    . ARG A 1 152 ? 28.09400 63.11500 2.05900   1.000 58.05000  ? 152 ARG A CA    1 
ATOM   1082 C  C     . ARG A 1 152 ? 27.91200 63.65900 0.64700   1.000 50.25000  ? 152 ARG A C     1 
ATOM   1083 O  O     . ARG A 1 152 ? 26.79500 63.81100 0.14500   1.000 48.71000  ? 152 ARG A O     1 
ATOM   1084 C  CB    . ARG A 1 152 ? 28.85200 61.78600 2.04200   1.000 69.00000  ? 152 ARG A CB    1 
ATOM   1085 C  CG    . ARG A 1 152 ? 29.31200 61.32700 3.42000   1.000 79.86000  ? 152 ARG A CG    1 
ATOM   1086 C  CD    . ARG A 1 152 ? 30.45800 60.32900 3.33300   1.000 82.40000  ? 152 ARG A CD    1 
ATOM   1087 N  NE    . ARG A 1 152 ? 31.59000 60.73300 4.16100   1.000 84.39000  ? 152 ARG A NE    1 
ATOM   1088 C  CZ    . ARG A 1 152 ? 32.72700 60.05200 4.26300   1.000 93.25000  ? 152 ARG A CZ    1 
ATOM   1089 N  NH1   . ARG A 1 152 ? 32.89500 58.92300 3.58700   1.000 91.21000  ? 152 ARG A NH1   1 
ATOM   1090 N  NH2   . ARG A 1 152 ? 33.70100 60.50100 5.04500   1.000 100.87000 ? 152 ARG A NH2   1 
ATOM   1091 N  N     . SER A 1 153 ? 29.04100 63.96400 0.00900   1.000 49.28000  ? 153 SER A N     1 
ATOM   1092 C  CA    . SER A 1 153 ? 29.03800 64.47800 -1.35300  1.000 52.36000  ? 153 SER A CA    1 
ATOM   1093 C  C     . SER A 1 153 ? 28.20900 63.58300 -2.26400  1.000 58.90000  ? 153 SER A C     1 
ATOM   1094 O  O     . SER A 1 153 ? 27.95200 62.41900 -1.93900  1.000 54.90000  ? 153 SER A O     1 
ATOM   1095 C  CB    . SER A 1 153 ? 30.46700 64.58700 -1.88200  1.000 53.87000  ? 153 SER A CB    1 
ATOM   1096 O  OG    . SER A 1 153 ? 30.80000 63.45000 -2.65600  1.000 62.88000  ? 153 SER A OG    1 
ATOM   1097 N  N     . SER A 1 154 ? 27.79000 64.11800 -3.41200  1.000 61.70000  ? 154 SER A N     1 
ATOM   1098 C  CA    . SER A 1 154 ? 26.94400 63.34900 -4.31700  1.000 57.54000  ? 154 SER A CA    1 
ATOM   1099 C  C     . SER A 1 154 ? 27.68200 62.15200 -4.90200  1.000 59.91000  ? 154 SER A C     1 
ATOM   1100 O  O     . SER A 1 154 ? 27.05900 61.12800 -5.20500  1.000 62.81000  ? 154 SER A O     1 
ATOM   1101 C  CB    . SER A 1 154 ? 26.42600 64.25800 -5.43300  1.000 62.60000  ? 154 SER A CB    1 
ATOM   1102 O  OG    . SER A 1 154 ? 27.28500 64.23100 -6.55800  1.000 79.92000  ? 154 SER A OG    1 
ATOM   1103 N  N     . GLY A 1 155 ? 28.99900 62.25500 -5.06000  1.000 60.31000  ? 155 GLY A N     1 
ATOM   1104 C  CA    . GLY A 1 155 ? 29.78300 61.16800 -5.61600  1.000 59.01000  ? 155 GLY A CA    1 
ATOM   1105 C  C     . GLY A 1 155 ? 30.01800 60.04500 -4.62900  1.000 57.46000  ? 155 GLY A C     1 
ATOM   1106 O  O     . GLY A 1 155 ? 29.99400 58.86700 -4.99900  1.000 55.09000  ? 155 GLY A O     1 
ATOM   1107 N  N     . ILE A 1 156 ? 30.26500 60.40000 -3.36700  1.000 57.36000  ? 156 ILE A N     1 
ATOM   1108 C  CA    . ILE A 1 156 ? 30.40700 59.38600 -2.32900  1.000 58.06000  ? 156 ILE A CA    1 
ATOM   1109 C  C     . ILE A 1 156 ? 29.09000 58.64700 -2.13400  1.000 55.59000  ? 156 ILE A C     1 
ATOM   1110 O  O     . ILE A 1 156 ? 29.05400 57.41400 -2.05200  1.000 54.43000  ? 156 ILE A O     1 
ATOM   1111 C  CB    . ILE A 1 156 ? 30.89300 60.02400 -1.01400  1.000 63.94000  ? 156 ILE A CB    1 
ATOM   1112 C  CG1   . ILE A 1 156 ? 32.32100 60.54500 -1.17800  1.000 67.86000  ? 156 ILE A CG1   1 
ATOM   1113 C  CG2   . ILE A 1 156 ? 30.80100 59.02100 0.12800   1.000 64.62000  ? 156 ILE A CG2   1 
ATOM   1114 C  CD1   . ILE A 1 156 ? 33.39200 59.54100 -0.80700  1.000 72.87000  ? 156 ILE A CD1   1 
ATOM   1115 N  N     . LYS A 1 157 ? 27.98800 59.39100 -2.05800  1.000 54.73000  ? 157 LYS A N     1 
ATOM   1116 C  CA    . LYS A 1 157 ? 26.69200 58.74600 -1.89600  1.000 58.02000  ? 157 LYS A CA    1 
ATOM   1117 C  C     . LYS A 1 157 ? 26.38900 57.82300 -3.06700  1.000 50.78000  ? 157 LYS A C     1 
ATOM   1118 O  O     . LYS A 1 157 ? 25.78900 56.75700 -2.88700  1.000 45.04000  ? 157 LYS A O     1 
ATOM   1119 C  CB    . LYS A 1 157 ? 25.60200 59.80600 -1.75700  1.000 64.37000  ? 157 LYS A CB    1 
ATOM   1120 C  CG    . LYS A 1 157 ? 24.19500 59.24600 -1.67100  1.000 72.79000  ? 157 LYS A CG    1 
ATOM   1121 C  CD    . LYS A 1 157 ? 23.14800 60.31000 -1.98500  1.000 87.10000  ? 157 LYS A CD    1 
ATOM   1122 C  CE    . LYS A 1 157 ? 23.64600 61.72700 -1.68800  1.000 97.13000  ? 157 LYS A CE    1 
ATOM   1123 N  NZ    . LYS A 1 157 ? 23.85000 61.95200 -0.23100  1.000 105.34000 ? 157 LYS A NZ    1 
ATOM   1124 N  N     . SER A 1 158 ? 26.78900 58.21600 -4.27900  1.000 50.28000  ? 158 SER A N     1 
ATOM   1125 C  CA    . SER A 1 158 ? 26.55700 57.37100 -5.44400  1.000 47.58000  ? 158 SER A CA    1 
ATOM   1126 C  C     . SER A 1 158 ? 27.37400 56.09000 -5.36100  1.000 44.50000  ? 158 SER A C     1 
ATOM   1127 O  O     . SER A 1 158 ? 26.87800 55.00400 -5.68400  1.000 42.40000  ? 158 SER A O     1 
ATOM   1128 C  CB    . SER A 1 158 ? 26.88900 58.14100 -6.72200  1.000 47.90000  ? 158 SER A CB    1 
ATOM   1129 O  OG    . SER A 1 158 ? 26.72000 57.32500 -7.86800  1.000 52.78000  ? 158 SER A OG    1 
ATOM   1130 N  N     . LEU A 1 159 ? 28.63500 56.19900 -4.93700  1.000 44.42000  ? 159 LEU A N     1 
ATOM   1131 C  CA    . LEU A 1 159 ? 29.46500 55.01400 -4.75500  1.000 40.34000  ? 159 LEU A CA    1 
ATOM   1132 C  C     . LEU A 1 159 ? 28.87900 54.09000 -3.69700  1.000 40.30000  ? 159 LEU A C     1 
ATOM   1133 O  O     . LEU A 1 159 ? 28.83500 52.86800 -3.88500  1.000 38.33000  ? 159 LEU A O     1 
ATOM   1134 C  CB    . LEU A 1 159 ? 30.88300 55.43100 -4.37200  1.000 41.77000  ? 159 LEU A CB    1 
ATOM   1135 C  CG    . LEU A 1 159 ? 31.90900 54.31900 -4.15400  1.000 41.30000  ? 159 LEU A CG    1 
ATOM   1136 C  CD1   . LEU A 1 159 ? 31.96100 53.40900 -5.36800  1.000 40.82000  ? 159 LEU A CD1   1 
ATOM   1137 C  CD2   . LEU A 1 159 ? 33.27800 54.91200 -3.85800  1.000 45.93000  ? 159 LEU A CD2   1 
ATOM   1138 N  N     . TYR A 1 160 ? 28.42000 54.65500 -2.57900  1.000 33.66000  ? 160 TYR A N     1 
ATOM   1139 C  CA    . TYR A 1 160 ? 27.86100 53.82100 -1.52200  1.000 34.63000  ? 160 TYR A CA    1 
ATOM   1140 C  C     . TYR A 1 160 ? 26.65800 53.03500 -2.02800  1.000 34.88000  ? 160 TYR A C     1 
ATOM   1141 O  O     . TYR A 1 160 ? 26.51900 51.83800 -1.75000  1.000 37.94000  ? 160 TYR A O     1 
ATOM   1142 C  CB    . TYR A 1 160 ? 27.44800 54.66300 -0.32100  1.000 30.75000  ? 160 TYR A CB    1 
ATOM   1143 C  CG    . TYR A 1 160 ? 26.62400 53.85100 0.64800   1.000 31.41000  ? 160 TYR A CG    1 
ATOM   1144 C  CD1   . TYR A 1 160 ? 27.24300 53.05400 1.59600   1.000 31.25000  ? 160 TYR A CD1   1 
ATOM   1145 C  CD2   . TYR A 1 160 ? 25.23600 53.84200 0.58600   1.000 33.19000  ? 160 TYR A CD2   1 
ATOM   1146 C  CE1   . TYR A 1 160 ? 26.51000 52.29000 2.47500   1.000 36.51000  ? 160 TYR A CE1   1 
ATOM   1147 C  CE2   . TYR A 1 160 ? 24.49100 53.07800 1.46400   1.000 31.87000  ? 160 TYR A CE2   1 
ATOM   1148 C  CZ    . TYR A 1 160 ? 25.13600 52.30300 2.40700   1.000 37.85000  ? 160 TYR A CZ    1 
ATOM   1149 O  OH    . TYR A 1 160 ? 24.41700 51.53200 3.28900   1.000 39.98000  ? 160 TYR A OH    1 
ATOM   1150 N  N     . VAL A 1 161 ? 25.76000 53.70700 -2.75100  1.000 36.54000  ? 161 VAL A N     1 
ATOM   1151 C  CA    . VAL A 1 161 ? 24.54800 53.05200 -3.23300  1.000 38.78000  ? 161 VAL A CA    1 
ATOM   1152 C  C     . VAL A 1 161 ? 24.89400 51.92300 -4.19300  1.000 36.42000  ? 161 VAL A C     1 
ATOM   1153 O  O     . VAL A 1 161 ? 24.23800 50.87400 -4.20600  1.000 40.85000  ? 161 VAL A O     1 
ATOM   1154 C  CB    . VAL A 1 161 ? 23.61100 54.08400 -3.88900  1.000 43.09000  ? 161 VAL A CB    1 
ATOM   1155 C  CG1   . VAL A 1 161 ? 22.55000 53.37900 -4.72700  1.000 41.44000  ? 161 VAL A CG1   1 
ATOM   1156 C  CG2   . VAL A 1 161 ? 22.97100 54.97200 -2.83300  1.000 41.99000  ? 161 VAL A CG2   1 
ATOM   1157 N  N     . ARG A 1 162 ? 25.92700 52.11400 -5.01300  1.000 37.99000  ? 162 ARG A N     1 
ATOM   1158 C  CA    . ARG A 1 162 ? 26.30100 51.07000 -5.96300  1.000 40.03000  ? 162 ARG A CA    1 
ATOM   1159 C  C     . ARG A 1 162 ? 26.88500 49.86300 -5.24100  1.000 38.66000  ? 162 ARG A C     1 
ATOM   1160 O  O     . ARG A 1 162 ? 26.49700 48.72000 -5.51300  1.000 34.73000  ? 162 ARG A O     1 
ATOM   1161 C  CB    . ARG A 1 162 ? 27.27000 51.64400 -7.00200  1.000 51.74000  ? 162 ARG A CB    1 
ATOM   1162 C  CG    . ARG A 1 162 ? 26.58300 52.65400 -7.92700  1.000 70.62000  ? 162 ARG A CG    1 
ATOM   1163 C  CD    . ARG A 1 162 ? 27.53500 53.38600 -8.86000  1.000 79.29000  ? 162 ARG A CD    1 
ATOM   1164 N  NE    . ARG A 1 162 ? 28.32400 52.48500 -9.69800  1.000 95.59000  ? 162 ARG A NE    1 
ATOM   1165 C  CZ    . ARG A 1 162 ? 27.81600 51.63400 -10.58500 1.000 105.40000 ? 162 ARG A CZ    1 
ATOM   1166 N  NH1   . ARG A 1 162 ? 26.50400 51.54300 -10.76600 1.000 104.85000 ? 162 ARG A NH1   1 
ATOM   1167 N  NH2   . ARG A 1 162 ? 28.62800 50.86500 -11.29900 1.000 108.52000 ? 162 ARG A NH2   1 
ATOM   1168 N  N     . LEU A 1 163 ? 27.78600 50.09400 -4.28800  1.000 38.83000  ? 163 LEU A N     1 
ATOM   1169 C  CA    . LEU A 1 163 ? 28.35200 48.97400 -3.54100  1.000 32.34000  ? 163 LEU A CA    1 
ATOM   1170 C  C     . LEU A 1 163 ? 27.30500 48.32200 -2.64300  1.000 31.36000  ? 163 LEU A C     1 
ATOM   1171 O  O     . LEU A 1 163 ? 27.28200 47.09500 -2.49700  1.000 27.50000  ? 163 LEU A O     1 
ATOM   1172 C  CB    . LEU A 1 163 ? 29.55300 49.44500 -2.72300  1.000 36.03000  ? 163 LEU A CB    1 
ATOM   1173 C  CG    . LEU A 1 163 ? 30.76800 49.83300 -3.56800  1.000 39.64000  ? 163 LEU A CG    1 
ATOM   1174 C  CD1   . LEU A 1 163 ? 31.85000 50.45200 -2.69600  1.000 46.81000  ? 163 LEU A CD1   1 
ATOM   1175 C  CD2   . LEU A 1 163 ? 31.31400 48.63100 -4.32800  1.000 39.06000  ? 163 LEU A CD2   1 
ATOM   1176 N  N     . ARG A 1 164 ? 26.43000 49.12600 -2.03600  1.000 30.50000  ? 164 ARG A N     1 
ATOM   1177 C  CA    . ARG A 1 164 ? 25.36000 48.57100 -1.21200  1.000 28.16000  ? 164 ARG A CA    1 
ATOM   1178 C  C     . ARG A 1 164 ? 24.46900 47.64100 -2.02800  1.000 30.34000  ? 164 ARG A C     1 
ATOM   1179 O  O     . ARG A 1 164 ? 24.11000 46.54800 -1.57500  1.000 29.44000  ? 164 ARG A O     1 
ATOM   1180 C  CB    . ARG A 1 164 ? 24.54300 49.70900 -0.59700  1.000 32.48000  ? 164 ARG A CB    1 
ATOM   1181 C  CG    . ARG A 1 164 ? 23.20100 49.29800 -0.01500  1.000 34.35000  ? 164 ARG A CG    1 
ATOM   1182 C  CD    . ARG A 1 164 ? 22.22600 50.46300 -0.02000  1.000 36.60000  ? 164 ARG A CD    1 
ATOM   1183 N  NE    . ARG A 1 164 ? 21.44200 50.51000 -1.25200  1.000 41.29000  ? 164 ARG A NE    1 
ATOM   1184 C  CZ    . ARG A 1 164 ? 20.39800 51.31000 -1.44900  1.000 45.17000  ? 164 ARG A CZ    1 
ATOM   1185 N  NH1   . ARG A 1 164 ? 20.00200 52.14400 -0.49600  1.000 44.32000  ? 164 ARG A NH1   1 
ATOM   1186 N  NH2   . ARG A 1 164 ? 19.74500 51.27800 -2.60700  1.000 47.60000  ? 164 ARG A NH2   1 
ATOM   1187 N  N     . ASN A 1 165 ? 24.08500 48.07000 -3.23200  1.000 33.81000  ? 165 ASN A N     1 
ATOM   1188 C  CA    . ASN A 1 165 ? 23.20700 47.25300 -4.06400  1.000 36.85000  ? 165 ASN A CA    1 
ATOM   1189 C  C     . ASN A 1 165 ? 23.88200 45.94200 -4.44200  1.000 28.64000  ? 165 ASN A C     1 
