data_8ZP6
# 
_entry.id   8ZP6 
# 
_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   8ZP6         pdb_00008zp6 10.2210/pdb8zp6/pdb 
WWPDB D_1300048272 ?            ?                   
# 
_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       2025-06-04 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8ZP6 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              yonghw@scut.edu.cn 
_pdbx_contact_author.name_first         Yonghua 
_pdbx_contact_author.name_last          Wang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8790-4357 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhou, Y.'   1 ? 
'Lan, D.M.'  2 ? 
'Wang, Y.H.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of Epoxide hydrolase MdEH (Mycobacterium dioxanotrophicus)' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zhou, Y.'   1 ? 
primary 'Lan, D.M.'  2 ? 
primary 'Wang, Y.H.' 3 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer man 'AB hydrolase-1 domain-containing protein' 33833.113 1   ? ? ? ? 
2 water   nat water                                      18.015    370 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Epoxide hydrolase' 
# 
_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       
;MTIRRPEHFTHHEVQLSDVKIHYVREGAGPTLLLLHGWPGFWWEWSKVIGPLSERFDVIVPDLRGFGDSEKPDLSDLAQY
SLERVADDQAELLNALGIDQAYVVGHDYSAIVVHKFIRKYPDRVVKAAIFDPITPDFGPFYLGFPHIAESWYSQFHQTDM
SVELVTSSREACRIYFKHFFDHWSYHAPLLTQDELDIYVDNCMKPNNVHGGFNYYRSNLSVTSDPWTDLDRTVSDLPVTM
LWGVGDPVVPSSLVHQVPNYYSNYTMELIQDAGHFMMVEKPEVVIDRLKAGFR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTIRRPEHFTHHEVQLSDVKIHYVREGAGPTLLLLHGWPGFWWEWSKVIGPLSERFDVIVPDLRGFGDSEKPDLSDLAQY
SLERVADDQAELLNALGIDQAYVVGHDYSAIVVHKFIRKYPDRVVKAAIFDPITPDFGPFYLGFPHIAESWYSQFHQTDM
SVELVTSSREACRIYFKHFFDHWSYHAPLLTQDELDIYVDNCMKPNNVHGGFNYYRSNLSVTSDPWTDLDRTVSDLPVTM
LWGVGDPVVPSSLVHQVPNYYSNYTMELIQDAGHFMMVEKPEVVIDRLKAGFR
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   THR n 
1 3   ILE n 
1 4   ARG n 
1 5   ARG n 
1 6   PRO n 
1 7   GLU n 
1 8   HIS n 
1 9   PHE n 
1 10  THR n 
1 11  HIS n 
1 12  HIS n 
1 13  GLU n 
1 14  VAL n 
1 15  GLN n 
1 16  LEU n 
1 17  SER n 
1 18  ASP n 
1 19  VAL n 
1 20  LYS n 
1 21  ILE n 
1 22  HIS n 
1 23  TYR n 
1 24  VAL n 
1 25  ARG n 
1 26  GLU n 
1 27  GLY n 
1 28  ALA n 
1 29  GLY n 
1 30  PRO n 
1 31  THR n 
1 32  LEU n 
1 33  LEU n 
1 34  LEU n 
1 35  LEU n 
1 36  HIS n 
1 37  GLY n 
1 38  TRP n 
1 39  PRO n 
1 40  GLY n 
1 41  PHE n 
1 42  TRP n 
1 43  TRP n 
1 44  GLU n 
1 45  TRP n 
1 46  SER n 
1 47  LYS n 
1 48  VAL n 
1 49  ILE n 
1 50  GLY n 
1 51  PRO n 
1 52  LEU n 
1 53  SER n 
1 54  GLU n 
1 55  ARG n 
1 56  PHE n 
1 57  ASP n 
1 58  VAL n 
1 59  ILE n 
1 60  VAL n 
1 61  PRO n 
1 62  ASP n 
1 63  LEU n 
1 64  ARG n 
1 65  GLY n 
1 66  PHE n 
1 67  GLY n 
1 68  ASP n 
1 69  SER n 
1 70  GLU n 
1 71  LYS n 
1 72  PRO n 
1 73  ASP n 
1 74  LEU n 
1 75  SER n 
1 76  ASP n 
1 77  LEU n 
1 78  ALA n 
1 79  GLN n 
1 80  TYR n 
1 81  SER n 
1 82  LEU n 
1 83  GLU n 
1 84  ARG n 
1 85  VAL n 
1 86  ALA n 
1 87  ASP n 
1 88  ASP n 
1 89  GLN n 
1 90  ALA n 
1 91  GLU n 
1 92  LEU n 
1 93  LEU n 
1 94  ASN n 
1 95  ALA n 
1 96  LEU n 
1 97  GLY n 
1 98  ILE n 
1 99  ASP n 
1 100 GLN n 
1 101 ALA n 
1 102 TYR n 
1 103 VAL n 
1 104 VAL n 
1 105 GLY n 
1 106 HIS n 
1 107 ASP n 
1 108 TYR n 
1 109 SER n 
1 110 ALA n 
1 111 ILE n 
1 112 VAL n 
1 113 VAL n 
1 114 HIS n 
1 115 LYS n 
1 116 PHE n 
1 117 ILE n 
1 118 ARG n 
1 119 LYS n 
1 120 TYR n 
1 121 PRO n 
1 122 ASP n 
1 123 ARG n 
1 124 VAL n 
1 125 VAL n 
1 126 LYS n 
1 127 ALA n 
1 128 ALA n 
1 129 ILE n 
1 130 PHE n 
1 131 ASP n 
1 132 PRO n 
1 133 ILE n 
1 134 THR n 
1 135 PRO n 
1 136 ASP n 
1 137 PHE n 
1 138 GLY n 
1 139 PRO n 
1 140 PHE n 
1 141 TYR n 
1 142 LEU n 
1 143 GLY n 
1 144 PHE n 
1 145 PRO n 
1 146 HIS n 
1 147 ILE n 
1 148 ALA n 
1 149 GLU n 
1 150 SER n 
1 151 TRP n 
1 152 TYR n 
1 153 SER n 
1 154 GLN n 
1 155 PHE n 
1 156 HIS n 
1 157 GLN n 
1 158 THR n 
1 159 ASP n 
1 160 MET n 
1 161 SER n 
1 162 VAL n 
1 163 GLU n 
1 164 LEU n 
1 165 VAL n 
1 166 THR n 
1 167 SER n 
1 168 SER n 
1 169 ARG n 
1 170 GLU n 
1 171 ALA n 
1 172 CYS n 
1 173 ARG n 
1 174 ILE n 
1 175 TYR n 
1 176 PHE n 
1 177 LYS n 
1 178 HIS n 
1 179 PHE n 
1 180 PHE n 
1 181 ASP n 
1 182 HIS n 
1 183 TRP n 
1 184 SER n 
1 185 TYR n 
1 186 HIS n 
1 187 ALA n 
1 188 PRO n 
1 189 LEU n 
1 190 LEU n 
1 191 THR n 
1 192 GLN n 
1 193 ASP n 
1 194 GLU n 
1 195 LEU n 
1 196 ASP n 
1 197 ILE n 
1 198 TYR n 
1 199 VAL n 
1 200 ASP n 
1 201 ASN n 
1 202 CYS n 
1 203 MET n 
1 204 LYS n 
1 205 PRO n 
1 206 ASN n 
1 207 ASN n 
1 208 VAL n 
1 209 HIS n 
1 210 GLY n 
1 211 GLY n 
1 212 PHE n 
1 213 ASN n 
1 214 TYR n 
1 215 TYR n 
1 216 ARG n 
1 217 SER n 
1 218 ASN n 
1 219 LEU n 
1 220 SER n 
1 221 VAL n 
1 222 THR n 
1 223 SER n 
1 224 ASP n 
1 225 PRO n 
1 226 TRP n 
1 227 THR n 
1 228 ASP n 
1 229 LEU n 
1 230 ASP n 
1 231 ARG n 
1 232 THR n 
1 233 VAL n 
1 234 SER n 
1 235 ASP n 
1 236 LEU n 
1 237 PRO n 
1 238 VAL n 
1 239 THR n 
1 240 MET n 
1 241 LEU n 
1 242 TRP n 
1 243 GLY n 
1 244 VAL n 
1 245 GLY n 
1 246 ASP n 
1 247 PRO n 
1 248 VAL n 
1 249 VAL n 
1 250 PRO n 
1 251 SER n 
1 252 SER n 
1 253 LEU n 
1 254 VAL n 
1 255 HIS n 
1 256 GLN n 
1 257 VAL n 
1 258 PRO n 
1 259 ASN n 
1 260 TYR n 
1 261 TYR n 
1 262 SER n 
1 263 ASN n 
1 264 TYR n 
1 265 THR n 
1 266 MET n 
1 267 GLU n 
1 268 LEU n 
1 269 ILE n 
1 270 GLN n 
1 271 ASP n 
1 272 ALA n 
1 273 GLY n 
1 274 HIS n 
1 275 PHE n 
1 276 MET n 
1 277 MET n 
1 278 VAL n 
1 279 GLU n 
1 280 LYS n 
1 281 PRO n 
1 282 GLU n 
1 283 VAL n 
1 284 VAL n 
1 285 ILE n 
1 286 ASP n 
1 287 ARG n 
1 288 LEU n 
1 289 LYS n 
1 290 ALA n 
1 291 GLY n 
1 292 PHE n 
1 293 ARG 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                   293 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 BTO20_37290 
_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      'Mycobacterium dioxanotrophicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     482462 
_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 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   THR 2   2   ?   ?   ?   A . n 
A 1 3   ILE 3   3   3   ILE ILE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   ARG 5   5   5   ARG ARG A . n 
A 1 6   PRO 6   6   6   PRO PRO A . n 
A 1 7   GLU 7   7   7   GLU GLU A . n 
A 1 8   HIS 8   8   8   HIS HIS A . n 
A 1 9   PHE 9   9   9   PHE PHE A . n 
A 1 10  THR 10  10  10  THR THR A . n 
A 1 11  HIS 11  11  11  HIS HIS A . n 
A 1 12  HIS 12  12  12  HIS HIS A . n 
A 1 13  GLU 13  13  13  GLU GLU A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  SER 17  17  17  SER SER A . n 
A 1 18  ASP 18  18  18  ASP ASP A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  LYS 20  20  20  LYS LYS A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  HIS 22  22  22  HIS HIS A . n 
A 1 23  TYR 23  23  23  TYR TYR A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  ARG 25  25  25  ARG ARG A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  THR 31  31  31  THR THR A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  LEU 35  35  35  LEU LEU A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  TRP 38  38  38  TRP TRP A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  GLY 40  40  40  GLY GLY A . n 
A 1 41  PHE 41  41  41  PHE PHE A . n 
A 1 42  TRP 42  42  42  TRP TRP A . n 
A 1 43  TRP 43  43  43  TRP TRP A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  TRP 45  45  45  TRP TRP A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  LYS 47  47  47  LYS LYS A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  ILE 49  49  49  ILE ILE A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  PRO 51  51  51  PRO PRO A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  ARG 55  55  55  ARG ARG A . n 
A 1 56  PHE 56  56  56  PHE PHE A . n 
A 1 57  ASP 57  57  57  ASP ASP A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  VAL 60  60  60  VAL VAL A . n 
A 1 61  PRO 61  61  61  PRO PRO A . n 
A 1 62  ASP 62  62  62  ASP ASP A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  ARG 64  64  64  ARG ARG A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  SER 69  69  69  SER SER A . n 
A 1 70  GLU 70  70  70  GLU GLU A . n 
A 1 71  LYS 71  71  71  LYS LYS A . n 
A 1 72  PRO 72  72  72  PRO PRO A . n 
A 1 73  ASP 73  73  73  ASP ASP A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  TYR 80  80  80  TYR TYR A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  ASP 88  88  88  ASP ASP A . n 
A 1 89  GLN 89  89  89  GLN GLN A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  ASN 94  94  94  ASN ASN A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  LEU 96  96  96  LEU LEU A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  ILE 98  98  98  ILE ILE A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 GLN 100 100 100 GLN GLN A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 TYR 102 102 102 TYR TYR A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 GLY 105 105 105 GLY GLY A . n 
A 1 106 HIS 106 106 106 HIS HIS A . n 
A 1 107 ASP 107 107 107 ASP ASP A . n 
A 1 108 TYR 108 108 108 TYR TYR A . n 
A 1 109 SER 109 109 109 SER SER A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 ILE 111 111 111 ILE ILE A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 HIS 114 114 114 HIS HIS A . n 
A 1 115 LYS 115 115 115 LYS LYS A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ILE 117 117 117 ILE ILE A . n 
A 1 118 ARG 118 118 118 ARG ARG A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 TYR 120 120 120 TYR TYR A . n 
A 1 121 PRO 121 121 121 PRO PRO A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 ARG 123 123 123 ARG ARG A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 LYS 126 126 126 LYS LYS A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 ILE 129 129 129 ILE ILE A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 ASP 131 131 131 ASP ASP A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 ILE 133 133 133 ILE ILE A . n 
A 1 134 THR 134 134 134 THR THR A . n 
A 1 135 PRO 135 135 135 PRO PRO A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 PHE 137 137 137 PHE PHE A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 PRO 139 139 139 PRO PRO A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 TYR 141 141 141 TYR TYR A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 PRO 145 145 145 PRO PRO A . n 
A 1 146 HIS 146 146 146 HIS HIS A . n 
A 1 147 ILE 147 147 147 ILE ILE A . n 
A 1 148 ALA 148 148 148 ALA ALA A . n 
A 1 149 GLU 149 149 149 GLU GLU A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 TRP 151 151 151 TRP TRP A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 SER 153 153 153 SER SER A . n 
A 1 154 GLN 154 154 154 GLN GLN A . n 
A 1 155 PHE 155 155 155 PHE PHE A . n 
A 1 156 HIS 156 156 156 HIS HIS A . n 
A 1 157 GLN 157 157 157 GLN GLN A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 ASP 159 159 159 ASP ASP A . n 
A 1 160 MET 160 160 160 MET MET A . n 
A 1 161 SER 161 161 161 SER SER A . n 
A 1 162 VAL 162 162 162 VAL VAL A . n 
A 1 163 GLU 163 163 163 GLU GLU A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 THR 166 166 166 THR THR A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 ARG 169 169 169 ARG ARG A . n 
A 1 170 GLU 170 170 170 GLU GLU A . n 
A 1 171 ALA 171 171 171 ALA ALA A . n 
A 1 172 CYS 172 172 172 CYS CYS A . n 
A 1 173 ARG 173 173 173 ARG ARG A . n 
A 1 174 ILE 174 174 174 ILE ILE A . n 
A 1 175 TYR 175 175 175 TYR TYR A . n 
A 1 176 PHE 176 176 176 PHE PHE A . n 
A 1 177 LYS 177 177 177 LYS LYS A . n 
A 1 178 HIS 178 178 178 HIS HIS A . n 
A 1 179 PHE 179 179 179 PHE PHE A . n 
A 1 180 PHE 180 180 180 PHE PHE A . n 
A 1 181 ASP 181 181 181 ASP ASP A . n 
A 1 182 HIS 182 182 182 HIS HIS A . n 
A 1 183 TRP 183 183 183 TRP TRP A . n 
A 1 184 SER 184 184 184 SER SER A . n 
A 1 185 TYR 185 185 185 TYR TYR A . n 
A 1 186 HIS 186 186 186 HIS HIS A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 PRO 188 188 188 PRO PRO A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 LEU 190 190 190 LEU LEU A . n 
A 1 191 THR 191 191 191 THR THR A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ASP 193 193 193 ASP ASP A . n 
A 1 194 GLU 194 194 194 GLU GLU A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 ASP 196 196 196 ASP ASP A . n 
A 1 197 ILE 197 197 197 ILE ILE A . n 
A 1 198 TYR 198 198 198 TYR TYR A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 ASN 201 201 201 ASN ASN A . n 
A 1 202 CYS 202 202 202 CYS CYS A . n 
A 1 203 MET 203 203 203 MET MET A . n 
A 1 204 LYS 204 204 204 LYS LYS A . n 
A 1 205 PRO 205 205 205 PRO PRO A . n 
A 1 206 ASN 206 206 206 ASN ASN A . n 
A 1 207 ASN 207 207 207 ASN ASN A . n 
A 1 208 VAL 208 208 208 VAL VAL A . n 
A 1 209 HIS 209 209 209 HIS HIS A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 GLY 211 211 211 GLY GLY A . n 
A 1 212 PHE 212 212 212 PHE PHE A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 TYR 214 214 214 TYR TYR A . n 
A 1 215 TYR 215 215 215 TYR TYR A . n 
A 1 216 ARG 216 216 216 ARG ARG A . n 
A 1 217 SER 217 217 217 SER SER A . n 
A 1 218 ASN 218 218 218 ASN ASN A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 VAL 221 221 221 VAL VAL A . n 
A 1 222 THR 222 222 222 THR THR A . n 
A 1 223 SER 223 223 223 SER SER A . n 
A 1 224 ASP 224 224 224 ASP ASP A . n 
A 1 225 PRO 225 225 225 PRO PRO A . n 
A 1 226 TRP 226 226 226 TRP TRP A . n 
A 1 227 THR 227 227 227 THR THR A . n 
A 1 228 ASP 228 228 228 ASP ASP A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 ASP 230 230 230 ASP ASP A . n 
A 1 231 ARG 231 231 231 ARG ARG A . n 
A 1 232 THR 232 232 232 THR THR A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 SER 234 234 234 SER SER A . n 
A 1 235 ASP 235 235 235 ASP ASP A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 VAL 238 238 238 VAL VAL A . n 
A 1 239 THR 239 239 239 THR THR A . n 
A 1 240 MET 240 240 240 MET MET A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 TRP 242 242 242 TRP TRP A . n 
A 1 243 GLY 243 243 243 GLY GLY A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 GLY 245 245 245 GLY GLY A . n 
A 1 246 ASP 246 246 246 ASP ASP A . n 
A 1 247 PRO 247 247 247 PRO PRO A . n 
A 1 248 VAL 248 248 248 VAL VAL A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 PRO 250 250 250 PRO PRO A . n 
A 1 251 SER 251 251 251 SER SER A . n 
A 1 252 SER 252 252 252 SER SER A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 VAL 254 254 254 VAL VAL A . n 
A 1 255 HIS 255 255 255 HIS HIS A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 PRO 258 258 258 PRO PRO A . n 
A 1 259 ASN 259 259 259 ASN ASN A . n 
A 1 260 TYR 260 260 260 TYR TYR A . n 
A 1 261 TYR 261 261 261 TYR TYR A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 ASN 263 263 263 ASN ASN A . n 
A 1 264 TYR 264 264 264 TYR TYR A . n 
A 1 265 THR 265 265 265 THR THR A . n 
A 1 266 MET 266 266 266 MET MET A . n 
A 1 267 GLU 267 267 267 GLU GLU A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 ILE 269 269 269 ILE ILE A . n 
A 1 270 GLN 270 270 270 GLN GLN A . n 
A 1 271 ASP 271 271 271 ASP ASP A . n 
A 1 272 ALA 272 272 272 ALA ALA A . n 
A 1 273 GLY 273 273 273 GLY GLY A . n 
A 1 274 HIS 274 274 274 HIS HIS A . n 
A 1 275 PHE 275 275 275 PHE PHE A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 MET 277 277 277 MET MET A . n 
A 1 278 VAL 278 278 278 VAL VAL A . n 
A 1 279 GLU 279 279 279 GLU GLU A . n 
A 1 280 LYS 280 280 280 LYS LYS A . n 
A 1 281 PRO 281 281 281 PRO PRO A . n 
A 1 282 GLU 282 282 282 GLU GLU A . n 
A 1 283 VAL 283 283 283 VAL VAL A . n 
A 1 284 VAL 284 284 284 VAL VAL A . n 
A 1 285 ILE 285 285 285 ILE ILE A . n 
A 1 286 ASP 286 286 286 ASP ASP A . n 
A 1 287 ARG 287 287 287 ARG ARG A . n 
A 1 288 LEU 288 288 288 LEU LEU A . n 
A 1 289 LYS 289 289 289 LYS LYS A . n 
A 1 290 ALA 290 290 290 ALA ALA A . n 
A 1 291 GLY 291 291 291 GLY GLY A . n 
A 1 292 PHE 292 292 292 PHE PHE A . n 
A 1 293 ARG 293 293 293 ARG ARG A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 HOH 1   301 245 HOH HOH A . 
B 2 HOH 2   302 365 HOH HOH A . 
B 2 HOH 3   303 142 HOH HOH A . 
B 2 HOH 4   304 334 HOH HOH A . 
B 2 HOH 5   305 211 HOH HOH A . 
B 2 HOH 6   306 91  HOH HOH A . 
B 2 HOH 7   307 102 HOH HOH A . 
B 2 HOH 8   308 49  HOH HOH A . 
B 2 HOH 9   309 15  HOH HOH A . 
B 2 HOH 10  310 62  HOH HOH A . 
B 2 HOH 11  311 146 HOH HOH A . 
B 2 HOH 12  312 197 HOH HOH A . 
B 2 HOH 13  313 186 HOH HOH A . 
B 2 HOH 14  314 159 HOH HOH A . 
B 2 HOH 15  315 86  HOH HOH A . 
B 2 HOH 16  316 148 HOH HOH A . 
B 2 HOH 17  317 133 HOH HOH A . 
B 2 HOH 18  318 10  HOH HOH A . 
B 2 HOH 19  319 110 HOH HOH A . 
B 2 HOH 20  320 74  HOH HOH A . 
B 2 HOH 21  321 291 HOH HOH A . 
B 2 HOH 22  322 126 HOH HOH A . 
B 2 HOH 23  323 350 HOH HOH A . 
B 2 HOH 24  324 48  HOH HOH A . 
B 2 HOH 25  325 1   HOH HOH A . 
B 2 HOH 26  326 150 HOH HOH A . 
B 2 HOH 27  327 28  HOH HOH A . 
B 2 HOH 28  328 260 HOH HOH A . 
B 2 HOH 29  329 128 HOH HOH A . 
B 2 HOH 30  330 21  HOH HOH A . 
B 2 HOH 31  331 17  HOH HOH A . 
B 2 HOH 32  332 61  HOH HOH A . 
B 2 HOH 33  333 123 HOH HOH A . 
B 2 HOH 34  334 103 HOH HOH A . 
B 2 HOH 35  335 11  HOH HOH A . 
B 2 HOH 36  336 4   HOH HOH A . 
B 2 HOH 37  337 96  HOH HOH A . 
B 2 HOH 38  338 90  HOH HOH A . 
B 2 HOH 39  339 55  HOH HOH A . 
B 2 HOH 40  340 43  HOH HOH A . 
B 2 HOH 41  341 161 HOH HOH A . 
B 2 HOH 42  342 201 HOH HOH A . 
B 2 HOH 43  343 32  HOH HOH A . 
B 2 HOH 44  344 35  HOH HOH A . 
B 2 HOH 45  345 139 HOH HOH A . 
B 2 HOH 46  346 5   HOH HOH A . 
B 2 HOH 47  347 3   HOH HOH A . 
B 2 HOH 48  348 65  HOH HOH A . 
B 2 HOH 49  349 71  HOH HOH A . 
B 2 HOH 50  350 178 HOH HOH A . 
B 2 HOH 51  351 268 HOH HOH A . 
B 2 HOH 52  352 27  HOH HOH A . 
B 2 HOH 53  353 130 HOH HOH A . 
B 2 HOH 54  354 121 HOH HOH A . 
B 2 HOH 55  355 30  HOH HOH A . 
B 2 HOH 56  356 134 HOH HOH A . 
B 2 HOH 57  357 64  HOH HOH A . 
B 2 HOH 58  358 24  HOH HOH A . 
B 2 HOH 59  359 46  HOH HOH A . 
B 2 HOH 60  360 57  HOH HOH A . 
B 2 HOH 61  361 18  HOH HOH A . 
B 2 HOH 62  362 63  HOH HOH A . 
B 2 HOH 63  363 112 HOH HOH A . 
B 2 HOH 64  364 31  HOH HOH A . 
B 2 HOH 65  365 78  HOH HOH A . 
B 2 HOH 66  366 69  HOH HOH A . 
B 2 HOH 67  367 155 HOH HOH A . 
B 2 HOH 68  368 25  HOH HOH A . 
B 2 HOH 69  369 14  HOH HOH A . 
B 2 HOH 70  370 68  HOH HOH A . 
B 2 HOH 71  371 236 HOH HOH A . 
B 2 HOH 72  372 188 HOH HOH A . 
B 2 HOH 73  373 127 HOH HOH A . 
B 2 HOH 74  374 141 HOH HOH A . 
B 2 HOH 75  375 99  HOH HOH A . 
B 2 HOH 76  376 85  HOH HOH A . 
B 2 HOH 77  377 67  HOH HOH A . 
B 2 HOH 78  378 275 HOH HOH A . 
B 2 HOH 79  379 2   HOH HOH A . 
B 2 HOH 80  380 33  HOH HOH A . 
B 2 HOH 81  381 45  HOH HOH A . 
B 2 HOH 82  382 122 HOH HOH A . 
B 2 HOH 83  383 307 HOH HOH A . 
B 2 HOH 84  384 164 HOH HOH A . 
B 2 HOH 85  385 51  HOH HOH A . 
B 2 HOH 86  386 60  HOH HOH A . 
B 2 HOH 87  387 220 HOH HOH A . 
B 2 HOH 88  388 238 HOH HOH A . 
B 2 HOH 89  389 184 HOH HOH A . 
B 2 HOH 90  390 137 HOH HOH A . 
B 2 HOH 91  391 44  HOH HOH A . 
B 2 HOH 92  392 6   HOH HOH A . 
B 2 HOH 93  393 22  HOH HOH A . 
B 2 HOH 94  394 320 HOH HOH A . 
B 2 HOH 95  395 89  HOH HOH A . 
B 2 HOH 96  396 276 HOH HOH A . 
B 2 HOH 97  397 321 HOH HOH A . 
B 2 HOH 98  398 111 HOH HOH A . 
B 2 HOH 99  399 244 HOH HOH A . 
B 2 HOH 100 400 172 HOH HOH A . 
B 2 HOH 101 401 107 HOH HOH A . 
B 2 HOH 102 402 194 HOH HOH A . 
B 2 HOH 103 403 75  HOH HOH A . 
B 2 HOH 104 404 76  HOH HOH A . 
B 2 HOH 105 405 215 HOH HOH A . 
B 2 HOH 106 406 138 HOH HOH A . 
B 2 HOH 107 407 12  HOH HOH A . 
B 2 HOH 108 408 36  HOH HOH A . 
B 2 HOH 109 409 316 HOH HOH A . 
B 2 HOH 110 410 152 HOH HOH A . 
B 2 HOH 111 411 153 HOH HOH A . 
B 2 HOH 112 412 160 HOH HOH A . 
B 2 HOH 113 413 166 HOH HOH A . 
B 2 HOH 114 414 23  HOH HOH A . 
B 2 HOH 115 415 230 HOH HOH A . 
B 2 HOH 116 416 129 HOH HOH A . 
B 2 HOH 117 417 53  HOH HOH A . 
B 2 HOH 118 418 241 HOH HOH A . 
B 2 HOH 119 419 266 HOH HOH A . 
B 2 HOH 120 420 72  HOH HOH A . 
B 2 HOH 121 421 156 HOH HOH A . 
B 2 HOH 122 422 132 HOH HOH A . 
B 2 HOH 123 423 212 HOH HOH A . 
B 2 HOH 124 424 109 HOH HOH A . 
B 2 HOH 125 425 97  HOH HOH A . 
B 2 HOH 126 426 41  HOH HOH A . 
B 2 HOH 127 427 93  HOH HOH A . 
B 2 HOH 128 428 277 HOH HOH A . 
B 2 HOH 129 429 117 HOH HOH A . 
B 2 HOH 130 430 345 HOH HOH A . 
B 2 HOH 131 431 26  HOH HOH A . 
B 2 HOH 132 432 40  HOH HOH A . 
B 2 HOH 133 433 119 HOH HOH A . 
B 2 HOH 134 434 192 HOH HOH A . 
B 2 HOH 135 435 101 HOH HOH A . 
B 2 HOH 136 436 362 HOH HOH A . 
B 2 HOH 137 437 170 HOH HOH A . 
B 2 HOH 138 438 195 HOH HOH A . 
B 2 HOH 139 439 54  HOH HOH A . 
B 2 HOH 140 440 79  HOH HOH A . 
B 2 HOH 141 441 218 HOH HOH A . 
B 2 HOH 142 442 229 HOH HOH A . 
B 2 HOH 143 443 16  HOH HOH A . 
B 2 HOH 144 444 355 HOH HOH A . 
B 2 HOH 145 445 13  HOH HOH A . 
B 2 HOH 146 446 352 HOH HOH A . 
B 2 HOH 147 447 174 HOH HOH A . 
B 2 HOH 148 448 81  HOH HOH A . 
B 2 HOH 149 449 369 HOH HOH A . 
B 2 HOH 150 450 42  HOH HOH A . 
B 2 HOH 151 451 181 HOH HOH A . 
B 2 HOH 152 452 52  HOH HOH A . 
B 2 HOH 153 453 38  HOH HOH A . 
B 2 HOH 154 454 106 HOH HOH A . 
B 2 HOH 155 455 349 HOH HOH A . 
B 2 HOH 156 456 207 HOH HOH A . 
B 2 HOH 157 457 326 HOH HOH A . 
B 2 HOH 158 458 113 HOH HOH A . 
B 2 HOH 159 459 359 HOH HOH A . 
B 2 HOH 160 460 80  HOH HOH A . 
B 2 HOH 161 461 37  HOH HOH A . 
B 2 HOH 162 462 189 HOH HOH A . 
B 2 HOH 163 463 87  HOH HOH A . 
B 2 HOH 164 464 9   HOH HOH A . 
B 2 HOH 165 465 168 HOH HOH A . 
B 2 HOH 166 466 262 HOH HOH A . 
B 2 HOH 167 467 8   HOH HOH A . 
B 2 HOH 168 468 84  HOH HOH A . 
B 2 HOH 169 469 253 HOH HOH A . 
B 2 HOH 170 470 176 HOH HOH A . 
B 2 HOH 171 471 73  HOH HOH A . 
B 2 HOH 172 472 29  HOH HOH A . 
B 2 HOH 173 473 124 HOH HOH A . 
B 2 HOH 174 474 185 HOH HOH A . 
B 2 HOH 175 475 39  HOH HOH A . 
B 2 HOH 176 476 50  HOH HOH A . 
B 2 HOH 177 477 232 HOH HOH A . 
B 2 HOH 178 478 120 HOH HOH A . 
B 2 HOH 179 479 295 HOH HOH A . 
B 2 HOH 180 480 56  HOH HOH A . 
B 2 HOH 181 481 199 HOH HOH A . 
B 2 HOH 182 482 219 HOH HOH A . 
B 2 HOH 183 483 358 HOH HOH A . 
B 2 HOH 184 484 7   HOH HOH A . 
B 2 HOH 185 485 283 HOH HOH A . 
B 2 HOH 186 486 47  HOH HOH A . 
B 2 HOH 187 487 257 HOH HOH A . 
B 2 HOH 188 488 140 HOH HOH A . 
B 2 HOH 189 489 280 HOH HOH A . 
B 2 HOH 190 490 66  HOH HOH A . 
B 2 HOH 191 491 366 HOH HOH A . 
B 2 HOH 192 492 203 HOH HOH A . 
B 2 HOH 193 493 288 HOH HOH A . 
B 2 HOH 194 494 94  HOH HOH A . 
B 2 HOH 195 495 343 HOH HOH A . 
B 2 HOH 196 496 175 HOH HOH A . 
B 2 HOH 197 497 162 HOH HOH A . 
B 2 HOH 198 498 157 HOH HOH A . 
B 2 HOH 199 499 19  HOH HOH A . 
B 2 HOH 200 500 58  HOH HOH A . 
B 2 HOH 201 501 100 HOH HOH A . 
B 2 HOH 202 502 83  HOH HOH A . 
B 2 HOH 203 503 265 HOH HOH A . 
B 2 HOH 204 504 143 HOH HOH A . 
B 2 HOH 205 505 274 HOH HOH A . 
B 2 HOH 206 506 346 HOH HOH A . 
B 2 HOH 207 507 329 HOH HOH A . 
B 2 HOH 208 508 330 HOH HOH A . 
B 2 HOH 209 509 125 HOH HOH A . 
B 2 HOH 210 510 340 HOH HOH A . 
B 2 HOH 211 511 149 HOH HOH A . 
B 2 HOH 212 512 354 HOH HOH A . 
B 2 HOH 213 513 92  HOH HOH A . 
B 2 HOH 214 514 77  HOH HOH A . 
B 2 HOH 215 515 242 HOH HOH A . 
B 2 HOH 216 516 163 HOH HOH A . 
B 2 HOH 217 517 263 HOH HOH A . 
B 2 HOH 218 518 246 HOH HOH A . 
B 2 HOH 219 519 190 HOH HOH A . 
B 2 HOH 220 520 136 HOH HOH A . 
B 2 HOH 221 521 173 HOH HOH A . 
B 2 HOH 222 522 290 HOH HOH A . 
B 2 HOH 223 523 196 HOH HOH A . 
B 2 HOH 224 524 224 HOH HOH A . 
B 2 HOH 225 525 209 HOH HOH A . 
B 2 HOH 226 526 171 HOH HOH A . 
B 2 HOH 227 527 353 HOH HOH A . 
B 2 HOH 228 528 335 HOH HOH A . 
B 2 HOH 229 529 269 HOH HOH A . 
B 2 HOH 230 530 82  HOH HOH A . 
B 2 HOH 231 531 210 HOH HOH A . 
B 2 HOH 232 532 344 HOH HOH A . 
B 2 HOH 233 533 214 HOH HOH A . 
B 2 HOH 234 534 271 HOH HOH A . 
B 2 HOH 235 535 240 HOH HOH A . 
B 2 HOH 236 536 315 HOH HOH A . 
B 2 HOH 237 537 306 HOH HOH A . 
B 2 HOH 238 538 115 HOH HOH A . 
B 2 HOH 239 539 234 HOH HOH A . 
B 2 HOH 240 540 233 HOH HOH A . 
B 2 HOH 241 541 370 HOH HOH A . 
B 2 HOH 242 542 363 HOH HOH A . 
B 2 HOH 243 543 258 HOH HOH A . 
B 2 HOH 244 544 296 HOH HOH A . 
B 2 HOH 245 545 261 HOH HOH A . 
B 2 HOH 246 546 360 HOH HOH A . 
B 2 HOH 247 547 286 HOH HOH A . 
B 2 HOH 248 548 364 HOH HOH A . 
B 2 HOH 249 549 256 HOH HOH A . 
B 2 HOH 250 550 198 HOH HOH A . 
B 2 HOH 251 551 284 HOH HOH A . 
B 2 HOH 252 552 235 HOH HOH A . 
B 2 HOH 253 553 305 HOH HOH A . 
B 2 HOH 254 554 361 HOH HOH A . 
B 2 HOH 255 555 251 HOH HOH A . 
B 2 HOH 256 556 297 HOH HOH A . 
B 2 HOH 257 557 200 HOH HOH A . 
B 2 HOH 258 558 287 HOH HOH A . 
B 2 HOH 259 559 281 HOH HOH A . 
B 2 HOH 260 560 191 HOH HOH A . 
B 2 HOH 261 561 116 HOH HOH A . 
B 2 HOH 262 562 20  HOH HOH A . 
B 2 HOH 263 563 319 HOH HOH A . 
B 2 HOH 264 564 34  HOH HOH A . 
B 2 HOH 265 565 98  HOH HOH A . 
B 2 HOH 266 566 309 HOH HOH A . 
B 2 HOH 267 567 249 HOH HOH A . 
B 2 HOH 268 568 213 HOH HOH A . 
B 2 HOH 269 569 248 HOH HOH A . 
B 2 HOH 270 570 299 HOH HOH A . 
B 2 HOH 271 571 259 HOH HOH A . 
B 2 HOH 272 572 301 HOH HOH A . 
B 2 HOH 273 573 314 HOH HOH A . 
B 2 HOH 274 574 135 HOH HOH A . 
B 2 HOH 275 575 351 HOH HOH A . 
B 2 HOH 276 576 204 HOH HOH A . 
B 2 HOH 277 577 339 HOH HOH A . 
B 2 HOH 278 578 70  HOH HOH A . 
B 2 HOH 279 579 325 HOH HOH A . 
B 2 HOH 280 580 158 HOH HOH A . 
B 2 HOH 281 581 348 HOH HOH A . 
B 2 HOH 282 582 108 HOH HOH A . 
B 2 HOH 283 583 328 HOH HOH A . 
B 2 HOH 284 584 332 HOH HOH A . 
B 2 HOH 285 585 193 HOH HOH A . 
B 2 HOH 286 586 292 HOH HOH A . 
B 2 HOH 287 587 318 HOH HOH A . 
B 2 HOH 288 588 317 HOH HOH A . 
B 2 HOH 289 589 347 HOH HOH A . 
B 2 HOH 290 590 228 HOH HOH A . 
B 2 HOH 291 591 327 HOH HOH A . 
B 2 HOH 292 592 225 HOH HOH A . 
B 2 HOH 293 593 237 HOH HOH A . 
B 2 HOH 294 594 293 HOH HOH A . 
B 2 HOH 295 595 356 HOH HOH A . 
B 2 HOH 296 596 179 HOH HOH A . 
B 2 HOH 297 597 222 HOH HOH A . 
B 2 HOH 298 598 182 HOH HOH A . 
B 2 HOH 299 599 311 HOH HOH A . 
B 2 HOH 300 600 323 HOH HOH A . 
B 2 HOH 301 601 226 HOH HOH A . 
B 2 HOH 302 602 59  HOH HOH A . 
B 2 HOH 303 603 165 HOH HOH A . 
B 2 HOH 304 604 243 HOH HOH A . 
B 2 HOH 305 605 302 HOH HOH A . 
B 2 HOH 306 606 208 HOH HOH A . 
B 2 HOH 307 607 285 HOH HOH A . 
B 2 HOH 308 608 221 HOH HOH A . 
B 2 HOH 309 609 223 HOH HOH A . 
B 2 HOH 310 610 104 HOH HOH A . 
B 2 HOH 311 611 308 HOH HOH A . 
B 2 HOH 312 612 217 HOH HOH A . 
B 2 HOH 313 613 304 HOH HOH A . 
B 2 HOH 314 614 341 HOH HOH A . 
B 2 HOH 315 615 247 HOH HOH A . 
B 2 HOH 316 616 312 HOH HOH A . 
B 2 HOH 317 617 267 HOH HOH A . 
B 2 HOH 318 618 145 HOH HOH A . 
B 2 HOH 319 619 303 HOH HOH A . 
B 2 HOH 320 620 206 HOH HOH A . 
B 2 HOH 321 621 337 HOH HOH A . 
B 2 HOH 322 622 147 HOH HOH A . 
B 2 HOH 323 623 294 HOH HOH A . 
B 2 HOH 324 624 114 HOH HOH A . 
B 2 HOH 325 625 187 HOH HOH A . 
B 2 HOH 326 626 254 HOH HOH A . 
B 2 HOH 327 627 298 HOH HOH A . 
B 2 HOH 328 628 88  HOH HOH A . 
B 2 HOH 329 629 183 HOH HOH A . 
B 2 HOH 330 630 177 HOH HOH A . 
B 2 HOH 331 631 131 HOH HOH A . 
B 2 HOH 332 632 282 HOH HOH A . 
B 2 HOH 333 633 118 HOH HOH A . 
B 2 HOH 334 634 227 HOH HOH A . 
B 2 HOH 335 635 95  HOH HOH A . 
B 2 HOH 336 636 367 HOH HOH A . 
B 2 HOH 337 637 202 HOH HOH A . 