ATOM   1190 O  O     . ASN A 1 165 ? 23.28800 44.86500 -4.32100  1.000 29.67000  ? 165 ASN A O     1 
ATOM   1191 C  CB    . ASN A 1 165 ? 22.80000 48.03500 -5.31000  1.000 39.08000  ? 165 ASN A CB    1 
ATOM   1192 C  CG    . ASN A 1 165 ? 21.83600 49.16100 -5.00000  1.000 46.26000  ? 165 ASN A CG    1 
ATOM   1193 O  OD1   . ASN A 1 165 ? 21.44100 49.35500 -3.85000  1.000 39.68000  ? 165 ASN A OD1   1 
ATOM   1194 N  ND2   . ASN A 1 165 ? 21.44900 49.91200 -6.02400  1.000 59.09000  ? 165 ASN A ND2   1 
ATOM   1195 N  N     . LEU A 1 166 ? 25.13000 46.01800 -4.91100  1.000 27.39000  ? 166 LEU A N     1 
ATOM   1196 C  CA    . LEU A 1 166 ? 25.89800 44.80900 -5.18600  1.000 30.97000  ? 166 LEU A CA    1 
ATOM   1197 C  C     . LEU A 1 166 ? 25.93200 43.89000 -3.97300  1.000 28.39000  ? 166 LEU A C     1 
ATOM   1198 O  O     . LEU A 1 166 ? 25.76900 42.67000 -4.09700  1.000 31.56000  ? 166 LEU A O     1 
ATOM   1199 C  CB    . LEU A 1 166 ? 27.32100 45.18400 -5.60200  1.000 34.55000  ? 166 LEU A CB    1 
ATOM   1200 C  CG    . LEU A 1 166 ? 28.26200 44.03200 -5.95500  1.000 40.77000  ? 166 LEU A CG    1 
ATOM   1201 C  CD1   . LEU A 1 166 ? 27.96400 43.55900 -7.36400  1.000 44.95000  ? 166 LEU A CD1   1 
ATOM   1202 C  CD2   . LEU A 1 166 ? 29.71600 44.45100 -5.82000  1.000 45.07000  ? 166 LEU A CD2   1 
ATOM   1203 N  N     . THR A 1 167 ? 26.14700 44.46300 -2.79000  1.000 26.01000  ? 167 THR A N     1 
ATOM   1204 C  CA    . THR A 1 167 ? 26.30100 43.65600 -1.58600  1.000 22.47000  ? 167 THR A CA    1 
ATOM   1205 C  C     . THR A 1 167 ? 24.98900 42.98500 -1.20400  1.000 21.84000  ? 167 THR A C     1 
ATOM   1206 O  O     . THR A 1 167 ? 24.94400 41.77100 -0.97700  1.000 26.72000  ? 167 THR A O     1 
ATOM   1207 C  CB    . THR A 1 167 ? 26.81600 44.53500 -0.44400  1.000 23.04000  ? 167 THR A CB    1 
ATOM   1208 O  OG1   . THR A 1 167 ? 28.19100 44.86900 -0.67700  1.000 28.48000  ? 167 THR A OG1   1 
ATOM   1209 C  CG2   . THR A 1 167 ? 26.68100 43.82000 0.89000   1.000 23.46000  ? 167 THR A CG2   1 
ATOM   1210 N  N     . VAL A 1 168 ? 23.90500 43.75900 -1.14200  1.000 28.39000  ? 168 VAL A N     1 
ATOM   1211 C  CA    . VAL A 1 168 ? 22.63000 43.22000 -0.67000  1.000 25.60000  ? 168 VAL A CA    1 
ATOM   1212 C  C     . VAL A 1 168 ? 22.13700 42.11700 -1.60100  1.000 26.94000  ? 168 VAL A C     1 
ATOM   1213 O  O     . VAL A 1 168 ? 21.70500 41.04700 -1.15600  1.000 24.67000  ? 168 VAL A O     1 
ATOM   1214 C  CB    . VAL A 1 168 ? 21.59200 44.34800 -0.53000  1.000 30.88000  ? 168 VAL A CB    1 
ATOM   1215 C  CG1   . VAL A 1 168 ? 20.18900 43.77200 -0.40200  1.000 35.45000  ? 168 VAL A CG1   1 
ATOM   1216 C  CG2   . VAL A 1 168 ? 21.92500 45.23700 0.66200   1.000 34.61000  ? 168 VAL A CG2   1 
ATOM   1217 N  N     . ILE A 1 169 ? 22.18400 42.36300 -2.90900  1.000 23.93000  ? 169 ILE A N     1 
ATOM   1218 C  CA    . ILE A 1 169 ? 21.62300 41.40400 -3.85500  1.000 24.79000  ? 169 ILE A CA    1 
ATOM   1219 C  C     . ILE A 1 169 ? 22.42100 40.10600 -3.83800  1.000 20.90000  ? 169 ILE A C     1 
ATOM   1220 O  O     . ILE A 1 169 ? 21.85200 39.01000 -3.78200  1.000 27.94000  ? 169 ILE A O     1 
ATOM   1221 C  CB    . ILE A 1 169 ? 21.56200 42.01300 -5.26600  1.000 28.31000  ? 169 ILE A CB    1 
ATOM   1222 C  CG1   . ILE A 1 169 ? 20.38200 42.98100 -5.36400  1.000 32.96000  ? 169 ILE A CG1   1 
ATOM   1223 C  CG2   . ILE A 1 169 ? 21.44000 40.91300 -6.31300  1.000 32.70000  ? 169 ILE A CG2   1 
ATOM   1224 C  CD1   . ILE A 1 169 ? 20.57200 44.08700 -6.37400  1.000 38.87000  ? 169 ILE A CD1   1 
ATOM   1225 N  N     . LEU A 1 170 ? 23.75000 40.20500 -3.86900  1.000 22.76000  ? 170 LEU A N     1 
ATOM   1226 C  CA    . LEU A 1 170 ? 24.56500 38.99600 -3.93900  1.000 19.00000  ? 170 LEU A CA    1 
ATOM   1227 C  C     . LEU A 1 170 ? 24.63400 38.27100 -2.59800  1.000 20.05000  ? 170 LEU A C     1 
ATOM   1228 O  O     . LEU A 1 170 ? 24.59000 37.03700 -2.55900  1.000 20.83000  ? 170 LEU A O     1 
ATOM   1229 C  CB    . LEU A 1 170 ? 25.96900 39.33600 -4.43300  1.000 22.25000  ? 170 LEU A CB    1 
ATOM   1230 C  CG    . LEU A 1 170 ? 26.01300 39.85000 -5.87200  1.000 25.91000  ? 170 LEU A CG    1 
ATOM   1231 C  CD1   . LEU A 1 170 ? 27.44300 40.03500 -6.34600  1.000 32.95000  ? 170 LEU A CD1   1 
ATOM   1232 C  CD2   . LEU A 1 170 ? 25.26200 38.91200 -6.80300  1.000 21.18000  ? 170 LEU A CD2   1 
ATOM   1233 N  N     . TRP A 1 171 ? 24.75300 39.00600 -1.48900  1.000 17.65000  ? 171 TRP A N     1 
ATOM   1234 C  CA    . TRP A 1 171 ? 24.79400 38.33500 -0.19500  1.000 20.95000  ? 171 TRP A CA    1 
ATOM   1235 C  C     . TRP A 1 171 ? 23.51300 37.55200 0.05800   1.000 23.87000  ? 171 TRP A C     1 
ATOM   1236 O  O     . TRP A 1 171 ? 23.54800 36.49800 0.70600   1.000 25.14000  ? 171 TRP A O     1 
ATOM   1237 C  CB    . TRP A 1 171 ? 25.01800 39.34300 0.93200   1.000 18.96000  ? 171 TRP A CB    1 
ATOM   1238 C  CG    . TRP A 1 171 ? 26.42400 39.87000 1.03300   1.000 16.57000  ? 171 TRP A CG    1 
ATOM   1239 C  CD1   . TRP A 1 171 ? 27.29300 40.09600 0.00500   1.000 18.93000  ? 171 TRP A CD1   1 
ATOM   1240 C  CD2   . TRP A 1 171 ? 27.11400 40.25100 2.23100   1.000 20.33000  ? 171 TRP A CD2   1 
ATOM   1241 N  NE1   . TRP A 1 171 ? 28.48100 40.59200 0.48900   1.000 20.83000  ? 171 TRP A NE1   1 
ATOM   1242 C  CE2   . TRP A 1 171 ? 28.39600 40.69700 1.85300   1.000 21.07000  ? 171 TRP A CE2   1 
ATOM   1243 C  CE3   . TRP A 1 171 ? 26.77000 40.26200 3.58700   1.000 21.80000  ? 171 TRP A CE3   1 
ATOM   1244 C  CZ2   . TRP A 1 171 ? 29.33500 41.14600 2.77800   1.000 19.93000  ? 171 TRP A CZ2   1 
ATOM   1245 C  CZ3   . TRP A 1 171 ? 27.70500 40.70600 4.50600   1.000 22.77000  ? 171 TRP A CZ3   1 
ATOM   1246 C  CH2   . TRP A 1 171 ? 28.97100 41.14200 4.09700   1.000 23.52000  ? 171 TRP A CH2   1 
ATOM   1247 N  N     . ALA A 1 172 ? 22.37900 38.03900 -0.45500  1.000 22.64000  ? 172 ALA A N     1 
ATOM   1248 C  CA    . ALA A 1 172 ? 21.10800 37.35200 -0.26500  1.000 24.24000  ? 172 ALA A CA    1 
ATOM   1249 C  C     . ALA A 1 172 ? 21.07000 36.00100 -0.96800  1.000 26.71000  ? 172 ALA A C     1 
ATOM   1250 O  O     . ALA A 1 172 ? 20.22300 35.16500 -0.63500  1.000 29.34000  ? 172 ALA A O     1 
ATOM   1251 C  CB    . ALA A 1 172 ? 19.95700 38.22300 -0.77100  1.000 27.14000  ? 172 ALA A CB    1 
ATOM   1252 N  N     . ILE A 1 173 ? 21.96900 35.77200 -1.92500  1.000 22.59000  ? 173 ILE A N     1 
ATOM   1253 C  CA    . ILE A 1 173 ? 21.97800 34.50800 -2.64900  1.000 21.84000  ? 173 ILE A CA    1 
ATOM   1254 C  C     . ILE A 1 173 ? 22.68600 33.42000 -1.84900  1.000 19.51000  ? 173 ILE A C     1 
ATOM   1255 O  O     . ILE A 1 173 ? 22.32700 32.24000 -1.94700  1.000 23.60000  ? 173 ILE A O     1 
ATOM   1256 C  CB    . ILE A 1 173 ? 22.63800 34.70100 -4.02600  1.000 25.67000  ? 173 ILE A CB    1 
ATOM   1257 C  CG1   . ILE A 1 173 ? 21.78600 35.62400 -4.89900  1.000 34.60000  ? 173 ILE A CG1   1 
ATOM   1258 C  CG2   . ILE A 1 173 ? 22.85900 33.36200 -4.71000  1.000 28.51000  ? 173 ILE A CG2   1 
ATOM   1259 C  CD1   . ILE A 1 173 ? 22.54300 36.23400 -6.05400  1.000 38.12000  ? 173 ILE A CD1   1 
ATOM   1260 N  N     . TYR A 1 174 ? 23.69300 33.78600 -1.06100  1.000 19.63000  ? 174 TYR A N     1 
ATOM   1261 C  CA    . TYR A 1 174 ? 24.45900 32.78700 -0.32100  1.000 24.50000  ? 174 TYR A CA    1 
ATOM   1262 C  C     . TYR A 1 174 ? 23.59400 31.84500 0.50600   1.000 23.09000  ? 174 TYR A C     1 
ATOM   1263 O  O     . TYR A 1 174 ? 23.82200 30.62600 0.45100   1.000 24.38000  ? 174 TYR A O     1 
ATOM   1264 C  CB    . TYR A 1 174 ? 25.46900 33.47000 0.61100   1.000 21.58000  ? 174 TYR A CB    1 
ATOM   1265 C  CG    . TYR A 1 174 ? 26.74200 33.93200 -0.04600  1.000 19.90000  ? 174 TYR A CG    1 
ATOM   1266 C  CD1   . TYR A 1 174 ? 26.79500 35.14900 -0.70200  1.000 18.87000  ? 174 TYR A CD1   1 
ATOM   1267 C  CD2   . TYR A 1 174 ? 27.90000 33.16700 0.01300   1.000 21.94000  ? 174 TYR A CD2   1 
ATOM   1268 C  CE1   . TYR A 1 174 ? 27.95200 35.58900 -1.29100  1.000 19.74000  ? 174 TYR A CE1   1 
ATOM   1269 C  CE2   . TYR A 1 174 ? 29.06900 33.60400 -0.57900  1.000 19.02000  ? 174 TYR A CE2   1 
ATOM   1270 C  CZ    . TYR A 1 174 ? 29.08900 34.81900 -1.22600  1.000 18.97000  ? 174 TYR A CZ    1 
ATOM   1271 O  OH    . TYR A 1 174 ? 30.24200 35.27300 -1.82300  1.000 24.08000  ? 174 TYR A OH    1 
ATOM   1272 N  N     . PRO A 1 175 ? 22.63300 32.31600 1.30700   1.000 21.30000  ? 175 PRO A N     1 
ATOM   1273 C  CA    . PRO A 1 175 ? 21.85000 31.36800 2.11500   1.000 23.18000  ? 175 PRO A CA    1 
ATOM   1274 C  C     . PRO A 1 175 ? 21.09800 30.35300 1.27200   1.000 23.44000  ? 175 PRO A C     1 
ATOM   1275 O  O     . PRO A 1 175 ? 20.88100 29.22000 1.71700   1.000 22.98000  ? 175 PRO A O     1 
ATOM   1276 C  CB    . PRO A 1 175 ? 20.89900 32.27100 2.91800   1.000 19.99000  ? 175 PRO A CB    1 
ATOM   1277 C  CG    . PRO A 1 175 ? 20.92800 33.60600 2.25400   1.000 20.06000  ? 175 PRO A CG    1 
ATOM   1278 C  CD    . PRO A 1 175 ? 22.26400 33.72000 1.56300   1.000 19.83000  ? 175 PRO A CD    1 
ATOM   1279 N  N     . PHE A 1 176 ? 20.70500 30.72300 0.05200   1.000 24.70000  ? 176 PHE A N     1 
ATOM   1280 C  CA    . PHE A 1 176 ? 20.04200 29.76800 -0.82900  1.000 25.33000  ? 176 PHE A CA    1 
ATOM   1281 C  C     . PHE A 1 176 ? 21.02200 28.72100 -1.34800  1.000 24.59000  ? 176 PHE A C     1 
ATOM   1282 O  O     . PHE A 1 176 ? 20.68600 27.53400 -1.41200  1.000 23.58000  ? 176 PHE A O     1 
ATOM   1283 C  CB    . PHE A 1 176 ? 19.36800 30.51200 -1.97700  1.000 29.27000  ? 176 PHE A CB    1 
ATOM   1284 C  CG    . PHE A 1 176 ? 18.27400 31.43600 -1.53000  1.000 33.19000  ? 176 PHE A CG    1 
ATOM   1285 C  CD1   . PHE A 1 176 ? 16.99500 30.95800 -1.30800  1.000 36.43000  ? 176 PHE A CD1   1 
ATOM   1286 C  CD2   . PHE A 1 176 ? 18.52900 32.77800 -1.30500  1.000 36.59000  ? 176 PHE A CD2   1 
ATOM   1287 C  CE1   . PHE A 1 176 ? 15.98800 31.80300 -0.88400  1.000 37.42000  ? 176 PHE A CE1   1 
ATOM   1288 C  CE2   . PHE A 1 176 ? 17.52700 33.62600 -0.88200  1.000 38.01000  ? 176 PHE A CE2   1 
ATOM   1289 C  CZ    . PHE A 1 176 ? 16.25400 33.13700 -0.67000  1.000 39.68000  ? 176 PHE A CZ    1 
ATOM   1290 N  N     . ILE A 1 177 ? 22.24000 29.13200 -1.70800  1.000 24.89000  ? 177 ILE A N     1 
ATOM   1291 C  CA    . ILE A 1 177 ? 23.23000 28.16000 -2.16300  1.000 27.95000  ? 177 ILE A CA    1 
ATOM   1292 C  C     . ILE A 1 177 ? 23.59000 27.20100 -1.03500  1.000 31.08000  ? 177 ILE A C     1 
ATOM   1293 O  O     . ILE A 1 177 ? 23.73400 25.99100 -1.24700  1.000 34.61000  ? 177 ILE A O     1 
ATOM   1294 C  CB    . ILE A 1 177 ? 24.48800 28.86800 -2.70100  1.000 35.97000  ? 177 ILE A CB    1 
ATOM   1295 C  CG1   . ILE A 1 177 ? 24.14000 29.89200 -3.78300  1.000 36.91000  ? 177 ILE A CG1   1 
ATOM   1296 C  CG2   . ILE A 1 177 ? 25.47300 27.83200 -3.24100  1.000 43.61000  ? 177 ILE A CG2   1 
ATOM   1297 C  CD1   . ILE A 1 177 ? 23.07200 29.45100 -4.74900  1.000 34.81000  ? 177 ILE A CD1   1 
ATOM   1298 N  N     . TRP A 1 178 ? 23.76800 27.73200 0.17800   1.000 29.55000  ? 178 TRP A N     1 
ATOM   1299 C  CA    . TRP A 1 178 ? 24.07200 26.89900 1.34100   1.000 27.75000  ? 178 TRP A CA    1 
ATOM   1300 C  C     . TRP A 1 178 ? 22.96900 25.87500 1.57000   1.000 31.58000  ? 178 TRP A C     1 
ATOM   1301 O  O     . TRP A 1 178 ? 23.23500 24.67600 1.71200   1.000 38.18000  ? 178 TRP A O     1 
ATOM   1302 C  CB    . TRP A 1 178 ? 24.25500 27.81300 2.55700   1.000 35.38000  ? 178 TRP A CB    1 
ATOM   1303 C  CG    . TRP A 1 178 ? 24.75100 27.20100 3.84000   1.000 33.18000  ? 178 TRP A CG    1 
ATOM   1304 C  CD1   . TRP A 1 178 ? 26.03100 27.22900 4.32300   1.000 33.28000  ? 178 TRP A CD1   1 
ATOM   1305 C  CD2   . TRP A 1 178 ? 23.96400 26.53500 4.83400   1.000 30.04000  ? 178 TRP A CD2   1 
ATOM   1306 N  NE1   . TRP A 1 178 ? 26.09000 26.60200 5.54500   1.000 38.27000  ? 178 TRP A NE1   1 
ATOM   1307 C  CE2   . TRP A 1 178 ? 24.83400 26.16800 5.88000   1.000 33.16000  ? 178 TRP A CE2   1 
ATOM   1308 C  CE3   . TRP A 1 178 ? 22.61000 26.19900 4.93400   1.000 39.40000  ? 178 TRP A CE3   1 
ATOM   1309 C  CZ2   . TRP A 1 178 ? 24.39500 25.47600 7.00800   1.000 37.46000  ? 178 TRP A CZ2   1 
ATOM   1310 C  CZ3   . TRP A 1 178 ? 22.17700 25.51400 6.05400   1.000 43.73000  ? 178 TRP A CZ3   1 
ATOM   1311 C  CH2   . TRP A 1 178 ? 23.06600 25.16100 7.07600   1.000 43.81000  ? 178 TRP A CH2   1 
ATOM   1312 N  N     . LEU A 1 179 ? 21.71700 26.33100 1.57200   1.000 33.19000  ? 179 LEU A N     1 
ATOM   1313 C  CA    . LEU A 1 179 ? 20.60200 25.44400 1.88500   1.000 36.74000  ? 179 LEU A CA    1 
ATOM   1314 C  C     . LEU A 1 179 ? 20.40100 24.38500 0.80800   1.000 42.69000  ? 179 LEU A C     1 
ATOM   1315 O  O     . LEU A 1 179 ? 20.04200 23.24300 1.11500   1.000 43.16000  ? 179 LEU A O     1 
ATOM   1316 C  CB    . LEU A 1 179 ? 19.33200 26.27100 2.06500   1.000 44.83000  ? 179 LEU A CB    1 
ATOM   1317 C  CG    . LEU A 1 179 ? 18.23700 25.71000 2.97000   1.000 51.97000  ? 179 LEU A CG    1 
ATOM   1318 C  CD1   . LEU A 1 179 ? 18.76100 25.46000 4.36700   1.000 52.41000  ? 179 LEU A CD1   1 
ATOM   1319 C  CD2   . LEU A 1 179 ? 17.06800 26.68700 2.98600   1.000 56.33000  ? 179 LEU A CD2   1 
ATOM   1320 N  N     . LEU A 1 180 ? 20.60400 24.74300 -0.45800  1.000 37.45000  ? 180 LEU A N     1 
ATOM   1321 C  CA    . LEU A 1 180 ? 20.42900 23.78000 -1.53800  1.000 38.91000  ? 180 LEU A CA    1 
ATOM   1322 C  C     . LEU A 1 180 ? 21.63300 22.86300 -1.70600  1.000 39.21000  ? 180 LEU A C     1 
ATOM   1323 O  O     . LEU A 1 180 ? 21.52900 21.85400 -2.41200  1.000 41.44000  ? 180 LEU A O     1 
ATOM   1324 C  CB    . LEU A 1 180 ? 20.15600 24.50400 -2.85700  1.000 38.60000  ? 180 LEU A CB    1 
ATOM   1325 C  CG    . LEU A 1 180 ? 18.76800 25.13200 -2.99300  1.000 42.89000  ? 180 LEU A CG    1 
ATOM   1326 C  CD1   . LEU A 1 180 ? 18.70400 26.05700 -4.19900  1.000 44.17000  ? 180 LEU A CD1   1 
ATOM   1327 C  CD2   . LEU A 1 180 ? 17.69900 24.05200 -3.08800  1.000 49.49000  ? 180 LEU A CD2   1 
ATOM   1328 N  N     . GLY A 1 181 ? 22.76000 23.18300 -1.07600  1.000 33.84000  ? 181 GLY A N     1 
ATOM   1329 C  CA    . GLY A 1 181 ? 23.96500 22.40600 -1.22300  1.000 31.12000  ? 181 GLY A CA    1 
ATOM   1330 C  C     . GLY A 1 181 ? 24.14400 21.38400 -0.11900  1.000 35.27000  ? 181 GLY A C     1 
ATOM   1331 O  O     . GLY A 1 181 ? 23.21500 21.07500 0.63200   1.000 38.34000  ? 181 GLY A O     1 
ATOM   1332 N  N     . PRO A 1 182 ? 25.35200 20.84000 -0.00700  1.000 40.10000  ? 182 PRO A N     1 
ATOM   1333 C  CA    . PRO A 1 182 ? 25.60800 19.76200 0.96100   1.000 40.99000  ? 182 PRO A CA    1 
ATOM   1334 C  C     . PRO A 1 182 ? 25.25300 20.15600 2.38500   1.000 46.58000  ? 182 PRO A C     1 
ATOM   1335 O  O     . PRO A 1 182 ? 24.72200 19.32400 3.13600   1.000 49.23000  ? 182 PRO A O     1 
ATOM   1336 C  CB    . PRO A 1 182 ? 27.11600 19.50400 0.81000   1.000 38.60000  ? 182 PRO A CB    1 
ATOM   1337 C  CG    . PRO A 1 182 ? 27.41500 19.89100 -0.60900  1.000 39.09000  ? 182 PRO A CG    1 
ATOM   1338 C  CD    . PRO A 1 182 ? 26.49500 21.05600 -0.91600  1.000 39.65000  ? 182 PRO A CD    1 
ATOM   1339 N  N     . PRO A 1 183 ? 25.53900 21.39100 2.81500   1.000 46.17000  ? 183 PRO A N     1 
ATOM   1340 C  CA    . PRO A 1 183 ? 25.22600 21.74200 4.21300   1.000 46.18000  ? 183 PRO A CA    1 
ATOM   1341 C  C     . PRO A 1 183 ? 23.75100 21.61300 4.54800   1.000 46.38000  ? 183 PRO A C     1 
ATOM   1342 O  O     . PRO A 1 183 ? 23.40700 21.34000 5.70500   1.000 46.95000  ? 183 PRO A O     1 
ATOM   1343 C  CB    . PRO A 1 183 ? 25.70000 23.19900 4.33700   1.000 39.87000  ? 183 PRO A CB    1 
ATOM   1344 C  CG    . PRO A 1 183 ? 26.66600 23.39700 3.21900   1.000 39.99000  ? 183 PRO A CG    1 
ATOM   1345 C  CD    . PRO A 1 183 ? 26.20600 22.49800 2.10500   1.000 40.80000  ? 183 PRO A CD    1 
ATOM   1346 N  N     . GLY A 1 184 ? 22.87300 21.80400 3.56900   1.000 42.97000  ? 184 GLY A N     1 
ATOM   1347 C  CA    . GLY A 1 184 ? 21.44700 21.72900 3.80300   1.000 42.24000  ? 184 GLY A CA    1 
ATOM   1348 C  C     . GLY A 1 184 ? 20.83100 20.46600 3.24600   1.000 48.50000  ? 184 GLY A C     1 
ATOM   1349 O  O     . GLY A 1 184 ? 21.17400 19.35800 3.67100   1.000 56.65000  ? 184 GLY A O     1 
ATOM   1350 N  N     . VAL A 1 185 ? 19.92900 20.61200 2.27700   1.000 45.74000  ? 185 VAL A N     1 
ATOM   1351 C  CA    . VAL A 1 185 ? 19.19000 19.47200 1.74600   1.000 51.07000  ? 185 VAL A CA    1 
ATOM   1352 C  C     . VAL A 1 185 ? 19.98800 18.81100 0.62900   1.000 59.39000  ? 185 VAL A C     1 
ATOM   1353 O  O     . VAL A 1 185 ? 19.41400 18.21900 -0.29200  1.000 62.30000  ? 185 VAL A O     1 
ATOM   1354 C  CB    . VAL A 1 185 ? 17.79500 19.90300 1.25600   1.000 49.37000  ? 185 VAL A CB    1 
ATOM   1355 C  CG1   . VAL A 1 185 ? 17.16000 20.85900 2.26000   1.000 53.24000  ? 185 VAL A CG1   1 
ATOM   1356 C  CG2   . VAL A 1 185 ? 17.88100 20.54500 -0.11700  1.000 47.73000  ? 185 VAL A CG2   1 
ATOM   1357 N  N     . ALA A 1 186 ? 21.31600 18.90800 0.71600   1.000 59.50000  ? 186 ALA A N     1 
ATOM   1358 C  CA    . ALA A 1 186 ? 22.25900 18.30300 -0.21900  1.000 53.10000  ? 186 ALA A CA    1 
ATOM   1359 C  C     . ALA A 1 186 ? 21.67500 17.98800 -1.58900  1.000 48.69000  ? 186 ALA A C     1 
ATOM   1360 O  O     . ALA A 1 186 ? 21.93300 16.91900 -2.15000  1.000 50.61000  ? 186 ALA A O     1 
ATOM   1361 C  CB    . ALA A 1 186 ? 22.83600 17.01700 0.38900   1.000 54.08000  ? 186 ALA A CB    1 
ATOM   1362 N  N     . LEU A 1 187 ? 20.89100 18.91200 -2.13200  1.000 44.15000  ? 187 LEU A N     1 
ATOM   1363 C  CA    . LEU A 1 187 ? 20.42600 18.80000 -3.50900  1.000 43.33000  ? 187 LEU A CA    1 
ATOM   1364 C  C     . LEU A 1 187 ? 21.62500 18.98100 -4.43000  1.000 51.71000  ? 187 LEU A C     1 
ATOM   1365 O  O     . LEU A 1 187 ? 22.16100 18.00400 -4.96400  1.000 62.21000  ? 187 LEU A O     1 
ATOM   1366 C  CB    . LEU A 1 187 ? 19.33900 19.83200 -3.78800  1.000 43.94000  ? 187 LEU A CB    1 
ATOM   1367 C  CG    . LEU A 1 187 ? 18.38900 19.58400 -4.96100  1.000 47.87000  ? 187 LEU A CG    1 
ATOM   1368 C  CD1   . LEU A 1 187 ? 17.98200 18.12800 -5.11300  1.000 55.22000  ? 187 LEU A CD1   1 
ATOM   1369 C  CD2   . LEU A 1 187 ? 17.14400 20.46400 -4.79900  1.000 44.15000  ? 187 LEU A CD2   1 
ATOM   1370 N  N     . LEU A 1 188 ? 22.06900 20.22500 -4.59700  1.000 50.06000  ? 188 LEU A N     1 
ATOM   1371 C  CA    . LEU A 1 188 ? 23.22800 20.51600 -5.42400  1.000 46.64000  ? 188 LEU A CA    1 
ATOM   1372 C  C     . LEU A 1 188 ? 24.42800 19.68700 -4.98600  1.000 46.18000  ? 188 LEU A C     1 
ATOM   1373 O  O     . LEU A 1 188 ? 24.64900 19.45900 -3.79300  1.000 48.67000  ? 188 LEU A O     1 
ATOM   1374 C  CB    . LEU A 1 188 ? 23.56700 22.00100 -5.34200  1.000 42.89000  ? 188 LEU A CB    1 
ATOM   1375 C  CG    . LEU A 1 188 ? 22.55200 22.97300 -5.93900  1.000 46.42000  ? 188 LEU A CG    1 
ATOM   1376 C  CD1   . LEU A 1 188 ? 22.91000 24.39900 -5.56000  1.000 43.16000  ? 188 LEU A CD1   1 
ATOM   1377 C  CD2   . LEU A 1 188 ? 22.50100 22.80700 -7.44200  1.000 55.85000  ? 188 LEU A CD2   1 
ATOM   1378 N  N     . THR A 1 189 ? 25.21500 19.24600 -5.96300  1.000 43.83000  ? 189 THR A N     1 
ATOM   1379 C  CA    . THR A 1 189 ? 26.41000 18.46900 -5.69100  1.000 42.83000  ? 189 THR A CA    1 
ATOM   1380 C  C     . THR A 1 189 ? 27.53400 19.37400 -5.20100  1.000 39.99000  ? 189 THR A C     1 
ATOM   1381 O  O     . THR A 1 189 ? 27.54800 20.57400 -5.48300  1.000 32.47000  ? 189 THR A O     1 
ATOM   1382 C  CB    . THR A 1 189 ? 26.86100 17.73200 -6.94600  1.000 50.76000  ? 189 THR A CB    1 
ATOM   1383 O  OG1   . THR A 1 189 ? 27.18700 18.68500 -7.96700  1.000 50.58000  ? 189 THR A OG1   1 
ATOM   1384 C  CG2   . THR A 1 189 ? 25.76500 16.80500 -7.44800  1.000 56.09000  ? 189 THR A CG2   1 
ATOM   1385 N  N     . PRO A 1 190 ? 28.50500 18.81400 -4.47700  1.000 39.78000  ? 190 PRO A N     1 
ATOM   1386 C  CA    . PRO A 1 190 ? 29.60300 19.65700 -3.97100  1.000 38.83000  ? 190 PRO A CA    1 
ATOM   1387 C  C     . PRO A 1 190 ? 30.30000 20.45300 -5.06300  1.000 37.58000  ? 190 PRO A C     1 
ATOM   1388 O  O     . PRO A 1 190 ? 30.65800 21.61600 -4.84400  1.000 34.18000  ? 190 PRO A O     1 
ATOM   1389 C  CB    . PRO A 1 190 ? 30.55100 18.64300 -3.31000  1.000 40.94000  ? 190 PRO A CB    1 
ATOM   1390 C  CG    . PRO A 1 190 ? 29.69800 17.43400 -3.02100  1.000 43.98000  ? 190 PRO A CG    1 
ATOM   1391 C  CD    . PRO A 1 190 ? 28.68300 17.39100 -4.12900  1.000 43.75000  ? 190 PRO A CD    1 
ATOM   1392 N  N     . THR A 1 191 ? 30.49200 19.86100 -6.24500  1.000 37.03000  ? 191 THR A N     1 
ATOM   1393 C  CA    . THR A 1 191 ? 31.24100 20.54500 -7.29400  1.000 36.63000  ? 191 THR A CA    1 
ATOM   1394 C  C     . THR A 1 191 ? 30.48500 21.76600 -7.80200  1.000 29.82000  ? 191 THR A C     1 
ATOM   1395 O  O     . THR A 1 191 ? 31.06300 22.84800 -7.95300  1.000 27.08000  ? 191 THR A O     1 
ATOM   1396 C  CB    . THR A 1 191 ? 31.53800 19.58400 -8.44500  1.000 41.54000  ? 191 THR A CB    1 
ATOM   1397 O  OG1   . THR A 1 191 ? 32.42900 18.55600 -7.99600  1.000 45.33000  ? 191 THR A OG1   1 
ATOM   1398 C  CG2   . THR A 1 191 ? 32.17400 20.33300 -9.60700  1.000 45.88000  ? 191 THR A CG2   1 
ATOM   1399 N  N     . VAL A 1 192 ? 29.19200 21.60800 -8.08800  1.000 29.06000  ? 192 VAL A N     1 
ATOM   1400 C  CA    . VAL A 1 192 ? 28.39700 22.74200 -8.54400  1.000 31.62000  ? 192 VAL A CA    1 
ATOM   1401 C  C     . VAL A 1 192 ? 28.26300 23.77700 -7.43500  1.000 27.97000  ? 192 VAL A C     1 
ATOM   1402 O  O     . VAL A 1 192 ? 28.38500 24.98400 -7.67400  1.000 26.95000  ? 192 VAL A O     1 
ATOM   1403 C  CB    . VAL A 1 192 ? 27.01900 22.26200 -9.03500  1.000 41.58000  ? 192 VAL A CB    1 
ATOM   1404 C  CG1   . VAL A 1 192 ? 26.16000 23.45000 -9.45200  1.000 39.64000  ? 192 VAL A CG1   1 
ATOM   1405 C  CG2   . VAL A 1 192 ? 27.17700 21.27300 -10.18200 1.000 50.52000  ? 192 VAL A CG2   1 
ATOM   1406 N  N     . ASP A 1 193 ? 28.01400 23.32300 -6.20500  1.000 28.16000  ? 193 ASP A N     1 
ATOM   1407 C  CA    . ASP A 1 193 ? 27.86900 24.24900 -5.08900  1.000 29.20000  ? 193 ASP A CA    1 