B 2 HOH 338 638 338 HOH HOH A . 
B 2 HOH 339 639 313 HOH HOH A . 
B 2 HOH 340 640 310 HOH HOH A . 
B 2 HOH 341 641 105 HOH HOH A . 
B 2 HOH 342 642 270 HOH HOH A . 
B 2 HOH 343 643 322 HOH HOH A . 
B 2 HOH 344 644 154 HOH HOH A . 
B 2 HOH 345 645 239 HOH HOH A . 
B 2 HOH 346 646 250 HOH HOH A . 
B 2 HOH 347 647 357 HOH HOH A . 
B 2 HOH 348 648 279 HOH HOH A . 
B 2 HOH 349 649 180 HOH HOH A . 
B 2 HOH 350 650 255 HOH HOH A . 
B 2 HOH 351 651 324 HOH HOH A . 
B 2 HOH 352 652 336 HOH HOH A . 
B 2 HOH 353 653 331 HOH HOH A . 
B 2 HOH 354 654 144 HOH HOH A . 
B 2 HOH 355 655 151 HOH HOH A . 
B 2 HOH 356 656 252 HOH HOH A . 
B 2 HOH 357 657 167 HOH HOH A . 
B 2 HOH 358 658 205 HOH HOH A . 
B 2 HOH 359 659 368 HOH HOH A . 
B 2 HOH 360 660 333 HOH HOH A . 
B 2 HOH 361 661 272 HOH HOH A . 
B 2 HOH 362 662 216 HOH HOH A . 
B 2 HOH 363 663 289 HOH HOH A . 
B 2 HOH 364 664 342 HOH HOH A . 
B 2 HOH 365 665 300 HOH HOH A . 
B 2 HOH 366 666 264 HOH HOH A . 
B 2 HOH 367 667 231 HOH HOH A . 
B 2 HOH 368 668 169 HOH HOH A . 
B 2 HOH 369 669 278 HOH HOH A . 
B 2 HOH 370 670 273 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.9_1692+SVN 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .            2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .            3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .            4 
# 
_cell.angle_alpha                  90.0 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.0 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.0 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZP6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     179.29 
_cell.length_a_esd                 ? 
_cell.length_b                     179.29 
_cell.length_b_esd                 ? 
_cell.length_c                     151.35 
_cell.length_c_esd                 ? 
_cell.volume                       4213327.24272 
_cell.volume_esd                   ? 
_cell.Z_PDB                        18 
_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                         8ZP6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                155 
_symmetry.space_group_name_Hall            
;R 3 2"
;
_symmetry.space_group_name_H-M             'H 3 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZP6 
_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             ? 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          ? 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.0 
_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    'Polyethylene glycol 3350, Ammonium sulfate, Bis-Tris' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-01-05 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.987 
_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                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ZP6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.01 
_reflns.d_resolution_low                               31.8 
_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                                     61853 
_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                                19.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          3.6 
_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                                   0.920 
_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                                    2.01 
_reflns_shell.d_res_low                                     2.06 
_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                             61853 
_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                                  0.684 
_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                               28.0799902565 
_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                                 8ZP6 
_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                            2.10007468686 
_refine.ls_d_res_low                             30.4202143907 
_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                     54289 
_refine.ls_number_reflns_R_free                  1755 
_refine.ls_number_reflns_R_work                  52534 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.9337321675 
_refine.ls_percent_reflns_R_free                 3.23269907348 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.240429651677 
_refine.ls_R_factor_R_free                       0.257517101071 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.239857369321 
_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                          1.33645361864 
_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       ? 
_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             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9 
_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                 27.0605106408 
_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                            0.253658741634 
_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                       2.10007468686 
_refine_hist.d_res_low                        30.4202143907 
_refine_hist.number_atoms_solvent             370 
_refine_hist.number_atoms_total               2749 
_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        2379 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.0064037845217 ? 2459 ? f_bond_d  ? ? 
'X-RAY DIFFRACTION' ? 1.00804985918   ? 3357 ? f_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' 2.1001 2.1568 . . 133 3988 99.6855345912 . . . . 0.272361782677 . . . . . . . . . . . 0.299683338977 
'X-RAY DIFFRACTION' 2.1568 2.2203 . . 135 4007 99.9758629013 . . . . 0.265316364574 . . . . . . . . . . . 0.307740454905 
'X-RAY DIFFRACTION' 2.2203 2.2919 . . 133 4014 99.9758919961 . . . . 0.275776508688 . . . . . . . . . . . 0.295016781866 
'X-RAY DIFFRACTION' 2.2919 2.3738 . . 134 4011 100.0         . . . . 0.272855995374 . . . . . . . . . . . 0.285580872542 
'X-RAY DIFFRACTION' 2.3738 2.4688 . . 134 4022 99.7120921305 . . . . 0.266549413615 . . . . . . . . . . . 0.295362476202 
'X-RAY DIFFRACTION' 2.4688 2.5811 . . 134 4024 99.9759557586 . . . . 0.268525037938 . . . . . . . . . . . 0.265031312838 
'X-RAY DIFFRACTION' 2.5811 2.7171 . . 134 4008 100.0         . . . . 0.272747328992 . . . . . . . . . . . 0.292521264167 
'X-RAY DIFFRACTION' 2.7171 2.8872 . . 136 4052 100.0         . . . . 0.26116003241  . . . . . . . . . . . 0.300888576003 
'X-RAY DIFFRACTION' 2.8872 3.11   . . 135 4040 100.0         . . . . 0.248835764687 . . . . . . . . . . . 0.244220532301 
'X-RAY DIFFRACTION' 3.11   3.4226 . . 135 4026 100.0         . . . . 0.231207896042 . . . . . . . . . . . 0.268288604502 
'X-RAY DIFFRACTION' 3.4226 3.9169 . . 135 4066 100.0         . . . . 0.215188682009 . . . . . . . . . . . 0.232214875648 
'X-RAY DIFFRACTION' 3.9169 4.9315 . . 137 4089 100.0         . . . . 0.208600237352 . . . . . . . . . . . 0.225163694676 
# 
_struct.entry_id                     8ZP6 
_struct.title                        'Crystal structure of Epoxide hydrolase MdEH (Mycobacterium dioxanotrophicus)' 
_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        8ZP6 
_struct_keywords.text            'Epoxide hydrolase, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A1Y0CH10_9MYCO 
_struct_ref.pdbx_db_accession          A0A1Y0CH10 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTIRRPEHFTHHEVQLSDVKIHYVREGAGPTLLLLHGWPGFWWEWSKVIGPLSERFDVIVPDLRGFGDSEKPDLSDLAQY
SLERVADDQAELLNALGIDQAYVVGHDYSAIVVHKFIRKYPDRVVKAAIFDPITPDFGPFYLGFPHIAESWYSQFHQTDM
SVELVTSSREACRIYFKHFFDHWSYHAPLLTQDELDIYVDNCMKPNNVHGGFNYYRSNLSVTSDPWTDLDRTVSDLPVTM
LWGVGDPVVPSSLVHQVPNYYSNYTMELIQDAGHFMMVEKPEVVIDRLKAGFR
;
_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              8ZP6 
_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                 293 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A1Y0CH10 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  293 
_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       293 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA hexameric 6 
2 author_and_software_defined_assembly PISA dimeric   2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 9710  ? 
1 MORE         -93   ? 
1 'SSA (A^2)'  58930 ? 
2 'ABSA (A^2)' 2160  ? 
2 MORE         -24   ? 
2 'SSA (A^2)'  20720 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1,2,3,4,5,6 A,B 
2 1,4         A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z                  1.0000000000  0.0000000000  0.0000000000 0.0000000000   0.0000000000  
1.0000000000  0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 2_665  -y+1,x-y+1,z           -0.5000000000 -0.8660254038 0.0000000000 89.6450000000  0.8660254038  
-0.5000000000 0.0000000000 155.2696946445 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
3 'crystal symmetry operation' 3_565  -x+y,-x+1,z            -0.5000000000 0.8660254038  0.0000000000 -89.6450000000 -0.8660254038 
-0.5000000000 0.0000000000 155.2696946445 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
4 'crystal symmetry operation' 10_455 y-1/3,x+1/3,-z+1/3     -0.5000000000 0.8660254038  0.0000000000 -89.6450000000 0.8660254038  
0.5000000000  0.0000000000 51.7565648815  0.0000000000 0.0000000000 -1.0000000000 50.4500000000 
5 'crystal symmetry operation' 11_565 x-y+2/3,-y+4/3,-z+1/3  1.0000000000  0.0000000000  0.0000000000 0.0000000000   0.0000000000  
-1.0000000000 0.0000000000 207.0262595260 0.0000000000 0.0000000000 -1.0000000000 50.4500000000 
6 'crystal symmetry operation' 12_555 -x+2/3,-x+y+1/3,-z+1/3 -0.5000000000 -0.8660254038 0.0000000000 89.6450000000  -0.8660254038 
0.5000000000  0.0000000000 51.7565648815  0.0000000000 0.0000000000 -1.0000000000 50.4500000000 
# 
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 ARG A 5   ? PHE A 9   ? ARG A 5   PHE A 9   5 ? 5  
HELX_P HELX_P2  AA2 PHE A 41  ? GLU A 44  ? PHE A 41  GLU A 44  5 ? 4  
HELX_P HELX_P3  AA3 TRP A 45  ? SER A 53  ? TRP A 45  SER A 53  1 ? 9  
HELX_P HELX_P4  AA4 ASP A 76  ? TYR A 80  ? ASP A 76  TYR A 80  5 ? 5  
HELX_P HELX_P5  AA5 SER A 81  ? LEU A 96  ? SER A 81  LEU A 96  1 ? 16 
HELX_P HELX_P6  AA6 ASP A 107 ? TYR A 120 ? ASP A 107 TYR A 120 1 ? 14 
HELX_P HELX_P7  AA7 ASP A 136 ? LEU A 142 ? ASP A 136 LEU A 142 1 ? 7  
HELX_P HELX_P8  AA8 HIS A 146 ? HIS A 156 ? HIS A 146 HIS A 156 1 ? 11 
HELX_P HELX_P9  AA9 THR A 158 ? THR A 166 ? THR A 158 THR A 166 1 ? 9  
HELX_P HELX_P10 AB1 SER A 168 ? TRP A 183 ? SER A 168 TRP A 183 1 ? 16 
HELX_P HELX_P11 AB2 THR A 191 ? MET A 203 ? THR A 191 MET A 203 1 ? 13 
HELX_P HELX_P12 AB3 ASN A 206 ? LEU A 219 ? ASN A 206 LEU A 219 1 ? 14 
HELX_P HELX_P13 AB4 ASP A 228 ? THR A 232 ? ASP A 228 THR A 232 5 ? 5  
HELX_P HELX_P14 AB5 PRO A 250 ? VAL A 257 ? PRO A 250 VAL A 257 5 ? 8  
HELX_P HELX_P15 AB6 PHE A 275 ? LYS A 280 ? PHE A 275 LYS A 280 1 ? 6  
HELX_P HELX_P16 AB7 LYS A 280 ? PHE A 292 ? LYS A 280 PHE A 292 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TRP 38  A . ? TRP 38  A PRO 39  A ? PRO 39  A 1 6.58 
2 PHE 144 A . ? PHE 144 A PRO 145 A ? PRO 145 A 1 5.35 
3 ALA 187 A . ? ALA 187 A PRO 188 A ? PRO 188 A 1 2.29 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 HIS A 11  ? GLN A 15  ? HIS A 11  GLN A 15  
AA1 2 LYS A 20  ? GLU A 26  ? LYS A 20  GLU A 26  
AA1 3 ASP A 57  ? PRO A 61  ? ASP A 57  PRO A 61  
AA1 4 THR A 31  ? LEU A 35  ? THR A 31  LEU A 35  
AA1 5 ALA A 101 ? HIS A 106 ? ALA A 101 HIS A 106 
AA1 6 VAL A 124 ? PHE A 130 ? VAL A 124 PHE A 130 
AA1 7 VAL A 238 ? GLY A 243 ? VAL A 238 GLY A 243 
AA1 8 TYR A 264 ? ILE A 269 ? TYR A 264 ILE A 269 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N HIS A 12  ? N HIS A 12  O TYR A 23  ? O TYR A 23  
AA1 2 3 N VAL A 24  ? N VAL A 24  O VAL A 60  ? O VAL A 60  
AA1 3 4 O ILE A 59  ? O ILE A 59  N LEU A 32  ? N LEU A 32  
AA1 4 5 N LEU A 33  ? N LEU A 33  O TYR A 102 ? O TYR A 102 
AA1 5 6 N VAL A 103 ? N VAL A 103 O ALA A 128 ? O ALA A 128 
AA1 6 7 N ALA A 127 ? N ALA A 127 O THR A 239 ? O THR A 239 
AA1 7 8 N TRP A 242 ? N TRP A 242 O ILE A 269 ? O ILE A 269 
# 
_pdbx_entry_details.entry_id                   8ZP6 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
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 O   A HOH 600 ? ? O A HOH 647 ? ? 1.90 
2  1 O   A HOH 313 ? ? O A HOH 447 ? ? 1.92 
3  1 O   A HOH 563 ? ? O A HOH 638 ? ? 1.94 
4  1 O   A HOH 574 ? ? O A HOH 597 ? ? 1.94 
5  1 O   A HOH 505 ? ? O A HOH 605 ? ? 1.98 
6  1 O   A HOH 539 ? ? O A HOH 545 ? ? 1.98 
7  1 OE2 A GLU 170 ? ? O A HOH 301 ? ? 2.02 
8  1 O   A HOH 554 ? ? O A HOH 595 ? ? 2.02 
9  1 O   A HOH 305 ? ? O A HOH 578 ? ? 2.08 
10 1 OD2 A ASP 122 ? ? O A HOH 302 ? ? 2.09 
11 1 O   A HOH 588 ? ? O A HOH 651 ? ? 2.10 
12 1 O   A HOH 550 ? ? O A HOH 639 ? ? 2.13 
13 1 O   A HOH 583 ? ? O A HOH 660 ? ? 2.16 
14 1 O   A HOH 409 ? ? O A HOH 459 ? ? 2.16 
15 1 O   A HOH 583 ? ? O A HOH 638 ? ? 2.16 
16 1 O   A HOH 367 ? ? O A HOH 640 ? ? 2.16 
17 1 O   A HOH 573 ? ? O A HOH 591 ? ? 2.18 
18 1 O   A HOH 456 ? ? O A HOH 608 ? ? 2.18 
19 1 O   A HOH 517 ? ? O A HOH 605 ? ? 2.19 
20 1 O   A HOH 304 ? ? O A HOH 394 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     657 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     662 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   10_455 
_pdbx_validate_symm_contact.dist              2.01 
# 
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 PHE A 41  ? ? -169.41 -167.20 
2 1 ASP A 73  ? ? -20.78  106.76  
3 1 ASP A 107 ? ? 58.69   -133.49 
4 1 ASN A 206 ? ? 71.44   -0.72   
5 1 ARG A 231 ? ? -89.22  37.91   
6 1 PHE A 275 ? ? -113.83 73.17   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 429 ? B HOH . 
2 1 A HOH 582 ? B HOH . 
3 1 A HOH 652 ? B HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1  x,y,z                  
2  -y,x-y,z               
3  -x+y,-x,z              
4  x-y,-y,-z              
5  -x,-x+y,-z             
6  y,x,-z                 
7  x+1/3,y+2/3,z+2/3      
8  -y+1/3,x-y+2/3,z+2/3   
9  -x+y+1/3,-x+2/3,z+2/3  
10 x-y+1/3,-y+2/3,-z+2/3  
11 -x+1/3,-x+y+2/3,-z+2/3 
12 y+1/3,x+2/3,-z+2/3     
13 x+2/3,y+1/3,z+1/3      
14 -y+2/3,x-y+1/3,z+1/3   
15 -x+y+2/3,-x+1/3,z+1/3  
16 x-y+2/3,-y+1/3,-z+1/3  
17 -x+2/3,-x+y+1/3,-z+1/3 
18 y+2/3,x+1/3,-z+1/3     
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 669 ? 5.82 . 
2 1 O ? A HOH 670 ? 6.98 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A THR 2 ? A THR 2 
# 
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  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
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  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'R 3 2 :H' 
_space_group.name_Hall        
;R 3 2"
;
_space_group.IT_number        155 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    8ZP6 
_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]   0.005578 
_atom_sites.fract_transf_matrix[1][2]   0.003220 
_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]   0.006440 
_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]   0.006607 
_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_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 25.62398 1.50364  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 19.97189 1.75589  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 15.80542 1.70748  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 1.23737  29.19336 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ILE A 1 3   ? 1.41725   46.46847 25.25639 1.000 52.03171 ? 3   ILE A N   1 
ATOM   2    C CA  . ILE A 1 3   ? 0.66228   47.26315 26.21776 1.000 44.18592 ? 3   ILE A CA  1 
ATOM   3    C C   . ILE A 1 3   ? 0.75575   46.65546 27.61785 1.000 43.77041 ? 3   ILE A C   1 
ATOM   4    O O   . ILE A 1 3   ? 0.65720   45.44368 27.79666 1.000 44.41009 ? 3   ILE A O   1 
ATOM   5    C CB  . ILE A 1 3   ? -0.82959  47.39906 25.80675 1.000 44.61204 ? 3   ILE A CB  1 
ATOM   6    C CG1 . ILE A 1 3   ? -1.57739  48.32007 26.77509 1.000 39.91736 ? 3   ILE A CG1 1 
ATOM   7    C CG2 . ILE A 1 3   ? -1.50526  46.03359 25.72758 1.000 46.98217 ? 3   ILE A CG2 1 
ATOM   8    C CD1 . ILE A 1 3   ? -3.07083  48.38180 26.54241 1.000 35.60497 ? 3   ILE A CD1 1 
ATOM   9    N N   . ARG A 1 4   ? 0.96789   47.50431 28.61385 1.000 37.60048 ? 4   ARG A N   1 
ATOM   10   C CA  . ARG A 1 4   ? 0.99536   47.04035 29.98655 1.000 35.83762 ? 4   ARG A CA  1 
ATOM   11   C C   . ARG A 1 4   ? -0.21182  47.58980 30.74568 1.000 29.98124 ? 4   ARG A C   1 
ATOM   12   O O   . ARG A 1 4   ? -0.23218  48.75361 31.14194 1.000 32.13378 ? 4   ARG A O   1 
ATOM   13   C CB  . ARG A 1 4   ? 2.30159   47.45348 30.65260 1.000 34.61761 ? 4   ARG A CB  1 
ATOM   14   C CG  . ARG A 1 4   ? 2.59575   46.68421 31.91582 1.000 36.96979 ? 4   ARG A CG  1 
ATOM   15   C CD  . ARG A 1 4   ? 3.98338   46.98941 32.43305 1.000 33.46399 ? 4   ARG A CD  1 
ATOM   16   N NE  . ARG A 1 4   ? 4.11155   46.54788 33.81207 1.000 33.57454 ? 4   ARG A NE  1 
ATOM   17   C CZ  . ARG A 1 4   ? 5.02819   46.99594 34.65420 1.000 33.19413 ? 4   ARG A CZ  1 
ATOM   18   N NH1 . ARG A 1 4   ? 5.90299   47.90452 34.24848 1.000 30.56434 ? 4   ARG A NH1 1 
ATOM   19   N NH2 . ARG A 1 4   ? 5.06360   46.53438 35.90133 1.000 31.80355 ? 4   ARG A NH2 1 
ATOM   20   N N   . ARG A 1 5   ? -1.21498  46.74402 30.93651 1.000 29.75113 ? 5   ARG A N   1 
ATOM   21   C CA  . ARG A 1 5   ? -2.50423  47.15787 31.48888 1.000 32.65815 ? 5   ARG A CA  1 
ATOM   22   C C   . ARG A 1 5   ? -2.39209  47.53042 32.96887 1.000 31.19142 ? 5   ARG A C   1 
ATOM   23   O O   . ARG A 1 5   ? -1.43453  47.13334 33.62602 1.000 29.38142 ? 5   ARG A O   1 
ATOM   24   C CB  . ARG A 1 5   ? -3.52747  46.04562 31.27991 1.000 33.36229 ? 5   ARG A CB  1 
ATOM   25   C CG  . ARG A 1 5   ? -3.67797  45.62617 29.82857 1.000 34.73186 ? 5   ARG A CG  1 
ATOM   26   C CD  . ARG A 1 5   ? -4.76534  44.57290 29.67790 1.000 35.20210 ? 5   ARG A CD  1 
ATOM   27   N NE  . ARG A 1 5   ? -6.04163  45.07914 30.16587 1.000 37.23730 ? 5   ARG A NE  1 
ATOM   28   C CZ  . ARG A 1 5   ? -6.93690  45.70181 29.40681 1.000 36.10662 ? 5   ARG A CZ  1 
ATOM   29   N NH1 . ARG A 1 5   ? -6.70645  45.87548 28.10957 1.000 36.40820 ? 5   ARG A NH1 1 
ATOM   30   N NH2 . ARG A 1 5   ? -8.06503  46.14115 29.94439 1.000 34.54794 ? 5   ARG A NH2 1 
ATOM   31   N N   . PRO A 1 6   ? -3.35786  48.31698 33.48808 1.000 29.76149 ? 6   PRO A N   1 
ATOM   32   C CA  . PRO A 1 6   ? -3.28248  48.81533 34.86721 1.000 26.94241 ? 6   PRO A CA  1 
ATOM   33   C C   . PRO A 1 6   ? -3.06039  47.71895 35.89756 1.000 29.68324 ? 6   PRO A C   1 
ATOM   34   O O   . PRO A 1 6   ? -2.29333  47.88933 36.84827 1.000 26.43359 ? 6   PRO A O   1 
ATOM   35   C CB  . PRO A 1 6   ? -4.64857  49.46515 35.07191 1.000 27.99912 ? 6   PRO A CB  1 
ATOM   36   C CG  . PRO A 1 6   ? -5.03312  49.92930 33.72930 1.000 27.41450 ? 6   PRO A CG  1 
ATOM   37   C CD  . PRO A 1 6   ? -4.51019  48.89328 32.77208 1.000 28.16059 ? 6   PRO A CD  1 
ATOM   38   N N   . GLU A 1 7   ? -3.72898  46.59198 35.69632 1.000 33.04734 ? 7   GLU A N   1 
ATOM   39   C CA  . GLU A 1 7   ? -3.67776  45.49633 36.65161 1.000 32.44517 ? 7   GLU A CA  1 
ATOM   40   C C   . GLU A 1 7   ? -2.31052  44.80036 36.67646 1.000 32.84861 ? 7   GLU A C   1 
ATOM   41   O O   . GLU A 1 7   ? -2.03899  43.99633 37.55866 1.000 35.43669 ? 7   GLU A O   1 
ATOM   42   C CB  . GLU A 1 7   ? -4.79354  44.48293 36.35136 1.000 33.95962 ? 7   GLU A CB  1 
ATOM   43   C CG  . GLU A 1 7   ? -4.75782  43.87995 34.95140 1.000 38.74027 ? 7   GLU A CG  1 
ATOM   44   C CD  . GLU A 1 7   ? -5.58241  44.65830 33.92634 1.000 38.17438 ? 7   GLU A CD  1 
ATOM   45   O OE1 . GLU A 1 7   ? -5.92195  44.06455 32.88543 1.000 38.83550 ? 7   GLU A OE1 1 
ATOM   46   O OE2 . GLU A 1 7   ? -5.88870  45.84972 34.14863 1.000 34.63678 ? 7   GLU A OE2 1 
ATOM   47   N N   . HIS A 1 8   ? -1.43779  45.12278 35.73010 1.000 33.00627 ? 8   HIS A N   1 
ATOM   48   C CA  . HIS A 1 8   ? -0.11234  44.51237 35.70854 1.000 33.16817 ? 8   HIS A CA  1 
ATOM   49   C C   . HIS A 1 8   ? 0.92751   45.38392 36.41838 1.000 31.84485 ? 8   HIS A C   1 
ATOM   50   O O   . HIS A 1 8   ? 2.12265   45.28030 36.16749 1.000 33.68733 ? 8   HIS A O   1 
ATOM   51   C CB  . HIS A 1 8   ? 0.30785   44.22172 34.26866 1.000 36.21740 ? 8   HIS A CB  1 
ATOM   52   C CG  . HIS A 1 8   ? -0.60624  43.26555 33.56589 1.000 42.73807 ? 8   HIS A CG  1 
ATOM   53   N ND1 . HIS A 1 8   ? -0.77856  43.26212 32.19815 1.000 48.72808 ? 8   HIS A ND1 1 
ATOM   54   C CD2 . HIS A 1 8   ? -1.41322  42.29066 34.04964 1.000 42.98059 ? 8   HIS A CD2 1 
ATOM   55   C CE1 . HIS A 1 8   ? -1.65022  42.32415 31.86878 1.000 47.85316 ? 8   HIS A CE1 1 
ATOM   56   N NE2 . HIS A 1 8   ? -2.05106  41.72192 32.97370 1.000 49.43071 ? 8   HIS A NE2 1 
ATOM   57   N N   . PHE A 1 9   ? 0.45903   46.24418 37.31327 1.000 29.68943 ? 9   PHE A N   1 
ATOM   58   C CA  . PHE A 1 9   ? 1.35340   46.99345 38.18030 1.000 28.77982 ? 9   PHE A CA  1 
ATOM   59   C C   . PHE A 1 9   ? 0.99091   46.68171 39.62997 1.000 29.17598 ? 9   PHE A C   1 
ATOM   60   O O   . PHE A 1 9   ? -0.07945  46.13778 39.89355 1.000 28.91336 ? 9   PHE A O   1 
ATOM   61   C CB  . PHE A 1 9   ? 1.24836   48.49788 37.91882 1.000 25.62309 ? 9   PHE A CB  1 
ATOM   62   C CG  . PHE A 1 9   ? 1.80640   48.93872 36.58781 1.000 24.65245 ? 9   PHE A CG  1 
ATOM   63   C CD1 . PHE A 1 9   ? 1.07846   48.77682 35.42227 1.000 27.24708 ? 9   PHE A CD1 1 
ATOM   64   C CD2 . PHE A 1 9   ? 3.04140   49.55155 36.51270 1.000 27.79851 ? 9   PHE A CD2 1 
ATOM   65   C CE1 . PHE A 1 9   ? 1.57960   49.21247 34.19955 1.000 24.67673 ? 9   PHE A CE1 1 
ATOM   66   C CE2 . PHE A 1 9   ? 3.54997   49.98381 35.28960 1.000 27.50436 ? 9   PHE A CE2 1 
ATOM   67   C CZ  . PHE A 1 9   ? 2.81615   49.80853 34.13923 1.000 24.26609 ? 9   PHE A CZ  1 
ATOM   68   N N   . THR A 1 10  ? 1.86461   47.03734 40.56501 1.000 27.58573 ? 10  THR A N   1 
ATOM   69   C CA  . THR A 1 10  ? 1.53183   46.90686 41.97836 1.000 29.68547 ? 10  THR A CA  1 
ATOM   70   C C   . THR A 1 10  ? 0.95130   48.20257 42.54446 1.000 26.34637 ? 10  THR A C   1 
ATOM   71   O O   . THR A 1 10  ? 1.57162   49.26486 42.47135 1.000 28.09801 ? 10  THR A O   1 
ATOM   72   C CB  . THR A 1 10  ? 2.74667   46.50174 42.81658 1.000 31.30834 ? 10  THR A CB  1 
ATOM   73   O OG1 . THR A 1 10  ? 3.28958   45.28324 42.29594 1.000 37.25299 ? 10  THR A OG1 1 
ATOM   74   C CG2 . THR A 1 10  ? 2.31975   46.29469 44.27673 1.000 29.39451 ? 10  THR A CG2 1 
ATOM   75   N N   . HIS A 1 11  ? -0.23641  48.08968 43.12199 1.000 22.73795 ? 11  HIS A N   1 
ATOM   76   C CA  . HIS A 1 11  ? -1.01454  49.23749 43.54407 1.000 24.20009 ? 11  HIS A CA  1 
ATOM   77   C C   . HIS A 1 11  ? -0.95149  49.49782 45.04442 1.000 27.87779 ? 11  HIS A C   1 
ATOM   78   O O   . HIS A 1 11  ? -1.08549  48.58107 45.85406 1.000 27.33673 ? 11  HIS A O   1 
ATOM   79   C CB  . HIS A 1 11  ? -2.45958  49.04659 43.09404 1.000 24.76415 ? 11  HIS A CB  1 
ATOM   80   C CG  . HIS A 1 11  ? -2.60633  49.03121 41.60813 1.000 26.69292 ? 11  HIS A CG  1 
ATOM   81   N ND1 . HIS A 1 11  ? -2.90159  50.16355 40.88282 1.000 25.71755 ? 11  HIS A ND1 1 
ATOM   82   C CD2 . HIS A 1 11  ? -2.44278  48.03517 40.70543 1.000 27.78051 ? 11  HIS A CD2 1 
ATOM   83   C CE1 . HIS A 1 11  ? -2.94227  49.85993 39.59788 1.000 27.31667 ? 11  HIS A CE1 1 
ATOM   84   N NE2 . HIS A 1 11  ? -2.66588  48.57507 39.46332 1.000 28.24578 ? 11  HIS A NE2 1 
ATOM   85   N N   . HIS A 1 12  ? -0.74272  50.76281 45.39602 1.000 24.83394 ? 12  HIS A N   1 
ATOM   86   C CA  . HIS A 1 12  ? -0.63016  51.18248 46.78092 1.000 26.67449 ? 12  HIS A CA  1 
ATOM   87   C C   . HIS A 1 12  ? -1.57173  52.32615 47.07884 1.000 26.09373 ? 12  HIS A C   1 
ATOM   88   O O   . HIS A 1 12  ? -1.94415  53.08125 46.18642 1.000 25.23558 ? 12  HIS A O   1 
ATOM   89   C CB  . HIS A 1 12  ? 0.78806   51.65145 47.11151 1.000 24.49167 ? 12  HIS A CB  1 
ATOM   90   C CG  . HIS A 1 12  ? 1.85680   50.66515 46.77848 1.000 26.39529 ? 12  HIS A CG  1 
ATOM   91   N ND1 . HIS A 1 12  ? 2.46512   49.88158 47.73628 1.000 25.63883 ? 12  HIS A ND1 1 
ATOM   92   C CD2 . HIS A 1 12  ? 2.45143   50.35540 45.60327 1.000 25.57290 ? 12  HIS A CD2 1 
ATOM   93   C CE1 . HIS A 1 12  ? 3.37600   49.12041 47.16071 1.000 27.08733 ? 12  HIS A CE1 1 
ATOM   94   N NE2 . HIS A 1 12  ? 3.38770   49.38764 45.86749 1.000 27.65005 ? 12  HIS A NE2 1 
ATOM   95   N N   . GLU A 1 13  ? -1.92029  52.46933 48.34897 1.000 25.31652 ? 13  GLU A N   1 
ATOM   96   C CA  . GLU A 1 13  ? -2.59475  53.66330 48.81960 1.000 26.07265 ? 13  GLU A CA  1 
ATOM   97   C C   . GLU A 1 13  ? -1.94366  54.12203 50.12161 1.000 26.65471 ? 13  GLU A C   1 
ATOM   98   O O   . GLU A 1 13  ? -1.50357  53.30245 50.91888 1.000 28.33937 ? 13  GLU A O   1 
ATOM   99   C CB  . GLU A 1 13  ? -4.09206  53.40222 49.01080 1.000 25.42495 ? 13  GLU A CB  1 
ATOM   100  C CG  . GLU A 1 13  ? -4.86564  54.63794 49.42665 1.000 32.33027 ? 13  GLU A CG  1 
ATOM   101  C CD  . GLU A 1 13  ? -6.33643  54.35528 49.68096 1.000 38.50556 ? 13  GLU A CD  1 
ATOM   102  O OE1 . GLU A 1 13  ? -7.05238  53.99613 48.71925 1.000 39.80481 ? 13  GLU A OE1 1 
ATOM   103  O OE2 . GLU A 1 13  ? -6.76598  54.48674 50.84810 1.000 41.42707 ? 13  GLU A OE2 1 
ATOM   104  N N   . VAL A 1 14  ? -1.86291  55.42820 50.32774 1.000 25.15486 ? 14  VAL A N   1 
ATOM   105  C CA  . VAL A 1 14  ? -1.29499  55.96250 51.54718 1.000 25.42776 ? 14  VAL A CA  1 
ATOM   106  C C   . VAL A 1 14  ? -2.17827  57.09556 52.03279 1.000 27.09111 ? 14  VAL A C   1 
ATOM   107  O O   . VAL A 1 14  ? -2.69508  57.87958 51.23742 1.000 27.58706 ? 14  VAL A O   1 
ATOM   108  C CB  . VAL A 1 14  ? 0.17075   56.45516 51.35278 1.000 25.85480 ? 14  VAL A CB  1 