ATOM   1408 C  C     . ASP A 1 193 ? 29.13700 25.07000 -4.89100  1.000 26.62000  ? 193 ASP A C     1 
ATOM   1409 O  O     . ASP A 1 193 ? 29.08200 26.29200 -4.70700  1.000 30.78000  ? 193 ASP A O     1 
ATOM   1410 C  CB    . ASP A 1 193 ? 27.52500 23.47600 -3.81600  1.000 29.88000  ? 193 ASP A CB    1 
ATOM   1411 C  CG    . ASP A 1 193 ? 26.84200 24.34000 -2.78100  1.000 34.27000  ? 193 ASP A CG    1 
ATOM   1412 O  OD1   . ASP A 1 193 ? 25.67900 24.73400 -3.01100  1.000 35.78000  ? 193 ASP A OD1   1 
ATOM   1413 O  OD2   . ASP A 1 193 ? 27.47300 24.62700 -1.74200  1.000 29.64000  ? 193 ASP A OD2   1 
ATOM   1414 N  N     . VAL A 1 194 ? 30.29400 24.41000 -4.92700  1.000 29.28000  ? 194 VAL A N     1 
ATOM   1415 C  CA    . VAL A 1 194 ? 31.56100 25.12000 -4.77900  1.000 23.81000  ? 194 VAL A CA    1 
ATOM   1416 C  C     . VAL A 1 194 ? 31.75100 26.10600 -5.92700  1.000 24.78000  ? 194 VAL A C     1 
ATOM   1417 O  O     . VAL A 1 194 ? 32.12900 27.26500 -5.71800  1.000 25.20000  ? 194 VAL A O     1 
ATOM   1418 C  CB    . VAL A 1 194 ? 32.72100 24.11200 -4.69300  1.000 26.95000  ? 194 VAL A CB    1 
ATOM   1419 C  CG1   . VAL A 1 194 ? 34.04500 24.78400 -5.02900  1.000 29.73000  ? 194 VAL A CG1   1 
ATOM   1420 C  CG2   . VAL A 1 194 ? 32.76900 23.48600 -3.30500  1.000 29.27000  ? 194 VAL A CG2   1 
ATOM   1421 N  N     . ALA A 1 195 ? 31.48700 25.66000 -7.15800  1.000 21.30000  ? 195 ALA A N     1 
ATOM   1422 C  CA    . ALA A 1 195 ? 31.64400 26.54400 -8.30700  1.000 24.68000  ? 195 ALA A CA    1 
ATOM   1423 C  C     . ALA A 1 195 ? 30.82500 27.81800 -8.14100  1.000 21.73000  ? 195 ALA A C     1 
ATOM   1424 O  O     . ALA A 1 195 ? 31.30400 28.91900 -8.43600  1.000 21.08000  ? 195 ALA A O     1 
ATOM   1425 C  CB    . ALA A 1 195 ? 31.24100 25.81900 -9.59200  1.000 26.92000  ? 195 ALA A CB    1 
ATOM   1426 N  N     . LEU A 1 196 ? 29.58800 27.68900 -7.66200  1.000 21.94000  ? 196 LEU A N     1 
ATOM   1427 C  CA    . LEU A 1 196 ? 28.74300 28.86300 -7.48900  1.000 21.22000  ? 196 LEU A CA    1 
ATOM   1428 C  C     . LEU A 1 196 ? 29.29800 29.79100 -6.41400  1.000 23.96000  ? 196 LEU A C     1 
ATOM   1429 O  O     . LEU A 1 196 ? 29.25600 31.01700 -6.56500  1.000 24.43000  ? 196 LEU A O     1 
ATOM   1430 C  CB    . LEU A 1 196 ? 27.31500 28.43500 -7.15700  1.000 27.84000  ? 196 LEU A CB    1 
ATOM   1431 C  CG    . LEU A 1 196 ? 26.54800 27.79900 -8.32200  1.000 28.89000  ? 196 LEU A CG    1 
ATOM   1432 C  CD1   . LEU A 1 196 ? 25.24900 27.16000 -7.84900  1.000 32.44000  ? 196 LEU A CD1   1 
ATOM   1433 C  CD2   . LEU A 1 196 ? 26.27100 28.83600 -9.40100  1.000 34.27000  ? 196 LEU A CD2   1 
ATOM   1434 N  N     . ILE A 1 197 ? 29.83900 29.23100 -5.32900  1.000 21.16000  ? 197 ILE A N     1 
ATOM   1435 C  CA    . ILE A 1 197 ? 30.33600 30.07900 -4.25100  1.000 21.09000  ? 197 ILE A CA    1 
ATOM   1436 C  C     . ILE A 1 197 ? 31.66200 30.73000 -4.62700  1.000 22.65000  ? 197 ILE A C     1 
ATOM   1437 O  O     . ILE A 1 197 ? 31.93600 31.86700 -4.22200  1.000 22.71000  ? 197 ILE A O     1 
ATOM   1438 C  CB    . ILE A 1 197 ? 30.45100 29.27600 -2.94100  1.000 19.22000  ? 197 ILE A CB    1 
ATOM   1439 C  CG1   . ILE A 1 197 ? 29.05600 29.03000 -2.36500  1.000 30.44000  ? 197 ILE A CG1   1 
ATOM   1440 C  CG2   . ILE A 1 197 ? 31.31400 30.03200 -1.92700  1.000 23.18000  ? 197 ILE A CG2   1 
ATOM   1441 C  CD1   . ILE A 1 197 ? 28.91700 27.72300 -1.62000  1.000 42.11000  ? 197 ILE A CD1   1 
ATOM   1442 N  N     . VAL A 1 198 ? 32.51100 30.04000 -5.39300  1.000 23.48000  ? 198 VAL A N     1 
ATOM   1443 C  CA    . VAL A 1 198 ? 33.73100 30.68900 -5.86400  1.000 20.00000  ? 198 VAL A CA    1 
ATOM   1444 C  C     . VAL A 1 198 ? 33.37800 31.91200 -6.69800  1.000 19.76000  ? 198 VAL A C     1 
ATOM   1445 O  O     . VAL A 1 198 ? 34.00400 32.97200 -6.57600  1.000 24.63000  ? 198 VAL A O     1 
ATOM   1446 C  CB    . VAL A 1 198 ? 34.61300 29.71400 -6.66200  1.000 23.21000  ? 198 VAL A CB    1 
ATOM   1447 C  CG1   . VAL A 1 198 ? 35.72700 30.48000 -7.36800  1.000 26.84000  ? 198 VAL A CG1   1 
ATOM   1448 C  CG2   . VAL A 1 198 ? 35.19600 28.64600 -5.75100  1.000 29.35000  ? 198 VAL A CG2   1 
ATOM   1449 N  N     . TYR A 1 199 ? 32.37000 31.78400 -7.56500  1.000 18.39000  ? 199 TYR A N     1 
ATOM   1450 C  CA    . TYR A 1 199 ? 31.93700 32.92800 -8.35600  1.000 21.69000  ? 199 TYR A CA    1 
ATOM   1451 C  C     . TYR A 1 199 ? 31.47200 34.06700 -7.45600  1.000 21.68000  ? 199 TYR A C     1 
ATOM   1452 O  O     . TYR A 1 199 ? 31.85400 35.22600 -7.65300  1.000 22.98000  ? 199 TYR A O     1 
ATOM   1453 C  CB    . TYR A 1 199 ? 30.81700 32.53100 -9.31600  1.000 20.84000  ? 199 TYR A CB    1 
ATOM   1454 C  CG    . TYR A 1 199 ? 30.25300 33.72200 -10.05900 1.000 23.46000  ? 199 TYR A CG    1 
ATOM   1455 C  CD1   . TYR A 1 199 ? 30.90300 34.23800 -11.17000 1.000 20.10000  ? 199 TYR A CD1   1 
ATOM   1456 C  CD2   . TYR A 1 199 ? 29.08800 34.34800 -9.63400  1.000 22.67000  ? 199 TYR A CD2   1 
ATOM   1457 C  CE1   . TYR A 1 199 ? 30.40500 35.33200 -11.84900 1.000 22.70000  ? 199 TYR A CE1   1 
ATOM   1458 C  CE2   . TYR A 1 199 ? 28.58000 35.44900 -10.30600 1.000 24.30000  ? 199 TYR A CE2   1 
ATOM   1459 C  CZ    . TYR A 1 199 ? 29.24500 35.93400 -11.41400 1.000 22.09000  ? 199 TYR A CZ    1 
ATOM   1460 O  OH    . TYR A 1 199 ? 28.75400 37.02600 -12.09100 1.000 26.20000  ? 199 TYR A OH    1 
ATOM   1461 N  N     . LEU A 1 200 ? 30.63900 33.75400 -6.46000  1.000 21.27000  ? 200 LEU A N     1 
ATOM   1462 C  CA    . LEU A 1 200 ? 30.10400 34.79600 -5.58900  1.000 19.08000  ? 200 LEU A CA    1 
ATOM   1463 C  C     . LEU A 1 200 ? 31.21200 35.44600 -4.76800  1.000 17.91000  ? 200 LEU A C     1 
ATOM   1464 O  O     . LEU A 1 200 ? 31.25900 36.67400 -4.63500  1.000 19.11000  ? 200 LEU A O     1 
ATOM   1465 C  CB    . LEU A 1 200 ? 29.02500 34.21600 -4.67200  1.000 21.49000  ? 200 LEU A CB    1 
ATOM   1466 C  CG    . LEU A 1 200 ? 27.69600 33.83300 -5.33100  1.000 24.14000  ? 200 LEU A CG    1 
ATOM   1467 C  CD1   . LEU A 1 200 ? 26.84500 33.00500 -4.37600  1.000 21.52000  ? 200 LEU A CD1   1 
ATOM   1468 C  CD2   . LEU A 1 200 ? 26.92800 35.05800 -5.79600  1.000 21.99000  ? 200 LEU A CD2   1 
ATOM   1469 N  N     . ASP A 1 201 ? 32.10500 34.63600 -4.19400  1.000 16.55000  ? 201 ASP A N     1 
ATOM   1470 C  CA    . ASP A 1 201 ? 33.21500 35.18700 -3.42500  1.000 19.56000  ? 201 ASP A CA    1 
ATOM   1471 C  C     . ASP A 1 201 ? 34.02000 36.17000 -4.26800  1.000 22.73000  ? 201 ASP A C     1 
ATOM   1472 O  O     . ASP A 1 201 ? 34.35300 37.27300 -3.81500  1.000 24.80000  ? 201 ASP A O     1 
ATOM   1473 C  CB    . ASP A 1 201 ? 34.12300 34.06500 -2.92000  1.000 22.90000  ? 201 ASP A CB    1 
ATOM   1474 C  CG    . ASP A 1 201 ? 33.55100 33.33000 -1.72400  1.000 24.59000  ? 201 ASP A CG    1 
ATOM   1475 O  OD1   . ASP A 1 201 ? 32.46500 33.71100 -1.24300  1.000 23.72000  ? 201 ASP A OD1   1 
ATOM   1476 O  OD2   . ASP A 1 201 ? 34.20000 32.36600 -1.26200  1.000 25.27000  ? 201 ASP A OD2   1 
ATOM   1477 N  N     . LEU A 1 202 ? 34.34000 35.78800 -5.50600  1.000 21.78000  ? 202 LEU A N     1 
ATOM   1478 C  CA    . LEU A 1 202 ? 35.14100 36.65900 -6.35800  1.000 22.95000  ? 202 LEU A CA    1 
ATOM   1479 C  C     . LEU A 1 202 ? 34.42000 37.97200 -6.64300  1.000 20.17000  ? 202 LEU A C     1 
ATOM   1480 O  O     . LEU A 1 202 ? 35.04100 39.04200 -6.63800  1.000 23.09000  ? 202 LEU A O     1 
ATOM   1481 C  CB    . LEU A 1 202 ? 35.49200 35.94200 -7.66300  1.000 21.15000  ? 202 LEU A CB    1 
ATOM   1482 C  CG    . LEU A 1 202 ? 36.57200 34.86200 -7.55200  1.000 22.77000  ? 202 LEU A CG    1 
ATOM   1483 C  CD1   . LEU A 1 202 ? 36.67100 34.05100 -8.83800  1.000 29.51000  ? 202 LEU A CD1   1 
ATOM   1484 C  CD2   . LEU A 1 202 ? 37.92700 35.47500 -7.20200  1.000 29.85000  ? 202 LEU A CD2   1 
ATOM   1485 N  N     . VAL A 1 203 ? 33.11000 37.91600 -6.88900  1.000 20.53000  ? 203 VAL A N     1 
ATOM   1486 C  CA    . VAL A 1 203 ? 32.39000 39.13900 -7.22700  1.000 19.12000  ? 203 VAL A CA    1 
ATOM   1487 C  C     . VAL A 1 203 ? 32.19400 40.01000 -5.98900  1.000 19.60000  ? 203 VAL A C     1 
ATOM   1488 O  O     . VAL A 1 203 ? 32.36800 41.23500 -6.04600  1.000 22.73000  ? 203 VAL A O     1 
ATOM   1489 C  CB    . VAL A 1 203 ? 31.04800 38.81100 -7.90700  1.000 21.27000  ? 203 VAL A CB    1 
ATOM   1490 C  CG1   . VAL A 1 203 ? 30.24600 40.08800 -8.13800  1.000 27.77000  ? 203 VAL A CG1   1 
ATOM   1491 C  CG2   . VAL A 1 203 ? 31.27900 38.08500 -9.22900  1.000 21.94000  ? 203 VAL A CG2   1 
ATOM   1492 N  N     . THR A 1 204 ? 31.83100 39.40900 -4.85300  1.000 21.67000  ? 204 THR A N     1 
ATOM   1493 C  CA    . THR A 1 204 ? 31.57600 40.21400 -3.66200  1.000 15.53000  ? 204 THR A CA    1 
ATOM   1494 C  C     . THR A 1 204 ? 32.84900 40.78300 -3.04800  1.000 22.21000  ? 204 THR A C     1 
ATOM   1495 O  O     . THR A 1 204 ? 32.75600 41.67700 -2.20000  1.000 30.27000  ? 204 THR A O     1 
ATOM   1496 C  CB    . THR A 1 204 ? 30.83200 39.40700 -2.59200  1.000 18.02000  ? 204 THR A CB    1 
ATOM   1497 O  OG1   . THR A 1 204 ? 31.62500 38.28600 -2.18700  1.000 18.76000  ? 204 THR A OG1   1 
ATOM   1498 C  CG2   . THR A 1 204 ? 29.48300 38.93200 -3.11400  1.000 22.88000  ? 204 THR A CG2   1 
ATOM   1499 N  N     . LYS A 1 205 ? 34.02300 40.29200 -3.44300  1.000 21.22000  ? 205 LYS A N     1 
ATOM   1500 C  CA    . LYS A 1 205 ? 35.29400 40.79800 -2.94300  1.000 21.81000  ? 205 LYS A CA    1 
ATOM   1501 C  C     . LYS A 1 205 ? 36.09000 41.51100 -4.02900  1.000 27.66000  ? 205 LYS A C     1 
ATOM   1502 O  O     . LYS A 1 205 ? 36.32900 42.71900 -3.93200  1.000 31.70000  ? 205 LYS A O     1 
ATOM   1503 C  CB    . LYS A 1 205 ? 36.12000 39.65000 -2.34100  1.000 18.07000  ? 205 LYS A CB    1 
ATOM   1504 C  CG    . LYS A 1 205 ? 35.51300 39.03400 -1.08300  1.000 18.92000  ? 205 LYS A CG    1 
ATOM   1505 C  CD    . LYS A 1 205 ? 36.38400 37.90500 -0.53200  1.000 23.94000  ? 205 LYS A CD    1 
ATOM   1506 C  CE    . LYS A 1 205 ? 35.97900 37.53500 0.89200   1.000 23.08000  ? 205 LYS A CE    1 
ATOM   1507 N  NZ    . LYS A 1 205 ? 34.82600 36.59500 0.90700   1.000 25.65000  ? 205 LYS A NZ    1 
ATOM   1508 N  N     . VAL A 1 206 ? 36.50700 40.79900 -5.07700  1.000 26.16000  ? 206 VAL A N     1 
ATOM   1509 C  CA    . VAL A 1 206 ? 37.33600 41.42700 -6.10300  1.000 25.44000  ? 206 VAL A CA    1 
ATOM   1510 C  C     . VAL A 1 206 ? 36.50300 42.36700 -6.96900  1.000 24.36000  ? 206 VAL A C     1 
ATOM   1511 O  O     . VAL A 1 206 ? 36.92500 43.49200 -7.26900  1.000 25.65000  ? 206 VAL A O     1 
ATOM   1512 C  CB    . VAL A 1 206 ? 38.05000 40.34900 -6.94000  1.000 32.24000  ? 206 VAL A CB    1 
ATOM   1513 C  CG1   . VAL A 1 206 ? 38.90300 40.99500 -8.02800  1.000 35.69000  ? 206 VAL A CG1   1 
ATOM   1514 C  CG2   . VAL A 1 206 ? 38.90800 39.46600 -6.03800  1.000 32.42000  ? 206 VAL A CG2   1 
ATOM   1515 N  N     . GLY A 1 207 ? 35.31400 41.93200 -7.38600  1.000 24.96000  ? 207 GLY A N     1 
ATOM   1516 C  CA    . GLY A 1 207 ? 34.43500 42.83200 -8.11900  1.000 23.91000  ? 207 GLY A CA    1 