ATOM   109  C CG1 . VAL A 1 14  ? 0.26275   57.50970 50.26025 1.000 24.48285 ? 14  VAL A CG1 1 
ATOM   110  C CG2 . VAL A 1 14  ? 0.73667   56.99142 52.66491 1.000 25.26908 ? 14  VAL A CG2 1 
ATOM   111  N N   . GLN A 1 15  ? -2.37454  57.15486 53.34244 1.000 25.26555 ? 15  GLN A N   1 
ATOM   112  C CA  . GLN A 1 15  ? -3.20501  58.17659 53.95177 1.000 26.78562 ? 15  GLN A CA  1 
ATOM   113  C C   . GLN A 1 15  ? -2.37034  59.40354 54.27328 1.000 27.62556 ? 15  GLN A C   1 
ATOM   114  O O   . GLN A 1 15  ? -1.52697  59.36341 55.15748 1.000 25.80041 ? 15  GLN A O   1 
ATOM   115  C CB  . GLN A 1 15  ? -3.87245  57.65406 55.22323 1.000 25.38156 ? 15  GLN A CB  1 
ATOM   116  C CG  . GLN A 1 15  ? -4.65598  58.72057 55.96538 1.000 29.66179 ? 15  GLN A CG  1 
ATOM   117  C CD  . GLN A 1 15  ? -5.90485  59.13503 55.21186 1.000 30.25002 ? 15  GLN A CD  1 
ATOM   118  O OE1 . GLN A 1 15  ? -6.83278  58.34934 55.06880 1.000 32.81454 ? 15  GLN A OE1 1 
ATOM   119  N NE2 . GLN A 1 15  ? -5.92682  60.36569 54.71398 1.000 27.57022 ? 15  GLN A NE2 1 
ATOM   120  N N   . LEU A 1 16  ? -2.59888  60.48809 53.54402 1.000 23.98364 ? 16  LEU A N   1 
ATOM   121  C CA  . LEU A 1 16  ? -1.89076  61.72942 53.81512 1.000 27.82959 ? 16  LEU A CA  1 
ATOM   122  C C   . LEU A 1 16  ? -2.77533  62.58142 54.70982 1.000 28.76302 ? 16  LEU A C   1 
ATOM   123  O O   . LEU A 1 16  ? -3.81252  62.10846 55.17462 1.000 27.38052 ? 16  LEU A O   1 
ATOM   124  C CB  . LEU A 1 16  ? -1.52571  62.45210 52.51250 1.000 27.20013 ? 16  LEU A CB  1 
ATOM   125  C CG  . LEU A 1 16  ? -0.72394  61.59338 51.53034 1.000 25.44415 ? 16  LEU A CG  1 
ATOM   126  C CD1 . LEU A 1 16  ? -0.34020  62.37694 50.28824 1.000 26.80522 ? 16  LEU A CD1 1 
ATOM   127  C CD2 . LEU A 1 16  ? 0.52666   61.02211 52.20196 1.000 26.86334 ? 16  LEU A CD2 1 
ATOM   128  N N   . SER A 1 17  ? -2.38587  63.82880 54.95036 1.000 29.07040 ? 17  SER A N   1 
ATOM   129  C CA  . SER A 1 17  ? -3.03977  64.59717 55.99676 1.000 31.89824 ? 17  SER A CA  1 
ATOM   130  C C   . SER A 1 17  ? -4.51601  64.85921 55.68610 1.000 34.40594 ? 17  SER A C   1 
ATOM   131  O O   . SER A 1 17  ? -5.33661  64.74357 56.58237 1.000 32.08820 ? 17  SER A O   1 
ATOM   132  C CB  . SER A 1 17  ? -2.29565  65.91295 56.25686 1.000 30.24376 ? 17  SER A CB  1 
ATOM   133  O OG  . SER A 1 17  ? -2.43961  66.80526 55.17390 1.000 35.80114 ? 17  SER A OG  1 
ATOM   134  N N   . ASP A 1 18  ? -4.87744  65.18123 54.44116 1.000 31.34605 ? 18  ASP A N   1 
ATOM   135  C CA  . ASP A 1 18  ? -6.31047  65.33169 54.14498 1.000 33.10881 ? 18  ASP A CA  1 
ATOM   136  C C   . ASP A 1 18  ? -6.82649  64.58181 52.91934 1.000 31.86802 ? 18  ASP A C   1 
ATOM   137  O O   . ASP A 1 18  ? -7.98293  64.74974 52.54566 1.000 33.06520 ? 18  ASP A O   1 
ATOM   138  C CB  . ASP A 1 18  ? -6.69862  66.81204 54.01116 1.000 38.98761 ? 18  ASP A CB  1 
ATOM   139  C CG  . ASP A 1 18  ? -5.61718  67.65777 53.39396 1.000 44.61452 ? 18  ASP A CG  1 
ATOM   140  O OD1 . ASP A 1 18  ? -4.90271  67.16600 52.49371 1.000 46.96621 ? 18  ASP A OD1 1 
ATOM   141  O OD2 . ASP A 1 18  ? -5.48424  68.82695 53.82101 1.000 48.44534 ? 18  ASP A OD2 1 
ATOM   142  N N   . VAL A 1 19  ? -5.99482  63.73573 52.32191 1.000 29.55373 ? 19  VAL A N   1 
ATOM   143  C CA  . VAL A 1 19  ? -6.43047  62.87145 51.22615 1.000 28.67621 ? 19  VAL A CA  1 
ATOM   144  C C   . VAL A 1 19  ? -5.71030  61.54228 51.26905 1.000 25.64369 ? 19  VAL A C   1 
ATOM   145  O O   . VAL A 1 19  ? -4.58398  61.45877 51.75441 1.000 26.38286 ? 19  VAL A O   1 
ATOM   146  C CB  . VAL A 1 19  ? -6.16893  63.48440 49.81682 1.000 25.78255 ? 19  VAL A CB  1 
ATOM   147  C CG1 . VAL A 1 19  ? -7.16981  64.57257 49.49435 1.000 28.46822 ? 19  VAL A CG1 1 
ATOM   148  C CG2 . VAL A 1 19  ? -4.73881  63.97920 49.70217 1.000 22.07994 ? 19  VAL A CG2 1 
ATOM   149  N N   . LYS A 1 20  ? -6.37180  60.51917 50.74009 1.000 25.65987 ? 20  LYS A N   1 
ATOM   150  C CA  . LYS A 1 20  ? -5.74670  59.24337 50.43874 1.000 27.10157 ? 20  LYS A CA  1 
ATOM   151  C C   . LYS A 1 20  ? -5.21613  59.31195 49.01708 1.000 24.63178 ? 20  LYS A C   1 
ATOM   152  O O   . LYS A 1 20  ? -5.94802  59.65704 48.09020 1.000 23.89054 ? 20  LYS A O   1 
ATOM   153  C CB  . LYS A 1 20  ? -6.74043  58.07765 50.57735 1.000 27.51898 ? 20  LYS A CB  1 
ATOM   154  C CG  . LYS A 1 20  ? -7.30204  57.88729 51.98145 1.000 34.55665 ? 20  LYS A CG  1 
ATOM   155  C CD  . LYS A 1 20  ? -8.47831  56.90321 52.00340 1.000 38.68737 ? 20  LYS A CD  1 
ATOM   156  C CE  . LYS A 1 20  ? -9.01899  56.67944 53.42255 1.000 42.14996 ? 20  LYS A CE  1 
ATOM   157  N NZ  . LYS A 1 20  ? -9.55059  57.93384 54.05359 1.000 43.96257 ? 20  LYS A NZ  1 
ATOM   158  N N   . ILE A 1 21  ? -3.94171  58.99468 48.84537 1.000 25.13549 ? 21  ILE A N   1 
ATOM   159  C CA  . ILE A 1 21  ? -3.35067  58.99173 47.52430 1.000 21.61443 ? 21  ILE A CA  1 
ATOM   160  C C   . ILE A 1 21  ? -3.03229  57.56831 47.07908 1.000 25.39195 ? 21  ILE A C   1 
ATOM   161  O O   . ILE A 1 21  ? -2.40025  56.80699 47.80742 1.000 22.82770 ? 21  ILE A O   1 
ATOM   162  C CB  . ILE A 1 21  ? -2.07207  59.84226 47.47587 1.000 21.97402 ? 21  ILE A CB  1 
ATOM   163  C CG1 . ILE A 1 21  ? -2.39551  61.32682 47.69230 1.000 21.23873 ? 21  ILE A CG1 1 
ATOM   164  C CG2 . ILE A 1 21  ? -1.33395  59.61683 46.17309 1.000 20.38385 ? 21  ILE A CG2 1 
ATOM   165  C CD1 . ILE A 1 21  ? -3.59398  61.84149 46.89921 1.000 20.72265 ? 21  ILE A CD1 1 
ATOM   166  N N   . HIS A 1 22  ? -3.49553  57.22642 45.87910 1.000 22.14952 ? 22  HIS A N   1 
ATOM   167  C CA  . HIS A 1 22  ? -3.16091  55.97734 45.21541 1.000 22.37543 ? 22  HIS A CA  1 
ATOM   168  C C   . HIS A 1 22  ? -1.92069  56.14051 44.33931 1.000 24.14021 ? 22  HIS A C   1 
ATOM   169  O O   . HIS A 1 22  ? -1.75224  57.16857 43.68990 1.000 23.17463 ? 22  HIS A O   1 
ATOM   170  C CB  . HIS A 1 22  ? -4.34118  55.50570 44.36512 1.000 21.33692 ? 22  HIS A CB  1 
ATOM   171  C CG  . HIS A 1 22  ? -3.97206  54.48912 43.33512 1.000 24.30140 ? 22  HIS A CG  1 
ATOM   172  N ND1 . HIS A 1 22  ? -3.64428  54.82686 42.03908 1.000 23.32975 ? 22  HIS A ND1 1 
ATOM   173  C CD2 . HIS A 1 22  ? -3.87585  53.14126 43.40718 1.000 24.44822 ? 22  HIS A CD2 1 
ATOM   174  C CE1 . HIS A 1 22  ? -3.37138  53.73150 41.35651 1.000 23.84031 ? 22  HIS A CE1 1 
ATOM   175  N NE2 . HIS A 1 22  ? -3.49659  52.69435 42.16600 1.000 26.70331 ? 22  HIS A NE2 1 
ATOM   176  N N   . TYR A 1 23  ? -1.05887  55.12801 44.31057 1.000 21.98874 ? 23  TYR A N   1 
ATOM   177  C CA  . TYR A 1 23  ? 0.10930   55.17387 43.44224 1.000 22.03866 ? 23  TYR A CA  1 
ATOM   178  C C   . TYR A 1 23  ? 0.58858   53.78514 43.05112 1.000 21.89125 ? 23  TYR A C   1 
ATOM   179  O O   . TYR A 1 23  ? 0.26024   52.78887 43.69182 1.000 23.65591 ? 23  TYR A O   1 
ATOM   180  C CB  . TYR A 1 23  ? 1.25641   55.94616 44.11453 1.000 21.91669 ? 23  TYR A CB  1 
ATOM   181  C CG  . TYR A 1 23  ? 1.81754   55.30245 45.37361 1.000 23.33668 ? 23  TYR A CG  1 
ATOM   182  C CD1 . TYR A 1 23  ? 1.29971   55.61259 46.62330 1.000 23.09133 ? 23  TYR A CD1 1 
ATOM   183  C CD2 . TYR A 1 23  ? 2.88349   54.40095 45.31042 1.000 23.41653 ? 23  TYR A CD2 1 
ATOM   184  C CE1 . TYR A 1 23  ? 1.81687   55.03174 47.78207 1.000 24.18152 ? 23  TYR A CE1 1 
ATOM   185  C CE2 . TYR A 1 23  ? 3.40585   53.82169 46.45660 1.000 19.89183 ? 23  TYR A CE2 1 
ATOM   186  C CZ  . TYR A 1 23  ? 2.86629   54.14129 47.68712 1.000 22.90651 ? 23  TYR A CZ  1 
ATOM   187  O OH  . TYR A 1 23  ? 3.36384   53.56496 48.83304 1.000 25.91444 ? 23  TYR A OH  1 
ATOM   188  N N   . VAL A 1 24  ? 1.37326   53.71390 41.99044 1.000 24.23206 ? 24  VAL A N   1 
ATOM   189  C CA  . VAL A 1 24  ? 2.11339   52.49117 41.71982 1.000 23.85279 ? 24  VAL A CA  1 
ATOM   190  C C   . VAL A 1 24  ? 3.58955   52.79672 41.93703 1.000 24.33346 ? 24  VAL A C   1 
ATOM   191  O O   . VAL A 1 24  ? 4.00982   53.96237 41.88940 1.000 21.82008 ? 24  VAL A O   1 
ATOM   192  C CB  . VAL A 1 24  ? 1.88055   51.94119 40.30076 1.000 23.92303 ? 24  VAL A CB  1 
ATOM   193  C CG1 . VAL A 1 24  ? 0.39463   51.77552 40.03055 1.000 22.15529 ? 24  VAL A CG1 1 
ATOM   194  C CG2 . VAL A 1 24  ? 2.53228   52.83513 39.26009 1.000 25.23140 ? 24  VAL A CG2 1 
ATOM   195  N N   . ARG A 1 25  ? 4.37050   51.75456 42.18164 1.000 22.35504 ? 25  ARG A N   1 
ATOM   196  C CA  . ARG A 1 25  ? 5.77579   51.92980 42.51960 1.000 24.88052 ? 25  ARG A CA  1 
ATOM   197  C C   . ARG A 1 25  ? 6.56833   50.72032 42.05390 1.000 26.73489 ? 25  ARG A C   1 
ATOM   198  O O   . ARG A 1 25  ? 6.10318   49.58854 42.12936 1.000 28.14057 ? 25  ARG A O   1 
ATOM   199  C CB  . ARG A 1 25  ? 5.95352   52.15326 44.02312 1.000 25.79202 ? 25  ARG A CB  1 
ATOM   200  C CG  . ARG A 1 25  ? 7.38788   52.44720 44.46784 1.000 26.59009 ? 25  ARG A CG  1 
ATOM   201  C CD  . ARG A 1 25  ? 7.45285   52.72728 45.96333 1.000 26.56993 ? 25  ARG A CD  1 
ATOM   202  N NE  . ARG A 1 25  ? 8.76144   53.22856 46.37323 1.000 26.03298 ? 25  ARG A NE  1 
ATOM   203  C CZ  . ARG A 1 25  ? 9.09563   53.54882 47.61914 1.000 26.59569 ? 25  ARG A CZ  1 
ATOM   204  N NH1 . ARG A 1 25  ? 8.22091   53.41340 48.61339 1.000 27.32816 ? 25  ARG A NH1 1 
ATOM   205  N NH2 . ARG A 1 25  ? 10.31548  53.99890 47.87272 1.000 25.72236 ? 25  ARG A NH2 1 
ATOM   206  N N   . GLU A 1 26  ? 7.77578   50.97333 41.57927 1.000 26.72449 ? 26  GLU A N   1 
ATOM   207  C CA  . GLU A 1 26  ? 8.52636   49.96554 40.87580 1.000 28.07335 ? 26  GLU A CA  1 
ATOM   208  C C   . GLU A 1 26  ? 9.96823   50.38935 40.74159 1.000 28.15788 ? 26  GLU A C   1 
ATOM   209  O O   . GLU A 1 26  ? 10.24613  51.54914 40.44828 1.000 25.62013 ? 26  GLU A O   1 
ATOM   210  C CB  . GLU A 1 26  ? 7.91639   49.76617 39.49479 1.000 33.21630 ? 26  GLU A CB  1 
ATOM   211  C CG  . GLU A 1 26  ? 8.06905   48.41948 38.92097 1.000 37.18927 ? 26  GLU A CG  1 
ATOM   212  C CD  . GLU A 1 26  ? 7.12757   48.22643 37.76137 1.000 37.24479 ? 26  GLU A CD  1 
ATOM   213  O OE1 . GLU A 1 26  ? 5.99589   47.76846 38.01337 1.000 36.75945 ? 26  GLU A OE1 1 
ATOM   214  O OE2 . GLU A 1 26  ? 7.51506   48.53581 36.61307 1.000 32.37588 ? 26  GLU A OE2 1 
ATOM   215  N N   . GLY A 1 27  ? 10.88813  49.45627 40.94720 1.000 31.33446 ? 27  GLY A N   1 
ATOM   216  C CA  . GLY A 1 27  ? 12.28009  49.69511 40.60878 1.000 29.50645 ? 27  GLY A CA  1 
ATOM   217  C C   . GLY A 1 27  ? 13.18250  49.94300 41.79421 1.000 29.44743 ? 27  GLY A C   1 
ATOM   218  O O   . GLY A 1 27  ? 12.75321  49.89668 42.93323 1.000 31.00527 ? 27  GLY A O   1 
ATOM   219  N N   . ALA A 1 28  ? 14.45056  50.20771 41.51771 1.000 28.29556 ? 28  ALA A N   1 
ATOM   220  C CA  . ALA A 1 28  ? 15.40044  50.49919 42.57274 1.000 30.96629 ? 28  ALA A CA  1 
ATOM   221  C C   . ALA A 1 28  ? 16.39461  51.57573 42.12943 1.000 30.63838 ? 28  ALA A C   1 
ATOM   222  O O   . ALA A 1 28  ? 16.77628  51.64407 40.95912 1.000 30.65139 ? 28  ALA A O   1 
ATOM   223  C CB  . ALA A 1 28  ? 16.13039  49.22167 42.98963 1.000 31.88543 ? 28  ALA A CB  1 
ATOM   224  N N   . GLY A 1 29  ? 16.80576  52.41345 43.07275 1.000 29.79674 ? 29  GLY A N   1 
ATOM   225  C CA  . GLY A 1 29  ? 17.72906  53.49133 42.78143 1.000 30.42348 ? 29  GLY A CA  1 
ATOM   226  C C   . GLY A 1 29  ? 17.24695  54.76858 43.42637 1.000 26.19770 ? 29  GLY A C   1 
ATOM   227  O O   . GLY A 1 29  ? 16.48410  54.72693 44.37772 1.000 31.04280 ? 29  GLY A O   1 
ATOM   228  N N   . PRO A 1 30  ? 17.70237  55.91823 42.91876 1.000 30.43820 ? 30  PRO A N   1 
ATOM   229  C CA  . PRO A 1 30  ? 17.14306  57.18563 43.37854 1.000 29.08513 ? 30  PRO A CA  1 
ATOM   230  C C   . PRO A 1 30  ? 15.65803  57.24096 43.04421 1.000 25.30443 ? 30  PRO A C   1 
ATOM   231  O O   . PRO A 1 30  ? 15.23859  56.62925 42.06794 1.000 26.62067 ? 30  PRO A O   1 
ATOM   232  C CB  . PRO A 1 30  ? 17.92894  58.22918 42.58594 1.000 31.46726 ? 30  PRO A CB  1 
ATOM   233  C CG  . PRO A 1 30  ? 19.15345  57.52644 42.13120 1.000 34.50054 ? 30  PRO A CG  1 
ATOM   234  C CD  . PRO A 1 30  ? 18.73972  56.11569 41.89738 1.000 31.19028 ? 30  PRO A CD  1 
ATOM   235  N N   . THR A 1 31  ? 14.87783  57.94972 43.84470 1.000 25.88172 ? 31  THR A N   1 
ATOM   236  C CA  . THR A 1 31  ? 13.44772  58.03490 43.59883 1.000 27.82122 ? 31  THR A CA  1 
ATOM   237  C C   . THR A 1 31  ? 13.12707  58.96863 42.43188 1.000 27.45681 ? 31  THR A C   1 
ATOM   238  O O   . THR A 1 31  ? 13.62877  60.09175 42.35368 1.000 27.53734 ? 31  THR A O   1 
ATOM   239  C CB  . THR A 1 31  ? 12.70208  58.50409 44.84421 1.000 26.69778 ? 31  THR A CB  1 
ATOM   240  O OG1 . THR A 1 31  ? 12.89828  57.55147 45.89370 1.000 30.77910 ? 31  THR A OG1 1 
ATOM   241  C CG2 . THR A 1 31  ? 11.21192  58.64762 44.55612 1.000 25.75299 ? 31  THR A CG2 1 
ATOM   242  N N   . LEU A 1 32  ? 12.29948  58.46880 41.52419 1.000 26.54796 ? 32  LEU A N   1 
ATOM   243  C CA  . LEU A 1 32  ? 11.79147  59.22971 40.38915 1.000 24.99103 ? 32  LEU A CA  1 
ATOM   244  C C   . LEU A 1 32  ? 10.27413  59.31864 40.49464 1.000 23.85896 ? 32  LEU A C   1 
ATOM   245  O O   . LEU A 1 32  ? 9.57486   58.30948 40.41456 1.000 22.41933 ? 32  LEU A O   1 
ATOM   246  C CB  . LEU A 1 32  ? 12.19810  58.57342 39.07420 1.000 20.45797 ? 32  LEU A CB  1 
ATOM   247  C CG  . LEU A 1 32  ? 11.70057  59.17932 37.76105 1.000 24.87173 ? 32  LEU A CG  1 
ATOM   248  C CD1 . LEU A 1 32  ? 12.17477  60.63364 37.57519 1.000 21.03560 ? 32  LEU A CD1 1 
ATOM   249  C CD2 . LEU A 1 32  ? 12.17598  58.29497 36.61701 1.000 25.79051 ? 32  LEU A CD2 1 
ATOM   250  N N   . LEU A 1 33  ? 9.77989   60.53369 40.69384 1.000 23.99922 ? 33  LEU A N   1 
ATOM   251  C CA  . LEU A 1 33  ? 8.36273   60.78379 40.87174 1.000 22.00823 ? 33  LEU A CA  1 
ATOM   252  C C   . LEU A 1 33  ? 7.76750   61.33783 39.57878 1.000 22.41789 ? 33  LEU A C   1 
ATOM   253  O O   . LEU A 1 33  ? 8.14280   62.42552 39.13849 1.000 25.97726 ? 33  LEU A O   1 
ATOM   254  C CB  . LEU A 1 33  ? 8.15384   61.75939 42.03670 1.000 20.03300 ? 33  LEU A CB  1 
ATOM   255  C CG  . LEU A 1 33  ? 6.71561   62.16197 42.35344 1.000 21.15788 ? 33  LEU A CG  1 
ATOM   256  C CD1 . LEU A 1 33  ? 5.94434   60.96544 42.88947 1.000 19.80236 ? 33  LEU A CD1 1 
ATOM   257  C CD2 . LEU A 1 33  ? 6.67433   63.33537 43.33158 1.000 20.62516 ? 33  LEU A CD2 1 
ATOM   258  N N   . LEU A 1 34  ? 6.85459   60.58795 38.97389 1.000 19.20316 ? 34  LEU A N   1 
ATOM   259  C CA  . LEU A 1 34  ? 6.24214   60.96318 37.69744 1.000 20.78274 ? 34  LEU A CA  1 
ATOM   260  C C   . LEU A 1 34  ? 4.79900   61.45160 37.89004 1.000 20.13914 ? 34  LEU A C   1 
ATOM   261  O O   . LEU A 1 34  ? 3.95596   60.72545 38.41656 1.000 23.00954 ? 34  LEU A O   1 
ATOM   262  C CB  . LEU A 1 34  ? 6.26947   59.77853 36.72309 1.000 19.10362 ? 34  LEU A CB  1 
ATOM   263  C CG  . LEU A 1 34  ? 7.62409   59.11627 36.43824 1.000 21.55588 ? 34  LEU A CG  1 
ATOM   264  C CD1 . LEU A 1 34  ? 7.43461   57.93044 35.49309 1.000 21.66273 ? 34  LEU A CD1 1 
ATOM   265  C CD2 . LEU A 1 34  ? 8.61970   60.11180 35.85379 1.000 21.03544 ? 34  LEU A CD2 1 
ATOM   266  N N   . LEU A 1 35  ? 4.51825   62.67409 37.45041 1.000 21.03775 ? 35  LEU A N   1 
ATOM   267  C CA  . LEU A 1 35  ? 3.24363   63.32536 37.75211 1.000 18.67041 ? 35  LEU A CA  1 
ATOM   268  C C   . LEU A 1 35  ? 2.40547   63.58807 36.48809 1.000 20.01861 ? 35  LEU A C   1 
ATOM   269  O O   . LEU A 1 35  ? 2.83640   64.28072 35.56472 1.000 20.08172 ? 35  LEU A O   1 
ATOM   270  C CB  . LEU A 1 35  ? 3.50542   64.61260 38.53210 1.000 18.06276 ? 35  LEU A CB  1 
ATOM   271  C CG  . LEU A 1 35  ? 4.23575   64.41959 39.86755 1.000 21.96159 ? 35  LEU A CG  1 
ATOM   272  C CD1 . LEU A 1 35  ? 4.60799   65.75064 40.49320 1.000 22.23293 ? 35  LEU A CD1 1 
ATOM   273  C CD2 . LEU A 1 35  ? 3.39054   63.59658 40.85031 1.000 20.15404 ? 35  LEU A CD2 1 
ATOM   274  N N   . HIS A 1 36  ? 1.20827   63.00100 36.45071 1.000 18.72052 ? 36  HIS A N   1 
ATOM   275  C CA  . HIS A 1 36  ? 0.36819   63.00993 35.24996 1.000 20.35587 ? 36  HIS A CA  1 
ATOM   276  C C   . HIS A 1 36  ? -0.42607  64.30659 35.08209 1.000 20.56826 ? 36  HIS A C   1 
ATOM   277  O O   . HIS A 1 36  ? -0.39827  65.18437 35.94495 1.000 20.75169 ? 36  HIS A O   1 
ATOM   278  C CB  . HIS A 1 36  ? -0.61207  61.82624 35.27887 1.000 20.69630 ? 36  HIS A CB  1 
ATOM   279  C CG  . HIS A 1 36  ? -1.70888  61.98638 36.28662 1.000 20.85780 ? 36  HIS A CG  1 
ATOM   280  N ND1 . HIS A 1 36  ? -2.87459  62.66542 36.01429 1.000 19.90650 ? 36  HIS A ND1 1 
ATOM   281  C CD2 . HIS A 1 36  ? -1.80416  61.57499 37.57460 1.000 19.89093 ? 36  HIS A CD2 1 
ATOM   282  C CE1 . HIS A 1 36  ? -3.64695  62.66061 37.08903 1.000 18.73607 ? 36  HIS A CE1 1 
ATOM   283  N NE2 . HIS A 1 36  ? -3.02030  62.00730 38.04923 1.000 19.48500 ? 36  HIS A NE2 1 
ATOM   284  N N   . GLY A 1 37  ? -1.16675  64.39859 33.98133 1.000 21.95976 ? 37  GLY A N   1 
ATOM   285  C CA  . GLY A 1 37  ? -2.08079  65.50789 33.77206 1.000 22.56505 ? 37  GLY A CA  1 
ATOM   286  C C   . GLY A 1 37  ? -3.51224  65.09691 33.45521 1.000 23.00704 ? 37  GLY A C   1 
ATOM   287  O O   . GLY A 1 37  ? -3.91431  63.95287 33.68622 1.000 23.42607 ? 37  GLY A O   1 
ATOM   288  N N   . TRP A 1 38  ? -4.27780  66.05041 32.92849 1.000 19.71663 ? 38  TRP A N   1 
ATOM   289  C CA  . TRP A 1 38  ? -5.64281  65.83275 32.45324 1.000 19.03625 ? 38  TRP A CA  1 
ATOM   290  C C   . TRP A 1 38  ? -5.60909  65.66044 30.92515 1.000 20.54487 ? 38  TRP A C   1 
ATOM   291  O O   . TRP A 1 38  ? -4.91563  66.40696 30.24541 1.000 24.31933 ? 38  TRP A O   1 
ATOM   292  C CB  . TRP A 1 38  ? -6.54406  67.02446 32.85226 1.000 18.86353 ? 38  TRP A CB  1 
ATOM   293  C CG  . TRP A 1 38  ? -8.00774  66.87936 32.44840 1.000 18.14722 ? 38  TRP A CG  1 
ATOM   294  C CD1 . TRP A 1 38  ? -9.02847  66.43881 33.23676 1.000 18.15205 ? 38  TRP A CD1 1 
ATOM   295  C CD2 . TRP A 1 38  ? -8.58749  67.16260 31.16390 1.000 16.37655 ? 38  TRP A CD2 1 
ATOM   296  N NE1 . TRP A 1 38  ? -10.20750 66.43336 32.53173 1.000 19.02742 ? 38  TRP A NE1 1 
ATOM   297  C CE2 . TRP A 1 38  ? -9.96093  66.87103 31.25406 1.000 18.19801 ? 38  TRP A CE2 1 
ATOM   298  C CE3 . TRP A 1 38  ? -8.07571  67.62900 29.94582 1.000 19.67987 ? 38  TRP A CE3 1 
ATOM   299  C CZ2 . TRP A 1 38  ? -10.83058 67.02571 30.17386 1.000 18.62407 ? 38  TRP A CZ2 1 
ATOM   300  C CZ3 . TRP A 1 38  ? -8.94646  67.79158 28.87179 1.000 18.13421 ? 38  TRP A CZ3 1 
ATOM   301  C CH2 . TRP A 1 38  ? -10.30603 67.48932 28.99696 1.000 17.79119 ? 38  TRP A CH2 1 
ATOM   302  N N   . PRO A 1 39  ? -6.39052  64.72046 30.36885 1.000 21.45626 ? 39  PRO A N   1 
ATOM   303  C CA  . PRO A 1 39  ? -7.41161  63.87146 30.99093 1.000 20.88242 ? 39  PRO A CA  1 
ATOM   304  C C   . PRO A 1 39  ? -6.94827  62.46819 31.37718 1.000 23.79884 ? 39  PRO A C   1 
ATOM   305  O O   . PRO A 1 39  ? -7.78168  61.56237 31.45749 1.000 29.74833 ? 39  PRO A O   1 
ATOM   306  C CB  . PRO A 1 39  ? -8.47242  63.77550 29.89810 1.000 21.05737 ? 39  PRO A CB  1 
ATOM   307  C CG  . PRO A 1 39  ? -7.66748  63.72753 28.64514 1.000 23.08307 ? 39  PRO A CG  1 
ATOM   308  C CD  . PRO A 1 39  ? -6.43876  64.61355 28.89854 1.000 21.72837 ? 39  PRO A CD  1 
ATOM   309  N N   . GLY A 1 40  ? -5.66013  62.28610 31.62240 1.000 24.62987 ? 40  GLY A N   1 
ATOM   310  C CA  . GLY A 1 40  ? -5.15723  60.98235 32.01839 1.000 23.95943 ? 40  GLY A CA  1 
ATOM   311  C C   . GLY A 1 40  ? -5.19466  60.72744 33.51728 1.000 23.74233 ? 40  GLY A C   1 
ATOM   312  O O   . GLY A 1 40  ? -6.05815  61.24000 34.23142 1.000 25.33145 ? 40  GLY A O   1 
ATOM   313  N N   . PHE A 1 41  ? -4.24632  59.90818 33.96801 1.000 22.91851 ? 41  PHE A N   1 
ATOM   314  C CA  . PHE A 1 41  ? -4.06916  59.51558 35.36268 1.000 22.54708 ? 41  PHE A CA  1 
ATOM   315  C C   . PHE A 1 41  ? -2.71760  58.80556 35.40100 1.000 23.12421 ? 41  PHE A C   1 
ATOM   316  O O   . PHE A 1 41  ? -1.97008  58.91060 34.43833 1.000 21.53367 ? 41  PHE A O   1 
ATOM   317  C CB  . PHE A 1 41  ? -5.23542  58.64516 35.89140 1.000 20.92515 ? 41  PHE A CB  1 
ATOM   318  C CG  . PHE A 1 41  ? -5.41753  57.29900 35.20609 1.000 22.63294 ? 41  PHE A CG  1 
ATOM   319  C CD1 . PHE A 1 41  ? -5.72135  57.20564 33.85898 1.000 20.69766 ? 41  PHE A CD1 1 
ATOM   320  C CD2 . PHE A 1 41  ? -5.38133  56.12261 35.95285 1.000 21.34747 ? 41  PHE A CD2 1 
ATOM   321  C CE1 . PHE A 1 41  ? -5.92159  55.96165 33.25468 1.000 23.06985 ? 41  PHE A CE1 1 
ATOM   322  C CE2 . PHE A 1 41  ? -5.57977  54.88570 35.35636 1.000 20.16049 ? 41  PHE A CE2 1 
ATOM   323  C CZ  . PHE A 1 41  ? -5.86010  54.80311 34.00994 1.000 20.56967 ? 41  PHE A CZ  1 
ATOM   324  N N   . TRP A 1 42  ? -2.38826  58.10516 36.48384 1.000 21.78836 ? 42  TRP A N   1 
ATOM   325  C CA  . TRP A 1 42  ? -1.04690  57.52546 36.62001 1.000 21.16917 ? 42  TRP A CA  1 
ATOM   326  C C   . TRP A 1 42  ? -0.65796  56.66189 35.41441 1.000 23.11388 ? 42  TRP A C   1 
ATOM   327  O O   . TRP A 1 42  ? 0.50842   56.63303 35.00846 1.000 23.85777 ? 42  TRP A O   1 
ATOM   328  C CB  . TRP A 1 42  ? -0.93779  56.68335 37.90747 1.000 21.74741 ? 42  TRP A CB  1 
ATOM   329  C CG  . TRP A 1 42  ? -1.63227  55.34848 37.78227 1.000 22.59184 ? 42  TRP A CG  1 
ATOM   330  C CD1 . TRP A 1 42  ? -2.91358  55.06453 38.13093 1.000 20.18001 ? 42  TRP A CD1 1 
ATOM   331  C CD2 . TRP A 1 42  ? -1.08830  54.14045 37.22942 1.000 22.71360 ? 42  TRP A CD2 1 
ATOM   332  N NE1 . TRP A 1 42  ? -3.20402  53.75324 37.84795 1.000 20.97483 ? 42  TRP A NE1 1 
ATOM   333  C CE2 . TRP A 1 42  ? -2.10234  53.16385 37.28761 1.000 22.43265 ? 42  TRP A CE2 1 
ATOM   334  C CE3 . TRP A 1 42  ? 0.15611   53.79106 36.69262 1.000 21.23853 ? 42  TRP A CE3 1 
ATOM   335  C CZ2 . TRP A 1 42  ? -1.91241  51.86005 36.83424 1.000 24.07999 ? 42  TRP A CZ2 1 
ATOM   336  C CZ3 . TRP A 1 42  ? 0.34370   52.49914 36.23835 1.000 21.49749 ? 42  TRP A CZ3 1 
ATOM   337  C CH2 . TRP A 1 42  ? -0.68315  51.54671 36.31265 1.000 23.69232 ? 42  TRP A CH2 1 
ATOM   338  N N   . TRP A 1 43  ? -1.63650  55.96910 34.83466 1.000 22.73682 ? 43  TRP A N   1 
ATOM   339  C CA  . TRP A 1 43  ? -1.35426  54.96970 33.79825 1.000 22.05636 ? 43  TRP A CA  1 
ATOM   340  C C   . TRP A 1 43  ? -0.82520  55.54709 32.48527 1.000 22.98472 ? 43  TRP A C   1 
ATOM   341  O O   . TRP A 1 43  ? -0.34020  54.80583 31.64631 1.000 24.50321 ? 43  TRP A O   1 
ATOM   342  C CB  . TRP A 1 43  ? -2.60644  54.13471 33.51206 1.000 22.73091 ? 43  TRP A CB  1 
ATOM   343  C CG  . TRP A 1 43  ? -2.37437  52.97210 32.57870 1.000 23.00172 ? 43  TRP A CG  1 
ATOM   344  C CD1 . TRP A 1 43  ? -1.68471  51.81688 32.85186 1.000 24.19993 ? 43  TRP A CD1 1 
ATOM   345  C CD2 . TRP A 1 43  ? -2.84021  52.84874 31.22716 1.000 24.37205 ? 43  TRP A CD2 1 
ATOM   346  N NE1 . TRP A 1 43  ? -1.68892  50.98933 31.74918 1.000 23.56802 ? 43  TRP A NE1 1 
ATOM   347  C CE2 . TRP A 1 43  ? -2.39143  51.59926 30.74009 1.000 25.06153 ? 43  TRP A CE2 1 
ATOM   348  C CE3 . TRP A 1 43  ? -3.58249  53.67742 30.37685 1.000 24.15006 ? 43  TRP A CE3 1 
ATOM   349  C CZ2 . TRP A 1 43  ? -2.66287  51.16116 29.44450 1.000 26.13083 ? 43  TRP A CZ2 1 
ATOM   350  C CZ3 . TRP A 1 43  ? -3.85294  53.23512 29.08808 1.000 26.08565 ? 43  TRP A CZ3 1 
ATOM   351  C CH2 . TRP A 1 43  ? -3.39666  51.98557 28.63799 1.000 26.78453 ? 43  TRP A CH2 1 
ATOM   352  N N   . GLU A 1 44  ? -0.89303  56.86183 32.30087 1.000 26.04248 ? 44  GLU A N   1 
ATOM   353  C CA  . GLU A 1 44  ? -0.37064  57.43548 31.06067 1.000 24.18687 ? 44  GLU A CA  1 
ATOM   354  C C   . GLU A 1 44  ? 1.14352   57.24131 30.99141 1.000 25.16248 ? 44  GLU A C   1 
ATOM   355  O O   . GLU A 1 44  ? 1.72598   57.24390 29.91451 1.000 24.19120 ? 44  GLU A O   1 
ATOM   356  C CB  . GLU A 1 44  ? -0.74849  58.91842 30.93171 1.000 24.64932 ? 44  GLU A CB  1 
ATOM   357  C CG  . GLU A 1 44  ? -0.09387  59.87499 31.91624 1.000 23.39898 ? 44  GLU A CG  1 
ATOM   358  C CD  . GLU A 1 44  ? -0.64945  61.28395 31.77008 1.000 27.26058 ? 44  GLU A CD  1 
ATOM   359  O OE1 . GLU A 1 44  ? 0.07633   62.25693 32.05052 1.000 25.98994 ? 44  GLU A OE1 1 
ATOM   360  O OE2 . GLU A 1 44  ? -1.82498  61.41470 31.37506 1.000 30.96709 ? 44  GLU A OE2 1 
ATOM   361  N N   . TRP A 1 45  ? 1.76416   57.03638 32.15188 1.000 22.56364 ? 45  TRP A N   1 
ATOM   362  C CA  . TRP A 1 45  ? 3.19572   56.76755 32.24111 1.000 20.81964 ? 45  TRP A CA  1 
ATOM   363  C C   . TRP A 1 45  ? 3.55287   55.29565 32.02550 1.000 22.36294 ? 45  TRP A C   1 
ATOM   364  O O   . TRP A 1 45  ? 4.71661   54.92746 32.14082 1.000 24.56516 ? 45  TRP A O   1 
ATOM   365  C CB  . TRP A 1 45  ? 3.73730   57.20507 33.61293 1.000 20.60101 ? 45  TRP A CB  1 
ATOM   366  C CG  . TRP A 1 45  ? 3.61137   58.67933 33.90644 1.000 21.80072 ? 45  TRP A CG  1 
ATOM   367  C CD1 . TRP A 1 45  ? 2.66141   59.28945 34.67840 1.000 20.43384 ? 45  TRP A CD1 1 
ATOM   368  C CD2 . TRP A 1 45  ? 4.47974   59.72104 33.44515 1.000 21.27495 ? 45  TRP A CD2 1 
ATOM   369  N NE1 . TRP A 1 45  ? 2.88923   60.64960 34.72496 1.000 21.16560 ? 45  TRP A NE1 1 
ATOM   370  C CE2 . TRP A 1 45  ? 3.99674   60.93717 33.97510 1.000 20.99585 ? 45  TRP A CE2 1 
ATOM   371  C CE3 . TRP A 1 45  ? 5.61365   59.74554 32.62504 1.000 19.04670 ? 45  TRP A CE3 1 
ATOM   372  C CZ2 . TRP A 1 45  ? 4.61076   62.15945 33.71459 1.000 20.89798 ? 45  TRP A CZ2 1 
ATOM   373  C CZ3 . TRP A 1 45  ? 6.22379   60.95610 32.37582 1.000 18.83702 ? 45  TRP A CZ3 1 
ATOM   374  C CH2 . TRP A 1 45  ? 5.71982   62.14670 32.91630 1.000 23.75485 ? 45  TRP A CH2 1 
ATOM   375  N N   . SER A 1 46  ? 2.56441   54.45738 31.72103 1.000 24.03046 ? 46  SER A N   1 
ATOM   376  C CA  . SER A 1 46  ? 2.76290   53.00074 31.75824 1.000 25.35044 ? 46  SER A CA  1 
ATOM   377  C C   . SER A 1 46  ? 3.82253   52.46277 30.79004 1.000 27.18619 ? 46  SER A C   1 
ATOM   378  O O   . SER A 1 46  ? 4.43068   51.42866 31.05662 1.000 26.94270 ? 46  SER A O   1 
ATOM   379  C CB  . SER A 1 46  ? 1.44203   52.27620 31.49727 1.000 24.84384 ? 46  SER A CB  1 
ATOM   380  O OG  . SER A 1 46  ? 0.93256   52.57700 30.21493 1.000 27.54222 ? 46  SER A OG  1 
ATOM   381  N N   . LYS A 1 47  ? 4.05311   53.16356 29.68438 1.000 26.19774 ? 47  LYS A N   1 
ATOM   382  C CA  . LYS A 1 47  ? 5.06999   52.74677 28.72184 1.000 23.86252 ? 47  LYS A CA  1 
ATOM   383  C C   . LYS A 1 47  ? 6.49570   53.00292 29.21320 1.000 24.30333 ? 47  LYS A C   1 
ATOM   384  O O   . LYS A 1 47  ? 7.41985   52.35707 28.75092 1.000 26.95095 ? 47  LYS A O   1 
ATOM   385  C CB  . LYS A 1 47  ? 4.86607   53.45006 27.36992 1.000 28.48311 ? 47  LYS A CB  1 
ATOM   386  C CG  . LYS A 1 47  ? 3.53883   53.14958 26.67830 1.000 31.73306 ? 47  LYS A CG  1 
ATOM   387  C CD  . LYS A 1 47  ? 3.44227   53.84218 25.30727 1.000 31.48924 ? 47  LYS A CD  1 
ATOM   388  C CE  . LYS A 1 47  ? 1.98795   53.93345 24.82928 1.000 35.26431 ? 47  LYS A CE  1 
ATOM   389  N NZ  . LYS A 1 47  ? 1.84241   54.54938 23.47484 1.000 27.35178 ? 47  LYS A NZ  1 
ATOM   390  N N   . VAL A 1 48  ? 6.69211   53.94031 30.13679 1.000 25.21967 ? 48  VAL A N   1 
ATOM   391  C CA  . VAL A 1 48  ? 8.05970   54.29465 30.51593 1.000 21.95359 ? 48  VAL A CA  1 
ATOM   392  C C   . VAL A 1 48  ? 8.44237   53.80597 31.91046 1.000 24.33591 ? 48  VAL A C   1 
ATOM   393  O O   . VAL A 1 48  ? 9.62140   53.76860 32.24154 1.000 26.44933 ? 48  VAL A O   1 
ATOM   394  C CB  . VAL A 1 48  ? 8.30909   55.83044 30.42706 1.000 22.29699 ? 48  VAL A CB  1 
ATOM   395  C CG1 . VAL A 1 48  ? 8.00344   56.34004 29.02232 1.000 22.25012 ? 48  VAL A CG1 1 
ATOM   396  C CG2 . VAL A 1 48  ? 7.50081   56.60304 31.45391 1.000 21.34930 ? 48  VAL A CG2 1 
ATOM   397  N N   . ILE A 1 49  ? 7.45522   53.42136 32.71468 1.000 22.76426 ? 49  ILE A N   1 
ATOM   398  C CA  . ILE A 1 49  ? 7.71292   53.02431 34.09927 1.000 24.24713 ? 49  ILE A CA  1 
ATOM   399  C C   . ILE A 1 49  ? 8.68620   51.85262 34.16399 1.000 26.80793 ? 49  ILE A C   1 
ATOM   400  O O   . ILE A 1 49  ? 9.68122   51.91699 34.87298 1.000 27.33463 ? 49  ILE A O   1 
ATOM   401  C CB  . ILE A 1 49  ? 6.40519   52.65509 34.85256 1.000 25.80069 ? 49  ILE A CB  1 
ATOM   402  C CG1 . ILE A 1 49  ? 5.56741   53.91270 35.09549 1.000 23.74403 ? 49  ILE A CG1 1 
ATOM   403  C CG2 . ILE A 1 49  ? 6.72806   51.98192 36.20260 1.000 23.78210 ? 49  ILE A CG2 1 
ATOM   404  C CD1 . ILE A 1 49  ? 4.14562   53.63704 35.53991 1.000 21.87272 ? 49  ILE A CD1 1 
ATOM   405  N N   . GLY A 1 50  ? 8.40047   50.80038 33.40458 1.000 27.60386 ? 50  GLY A N   1 
ATOM   406  C CA  . GLY A 1 50  ? 9.24180   49.61498 33.37747 1.000 27.11279 ? 50  GLY A CA  1 
ATOM   407  C C   . GLY A 1 50  ? 10.68566  49.93387 33.03705 1.000 29.25287 ? 50  GLY A C   1 
ATOM   408  O O   . GLY A 1 50  ? 11.57059  49.65742 33.83093 1.000 30.44197 ? 50  GLY A O   1 
ATOM   409  N N   . PRO A 1 51  ? 10.92854  50.52037 31.85219 1.000 29.71124 ? 51  PRO A N   1 
ATOM   410  C CA  . PRO A 1 51  ? 12.29358  50.89498 31.46375 1.000 30.68508 ? 51  PRO A CA  1 
ATOM   411  C C   . PRO A 1 51  ? 12.99401  51.79456 32.47662 1.000 29.49140 ? 51  PRO A C   1 
ATOM   412  O O   . PRO A 1 51  ? 14.16172  51.57576 32.76889 1.000 32.61329 ? 51  PRO A O   1 
ATOM   413  C CB  . PRO A 1 51  ? 12.08538  51.62513 30.13680 1.000 28.86756 ? 51  PRO A CB  1 
ATOM   414  C CG  . PRO A 1 51  ? 10.88530  50.95313 29.54662 1.000 27.96489 ? 51  PRO A CG  1 
ATOM   415  C CD  . PRO A 1 51  ? 9.98369   50.64824 30.72641 1.000 27.05612 ? 51  PRO A CD  1 
ATOM   416  N N   . LEU A 1 52  ? 12.29146  52.77933 33.01782 1.000 27.66820 ? 52  LEU A N   1 
ATOM   417  C CA  . LEU A 1 52  ? 12.90583  53.69132 33.97142 1.000 27.27155 ? 52  LEU A CA  1 
ATOM   418  C C   . LEU A 1 52  ? 13.22250  53.01065 35.30717 1.000 28.26941 ? 52  LEU A C   1 
ATOM   419  O O   . LEU A 1 52  ? 14.15055  53.41227 35.99920 1.000 26.22618 ? 52  LEU A O   1 
ATOM   420  C CB  . LEU A 1 52  ? 12.00279  54.90847 34.18436 1.000 27.09704 ? 52  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 52  ? 12.01382  55.90210 33.01022 1.000 25.99431 ? 52  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 52  ? 10.86542  56.88826 33.10913 1.000 20.29812 ? 52  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 52  ? 13.35801  56.63914 32.93806 1.000 26.54517 ? 52  LEU A CD2 1 
ATOM   424  N N   . SER A 1 53  ? 12.46075  51.97311 35.65421 1.000 27.92540 ? 53  SER A N   1 
ATOM   425  C CA  . SER A 1 53  ? 12.64195  51.26626 36.92548 1.000 28.49301 ? 53  SER A CA  1 
ATOM   426  C C   . SER A 1 53  ? 13.95824  50.49211 36.97276 1.000 28.73516 ? 53  SER A C   1 
ATOM   427  O O   . SER A 1 53  ? 14.36898  50.04255 38.02403 1.000 30.17095 ? 53  SER A O   1 
ATOM   428  C CB  . SER A 1 53  ? 11.48408  50.30391 37.17341 1.000 26.17413 ? 53  SER A CB  1 
ATOM   429  O OG  . SER A 1 53  ? 11.54361  49.21339 36.27479 1.000 30.47180 ? 53  SER A OG  1 
ATOM   430  N N   . GLU A 1 54  ? 14.60104  50.32528 35.82224 1.000 32.44892 ? 54  GLU A N   1 
ATOM   431  C CA  . GLU A 1 54  ? 15.92694  49.72021 35.76068 1.000 32.60488 ? 54  GLU A CA  1 
ATOM   432  C C   . GLU A 1 54  ? 16.99126  50.61321 36.40229 1.000 33.12602 ? 54  GLU A C   1 
ATOM   433  O O   . GLU A 1 54  ? 18.07291  50.15025 36.74300 1.000 34.53212 ? 54  GLU A O   1 
ATOM   434  C CB  . GLU A 1 54  ? 16.31476  49.42796 34.30704 1.000 34.36742 ? 54  GLU A CB  1 
ATOM   435  C CG  . GLU A 1 54  ? 15.34380  48.54320 33.55857 1.000 38.37664 ? 54  GLU A CG  1 
ATOM   436  C CD  . GLU A 1 54  ? 15.61433  48.52280 32.05940 1.000 48.29458 ? 54  GLU A CD  1 
ATOM   437  O OE1 . GLU A 1 54  ? 14.94856  47.74147 31.34308 1.000 46.44670 ? 54  GLU A OE1 1 
ATOM   438  O OE2 . GLU A 1 54  ? 16.48533  49.29654 31.59596 1.000 49.09038 ? 54  GLU A OE2 1 
ATOM   439  N N   . ARG A 1 55  ? 16.69069  51.89613 36.56118 1.000 31.44394 ? 55  ARG A N   1 
ATOM   440  C CA  . ARG A 1 55  ? 17.67246  52.83525 37.09493 1.000 29.85375 ? 55  ARG A CA  1 
ATOM   441  C C   . ARG A 1 55  ? 17.13299  53.62770 38.27844 1.000 32.05037 ? 55  ARG A C   1 
ATOM   442  O O   . ARG A 1 55  ? 17.89997  54.23951 39.02125 1.000 33.46234 ? 55  ARG A O   1 
ATOM   443  C CB  . ARG A 1 55  ? 18.13659  53.80886 35.99853 1.000 37.07822 ? 55  ARG A CB  1 
ATOM   444  C CG  . ARG A 1 55  ? 19.01602  53.19603 34.91414 1.000 42.25904 ? 55  ARG A CG  1 
ATOM   445  C CD  . ARG A 1 55  ? 20.40911  52.85113 35.45277 1.000 50.64092 ? 55  ARG A CD  1 
ATOM   446  N NE  . ARG A 1 55  ? 21.29147  52.29783 34.42599 1.000 60.77316 ? 55  ARG A NE  1 
ATOM   447  C CZ  . ARG A 1 55  ? 21.45433  50.99659 34.19306 1.000 61.37418 ? 55  ARG A CZ  1 
ATOM   448  N NH1 . ARG A 1 55  ? 20.79438  50.09864 34.91250 1.000 52.51747 ? 55  ARG A NH1 1 
ATOM   449  N NH2 . ARG A 1 55  ? 22.27829  50.59067 33.23546 1.000 62.62618 ? 55  ARG A NH2 1 
ATOM   450  N N   . PHE A 1 56  ? 15.81411  53.63163 38.44685 1.000 28.44295 ? 56  PHE A N   1 
ATOM   451  C CA  . PHE A 1 56  ? 15.18687  54.43785 39.48495 1.000 25.76445 ? 56  PHE A CA  1 
ATOM   452  C C   . PHE A 1 56  ? 14.13787  53.67392 40.28239 1.000 27.02140 ? 56  PHE A C   1 
ATOM   453  O O   . PHE A 1 56  ? 13.53855  52.72466 39.79415 1.000 28.34436 ? 56  PHE A O   1 
ATOM   454  C CB  . PHE A 1 56  ? 14.49803  55.68083 38.88313 1.000 28.26455 ? 56  PHE A CB  1 
ATOM   455  C CG  . PHE A 1 56  ? 15.40732  56.58038 38.10410 1.000 25.20423 ? 56  PHE A CG  1 
ATOM   456  C CD1 . PHE A 1 56  ? 16.09572  57.60340 38.73217 1.000 27.40206 ? 56  PHE A CD1 1 
ATOM   457  C CD2 . PHE A 1 56  ? 15.54633  56.42222 36.74025 1.000 26.38825 ? 56  PHE A CD2 1 
ATOM   458  C CE1 . PHE A 1 56  ? 16.93152  58.43793 38.01889 1.000 29.86171 ? 56  PHE A CE1 1 
ATOM   459  C CE2 . PHE A 1 56  ? 16.37745  57.26338 36.01224 1.000 32.66529 ? 56  PHE A CE2 1 
ATOM   460  C CZ  . PHE A 1 56  ? 17.07451  58.27178 36.65761 1.000 30.83433 ? 56  PHE A CZ  1 
ATOM   461  N N   . ASP A 1 57  ? 13.90758  54.14058 41.50274 1.000 26.97373 ? 57  ASP A N   1 
ATOM   462  C CA  . ASP A 1 57  ? 12.71768  53.81929 42.27451 1.000 26.46027 ? 57  ASP A CA  1 
ATOM   463  C C   . ASP A 1 57  ? 11.56926  54.70792 41.76253 1.000 23.39279 ? 57  ASP A C   1 
ATOM   464  O O   . ASP A 1 57  ? 11.37250  55.82884 42.22417 1.000 25.02547 ? 57  ASP A O   1 
ATOM   465  C CB  . ASP A 1 57  ? 13.00448  54.02826 43.77163 1.000 25.52270 ? 57  ASP A CB  1 
ATOM   466  C CG  . ASP A 1 57  ? 11.74926  54.16225 44.62409 1.000 26.71599 ? 57  ASP A CG  1 
ATOM   467  O OD1 . ASP A 1 57  ? 10.73206  53.49405 44.34767 1.000 27.37295 ? 57  ASP A OD1 1 
ATOM   468  O OD2 . ASP A 1 57  ? 11.79411  54.94316 45.59803 1.000 28.61260 ? 57  ASP A OD2 1 
ATOM   469  N N   . VAL A 1 58  ? 10.83228  54.20083 40.78490 1.000 24.21852 ? 58  VAL A N   1 
ATOM   470  C CA  . VAL A 1 58  ? 9.79456   54.98573 40.12124 1.000 23.40465 ? 58  VAL A CA  1 
ATOM   471  C C   . VAL A 1 58  ? 8.49860   54.98794 40.91897 1.000 23.95491 ? 58  VAL A C   1 
ATOM   472  O O   . VAL A 1 58  ? 7.94742   53.93195 41.22963 1.000 25.97256 ? 58  VAL A O   1 
ATOM   473  C CB  . VAL A 1 58  ? 9.52183   54.45782 38.70834 1.000 24.10367 ? 58  VAL A CB  1 
ATOM   474  C CG1 . VAL A 1 58  ? 8.54507   55.36498 37.97335 1.000 22.59377 ? 58  VAL A CG1 1 
ATOM   475  C CG2 . VAL A 1 58  ? 10.82198  54.34906 37.93588 1.000 24.78427 ? 58  VAL A CG2 1 
ATOM   476  N N   . ILE A 1 59  ? 8.02939   56.18181 41.26811 1.000 23.72569 ? 59  ILE A N   1 
ATOM   477  C CA  . ILE A 1 59  ? 6.77309   56.34820 41.99713 1.000 20.70931 ? 59  ILE A CA  1 
ATOM   478  C C   . ILE A 1 59  ? 5.78978   57.16076 41.16024 1.000 21.95609 ? 59  ILE A C   1 
ATOM   479  O O   . ILE A 1 59  ? 6.10748   58.26006 40.72780 1.000 21.92118 ? 59  ILE A O   1 
ATOM   480  C CB  . ILE A 1 59  ? 6.99939   57.05278 43.35223 1.000 24.56491 ? 59  ILE A CB  1 
ATOM   481  C CG1 . ILE A 1 59  ? 7.97820   56.25245 44.21545 1.000 24.87218 ? 59  ILE A CG1 1 
ATOM   482  C CG2 . ILE A 1 59  ? 5.67592   57.27346 44.07690 1.000 23.30852 ? 59  ILE A CG2 1 
ATOM   483  C CD1 . ILE A 1 59  ? 8.26041   56.88804 45.53974 1.000 23.45527 ? 59  ILE A CD1 1 
ATOM   484  N N   . VAL A 1 60  ? 4.59687   56.62392 40.92843 1.000 22.68509 ? 60  VAL A N   1 
ATOM   485  C CA  . VAL A 1 60  ? 3.63867   57.27544 40.04165 1.000 20.36914 ? 60  VAL A CA  1 
ATOM   486  C C   . VAL A 1 60  ? 2.26055   57.35827 40.68710 1.000 22.41532 ? 60  VAL A C   1 
ATOM   487  O O   . VAL A 1 60  ? 1.50201   56.38643 40.64924 1.000 21.47367 ? 60  VAL A O   1 
ATOM   488  C CB  . VAL A 1 60  ? 3.50866   56.52616 38.69310 1.000 22.27811 ? 60  VAL A CB  1 
ATOM   489  C CG1 . VAL A 1 60  ? 2.75326   57.37542 37.67256 1.000 21.70933 ? 60  VAL A CG1 1 
ATOM   490  C CG2 . VAL A 1 60  ? 4.86822   56.14039 38.15416 1.000 21.60153 ? 60  VAL A CG2 1 
ATOM   491  N N   . PRO A 1 61  ? 1.93598   58.51365 41.28812 1.000 21.55070 ? 61  PRO A N   1 
ATOM   492  C CA  . PRO A 1 61  ? 0.64711   58.67556 41.96039 1.000 20.75742 ? 61  PRO A CA  1 
ATOM   493  C C   . PRO A 1 61  ? -0.44604  59.22210 41.05639 1.000 23.94363 ? 61  PRO A C   1 
ATOM   494  O O   . PRO A 1 61  ? -0.16473  59.85981 40.03318 1.000 25.18005 ? 61  PRO A O   1 
ATOM   495  C CB  . PRO A 1 61  ? 0.96508   59.68398 43.05520 1.000 19.24909 ? 61  PRO A CB  1 
ATOM   496  C CG  . PRO A 1 61  ? 1.97127   60.59546 42.39079 1.000 20.53067 ? 61  PRO A CG  1 
ATOM   497  C CD  . PRO A 1 61  ? 2.79070   59.70067 41.47244 1.000 19.64424 ? 61  PRO A CD  1 
ATOM   498  N N   . ASP A 1 62  ? -1.68834  58.95771 41.44185 1.000 20.29015 ? 62  ASP A N   1 
ATOM   499  C CA  . ASP A 1 62  ? -2.82061  59.70672 40.94228 1.000 21.43473 ? 62  ASP A CA  1 
ATOM   500  C C   . ASP A 1 62  ? -2.87850  60.99527 41.73123 1.000 21.57839 ? 62  ASP A C   1 
ATOM   501  O O   . ASP A 1 62  ? -2.78195  60.97373 42.96349 1.000 23.05983 ? 62  ASP A O   1 
ATOM   502  C CB  . ASP A 1 62  ? -4.13618  58.94140 41.10558 1.000 18.25553 ? 62  ASP A CB  1 
ATOM   503  C CG  . ASP A 1 62  ? -4.31177  57.85179 40.08078 1.000 23.13630 ? 62  ASP A CG  1 
ATOM   504  O OD1 . ASP A 1 62  ? -3.95443  58.06830 38.89410 1.000 23.42362 ? 62  ASP A OD1 1 
ATOM   505  O OD2 . ASP A 1 62  ? -4.81450  56.77336 40.46472 1.000 21.86437 ? 62  ASP A OD2 1 
ATOM   506  N N   . LEU A 1 63  ? -3.04674  62.11491 41.03915 1.000 20.25854 ? 63  LEU A N   1 
ATOM   507  C CA  . LEU A 1 63  ? -3.28230  63.37848 41.73183 1.000 20.61077 ? 63  LEU A CA  1 
ATOM   508  C C   . LEU A 1 63  ? -4.59506  63.29578 42.51039 1.000 21.11019 ? 63  LEU A C   1 
ATOM   509  O O   . LEU A 1 63  ? -5.49097  62.55866 42.11146 1.000 20.42647 ? 63  LEU A O   1 
ATOM   510  C CB  . LEU A 1 63  ? -3.33062  64.54347 40.74181 1.000 20.84563 ? 63  LEU A CB  1 
ATOM   511  C CG  . LEU A 1 63  ? -2.12035  64.79747 39.84120 1.000 23.22677 ? 63  LEU A CG  1 
ATOM   512  C CD1 . LEU A 1 63  ? -2.36571  66.04842 38.99304 1.000 17.67518 ? 63  LEU A CD1 1 
ATOM   513  C CD2 . LEU A 1 63  ? -0.85167  64.93858 40.65423 1.000 19.70243 ? 63  LEU A CD2 1 
ATOM   514  N N   . ARG A 1 64  ? -4.71000  64.04601 43.60836 1.000 20.40158 ? 64  ARG A N   1 
ATOM   515  C CA  . ARG A 1 64  ? -5.98347  64.13079 44.31211 1.000 22.04265 ? 64  ARG A CA  1 
ATOM   516  C C   . ARG A 1 64  ? -7.05159  64.52878 43.30071 1.000 23.26014 ? 64  ARG A C   1 
ATOM   517  O O   . ARG A 1 64  ? -6.82855  65.39248 42.45914 1.000 21.64558 ? 64  ARG A O   1 
ATOM   518  C CB  . ARG A 1 64  ? -5.93708  65.13651 45.48189 1.000 21.83820 ? 64  ARG A CB  1 
ATOM   519  C CG  . ARG A 1 64  ? -5.64128  66.59215 45.07280 1.000 23.49076 ? 64  ARG A CG  1 
ATOM   520  C CD  . ARG A 1 64  ? -6.00449  67.58928 46.17310 1.000 21.54508 ? 64  ARG A CD  1 
ATOM   521  N NE  . ARG A 1 64  ? -5.19757  67.40859 47.38396 1.000 22.05971 ? 64  ARG A NE  1 
ATOM   522  C CZ  . ARG A 1 64  ? -5.48130  67.96113 48.56024 1.000 23.10168 ? 64  ARG A CZ  1 
ATOM   523  N NH1 . ARG A 1 64  ? -6.55695  68.72002 48.70190 1.000 22.52712 ? 64  ARG A NH1 1 
ATOM   524  N NH2 . ARG A 1 64  ? -4.69702  67.74169 49.60329 1.000 26.38022 ? 64  ARG A NH2 1 
ATOM   525  N N   . GLY A 1 65  ? -8.20403  63.87611 43.36067 1.000 24.05326 ? 65  GLY A N   1 
ATOM   526  C CA  . GLY A 1 65  ? -9.26862  64.18594 42.43010 1.000 21.07944 ? 65  GLY A CA  1 
ATOM   527  C C   . GLY A 1 65  ? -9.19453  63.40484 41.13140 1.000 20.20941 ? 65  GLY A C   1 
ATOM   528  O O   . GLY A 1 65  ? -10.05362 63.57352 40.26812 1.000 24.42099 ? 65  GLY A O   1 
ATOM   529  N N   . PHE A 1 66  ? -8.17102  62.56322 40.99005 1.000 22.33444 ? 66  PHE A N   1 
ATOM   530  C CA  . PHE A 1 66  ? -7.94797  61.76720 39.77292 1.000 19.79569 ? 66  PHE A CA  1 
ATOM   531  C C   . PHE A 1 66  ? -7.81779  60.27236 40.07515 1.000 22.39372 ? 66  PHE A C   1 
ATOM   532  O O   . PHE A 1 66  ? -7.45382  59.89810 41.19106 1.000 22.05555 ? 66  PHE A O   1 
ATOM   533  C CB  . PHE A 1 66  ? -6.68022  62.21684 39.05129 1.000 19.23229 ? 66  PHE A CB  1 
ATOM   534  C CG  . PHE A 1 66  ? -6.83885  63.47854 38.24390 1.000 21.66156 ? 66  PHE A CG  1 
ATOM   535  C CD1 . PHE A 1 66  ? -6.84355  64.71860 38.86275 1.000 18.55901 ? 66  PHE A CD1 1 
ATOM   536  C CD2 . PHE A 1 66  ? -6.95338  63.42201 36.86325 1.000 22.65789 ? 66  PHE A CD2 1 
ATOM   537  C CE1 . PHE A 1 66  ? -6.96950  65.88856 38.12071 1.000 20.87398 ? 66  PHE A CE1 1 
ATOM   538  C CE2 . PHE A 1 66  ? -7.08217  64.59513 36.10782 1.000 21.77422 ? 66  PHE A CE2 1 
ATOM   539  C CZ  . PHE A 1 66  ? -7.09558  65.82606 36.74554 1.000 20.57795 ? 66  PHE A CZ  1 
ATOM   540  N N   . GLY A 1 67  ? -8.07779  59.43328 39.07101 1.000 20.81237 ? 67  GLY A N   1 
ATOM   541  C CA  . GLY A 1 67  ? -7.79879  58.00873 39.16355 1.000 21.80390 ? 67  GLY A CA  1 
ATOM   542  C C   . GLY A 1 67  ? -8.42721  57.32845 40.37120 1.000 22.97591 ? 67  GLY A C   1 
ATOM   543  O O   . GLY A 1 67  ? -9.62631  57.44999 40.60564 1.000 22.39579 ? 67  GLY A O   1 
ATOM   544  N N   . ASP A 1 68  ? -7.60484  56.62890 41.14796 1.000 24.06785 ? 68  ASP A N   1 
ATOM   545  C CA  . ASP A 1 68  ? -8.07852  55.97307 42.35904 1.000 24.94294 ? 68  ASP A CA  1 
ATOM   546  C C   . ASP A 1 68  ? -7.71539  56.74811 43.60461 1.000 25.09810 ? 68  ASP A C   1 
ATOM   547  O O   . ASP A 1 68  ? -7.90221  56.24931 44.70977 1.000 23.98292 ? 68  ASP A O   1 
ATOM   548  C CB  . ASP A 1 68  ? -7.51938  54.55979 42.47254 1.000 24.10923 ? 68  ASP A CB  1 
ATOM   549  C CG  . ASP A 1 68  ? -8.11277  53.62565 41.45366 1.000 30.96623 ? 68  ASP A CG  1 
ATOM   550  O OD1 . ASP A 1 68  ? -9.35920  53.60301 41.31526 1.000 31.66998 ? 68  ASP A OD1 1 
ATOM   551  O OD2 . ASP A 1 68  ? -7.32790  52.92799 40.77942 1.000 30.31456 ? 68  ASP A OD2 1 
ATOM   552  N N   . SER A 1 69  ? -7.17300  57.95199 43.43885 1.000 23.65600 ? 69  SER A N   1 
ATOM   553  C CA  . SER A 1 69  ? -6.92418  58.78426 44.61002 1.000 22.52786 ? 69  SER A CA  1 
ATOM   554  C C   . SER A 1 69  ? -8.23802  59.36487 45.07205 1.000 22.51198 ? 69  SER A C   1 
ATOM   555  O O   . SER A 1 69  ? -9.19125  59.43289 44.30198 1.000 26.27223 ? 69  SER A O   1 
ATOM   556  C CB  . SER A 1 69  ? -5.91478  59.89111 44.31731 1.000 20.59273 ? 69  SER A CB  1 
ATOM   557  O OG  . SER A 1 69  ? -4.59803  59.35946 44.30178 1.000 21.34957 ? 69  SER A OG  1 
ATOM   558  N N   . GLU A 1 70  ? -8.28984  59.77646 46.33229 1.000 24.92382 ? 70  GLU A N   1 
ATOM   559  C CA  . GLU A 1 70  ? -9.50429  60.34354 46.89465 1.000 25.08478 ? 70  GLU A CA  1 
ATOM   560  C C   . GLU A 1 70  ? -9.95505  61.60726 46.15877 1.000 24.73010 ? 70  GLU A C   1 
ATOM   561  O O   . GLU A 1 70  ? -9.13634  62.43826 45.78194 1.000 24.76639 ? 70  GLU A O   1 
ATOM   562  C CB  . GLU A 1 70  ? -9.30300  60.66399 48.37168 1.000 24.50501 ? 70  GLU A CB  1 
ATOM   563  C CG  . GLU A 1 70  ? -10.55993 61.17555 49.07361 1.000 27.54044 ? 70  GLU A CG  1 
ATOM   564  C CD  . GLU A 1 70  ? -10.33669 61.44702 50.55310 1.000 27.21344 ? 70  GLU A CD  1 
ATOM   565  O OE1 . GLU A 1 70  ? -11.23245 62.02071 51.19923 1.000 31.90611 ? 70  GLU A OE1 1 
ATOM   566  O OE2 . GLU A 1 70  ? -9.26588  61.08849 51.07206 1.000 29.39203 ? 70  GLU A OE2 1 
ATOM   567  N N   . LYS A 1 71  ? -11.26462 61.72636 45.95736 1.000 21.81674 ? 71  LYS A N   1 
ATOM   568  C CA  . LYS A 1 71  ? -11.89030 62.97441 45.54156 1.000 22.66112 ? 71  LYS A CA  1 
ATOM   569  C C   . LYS A 1 71  ? -12.33732 63.72570 46.79367 1.000 25.56725 ? 71  LYS A C   1 
ATOM   570  O O   . LYS A 1 71  ? -13.29454 63.31526 47.45585 1.000 25.27487 ? 71  LYS A O   1 
ATOM   571  C CB  . LYS A 1 71  ? -13.09312 62.71343 44.61341 1.000 21.73517 ? 71  LYS A CB  1 
ATOM   572  C CG  . LYS A 1 71  ? -12.76438 62.63603 43.10665 1.000 21.54870 ? 71  LYS A CG  1 
ATOM   573  C CD  . LYS A 1 71  ? -11.69507 61.59457 42.77319 1.000 20.48909 ? 71  LYS A CD  1 
ATOM   574  C CE  . LYS A 1 71  ? -12.19417 60.17227 42.94878 1.000 23.21378 ? 71  LYS A CE  1 
ATOM   575  N NZ  . LYS A 1 71  ? -11.21907 59.18520 42.39106 1.000 22.58501 ? 71  LYS A NZ  1 
ATOM   576  N N   . PRO A 1 72  ? -11.63244 64.81487 47.14344 1.000 26.04564 ? 72  PRO A N   1 
ATOM   577  C CA  . PRO A 1 72  ? -12.08429 65.61303 48.28362 1.000 24.11992 ? 72  PRO A CA  1 
ATOM   578  C C   . PRO A 1 72  ? -13.47652 66.17836 48.01709 1.000 28.17168 ? 72  PRO A C   1 
ATOM   579  O O   . PRO A 1 72  ? -13.87945 66.23266 46.84933 1.000 25.80591 ? 72  PRO A O   1 
ATOM   580  C CB  . PRO A 1 72  ? -11.04376 66.74045 48.37379 1.000 25.10726 ? 72  PRO A CB  1 
ATOM   581  C CG  . PRO A 1 72  ? -9.90512  66.30867 47.54143 1.000 24.41153 ? 72  PRO A CG  1 
ATOM   582  C CD  . PRO A 1 72  ? -10.45685 65.40797 46.48358 1.000 23.84589 ? 72  PRO A CD  1 
ATOM   583  N N   . ASP A 1 73  ? -14.18836 66.53717 49.08526 1.000 26.63241 ? 73  ASP A N   1 
ATOM   584  C CA  . ASP A 1 73  ? -15.44657 67.28420 49.03880 1.000 28.47997 ? 73  ASP A CA  1 
ATOM   585  C C   . ASP A 1 73  ? -15.59706 68.03705 47.71930 1.000 27.82509 ? 73  ASP A C   1 
ATOM   586  O O   . ASP A 1 73  ? -14.90925 69.02495 47.47325 1.000 28.43160 ? 73  ASP A O   1 
ATOM   587  C CB  . ASP A 1 73  ? -15.50011 68.25114 50.23559 1.000 31.60354 ? 73  ASP A CB  1 
ATOM   588  C CG  . ASP A 1 73  ? -16.81214 69.02843 50.33605 1.000 34.26383 ? 73  ASP A CG  1 
ATOM   589  O OD1 . ASP A 1 73  ? -17.67054 68.94881 49.42949 1.000 32.23309 ? 73  ASP A OD1 1 
ATOM   590  O OD2 . ASP A 1 73  ? -16.96630 69.74959 51.34275 1.000 34.72979 ? 73  ASP A OD2 1 
ATOM   591  N N   . LEU A 1 74  ? -16.48090 67.53562 46.86634 1.000 28.83748 ? 74  LEU A N   1 
ATOM   592  C CA  . LEU A 1 74  ? -16.60704 68.03321 45.50276 1.000 27.57076 ? 74  LEU A CA  1 
ATOM   593  C C   . LEU A 1 74  ? -17.13691 69.46564 45.43693 1.000 31.00250 ? 74  LEU A C   1 
ATOM   594  O O   . LEU A 1 74  ? -16.98282 70.14049 44.41950 1.000 29.09299 ? 74  LEU A O   1 
ATOM   595  C CB  . LEU A 1 74  ? -17.50449 67.10062 44.69431 1.000 26.95878 ? 74  LEU A CB  1 
ATOM   596  C CG  . LEU A 1 74  ? -16.84358 65.77653 44.29655 1.000 26.43243 ? 74  LEU A CG  1 
ATOM   597  C CD1 . LEU A 1 74  ? -17.88188 64.74335 43.85553 1.000 27.92024 ? 74  LEU A CD1 1 
ATOM   598  C CD2 . LEU A 1 74  ? -15.81396 65.98595 43.20044 1.000 24.04065 ? 74  LEU A CD2 1 
ATOM   599  N N   . SER A 1 75  ? -17.74575 69.92663 46.52804 1.000 29.00246 ? 75  SER A N   1 
ATOM   600  C CA  . SER A 1 75  ? -18.25874 71.28713 46.60434 1.000 30.07913 ? 75  SER A CA  1 
ATOM   601  C C   . SER A 1 75  ? -17.21265 72.28974 47.11378 1.000 30.06977 ? 75  SER A C   1 
ATOM   602  O O   . SER A 1 75  ? -17.44755 73.49334 47.09114 1.000 33.46874 ? 75  SER A O   1 
ATOM   603  C CB  . SER A 1 75  ? -19.49024 71.33207 47.50866 1.000 31.36910 ? 75  SER A CB  1 
ATOM   604  O OG  . SER A 1 75  ? -19.10521 71.21250 48.86863 1.000 35.29338 ? 75  SER A OG  1 
ATOM   605  N N   . ASP A 1 76  ? -16.06360 71.79414 47.56701 1.000 28.39877 ? 76  ASP A N   1 
ATOM   606  C CA  . ASP A 1 76  ? -15.02827 72.64841 48.15377 1.000 28.37558 ? 76  ASP A CA  1 
ATOM   607  C C   . ASP A 1 76  ? -13.83622 72.84309 47.20992 1.000 26.73946 ? 76  ASP A C   1 
ATOM   608  O O   . ASP A 1 76  ? -12.88535 72.06378 47.23901 1.000 23.85763 ? 76  ASP A O   1 
ATOM   609  C CB  . ASP A 1 76  ? -14.55229 72.04982 49.48376 1.000 30.44898 ? 76  ASP A CB  1 
ATOM   610  C CG  . ASP A 1 76  ? -13.64237 72.99031 50.26955 1.000 32.37941 ? 76  ASP A CG  1 
ATOM   611  O OD1 . ASP A 1 76  ? -13.29227 74.07230 49.75894 1.000 32.87396 ? 76  ASP A OD1 1 
ATOM   612  O OD2 . ASP A 1 76  ? -13.26131 72.63545 51.40428 1.000 35.00587 ? 76  ASP A OD2 1 
ATOM   613  N N   . LEU A 1 77  ? -13.87917 73.90039 46.39896 1.000 27.78317 ? 77  LEU A N   1 
ATOM   614  C CA  . LEU A 1 77  ? -12.85632 74.12444 45.37041 1.000 27.51815 ? 77  LEU A CA  1 
ATOM   615  C C   . LEU A 1 77  ? -11.47088 74.39534 45.95357 1.000 27.68226 ? 77  LEU A C   1 
ATOM   616  O O   . LEU A 1 77  ? -10.46627 74.20688 45.27309 1.000 27.74424 ? 77  LEU A O   1 
ATOM   617  C CB  . LEU A 1 77  ? -13.26033 75.27811 44.44830 1.000 27.19281 ? 77  LEU A CB  1 
ATOM   618  C CG  . LEU A 1 77  ? -14.53626 75.03535 43.63204 1.000 30.73939 ? 77  LEU A CG  1 
ATOM   619  C CD1 . LEU A 1 77  ? -14.83711 76.19846 42.68551 1.000 28.72443 ? 77  LEU A CD1 1 
ATOM   620  C CD2 . LEU A 1 77  ? -14.44191 73.72826 42.87409 1.000 26.22476 ? 77  LEU A CD2 1 
ATOM   621  N N   . ALA A 1 78  ? -11.40879 74.82854 47.20922 1.000 27.14457 ? 78  ALA A N   1 
ATOM   622  C CA  . ALA A 1 78  ? -10.11402 75.04154 47.85873 1.000 28.01899 ? 78  ALA A CA  1 
ATOM   623  C C   . ALA A 1 78  ? -9.32736  73.72939 47.95609 1.000 27.65440 ? 78  ALA A C   1 
ATOM   624  O O   . ALA A 1 78  ? -8.09652  73.72811 47.98420 1.000 28.08123 ? 78  ALA A O   1 
ATOM   625  C CB  . ALA A 1 78  ? -10.30079 75.65593 49.24722 1.000 30.84614 ? 78  ALA A CB  1 
ATOM   626  N N   . GLN A 1 79  ? -10.04050 72.60979 47.98402 1.000 25.92058 ? 79  GLN A N   1 
ATOM   627  C CA  . GLN A 1 79  ? -9.38442  71.30826 48.06435 1.000 27.62557 ? 79  GLN A CA  1 
ATOM   628  C C   . GLN A 1 79  ? -8.91379  70.81712 46.70525 1.000 25.09718 ? 79  GLN A C   1 
ATOM   629  O O   . GLN A 1 79  ? -8.34095  69.74189 46.60030 1.000 24.06440 ? 79  GLN A O   1 
ATOM   630  C CB  . GLN A 1 79  ? -10.31860 70.28242 48.69621 1.000 30.98545 ? 79  GLN A CB  1 
ATOM   631  C CG  . GLN A 1 79  ? -10.90288 70.77438 50.01805 1.000 32.75122 ? 79  GLN A CG  1 
ATOM   632  C CD  . GLN A 1 79  ? -10.96207 69.69961 51.06643 1.000 38.20594 ? 79  GLN A CD  1 
ATOM   633  O OE1 . GLN A 1 79  ? -12.02926 69.41131 51.61565 1.000 44.76319 ? 79  GLN A OE1 1 
ATOM   634  N NE2 . GLN A 1 79  ? -9.81018  69.10357 51.36996 1.000 39.08342 ? 79  GLN A NE2 1 
ATOM   635  N N   . TYR A 1 80  ? -9.14448  71.61952 45.66963 1.000 24.12628 ? 80  TYR A N   1 
ATOM   636  C CA  . TYR A 1 80  ? -8.66384  71.30092 44.33212 1.000 23.68286 ? 80  TYR A CA  1 
ATOM   637  C C   . TYR A 1 80  ? -7.68018  72.35463 43.82577 1.000 22.91686 ? 80  TYR A C   1 
ATOM   638  O O   . TYR A 1 80  ? -7.38784  72.42191 42.63588 1.000 22.75712 ? 80  TYR A O   1 
ATOM   639  C CB  . TYR A 1 80  ? -9.84555  71.14855 43.36380 1.000 21.34155 ? 80  TYR A CB  1 
ATOM   640  C CG  . TYR A 1 80  ? -10.64709 69.89304 43.64576 1.000 22.51450 ? 80  TYR A CG  1 
ATOM   641  C CD1 . TYR A 1 80  ? -11.60210 69.86476 44.66146 1.000 22.44330 ? 80  TYR A CD1 1 
ATOM   642  C CD2 . TYR A 1 80  ? -10.43550 68.73702 42.91286 1.000 20.77091 ? 80  TYR A CD2 1 
ATOM   643  C CE1 . TYR A 1 80  ? -12.32421 68.71878 44.93352 1.000 22.67737 ? 80  TYR A CE1 1 
ATOM   644  C CE2 . TYR A 1 80  ? -11.14765 67.58540 43.17726 1.000 22.11272 ? 80  TYR A CE2 1 
ATOM   645  C CZ  . TYR A 1 80  ? -12.08547 67.57928 44.19122 1.000 22.12501 ? 80  TYR A CZ  1 
ATOM   646  O OH  . TYR A 1 80  ? -12.79871 66.43532 44.44636 1.000 21.91162 ? 80  TYR A OH  1 