ATOM   1517 C  C     . GLY A 1 207 ? 34.10100 44.07800 -7.32100  1.000 32.11000  ? 207 GLY A C     1 
ATOM   1518 O  O     . GLY A 1 207 ? 34.26300 45.20400 -7.79900  1.000 28.22000  ? 207 GLY A O     1 
ATOM   1519 N  N     . PHE A 1 208 ? 33.60400 43.88300 -6.09800  1.000 31.31000  ? 208 PHE A N     1 
ATOM   1520 C  CA    . PHE A 1 208 ? 33.44500 44.96400 -5.12900  1.000 26.92000  ? 208 PHE A CA    1 
ATOM   1521 C  C     . PHE A 1 208 ? 34.63400 45.91800 -5.16000  1.000 28.97000  ? 208 PHE A C     1 
ATOM   1522 O  O     . PHE A 1 208 ? 34.47300 47.13000 -5.34200  1.000 26.50000  ? 208 PHE A O     1 
ATOM   1523 C  CB    . PHE A 1 208 ? 33.26900 44.32200 -3.74400  1.000 24.74000  ? 208 PHE A CB    1 
ATOM   1524 C  CG    . PHE A 1 208 ? 32.94200 45.28300 -2.63700  1.000 28.66000  ? 208 PHE A CG    1 
ATOM   1525 C  CD1   . PHE A 1 208 ? 33.95000 45.93000 -1.94300  1.000 31.18000  ? 208 PHE A CD1   1 
ATOM   1526 C  CD2   . PHE A 1 208 ? 31.62700 45.50300 -2.25500  1.000 30.81000  ? 208 PHE A CD2   1 
ATOM   1527 C  CE1   . PHE A 1 208 ? 33.65400 46.80000 -0.91000  1.000 32.42000  ? 208 PHE A CE1   1 
ATOM   1528 C  CE2   . PHE A 1 208 ? 31.32500 46.37100 -1.22300  1.000 32.38000  ? 208 PHE A CE2   1 
ATOM   1529 C  CZ    . PHE A 1 208 ? 32.34100 47.01900 -0.55000  1.000 33.47000  ? 208 PHE A CZ    1 
ATOM   1530 N  N     . GLY A 1 209 ? 35.84200 45.37700 -5.00700  1.000 34.30000  ? 209 GLY A N     1 
ATOM   1531 C  CA    . GLY A 1 209 ? 37.01700 46.22800 -4.94900  1.000 39.21000  ? 209 GLY A CA    1 
ATOM   1532 C  C     . GLY A 1 209 ? 37.22100 47.05000 -6.20800  1.000 40.55000  ? 209 GLY A C     1 
ATOM   1533 O  O     . GLY A 1 209 ? 37.51400 48.24600 -6.13800  1.000 40.26000  ? 209 GLY A O     1 
ATOM   1534 N  N     . PHE A 1 210 ? 37.07200 46.42600 -7.37600  1.000 38.54000  ? 210 PHE A N     1 
ATOM   1535 C  CA    . PHE A 1 210 ? 37.35300 47.13800 -8.61700  1.000 37.86000  ? 210 PHE A CA    1 
ATOM   1536 C  C     . PHE A 1 210 ? 36.32800 48.23400 -8.88200  1.000 38.86000  ? 210 PHE A C     1 
ATOM   1537 O  O     . PHE A 1 210 ? 36.67700 49.28100 -9.44100  1.000 41.22000  ? 210 PHE A O     1 
ATOM   1538 C  CB    . PHE A 1 210 ? 37.41800 46.15600 -9.78300  1.000 38.25000  ? 210 PHE A CB    1 
ATOM   1539 C  CG    . PHE A 1 210 ? 38.76600 45.50900 -9.94200  1.000 45.12000  ? 210 PHE A CG    1 
ATOM   1540 C  CD1   . PHE A 1 210 ? 39.91900 46.27700 -9.96200  1.000 53.61000  ? 210 PHE A CD1   1 
ATOM   1541 C  CD2   . PHE A 1 210 ? 38.88300 44.13500 -10.05500 1.000 46.58000  ? 210 PHE A CD2   1 
ATOM   1542 C  CE1   . PHE A 1 210 ? 41.16000 45.69000 -10.10300 1.000 55.92000  ? 210 PHE A CE1   1 
ATOM   1543 C  CE2   . PHE A 1 210 ? 40.12500 43.54100 -10.19500 1.000 47.36000  ? 210 PHE A CE2   1 
ATOM   1544 C  CZ    . PHE A 1 210 ? 41.26300 44.32000 -10.21700 1.000 50.50000  ? 210 PHE A CZ    1 
ATOM   1545 N  N     . ILE A 1 211 ? 35.07200 48.02800 -8.48000  1.000 41.37000  ? 211 ILE A N     1 
ATOM   1546 C  CA    . ILE A 1 211 ? 34.09700 49.10800 -8.59300  1.000 42.34000  ? 211 ILE A CA    1 
ATOM   1547 C  C     . ILE A 1 211 ? 34.52800 50.30000 -7.75100  1.000 44.36000  ? 211 ILE A C     1 
ATOM   1548 O  O     . ILE A 1 211 ? 34.30000 51.45500 -8.13200  1.000 48.81000  ? 211 ILE A O     1 
ATOM   1549 C  CB    . ILE A 1 211 ? 32.69300 48.61600 -8.18800  1.000 40.84000  ? 211 ILE A CB    1 
ATOM   1550 C  CG1   . ILE A 1 211 ? 32.14500 47.65500 -9.24200  1.000 43.13000  ? 211 ILE A CG1   1 
ATOM   1551 C  CG2   . ILE A 1 211 ? 31.75500 49.80000 -8.00300  1.000 37.29000  ? 211 ILE A CG2   1 
ATOM   1552 C  CD1   . ILE A 1 211 ? 31.07900 46.72100 -8.71500  1.000 42.02000  ? 211 ILE A CD1   1 
ATOM   1553 N  N     . ALA A 1 212 ? 35.15300 50.04900 -6.59900  1.000 45.22000  ? 212 ALA A N     1 
ATOM   1554 C  CA    . ALA A 1 212 ? 35.63400 51.14800 -5.76900  1.000 48.33000  ? 212 ALA A CA    1 
ATOM   1555 C  C     . ALA A 1 212 ? 36.80700 51.85800 -6.43700  1.000 50.68000  ? 212 ALA A C     1 
ATOM   1556 O  O     . ALA A 1 212 ? 36.84200 53.09200 -6.50600  1.000 48.75000  ? 212 ALA A O     1 
ATOM   1557 C  CB    . ALA A 1 212 ? 36.02900 50.63300 -4.38400  1.000 40.32000  ? 212 ALA A CB    1 
ATOM   1558 N  N     . LEU A 1 213 ? 37.77700 51.09100 -6.93800  1.000 53.00000  ? 213 LEU A N     1 
ATOM   1559 C  CA    . LEU A 1 213 ? 38.90400 51.69300 -7.64400  1.000 57.73000  ? 213 LEU A CA    1 
ATOM   1560 C  C     . LEU A 1 213 ? 38.42100 52.57700 -8.78700  1.000 56.76000  ? 213 LEU A C     1 
ATOM   1561 O  O     . LEU A 1 213 ? 38.88200 53.71300 -8.95100  1.000 56.40000  ? 213 LEU A O     1 
ATOM   1562 C  CB    . LEU A 1 213 ? 39.82900 50.60400 -8.18200  1.000 56.50000  ? 213 LEU A CB    1 
ATOM   1563 C  CG    . LEU A 1 213 ? 40.67500 49.77800 -7.21600  1.000 61.78000  ? 213 LEU A CG    1 
ATOM   1564 C  CD1   . LEU A 1 213 ? 41.69400 48.97000 -8.02300  1.000 63.16000  ? 213 LEU A CD1   1 
ATOM   1565 C  CD2   . LEU A 1 213 ? 41.36500 50.63900 -6.18500  1.000 64.78000  ? 213 LEU A CD2   1 
ATOM   1566 N  N     . ASP A 1 214 ? 37.49100 52.06200 -9.59400  1.000 57.09000  ? 214 ASP A N     1 
ATOM   1567 C  CA    . ASP A 1 214 ? 36.99000 52.82100 -10.73500 1.000 59.91000  ? 214 ASP A CA    1 
ATOM   1568 C  C     . ASP A 1 214 ? 36.49300 54.19400 -10.30800 1.000 64.40000  ? 214 ASP A C     1 
ATOM   1569 O  O     . ASP A 1 214 ? 36.75700 55.19600 -10.98100 1.000 69.15000  ? 214 ASP A O     1 
ATOM   1570 C  CB    . ASP A 1 214 ? 35.87100 52.04300 -11.42700 1.000 62.88000  ? 214 ASP A CB    1 
ATOM   1571 C  CG    . ASP A 1 214 ? 35.50800 52.62200 -12.77700 1.000 67.50000  ? 214 ASP A CG    1 
ATOM   1572 O  OD1   . ASP A 1 214 ? 36.42900 52.86900 -13.58300 1.000 71.08000  ? 214 ASP A OD1   1 
ATOM   1573 O  OD2   . ASP A 1 214 ? 34.30200 52.83700 -13.03000 1.000 72.01000  ? 214 ASP A OD2   1 
ATOM   1574 N  N     . ALA A 1 215 ? 35.77200 54.26000 -9.18700  1.000 64.49000  ? 215 ALA A N     1 
ATOM   1575 C  CA    . ALA A 1 215 ? 35.22800 55.53500 -8.73700  1.000 64.74000  ? 215 ALA A CA    1 
ATOM   1576 C  C     . ALA A 1 215 ? 36.30800 56.43700 -8.15800  1.000 72.52000  ? 215 ALA A C     1 
ATOM   1577 O  O     . ALA A 1 215 ? 36.19500 57.66600 -8.23900  1.000 78.49000  ? 215 ALA A O     1 
ATOM   1578 C  CB    . ALA A 1 215 ? 34.12500 55.29600 -7.70600  1.000 57.39000  ? 215 ALA A CB    1 
ATOM   1579 N  N     . ALA A 1 216 ? 37.36000 55.85500 -7.57900  1.000 75.43000  ? 216 ALA A N     1 
ATOM   1580 C  CA    . ALA A 1 216 ? 38.42700 56.66100 -6.99600  1.000 79.46000  ? 216 ALA A CA    1 
ATOM   1581 C  C     . ALA A 1 216 ? 39.21500 57.43100 -8.04900  1.000 85.25000  ? 216 ALA A C     1 
ATOM   1582 O  O     . ALA A 1 216 ? 39.85100 58.43600 -7.71600  1.000 83.60000  ? 216 ALA A O     1 
ATOM   1583 C  CB    . ALA A 1 216 ? 39.37600 55.77400 -6.18800  1.000 81.34000  ? 216 ALA A CB    1 
ATOM   1584 N  N     . ALA A 1 217 ? 39.19500 56.98100 -9.30200  1.000 89.97000  ? 217 ALA A N     1 
ATOM   1585 C  CA    . ALA A 1 217 ? 39.84200 57.71200 -10.38400 1.000 95.99000  ? 217 ALA A CA    1 
ATOM   1586 C  C     . ALA A 1 217 ? 38.91700 58.73300 -11.02800 1.000 99.97000  ? 217 ALA A C     1 
ATOM   1587 O  O     . ALA A 1 217 ? 39.39400 59.73500 -11.57200 1.000 106.17000 ? 217 ALA A O     1 
ATOM   1588 C  CB    . ALA A 1 217 ? 40.34500 56.73800 -11.45300 1.000 97.39000  ? 217 ALA A CB    1 
ATOM   1589 N  N     . THR A 1 218 ? 37.60200 58.50400 -10.97500 1.000 103.17000 ? 218 THR A N     1 
ATOM   1590 C  CA    . THR A 1 218 ? 36.64800 59.42600 -11.57500 1.000 109.53000 ? 218 THR A CA    1 
ATOM   1591 C  C     . THR A 1 218 ? 36.49300 60.71500 -10.77900 1.000 105.74000 ? 218 THR A C     1 
ATOM   1592 O  O     . THR A 1 218 ? 35.82800 61.64000 -11.25900 1.000 103.08000 ? 218 THR A O     1 
ATOM   1593 C  CB    . THR A 1 218 ? 35.27900 58.75400 -11.71400 1.000 109.63000 ? 218 THR A CB    1 
ATOM   1594 O  OG1   . THR A 1 218 ? 34.84800 58.26400 -10.43800 1.000 111.76000 ? 218 THR A OG1   1 
ATOM   1595 C  CG2   . THR A 1 218 ? 35.34500 57.59900 -12.70500 1.000 104.98000 ? 218 THR A CG2   1 
ATOM   1596 N  N     . LEU A 1 219 ? 37.07600 60.79800 -9.58800  1.000 103.40000 ? 219 LEU A N     1 
ATOM   1597 C  CA    . LEU A 1 219 ? 37.00100 62.00500 -8.77400  1.000 110.01000 ? 219 LEU A CA    1 
ATOM   1598 C  C     . LEU A 1 219 ? 37.36600 63.24000 -9.59200  1.000 115.01000 ? 219 LEU A C     1 
ATOM   1599 O  O     . LEU A 1 219 ? 37.00200 64.36200 -9.24000  1.000 112.18000 ? 219 LEU A O     1 
ATOM   1600 C  CB    . LEU A 1 219 ? 37.92900 61.89300 -7.56400  1.000 110.39000 ? 219 LEU A CB    1 
ATOM   1601 C  CG    . LEU A 1 219 ? 37.69700 60.74600 -6.57800  1.000 107.94000 ? 219 LEU A CG    1 
ATOM   1602 C  CD1   . LEU A 1 219 ? 38.22000 61.14000 -5.19800  1.000 106.30000 ? 219 LEU A CD1   1 
ATOM   1603 C  CD2   . LEU A 1 219 ? 36.23300 60.35300 -6.50500  1.000 108.12000 ? 219 LEU A CD2   1 
HETATM 1604 C  C1    . RET B 2 .   ? 25.06100 31.73800 5.61600   1.000 23.16000  ? 301 RET A C1    1 
HETATM 1605 C  C2    . RET B 2 .   ? 24.20700 30.70600 6.36900   1.000 20.96000  ? 301 RET A C2    1 
HETATM 1606 C  C3    . RET B 2 .   ? 23.32200 31.28700 7.45900   1.000 23.22000  ? 301 RET A C3    1 
HETATM 1607 C  C4    . RET B 2 .   ? 22.41300 32.36800 6.91100   1.000 22.84000  ? 301 RET A C4    1 
HETATM 1608 C  C5    . RET B 2 .   ? 23.06800 33.26700 5.89500   1.000 22.60000  ? 301 RET A C5    1 
HETATM 1609 C  C6    . RET B 2 .   ? 24.32800 33.07800 5.46400   1.000 18.98000  ? 301 RET A C6    1 
HETATM 1610 C  C7    . RET B 2 .   ? 25.02200 34.13200 4.73900   1.000 19.26000  ? 301 RET A C7    1 
HETATM 1611 C  C8    . RET B 2 .   ? 26.22600 34.09700 4.11200   1.000 18.73000  ? 301 RET A C8    1 
HETATM 1612 C  C9    . RET B 2 .   ? 26.86600 35.20400 3.41500   1.000 21.47000  ? 301 RET A C9    1 
HETATM 1613 C  C10   . RET B 2 .   ? 28.14200 35.05500 2.98000   1.000 21.64000  ? 301 RET A C10   1 
HETATM 1614 C  C11   . RET B 2 .   ? 28.96300 36.03200 2.32100   1.000 22.62000  ? 301 RET A C11   1 
HETATM 1615 C  C12   . RET B 2 .   ? 30.25100 35.80400 2.02900   1.000 21.57000  ? 301 RET A C12   1 
HETATM 1616 C  C13   . RET B 2 .   ? 31.18500 36.73900 1.42400   1.000 20.47000  ? 301 RET A C13   1 
HETATM 1617 C  C14   . RET B 2 .   ? 32.49100 36.39100 1.32400   1.000 20.50000  ? 301 RET A C14   1 
HETATM 1618 C  C15   . RET B 2 .   ? 33.56900 37.18300 0.79400   1.000 20.26000  ? 301 RET A C15   1 
HETATM 1619 C  C16   . RET B 2 .   ? 26.36500 31.92700 6.40200   1.000 19.88000  ? 301 RET A C16   1 
HETATM 1620 C  C17   . RET B 2 .   ? 25.39200 31.14200 4.24200   1.000 25.75000  ? 301 RET A C17   1 
HETATM 1621 C  C18   . RET B 2 .   ? 22.29200 34.53900 5.68600   1.000 22.81000  ? 301 RET A C18   1 
HETATM 1622 C  C19   . RET B 2 .   ? 26.07200 36.46500 3.20800   1.000 18.55000  ? 301 RET A C19   1 
HETATM 1623 C  C20   . RET B 2 .   ? 30.66200 38.08100 0.99300   1.000 22.32000  ? 301 RET A C20   1 
HETATM 1624 CL CL    . CL  C 3 .   ? 30.91700 23.90200 3.54300   1.000 49.05000  ? 302 CL  A CL    1 