ATOM   647  N N   . SER A 1 81  ? -7.15181  73.16636 44.73211 1.000 24.10341 ? 81  SER A N   1 
ATOM   648  C CA  . SER A 1 81  ? -6.14414  74.13694 44.33246 1.000 23.14244 ? 81  SER A CA  1 
ATOM   649  C C   . SER A 1 81  ? -4.82175  73.41859 44.08838 1.000 24.29919 ? 81  SER A C   1 
ATOM   650  O O   . SER A 1 81  ? -4.48512  72.46747 44.79228 1.000 23.66982 ? 81  SER A O   1 
ATOM   651  C CB  . SER A 1 81  ? -5.97447  75.22115 45.38671 1.000 24.89160 ? 81  SER A CB  1 
ATOM   652  O OG  . SER A 1 81  ? -5.31674  74.68999 46.51754 1.000 31.02985 ? 81  SER A OG  1 
ATOM   653  N N   . LEU A 1 82  ? -4.08449  73.86989 43.07914 1.000 20.58006 ? 82  LEU A N   1 
ATOM   654  C CA  . LEU A 1 82  ? -2.81753  73.24500 42.70699 1.000 21.08771 ? 82  LEU A CA  1 
ATOM   655  C C   . LEU A 1 82  ? -1.75067  73.36108 43.79441 1.000 22.54335 ? 82  LEU A C   1 
ATOM   656  O O   . LEU A 1 82  ? -0.83898  72.53955 43.85325 1.000 22.51662 ? 82  LEU A O   1 
ATOM   657  C CB  . LEU A 1 82  ? -2.29827  73.85489 41.40036 1.000 20.22073 ? 82  LEU A CB  1 
ATOM   658  C CG  . LEU A 1 82  ? -3.10765  73.40604 40.18171 1.000 23.41667 ? 82  LEU A CG  1 
ATOM   659  C CD1 . LEU A 1 82  ? -2.97223  74.36555 39.00398 1.000 21.33208 ? 82  LEU A CD1 1 
ATOM   660  C CD2 . LEU A 1 82  ? -2.69935  71.99251 39.77517 1.000 21.27422 ? 82  LEU A CD2 1 
ATOM   661  N N   . GLU A 1 83  ? -1.85902  74.38121 44.64567 1.000 22.19629 ? 83  GLU A N   1 
ATOM   662  C CA  . GLU A 1 83  ? -0.93398  74.53011 45.76988 1.000 23.66410 ? 83  GLU A CA  1 
ATOM   663  C C   . GLU A 1 83  ? -1.01054  73.31537 46.70226 1.000 23.62774 ? 83  GLU A C   1 
ATOM   664  O O   . GLU A 1 83  ? 0.00291   72.83031 47.19025 1.000 25.60408 ? 83  GLU A O   1 
ATOM   665  C CB  . GLU A 1 83  ? -1.23547  75.81433 46.54794 1.000 25.49783 ? 83  GLU A CB  1 
ATOM   666  C CG  . GLU A 1 83  ? -0.27158  76.10124 47.69564 1.000 30.84532 ? 83  GLU A CG  1 
ATOM   667  C CD  . GLU A 1 83  ? 1.03568   76.72447 47.22678 1.000 30.14191 ? 83  GLU A CD  1 
ATOM   668  O OE1 . GLU A 1 83  ? 1.15828   77.01273 46.02281 1.000 29.81497 ? 83  GLU A OE1 1 
ATOM   669  O OE2 . GLU A 1 83  ? 1.94204   76.92462 48.06081 1.000 30.65534 ? 83  GLU A OE2 1 
ATOM   670  N N   . ARG A 1 84  ? -2.22079  72.82834 46.95184 1.000 23.56713 ? 84  ARG A N   1 
ATOM   671  C CA  . ARG A 1 84  ? -2.39169  71.64593 47.78999 1.000 25.10769 ? 84  ARG A CA  1 
ATOM   672  C C   . ARG A 1 84  ? -1.90990  70.37521 47.09894 1.000 24.05874 ? 84  ARG A C   1 
ATOM   673  O O   . ARG A 1 84  ? -1.42245  69.44885 47.75668 1.000 23.38550 ? 84  ARG A O   1 
ATOM   674  C CB  . ARG A 1 84  ? -3.85513  71.50839 48.21502 1.000 28.01104 ? 84  ARG A CB  1 
ATOM   675  C CG  . ARG A 1 84  ? -4.27683  72.66958 49.07475 1.000 28.77429 ? 84  ARG A CG  1 
ATOM   676  C CD  . ARG A 1 84  ? -5.56253  72.44399 49.81671 1.000 35.10122 ? 84  ARG A CD  1 
ATOM   677  N NE  . ARG A 1 84  ? -5.90227  73.65122 50.56214 1.000 38.22145 ? 84  ARG A NE  1 
ATOM   678  C CZ  . ARG A 1 84  ? -6.96965  73.79032 51.33970 1.000 39.19706 ? 84  ARG A CZ  1 
ATOM   679  N NH1 . ARG A 1 84  ? -7.82540  72.78598 51.48807 1.000 41.49842 ? 84  ARG A NH1 1 
ATOM   680  N NH2 . ARG A 1 84  ? -7.18089  74.94272 51.96684 1.000 36.34487 ? 84  ARG A NH2 1 
ATOM   681  N N   . VAL A 1 85  ? -2.03525  70.32982 45.77393 1.000 22.42833 ? 85  VAL A N   1 
ATOM   682  C CA  . VAL A 1 85  ? -1.54036  69.18395 45.01959 1.000 20.78475 ? 85  VAL A CA  1 
ATOM   683  C C   . VAL A 1 85  ? -0.01476  69.11381 45.11728 1.000 21.91713 ? 85  VAL A C   1 
ATOM   684  O O   . VAL A 1 85  ? 0.56037   68.03318 45.19844 1.000 23.03057 ? 85  VAL A O   1 
ATOM   685  C CB  . VAL A 1 85  ? -1.98050  69.24479 43.54183 1.000 21.69810 ? 85  VAL A CB  1 
ATOM   686  C CG1 . VAL A 1 85  ? -1.42464  68.05979 42.75997 1.000 19.10402 ? 85  VAL A CG1 1 
ATOM   687  C CG2 . VAL A 1 85  ? -3.49791  69.28599 43.44894 1.000 19.15211 ? 85  VAL A CG2 1 
ATOM   688  N N   . ALA A 1 86  ? 0.64249   70.26910 45.11865 1.000 22.02825 ? 86  ALA A N   1 
ATOM   689  C CA  . ALA A 1 86  ? 2.08363   70.30273 45.32894 1.000 24.69829 ? 86  ALA A CA  1 
ATOM   690  C C   . ALA A 1 86  ? 2.43035   69.88463 46.76707 1.000 23.34056 ? 86  ALA A C   1 
ATOM   691  O O   . ALA A 1 86  ? 3.38983   69.15971 46.99085 1.000 24.48552 ? 86  ALA A O   1 
ATOM   692  C CB  . ALA A 1 86  ? 2.63616   71.68490 45.02508 1.000 22.74976 ? 86  ALA A CB  1 
ATOM   693  N N   . ASP A 1 87  ? 1.64360   70.33853 47.73747 1.000 24.28930 ? 87  ASP A N   1 
ATOM   694  C CA  . ASP A 1 87  ? 1.83693   69.90134 49.12101 1.000 25.16611 ? 87  ASP A CA  1 
ATOM   695  C C   . ASP A 1 87  ? 1.70754   68.38011 49.25549 1.000 24.47012 ? 87  ASP A C   1 
ATOM   696  O O   . ASP A 1 87  ? 2.44519   67.77264 50.02149 1.000 25.33733 ? 87  ASP A O   1 
ATOM   697  C CB  . ASP A 1 87  ? 0.84248   70.58934 50.05668 1.000 23.27529 ? 87  ASP A CB  1 
ATOM   698  C CG  . ASP A 1 87  ? 1.09029   72.08699 50.18465 1.000 26.34609 ? 87  ASP A CG  1 
ATOM   699  O OD1 . ASP A 1 87  ? 2.21555   72.55404 49.89155 1.000 26.96611 ? 87  ASP A OD1 1 
ATOM   700  O OD2 . ASP A 1 87  ? 0.15043   72.79684 50.58509 1.000 25.26494 ? 87  ASP A OD2 1 
ATOM   701  N N   . ASP A 1 88  ? 0.77870   67.77488 48.51006 1.000 24.04451 ? 88  ASP A N   1 
ATOM   702  C CA  . ASP A 1 88  ? 0.57435   66.31864 48.54302 1.000 24.29149 ? 88  ASP A CA  1 
ATOM   703  C C   . ASP A 1 88  ? 1.83531   65.54477 48.17580 1.000 24.38910 ? 88  ASP A C   1 
ATOM   704  O O   . ASP A 1 88  ? 2.04254   64.41831 48.63215 1.000 25.62694 ? 88  ASP A O   1 
ATOM   705  C CB  . ASP A 1 88  ? -0.54242  65.88263 47.58489 1.000 23.05857 ? 88  ASP A CB  1 
ATOM   706  C CG  . ASP A 1 88  ? -1.93563  66.24452 48.07633 1.000 25.67000 ? 88  ASP A CG  1 
ATOM   707  O OD1 . ASP A 1 88  ? -2.09534  66.59267 49.26417 1.000 26.78843 ? 88  ASP A OD1 1 
ATOM   708  O OD2 . ASP A 1 88  ? -2.88345  66.15511 47.25833 1.000 24.05042 ? 88  ASP A OD2 1 
ATOM   709  N N   . GLN A 1 89  ? 2.65875   66.13226 47.31523 1.000 22.96134 ? 89  GLN A N   1 
ATOM   710  C CA  . GLN A 1 89  ? 3.84842   65.44118 46.84836 1.000 22.26831 ? 89  GLN A CA  1 
ATOM   711  C C   . GLN A 1 89  ? 4.91937   65.45567 47.94440 1.000 24.18350 ? 89  GLN A C   1 
ATOM   712  O O   . GLN A 1 89  ? 5.63999   64.47079 48.14034 1.000 23.27333 ? 89  GLN A O   1 
ATOM   713  C CB  . GLN A 1 89  ? 4.37115   66.06211 45.54710 1.000 20.86553 ? 89  GLN A CB  1 
ATOM   714  C CG  . GLN A 1 89  ? 3.28970   66.23496 44.44048 1.000 20.87541 ? 89  GLN A CG  1 
ATOM   715  C CD  . GLN A 1 89  ? 2.37030   65.02191 44.28733 1.000 22.49239 ? 89  GLN A CD  1 
ATOM   716  O OE1 . GLN A 1 89  ? 2.81956   63.87734 44.32263 1.000 23.18252 ? 89  GLN A OE1 1 
ATOM   717  N NE2 . GLN A 1 89  ? 1.07274   65.27626 44.10625 1.000 20.98768 ? 89  GLN A NE2 1 
ATOM   718  N N   . ALA A 1 90  ? 5.01549   66.56566 48.66319 1.000 22.58036 ? 90  ALA A N   1 
ATOM   719  C CA  . ALA A 1 90  ? 5.90630   66.62733 49.81112 1.000 23.76916 ? 90  ALA A CA  1 
ATOM   720  C C   . ALA A 1 90  ? 5.45387   65.61113 50.87324 1.000 25.10525 ? 90  ALA A C   1 
ATOM   721  O O   . ALA A 1 90  ? 6.26219   64.86725 51.41751 1.000 27.08577 ? 90  ALA A O   1 
ATOM   722  C CB  . ALA A 1 90  ? 5.94332   68.02735 50.37983 1.000 23.26056 ? 90  ALA A CB  1 
ATOM   723  N N   . GLU A 1 91  ? 4.15605   65.56015 51.13683 1.000 24.23986 ? 91  GLU A N   1 
ATOM   724  C CA  . GLU A 1 91  ? 3.63074   64.60312 52.10348 1.000 28.72856 ? 91  GLU A CA  1 
ATOM   725  C C   . GLU A 1 91  ? 3.84948   63.15986 51.66080 1.000 28.16488 ? 91  GLU A C   1 
ATOM   726  O O   . GLU A 1 91  ? 4.09398   62.28573 52.49032 1.000 26.73857 ? 91  GLU A O   1 
ATOM   727  C CB  . GLU A 1 91  ? 2.14108   64.83568 52.34917 1.000 25.25778 ? 91  GLU A CB  1 
ATOM   728  C CG  . GLU A 1 91  ? 1.81312   66.14305 53.04812 1.000 30.75154 ? 91  GLU A CG  1 
ATOM   729  C CD  . GLU A 1 91  ? 0.38061   66.17479 53.54532 1.000 32.27096 ? 91  GLU A CD  1 
ATOM   730  O OE1 . GLU A 1 91  ? -0.12079  65.11299 53.95977 1.000 37.50739 ? 91  GLU A OE1 1 
ATOM   731  O OE2 . GLU A 1 91  ? -0.25067  67.24717 53.51820 1.000 34.30676 ? 91  GLU A OE2 1 
ATOM   732  N N   . LEU A 1 92  ? 3.73412   62.90541 50.36009 1.000 23.68875 ? 92  LEU A N   1 
ATOM   733  C CA  . LEU A 1 92  ? 3.95014   61.56390 49.84982 1.000 22.57489 ? 92  LEU A CA  1 
ATOM   734  C C   . LEU A 1 92  ? 5.38338   61.12370 50.13408 1.000 25.65997 ? 92  LEU A C   1 
ATOM   735  O O   . LEU A 1 92  ? 5.60980   60.01488 50.62234 1.000 24.94559 ? 92  LEU A O   1 
ATOM   736  C CB  . LEU A 1 92  ? 3.65371   61.48649 48.34738 1.000 22.27722 ? 92  LEU A CB  1 
ATOM   737  C CG  . LEU A 1 92  ? 3.95920   60.13960 47.69309 1.000 21.53722 ? 92  LEU A CG  1 
ATOM   738  C CD1 . LEU A 1 92  ? 3.10501   59.05244 48.33207 1.000 23.85308 ? 92  LEU A CD1 1 
ATOM   739  C CD2 . LEU A 1 92  ? 3.73569   60.18291 46.17772 1.000 21.73327 ? 92  LEU A CD2 1 
ATOM   740  N N   . LEU A 1 93  ? 6.34634   61.99101 49.82415 1.000 23.59023 ? 93  LEU A N   1 
ATOM   741  C CA  . LEU A 1 93  ? 7.75100   61.69638 50.08810 1.000 26.19677 ? 93  LEU A CA  1 
ATOM   742  C C   . LEU A 1 93  ? 8.01448   61.46675 51.58141 1.000 27.22552 ? 93  LEU A C   1 
ATOM   743  O O   . LEU A 1 93  ? 8.68198   60.50032 51.93898 1.000 28.52680 ? 93  LEU A O   1 
ATOM   744  C CB  . LEU A 1 93  ? 8.64839   62.82067 49.55854 1.000 26.69189 ? 93  LEU A CB  1 
ATOM   745  C CG  . LEU A 1 93  ? 8.60751   63.03934 48.03877 1.000 26.58652 ? 93  LEU A CG  1 
ATOM   746  C CD1 . LEU A 1 93  ? 9.64528   64.06731 47.61029 1.000 29.51967 ? 93  LEU A CD1 1 
ATOM   747  C CD2 . LEU A 1 93  ? 8.79292   61.73719 47.27496 1.000 22.82622 ? 93  LEU A CD2 1 
ATOM   748  N N   . ASN A 1 94  ? 7.49115   62.34522 52.44056 1.000 28.01514 ? 94  ASN A N   1 
ATOM   749  C CA  . ASN A 1 94  ? 7.57574   62.15248 53.89278 1.000 28.06088 ? 94  ASN A CA  1 
ATOM   750  C C   . ASN A 1 94  ? 7.04391   60.79547 54.33608 1.000 32.06485 ? 94  ASN A C   1 
ATOM   751  O O   . ASN A 1 94  ? 7.68276   60.09549 55.11777 1.000 30.31799 ? 94  ASN A O   1 
ATOM   752  C CB  . ASN A 1 94  ? 6.80014   63.23472 54.64334 1.000 28.16292 ? 94  ASN A CB  1 
ATOM   753  C CG  . ASN A 1 94  ? 7.48137   64.58544 54.60517 1.000 31.81295 ? 94  ASN A CG  1 
ATOM   754  O OD1 . ASN A 1 94  ? 8.64836   64.70063 54.23738 1.000 33.30346 ? 94  ASN A OD1 1 
ATOM   755  N ND2 . ASN A 1 94  ? 6.74887   65.62086 54.99850 1.000 33.11337 ? 94  ASN A ND2 1 
ATOM   756  N N   . ALA A 1 95  ? 5.86007   60.44690 53.83632 1.000 28.18682 ? 95  ALA A N   1 
ATOM   757  C CA  . ALA A 1 95  ? 5.18713   59.21313 54.20663 1.000 28.12836 ? 95  ALA A CA  1 
ATOM   758  C C   . ALA A 1 95  ? 5.96352   57.98319 53.76546 1.000 30.93825 ? 95  ALA A C   1 
ATOM   759  O O   . ALA A 1 95  ? 5.85912   56.92596 54.38007 1.000 32.00512 ? 95  ALA A O   1 
ATOM   760  C CB  . ALA A 1 95  ? 3.78069   59.18395 53.62062 1.000 28.81906 ? 95  ALA A CB  1 
ATOM   761  N N   . LEU A 1 96  ? 6.74413   58.11334 52.70023 1.000 30.15115 ? 96  LEU A N   1 
ATOM   762  C CA  . LEU A 1 96  ? 7.50157   56.97148 52.19865 1.000 27.92926 ? 96  LEU A CA  1 
ATOM   763  C C   . LEU A 1 96  ? 8.95169   56.97519 52.69102 1.000 28.69014 ? 96  LEU A C   1 
ATOM   764  O O   . LEU A 1 96  ? 9.74828   56.13817 52.27425 1.000 29.68055 ? 96  LEU A O   1 
ATOM   765  C CB  . LEU A 1 96  ? 7.46425   56.93437 50.66631 1.000 25.85448 ? 96  LEU A CB  1 
ATOM   766  C CG  . LEU A 1 96  ? 6.06924   56.84965 50.03639 1.000 30.03510 ? 96  LEU A CG  1 
ATOM   767  C CD1 . LEU A 1 96  ? 6.12734   56.52769 48.53681 1.000 25.13255 ? 96  LEU A CD1 1 
ATOM   768  C CD2 . LEU A 1 96  ? 5.20237   55.84299 50.76750 1.000 29.47443 ? 96  LEU A CD2 1 
ATOM   769  N N   . GLY A 1 97  ? 9.27951   57.92388 53.56726 1.000 30.69708 ? 97  GLY A N   1 
ATOM   770  C CA  . GLY A 1 97  ? 10.61710  58.06085 54.11693 1.000 29.80161 ? 97  GLY A CA  1 
ATOM   771  C C   . GLY A 1 97  ? 11.66343  58.46051 53.09288 1.000 35.55677 ? 97  GLY A C   1 
ATOM   772  O O   . GLY A 1 97  ? 12.81603  58.04242 53.17112 1.000 30.81539 ? 97  GLY A O   1 
ATOM   773  N N   . ILE A 1 98  ? 11.26555  59.28133 52.12689 1.000 32.20690 ? 98  ILE A N   1 
ATOM   774  C CA  . ILE A 1 98  ? 12.17104  59.68726 51.06315 1.000 31.26498 ? 98  ILE A CA  1 
ATOM   775  C C   . ILE A 1 98  ? 12.59195  61.13998 51.23925 1.000 31.03109 ? 98  ILE A C   1 
ATOM   776  O O   . ILE A 1 98  ? 11.75383  62.03110 51.30897 1.000 30.16746 ? 98  ILE A O   1 
ATOM   777  C CB  . ILE A 1 98  ? 11.52202  59.48600 49.68177 1.000 29.83643 ? 98  ILE A CB  1 
ATOM   778  C CG1 . ILE A 1 98  ? 11.28310  57.99588 49.44502 1.000 29.66310 ? 98  ILE A CG1 1 
ATOM   779  C CG2 . ILE A 1 98  ? 12.39032  60.08969 48.58148 1.000 29.03077 ? 98  ILE A CG2 1 
ATOM   780  C CD1 . ILE A 1 98  ? 10.44872  57.70558 48.24007 1.000 32.25899 ? 98  ILE A CD1 1 
ATOM   781  N N   . ASP A 1 99  ? 13.89769  61.36522 51.32573 1.000 30.96191 ? 99  ASP A N   1 
ATOM   782  C CA  . ASP A 1 99  ? 14.43446  62.70222 51.57056 1.000 33.87759 ? 99  ASP A CA  1 
ATOM   783  C C   . ASP A 1 99  ? 14.41166  63.56676 50.31535 1.000 29.38980 ? 99  ASP A C   1 
ATOM   784  O O   . ASP A 1 99  ? 14.00453  64.72032 50.35454 1.000 32.29062 ? 99  ASP A O   1 
ATOM   785  C CB  . ASP A 1 99  ? 15.86355  62.61540 52.10650 1.000 34.99342 ? 99  ASP A CB  1 
ATOM   786  C CG  . ASP A 1 99  ? 15.92184  62.14457 53.55054 1.000 48.22531 ? 99  ASP A CG  1 
ATOM   787  O OD1 . ASP A 1 99  ? 14.87386  62.14806 54.23699 1.000 54.20104 ? 99  ASP A OD1 1 
ATOM   788  O OD2 . ASP A 1 99  ? 17.02556  61.77881 54.00744 1.000 58.64390 ? 99  ASP A OD2 1 
ATOM   789  N N   . GLN A 1 100 ? 14.84946  62.99604 49.20397 1.000 28.73450 ? 100 GLN A N   1 
ATOM   790  C CA  . GLN A 1 100 ? 14.93935  63.72707 47.94991 1.000 30.27386 ? 100 GLN A CA  1 
ATOM   791  C C   . GLN A 1 100 ? 14.48862  62.86200 46.79059 1.000 29.04589 ? 100 GLN A C   1 
ATOM   792  O O   . GLN A 1 100 ? 14.70743  61.65616 46.79816 1.000 30.52770 ? 100 GLN A O   1 
ATOM   793  C CB  . GLN A 1 100 ? 16.37335  64.19063 47.69221 1.000 31.29660 ? 100 GLN A CB  1 
ATOM   794  C CG  . GLN A 1 100 ? 16.89844  65.22867 48.64122 1.000 35.29784 ? 100 GLN A CG  1 
ATOM   795  C CD  . GLN A 1 100 ? 18.14582  65.90024 48.10007 1.000 38.94101 ? 100 GLN A CD  1 
ATOM   796  O OE1 . GLN A 1 100 ? 19.01551  65.24993 47.52000 1.000 39.93052 ? 100 GLN A OE1 1 
ATOM   797  N NE2 . GLN A 1 100 ? 18.22912  67.21151 48.27381 1.000 38.96319 ? 100 GLN A NE2 1 
ATOM   798  N N   . ALA A 1 101 ? 13.89202  63.48226 45.78029 1.000 27.60137 ? 101 ALA A N   1 
ATOM   799  C CA  . ALA A 1 101 ? 13.51784  62.76212 44.56639 1.000 29.08015 ? 101 ALA A CA  1 
ATOM   800  C C   . ALA A 1 101 ? 13.80752  63.57771 43.31817 1.000 27.32930 ? 101 ALA A C   1 
ATOM   801  O O   . ALA A 1 101 ? 13.90718  64.79765 43.37375 1.000 27.13712 ? 101 ALA A O   1 
ATOM   802  C CB  . ALA A 1 101 ? 12.04773  62.38593 44.60226 1.000 26.39508 ? 101 ALA A CB  1 
ATOM   803  N N   . TYR A 1 102 ? 13.95729  62.88545 42.19949 1.000 26.80700 ? 102 TYR A N   1 
ATOM   804  C CA  . TYR A 1 102 ? 13.82327  63.51723 40.89951 1.000 26.49146 ? 102 TYR A CA  1 
ATOM   805  C C   . TYR A 1 102 ? 12.33630  63.65481 40.62956 1.000 26.60414 ? 102 TYR A C   1 
ATOM   806  O O   . TYR A 1 102 ? 11.58975  62.69217 40.83406 1.000 25.14473 ? 102 TYR A O   1 
ATOM   807  C CB  . TYR A 1 102 ? 14.48326  62.68416 39.80618 1.000 24.15023 ? 102 TYR A CB  1 
ATOM   808  C CG  . TYR A 1 102 ? 15.98712  62.56604 39.90927 1.000 28.64052 ? 102 TYR A CG  1 
ATOM   809  C CD1 . TYR A 1 102 ? 16.57809  61.50609 40.58448 1.000 30.33241 ? 102 TYR A CD1 1 
ATOM   810  C CD2 . TYR A 1 102 ? 16.81566  63.50318 39.30783 1.000 29.29570 ? 102 TYR A CD2 1 
ATOM   811  C CE1 . TYR A 1 102 ? 17.95504  61.38203 40.66018 1.000 33.36367 ? 102 TYR A CE1 1 
ATOM   812  C CE2 . TYR A 1 102 ? 18.19069  63.39057 39.37568 1.000 31.13453 ? 102 TYR A CE2 1 
ATOM   813  C CZ  . TYR A 1 102 ? 18.75798  62.33131 40.05558 1.000 34.99623 ? 102 TYR A CZ  1 
ATOM   814  O OH  . TYR A 1 102 ? 20.13010  62.22167 40.13102 1.000 34.59744 ? 102 TYR A OH  1 
ATOM   815  N N   . VAL A 1 103 ? 11.89525  64.83028 40.18687 1.000 24.73154 ? 103 VAL A N   1 
ATOM   816  C CA  . VAL A 1 103 ? 10.47787  65.03118 39.91551 1.000 22.40897 ? 103 VAL A CA  1 
ATOM   817  C C   . VAL A 1 103 ? 10.21570  65.44021 38.46005 1.000 25.79706 ? 103 VAL A C   1 
ATOM   818  O O   . VAL A 1 103 ? 10.93588  66.26166 37.88281 1.000 24.45785 ? 103 VAL A O   1 
ATOM   819  C CB  . VAL A 1 103 ? 9.87260   66.07245 40.89162 1.000 23.96947 ? 103 VAL A CB  1 
ATOM   820  C CG1 . VAL A 1 103 ? 10.11209  65.64149 42.33259 1.000 24.84183 ? 103 VAL A CG1 1 
ATOM   821  C CG2 . VAL A 1 103 ? 10.46371  67.47266 40.66538 1.000 27.78822 ? 103 VAL A CG2 1 
ATOM   822  N N   . VAL A 1 104 ? 9.18586   64.83755 37.86848 1.000 24.43525 ? 104 VAL A N   1 
ATOM   823  C CA  . VAL A 1 104 ? 8.83268   65.05895 36.47222 1.000 20.20765 ? 104 VAL A CA  1 
ATOM   824  C C   . VAL A 1 104 ? 7.33579   65.36443 36.35626 1.000 23.42715 ? 104 VAL A C   1 
ATOM   825  O O   . VAL A 1 104 ? 6.50082   64.65346 36.92649 1.000 22.77882 ? 104 VAL A O   1 
ATOM   826  C CB  . VAL A 1 104 ? 9.15876   63.83357 35.58049 1.000 25.25665 ? 104 VAL A CB  1 
ATOM   827  C CG1 . VAL A 1 104 ? 8.89127   64.14969 34.10135 1.000 19.28284 ? 104 VAL A CG1 1 
ATOM   828  C CG2 . VAL A 1 104 ? 10.60122  63.37108 35.77527 1.000 23.53752 ? 104 VAL A CG2 1 
ATOM   829  N N   . GLY A 1 105 ? 6.99912   66.42115 35.62472 1.000 20.20034 ? 105 GLY A N   1 
ATOM   830  C CA  . GLY A 1 105 ? 5.60838   66.75703 35.39858 1.000 21.50390 ? 105 GLY A CA  1 
ATOM   831  C C   . GLY A 1 105 ? 5.30967   67.34921 34.03356 1.000 21.33431 ? 105 GLY A C   1 
ATOM   832  O O   . GLY A 1 105 ? 6.20447   67.79128 33.31227 1.000 20.35032 ? 105 GLY A O   1 
ATOM   833  N N   . HIS A 1 106 ? 4.03025   67.35250 33.68278 1.000 19.94116 ? 106 HIS A N   1 
ATOM   834  C CA  . HIS A 1 106 ? 3.54784   68.06868 32.50907 1.000 21.86643 ? 106 HIS A CA  1 
ATOM   835  C C   . HIS A 1 106 ? 2.08595   68.41225 32.74151 1.000 21.82338 ? 106 HIS A C   1 
ATOM   836  O O   . HIS A 1 106 ? 1.47400   67.90924 33.68567 1.000 22.22415 ? 106 HIS A O   1 
ATOM   837  C CB  . HIS A 1 106 ? 3.69430   67.23950 31.23521 1.000 20.94927 ? 106 HIS A CB  1 
ATOM   838  C CG  . HIS A 1 106 ? 2.60396   66.23008 31.05394 1.000 21.72698 ? 106 HIS A CG  1 
ATOM   839  N ND1 . HIS A 1 106 ? 1.81769   66.17875 29.92746 1.000 22.49836 ? 106 HIS A ND1 1 
ATOM   840  C CD2 . HIS A 1 106 ? 2.17094   65.23313 31.86450 1.000 22.74935 ? 106 HIS A CD2 1 
ATOM   841  C CE1 . HIS A 1 106 ? 0.94372   65.19141 30.04972 1.000 23.65813 ? 106 HIS A CE1 1 
ATOM   842  N NE2 . HIS A 1 106 ? 1.13921   64.60409 31.21476 1.000 19.60289 ? 106 HIS A NE2 1 
ATOM   843  N N   . ASP A 1 107 ? 1.53550   69.26047 31.87816 1.000 22.30576 ? 107 ASP A N   1 
ATOM   844  C CA  . ASP A 1 107 ? 0.12686   69.62335 31.96170 1.000 21.83251 ? 107 ASP A CA  1 
ATOM   845  C C   . ASP A 1 107 ? -0.09303  70.23529 33.34370 1.000 22.10642 ? 107 ASP A C   1 
ATOM   846  O O   . ASP A 1 107 ? 0.70577   71.05950 33.76442 1.000 21.69415 ? 107 ASP A O   1 
ATOM   847  C CB  . ASP A 1 107 ? -0.76463  68.39756 31.70770 1.000 20.72561 ? 107 ASP A CB  1 
ATOM   848  C CG  . ASP A 1 107 ? -2.21990  68.75940 31.52312 1.000 22.06536 ? 107 ASP A CG  1 
ATOM   849  O OD1 . ASP A 1 107 ? -2.58045  69.22188 30.42729 1.000 21.15981 ? 107 ASP A OD1 1 
ATOM   850  O OD2 . ASP A 1 107 ? -3.00428  68.56906 32.47529 1.000 23.39414 ? 107 ASP A OD2 1 
ATOM   851  N N   . TYR A 1 108 ? -1.14385  69.83355 34.06068 1.000 22.04789 ? 108 TYR A N   1 
ATOM   852  C CA  . TYR A 1 108 ? -1.35170  70.34665 35.41573 1.000 20.66206 ? 108 TYR A CA  1 
ATOM   853  C C   . TYR A 1 108 ? -0.13384  70.13583 36.31222 1.000 20.24849 ? 108 TYR A C   1 
ATOM   854  O O   . TYR A 1 108 ? 0.17995   70.97014 37.16064 1.000 22.33134 ? 108 TYR A O   1 
ATOM   855  C CB  . TYR A 1 108 ? -2.56934  69.69394 36.06227 1.000 19.81233 ? 108 TYR A CB  1 
ATOM   856  C CG  . TYR A 1 108 ? -3.86843  70.43236 35.82341 1.000 21.37713 ? 108 TYR A CG  1 
ATOM   857  C CD1 . TYR A 1 108 ? -4.04424  71.73186 36.27977 1.000 19.78942 ? 108 TYR A CD1 1 
ATOM   858  C CD2 . TYR A 1 108 ? -4.93071  69.81533 35.16462 1.000 19.43645 ? 108 TYR A CD2 1 
ATOM   859  C CE1 . TYR A 1 108 ? -5.23824  72.40475 36.07317 1.000 21.61850 ? 108 TYR A CE1 1 
ATOM   860  C CE2 . TYR A 1 108 ? -6.12812  70.47341 34.97036 1.000 19.31831 ? 108 TYR A CE2 1 
ATOM   861  C CZ  . TYR A 1 108 ? -6.27964  71.76778 35.42294 1.000 21.53270 ? 108 TYR A CZ  1 
ATOM   862  O OH  . TYR A 1 108 ? -7.48023  72.42750 35.22616 1.000 23.14844 ? 108 TYR A OH  1 
ATOM   863  N N   . SER A 1 109 ? 0.55112   69.01741 36.11665 1.000 19.88210 ? 109 SER A N   1 
ATOM   864  C CA  . SER A 1 109 ? 1.71815   68.69916 36.91767 1.000 18.68674 ? 109 SER A CA  1 
ATOM   865  C C   . SER A 1 109 ? 2.93884   69.53022 36.53826 1.000 20.90338 ? 109 SER A C   1 
ATOM   866  O O   . SER A 1 109 ? 3.91681   69.55401 37.27755 1.000 22.30560 ? 109 SER A O   1 
ATOM   867  C CB  . SER A 1 109 ? 2.03638   67.20984 36.81416 1.000 20.12556 ? 109 SER A CB  1 
ATOM   868  O OG  . SER A 1 109 ? 1.12008   66.47410 37.60994 1.000 24.34589 ? 109 SER A OG  1 
ATOM   869  N N   . ALA A 1 110 ? 2.88315   70.21887 35.40082 1.000 21.30883 ? 110 ALA A N   1 
ATOM   870  C CA  . ALA A 1 110 ? 3.89739   71.22387 35.09474 1.000 21.03543 ? 110 ALA A CA  1 
ATOM   871  C C   . ALA A 1 110 ? 3.83465   72.34770 36.13757 1.000 21.33210 ? 110 ALA A C   1 
ATOM   872  O O   . ALA A 1 110 ? 4.85571   72.85764 36.58721 1.000 21.69364 ? 110 ALA A O   1 
ATOM   873  C CB  . ALA A 1 110 ? 3.71060   71.77445 33.69443 1.000 19.45926 ? 110 ALA A CB  1 
ATOM   874  N N   . ILE A 1 111 ? 2.62238   72.71421 36.53273 1.000 21.43173 ? 111 ILE A N   1 
ATOM   875  C CA  . ILE A 1 111 ? 2.43339   73.73028 37.55995 1.000 19.54557 ? 111 ILE A CA  1 
ATOM   876  C C   . ILE A 1 111 ? 2.80437   73.17401 38.94173 1.000 21.82451 ? 111 ILE A C   1 
ATOM   877  O O   . ILE A 1 111 ? 3.47058   73.84406 39.73838 1.000 21.48434 ? 111 ILE A O   1 
ATOM   878  C CB  . ILE A 1 111 ? 0.98552   74.23659 37.54613 1.000 20.78224 ? 111 ILE A CB  1 
ATOM   879  C CG1 . ILE A 1 111 ? 0.72209   74.97940 36.23202 1.000 20.60235 ? 111 ILE A CG1 1 
ATOM   880  C CG2 . ILE A 1 111 ? 0.68685   75.10532 38.76666 1.000 21.62421 ? 111 ILE A CG2 1 
ATOM   881  C CD1 . ILE A 1 111 ? -0.71863  75.28452 35.98919 1.000 25.33803 ? 111 ILE A CD1 1 
ATOM   882  N N   . VAL A 1 112 ? 2.39132   71.93833 39.20824 1.000 19.03163 ? 112 VAL A N   1 
ATOM   883  C CA  . VAL A 1 112 ? 2.75609   71.26149 40.45113 1.000 23.39210 ? 112 VAL A CA  1 
ATOM   884  C C   . VAL A 1 112 ? 4.27768   71.23695 40.65348 1.000 21.00549 ? 112 VAL A C   1 
ATOM   885  O O   . VAL A 1 112 ? 4.76922   71.51769 41.74166 1.000 23.79021 ? 112 VAL A O   1 
ATOM   886  C CB  . VAL A 1 112 ? 2.22152   69.81059 40.48984 1.000 22.73477 ? 112 VAL A CB  1 
ATOM   887  C CG1 . VAL A 1 112 ? 2.70631   69.10092 41.75328 1.000 21.67983 ? 112 VAL A CG1 1 
ATOM   888  C CG2 . VAL A 1 112 ? 0.68973   69.79974 40.40692 1.000 21.17028 ? 112 VAL A CG2 1 
ATOM   889  N N   . VAL A 1 113 ? 5.01717   70.90439 39.60368 1.000 21.04407 ? 113 VAL A N   1 
ATOM   890  C CA  . VAL A 1 113 ? 6.47423   70.84980 39.69551 1.000 20.85277 ? 113 VAL A CA  1 
ATOM   891  C C   . VAL A 1 113 ? 7.06328   72.25496 39.83763 1.000 22.54347 ? 113 VAL A C   1 
ATOM   892  O O   . VAL A 1 113 ? 7.95572   72.46610 40.65393 1.000 22.39831 ? 113 VAL A O   1 
ATOM   893  C CB  . VAL A 1 113 ? 7.08953   70.13426 38.48133 1.000 21.49455 ? 113 VAL A CB  1 
ATOM   894  C CG1 . VAL A 1 113 ? 8.60396   70.29183 38.47655 1.000 19.26877 ? 113 VAL A CG1 1 
ATOM   895  C CG2 . VAL A 1 113 ? 6.70479   68.65631 38.50813 1.000 21.22308 ? 113 VAL A CG2 1 
ATOM   896  N N   . HIS A 1 114 ? 6.54800   73.20805 39.05999 1.000 21.97122 ? 114 HIS A N   1 
ATOM   897  C CA  . HIS A 1 114 ? 6.91894   74.61249 39.21849 1.000 20.21052 ? 114 HIS A CA  1 
ATOM   898  C C   . HIS A 1 114 ? 6.84579   75.03049 40.68157 1.000 22.93029 ? 114 HIS A C   1 
ATOM   899  O O   . HIS A 1 114 ? 7.80796   75.56311 41.23016 1.000 23.77996 ? 114 HIS A O   1 
ATOM   900  C CB  . HIS A 1 114 ? 6.01332   75.53301 38.38597 1.000 21.20072 ? 114 HIS A CB  1 
ATOM   901  C CG  . HIS A 1 114 ? 6.41271   76.97419 38.44438 1.000 20.80282 ? 114 HIS A CG  1 
ATOM   902  N ND1 . HIS A 1 114 ? 7.10295   77.59713 37.42732 1.000 23.07978 ? 114 HIS A ND1 1 
ATOM   903  C CD2 . HIS A 1 114 ? 6.24786   77.90751 39.41071 1.000 20.35474 ? 114 HIS A CD2 1 
ATOM   904  C CE1 . HIS A 1 114 ? 7.33038   78.85651 37.75641 1.000 19.37108 ? 114 HIS A CE1 1 
ATOM   905  N NE2 . HIS A 1 114 ? 6.82413   79.06945 38.95708 1.000 22.24152 ? 114 HIS A NE2 1 
ATOM   906  N N   . LYS A 1 115 ? 5.69306   74.78786 41.29457 1.000 20.58347 ? 115 LYS A N   1 
ATOM   907  C CA  . LYS A 1 115 ? 5.46072   75.09672 42.70206 1.000 21.62427 ? 115 LYS A CA  1 
ATOM   908  C C   . LYS A 1 115 ? 6.35859   74.29449 43.64186 1.000 23.77679 ? 115 LYS A C   1 
ATOM   909  O O   . LYS A 1 115 ? 6.90839   74.83803 44.59134 1.000 22.20211 ? 115 LYS A O   1 
ATOM   910  C CB  . LYS A 1 115 ? 4.00508   74.82196 43.07925 1.000 22.65565 ? 115 LYS A CB  1 
ATOM   911  C CG  . LYS A 1 115 ? 3.00107   75.81852 42.55720 1.000 22.65768 ? 115 LYS A CG  1 
ATOM   912  C CD  . LYS A 1 115 ? 1.58798   75.32546 42.83700 1.000 22.55722 ? 115 LYS A CD  1 
ATOM   913  C CE  . LYS A 1 115 ? 0.54720   76.39532 42.55114 1.000 20.85430 ? 115 LYS A CE  1 
ATOM   914  N NZ  . LYS A 1 115 ? 0.80114   77.64642 43.33048 1.000 23.11948 ? 115 LYS A NZ  1 
ATOM   915  N N   . PHE A 1 116 ? 6.47334   72.99773 43.37340 1.000 21.36722 ? 116 PHE A N   1 
ATOM   916  C CA  . PHE A 1 116 ? 7.15702   72.08216 44.27454 1.000 22.50569 ? 116 PHE A CA  1 
ATOM   917  C C   . PHE A 1 116 ? 8.62861   72.41112 44.43130 1.000 24.30315 ? 116 PHE A C   1 
ATOM   918  O O   . PHE A 1 116 ? 9.15270   72.41062 45.54407 1.000 26.10765 ? 116 PHE A O   1 
ATOM   919  C CB  . PHE A 1 116 ? 7.01283   70.64174 43.78331 1.000 22.01557 ? 116 PHE A CB  1 
ATOM   920  C CG  . PHE A 1 116 ? 7.61938   69.61951 44.70655 1.000 24.64840 ? 116 PHE A CG  1 
ATOM   921  C CD1 . PHE A 1 116 ? 6.87738   69.08248 45.74625 1.000 23.12091 ? 116 PHE A CD1 1 
ATOM   922  C CD2 . PHE A 1 116 ? 8.92805   69.19841 44.53905 1.000 24.48412 ? 116 PHE A CD2 1 
ATOM   923  C CE1 . PHE A 1 116 ? 7.43408   68.13895 46.60131 1.000 25.23775 ? 116 PHE A CE1 1 
ATOM   924  C CE2 . PHE A 1 116 ? 9.48834   68.25468 45.39299 1.000 25.10985 ? 116 PHE A CE2 1 
ATOM   925  C CZ  . PHE A 1 116 ? 8.73908   67.72424 46.41845 1.000 24.61784 ? 116 PHE A CZ  1 
ATOM   926  N N   . ILE A 1 117 ? 9.30828   72.67424 43.32083 1.000 23.71585 ? 117 ILE A N   1 
ATOM   927  C CA  . ILE A 1 117 ? 10.74828  72.85726 43.39318 1.000 24.81451 ? 117 ILE A CA  1 
ATOM   928  C C   . ILE A 1 117 ? 11.09596  74.16644 44.08218 1.000 25.50851 ? 117 ILE A C   1 
ATOM   929  O O   . ILE A 1 117 ? 12.20334  74.32379 44.56239 1.000 26.98153 ? 117 ILE A O   1 
ATOM   930  C CB  . ILE A 1 117 ? 11.42165  72.80731 42.00684 1.000 25.95871 ? 117 ILE A CB  1 
ATOM   931  C CG1 . ILE A 1 117 ? 10.95105  73.94891 41.10656 1.000 23.64609 ? 117 ILE A CG1 1 
ATOM   932  C CG2 . ILE A 1 117 ? 11.19529  71.45629 41.34656 1.000 26.22860 ? 117 ILE A CG2 1 
ATOM   933  C CD1 . ILE A 1 117 ? 11.52073  73.86114 39.72798 1.000 24.91149 ? 117 ILE A CD1 1 
ATOM   934  N N   . ARG A 1 118 ? 10.14600  75.09367 44.15494 1.000 26.25521 ? 118 ARG A N   1 
ATOM   935  C CA  . ARG A 1 118 ? 10.39290  76.37232 44.82145 1.000 24.56202 ? 118 ARG A CA  1 
ATOM   936  C C   . ARG A 1 118 ? 9.97608   76.32872 46.28888 1.000 26.98111 ? 118 ARG A C   1 
ATOM   937  O O   . ARG A 1 118 ? 10.61151  76.94976 47.13906 1.000 28.09051 ? 118 ARG A O   1 
ATOM   938  C CB  . ARG A 1 118 ? 9.66154   77.51226 44.10619 1.000 23.39840 ? 118 ARG A CB  1 
ATOM   939  C CG  . ARG A 1 118 ? 10.23178  77.84393 42.73498 1.000 24.82941 ? 118 ARG A CG  1 
ATOM   940  C CD  . ARG A 1 118 ? 9.31394   78.77879 41.94115 1.000 22.17366 ? 118 ARG A CD  1 
ATOM   941  N NE  . ARG A 1 118 ? 9.96661   79.20411 40.70625 1.000 22.60521 ? 118 ARG A NE  1 
ATOM   942  C CZ  . ARG A 1 118 ? 10.10242  78.45283 39.61822 1.000 20.98445 ? 118 ARG A CZ  1 
ATOM   943  N NH1 . ARG A 1 118 ? 9.60679   77.21423 39.56771 1.000 20.22977 ? 118 ARG A NH1 1 
ATOM   944  N NH2 . ARG A 1 118 ? 10.73729  78.94419 38.56697 1.000 21.24705 ? 118 ARG A NH2 1 
ATOM   945  N N   . LYS A 1 119 ? 8.91188   75.58908 46.57992 1.000 23.59719 ? 119 LYS A N   1 
ATOM   946  C CA  . LYS A 1 119 ? 8.40515   75.47415 47.94193 1.000 27.43444 ? 119 LYS A CA  1 
ATOM   947  C C   . LYS A 1 119 ? 9.14682   74.42304 48.76767 1.000 26.77839 ? 119 LYS A C   1 
ATOM   948  O O   . LYS A 1 119 ? 9.29497   74.57625 49.97038 1.000 29.10613 ? 119 LYS A O   1 
ATOM   949  C CB  . LYS A 1 119 ? 6.91362   75.14208 47.92415 1.000 26.26387 ? 119 LYS A CB  1 
ATOM   950  C CG  . LYS A 1 119 ? 6.21924   75.36471 49.25295 1.000 26.72352 ? 119 LYS A CG  1 
ATOM   951  C CD  . LYS A 1 119 ? 4.71950   75.21976 49.09973 1.000 25.41664 ? 119 LYS A CD  1 
ATOM   952  C CE  . LYS A 1 119 ? 3.99637   75.37592 50.42951 1.000 26.43273 ? 119 LYS A CE  1 
ATOM   953  N NZ  . LYS A 1 119 ? 2.53181   75.32518 50.22114 1.000 27.94629 ? 119 LYS A NZ  1 
ATOM   954  N N   . TYR A 1 120 ? 9.60089   73.35863 48.11623 1.000 27.21174 ? 120 TYR A N   1 
ATOM   955  C CA  . TYR A 1 120 ? 10.31791  72.27548 48.78789 1.000 27.13478 ? 120 TYR A CA  1 
ATOM   956  C C   . TYR A 1 120 ? 11.66905  72.01738 48.12864 1.000 27.91352 ? 120 TYR A C   1 
ATOM   957  O O   . TYR A 1 120 ? 11.96263  70.89348 47.72667 1.000 26.48509 ? 120 TYR A O   1 
ATOM   958  C CB  . TYR A 1 120 ? 9.47124   70.99926 48.77157 1.000 26.75760 ? 120 TYR A CB  1 
ATOM   959  C CG  . TYR A 1 120 ? 8.11425   71.20589 49.39836 1.000 28.64583 ? 120 TYR A CG  1 
ATOM   960  C CD1 . TYR A 1 120 ? 7.96862   71.25380 50.77761 1.000 29.40411 ? 120 TYR A CD1 1 
ATOM   961  C CD2 . TYR A 1 120 ? 6.97990   71.37570 48.61254 1.000 25.96466 ? 120 TYR A CD2 1 
ATOM   962  C CE1 . TYR A 1 120 ? 6.72471   71.46297 51.36129 1.000 29.03790 ? 120 TYR A CE1 1 
ATOM   963  C CE2 . TYR A 1 120 ? 5.73753   71.57841 49.18703 1.000 25.37664 ? 120 TYR A CE2 1 
ATOM   964  C CZ  . TYR A 1 120 ? 5.61587   71.61802 50.56232 1.000 25.58192 ? 120 TYR A CZ  1 
ATOM   965  O OH  . TYR A 1 120 ? 4.37701   71.82191 51.13451 1.000 26.36290 ? 120 TYR A OH  1 
ATOM   966  N N   . PRO A 1 121 ? 12.50716  73.06176 48.02115 1.000 30.07616 ? 121 PRO A N   1 
ATOM   967  C CA  . PRO A 1 121 ? 13.70765  72.94133 47.18650 1.000 29.52004 ? 121 PRO A CA  1 
ATOM   968  C C   . PRO A 1 121 ? 14.68500  71.87456 47.68505 1.000 29.93258 ? 121 PRO A C   1 
ATOM   969  O O   . PRO A 1 121 ? 15.42601  71.29302 46.89870 1.000 32.86611 ? 121 PRO A O   1 
ATOM   970  C CB  . PRO A 1 121 ? 14.32756  74.33942 47.26693 1.000 28.47656 ? 121 PRO A CB  1 
ATOM   971  C CG  . PRO A 1 121 ? 13.86919  74.88572 48.56087 1.000 29.46697 ? 121 PRO A CG  1 
ATOM   972  C CD  . PRO A 1 121 ? 12.48330  74.32589 48.77972 1.000 28.02453 ? 121 PRO A CD  1 
ATOM   973  N N   . ASP A 1 122 ? 14.65150  71.59625 48.97671 1.000 31.62199 ? 122 ASP A N   1 
ATOM   974  C CA  . ASP A 1 122 ? 15.54468  70.61010 49.56904 1.000 35.50486 ? 122 ASP A CA  1 
ATOM   975  C C   . ASP A 1 122 ? 15.08809  69.15847 49.34940 1.000 34.44926 ? 122 ASP A C   1 
ATOM   976  O O   . ASP A 1 122 ? 15.79651  68.22068 49.71602 1.000 33.31601 ? 122 ASP A O   1 
ATOM   977  C CB  . ASP A 1 122 ? 15.69251  70.89800 51.06489 1.000 39.84041 ? 122 ASP A CB  1 
ATOM   978  C CG  . ASP A 1 122 ? 14.35336  71.14510 51.74892 1.000 44.94466 ? 122 ASP A CG  1 
ATOM   979  O OD1 . ASP A 1 122 ? 13.45436  71.78459 51.13997 1.000 40.37549 ? 122 ASP A OD1 1 
ATOM   980  O OD2 . ASP A 1 122 ? 14.20071  70.69328 52.90359 1.000 55.49092 ? 122 ASP A OD2 1 
ATOM   981  N N   . ARG A 1 123 ? 13.92107  68.97634 48.73535 1.000 30.57083 ? 123 ARG A N   1 
ATOM   982  C CA  . ARG A 1 123 ? 13.39690  67.63923 48.46098 1.000 28.55668 ? 123 ARG A CA  1 
ATOM   983  C C   . ARG A 1 123 ? 13.57076  67.21959 47.00560 1.000 29.72726 ? 123 ARG A C   1 
ATOM   984  O O   . ARG A 1 123 ? 13.07985  66.16950 46.59791 1.000 30.27298 ? 123 ARG A O   1 
ATOM   985  C CB  . ARG A 1 123 ? 11.91618  67.56725 48.83132 1.000 28.88521 ? 123 ARG A CB  1 
ATOM   986  C CG  . ARG A 1 123 ? 11.58294  68.16796 50.19064 1.000 31.05582 ? 123 ARG A CG  1 
ATOM   987  C CD  . ARG A 1 123 ? 12.33453  67.47150 51.32040 1.000 34.59455 ? 123 ARG A CD  1 
ATOM   988  N NE  . ARG A 1 123 ? 11.93995  66.07132 51.46891 1.000 35.48137 ? 123 ARG A NE  1 
ATOM   989  C CZ  . ARG A 1 123 ? 10.87204  65.66300 52.15146 1.000 32.16142 ? 123 ARG A CZ  1 
ATOM   990  N NH1 . ARG A 1 123 ? 10.08367  66.54601 52.74626 1.000 33.60410 ? 123 ARG A NH1 1 
ATOM   991  N NH2 . ARG A 1 123 ? 10.58908  64.37029 52.23800 1.000 33.58801 ? 123 ARG A NH2 1 
ATOM   992  N N   . VAL A 1 124 ? 14.25971  68.04034 46.22187 1.000 28.67886 ? 124 VAL A N   1 
ATOM   993  C CA  . VAL A 1 124 ? 14.45450  67.77289 44.79435 1.000 29.24082 ? 124 VAL A CA  1 
ATOM   994  C C   . VAL A 1 124 ? 15.92517  67.54931 44.46928 1.000 29.90015 ? 124 VAL A C   1 
ATOM   995  O O   . VAL A 1 124 ? 16.77848  68.31266 44.90954 1.000 31.52984 ? 124 VAL A O   1 
ATOM   996  C CB  . VAL A 1 124 ? 13.95215  68.94791 43.91242 1.000 30.60850 ? 124 VAL A CB  1 
ATOM   997  C CG1 . VAL A 1 124 ? 13.86026  68.53343 42.44280 1.000 27.50416 ? 124 VAL A CG1 1 
ATOM   998  C CG2 . VAL A 1 124 ? 12.63276  69.45256 44.40238 1.000 30.28825 ? 124 VAL A CG2 1 
ATOM   999  N N   . VAL A 1 125 ? 16.21960  66.52003 43.68620 1.000 30.01561 ? 125 VAL A N   1 
ATOM   1000 C CA  . VAL A 1 125 ? 17.56715  66.34776 43.15810 1.000 31.17962 ? 125 VAL A CA  1 
ATOM   1001 C C   . VAL A 1 125 ? 17.67779  67.16312 41.87331 1.000 30.38256 ? 125 VAL A C   1 
ATOM   1002 O O   . VAL A 1 125 ? 18.41450  68.14522 41.81180 1.000 28.97282 ? 125 VAL A O   1 
ATOM   1003 C CB  . VAL A 1 125 ? 17.90476  64.86767 42.88566 1.000 30.42544 ? 125 VAL A CB  1 
ATOM   1004 C CG1 . VAL A 1 125 ? 19.35810  64.72855 42.47417 1.000 31.18725 ? 125 VAL A CG1 1 
ATOM   1005 C CG2 . VAL A 1 125 ? 17.62608  64.02099 44.12089 1.000 30.52073 ? 125 VAL A CG2 1 
ATOM   1006 N N   . LYS A 1 126 ? 16.93413  66.74349 40.85183 1.000 28.51261 ? 126 LYS A N   1 
ATOM   1007 C CA  . LYS A 1 126 ? 16.74923  67.52213 39.63068 1.000 26.91649 ? 126 LYS A CA  1 
ATOM   1008 C C   . LYS A 1 126 ? 15.30437  67.38663 39.19642 1.000 26.77801 ? 126 LYS A C   1 
ATOM   1009 O O   . LYS A 1 126 ? 14.59805  66.50098 39.66468 1.000 26.38230 ? 126 LYS A O   1 
ATOM   1010 C CB  . LYS A 1 126 ? 17.67654  67.04452 38.51180 1.000 26.56160 ? 126 LYS A CB  1 
ATOM   1011 C CG  . LYS A 1 126 ? 19.14761  67.26287 38.78059 1.000 28.51412 ? 126 LYS A CG  1 
ATOM   1012 C CD  . LYS A 1 126 ? 19.97407  66.78100 37.61309 1.000 30.95335 ? 126 LYS A CD  1 
ATOM   1013 C CE  . LYS A 1 126 ? 21.45943  66.96351 37.87496 1.000 35.00997 ? 126 LYS A CE  1 
ATOM   1014 N NZ  . LYS A 1 126 ? 22.25421  66.30632 36.80235 1.000 41.06575 ? 126 LYS A NZ  1 
ATOM   1015 N N   . ALA A 1 127 ? 14.86051  68.24550 38.29393 1.000 25.91839 ? 127 ALA A N   1 
ATOM   1016 C CA  . ALA A 1 127 ? 13.49076  68.13569 37.80963 1.000 24.10373 ? 127 ALA A CA  1 
ATOM   1017 C C   . ALA A 1 127 ? 13.42825  68.08211 36.29397 1.000 23.73746 ? 127 ALA A C   1 
ATOM   1018 O O   . ALA A 1 127 ? 14.38806  68.43799 35.60640 1.000 23.63139 ? 127 ALA A O   1 
ATOM   1019 C CB  . ALA A 1 127 ? 12.64595  69.29005 38.33183 1.000 21.20290 ? 127 ALA A CB  1 
ATOM   1020 N N   . ALA A 1 128 ? 12.28576  67.62890 35.78217 1.000 22.73075 ? 128 ALA A N   1 
ATOM   1021 C CA  . ALA A 1 128 ? 11.98803  67.72009 34.36294 1.000 19.74106 ? 128 ALA A CA  1 
ATOM   1022 C C   . ALA A 1 128 ? 10.54242  68.16993 34.15258 1.000 21.13633 ? 128 ALA A C   1 
ATOM   1023 O O   . ALA A 1 128 ? 9.63956   67.75508 34.88065 1.000 23.10135 ? 128 ALA A O   1 
ATOM   1024 C CB  . ALA A 1 128 ? 12.24765  66.38218 33.65700 1.000 19.45225 ? 128 ALA A CB  1 
ATOM   1025 N N   . ILE A 1 129 ? 10.32983  69.03741 33.16819 1.000 20.65467 ? 129 ILE A N   1 
ATOM   1026 C CA  . ILE A 1 129 ? 8.98255   69.46848 32.80641 1.000 21.46710 ? 129 ILE A CA  1 
ATOM   1027 C C   . ILE A 1 129 ? 8.75339   69.34193 31.30196 1.000 23.39676 ? 129 ILE A C   1 
ATOM   1028 O O   . ILE A 1 129 ? 9.59835   69.74114 30.50046 1.000 22.99010 ? 129 ILE A O   1 
ATOM   1029 C CB  . ILE A 1 129 ? 8.71092   70.92546 33.24694 1.000 24.28276 ? 129 ILE A CB  1 
ATOM   1030 C CG1 . ILE A 1 129 ? 9.14666   71.13750 34.70133 1.000 22.33449 ? 129 ILE A CG1 1 
ATOM   1031 C CG2 . ILE A 1 129 ? 7.23177   71.25458 33.09486 1.000 21.78889 ? 129 ILE A CG2 1 
ATOM   1032 C CD1 . ILE A 1 129 ? 8.91292   72.53722 35.21824 1.000 24.23795 ? 129 ILE A CD1 1 
ATOM   1033 N N   . PHE A 1 130 ? 7.61287   68.78240 30.91082 1.000 21.89102 ? 130 PHE A N   1 
ATOM   1034 C CA  . PHE A 1 130 ? 7.27466   68.74293 29.49452 1.000 22.09465 ? 130 PHE A CA  1 
ATOM   1035 C C   . PHE A 1 130 ? 6.21931   69.80900 29.21616 1.000 23.68178 ? 130 PHE A C   1 
ATOM   1036 O O   . PHE A 1 130 ? 5.24870   69.93070 29.95989 1.000 20.84084 ? 130 PHE A O   1 
ATOM   1037 C CB  . PHE A 1 130 ? 6.77490   67.36245 29.06656 1.000 22.79808 ? 130 PHE A CB  1 
ATOM   1038 C CG  . PHE A 1 130 ? 7.65704   66.22369 29.50778 1.000 23.84760 ? 130 PHE A CG  1 
ATOM   1039 C CD1 . PHE A 1 130 ? 9.01194   66.41441 29.74760 1.000 23.61560 ? 130 PHE A CD1 1 
ATOM   1040 C CD2 . PHE A 1 130 ? 7.12866   64.95417 29.67159 1.000 24.64706 ? 130 PHE A CD2 1 
ATOM   1041 C CE1 . PHE A 1 130 ? 9.82365   65.36211 30.16220 1.000 24.42083 ? 130 PHE A CE1 1 
ATOM   1042 C CE2 . PHE A 1 130 ? 7.92985   63.89678 30.08101 1.000 23.37592 ? 130 PHE A CE2 1 
ATOM   1043 C CZ  . PHE A 1 130 ? 9.28150   64.10148 30.33093 1.000 24.84590 ? 130 PHE A CZ  1 
ATOM   1044 N N   . ASP A 1 131 ? 6.42782   70.57556 28.14761 1.000 24.05987 ? 131 ASP A N   1 
ATOM   1045 C CA  . ASP A 1 131 ? 5.57679   71.71488 27.80037 1.000 22.97787 ? 131 ASP A CA  1 
ATOM   1046 C C   . ASP A 1 131 ? 5.24802   72.55808 29.04212 1.000 23.78279 ? 131 ASP A C   1 
ATOM   1047 O O   . ASP A 1 131 ? 4.09276   72.62450 29.46232 1.000 23.72650 ? 131 ASP A O   1 
ATOM   1048 C CB  . ASP A 1 131 ? 4.29826   71.21968 27.10410 1.000 23.63052 ? 131 ASP A CB  1 
ATOM   1049 C CG  . ASP A 1 131 ? 4.60317   70.34348 25.87573 1.000 24.72957 ? 131 ASP A CG  1 
ATOM   1050 O OD1 . ASP A 1 131 ? 5.72779   69.82892 25.75992 1.000 26.97464 ? 131 ASP A OD1 1 
ATOM   1051 O OD2 . ASP A 1 131 ? 3.72730   70.15880 25.01943 1.000 24.89624 ? 131 ASP A OD2 1 
ATOM   1052 N N   . PRO A 1 132 ? 6.28187   73.16722 29.65472 1.000 22.71052 ? 132 PRO A N   1 
ATOM   1053 C CA  . PRO A 1 132 ? 6.12296   73.89401 30.91599 1.000 21.63583 ? 132 PRO A CA  1 
ATOM   1054 C C   . PRO A 1 132 ? 5.20313   75.10900 30.84378 1.000 24.13729 ? 132 PRO A C   1 
ATOM   1055 O O   . PRO A 1 132 ? 5.06952   75.77941 29.80955 1.000 24.01728 ? 132 PRO A O   1 
ATOM   1056 C CB  . PRO A 1 132 ? 7.55520   74.32636 31.26095 1.000 23.74636 ? 132 PRO A CB  1 
ATOM   1057 C CG  . PRO A 1 132 ? 8.30171   74.27359 29.98117 1.000 23.23559 ? 132 PRO A CG  1 
ATOM   1058 C CD  . PRO A 1 132 ? 7.69369   73.12300 29.23607 1.000 22.90971 ? 132 PRO A CD  1 
ATOM   1059 N N   . ILE A 1 133 ? 4.56683   75.35454 31.98447 1.000 22.07476 ? 133 ILE A N   1 
ATOM   1060 C CA  . ILE A 1 133 ? 3.57172   76.39376 32.18664 1.000 22.56512 ? 133 ILE A CA  1 
ATOM   1061 C C   . ILE A 1 133 ? 4.06116   77.29495 33.32480 1.000 23.11087 ? 133 ILE A C   1 
ATOM   1062 O O   . ILE A 1 133 ? 4.40763   76.80090 34.39459 1.000 23.45040 ? 133 ILE A O   1 
ATOM   1063 C CB  . ILE A 1 133 ? 2.19140   75.77374 32.52596 1.000 24.71422 ? 133 ILE A CB  1 
ATOM   1064 C CG1 . ILE A 1 133 ? 1.69191   74.93554 31.34489 1.000 24.24838 ? 133 ILE A CG1 1 
ATOM   1065 C CG2 . ILE A 1 133 ? 1.17831   76.84256 32.91345 1.000 21.09486 ? 133 ILE A CG2 1 
ATOM   1066 C CD1 . ILE A 1 133 ? 0.46170   74.10825 31.64538 1.000 24.58822 ? 133 ILE A CD1 1 
ATOM   1067 N N   . THR A 1 134 ? 4.12861   78.60257 33.08062 1.000 23.25331 ? 134 THR A N   1 
ATOM   1068 C CA  . THR A 1 134 ? 4.66538   79.54596 34.06372 1.000 21.97750 ? 134 THR A CA  1 
ATOM   1069 C C   . THR A 1 134 ? 3.55116   80.47359 34.53638 1.000 23.19108 ? 134 THR A C   1 
ATOM   1070 O O   . THR A 1 134 ? 2.44783   80.42347 33.99523 1.000 25.31105 ? 134 THR A O   1 
ATOM   1071 C CB  . THR A 1 134 ? 5.83134   80.38763 33.47402 1.000 22.39745 ? 134 THR A CB  1 
ATOM   1072 O OG1 . THR A 1 134 ? 5.30742   81.44507 32.66340 1.000 24.54171 ? 134 THR A OG1 1 
ATOM   1073 C CG2 . THR A 1 134 ? 6.77615   79.52781 32.65109 1.000 24.57890 ? 134 THR A CG2 1 
ATOM   1074 N N   . PRO A 1 135 ? 3.82459   81.31705 35.54623 1.000 23.73128 ? 135 PRO A N   1 
ATOM   1075 C CA  . PRO A 1 135 ? 2.83017   82.30607 35.98934 1.000 24.13349 ? 135 PRO A CA  1 
ATOM   1076 C C   . PRO A 1 135 ? 2.30318   83.27654 34.92939 1.000 25.37430 ? 135 PRO A C   1 
ATOM   1077 O O   . PRO A 1 135 ? 1.30021   83.93883 35.18940 1.000 26.92191 ? 135 PRO A O   1 
ATOM   1078 C CB  . PRO A 1 135 ? 3.58647   83.06915 37.07076 1.000 27.46793 ? 135 PRO A CB  1 
ATOM   1079 C CG  . PRO A 1 135 ? 4.39949   82.00273 37.72079 1.000 24.05381 ? 135 PRO A CG  1 
ATOM   1080 C CD  . PRO A 1 135 ? 4.88513   81.14482 36.56115 1.000 24.06345 ? 135 PRO A CD  1 
ATOM   1081 N N   . ASP A 1 136 ? 2.94544   83.34754 33.76894 1.000 24.71539 ? 136 ASP A N   1 
ATOM   1082 C CA  . ASP A 1 136 ? 2.51433   84.24859 32.70351 1.000 26.90398 ? 136 ASP A CA  1 
ATOM   1083 C C   . ASP A 1 136 ? 1.64071   83.55382 31.65765 1.000 25.05440 ? 136 ASP A C   1 
ATOM   1084 O O   . ASP A 1 136 ? 1.29682   84.14513 30.63984 1.000 24.86020 ? 136 ASP A O   1 
ATOM   1085 C CB  . ASP A 1 136 ? 3.73613   84.87365 32.03498 1.000 26.48483 ? 136 ASP A CB  1 
ATOM   1086 C CG  . ASP A 1 136 ? 4.49653   85.79404 32.97496 1.000 27.66717 ? 136 ASP A CG  1 
ATOM   1087 O OD1 . ASP A 1 136 ? 3.84777   86.57233 33.69958 1.000 31.53015 ? 136 ASP A OD1 1 
ATOM   1088 O OD2 . ASP A 1 136 ? 5.73063   85.73128 33.00036 1.000 28.10862 ? 136 ASP A OD2 1 
ATOM   1089 N N   . PHE A 1 137 ? 1.29523   82.29859 31.92864 1.000 22.42836 ? 137 PHE A N   1 
ATOM   1090 C CA  . PHE A 1 137 ? 0.42916   81.48001 31.07338 1.000 23.69353 ? 137 PHE A CA  1 
ATOM   1091 C C   . PHE A 1 137 ? -0.97111  82.06208 30.86974 1.000 24.64202 ? 137 PHE A C   1 
ATOM   1092 O O   . PHE A 1 137 ? -1.48765  82.11024 29.74471 1.000 23.91165 ? 137 PHE A O   1 
ATOM   1093 C CB  . PHE A 1 137 ? 0.29701   80.09033 31.68765 1.000 22.60330 ? 137 PHE A CB  1 
ATOM   1094 C CG  . PHE A 1 137 ? -0.41510  79.08661 30.82511 1.000 21.59415 ? 137 PHE A CG  1 
ATOM   1095 C CD1 . PHE A 1 137 ? 0.11167   78.69808 29.60632 1.000 21.67824 ? 137 PHE A CD1 1 
ATOM   1096 C CD2 . PHE A 1 137 ? -1.57736  78.47760 31.27325 1.000 22.03122 ? 137 PHE A CD2 1 
ATOM   1097 C CE1 . PHE A 1 137 ? -0.52046  77.73608 28.82822 1.000 22.08901 ? 137 PHE A CE1 1 
ATOM   1098 C CE2 . PHE A 1 137 ? -2.21978  77.52260 30.50333 1.000 24.16623 ? 137 PHE A CE2 1 
ATOM   1099 C CZ  . PHE A 1 137 ? -1.68570  77.14670 29.27846 1.000 23.18742 ? 137 PHE A CZ  1 
ATOM   1100 N N   . GLY A 1 138 ? -1.57393  82.47330 31.97908 1.000 26.38367 ? 138 GLY A N   1 
ATOM   1101 C CA  . GLY A 1 138 ? -2.96220  82.90110 32.02475 1.000 26.75170 ? 138 GLY A CA  1 
ATOM   1102 C C   . GLY A 1 138 ? -3.43477  83.82250 30.91726 1.000 25.26490 ? 138 GLY A C   1 
ATOM   1103 O O   . GLY A 1 138 ? -4.37748  83.48257 30.21387 1.000 27.50487 ? 138 GLY A O   1 
ATOM   1104 N N   . PRO A 1 139 ? -2.80319  85.00134 30.76990 1.000 28.11159 ? 139 PRO A N   1 
ATOM   1105 C CA  . PRO A 1 139 ? -3.21437  85.94743 29.72299 1.000 26.22073 ? 139 PRO A CA  1 
ATOM   1106 C C   . PRO A 1 139 ? -3.12489  85.38402 28.30435 1.000 27.11267 ? 139 PRO A C   1 
ATOM   1107 O O   . PRO A 1 139 ? -3.93933  85.75415 27.46547 1.000 27.26666 ? 139 PRO A O   1 
ATOM   1108 C CB  . PRO A 1 139 ? -2.24215  87.11310 29.90584 1.000 27.64947 ? 139 PRO A CB  1 
ATOM   1109 C CG  . PRO A 1 139 ? -1.92321  87.08856 31.35696 1.000 29.63078 ? 139 PRO A CG  1 
ATOM   1110 C CD  . PRO A 1 139 ? -1.87615  85.62380 31.73392 1.000 27.07001 ? 139 PRO A CD  1 
ATOM   1111 N N   . PHE A 1 140 ? -2.15699  84.51504 28.03453 1.000 25.97640 ? 140 PHE A N   1 
ATOM   1112 C CA  . PHE A 1 140 ? -2.09417  83.86787 26.73098 1.000 22.96842 ? 140 PHE A CA  1 
ATOM   1113 C C   . PHE A 1 140 ? -3.23539  82.85562 26.56777 1.000 24.46173 ? 140 PHE A C   1 
ATOM   1114 O O   . PHE A 1 140 ? -3.96918  82.88523 25.58758 1.000 23.30600 ? 140 PHE A O   1 
ATOM   1115 C CB  . PHE A 1 140 ? -0.74428  83.16982 26.52613 1.000 23.24850 ? 140 PHE A CB  1 
ATOM   1116 C CG  . PHE A 1 140 ? -0.72334  82.23244 25.34417 1.000 24.28359 ? 140 PHE A CG  1 
ATOM   1117 C CD1 . PHE A 1 140 ? -0.51276  82.71498 24.06605 1.000 26.58195 ? 140 PHE A CD1 1 
ATOM   1118 C CD2 . PHE A 1 140 ? -0.91816  80.87575 25.51369 1.000 24.77443 ? 140 PHE A CD2 1 
ATOM   1119 C CE1 . PHE A 1 140 ? -0.49626  81.86249 22.97462 1.000 28.59452 ? 140 PHE A CE1 1 
ATOM   1120 C CE2 . PHE A 1 140 ? -0.90304  80.01417 24.42377 1.000 24.12504 ? 140 PHE A CE2 1 
ATOM   1121 C CZ  . PHE A 1 140 ? -0.69408  80.51144 23.15580 1.000 24.39576 ? 140 PHE A CZ  1 
ATOM   1122 N N   . TYR A 1 141 ? -3.37212  81.97192 27.54890 1.000 23.46577 ? 141 TYR A N   1 
ATOM   1123 C CA  . TYR A 1 141 ? -4.23101  80.80030 27.43988 1.000 21.98758 ? 141 TYR A CA  1 
ATOM   1124 C C   . TYR A 1 141 ? -5.71576  81.15934 27.29947 1.000 23.53534 ? 141 TYR A C   1 
ATOM   1125 O O   . TYR A 1 141 ? -6.43271  80.57887 26.47789 1.000 22.61365 ? 141 TYR A O   1 
ATOM   1126 C CB  . TYR A 1 141 ? -3.99891  79.90973 28.65908 1.000 21.94027 ? 141 TYR A CB  1 
ATOM   1127 C CG  . TYR A 1 141 ? -4.87080  78.68235 28.77361 1.000 21.77633 ? 141 TYR A CG  1 
ATOM   1128 C CD1 . TYR A 1 141 ? -4.61939  77.54775 28.00742 1.000 20.94267 ? 141 TYR A CD1 1 
ATOM   1129 C CD2 . TYR A 1 141 ? -5.91269  78.63822 29.69294 1.000 22.45571 ? 141 TYR A CD2 1 
ATOM   1130 C CE1 . TYR A 1 141 ? -5.38414  76.41697 28.14806 1.000 21.24723 ? 141 TYR A CE1 1 
ATOM   1131 C CE2 . TYR A 1 141 ? -6.69074  77.50801 29.83385 1.000 23.06106 ? 141 TYR A CE2 1 
ATOM   1132 C CZ  . TYR A 1 141 ? -6.42000  76.40387 29.05797 1.000 22.96872 ? 141 TYR A CZ  1 
ATOM   1133 O OH  . TYR A 1 141 ? -7.19129  75.28678 29.19523 1.000 23.01364 ? 141 TYR A OH  1 
ATOM   1134 N N   . LEU A 1 142 ? -6.16982  82.13071 28.08009 1.000 23.67292 ? 142 LEU A N   1 
ATOM   1135 C CA  . LEU A 1 142 ? -7.55696  82.57676 27.99448 1.000 25.52056 ? 142 LEU A CA  1 
ATOM   1136 C C   . LEU A 1 142 ? -7.67950  83.81281 27.10298 1.000 23.79620 ? 142 LEU A C   1 
ATOM   1137 O O   . LEU A 1 142 ? -8.72773  84.44007 27.04739 1.000 25.82692 ? 142 LEU A O   1 
ATOM   1138 C CB  . LEU A 1 142 ? -8.12021  82.86326 29.39459 1.000 23.31654 ? 142 LEU A CB  1 
ATOM   1139 C CG  . LEU A 1 142 ? -8.24969  81.64913 30.32676 1.000 26.16890 ? 142 LEU A CG  1 
ATOM   1140 C CD1 . LEU A 1 142 ? -8.81679  82.04055 31.67962 1.000 30.90986 ? 142 LEU A CD1 1 
ATOM   1141 C CD2 . LEU A 1 142 ? -9.08435  80.54187 29.69081 1.000 25.65788 ? 142 LEU A CD2 1 
ATOM   1142 N N   . GLY A 1 143 ? -6.60137  84.15131 26.40308 1.000 25.60499 ? 143 GLY A N   1 
ATOM   1143 C CA  . GLY A 1 143 ? -6.60866  85.29170 25.50343 1.000 23.47302 ? 143 GLY A CA  1 
ATOM   1144 C C   . GLY A 1 143 ? -7.13300  84.94399 24.11664 1.000 28.11044 ? 143 GLY A C   1 
ATOM   1145 O O   . GLY A 1 143 ? -7.54870  83.81601 23.86447 1.000 26.15737 ? 143 GLY A O   1 
ATOM   1146 N N   . PHE A 1 144 ? -7.11827  85.92918 23.22482 1.000 28.05650 ? 144 PHE A N   1 
ATOM   1147 C CA  . PHE A 1 144 ? -7.50665  85.74934 21.83340 1.000 25.52412 ? 144 PHE A CA  1 
ATOM   1148 C C   . PHE A 1 144 ? -6.22767  85.73580 21.01558 1.000 23.98616 ? 144 PHE A C   1 
ATOM   1149 O O   . PHE A 1 144 ? -5.37939  86.59654 21.20662 1.000 26.69202 ? 144 PHE A O   1 
ATOM   1150 C CB  . PHE A 1 144 ? -8.45382  86.87249 21.37945 1.000 24.45114 ? 144 PHE A CB  1 
ATOM   1151 C CG  . PHE A 1 144 ? -8.84268  86.79791 19.92010 1.000 26.56040 ? 144 PHE A CG  1 
ATOM   1152 C CD1 . PHE A 1 144 ? -8.01447  87.31143 18.93323 1.000 26.20237 ? 144 PHE A CD1 1 
ATOM   1153 C CD2 . PHE A 1 144 ? -10.04254 86.20830 19.53794 1.000 27.06632 ? 144 PHE A CD2 1 
ATOM   1154 C CE1 . PHE A 1 144 ? -8.37449  87.24090 17.58759 1.000 24.58110 ? 144 PHE A CE1 1 
ATOM   1155 C CE2 . PHE A 1 144 ? -10.40684 86.13742 18.19531 1.000 27.48877 ? 144 PHE A CE2 1 
ATOM   1156 C CZ  . PHE A 1 144 ? -9.57246  86.65523 17.22225 1.000 25.07068 ? 144 PHE A CZ  1 
ATOM   1157 N N   . PRO A 1 145 ? -6.08427  84.77515 20.08951 1.000 22.91674 ? 145 PRO A N   1 
ATOM   1158 C CA  . PRO A 1 145 ? -7.05845  83.76568 19.66819 1.000 25.21711 ? 145 PRO A CA  1 
ATOM   1159 C C   . PRO A 1 145 ? -6.98187  82.39967 20.37290 1.000 24.46494 ? 145 PRO A C   1 
ATOM   1160 O O   . PRO A 1 145 ? -7.62321  81.46417 19.89073 1.000 23.05402 ? 145 PRO A O   1 
ATOM   1161 C CB  . PRO A 1 145 ? -6.72323  83.59461 18.18564 1.000 24.06381 ? 145 PRO A CB  1 
ATOM   1162 C CG  . PRO A 1 145 ? -5.23177  83.75216 18.15231 1.000 22.99836 ? 145 PRO A CG  1 
ATOM   1163 C CD  . PRO A 1 145 ? -4.89896  84.77417 19.21561 1.000 24.94420 ? 145 PRO A CD  1 
ATOM   1164 N N   . HIS A 1 146 ? -6.24119  82.26664 21.47063 1.000 23.98440 ? 146 HIS A N   1 
ATOM   1165 C CA  . HIS A 1 146 ? -6.06060  80.93020 22.04009 1.000 24.13411 ? 146 HIS A CA  1 
ATOM   1166 C C   . HIS A 1 146 ? -7.34232  80.31935 22.62713 1.000 20.32293 ? 146 HIS A C   1 
ATOM   1167 O O   . HIS A 1 146 ? -7.37797  79.11195 22.86972 1.000 22.34103 ? 146 HIS A O   1 
ATOM   1168 C CB  . HIS A 1 146 ? -4.97295  80.91283 23.11245 1.000 20.43494 ? 146 HIS A CB  1 
ATOM   1169 C CG  . HIS A 1 146 ? -4.37589  79.55187 23.32649 1.000 19.58625 ? 146 HIS A CG  1 
ATOM   1170 N ND1 . HIS A 1 146 ? -3.63044  78.90710 22.36172 1.000 22.09026 ? 146 HIS A ND1 1 
ATOM   1171 C CD2 . HIS A 1 146 ? -4.44677  78.69868 24.37684 1.000 20.84481 ? 146 HIS A CD2 1 
ATOM   1172 C CE1 . HIS A 1 146 ? -3.24797  77.72574 22.81561 1.000 18.47251 ? 146 HIS A CE1 1 
ATOM   1173 N NE2 . HIS A 1 146 ? -3.73397  77.57180 24.03443 1.000 21.18215 ? 146 HIS A NE2 1 
ATOM   1174 N N   . ILE A 1 147 ? -8.38887  81.12186 22.83437 1.000 21.60922 ? 147 ILE A N   1 
ATOM   1175 C CA  . ILE A 1 147 ? -9.67840  80.56461 23.26163 1.000 21.13599 ? 147 ILE A CA  1 
ATOM   1176 C C   . ILE A 1 147 ? -10.22266 79.52538 22.28304 1.000 21.58174 ? 147 ILE A C   1 
ATOM   1177 O O   . ILE A 1 147 ? -11.06858 78.71072 22.65074 1.000 22.01171 ? 147 ILE A O   1 
ATOM   1178 C CB  . ILE A 1 147 ? -10.77313 81.63752 23.46630 1.000 25.23085 ? 147 ILE A CB  1 
ATOM   1179 C CG1 . ILE A 1 147 ? -11.24848 82.23203 22.13072 1.000 26.48604 ? 147 ILE A CG1 1 
ATOM   1180 C CG2 . ILE A 1 147 ? -10.30081 82.68682 24.43264 1.000 30.25900 ? 147 ILE A CG2 1 
ATOM   1181 C CD1 . ILE A 1 147 ? -10.45020 83.38226 21.65370 1.000 31.44120 ? 147 ILE A CD1 1 
ATOM   1182 N N   . ALA A 1 148 ? -9.73269  79.53217 21.04816 1.000 21.64475 ? 148 ALA A N   1 
ATOM   1183 C CA  . ALA A 1 148 ? -10.10822 78.48960 20.10234 1.000 21.27804 ? 148 ALA A CA  1 
ATOM   1184 C C   . ALA A 1 148 ? -9.63182  77.13415 20.61276 1.000 21.81872 ? 148 ALA A C   1 