HETATM 1625 C  C1    . BOG D 4 .   ? 41.97900 21.96400 10.14000  1.000 116.31000 ? 303 BOG A C1    1 
HETATM 1626 O  O1    . BOG D 4 .   ? 41.48700 23.19500 9.79600   1.000 111.83000 ? 303 BOG A O1    1 
HETATM 1627 C  C2    . BOG D 4 .   ? 40.86300 21.15200 10.80800  1.000 122.49000 ? 303 BOG A C2    1 
HETATM 1628 O  O2    . BOG D 4 .   ? 40.66800 21.59500 12.15400  1.000 128.27000 ? 303 BOG A O2    1 
HETATM 1629 C  C3    . BOG D 4 .   ? 41.13400 19.67500 10.82100  1.000 128.14000 ? 303 BOG A C3    1 
HETATM 1630 O  O3    . BOG D 4 .   ? 40.73900 19.15300 12.10600  1.000 133.58000 ? 303 BOG A O3    1 
HETATM 1631 C  C4    . BOG D 4 .   ? 42.60000 19.38300 10.57600  1.000 130.29000 ? 303 BOG A C4    1 
HETATM 1632 O  O4    . BOG D 4 .   ? 42.85500 17.98900 10.67500  1.000 136.66000 ? 303 BOG A O4    1 
HETATM 1633 C  C5    . BOG D 4 .   ? 43.02100 19.89900 9.18100   1.000 142.08000 ? 303 BOG A C5    1 
HETATM 1634 O  O5    . BOG D 4 .   ? 42.51300 21.26900 8.90900   1.000 122.16000 ? 303 BOG A O5    1 
HETATM 1635 C  C6    . BOG D 4 .   ? 42.50400 18.96400 8.11300   1.000 156.59000 ? 303 BOG A C6    1 
HETATM 1636 O  O6    . BOG D 4 .   ? 43.46800 18.78900 7.12600   1.000 159.80000 ? 303 BOG A O6    1 
HETATM 1637 C  "C1'" . BOG D 4 .   ? 42.46700 24.17400 9.52200   1.000 109.37000 ? 303 BOG A "C1'" 1 
HETATM 1638 C  "C2'" . BOG D 4 .   ? 41.78000 25.37400 8.86100   1.000 103.19000 ? 303 BOG A "C2'" 1 
HETATM 1639 C  "C3'" . BOG D 4 .   ? 42.70600 26.57300 8.62200   1.000 95.06000  ? 303 BOG A "C3'" 1 
HETATM 1640 C  "C4'" . BOG D 4 .   ? 42.06300 27.60000 7.69100   1.000 87.62000  ? 303 BOG A "C4'" 1 
HETATM 1641 C  "C5'" . BOG D 4 .   ? 42.48300 29.04200 7.95600   1.000 80.26000  ? 303 BOG A "C5'" 1 
HETATM 1642 C  "C6'" . BOG D 4 .   ? 42.45100 29.88500 6.68700   1.000 71.24000  ? 303 BOG A "C6'" 1 
HETATM 1643 C  "C7'" . BOG D 4 .   ? 42.10100 31.34400 6.92800   1.000 66.28000  ? 303 BOG A "C7'" 1 
HETATM 1644 C  "C8'" . BOG D 4 .   ? 43.28800 32.14200 7.44000   1.000 63.61000  ? 303 BOG A "C8'" 1 
HETATM 1645 C  C1    . BOG E 4 .   ? 30.28200 18.49000 -12.79300 1.000 96.28000  ? 304 BOG A C1    1 
HETATM 1646 O  O1    . BOG E 4 .   ? 30.03600 19.83900 -12.75700 1.000 97.56000  ? 304 BOG A O1    1 
HETATM 1647 C  C2    . BOG E 4 .   ? 31.76100 18.14200 -12.70300 1.000 96.48000  ? 304 BOG A C2    1 
HETATM 1648 O  O2    . BOG E 4 .   ? 32.22600 17.82300 -14.01800 1.000 105.20000 ? 304 BOG A O2    1 
HETATM 1649 C  C3    . BOG E 4 .   ? 32.05200 16.99400 -11.78400 1.000 100.52000 ? 304 BOG A C3    1 
HETATM 1650 O  O3    . BOG E 4 .   ? 33.23000 16.32200 -12.30100 1.000 108.84000 ? 304 BOG A O3    1 
HETATM 1651 C  C4    . BOG E 4 .   ? 31.00000 15.91600 -11.63500 1.000 103.95000 ? 304 BOG A C4    1 
HETATM 1652 O  O4    . BOG E 4 .   ? 31.35400 15.10400 -10.51500 1.000 107.44000 ? 304 BOG A O4    1 
HETATM 1653 C  C5    . BOG E 4 .   ? 29.58500 16.46900 -11.44500 1.000 104.19000 ? 304 BOG A C5    1 
HETATM 1654 O  O5    . BOG E 4 .   ? 29.50800 17.93700 -11.61900 1.000 102.61000 ? 304 BOG A O5    1 
HETATM 1655 C  C6    . BOG E 4 .   ? 29.01400 16.17900 -10.09000 1.000 121.54000 ? 304 BOG A C6    1 
HETATM 1656 O  O6    . BOG E 4 .   ? 27.91500 17.00400 -9.89800  1.000 124.40000 ? 304 BOG A O6    1 
HETATM 1657 C  "C1'" . BOG E 4 .   ? 30.84200 20.67300 -13.55700 1.000 97.67000  ? 304 BOG A "C1'" 1 
HETATM 1658 C  "C2'" . BOG E 4 .   ? 30.05000 21.94400 -13.86100 1.000 93.33000  ? 304 BOG A "C2'" 1 
HETATM 1659 C  "C3'" . BOG E 4 .   ? 30.29900 23.07300 -12.85900 1.000 88.01000  ? 304 BOG A "C3'" 1 
HETATM 1660 C  "C4'" . BOG E 4 .   ? 30.42200 24.42600 -13.55000 1.000 91.59000  ? 304 BOG A "C4'" 1 
HETATM 1661 C  "C5'" . BOG E 4 .   ? 31.86700 24.74600 -13.92100 1.000 91.33000  ? 304 BOG A "C5'" 1 
HETATM 1662 C  "C6'" . BOG E 4 .   ? 32.06300 26.23300 -14.16300 1.000 88.72000  ? 304 BOG A "C6'" 1 
HETATM 1663 C  "C7'" . BOG E 4 .   ? 33.47400 26.70600 -13.85700 1.000 81.21000  ? 304 BOG A "C7'" 1 
HETATM 1664 C  "C8'" . BOG E 4 .   ? 33.49400 28.18200 -13.50500 1.000 79.22000  ? 304 BOG A "C8'" 1 
HETATM 1665 C  C1    . BOG F 4 .   ? 50.16700 44.02700 2.35000   1.000 131.33000 ? 305 BOG A C1    1 
HETATM 1666 O  O1    . BOG F 4 .   ? 50.19200 44.28400 3.67600   1.000 128.96000 ? 305 BOG A O1    1 
HETATM 1667 C  C2    . BOG F 4 .   ? 51.30500 44.76000 1.62800   1.000 138.13000 ? 305 BOG A C2    1 
HETATM 1668 O  O2    . BOG F 4 .   ? 51.36100 46.13800 1.95000   1.000 131.86000 ? 305 BOG A O2    1 
HETATM 1669 C  C3    . BOG F 4 .   ? 51.14300 44.59200 0.14500   1.000 140.84000 ? 305 BOG A C3    1 
HETATM 1670 O  O3    . BOG F 4 .   ? 52.16800 45.31400 -0.58200  1.000 134.86000 ? 305 BOG A O3    1 
HETATM 1671 C  C4    . BOG F 4 .   ? 51.19100 43.12300 -0.24800  1.000 143.06000 ? 305 BOG A C4    1 
HETATM 1672 O  O4    . BOG F 4 .   ? 50.82800 42.97600 -1.59600  1.000 140.41000 ? 305 BOG A O4    1 
HETATM 1673 C  C5    . BOG F 4 .   ? 50.26500 42.23600 0.62600   1.000 144.12000 ? 305 BOG A C5    1 
HETATM 1674 O  O5    . BOG F 4 .   ? 50.29900 42.53000 2.06500   1.000 135.98000 ? 305 BOG A O5    1 
HETATM 1675 C  C6    . BOG F 4 .   ? 50.67800 40.79000 0.42500   1.000 151.20000 ? 305 BOG A C6    1 
HETATM 1676 O  O6    . BOG F 4 .   ? 50.22900 39.97500 1.46400   1.000 157.47000 ? 305 BOG A O6    1 
HETATM 1677 C  "C1'" . BOG F 4 .   ? 49.04500 45.07100 4.10100   1.000 126.86000 ? 305 BOG A "C1'" 1 
HETATM 1678 C  "C2'" . BOG F 4 .   ? 49.27300 46.56600 3.84900   1.000 128.69000 ? 305 BOG A "C2'" 1 
HETATM 1679 C  "C3'" . BOG F 4 .   ? 48.65600 46.98400 2.53300   1.000 134.72000 ? 305 BOG A "C3'" 1 
HETATM 1680 C  "C4'" . BOG F 4 .   ? 49.37900 48.25500 1.98700   1.000 129.77000 ? 305 BOG A "C4'" 1 
HETATM 1681 C  "C5'" . BOG F 4 .   ? 48.43200 49.02600 0.99100   1.000 120.98000 ? 305 BOG A "C5'" 1 
HETATM 1682 C  "C6'" . BOG F 4 .   ? 49.23500 49.84200 -0.00800  1.000 114.71000 ? 305 BOG A "C6'" 1 
HETATM 1683 C  "C7'" . BOG F 4 .   ? 50.20200 50.78300 0.71400   1.000 118.19000 ? 305 BOG A "C7'" 1 
HETATM 1684 C  "C8'" . BOG F 4 .   ? 49.41500 51.74700 1.67500   1.000 110.79000 ? 305 BOG A "C8'" 1 
HETATM 1685 C  C2    . MPG G 5 .   ? 37.31400 28.12300 15.15400  1.000 106.21000 ? 306 MPG A C2    1 
HETATM 1686 C  C3    . MPG G 5 .   ? 37.72900 29.59600 15.13100  1.000 106.04000 ? 306 MPG A C3    1 
HETATM 1687 C  C4    . MPG G 5 .   ? 36.49900 30.48900 14.94600  1.000 95.43000  ? 306 MPG A C4    1 
HETATM 1688 C  C5    . MPG G 5 .   ? 36.93000 31.95300 14.82900  1.000 87.52000  ? 306 MPG A C5    1 
HETATM 1689 C  C6    . MPG G 5 .   ? 36.19400 32.83400 15.84600  1.000 91.36000  ? 306 MPG A C6    1 
HETATM 1690 C  C7    . MPG G 5 .   ? 35.71500 34.11200 15.14900  1.000 86.16000  ? 306 MPG A C7    1 
HETATM 1691 C  C8    . MPG G 5 .   ? 35.45700 35.26700 16.12500  1.000 93.96000  ? 306 MPG A C8    1 
HETATM 1692 C  C9    . MPG G 5 .   ? 35.80600 36.57500 15.40400  1.000 94.52000  ? 306 MPG A C9    1 
HETATM 1693 C  C10   . MPG G 5 .   ? 34.88700 37.47900 15.11100  1.000 96.65000  ? 306 MPG A C10   1 
HETATM 1694 C  C11   . MPG G 5 .   ? 35.29300 38.75900 14.37200  1.000 100.06000 ? 306 MPG A C11   1 
HETATM 1695 C  C12   . MPG G 5 .   ? 34.84900 40.01100 15.12400  1.000 102.99000 ? 306 MPG A C12   1 
HETATM 1696 C  C13   . MPG G 5 .   ? 34.96300 41.26700 14.24900  1.000 99.84000  ? 306 MPG A C13   1 
HETATM 1697 C  C14   . MPG G 5 .   ? 36.10300 41.16200 13.23200  1.000 90.81000  ? 306 MPG A C14   1 
HETATM 1698 C  C15   . MPG G 5 .   ? 36.42200 42.54200 12.64900  1.000 83.17000  ? 306 MPG A C15   1 
HETATM 1699 C  C16   . MPG G 5 .   ? 37.90300 42.61900 12.27200  1.000 73.00000  ? 306 MPG A C16   1 
HETATM 1700 C  C17   . MPG G 5 .   ? 38.16400 41.85400 10.97600  1.000 77.08000  ? 306 MPG A C17   1 
HETATM 1701 C  C18   . MPG G 5 .   ? 39.63100 41.43300 10.91100  1.000 84.02000  ? 306 MPG A C18   1 
HETATM 1702 O  O1    . MPG G 5 .   ? 38.13600 25.90400 14.73500  1.000 96.99000  ? 306 MPG A O1    1 
HETATM 1703 C  C1    . MPG G 5 .   ? 38.36500 27.25900 14.45100  1.000 99.30000  ? 306 MPG A C1    1 
HETATM 1704 C  CXD   . MPG G 5 .   ? 37.38700 24.17500 13.04100  1.000 109.76000 ? 306 MPG A CXD   1 
HETATM 1705 O  O2    . MPG G 5 .   ? 36.46100 23.71600 13.96700  1.000 105.77000 ? 306 MPG A O2    1 
HETATM 1706 C  C21   . MPG G 5 .   ? 37.97800 22.96700 12.32100  1.000 114.19000 ? 306 MPG A C21   1 
HETATM 1707 O  O3    . MPG G 5 .   ? 36.96900 22.07100 12.00200  1.000 107.81000 ? 306 MPG A O3    1 
HETATM 1708 O  O4    . MPG G 5 .   ? 39.59800 24.91000 13.34600  1.000 98.53000  ? 306 MPG A O4    1 
HETATM 1709 C  CX3   . MPG G 5 .   ? 38.47400 25.01100 13.70700  1.000 104.67000 ? 306 MPG A CX3   1 
HETATM 1710 C  C1    . BOG H 4 .   ? 47.68200 24.17800 8.16300   1.000 131.23000 ? 307 BOG A C1    1 
HETATM 1711 O  O1    . BOG H 4 .   ? 48.14400 25.45100 8.05500   1.000 121.40000 ? 307 BOG A O1    1 
HETATM 1712 C  C2    . BOG H 4 .   ? 48.82100 23.20000 7.90900   1.000 137.23000 ? 307 BOG A C2    1 
HETATM 1713 O  O2    . BOG H 4 .   ? 49.30900 23.38100 6.58200   1.000 127.03000 ? 307 BOG A O2    1 
HETATM 1714 C  C3    . BOG H 4 .   ? 48.37000 21.79400 8.12100   1.000 136.19000 ? 307 BOG A C3    1 
HETATM 1715 O  O3    . BOG H 4 .   ? 49.50000 20.90700 7.94700   1.000 129.22000 ? 307 BOG A O3    1 
HETATM 1716 C  C4    . BOG H 4 .   ? 47.76100 21.57700 9.49700   1.000 132.64000 ? 307 BOG A C4    1 
HETATM 1717 O  O4    . BOG H 4 .   ? 47.21300 20.28800 9.55700   1.000 137.06000 ? 307 BOG A O4    1 
HETATM 1718 C  C5    . BOG H 4 .   ? 46.65100 22.61000 9.80900   1.000 123.23000 ? 307 BOG A C5    1 
HETATM 1719 O  O5    . BOG H 4 .   ? 47.05100 23.99500 9.53600   1.000 122.74000 ? 307 BOG A O5    1 
HETATM 1720 C  C6    . BOG H 4 .   ? 46.27900 22.50500 11.27300  1.000 130.20000 ? 307 BOG A C6    1 
HETATM 1721 O  O6    . BOG H 4 .   ? 45.68800 21.27100 11.55200  1.000 128.07000 ? 307 BOG A O6    1 
HETATM 1722 C  "C1'" . BOG H 4 .   ? 47.44300 26.26400 7.07900   1.000 110.69000 ? 307 BOG A "C1'" 1 
HETATM 1723 C  "C2'" . BOG H 4 .   ? 47.55800 27.74400 7.45300   1.000 109.62000 ? 307 BOG A "C2'" 1 
HETATM 1724 C  "C3'" . BOG H 4 .   ? 48.69500 28.38000 6.68900   1.000 114.83000 ? 307 BOG A "C3'" 1 
HETATM 1725 C  "C4'" . BOG H 4 .   ? 48.71900 29.91700 6.96100   1.000 110.95000 ? 307 BOG A "C4'" 1 
HETATM 1726 C  "C5'" . BOG H 4 .   ? 50.08000 30.51600 6.44300   1.000 112.10000 ? 307 BOG A "C5'" 1 
HETATM 1727 C  "C6'" . BOG H 4 .   ? 49.96500 32.02100 6.28500   1.000 119.30000 ? 307 BOG A "C6'" 1 
HETATM 1728 C  "C7'" . BOG H 4 .   ? 51.13800 32.53400 5.44600   1.000 118.41000 ? 307 BOG A "C7'" 1 
HETATM 1729 C  "C8'" . BOG H 4 .   ? 50.85700 34.01000 4.98200   1.000 111.73000 ? 307 BOG A "C8'" 1 
HETATM 1730 C  C1    . BOG I 4 .   ? 50.72500 19.37700 1.11000   1.000 134.42000 ? 308 BOG A C1    1 
HETATM 1731 O  O1    . BOG I 4 .   ? 49.46100 18.89400 1.27200   1.000 137.24000 ? 308 BOG A O1    1 
HETATM 1732 C  C2    . BOG I 4 .   ? 50.92000 19.69700 -0.37600  1.000 136.79000 ? 308 BOG A C2    1 
HETATM 1733 O  O2    . BOG I 4 .   ? 51.00800 18.48100 -1.12300  1.000 147.32000 ? 308 BOG A O2    1 