ATOM   1185 O O   . ALA A 1 148 ? -10.21336 76.10793 20.29272 1.000 21.02930 ? 148 ALA A O   1 
ATOM   1186 C CB  . ALA A 1 148 ? -9.53434  78.77028 18.71975 1.000 22.35844 ? 148 ALA A CB  1 
ATOM   1187 N N   . GLU A 1 149 ? -8.57284  77.14850 21.41880 1.000 22.21800 ? 149 GLU A N   1 
ATOM   1188 C CA  . GLU A 1 149 ? -8.02380  75.92908 21.99296 1.000 22.90314 ? 149 GLU A CA  1 
ATOM   1189 C C   . GLU A 1 149 ? -8.42519  75.73325 23.45367 1.000 20.59243 ? 149 GLU A C   1 
ATOM   1190 O O   . GLU A 1 149 ? -8.54525  74.59892 23.90618 1.000 23.74875 ? 149 GLU A O   1 
ATOM   1191 C CB  . GLU A 1 149 ? -6.49345  75.92541 21.89073 1.000 21.17243 ? 149 GLU A CB  1 
ATOM   1192 C CG  . GLU A 1 149 ? -5.95625  75.97905 20.47913 1.000 22.20925 ? 149 GLU A CG  1 
ATOM   1193 C CD  . GLU A 1 149 ? -6.28152  74.73031 19.68880 1.000 24.48544 ? 149 GLU A CD  1 
ATOM   1194 O OE1 . GLU A 1 149 ? -6.37468  74.82231 18.44903 1.000 29.11378 ? 149 GLU A OE1 1 
ATOM   1195 O OE2 . GLU A 1 149 ? -6.46087  73.66354 20.30670 1.000 24.09233 ? 149 GLU A OE2 1 
ATOM   1196 N N   . SER A 1 150 ? -8.61562  76.82783 24.18929 1.000 19.41829 ? 150 SER A N   1 
ATOM   1197 C CA  . SER A 1 150 ? -8.84578  76.74495 25.63686 1.000 20.73735 ? 150 SER A CA  1 
ATOM   1198 C C   . SER A 1 150 ? -10.31454 76.75569 26.07501 1.000 20.65916 ? 150 SER A C   1 
ATOM   1199 O O   . SER A 1 150 ? -10.58960 76.74742 27.27293 1.000 23.25755 ? 150 SER A O   1 
ATOM   1200 C CB  . SER A 1 150 ? -8.11810  77.88511 26.34835 1.000 22.11662 ? 150 SER A CB  1 
ATOM   1201 O OG  . SER A 1 150 ? -8.59995  79.14809 25.91646 1.000 23.29283 ? 150 SER A OG  1 
ATOM   1202 N N   . TRP A 1 151 ? -11.23419 76.77228 25.11139 1.000 22.29101 ? 151 TRP A N   1 
ATOM   1203 C CA  . TRP A 1 151 ? -12.68038 76.81586 25.36580 1.000 22.28121 ? 151 TRP A CA  1 
ATOM   1204 C C   . TRP A 1 151 ? -13.12751 75.77483 26.40358 1.000 21.66578 ? 151 TRP A C   1 
ATOM   1205 O O   . TRP A 1 151 ? -14.02360 76.03001 27.19246 1.000 20.28404 ? 151 TRP A O   1 
ATOM   1206 C CB  . TRP A 1 151 ? -13.46712 76.59311 24.05185 1.000 19.91944 ? 151 TRP A CB  1 
ATOM   1207 C CG  . TRP A 1 151 ? -13.20075 75.22354 23.48328 1.000 19.91900 ? 151 TRP A CG  1 
ATOM   1208 C CD1 . TRP A 1 151 ? -12.23707 74.89085 22.57676 1.000 19.49928 ? 151 TRP A CD1 1 
ATOM   1209 C CD2 . TRP A 1 151 ? -13.85841 73.99644 23.83503 1.000 19.78649 ? 151 TRP A CD2 1 
ATOM   1210 N NE1 . TRP A 1 151 ? -12.26173 73.54032 22.33390 1.000 21.34792 ? 151 TRP A NE1 1 
ATOM   1211 C CE2 . TRP A 1 151 ? -13.24558 72.96811 23.09403 1.000 19.92091 ? 151 TRP A CE2 1 
ATOM   1212 C CE3 . TRP A 1 151 ? -14.91227 73.67047 24.69571 1.000 21.94468 ? 151 TRP A CE3 1 
ATOM   1213 C CZ2 . TRP A 1 151 ? -13.64584 71.64228 23.18748 1.000 20.18877 ? 151 TRP A CZ2 1 
ATOM   1214 C CZ3 . TRP A 1 151 ? -15.28929 72.34633 24.81043 1.000 19.71924 ? 151 TRP A CZ3 1 
ATOM   1215 C CH2 . TRP A 1 151 ? -14.66116 71.34957 24.05526 1.000 21.52948 ? 151 TRP A CH2 1 
ATOM   1216 N N   . TYR A 1 152 ? -12.49561 74.60483 26.39162 1.000 20.31132 ? 152 TYR A N   1 
ATOM   1217 C CA  . TYR A 1 152 ? -12.91361 73.49289 27.24488 1.000 20.02062 ? 152 TYR A CA  1 
ATOM   1218 C C   . TYR A 1 152 ? -12.74114 73.82734 28.72732 1.000 21.59985 ? 152 TYR A C   1 
ATOM   1219 O O   . TYR A 1 152 ? -13.48896 73.32768 29.56519 1.000 22.12332 ? 152 TYR A O   1 
ATOM   1220 C CB  . TYR A 1 152 ? -12.14168 72.21293 26.87374 1.000 20.39539 ? 152 TYR A CB  1 
ATOM   1221 C CG  . TYR A 1 152 ? -10.68750 72.31837 27.21819 1.000 20.96941 ? 152 TYR A CG  1 
ATOM   1222 C CD1 . TYR A 1 152 ? -9.80594  73.00174 26.38572 1.000 21.50433 ? 152 TYR A CD1 1 
ATOM   1223 C CD2 . TYR A 1 152 ? -10.19717 71.76909 28.38261 1.000 19.53061 ? 152 TYR A CD2 1 
ATOM   1224 C CE1 . TYR A 1 152 ? -8.48048  73.13243 26.71750 1.000 20.79899 ? 152 TYR A CE1 1 
ATOM   1225 C CE2 . TYR A 1 152 ? -8.87210  71.89004 28.71740 1.000 20.48312 ? 152 TYR A CE2 1 
ATOM   1226 C CZ  . TYR A 1 152 ? -8.02169  72.57476 27.88313 1.000 19.39084 ? 152 TYR A CZ  1 
ATOM   1227 O OH  . TYR A 1 152 ? -6.70162  72.70770 28.21852 1.000 21.53191 ? 152 TYR A OH  1 
ATOM   1228 N N   . SER A 1 153 ? -11.77431 74.68627 29.04930 1.000 20.93741 ? 153 SER A N   1 
ATOM   1229 C CA  . SER A 1 153 ? -11.54663 75.07572 30.44047 1.000 20.84962 ? 153 SER A CA  1 
ATOM   1230 C C   . SER A 1 153 ? -12.76075 75.83238 30.98355 1.000 20.59873 ? 153 SER A C   1 
ATOM   1231 O O   . SER A 1 153 ? -13.03164 75.82711 32.18695 1.000 20.30479 ? 153 SER A O   1 
ATOM   1232 C CB  . SER A 1 153 ? -10.27845 75.93331 30.57924 1.000 19.69510 ? 153 SER A CB  1 
ATOM   1233 O OG  . SER A 1 153 ? -10.46455 77.22334 30.02407 1.000 22.68622 ? 153 SER A OG  1 
ATOM   1234 N N   . GLN A 1 154 ? -13.49699 76.47525 30.08778 1.000 20.89899 ? 154 GLN A N   1 
ATOM   1235 C CA  . GLN A 1 154 ? -14.68030 77.22706 30.48660 1.000 20.91805 ? 154 GLN A CA  1 
ATOM   1236 C C   . GLN A 1 154 ? -15.95173 76.36663 30.42252 1.000 20.85819 ? 154 GLN A C   1 
ATOM   1237 O O   . GLN A 1 154 ? -16.84704 76.52277 31.25073 1.000 20.29204 ? 154 GLN A O   1 
ATOM   1238 C CB  . GLN A 1 154 ? -14.80979 78.47732 29.61895 1.000 20.85692 ? 154 GLN A CB  1 
ATOM   1239 C CG  . GLN A 1 154 ? -13.55661 79.34760 29.68279 1.000 21.32140 ? 154 GLN A CG  1 
ATOM   1240 C CD  . GLN A 1 154 ? -13.20209 79.72073 31.10576 1.000 23.01784 ? 154 GLN A CD  1 
ATOM   1241 O OE1 . GLN A 1 154 ? -13.98500 80.37557 31.78649 1.000 24.47141 ? 154 GLN A OE1 1 
ATOM   1242 N NE2 . GLN A 1 154 ? -12.03166 79.27415 31.57777 1.000 20.79108 ? 154 GLN A NE2 1 
ATOM   1243 N N   . PHE A 1 155 ? -16.02465 75.46720 29.44159 1.000 19.03536 ? 155 PHE A N   1 
ATOM   1244 C CA  . PHE A 1 155 ? -17.07452 74.43451 29.40900 1.000 20.78790 ? 155 PHE A CA  1 
ATOM   1245 C C   . PHE A 1 155 ? -17.15795 73.69386 30.75741 1.000 21.99313 ? 155 PHE A C   1 
ATOM   1246 O O   . PHE A 1 155 ? -18.24223 73.45571 31.30246 1.000 19.81992 ? 155 PHE A O   1 
ATOM   1247 C CB  . PHE A 1 155 ? -16.79501 73.44574 28.26354 1.000 18.90601 ? 155 PHE A CB  1 
ATOM   1248 C CG  . PHE A 1 155 ? -17.76757 72.29813 28.17776 1.000 21.13763 ? 155 PHE A CG  1 
ATOM   1249 C CD1 . PHE A 1 155 ? -19.13412 72.51710 28.24021 1.000 20.09573 ? 155 PHE A CD1 1 
ATOM   1250 C CD2 . PHE A 1 155 ? -17.31042 70.99784 27.99761 1.000 19.52563 ? 155 PHE A CD2 1 
ATOM   1251 C CE1 . PHE A 1 155 ? -20.02616 71.47170 28.13871 1.000 20.64136 ? 155 PHE A CE1 1 
ATOM   1252 C CE2 . PHE A 1 155 ? -18.20182 69.94636 27.90066 1.000 20.00911 ? 155 PHE A CE2 1 
ATOM   1253 C CZ  . PHE A 1 155 ? -19.56675 70.18967 27.95961 1.000 18.59808 ? 155 PHE A CZ  1 
ATOM   1254 N N   . HIS A 1 156 ? -15.99178 73.36579 31.30155 1.000 20.74572 ? 156 HIS A N   1 
ATOM   1255 C CA  . HIS A 1 156 ? -15.89039 72.61230 32.55546 1.000 20.32537 ? 156 HIS A CA  1 
ATOM   1256 C C   . HIS A 1 156 ? -16.40330 73.36063 33.78484 1.000 20.07645 ? 156 HIS A C   1 
ATOM   1257 O O   . HIS A 1 156 ? -16.58454 72.75394 34.83572 1.000 21.10277 ? 156 HIS A O   1 
ATOM   1258 C CB  . HIS A 1 156 ? -14.43416 72.19640 32.79771 1.000 18.25130 ? 156 HIS A CB  1 
ATOM   1259 C CG  . HIS A 1 156 ? -13.91573 71.21868 31.79433 1.000 18.94127 ? 156 HIS A CG  1 
ATOM   1260 N ND1 . HIS A 1 156 ? -12.60162 70.80929 31.76295 1.000 20.28425 ? 156 HIS A ND1 1 
ATOM   1261 C CD2 . HIS A 1 156 ? -14.53461 70.57571 30.77486 1.000 20.91861 ? 156 HIS A CD2 1 
ATOM   1262 C CE1 . HIS A 1 156 ? -12.43402 69.95441 30.76972 1.000 19.95090 ? 156 HIS A CE1 1 
ATOM   1263 N NE2 . HIS A 1 156 ? -13.59263 69.79765 30.15299 1.000 19.57206 ? 156 HIS A NE2 1 
ATOM   1264 N N   . GLN A 1 157 ? -16.61330 74.66894 33.65929 1.000 19.52197 ? 157 GLN A N   1 
ATOM   1265 C CA  . GLN A 1 157 ? -17.17649 75.45824 34.74670 1.000 21.09540 ? 157 GLN A CA  1 
ATOM   1266 C C   . GLN A 1 157 ? -18.66037 75.13178 34.92857 1.000 21.83757 ? 157 GLN A C   1 
ATOM   1267 O O   . GLN A 1 157 ? -19.23709 75.43748 35.96639 1.000 20.75294 ? 157 GLN A O   1 
ATOM   1268 C CB  . GLN A 1 157 ? -17.01840 76.97132 34.49940 1.000 22.03972 ? 157 GLN A CB  1 
ATOM   1269 C CG  . GLN A 1 157 ? -15.61235 77.46106 34.12496 1.000 19.80685 ? 157 GLN A CG  1 
ATOM   1270 C CD  . GLN A 1 157 ? -14.60938 77.33002 35.25589 1.000 20.60612 ? 157 GLN A CD  1 
ATOM   1271 O OE1 . GLN A 1 157 ? -14.95111 77.46237 36.42822 1.000 21.35705 ? 157 GLN A OE1 1 
ATOM   1272 N NE2 . GLN A 1 157 ? -13.36248 77.05295 34.90427 1.000 21.37709 ? 157 GLN A NE2 1 
ATOM   1273 N N   . THR A 1 158 ? -19.28581 74.53116 33.92055 1.000 21.82390 ? 158 THR A N   1 
ATOM   1274 C CA  . THR A 1 158 ? -20.74105 74.35559 33.96705 1.000 20.92309 ? 158 THR A CA  1 
ATOM   1275 C C   . THR A 1 158 ? -21.12693 73.01254 34.54880 1.000 22.45493 ? 158 THR A C   1 
ATOM   1276 O O   . THR A 1 158 ? -20.41359 72.02973 34.37353 1.000 22.66889 ? 158 THR A O   1 
ATOM   1277 C CB  . THR A 1 158 ? -21.38960 74.47623 32.57798 1.000 21.32640 ? 158 THR A CB  1 
ATOM   1278 O OG1 . THR A 1 158 ? -21.05028 73.33621 31.77735 1.000 21.46269 ? 158 THR A OG1 1 
ATOM   1279 C CG2 . THR A 1 158 ? -20.95426 75.76169 31.87721 1.000 19.09767 ? 158 THR A CG2 1 
ATOM   1280 N N   . ASP A 1 159 ? -22.26043 72.96447 35.23884 1.000 23.42099 ? 159 ASP A N   1 
ATOM   1281 C CA  . ASP A 1 159 ? -22.78251 71.68425 35.70364 1.000 24.62004 ? 159 ASP A CA  1 
ATOM   1282 C C   . ASP A 1 159 ? -23.12854 70.79200 34.51979 1.000 24.90820 ? 159 ASP A C   1 
ATOM   1283 O O   . ASP A 1 159 ? -22.99452 69.56889 34.58944 1.000 23.97291 ? 159 ASP A O   1 
ATOM   1284 C CB  . ASP A 1 159 ? -24.00830 71.88274 36.59414 1.000 25.65398 ? 159 ASP A CB  1 
ATOM   1285 C CG  . ASP A 1 159 ? -23.64400 72.43005 37.95885 1.000 29.35645 ? 159 ASP A CG  1 
ATOM   1286 O OD1 . ASP A 1 159 ? -22.52203 72.14895 38.43615 1.000 31.34274 ? 159 ASP A OD1 1 
ATOM   1287 O OD2 . ASP A 1 159 ? -24.46681 73.15179 38.54366 1.000 31.28142 ? 159 ASP A OD2 1 
ATOM   1288 N N   . MET A 1 160 ? -23.56903 71.40744 33.43031 1.000 23.04948 ? 160 MET A N   1 
ATOM   1289 C CA  . MET A 1 160 ? -23.99706 70.64235 32.26994 1.000 22.59619 ? 160 MET A CA  1 
ATOM   1290 C C   . MET A 1 160 ? -22.85158 69.82117 31.68640 1.000 22.63021 ? 160 MET A C   1 
ATOM   1291 O O   . MET A 1 160 ? -23.08245 68.73345 31.17953 1.000 24.35965 ? 160 MET A O   1 
ATOM   1292 C CB  . MET A 1 160 ? -24.59339 71.55902 31.19723 1.000 22.38530 ? 160 MET A CB  1 
ATOM   1293 C CG  . MET A 1 160 ? -25.05266 70.80649 29.94393 1.000 21.88274 ? 160 MET A CG  1 
ATOM   1294 S SD  . MET A 1 160 ? -23.75382 70.65370 28.69133 1.000 21.54905 ? 160 MET A SD  1 
ATOM   1295 C CE  . MET A 1 160 ? -23.81777 72.31534 27.99627 1.000 20.04260 ? 160 MET A CE  1 
ATOM   1296 N N   . SER A 1 161 ? -21.62127 70.32686 31.75790 1.000 21.04847 ? 161 SER A N   1 
ATOM   1297 C CA  . SER A 1 161 ? -20.50052 69.56059 31.23543 1.000 20.88149 ? 161 SER A CA  1 
ATOM   1298 C C   . SER A 1 161 ? -20.37825 68.20416 31.93616 1.000 20.20939 ? 161 SER A C   1 
ATOM   1299 O O   . SER A 1 161 ? -20.18782 67.19739 31.27496 1.000 22.13151 ? 161 SER A O   1 
ATOM   1300 C CB  . SER A 1 161 ? -19.18365 70.33637 31.35449 1.000 19.49995 ? 161 SER A CB  1 
ATOM   1301 O OG  . SER A 1 161 ? -18.87690 70.63697 32.69674 1.000 21.17254 ? 161 SER A OG  1 
ATOM   1302 N N   . VAL A 1 162 ? -20.49653 68.17472 33.25915 1.000 20.85343 ? 162 VAL A N   1 
ATOM   1303 C CA  . VAL A 1 162 ? -20.43004 66.90132 33.97904 1.000 21.14579 ? 162 VAL A CA  1 
ATOM   1304 C C   . VAL A 1 162 ? -21.59755 65.99374 33.58204 1.000 22.72440 ? 162 VAL A C   1 
ATOM   1305 O O   . VAL A 1 162 ? -21.40826 64.81810 33.28669 1.000 22.42618 ? 162 VAL A O   1 
ATOM   1306 C CB  . VAL A 1 162 ? -20.44482 67.09372 35.52188 1.000 22.55282 ? 162 VAL A CB  1 
ATOM   1307 C CG1 . VAL A 1 162 ? -20.41974 65.73523 36.24253 1.000 24.13971 ? 162 VAL A CG1 1 
ATOM   1308 C CG2 . VAL A 1 162 ? -19.27812 67.96086 35.97906 1.000 21.96619 ? 162 VAL A CG2 1 
ATOM   1309 N N   . GLU A 1 163 ? -22.80115 66.55583 33.56194 1.000 21.87249 ? 163 GLU A N   1 
ATOM   1310 C CA  . GLU A 1 163 ? -24.00246 65.79824 33.22282 1.000 22.21486 ? 163 GLU A CA  1 
ATOM   1311 C C   . GLU A 1 163 ? -23.88069 65.17058 31.84355 1.000 22.33051 ? 163 GLU A C   1 
ATOM   1312 O O   . GLU A 1 163 ? -24.20148 63.99583 31.65014 1.000 21.87934 ? 163 GLU A O   1 
ATOM   1313 C CB  . GLU A 1 163 ? -25.24236 66.70232 33.28430 1.000 24.99977 ? 163 GLU A CB  1 
ATOM   1314 C CG  . GLU A 1 163 ? -26.54869 65.95897 33.05838 1.000 27.05408 ? 163 GLU A CG  1 
ATOM   1315 C CD  . GLU A 1 163 ? -27.76830 66.87429 32.99834 1.000 30.89966 ? 163 GLU A CD  1 
ATOM   1316 O OE1 . GLU A 1 163 ? -27.61722 68.11683 32.92204 1.000 32.38151 ? 163 GLU A OE1 1 
ATOM   1317 O OE2 . GLU A 1 163 ? -28.89008 66.33354 33.04254 1.000 30.55054 ? 163 GLU A OE2 1 
ATOM   1318 N N   . LEU A 1 164 ? -23.38999 65.95475 30.88764 1.000 22.13438 ? 164 LEU A N   1 
ATOM   1319 C CA  . LEU A 1 164 ? -23.26505 65.49290 29.50686 1.000 20.49038 ? 164 LEU A CA  1 
ATOM   1320 C C   . LEU A 1 164 ? -22.18733 64.41781 29.35220 1.000 21.30312 ? 164 LEU A C   1 
ATOM   1321 O O   . LEU A 1 164 ? -22.42404 63.36210 28.76985 1.000 21.37146 ? 164 LEU A O   1 
ATOM   1322 C CB  . LEU A 1 164 ? -22.95423 66.67149 28.57541 1.000 18.22985 ? 164 LEU A CB  1 
ATOM   1323 C CG  . LEU A 1 164 ? -22.74027 66.33441 27.09126 1.000 17.85684 ? 164 LEU A CG  1 
ATOM   1324 C CD1 . LEU A 1 164 ? -23.96029 65.59731 26.53791 1.000 21.47343 ? 164 LEU A CD1 1 
ATOM   1325 C CD2 . LEU A 1 164 ? -22.48117 67.58342 26.27577 1.000 17.45861 ? 164 LEU A CD2 1 
ATOM   1326 N N   . VAL A 1 165 ? -20.99403 64.70566 29.85634 1.000 21.03123 ? 165 VAL A N   1 
ATOM   1327 C CA  . VAL A 1 165 ? -19.85400 63.82312 29.64687 1.000 20.47555 ? 165 VAL A CA  1 
ATOM   1328 C C   . VAL A 1 165 ? -20.02327 62.48091 30.38824 1.000 22.49248 ? 165 VAL A C   1 
ATOM   1329 O O   . VAL A 1 165 ? -19.54796 61.45614 29.91928 1.000 25.35529 ? 165 VAL A O   1 
ATOM   1330 C CB  . VAL A 1 165 ? -18.53786 64.53908 30.06088 1.000 20.41238 ? 165 VAL A CB  1 
ATOM   1331 C CG1 . VAL A 1 165 ? -17.34134 63.60253 30.00262 1.000 18.49290 ? 165 VAL A CG1 1 
ATOM   1332 C CG2 . VAL A 1 165 ? -18.29273 65.72532 29.11966 1.000 20.01796 ? 165 VAL A CG2 1 
ATOM   1333 N N   . THR A 1 166 ? -20.73757 62.47521 31.51097 1.000 23.65767 ? 166 THR A N   1 
ATOM   1334 C CA  . THR A 1 166 ? -20.96104 61.22686 32.25173 1.000 25.23805 ? 166 THR A CA  1 
ATOM   1335 C C   . THR A 1 166 ? -22.29879 60.56655 31.92116 1.000 25.45848 ? 166 THR A C   1 
ATOM   1336 O O   . THR A 1 166 ? -22.66088 59.57862 32.54877 1.000 30.61177 ? 166 THR A O   1 
ATOM   1337 C CB  . THR A 1 166 ? -20.92388 61.44439 33.77429 1.000 23.57492 ? 166 THR A CB  1 
ATOM   1338 O OG1 . THR A 1 166 ? -22.03196 62.26888 34.17357 1.000 24.63293 ? 166 THR A OG1 1 
ATOM   1339 C CG2 . THR A 1 166 ? -19.62035 62.09714 34.19186 1.000 23.60182 ? 166 THR A CG2 1 
ATOM   1340 N N   . SER A 1 167 ? -23.03372 61.11023 30.95066 1.000 26.37876 ? 167 SER A N   1 
ATOM   1341 C CA  . SER A 1 167 ? -24.38701 60.62346 30.66581 1.000 27.57836 ? 167 SER A CA  1 
ATOM   1342 C C   . SER A 1 167 ? -24.36384 59.18854 30.14693 1.000 28.65630 ? 167 SER A C   1 
ATOM   1343 O O   . SER A 1 167 ? -25.32466 58.44555 30.31598 1.000 29.02388 ? 167 SER A O   1 
ATOM   1344 C CB  . SER A 1 167 ? -25.11440 61.54245 29.66963 1.000 23.72518 ? 167 SER A CB  1 
ATOM   1345 O OG  . SER A 1 167 ? -24.50400 61.57205 28.38936 1.000 25.51385 ? 167 SER A OG  1 
ATOM   1346 N N   . SER A 1 168 ? -23.26365 58.80595 29.51544 1.000 26.85184 ? 168 SER A N   1 
ATOM   1347 C CA  . SER A 1 168 ? -23.07196 57.42878 29.09498 1.000 26.35463 ? 168 SER A CA  1 
ATOM   1348 C C   . SER A 1 168 ? -21.60464 57.20978 28.79728 1.000 27.75113 ? 168 SER A C   1 
ATOM   1349 O O   . SER A 1 168 ? -20.85654 58.16609 28.62051 1.000 27.49322 ? 168 SER A O   1 
ATOM   1350 C CB  . SER A 1 168 ? -23.92527 57.09105 27.86995 1.000 28.14441 ? 168 SER A CB  1 
ATOM   1351 O OG  . SER A 1 168 ? -23.43491 57.72380 26.70724 1.000 25.79777 ? 168 SER A OG  1 
ATOM   1352 N N   . ARG A 1 169 ? -21.19511 55.94804 28.76696 1.000 27.22385 ? 169 ARG A N   1 
ATOM   1353 C CA  . ARG A 1 169 ? -19.82714 55.60009 28.44827 1.000 26.60722 ? 169 ARG A CA  1 
ATOM   1354 C C   . ARG A 1 169 ? -19.50251 56.06502 27.03045 1.000 26.70140 ? 169 ARG A C   1 
ATOM   1355 O O   . ARG A 1 169 ? -18.40407 56.53548 26.75437 1.000 24.97439 ? 169 ARG A O   1 
ATOM   1356 C CB  . ARG A 1 169 ? -19.61874 54.09426 28.59639 1.000 25.89506 ? 169 ARG A CB  1 
ATOM   1357 C CG  . ARG A 1 169 ? -18.25719 53.63732 28.18138 1.000 30.65943 ? 169 ARG A CG  1 
ATOM   1358 C CD  . ARG A 1 169 ? -18.04871 52.13320 28.35366 1.000 31.53617 ? 169 ARG A CD  1 
ATOM   1359 N NE  . ARG A 1 169 ? -16.70830 51.80273 27.89333 1.000 33.07825 ? 169 ARG A NE  1 
ATOM   1360 C CZ  . ARG A 1 169 ? -15.63896 51.74858 28.67993 1.000 36.71497 ? 169 ARG A CZ  1 
ATOM   1361 N NH1 . ARG A 1 169 ? -15.75185 51.96027 29.99361 1.000 33.98319 ? 169 ARG A NH1 1 
ATOM   1362 N NH2 . ARG A 1 169 ? -14.45606 51.45964 28.15376 1.000 31.48627 ? 169 ARG A NH2 1 
ATOM   1363 N N   . GLU A 1 170 ? -20.48025 55.94688 26.14019 1.000 28.87804 ? 170 GLU A N   1 
ATOM   1364 C CA  . GLU A 1 170 ? -20.34555 56.42563 24.76842 1.000 28.11752 ? 170 GLU A CA  1 
ATOM   1365 C C   . GLU A 1 170 ? -20.10298 57.94524 24.70082 1.000 25.74745 ? 170 GLU A C   1 
ATOM   1366 O O   . GLU A 1 170 ? -19.21906 58.39321 23.98371 1.000 27.06005 ? 170 GLU A O   1 
ATOM   1367 C CB  . GLU A 1 170 ? -21.59244 56.04869 23.96090 1.000 34.02230 ? 170 GLU A CB  1 
ATOM   1368 C CG  . GLU A 1 170 ? -21.70306 56.69504 22.59393 1.000 40.52597 ? 170 GLU A CG  1 
ATOM   1369 C CD  . GLU A 1 170 ? -23.10891 56.58094 21.98816 1.000 51.13777 ? 170 GLU A CD  1 
ATOM   1370 O OE1 . GLU A 1 170 ? -24.12047 56.66475 22.73811 1.000 52.92745 ? 170 GLU A OE1 1 
ATOM   1371 O OE2 . GLU A 1 170 ? -23.19515 56.41477 20.75250 1.000 52.76164 ? 170 GLU A OE2 1 
ATOM   1372 N N   . ALA A 1 171 ? -20.88586 58.73542 25.43071 1.000 25.61091 ? 171 ALA A N   1 
ATOM   1373 C CA  . ALA A 1 171 ? -20.67028 60.18700 25.45038 1.000 24.01024 ? 171 ALA A CA  1 
ATOM   1374 C C   . ALA A 1 171 ? -19.27027 60.51525 25.98840 1.000 23.81595 ? 171 ALA A C   1 
ATOM   1375 O O   . ALA A 1 171 ? -18.55742 61.35958 25.45211 1.000 23.31597 ? 171 ALA A O   1 
ATOM   1376 C CB  . ALA A 1 171 ? -21.74412 60.87860 26.29536 1.000 22.60830 ? 171 ALA A CB  1 
ATOM   1377 N N   . CYS A 1 172 ? -18.89057 59.81178 27.04806 1.000 23.18632 ? 172 CYS A N   1 
ATOM   1378 C CA  . CYS A 1 172 ? -17.59721 59.98320 27.68847 1.000 23.80472 ? 172 CYS A CA  1 
ATOM   1379 C C   . CYS A 1 172 ? -16.44860 59.71908 26.71623 1.000 23.78413 ? 172 CYS A C   1 
ATOM   1380 O O   . CYS A 1 172 ? -15.51726 60.51818 26.60621 1.000 24.39103 ? 172 CYS A O   1 
ATOM   1381 C CB  . CYS A 1 172 ? -17.49806 59.05195 28.90378 1.000 22.06179 ? 172 CYS A CB  1 
ATOM   1382 S SG  . CYS A 1 172 ? -16.05202 59.33603 29.93478 1.000 26.31954 ? 172 CYS A SG  1 
ATOM   1383 N N   . ARG A 1 173 ? -16.52955 58.59888 26.00425 1.000 23.81481 ? 173 ARG A N   1 
ATOM   1384 C CA  . ARG A 1 173 ? -15.52023 58.23130 25.01871 1.000 27.32661 ? 173 ARG A CA  1 
ATOM   1385 C C   . ARG A 1 173 ? -15.39331 59.28619 23.91788 1.000 25.12607 ? 173 ARG A C   1 
ATOM   1386 O O   . ARG A 1 173 ? -14.29403 59.69335 23.56615 1.000 22.45213 ? 173 ARG A O   1 
ATOM   1387 C CB  . ARG A 1 173 ? -15.84950 56.87021 24.39893 1.000 28.13367 ? 173 ARG A CB  1 
ATOM   1388 C CG  . ARG A 1 173 ? -14.67014 56.19087 23.71490 1.000 32.23936 ? 173 ARG A CG  1 
ATOM   1389 C CD  . ARG A 1 173 ? -15.12047 55.08435 22.75297 1.000 36.28654 ? 173 ARG A CD  1 
ATOM   1390 N NE  . ARG A 1 173 ? -15.26315 55.63433 21.40596 1.000 53.91629 ? 173 ARG A NE  1 
ATOM   1391 C CZ  . ARG A 1 173 ? -16.39100 56.12919 20.89797 1.000 51.29041 ? 173 ARG A CZ  1 
ATOM   1392 N NH1 . ARG A 1 173 ? -16.39622 56.62413 19.66852 1.000 46.25560 ? 173 ARG A NH1 1 
ATOM   1393 N NH2 . ARG A 1 173 ? -17.51401 56.12399 21.60890 1.000 55.44354 ? 173 ARG A NH2 1 
ATOM   1394 N N   . ILE A 1 174 ? -16.52939 59.71381 23.37985 1.000 24.99525 ? 174 ILE A N   1 
ATOM   1395 C CA  . ILE A 1 174 ? -16.56245 60.72857 22.33791 1.000 24.39190 ? 174 ILE A CA  1 
ATOM   1396 C C   . ILE A 1 174 ? -15.83788 62.00214 22.77346 1.000 21.09986 ? 174 ILE A C   1 
ATOM   1397 O O   . ILE A 1 174 ? -15.00794 62.54263 22.04194 1.000 21.34278 ? 174 ILE A O   1 
ATOM   1398 C CB  . ILE A 1 174 ? -18.02001 61.05892 21.94860 1.000 24.90581 ? 174 ILE A CB  1 
ATOM   1399 C CG1 . ILE A 1 174 ? -18.63425 59.87515 21.17707 1.000 25.06410 ? 174 ILE A CG1 1 
ATOM   1400 C CG2 . ILE A 1 174 ? -18.09450 62.35826 21.12698 1.000 20.86667 ? 174 ILE A CG2 1 
ATOM   1401 C CD1 . ILE A 1 174 ? -20.12268 59.98285 20.96648 1.000 25.11663 ? 174 ILE A CD1 1 
ATOM   1402 N N   . TYR A 1 175 ? -16.14123 62.45312 23.98325 1.000 22.11989 ? 175 TYR A N   1 
ATOM   1403 C CA  . TYR A 1 175 ? -15.58743 63.69516 24.49216 1.000 21.86597 ? 175 TYR A CA  1 
ATOM   1404 C C   . TYR A 1 175 ? -14.07480 63.61278 24.63937 1.000 21.17587 ? 175 TYR A C   1 
ATOM   1405 O O   . TYR A 1 175 ? -13.34895 64.40812 24.05969 1.000 19.71485 ? 175 TYR A O   1 
ATOM   1406 C CB  . TYR A 1 175 ? -16.22754 64.05570 25.83084 1.000 20.91951 ? 175 TYR A CB  1 
ATOM   1407 C CG  . TYR A 1 175 ? -15.77899 65.40139 26.34185 1.000 23.17349 ? 175 TYR A CG  1 
ATOM   1408 C CD1 . TYR A 1 175 ? -16.24223 66.56873 25.75004 1.000 20.35384 ? 175 TYR A CD1 1 
ATOM   1409 C CD2 . TYR A 1 175 ? -14.88788 65.50627 27.40952 1.000 18.26704 ? 175 TYR A CD2 1 
ATOM   1410 C CE1 . TYR A 1 175 ? -15.83788 67.80456 26.20230 1.000 21.53851 ? 175 TYR A CE1 1 
ATOM   1411 C CE2 . TYR A 1 175 ? -14.47179 66.74142 27.87594 1.000 21.42202 ? 175 TYR A CE2 1 
ATOM   1412 C CZ  . TYR A 1 175 ? -14.95707 67.89050 27.26635 1.000 22.38157 ? 175 TYR A CZ  1 
ATOM   1413 O OH  . TYR A 1 175 ? -14.56476 69.12264 27.70365 1.000 21.44109 ? 175 TYR A OH  1 
ATOM   1414 N N   . PHE A 1 176 ? -13.60136 62.63103 25.40137 1.000 23.62039 ? 176 PHE A N   1 
ATOM   1415 C CA  . PHE A 1 176 ? -12.18068 62.55815 25.74023 1.000 22.94967 ? 176 PHE A CA  1 
ATOM   1416 C C   . PHE A 1 176 ? -11.29983 62.19877 24.55220 1.000 21.58784 ? 176 PHE A C   1 
ATOM   1417 O O   . PHE A 1 176 ? -10.16371 62.64637 24.48237 1.000 23.24594 ? 176 PHE A O   1 
ATOM   1418 C CB  . PHE A 1 176 ? -11.96400 61.57724 26.90280 1.000 19.85272 ? 176 PHE A CB  1 
ATOM   1419 C CG  . PHE A 1 176 ? -12.43065 62.12332 28.22701 1.000 21.18922 ? 176 PHE A CG  1 
ATOM   1420 C CD1 . PHE A 1 176 ? -11.72370 63.13537 28.85497 1.000 21.42982 ? 176 PHE A CD1 1 
ATOM   1421 C CD2 . PHE A 1 176 ? -13.60350 61.66800 28.81627 1.000 21.44613 ? 176 PHE A CD2 1 
ATOM   1422 C CE1 . PHE A 1 176 ? -12.15509 63.66445 30.05357 1.000 21.54145 ? 176 PHE A CE1 1 
ATOM   1423 C CE2 . PHE A 1 176 ? -14.03766 62.19104 30.01302 1.000 19.49306 ? 176 PHE A CE2 1 
ATOM   1424 C CZ  . PHE A 1 176 ? -13.31143 63.18876 30.63614 1.000 21.75978 ? 176 PHE A CZ  1 
ATOM   1425 N N   . LYS A 1 177 ? -11.82411 61.42059 23.60927 1.000 23.14581 ? 177 LYS A N   1 
ATOM   1426 C CA  . LYS A 1 177 ? -11.05710 61.06658 22.41587 1.000 22.80232 ? 177 LYS A CA  1 
ATOM   1427 C C   . LYS A 1 177 ? -10.56796 62.30146 21.65010 1.000 23.00248 ? 177 LYS A C   1 
ATOM   1428 O O   . LYS A 1 177 ? -9.45878  62.31185 21.12419 1.000 21.62420 ? 177 LYS A O   1 
ATOM   1429 C CB  . LYS A 1 177 ? -11.88008 60.18547 21.47719 1.000 23.97237 ? 177 LYS A CB  1 
ATOM   1430 C CG  . LYS A 1 177 ? -11.09611 59.70694 20.26920 1.000 27.02543 ? 177 LYS A CG  1 
ATOM   1431 C CD  . LYS A 1 177 ? -11.74891 58.50191 19.61484 1.000 33.75163 ? 177 LYS A CD  1 
ATOM   1432 C CE  . LYS A 1 177 ? -12.43577 58.87780 18.32187 1.000 44.06008 ? 177 LYS A CE  1 
ATOM   1433 N NZ  . LYS A 1 177 ? -13.34990 57.79485 17.84466 1.000 49.02376 ? 177 LYS A NZ  1 
ATOM   1434 N N   . HIS A 1 178 ? -11.40000 63.33648 21.59595 1.000 21.51575 ? 178 HIS A N   1 
ATOM   1435 C CA  . HIS A 1 178 ? -11.03401 64.57435 20.91531 1.000 19.91890 ? 178 HIS A CA  1 
ATOM   1436 C C   . HIS A 1 178 ? -9.72342  65.13935 21.45477 1.000 20.02315 ? 178 HIS A C   1 
ATOM   1437 O O   . HIS A 1 178 ? -8.84929  65.54598 20.69484 1.000 20.76604 ? 178 HIS A O   1 
ATOM   1438 C CB  . HIS A 1 178 ? -12.14827 65.61496 21.06327 1.000 20.99614 ? 178 HIS A CB  1 
ATOM   1439 C CG  . HIS A 1 178 ? -11.69929 67.01253 20.78436 1.000 20.89291 ? 178 HIS A CG  1 
ATOM   1440 N ND1 . HIS A 1 178 ? -11.55411 67.50189 19.50690 1.000 20.79353 ? 178 HIS A ND1 1 
ATOM   1441 C CD2 . HIS A 1 178 ? -11.34343 68.01916 21.61768 1.000 19.98446 ? 178 HIS A CD2 1 
ATOM   1442 C CE1 . HIS A 1 178 ? -11.13330 68.75365 19.56366 1.000 23.51579 ? 178 HIS A CE1 1 
ATOM   1443 N NE2 . HIS A 1 178 ? -10.99546 69.09111 20.83217 1.000 20.79846 ? 178 HIS A NE2 1 
ATOM   1444 N N   . PHE A 1 179 ? -9.57633  65.14435 22.77211 1.000 20.34394 ? 179 PHE A N   1 
ATOM   1445 C CA  . PHE A 1 179 ? -8.39850  65.75892 23.37437 1.000 20.39084 ? 179 PHE A CA  1 
ATOM   1446 C C   . PHE A 1 179 ? -7.14640  64.91614 23.18041 1.000 21.98892 ? 179 PHE A C   1 
ATOM   1447 O O   . PHE A 1 179 ? -6.09722  65.45990 22.85238 1.000 23.11114 ? 179 PHE A O   1 
ATOM   1448 C CB  . PHE A 1 179 ? -8.66139  66.04024 24.85004 1.000 21.33757 ? 179 PHE A CB  1 
ATOM   1449 C CG  . PHE A 1 179 ? -9.78196  67.01611 25.06219 1.000 19.44606 ? 179 PHE A CG  1 
ATOM   1450 C CD1 . PHE A 1 179 ? -9.54712  68.38112 24.99255 1.000 18.12922 ? 179 PHE A CD1 1 
ATOM   1451 C CD2 . PHE A 1 179 ? -11.07237 66.57050 25.26960 1.000 18.03209 ? 179 PHE A CD2 1 
ATOM   1452 C CE1 . PHE A 1 179 ? -10.58212 69.28465 25.15952 1.000 19.29424 ? 179 PHE A CE1 1 
ATOM   1453 C CE2 . PHE A 1 179 ? -12.12039 67.46184 25.42468 1.000 19.28289 ? 179 PHE A CE2 1 