HETATM 1734 C  C3    . BOG I 4 .   ? 52.15300 20.51400 -0.60300  1.000 129.62000 ? 308 BOG A C3    1 
HETATM 1735 O  O3    . BOG I 4 .   ? 52.24800 20.88400 -1.99800  1.000 124.51000 ? 308 BOG A O3    1 
HETATM 1736 C  C4    . BOG I 4 .   ? 52.16300 21.76900 0.25700   1.000 124.74000 ? 308 BOG A C4    1 
HETATM 1737 O  O4    . BOG I 4 .   ? 53.31900 22.51200 0.01200   1.000 122.33000 ? 308 BOG A O4    1 
HETATM 1738 C  C5    . BOG I 4 .   ? 52.07700 21.40100 1.75500   1.000 127.79000 ? 308 BOG A C5    1 
HETATM 1739 O  O5    . BOG I 4 .   ? 50.89100 20.57700 2.04100   1.000 129.83000 ? 308 BOG A O5    1 
HETATM 1740 C  C6    . BOG I 4 .   ? 52.01300 22.65800 2.60300   1.000 124.09000 ? 308 BOG A C6    1 
HETATM 1741 O  O6    . BOG I 4 .   ? 53.09100 23.50300 2.30800   1.000 120.62000 ? 308 BOG A O6    1 
HETATM 1742 C  "C1'" . BOG I 4 .   ? 49.27500 17.91800 2.32700   1.000 128.35000 ? 308 BOG A "C1'" 1 
HETATM 1743 C  "C2'" . BOG I 4 .   ? 49.28000 18.59300 3.70100   1.000 120.13000 ? 308 BOG A "C2'" 1 
HETATM 1744 C  "C3'" . BOG I 4 .   ? 49.02400 17.53800 4.75300   1.000 117.07000 ? 308 BOG A "C3'" 1 
HETATM 1745 C  "C4'" . BOG I 4 .   ? 48.75800 18.19300 6.14500   1.000 114.14000 ? 308 BOG A "C4'" 1 
HETATM 1746 C  "C5'" . BOG I 4 .   ? 47.21000 18.32500 6.41800   1.000 108.59000 ? 308 BOG A "C5'" 1 
HETATM 1747 C  "C6'" . BOG I 4 .   ? 46.55800 16.95600 6.51100   1.000 109.43000 ? 308 BOG A "C6'" 1 
HETATM 1748 C  "C7'" . BOG I 4 .   ? 46.27300 16.59800 7.97100   1.000 114.01000 ? 308 BOG A "C7'" 1 
HETATM 1749 C  "C8'" . BOG I 4 .   ? 47.62000 16.24100 8.69900   1.000 115.45000 ? 308 BOG A "C8'" 1 
HETATM 1750 C  C2    . MPG J 5 .   ? 25.84400 31.38900 17.51000  1.000 103.06000 ? 309 MPG A C2    1 
HETATM 1751 C  C3    . MPG J 5 .   ? 26.63600 32.66000 17.82800  1.000 110.56000 ? 309 MPG A C3    1 
HETATM 1752 C  C4    . MPG J 5 .   ? 25.76800 33.67300 18.58200  1.000 112.17000 ? 309 MPG A C4    1 
HETATM 1753 C  C5    . MPG J 5 .   ? 26.61700 34.41700 19.61900  1.000 102.73000 ? 309 MPG A C5    1 
HETATM 1754 C  C6    . MPG J 5 .   ? 26.81100 35.88900 19.23200  1.000 90.67000  ? 309 MPG A C6    1 
HETATM 1755 C  C7    . MPG J 5 .   ? 28.22100 36.33400 19.63100  1.000 86.45000  ? 309 MPG A C7    1 
HETATM 1756 C  C8    . MPG J 5 .   ? 28.62000 37.71800 19.09200  1.000 89.72000  ? 309 MPG A C8    1 
HETATM 1757 C  C9    . MPG J 5 .   ? 30.09300 37.91200 19.47300  1.000 94.36000  ? 309 MPG A C9    1 
HETATM 1758 C  C10   . MPG J 5 .   ? 30.80200 39.02200 19.31100  1.000 91.90000  ? 309 MPG A C10   1 
HETATM 1759 C  C11   . MPG J 5 .   ? 30.28700 40.33300 18.70900  1.000 93.34000  ? 309 MPG A C11   1 
HETATM 1760 C  C12   . MPG J 5 .   ? 31.18700 41.45900 19.23900  1.000 100.94000 ? 309 MPG A C12   1 
HETATM 1761 C  C13   . MPG J 5 .   ? 31.50900 42.54000 18.20000  1.000 111.51000 ? 309 MPG A C13   1 
HETATM 1762 C  C14   . MPG J 5 .   ? 31.56600 43.89700 18.91300  1.000 110.85000 ? 309 MPG A C14   1 
HETATM 1763 C  C15   . MPG J 5 .   ? 32.37700 44.94500 18.14300  1.000 104.89000 ? 309 MPG A C15   1 
HETATM 1764 C  C16   . MPG J 5 .   ? 32.35700 46.25900 18.93300  1.000 98.49000  ? 309 MPG A C16   1 
HETATM 1765 C  C17   . MPG J 5 .   ? 32.62700 47.45600 18.02000  1.000 92.30000  ? 309 MPG A C17   1 
HETATM 1766 C  C18   . MPG J 5 .   ? 32.29700 48.75500 18.75800  1.000 82.34000  ? 309 MPG A C18   1 
HETATM 1767 O  O1    . MPG J 5 .   ? 27.08300 29.86900 18.91900  1.000 98.52000  ? 309 MPG A O1    1 
HETATM 1768 C  C1    . MPG J 5 .   ? 26.75600 30.16000 17.58400  1.000 99.85000  ? 309 MPG A C1    1 
HETATM 1769 C  CXD   . MPG J 5 .   ? 26.97300 28.13100 20.79300  1.000 113.22000 ? 309 MPG A CXD   1 
HETATM 1770 O  O2    . MPG J 5 .   ? 27.77500 29.05800 21.45000  1.000 115.90000 ? 309 MPG A O2    1 
HETATM 1771 C  C21   . MPG J 5 .   ? 27.75700 26.84000 20.48900  1.000 109.81000 ? 309 MPG A C21   1 
HETATM 1772 O  O3    . MPG J 5 .   ? 27.68400 25.95100 21.56000  1.000 102.12000 ? 309 MPG A O3    1 
HETATM 1773 O  O4    . MPG J 5 .   ? 25.53700 28.22700 18.92200  1.000 111.21000 ? 309 MPG A O4    1 
HETATM 1774 C  CX3   . MPG J 5 .   ? 26.46000 28.73100 19.47200  1.000 106.95000 ? 309 MPG A CX3   1 
HETATM 1775 C  C2    . MPG K 5 .   ? 45.65400 40.89200 5.84000   1.000 96.01000  ? 310 MPG A C2    1 
HETATM 1776 C  C3    . MPG K 5 .   ? 46.17000 41.98400 6.77800   1.000 100.18000 ? 310 MPG A C3    1 
HETATM 1777 C  C4    . MPG K 5 .   ? 45.46200 43.31000 6.48400   1.000 95.96000  ? 310 MPG A C4    1 
HETATM 1778 C  C5    . MPG K 5 .   ? 44.26600 43.49200 7.42200   1.000 99.67000  ? 310 MPG A C5    1 
HETATM 1779 C  C6    . MPG K 5 .   ? 43.61400 44.86400 7.21300   1.000 108.57000 ? 310 MPG A C6    1 
HETATM 1780 C  C7    . MPG K 5 .   ? 42.88900 45.29100 8.49400   1.000 106.17000 ? 310 MPG A C7    1 
HETATM 1781 C  C8    . MPG K 5 .   ? 41.98600 46.51000 8.26000   1.000 98.99000  ? 310 MPG A C8    1 
HETATM 1782 C  C9    . MPG K 5 .   ? 42.18200 47.51600 9.40000   1.000 94.13000  ? 310 MPG A C9    1 
HETATM 1783 C  C10   . MPG K 5 .   ? 41.26000 47.75500 10.32400  1.000 89.97000  ? 310 MPG A C10   1 
HETATM 1784 C  C11   . MPG K 5 .   ? 39.89900 47.05500 10.32900  1.000 92.14000  ? 310 MPG A C11   1 
HETATM 1785 C  C12   . MPG K 5 .   ? 39.15500 47.24100 11.65700  1.000 94.16000  ? 310 MPG A C12   1 
HETATM 1786 C  C13   . MPG K 5 .   ? 39.11100 48.70100 12.11700  1.000 96.92000  ? 310 MPG A C13   1 
HETATM 1787 C  C14   . MPG K 5 .   ? 38.15300 48.83300 13.30600  1.000 101.65000 ? 310 MPG A C14   1 
HETATM 1788 C  C15   . MPG K 5 .   ? 37.80800 50.30200 13.55600  1.000 107.52000 ? 310 MPG A C15   1 
HETATM 1789 C  C16   . MPG K 5 .   ? 36.85900 50.41600 14.75100  1.000 102.43000 ? 310 MPG A C16   1 
HETATM 1790 C  C17   . MPG K 5 .   ? 35.53500 51.04500 14.31500  1.000 117.14000 ? 310 MPG A C17   1 
HETATM 1791 C  C18   . MPG K 5 .   ? 34.42200 50.59700 15.26100  1.000 126.00000 ? 310 MPG A C18   1 
HETATM 1792 O  O1    . MPG K 5 .   ? 46.34700 39.19300 4.30100   1.000 114.73000 ? 310 MPG A O1    1 
HETATM 1793 C  C1    . MPG K 5 .   ? 46.80000 40.32100 5.00000   1.000 103.39000 ? 310 MPG A C1    1 
HETATM 1794 C  CXD   . MPG K 5 .   ? 48.37900 38.47900 2.95200   1.000 105.37000 ? 310 MPG A CXD   1 
HETATM 1795 O  O2    . MPG K 5 .   ? 48.05100 39.63100 2.25400   1.000 107.83000 ? 310 MPG A O2    1 
HETATM 1796 C  C21   . MPG K 5 .   ? 48.50300 37.28700 1.99700   1.000 95.54000  ? 310 MPG A C21   1 
HETATM 1797 O  O3    . MPG K 5 .   ? 49.15200 37.66300 0.82400   1.000 90.32000  ? 310 MPG A O3    1 
HETATM 1798 O  O4    . MPG K 5 .   ? 47.28300 37.17600 4.59100   1.000 111.56000 ? 310 MPG A O4    1 
HETATM 1799 C  CX3   . MPG K 5 .   ? 47.31200 38.21500 4.01800   1.000 112.38000 ? 310 MPG A CX3   1 
HETATM 1800 C  C2    . MPG L 5 .   ? 35.37600 41.30300 -11.90500 1.000 83.62000  ? 311 MPG A C2    1 
HETATM 1801 C  C3    . MPG L 5 .   ? 36.53100 42.19900 -12.35200 1.000 83.64000  ? 311 MPG A C3    1 
HETATM 1802 C  C4    . MPG L 5 .   ? 36.03800 43.24500 -13.35400 1.000 79.64000  ? 311 MPG A C4    1 
HETATM 1803 C  C5    . MPG L 5 .   ? 35.12300 44.25100 -12.65800 1.000 85.67000  ? 311 MPG A C5    1 
HETATM 1804 C  C6    . MPG L 5 .   ? 34.79000 45.39900 -13.61100 1.000 90.97000  ? 311 MPG A C6    1 
HETATM 1805 C  C7    . MPG L 5 .   ? 33.87000 46.39500 -12.90300 1.000 82.46000  ? 311 MPG A C7    1 
HETATM 1806 C  C8    . MPG L 5 .   ? 34.67200 47.59700 -12.38600 1.000 78.69000  ? 311 MPG A C8    1 
HETATM 1807 C  C9    . MPG L 5 .   ? 34.73100 48.63200 -13.50900 1.000 85.06000  ? 311 MPG A C9    1 
HETATM 1808 C  C10   . MPG L 5 .   ? 33.89200 49.65600 -13.57000 1.000 83.00000  ? 311 MPG A C10   1 
HETATM 1809 C  C11   . MPG L 5 .   ? 32.81900 49.87400 -12.55600 1.000 72.56000  ? 311 MPG A C11   1 
HETATM 1810 O  O1    . MPG L 5 .   ? 36.11100 39.02400 -11.71400 1.000 91.63000  ? 311 MPG A O1    1 
HETATM 1811 C  C1    . MPG L 5 .   ? 35.89300 40.19800 -10.98000 1.000 82.77000  ? 311 MPG A C1    1 
HETATM 1812 C  CXD   . MPG L 5 .   ? 34.98800 36.99200 -12.75700 1.000 110.45000 ? 311 MPG A CXD   1 
HETATM 1813 O  O2    . MPG L 5 .   ? 33.80600 37.14200 -13.47400 1.000 100.98000 ? 311 MPG A O2    1 
HETATM 1814 C  C21   . MPG L 5 .   ? 35.01800 35.58900 -12.12400 1.000 117.44000 ? 311 MPG A C21   1 
HETATM 1815 O  O3    . MPG L 5 .   ? 35.11000 34.62000 -13.11800 1.000 117.41000 ? 311 MPG A O3    1 
HETATM 1816 O  O4    . MPG L 5 .   ? 34.30800 38.06300 -10.75700 1.000 105.76000 ? 311 MPG A O4    1 
HETATM 1817 C  CX3   . MPG L 5 .   ? 35.08400 38.06100 -11.65500 1.000 105.38000 ? 311 MPG A CX3   1 
HETATM 1818 C  C2    . MPG M 5 .   ? 49.40300 38.75600 -13.28300 1.000 103.37000 ? 312 MPG A C2    1 
HETATM 1819 C  C3    . MPG M 5 .   ? 49.73400 39.79900 -12.21600 1.000 109.53000 ? 312 MPG A C3    1 
HETATM 1820 C  C4    . MPG M 5 .   ? 49.02600 41.11100 -12.54900 1.000 112.59000 ? 312 MPG A C4    1 
HETATM 1821 C  C5    . MPG M 5 .   ? 48.35500 41.67700 -11.29800 1.000 111.14000 ? 312 MPG A C5    1 
HETATM 1822 C  C6    . MPG M 5 .   ? 47.80900 43.07200 -11.60500 1.000 110.91000 ? 312 MPG A C6    1 
HETATM 1823 C  C7    . MPG M 5 .   ? 48.48900 44.10300 -10.70300 1.000 110.10000 ? 312 MPG A C7    1 
HETATM 1824 C  C8    . MPG M 5 .   ? 49.36800 45.05500 -11.51900 1.000 110.04000 ? 312 MPG A C8    1 
HETATM 1825 C  C9    . MPG M 5 .   ? 50.32500 45.77500 -10.56700 1.000 104.99000 ? 312 MPG A C9    1 
HETATM 1826 C  C10   . MPG M 5 .   ? 50.96100 46.88300 -10.90700 1.000 96.99000  ? 312 MPG A C10   1 
HETATM 1827 C  C11   . MPG M 5 .   ? 50.78300 47.53500 -12.28000 1.000 99.81000  ? 312 MPG A C11   1 
HETATM 1828 C  C12   . MPG M 5 .   ? 49.48100 48.33600 -12.31300 1.000 103.52000 ? 312 MPG A C12   1 
HETATM 1829 C  C13   . MPG M 5 .   ? 49.71300 49.71500 -12.93200 1.000 111.38000 ? 312 MPG A C13   1 
HETATM 1830 C  C14   . MPG M 5 .   ? 48.38300 50.46700 -13.00600 1.000 108.90000 ? 312 MPG A C14   1 
HETATM 1831 C  C15   . MPG M 5 .   ? 48.62800 51.96200 -13.21200 1.000 102.30000 ? 312 MPG A C15   1 
HETATM 1832 C  C16   . MPG M 5 .   ? 48.99600 52.62600 -11.88500 1.000 96.80000  ? 312 MPG A C16   1 
HETATM 1833 C  C17   . MPG M 5 .   ? 49.41700 54.07000 -12.15100 1.000 98.06000  ? 312 MPG A C17   1 
HETATM 1834 C  C18   . MPG M 5 .   ? 49.70200 54.78300 -10.83100 1.000 94.88000  ? 312 MPG A C18   1 
HETATM 1835 O  O1    . MPG M 5 .   ? 49.96800 36.54800 -14.01400 1.000 109.10000 ? 312 MPG A O1    1 
HETATM 1836 C  C1    . MPG M 5 .   ? 50.41000 37.61000 -13.21500 1.000 98.07000  ? 312 MPG A C1    1 
HETATM 1837 C  CXD   . MPG M 5 .   ? 49.94600 34.12600 -13.23600 1.000 137.03000 ? 312 MPG A CXD   1 
HETATM 1838 O  O2    . MPG M 5 .   ? 49.79600 33.45700 -14.44400 1.000 146.23000 ? 312 MPG A O2    1 
HETATM 1839 C  C21   . MPG M 5 .   ? 49.24500 33.36200 -12.10600 1.000 132.51000 ? 312 MPG A C21   1 
HETATM 1840 O  O3    . MPG M 5 .   ? 49.06800 34.17000 -10.99000 1.000 113.00000 ? 312 MPG A O3    1 
HETATM 1841 O  O4    . MPG M 5 .   ? 48.27600 35.75300 -12.77700 1.000 104.64000 ? 312 MPG A O4    1 
HETATM 1842 C  CX3   . MPG M 5 .   ? 49.31400 35.52500 -13.31500 1.000 115.93000 ? 312 MPG A CX3   1 
HETATM 1843 C  C1    . BOG N 4 .   ? 49.27200 45.23900 8.87400   1.000 140.74000 ? 313 BOG A C1    1 
HETATM 1844 O  O1    . BOG N 4 .   ? 50.15900 46.19600 8.47700   1.000 135.83000 ? 313 BOG A O1    1 
HETATM 1845 C  C2    . BOG N 4 .   ? 50.03900 43.91000 8.93000   1.000 145.87000 ? 313 BOG A C2    1 
HETATM 1846 O  O2    . BOG N 4 .   ? 50.41800 43.49700 7.61600   1.000 149.75000 ? 313 BOG A O2    1 
HETATM 1847 C  C3    . BOG N 4 .   ? 49.23000 42.84400 9.59300   1.000 147.79000 ? 313 BOG A C3    1 
HETATM 1848 O  O3    . BOG N 4 .   ? 49.98200 41.61800 9.68400   1.000 148.21000 ? 313 BOG A O3    1 
HETATM 1849 C  C4    . BOG N 4 .   ? 48.76100 43.27300 10.97500  1.000 148.29000 ? 313 BOG A C4    1 
HETATM 1850 O  O4    . BOG N 4 .   ? 48.05500 42.23200 11.58000  1.000 148.08000 ? 313 BOG A O4    1 
HETATM 1851 C  C5    . BOG N 4 .   ? 47.91100 44.56100 10.87400  1.000 144.44000 ? 313 BOG A C5    1 
HETATM 1852 O  O5    . BOG N 4 .   ? 48.64700 45.64700 10.20500  1.000 139.65000 ? 313 BOG A O5    1 
HETATM 1853 C  C6    . BOG N 4 .   ? 47.52000 45.05000 12.25300  1.000 145.32000 ? 313 BOG A C6    1 
HETATM 1854 O  O6    . BOG N 4 .   ? 46.38000 45.86000 12.18800  1.000 144.54000 ? 313 BOG A O6    1 
HETATM 1855 C  "C1'" . BOG N 4 .   ? 49.60100 47.48900 8.12800   1.000 138.95000 ? 313 BOG A "C1'" 1 
HETATM 1856 C  "C2'" . BOG N 4 .   ? 50.45600 48.14900 7.04000   1.000 143.28000 ? 313 BOG A "C2'" 1 
HETATM 1857 C  "C3'" . BOG N 4 .   ? 50.08000 49.60800 6.91200   1.000 137.57000 ? 313 BOG A "C3'" 1 
HETATM 1858 C  "C4'" . BOG N 4 .   ? 50.05500 50.04000 5.41100   1.000 137.74000 ? 313 BOG A "C4'" 1 
HETATM 1859 C  "C5'" . BOG N 4 .   ? 51.51100 50.23900 4.83500   1.000 139.53000 ? 313 BOG A "C5'" 1 
HETATM 1860 C  "C6'" . BOG N 4 .   ? 52.35200 51.08200 5.77500   1.000 137.78000 ? 313 BOG A "C6'" 1 
HETATM 1861 C  "C7'" . BOG N 4 .   ? 53.36100 51.92900 5.00100   1.000 130.14000 ? 313 BOG A "C7'" 1 
HETATM 1862 C  "C8'" . BOG N 4 .   ? 54.27800 52.68200 6.03200   1.000 129.64000 ? 313 BOG A "C8'" 1 
HETATM 1863 C  C2    . MPG O 5 .   ? 15.07400 26.91600 7.83400   1.000 104.87000 ? 314 MPG A C2    1 
HETATM 1864 C  C3    . MPG O 5 .   ? 14.20700 26.63400 6.60300   1.000 106.49000 ? 314 MPG A C3    1 
HETATM 1865 C  C4    . MPG O 5 .   ? 14.24600 25.14000 6.27500   1.000 113.42000 ? 314 MPG A C4    1 
HETATM 1866 C  C5    . MPG O 5 .   ? 13.44100 24.39100 7.33700   1.000 117.10000 ? 314 MPG A C5    1 
HETATM 1867 C  C6    . MPG O 5 .   ? 13.65400 22.88100 7.23300   1.000 110.12000 ? 314 MPG A C6    1 
HETATM 1868 C  C7    . MPG O 5 .   ? 13.00300 22.20700 8.44300   1.000 106.19000 ? 314 MPG A C7    1 
HETATM 1869 C  C8    . MPG O 5 .   ? 13.46200 20.75200 8.54600   1.000 108.35000 ? 314 MPG A C8    1 
HETATM 1870 C  C9    . MPG O 5 .   ? 12.71800 19.92800 7.49700   1.000 112.06000 ? 314 MPG A C9    1 
HETATM 1871 C  C10   . MPG O 5 .   ? 13.21900 18.83300 6.94900   1.000 113.41000 ? 314 MPG A C10   1 
HETATM 1872 C  C11   . MPG O 5 .   ? 14.58700 18.26200 7.31700   1.000 107.01000 ? 314 MPG A C11   1 
HETATM 1873 C  C12   . MPG O 5 .   ? 14.41200 16.89600 7.99800   1.000 107.69000 ? 314 MPG A C12   1 
HETATM 1874 C  C13   . MPG O 5 .   ? 13.48000 15.99200 7.27200   1.000 113.98000 ? 314 MPG A C13   1 
HETATM 1875 O  O1    . MPG O 5 .   ? 13.57600 26.48000 9.68300   1.000 116.81000 ? 314 MPG A O1    1 
HETATM 1876 C  C1    . MPG O 5 .   ? 14.24900 27.49900 8.98700   1.000 113.58000 ? 314 MPG A C1    1 
HETATM 1877 C  CXD   . MPG O 5 .   ? 13.36300 25.03300 11.77600  1.000 105.91000 ? 314 MPG A CXD   1 
HETATM 1878 O  O2    . MPG O 5 .   ? 12.80800 25.58300 12.92800  1.000 104.55000 ? 314 MPG A O2    1 
HETATM 1879 C  C21   . MPG O 5 .   ? 14.35900 23.93300 12.17400  1.000 98.19000  ? 314 MPG A C21   1 
HETATM 1880 O  O3    . MPG O 5 .   ? 13.88500 23.21200 13.26700  1.000 88.01000  ? 314 MPG A O3    1 
HETATM 1881 O  O4    . MPG O 5 .   ? 14.99800 26.69800 11.42500  1.000 99.49000  ? 314 MPG A O4    1 
HETATM 1882 C  CX3   . MPG O 5 .   ? 14.05800 26.14100 10.96600  1.000 108.83000 ? 314 MPG A CX3   1 
HETATM 1883 C  C1    . BOG P 4 .   ? 48.90000 23.75300 -9.07600  1.000 122.49000 ? 315 BOG A C1    1 
HETATM 1884 O  O1    . BOG P 4 .   ? 49.18900 22.86800 -8.08200  1.000 122.71000 ? 315 BOG A O1    1 
HETATM 1885 C  C2    . BOG P 4 .   ? 47.47200 23.54100 -9.57200  1.000 115.19000 ? 315 BOG A C2    1 
HETATM 1886 O  O2    . BOG P 4 .   ? 47.36900 22.23000 -10.11500 1.000 112.88000 ? 315 BOG A O2    1 
HETATM 1887 C  C3    . BOG P 4 .   ? 47.15400 24.57100 -10.59600 1.000 108.16000 ? 315 BOG A C3    1 
HETATM 1888 O  O3    . BOG P 4 .   ? 45.79800 24.42300 -11.07800 1.000 104.38000 ? 315 BOG A O3    1 
HETATM 1889 C  C4    . BOG P 4 .   ? 47.33000 25.98600 -10.07500 1.000 126.33000 ? 315 BOG A C4    1 
HETATM 1890 O  O4    . BOG P 4 .   ? 47.11700 26.88200 -11.13100 1.000 132.60000 ? 315 BOG A O4    1 
HETATM 1891 C  C5    . BOG P 4 .   ? 48.70200 26.25500 -9.43000  1.000 132.48000 ? 315 BOG A C5    1 
HETATM 1892 O  O5    . BOG P 4 .   ? 49.15700 25.16500 -8.55800  1.000 126.89000 ? 315 BOG A O5    1 
HETATM 1893 C  C6    . BOG P 4 .   ? 48.60900 27.50900 -8.56600  1.000 137.61000 ? 315 BOG A C6    1 
HETATM 1894 O  O6    . BOG P 4 .   ? 49.45400 28.53500 -9.01200  1.000 138.60000 ? 315 BOG A O6    1 
HETATM 1895 C  "C1'" . BOG P 4 .   ? 50.43500 23.15300 -7.39200  1.000 118.71000 ? 315 BOG A "C1'" 1 
HETATM 1896 C  "C2'" . BOG P 4 .   ? 50.68900 22.14900 -6.26100  1.000 112.47000 ? 315 BOG A "C2'" 1 
HETATM 1897 C  "C3'" . BOG P 4 .   ? 51.98500 22.49800 -5.55700  1.000 109.02000 ? 315 BOG A "C3'" 1 
HETATM 1898 C  "C4'" . BOG P 4 .   ? 51.73600 22.99800 -4.14500  1.000 107.47000 ? 315 BOG A "C4'" 1 
HETATM 1899 C  C1    . BOG Q 4 .   ? 30.88200 25.60800 17.13400  1.000 135.63000 ? 316 BOG A C1    1 
HETATM 1900 O  O1    . BOG Q 4 .   ? 30.40500 24.61200 17.92900  1.000 124.11000 ? 316 BOG A O1    1 
HETATM 1901 C  C2    . BOG Q 4 .   ? 30.33000 26.94100 17.63000  1.000 134.95000 ? 316 BOG A C2    1 
HETATM 1902 O  O2    . BOG Q 4 .   ? 28.90300 26.91300 17.62900  1.000 136.20000 ? 316 BOG A O2    1 
HETATM 1903 C  C3    . BOG Q 4 .   ? 30.78400 28.09400 16.79500  1.000 145.85000 ? 316 BOG A C3    1 
HETATM 1904 O  O3    . BOG Q 4 .   ? 30.84400 29.28800 17.61700  1.000 133.17000 ? 316 BOG A O3    1 
HETATM 1905 C  C4    . BOG Q 4 .   ? 32.13200 27.86700 16.13300  1.000 171.73000 ? 316 BOG A C4    1 
HETATM 1906 O  O4    . BOG Q 4 .   ? 31.92900 27.34900 14.84300  1.000 188.90000 ? 316 BOG A O4    1 
HETATM 1907 C  C5    . BOG Q 4 .   ? 33.03600 26.89800 16.92800  1.000 160.16000 ? 316 BOG A C5    1 
HETATM 1908 O  O5    . BOG Q 4 .   ? 32.40900 25.59000 17.17600  1.000 159.15000 ? 316 BOG A O5    1 
HETATM 1909 C  C6    . BOG Q 4 .   ? 33.42600 27.52600 18.26500  1.000 131.26000 ? 316 BOG A C6    1 
HETATM 1910 O  O6    . BOG Q 4 .   ? 33.51000 28.92700 18.18700  1.000 129.33000 ? 316 BOG A O6    1 
HETATM 1911 C  "C1'" . BOG Q 4 .   ? 29.42200 23.72900 17.32100  1.000 117.69000 ? 316 BOG A "C1'" 1 
HETATM 1912 C  "C2'" . BOG Q 4 .   ? 30.12300 22.54800 16.64000  1.000 113.09000 ? 316 BOG A "C2'" 1 
HETATM 1913 C  "C3'" . BOG Q 4 .   ? 29.32900 21.26500 16.78600  1.000 125.18000 ? 316 BOG A "C3'" 1 
HETATM 1914 C  "C4'" . BOG Q 4 .   ? 30.26700 20.16000 17.37200  1.000 134.24000 ? 316 BOG A "C4'" 1 
HETATM 1915 C  "C5'" . BOG Q 4 .   ? 29.75400 18.69700 17.07400  1.000 128.37000 ? 316 BOG A "C5'" 1 
HETATM 1916 C  "C6'" . BOG Q 4 .   ? 28.25000 18.58500 17.23700  1.000 111.51000 ? 316 BOG A "C6'" 1 
HETATM 1917 C  "C7'" . BOG Q 4 .   ? 27.86000 17.21200 17.79900  1.000 106.21000 ? 316 BOG A "C7'" 1 
HETATM 1918 C  "C8'" . BOG Q 4 .   ? 28.59500 16.04900 17.03500  1.000 106.27000 ? 316 BOG A "C8'" 1 
HETATM 1919 O  O     . HOH R 6 .   ? 22.863   51.464   20.412    1.000 73.83000  ? 401 HOH A O     1 
HETATM 1920 O  O     . HOH R 6 .   ? 49.67400 21.50300 3.71700   1.000 94.68000  ? 402 HOH A O     1 
HETATM 1921 O  O     . HOH R 6 .   ? 34.10200 54.82500 -11.76300 1.000 81.97000  ? 403 HOH A O     1 
HETATM 1922 O  O     . HOH R 6 .   ? 44.87500 26.01700 -12.75000 0.500 74.32000  ? 404 HOH A O     1 
HETATM 1923 O  O     . HOH R 6 .   ? 40.15700 19.45900 -13.40500 1.000 79.53000  ? 405 HOH A O     1 
HETATM 1924 O  O     A HOH R 6 .   ? 36.99200 31.01200 1.13000   1.000 37.31000  ? 406 HOH A O     1 
HETATM 1925 O  O     . HOH R 6 .   ? 29.95900 24.55900 -1.06700  1.000 35.99000  ? 407 HOH A O     1 
HETATM 1926 O  O     A HOH R 6 .   ? 35.95200 34.23200 -0.16400  1.000 36.59000  ? 408 HOH A O     1 
HETATM 1927 O  O     . HOH R 6 .   ? 20.84400 19.85200 -6.93900  1.000 146.82000 ? 409 HOH A O     1 
HETATM 1928 O  O     . HOH R 6 .   ? 41.41300 17.93700 5.00500   1.000 56.34000  ? 410 HOH A O     1 
HETATM 1929 O  O     . HOH R 6 .   ? 23.87200 16.74500 15.74500  1.000 78.26000  ? 411 HOH A O     1 
HETATM 1930 O  O     . HOH R 6 .   ? 31.68900 18.59100 13.10300  1.000 65.89000  ? 412 HOH A O     1 
HETATM 1931 O  O     . HOH R 6 .   ? 48.19900 17.96600 -1.24900  1.000 77.00000  ? 413 HOH A O     1 
HETATM 1932 O  O     . HOH R 6 .   ? 30.22200 42.51800 -1.17800  1.000 24.82000  ? 414 HOH A O     1 
HETATM 1933 O  O     A HOH R 6 .   ? 34.53000 30.05600 0.39700   1.000 32.98000  ? 415 HOH A O     1 
HETATM 1934 O  O     . HOH R 6 .   ? 31.97500 38.23800 11.34100  1.000 34.78000  ? 416 HOH A O     1 
HETATM 1935 O  O     . HOH R 6 .   ? 29.12100 21.11500 4.10700   1.000 68.93000  ? 417 HOH A O     1 
HETATM 1936 O  O     . HOH R 6 .   ? 30.34800 16.61500 -7.05300  1.000 51.98000  ? 418 HOH A O     1 
HETATM 1937 O  O     . HOH R 6 .   ? 39.65100 17.24900 -6.53800  1.000 57.56000  ? 419 HOH A O     1 
HETATM 1938 O  O     . HOH R 6 .   ? 18.49000 51.82700 14.79800  1.000 80.95000  ? 420 HOH A O     1 
HETATM 1939 O  O     . HOH R 6 .   ? 34.00600 27.96400 -2.63400  1.000 38.63000  ? 421 HOH A O     1 
HETATM 1940 O  O     . HOH R 6 .   ? 30.12800 22.12000 1.41500   1.000 64.17000  ? 422 HOH A O     1 
HETATM 1941 O  O     . HOH R 6 .   ? 17.26500 17.40600 5.35300   1.000 69.56000  ? 423 HOH A O     1 
HETATM 1942 O  O     . HOH R 6 .   ? 52.26200 15.89800 -2.83400  1.000 90.95000  ? 424 HOH A O     1 
HETATM 1943 O  O     . HOH R 6 .   ? 25.149   65.954   -8.501    1.000 90.92000  ? 425 HOH A O     1 
HETATM 1944 O  O     . HOH R 6 .   ? 49.02400 34.31600 -0.12400  1.000 67.45000  ? 426 HOH A O     1 
HETATM 1945 O  O     . HOH R 6 .   ? 34.71000 15.57400 -1.01200  1.000 66.52000  ? 427 HOH A O     1 
HETATM 1946 O  O     . HOH R 6 .   ? 53.89600 16.50100 -0.42100  1.000 93.05000  ? 428 HOH A O     1 
HETATM 1947 O  O     . HOH R 6 .   ? 24.66300 55.77400 13.47900  1.000 63.43000  ? 429 HOH A O     1 
HETATM 1948 O  O     . HOH R 6 .   ? 34.17400 30.47300 -11.61800 1.000 30.00000  ? 430 HOH A O     1 
HETATM 1949 O  O     . HOH R 6 .   ? 37.24900 55.22800 -2.42100  1.000 65.80000  ? 431 HOH A O     1 
HETATM 1950 O  O     . HOH R 6 .   ? 17.18600 34.36500 3.65200   1.000 60.74000  ? 432 HOH A O     1 
HETATM 1951 O  O     . HOH R 6 .   ? 51.32000 26.84200 -2.67900  1.000 62.53000  ? 433 HOH A O     1 
# 