ATOM   1454 C CZ  . PHE A 1 179 ? -11.88169 68.81859 25.37834 1.000 19.98900 ? 179 PHE A CZ  1 
ATOM   1455 N N   . PHE A 1 180 ? -7.25231  63.59902 23.35722 1.000 19.84357 ? 180 PHE A N   1 
ATOM   1456 C CA  . PHE A 1 180 ? -6.12622  62.71054 23.05859 1.000 22.30197 ? 180 PHE A CA  1 
ATOM   1457 C C   . PHE A 1 180 ? -5.63398  62.88432 21.62573 1.000 23.23587 ? 180 PHE A C   1 
ATOM   1458 O O   . PHE A 1 180 ? -4.43100  62.94462 21.37072 1.000 22.63508 ? 180 PHE A O   1 
ATOM   1459 C CB  . PHE A 1 180 ? -6.50911  61.24142 23.28264 1.000 22.98916 ? 180 PHE A CB  1 
ATOM   1460 C CG  . PHE A 1 180 ? -6.69102  60.87947 24.72842 1.000 22.16463 ? 180 PHE A CG  1 
ATOM   1461 C CD1 . PHE A 1 180 ? -5.65293  61.05103 25.63174 1.000 21.59728 ? 180 PHE A CD1 1 
ATOM   1462 C CD2 . PHE A 1 180 ? -7.89484  60.36754 25.18346 1.000 21.48859 ? 180 PHE A CD2 1 
ATOM   1463 C CE1 . PHE A 1 180 ? -5.81213  60.71823 26.96525 1.000 23.29767 ? 180 PHE A CE1 1 
ATOM   1464 C CE2 . PHE A 1 180 ? -8.05704  60.02470 26.51590 1.000 22.85696 ? 180 PHE A CE2 1 
ATOM   1465 C CZ  . PHE A 1 180 ? -7.01729  60.20324 27.40693 1.000 21.12562 ? 180 PHE A CZ  1 
ATOM   1466 N N   . ASP A 1 181 ? -6.57039  62.95420 20.68733 1.000 21.60183 ? 181 ASP A N   1 
ATOM   1467 C CA  . ASP A 1 181 ? -6.20041  63.03825 19.27832 1.000 22.57713 ? 181 ASP A CA  1 
ATOM   1468 C C   . ASP A 1 181 ? -5.77165  64.45155 18.84004 1.000 21.69000 ? 181 ASP A C   1 
ATOM   1469 O O   . ASP A 1 181 ? -4.71607  64.61003 18.24175 1.000 24.28245 ? 181 ASP A O   1 
ATOM   1470 C CB  . ASP A 1 181 ? -7.35207  62.53286 18.40491 1.000 23.48764 ? 181 ASP A CB  1 
ATOM   1471 C CG  . ASP A 1 181 ? -7.44806  61.01149 18.38694 1.000 25.14631 ? 181 ASP A CG  1 
ATOM   1472 O OD1 . ASP A 1 181 ? -6.52058  60.33590 18.88430 1.000 25.84438 ? 181 ASP A OD1 1 
ATOM   1473 O OD2 . ASP A 1 181 ? -8.44351  60.48854 17.85644 1.000 26.90175 ? 181 ASP A OD2 1 
ATOM   1474 N N   . HIS A 1 182 ? -6.56892  65.47141 19.14519 1.000 20.71292 ? 182 HIS A N   1 
ATOM   1475 C CA  . HIS A 1 182 ? -6.26211  66.83840 18.70556 1.000 20.49441 ? 182 HIS A CA  1 
ATOM   1476 C C   . HIS A 1 182 ? -4.98025  67.40209 19.34802 1.000 23.49428 ? 182 HIS A C   1 
ATOM   1477 O O   . HIS A 1 182 ? -4.26642  68.19641 18.74392 1.000 23.74947 ? 182 HIS A O   1 
ATOM   1478 C CB  . HIS A 1 182 ? -7.45248  67.76710 18.99583 1.000 22.82488 ? 182 HIS A CB  1 
ATOM   1479 C CG  . HIS A 1 182 ? -7.17620  69.21513 18.72652 1.000 23.91361 ? 182 HIS A CG  1 
ATOM   1480 N ND1 . HIS A 1 182 ? -6.78415  69.67968 17.49158 1.000 25.55337 ? 182 HIS A ND1 1 
ATOM   1481 C CD2 . HIS A 1 182 ? -7.23961  70.30175 19.53593 1.000 22.27370 ? 182 HIS A CD2 1 
ATOM   1482 C CE1 . HIS A 1 182 ? -6.61400  70.99114 17.54934 1.000 25.92712 ? 182 HIS A CE1 1 
ATOM   1483 N NE2 . HIS A 1 182 ? -6.88107  71.39189 18.77978 1.000 26.28666 ? 182 HIS A NE2 1 
ATOM   1484 N N   . TRP A 1 183 ? -4.67809  66.97901 20.56704 1.000 22.28954 ? 183 TRP A N   1 
ATOM   1485 C CA  . TRP A 1 183 ? -3.49942  67.48583 21.24873 1.000 21.20944 ? 183 TRP A CA  1 
ATOM   1486 C C   . TRP A 1 183 ? -2.23312  66.69778 20.88559 1.000 22.50612 ? 183 TRP A C   1 
ATOM   1487 O O   . TRP A 1 183 ? -1.14581  67.03329 21.32616 1.000 20.66754 ? 183 TRP A O   1 
ATOM   1488 C CB  . TRP A 1 183 ? -3.70065  67.46028 22.75678 1.000 20.67957 ? 183 TRP A CB  1 
ATOM   1489 C CG  . TRP A 1 183 ? -4.70319  68.43204 23.26325 1.000 19.75340 ? 183 TRP A CG  1 
ATOM   1490 C CD1 . TRP A 1 183 ? -5.40541  69.35802 22.53510 1.000 20.60838 ? 183 TRP A CD1 1 
ATOM   1491 C CD2 . TRP A 1 183 ? -5.11705  68.59239 24.62484 1.000 18.56928 ? 183 TRP A CD2 1 
ATOM   1492 N NE1 . TRP A 1 183 ? -6.23501  70.07871 23.36636 1.000 20.39272 ? 183 TRP A NE1 1 
ATOM   1493 C CE2 . TRP A 1 183 ? -6.07629  69.62329 24.65292 1.000 19.06174 ? 183 TRP A CE2 1 
ATOM   1494 C CE3 . TRP A 1 183 ? -4.77051  67.95860 25.82359 1.000 21.18877 ? 183 TRP A CE3 1 
ATOM   1495 C CZ2 . TRP A 1 183 ? -6.68373  70.03981 25.83212 1.000 21.15860 ? 183 TRP A CZ2 1 
ATOM   1496 C CZ3 . TRP A 1 183 ? -5.38118  68.37517 26.99694 1.000 18.37381 ? 183 TRP A CZ3 1 
ATOM   1497 C CH2 . TRP A 1 183 ? -6.32445  69.40120 26.99237 1.000 20.10480 ? 183 TRP A CH2 1 
ATOM   1498 N N   . SER A 1 184 ? -2.37519  65.66105 20.07204 1.000 22.76110 ? 184 SER A N   1 
ATOM   1499 C CA  . SER A 1 184 ? -1.21497  64.87955 19.66188 1.000 23.51169 ? 184 SER A CA  1 
ATOM   1500 C C   . SER A 1 184 ? -0.68058  65.30768 18.30701 1.000 23.85260 ? 184 SER A C   1 
ATOM   1501 O O   . SER A 1 184 ? -1.37608  65.95055 17.52617 1.000 25.81249 ? 184 SER A O   1 
ATOM   1502 C CB  . SER A 1 184 ? -1.55412  63.39431 19.62329 1.000 23.82192 ? 184 SER A CB  1 
ATOM   1503 O OG  . SER A 1 184 ? -1.96571  62.96343 20.89970 1.000 28.66521 ? 184 SER A OG  1 
ATOM   1504 N N   . TYR A 1 185 ? 0.56401   64.94087 18.03755 1.000 24.14870 ? 185 TYR A N   1 
ATOM   1505 C CA  . TYR A 1 185 ? 1.18027   65.25470 16.76141 1.000 27.40892 ? 185 TYR A CA  1 
ATOM   1506 C C   . TYR A 1 185 ? 0.54082   64.45327 15.62229 1.000 28.60218 ? 185 TYR A C   1 
ATOM   1507 O O   . TYR A 1 185 ? 0.23207   65.00214 14.57130 1.000 28.93445 ? 185 TYR A O   1 
ATOM   1508 C CB  . TYR A 1 185 ? 2.68827   64.99327 16.80867 1.000 26.54577 ? 185 TYR A CB  1 
ATOM   1509 C CG  . TYR A 1 185 ? 3.34374   65.15807 15.45917 1.000 28.39722 ? 185 TYR A CG  1 
ATOM   1510 C CD1 . TYR A 1 185 ? 3.61044   66.42089 14.94963 1.000 31.07179 ? 185 TYR A CD1 1 
ATOM   1511 C CD2 . TYR A 1 185 ? 3.68219   64.05517 14.68922 1.000 32.62574 ? 185 TYR A CD2 1 
ATOM   1512 C CE1 . TYR A 1 185 ? 4.19639   66.58230 13.71766 1.000 33.56833 ? 185 TYR A CE1 1 
ATOM   1513 C CE2 . TYR A 1 185 ? 4.27258   64.20820 13.44375 1.000 33.65176 ? 185 TYR A CE2 1 
ATOM   1514 C CZ  . TYR A 1 185 ? 4.52609   65.47745 12.97015 1.000 33.85655 ? 185 TYR A CZ  1 
ATOM   1515 O OH  . TYR A 1 185 ? 5.11024   65.64354 11.74247 1.000 41.50309 ? 185 TYR A OH  1 
ATOM   1516 N N   . HIS A 1 186 ? 0.34447   63.15648 15.83925 1.000 27.88249 ? 186 HIS A N   1 
ATOM   1517 C CA  . HIS A 1 186 ? -0.27450  62.30095 14.83184 1.000 30.60387 ? 186 HIS A CA  1 
ATOM   1518 C C   . HIS A 1 186 ? -1.40837  61.45482 15.41233 1.000 29.08866 ? 186 HIS A C   1 
ATOM   1519 O O   . HIS A 1 186 ? -1.16642  60.51998 16.16799 1.000 32.20947 ? 186 HIS A O   1 
ATOM   1520 C CB  . HIS A 1 186 ? 0.77298   61.38953 14.18790 1.000 31.97106 ? 186 HIS A CB  1 
ATOM   1521 C CG  . HIS A 1 186 ? 0.18825   60.31791 13.31722 1.000 37.52006 ? 186 HIS A CG  1 
ATOM   1522 N ND1 . HIS A 1 186 ? -0.19419  60.54275 12.00874 1.000 43.91972 ? 186 HIS A ND1 1 
ATOM   1523 C CD2 . HIS A 1 186 ? -0.08616  59.01517 13.56693 1.000 35.88080 ? 186 HIS A CD2 1 
ATOM   1524 C CE1 . HIS A 1 186 ? -0.67456  59.42707 11.49275 1.000 42.44057 ? 186 HIS A CE1 1 
ATOM   1525 N NE2 . HIS A 1 186 ? -0.62356  58.48444 12.41924 1.000 43.95397 ? 186 HIS A NE2 1 
ATOM   1526 N N   . ALA A 1 187 ? -2.64182  61.79098 15.05690 1.000 26.38547 ? 187 ALA A N   1 
ATOM   1527 C CA  . ALA A 1 187 ? -3.80312  61.03390 15.50862 1.000 28.54653 ? 187 ALA A CA  1 
ATOM   1528 C C   . ALA A 1 187 ? -3.96661  59.80641 14.62155 1.000 29.10523 ? 187 ALA A C   1 
ATOM   1529 O O   . ALA A 1 187 ? -3.68768  59.87894 13.43364 1.000 29.94824 ? 187 ALA A O   1 
ATOM   1530 C CB  . ALA A 1 187 ? -5.05497  61.89475 15.47548 1.000 25.43422 ? 187 ALA A CB  1 
ATOM   1531 N N   . PRO A 1 188 ? -4.42983  58.67964 15.18559 1.000 29.10077 ? 188 PRO A N   1 
ATOM   1532 C CA  . PRO A 1 188 ? -4.84871  58.50499 16.58005 1.000 28.60258 ? 188 PRO A CA  1 
ATOM   1533 C C   . PRO A 1 188 ? -3.68103  58.35335 17.54799 1.000 26.81889 ? 188 PRO A C   1 
ATOM   1534 O O   . PRO A 1 188 ? -2.67843  57.74082 17.22076 1.000 29.46689 ? 188 PRO A O   1 
ATOM   1535 C CB  . PRO A 1 188 ? -5.67723  57.21586 16.54022 1.000 28.14360 ? 188 PRO A CB  1 
ATOM   1536 C CG  . PRO A 1 188 ? -5.11652  56.44292 15.38593 1.000 27.93995 ? 188 PRO A CG  1 
ATOM   1537 C CD  . PRO A 1 188 ? -4.67526  57.46956 14.37406 1.000 30.26480 ? 188 PRO A CD  1 
ATOM   1538 N N   . LEU A 1 189 ? -3.82608  58.92007 18.73637 1.000 27.91498 ? 189 LEU A N   1 
ATOM   1539 C CA  . LEU A 1 189 ? -2.86516  58.70701 19.80203 1.000 26.46076 ? 189 LEU A CA  1 
ATOM   1540 C C   . LEU A 1 189 ? -2.92171  57.27682 20.31830 1.000 28.26399 ? 189 LEU A C   1 
ATOM   1541 O O   . LEU A 1 189 ? -1.89468  56.65322 20.59154 1.000 27.25227 ? 189 LEU A O   1 
ATOM   1542 C CB  . LEU A 1 189 ? -3.12516  59.66835 20.95855 1.000 23.28817 ? 189 LEU A CB  1 
ATOM   1543 C CG  . LEU A 1 189 ? -2.16652  59.54146 22.14804 1.000 25.40666 ? 189 LEU A CG  1 
ATOM   1544 C CD1 . LEU A 1 189 ? -0.76243  60.00867 21.76504 1.000 24.33588 ? 189 LEU A CD1 1 
ATOM   1545 C CD2 . LEU A 1 189 ? -2.68962  60.31666 23.35412 1.000 21.94185 ? 189 LEU A CD2 1 
ATOM   1546 N N   . LEU A 1 190 ? -4.13795  56.77148 20.45881 1.000 24.96007 ? 190 LEU A N   1 
ATOM   1547 C CA  . LEU A 1 190 ? -4.36822  55.54724 21.20486 1.000 27.18156 ? 190 LEU A CA  1 
ATOM   1548 C C   . LEU A 1 190 ? -4.98723  54.45458 20.34348 1.000 28.89507 ? 190 LEU A C   1 
ATOM   1549 O O   . LEU A 1 190 ? -5.74964  54.73337 19.41362 1.000 27.96075 ? 190 LEU A O   1 
ATOM   1550 C CB  . LEU A 1 190 ? -5.28463  55.82742 22.40083 1.000 25.56018 ? 190 LEU A CB  1 
ATOM   1551 C CG  . LEU A 1 190 ? -4.88405  56.94897 23.36911 1.000 23.41602 ? 190 LEU A CG  1 
ATOM   1552 C CD1 . LEU A 1 190 ? -6.01235  57.24223 24.35610 1.000 23.83681 ? 190 LEU A CD1 1 
ATOM   1553 C CD2 . LEU A 1 190 ? -3.59674  56.59266 24.12008 1.000 24.41558 ? 190 LEU A CD2 1 
ATOM   1554 N N   . THR A 1 191 ? -4.65715  53.20959 20.66728 1.000 30.10426 ? 191 THR A N   1 
ATOM   1555 C CA  . THR A 1 191 ? -5.43655  52.08017 20.19085 1.000 29.85490 ? 191 THR A CA  1 
ATOM   1556 C C   . THR A 1 191 ? -6.79082  52.10714 20.87985 1.000 29.35317 ? 191 THR A C   1 
ATOM   1557 O O   . THR A 1 191 ? -6.98241  52.79199 21.88535 1.000 25.69999 ? 191 THR A O   1 
ATOM   1558 C CB  . THR A 1 191 ? -4.76956  50.72413 20.49072 1.000 30.63298 ? 191 THR A CB  1 
ATOM   1559 O OG1 . THR A 1 191 ? -4.87420  50.44926 21.89094 1.000 28.55065 ? 191 THR A OG1 1 
ATOM   1560 C CG2 . THR A 1 191 ? -3.29864  50.71988 20.07410 1.000 29.14151 ? 191 THR A CG2 1 
ATOM   1561 N N   . GLN A 1 192 ? -7.71777  51.32973 20.34587 1.000 28.37878 ? 192 GLN A N   1 
ATOM   1562 C CA  . GLN A 1 192 ? -9.04212  51.19328 20.92505 1.000 32.31032 ? 192 GLN A CA  1 
ATOM   1563 C C   . GLN A 1 192 ? -8.98717  50.68589 22.37129 1.000 32.54795 ? 192 GLN A C   1 
ATOM   1564 O O   . GLN A 1 192 ? -9.68793  51.19637 23.24201 1.000 31.00308 ? 192 GLN A O   1 
ATOM   1565 C CB  . GLN A 1 192 ? -9.87841  50.25489 20.05857 1.000 36.25982 ? 192 GLN A CB  1 
ATOM   1566 C CG  . GLN A 1 192 ? -11.31871 50.09892 20.48155 1.000 42.71496 ? 192 GLN A CG  1 
ATOM   1567 C CD  . GLN A 1 192 ? -12.06555 49.13464 19.56980 1.000 57.19947 ? 192 GLN A CD  1 
ATOM   1568 O OE1 . GLN A 1 192 ? -12.71987 48.19921 20.03481 1.000 64.27536 ? 192 GLN A OE1 1 
ATOM   1569 N NE2 . GLN A 1 192 ? -11.96025 49.35630 18.26093 1.000 60.29382 ? 192 GLN A NE2 1 
ATOM   1570 N N   . ASP A 1 193 ? -8.15052  49.68669 22.62524 1.000 30.72558 ? 193 ASP A N   1 
ATOM   1571 C CA  . ASP A 1 193 ? -8.01794  49.13953 23.97131 1.000 30.60814 ? 193 ASP A CA  1 
ATOM   1572 C C   . ASP A 1 193 ? -7.45576  50.16617 24.94567 1.000 28.22417 ? 193 ASP A C   1 
ATOM   1573 O O   . ASP A 1 193 ? -7.87872  50.22347 26.09630 1.000 27.26599 ? 193 ASP A O   1 
ATOM   1574 C CB  . ASP A 1 193 ? -7.13129  47.89307 23.96767 1.000 30.00623 ? 193 ASP A CB  1 
ATOM   1575 C CG  . ASP A 1 193 ? -7.81294  46.70018 23.33645 1.000 34.15457 ? 193 ASP A CG  1 
ATOM   1576 O OD1 . ASP A 1 193 ? -9.04950  46.73410 23.18019 1.000 38.41302 ? 193 ASP A OD1 1 
ATOM   1577 O OD2 . ASP A 1 193 ? -7.11514  45.72456 23.00503 1.000 38.03428 ? 193 ASP A OD2 1 
ATOM   1578 N N   . GLU A 1 194 ? -6.49845  50.96662 24.48748 1.000 27.23614 ? 194 GLU A N   1 
ATOM   1579 C CA  . GLU A 1 194 ? -5.90673  51.98969 25.34144 1.000 24.66252 ? 194 GLU A CA  1 
ATOM   1580 C C   . GLU A 1 194 ? -6.92469  53.06196 25.68273 1.000 23.78945 ? 194 GLU A C   1 
ATOM   1581 O O   . GLU A 1 194 ? -7.03003  53.46584 26.83682 1.000 27.45205 ? 194 GLU A O   1 
ATOM   1582 C CB  . GLU A 1 194 ? -4.67645  52.61685 24.67932 1.000 27.06060 ? 194 GLU A CB  1 
ATOM   1583 C CG  . GLU A 1 194 ? -3.47510  51.69171 24.60690 1.000 29.75443 ? 194 GLU A CG  1 
ATOM   1584 C CD  . GLU A 1 194 ? -2.35733  52.25975 23.74384 1.000 34.16090 ? 194 GLU A CD  1 
ATOM   1585 O OE1 . GLU A 1 194 ? -1.18331  51.91731 23.99507 1.000 41.56951 ? 194 GLU A OE1 1 
ATOM   1586 O OE2 . GLU A 1 194 ? -2.65021  53.04477 22.81434 1.000 31.64287 ? 194 GLU A OE2 1 
ATOM   1587 N N   . LEU A 1 195 ? -7.69471  53.50532 24.69384 1.000 25.04330 ? 195 LEU A N   1 
ATOM   1588 C CA  . LEU A 1 195 ? -8.73871  54.49647 24.95286 1.000 25.93708 ? 195 LEU A CA  1 
ATOM   1589 C C   . LEU A 1 195 ? -9.80590  53.95578 25.91117 1.000 26.05218 ? 195 LEU A C   1 
ATOM   1590 O O   . LEU A 1 195 ? -10.29105 54.67657 26.77750 1.000 26.48148 ? 195 LEU A O   1 
ATOM   1591 C CB  . LEU A 1 195 ? -9.38550  54.95337 23.64405 1.000 24.66811 ? 195 LEU A CB  1 
ATOM   1592 C CG  . LEU A 1 195 ? -10.53252 55.96128 23.76507 1.000 25.45393 ? 195 LEU A CG  1 
ATOM   1593 C CD1 . LEU A 1 195 ? -10.09532 57.24898 24.46347 1.000 22.40046 ? 195 LEU A CD1 1 
ATOM   1594 C CD2 . LEU A 1 195 ? -11.09283 56.27472 22.39137 1.000 29.83514 ? 195 LEU A CD2 1 
ATOM   1595 N N   . ASP A 1 196 ? -10.16072 52.68439 25.76675 1.000 26.90834 ? 196 ASP A N   1 
ATOM   1596 C CA  . ASP A 1 196 ? -11.12208 52.06400 26.67499 1.000 27.78094 ? 196 ASP A CA  1 
ATOM   1597 C C   . ASP A 1 196 ? -10.66591 52.12473 28.13207 1.000 24.85902 ? 196 ASP A C   1 
ATOM   1598 O O   . ASP A 1 196 ? -11.47708 52.29081 29.03702 1.000 24.55524 ? 196 ASP A O   1 
ATOM   1599 C CB  . ASP A 1 196 ? -11.37123 50.60966 26.27992 1.000 27.17384 ? 196 ASP A CB  1 
ATOM   1600 C CG  . ASP A 1 196 ? -12.29067 50.48225 25.08050 1.000 31.98970 ? 196 ASP A CG  1 
ATOM   1601 O OD1 . ASP A 1 196 ? -13.09161 51.40585 24.85322 1.000 36.93308 ? 196 ASP A OD1 1 
ATOM   1602 O OD2 . ASP A 1 196 ? -12.22065 49.45655 24.37353 1.000 37.81658 ? 196 ASP A OD2 1 
ATOM   1603 N N   . ILE A 1 197 ? -9.36403  51.98502 28.34561 1.000 24.04529 ? 197 ILE A N   1 
ATOM   1604 C CA  . ILE A 1 197 ? -8.81002  52.03716 29.69061 1.000 24.75255 ? 197 ILE A CA  1 
ATOM   1605 C C   . ILE A 1 197 ? -8.90809  53.45160 30.25678 1.000 23.91332 ? 197 ILE A C   1 
ATOM   1606 O O   . ILE A 1 197 ? -9.29704  53.63071 31.41324 1.000 25.44509 ? 197 ILE A O   1 
ATOM   1607 C CB  . ILE A 1 197 ? -7.35224  51.52575 29.70693 1.000 24.25802 ? 197 ILE A CB  1 
ATOM   1608 C CG1 . ILE A 1 197 ? -7.35389  50.00259 29.51569 1.000 27.27518 ? 197 ILE A CG1 1 
ATOM   1609 C CG2 . ILE A 1 197 ? -6.66283  51.88538 31.00356 1.000 23.25112 ? 197 ILE A CG2 1 
ATOM   1610 C CD1 . ILE A 1 197 ? -6.01030  49.40493 29.12339 1.000 29.05588 ? 197 ILE A CD1 1 
ATOM   1611 N N   . TYR A 1 198 ? -8.60464  54.46095 29.44492 1.000 21.97682 ? 198 TYR A N   1 
ATOM   1612 C CA  . TYR A 1 198 ? -8.79005  55.83620 29.90034 1.000 24.00352 ? 198 TYR A CA  1 
ATOM   1613 C C   . TYR A 1 198 ? -10.25779 56.12442 30.19841 1.000 21.71949 ? 198 TYR A C   1 
ATOM   1614 O O   . TYR A 1 198 ? -10.56964 56.81120 31.16022 1.000 25.22718 ? 198 TYR A O   1 
ATOM   1615 C CB  . TYR A 1 198 ? -8.26637  56.84267 28.87089 1.000 21.98159 ? 198 TYR A CB  1 
ATOM   1616 C CG  . TYR A 1 198 ? -6.76876  56.97884 28.85866 1.000 22.23667 ? 198 TYR A CG  1 
ATOM   1617 C CD1 . TYR A 1 198 ? -6.11204  57.71253 29.83351 1.000 24.37354 ? 198 TYR A CD1 1 
ATOM   1618 C CD2 . TYR A 1 198 ? -6.00874  56.36862 27.87500 1.000 24.07055 ? 198 TYR A CD2 1 
ATOM   1619 C CE1 . TYR A 1 198 ? -4.74384  57.84272 29.82254 1.000 25.68206 ? 198 TYR A CE1 1 
ATOM   1620 C CE2 . TYR A 1 198 ? -4.63895  56.49451 27.85729 1.000 26.07971 ? 198 TYR A CE2 1 
ATOM   1621 C CZ  . TYR A 1 198 ? -4.01316  57.23100 28.83047 1.000 26.69662 ? 198 TYR A CZ  1 
ATOM   1622 O OH  . TYR A 1 198 ? -2.64557  57.35551 28.80232 1.000 27.52333 ? 198 TYR A OH  1 
ATOM   1623 N N   . VAL A 1 199 ? -11.15521 55.59060 29.37707 1.000 24.04563 ? 199 VAL A N   1 
ATOM   1624 C CA  . VAL A 1 199 ? -12.58525 55.81410 29.58234 1.000 23.42897 ? 199 VAL A CA  1 
ATOM   1625 C C   . VAL A 1 199 ? -13.07213 55.10644 30.84367 1.000 25.78383 ? 199 VAL A C   1 
ATOM   1626 O O   . VAL A 1 199 ? -13.84329 55.68557 31.61586 1.000 25.63128 ? 199 VAL A O   1 
ATOM   1627 C CB  . VAL A 1 199 ? -13.40230 55.36149 28.35248 1.000 24.92002 ? 199 VAL A CB  1 
ATOM   1628 C CG1 . VAL A 1 199 ? -14.88186 55.38357 28.64239 1.000 23.24646 ? 199 VAL A CG1 1 
ATOM   1629 C CG2 . VAL A 1 199 ? -13.09632 56.27707 27.18160 1.000 27.88449 ? 199 VAL A CG2 1 
ATOM   1630 N N   . ASP A 1 200 ? -12.61371 53.86930 31.05874 1.000 24.83814 ? 200 ASP A N   1 
ATOM   1631 C CA  . ASP A 1 200 ? -12.88699 53.15247 32.30780 1.000 26.20833 ? 200 ASP A CA  1 
ATOM   1632 C C   . ASP A 1 200 ? -12.57261 54.03938 33.50891 1.000 23.79185 ? 200 ASP A C   1 
ATOM   1633 O O   . ASP A 1 200 ? -13.34960 54.12567 34.44123 1.000 23.63100 ? 200 ASP A O   1 
ATOM   1634 C CB  . ASP A 1 200 ? -12.05826 51.85988 32.42735 1.000 27.58034 ? 200 ASP A CB  1 
ATOM   1635 C CG  . ASP A 1 200 ? -12.49031 50.76401 31.45662 1.000 31.29002 ? 200 ASP A CG  1 
ATOM   1636 O OD1 . ASP A 1 200 ? -13.56830 50.87673 30.83205 1.000 33.07762 ? 200 ASP A OD1 1 
ATOM   1637 O OD2 . ASP A 1 200 ? -11.72721 49.77332 31.32678 1.000 33.46759 ? 200 ASP A OD2 1 
ATOM   1638 N N   . ASN A 1 201 ? -11.41883 54.69377 33.47666 1.000 24.48638 ? 201 ASN A N   1 
ATOM   1639 C CA  . ASN A 1 201 ? -11.00538 55.53627 34.58976 1.000 22.13995 ? 201 ASN A CA  1 
ATOM   1640 C C   . ASN A 1 201 ? -11.87770 56.78152 34.74029 1.000 23.23399 ? 201 ASN A C   1 
ATOM   1641 O O   . ASN A 1 201 ? -12.27942 57.12019 35.84680 1.000 24.13977 ? 201 ASN A O   1 
ATOM   1642 C CB  . ASN A 1 201 ? -9.54240  55.94290 34.42942 1.000 22.79039 ? 201 ASN A CB  1 
ATOM   1643 C CG  . ASN A 1 201 ? -9.10450  56.94568 35.46877 1.000 22.64493 ? 201 ASN A CG  1 
ATOM   1644 O OD1 . ASN A 1 201 ? -8.95913  56.61228 36.64347 1.000 23.74653 ? 201 ASN A OD1 1 
ATOM   1645 N ND2 . ASN A 1 201 ? -8.89817  58.18767 35.04300 1.000 21.23183 ? 201 ASN A ND2 1 
ATOM   1646 N N   . CYS A 1 202 ? -12.16738 57.45500 33.62899 1.000 23.00179 ? 202 CYS A N   1 
ATOM   1647 C CA  . CYS A 1 202 ? -13.02313 58.64559 33.64433 1.000 24.12044 ? 202 CYS A CA  1 
ATOM   1648 C C   . CYS A 1 202 ? -14.43070 58.35563 34.15488 1.000 24.69942 ? 202 CYS A C   1 
ATOM   1649 O O   . CYS A 1 202 ? -15.06876 59.21410 34.77261 1.000 25.82473 ? 202 CYS A O   1 
ATOM   1650 C CB  . CYS A 1 202 ? -13.11527 59.26496 32.24230 1.000 24.28929 ? 202 CYS A CB  1 
ATOM   1651 S SG  . CYS A 1 202 ? -11.59911 60.09085 31.70255 1.000 30.31699 ? 202 CYS A SG  1 
ATOM   1652 N N   . MET A 1 203 ? -14.90666 57.14502 33.89116 1.000 25.09891 ? 203 MET A N   1 
ATOM   1653 C CA  . MET A 1 203 ? -16.25745 56.74802 34.26578 1.000 25.59972 ? 203 MET A CA  1 
ATOM   1654 C C   . MET A 1 203 ? -16.36392 56.27091 35.72669 1.000 26.90202 ? 203 MET A C   1 
ATOM   1655 O O   . MET A 1 203 ? -17.46845 56.06965 36.22809 1.000 27.50278 ? 203 MET A O   1 
ATOM   1656 C CB  . MET A 1 203 ? -16.76874 55.65623 33.31846 1.000 24.86811 ? 203 MET A CB  1 
ATOM   1657 C CG  . MET A 1 203 ? -17.16954 56.15192 31.92222 1.000 25.55185 ? 203 MET A CG  1 
ATOM   1658 S SD  . MET A 1 203 ? -18.44699 57.42465 31.92494 1.000 31.29361 ? 203 MET A SD  1 
ATOM   1659 C CE  . MET A 1 203 ? -19.88503 56.43891 32.34119 1.000 28.81754 ? 203 MET A CE  1 
ATOM   1660 N N   . LYS A 1 204 ? -15.23337 56.09981 36.40997 1.000 24.89478 ? 204 LYS A N   1 
ATOM   1661 C CA  . LYS A 1 204 ? -15.27589 55.85111 37.85017 1.000 25.08161 ? 204 LYS A CA  1 
ATOM   1662 C C   . LYS A 1 204 ? -15.99962 56.99398 38.53860 1.000 25.22296 ? 204 LYS A C   1 
ATOM   1663 O O   . LYS A 1 204 ? -15.89746 58.14563 38.10120 1.000 27.78315 ? 204 LYS A O   1 
ATOM   1664 C CB  . LYS A 1 204 ? -13.87305 55.68424 38.43413 1.000 26.04238 ? 204 LYS A CB  1 
ATOM   1665 C CG  . LYS A 1 204 ? -13.19441 54.41114 37.99244 1.000 25.08642 ? 204 LYS A CG  1 
ATOM   1666 C CD  . LYS A 1 204 ? -11.81051 54.30417 38.58464 1.000 25.43370 ? 204 LYS A CD  1 
ATOM   1667 C CE  . LYS A 1 204 ? -11.21117 52.93444 38.28366 1.000 32.73888 ? 204 LYS A CE  1 
ATOM   1668 N NZ  . LYS A 1 204 ? -9.93276  52.74078 39.00514 1.000 36.57711 ? 204 LYS A NZ  1 
ATOM   1669 N N   . PRO A 1 205 ? -16.75464 56.67695 39.60175 1.000 26.00381 ? 205 PRO A N   1 
ATOM   1670 C CA  . PRO A 1 205 ? -17.57239 57.67560 40.29545 1.000 24.69830 ? 205 PRO A CA  1 
ATOM   1671 C C   . PRO A 1 205 ? -16.77721 58.91414 40.67648 1.000 23.68251 ? 205 PRO A C   1 
ATOM   1672 O O   . PRO A 1 205 ? -15.69418 58.79740 41.24336 1.000 23.82451 ? 205 PRO A O   1 
ATOM   1673 C CB  . PRO A 1 205 ? -18.05891 56.92519 41.53898 1.000 28.59680 ? 205 PRO A CB  1 
ATOM   1674 C CG  . PRO A 1 205 ? -18.10385 55.49093 41.09639 1.000 31.51094 ? 205 PRO A CG  1 
ATOM   1675 C CD  . PRO A 1 205 ? -16.92636 55.32765 40.17591 1.000 27.35773 ? 205 PRO A CD  1 
ATOM   1676 N N   . ASN A 1 206 ? -17.31939 60.07065 40.30453 1.000 24.18437 ? 206 ASN A N   1 
ATOM   1677 C CA  . ASN A 1 206 ? -16.78179 61.39395 40.61349 1.000 23.24501 ? 206 ASN A CA  1 
ATOM   1678 C C   . ASN A 1 206 ? -15.49659 61.79368 39.86707 1.000 23.24307 ? 206 ASN A C   1 
ATOM   1679 O O   . ASN A 1 206 ? -15.00873 62.91288 40.04848 1.000 24.70511 ? 206 ASN A O   1 
ATOM   1680 C CB  . ASN A 1 206 ? -16.55089 61.52561 42.12244 1.000 24.83366 ? 206 ASN A CB  1 
ATOM   1681 C CG  . ASN A 1 206 ? -17.82463 61.31682 42.92297 1.000 27.33334 ? 206 ASN A CG  1 
ATOM   1682 O OD1 . ASN A 1 206 ? -18.89439 61.75428 42.52204 1.000 28.54687 ? 206 ASN A OD1 1 
ATOM   1683 N ND2 . ASN A 1 206 ? -17.71210 60.62962 44.04397 1.000 25.70067 ? 206 ASN A ND2 1 
ATOM   1684 N N   . ASN A 1 207 ? -14.95771 60.92402 39.01685 1.000 22.92502 ? 207 ASN A N   1 
ATOM   1685 C CA  . ASN A 1 207 ? -13.69545 61.27497 38.35092 1.000 24.80604 ? 207 ASN A CA  1 
ATOM   1686 C C   . ASN A 1 207 ? -13.80363 62.38134 37.29168 1.000 21.22504 ? 207 ASN A C   1 
ATOM   1687 O O   . ASN A 1 207 ? -12.91271 63.22967 37.18817 1.000 22.24158 ? 207 ASN A O   1 
ATOM   1688 C CB  . ASN A 1 207 ? -13.04733 60.02833 37.74419 1.000 22.86588 ? 207 ASN A CB  1 
ATOM   1689 C CG  . ASN A 1 207 ? -12.05866 59.38698 38.70170 1.000 22.11620 ? 207 ASN A CG  1 
ATOM   1690 O OD1 . ASN A 1 207 ? -11.88314 59.86260 39.82503 1.000 22.43760 ? 207 ASN A OD1 1 
ATOM   1691 N ND2 . ASN A 1 207 ? -11.42511 58.31016 38.27636 1.000 21.78254 ? 207 ASN A ND2 1 
ATOM   1692 N N   . VAL A 1 208 ? -14.88012 62.40560 36.51759 1.000 21.68582 ? 208 VAL A N   1 
ATOM   1693 C CA  . VAL A 1 208 ? -15.04041 63.50395 35.56942 1.000 21.75796 ? 208 VAL A CA  1 
ATOM   1694 C C   . VAL A 1 208 ? -15.21864 64.82400 36.34813 1.000 20.50776 ? 208 VAL A C   1 
ATOM   1695 O O   . VAL A 1 208 ? -14.53799 65.81432 36.06788 1.000 22.13067 ? 208 VAL A O   1 
ATOM   1696 C CB  . VAL A 1 208 ? -16.22241 63.26063 34.60149 1.000 21.23004 ? 208 VAL A CB  1 
ATOM   1697 C CG1 . VAL A 1 208 ? -16.67969 64.57064 33.92833 1.000 19.31977 ? 208 VAL A CG1 1 
ATOM   1698 C CG2 . VAL A 1 208 ? -15.83690 62.21060 33.55289 1.000 21.69295 ? 208 VAL A CG2 1 
ATOM   1699 N N   . HIS A 1 209 ? -16.11468 64.81040 37.33456 1.000 21.93225 ? 209 HIS A N   1 
ATOM   1700 C CA  . HIS A 1 209 ? -16.37711 65.94998 38.22446 1.000 20.66390 ? 209 HIS A CA  1 
ATOM   1701 C C   . HIS A 1 209 ? -15.08326 66.40687 38.91645 1.000 22.76425 ? 209 HIS A C   1 
ATOM   1702 O O   . HIS A 1 209 ? -14.77090 67.60211 38.94537 1.000 21.87103 ? 209 HIS A O   1 
ATOM   1703 C CB  . HIS A 1 209 ? -17.44394 65.54705 39.25734 1.000 21.08431 ? 209 HIS A CB  1 
ATOM   1704 C CG  . HIS A 1 209 ? -18.09212 66.68588 39.98849 1.000 24.15382 ? 209 HIS A CG  1 
ATOM   1705 N ND1 . HIS A 1 209 ? -17.56080 67.95938 40.03929 1.000 26.93287 ? 209 HIS A ND1 1 
ATOM   1706 C CD2 . HIS A 1 209 ? -19.22402 66.72932 40.73439 1.000 25.94783 ? 209 HIS A CD2 1 
ATOM   1707 C CE1 . HIS A 1 209 ? -18.33991 68.73453 40.77180 1.000 23.29564 ? 209 HIS A CE1 1 
ATOM   1708 N NE2 . HIS A 1 209 ? -19.35915 68.01193 41.20433 1.000 26.92753 ? 209 HIS A NE2 1 
ATOM   1709 N N   . GLY A 1 210 ? -14.33935 65.44493 39.47112 1.000 21.41876 ? 210 GLY A N   1 
ATOM   1710 C CA  . GLY A 1 210 ? -13.07394 65.72297 40.12878 1.000 18.83608 ? 210 GLY A CA  1 
ATOM   1711 C C   . GLY A 1 210 ? -12.11383 66.46637 39.21893 1.000 20.48282 ? 210 GLY A C   1 
ATOM   1712 O O   . GLY A 1 210 ? -11.52392 67.46431 39.61254 1.000 20.15445 ? 210 GLY A O   1 
ATOM   1713 N N   . GLY A 1 211 ? -11.97296 65.98397 37.98919 1.000 20.32160 ? 211 GLY A N   1 
ATOM   1714 C CA  . GLY A 1 211 ? -11.09204 66.60979 37.02498 1.000 18.94665 ? 211 GLY A CA  1 
ATOM   1715 C C   . GLY A 1 211 ? -11.55592 68.00436 36.65126 1.000 20.60320 ? 211 GLY A C   1 
ATOM   1716 O O   . GLY A 1 211 ? -10.74163 68.92616 36.58100 1.000 20.41655 ? 211 GLY A O   1 
ATOM   1717 N N   . PHE A 1 212 ? -12.86148 68.16517 36.42947 1.000 19.87574 ? 212 PHE A N   1 
ATOM   1718 C CA  . PHE A 1 212 ? -13.41549 69.47259 36.07094 1.000 19.50703 ? 212 PHE A CA  1 
ATOM   1719 C C   . PHE A 1 212 ? -13.25280 70.49101 37.21403 1.000 22.28949 ? 212 PHE A C   1 
ATOM   1720 O O   . PHE A 1 212 ? -13.11845 71.70161 36.97260 1.000 21.63328 ? 212 PHE A O   1 
ATOM   1721 C CB  . PHE A 1 212 ? -14.88929 69.34487 35.66585 1.000 19.32551 ? 212 PHE A CB  1 
ATOM   1722 C CG  . PHE A 1 212 ? -15.10443 68.67524 34.31602 1.000 19.84731 ? 212 PHE A CG  1 
ATOM   1723 C CD1 . PHE A 1 212 ? -14.04505 68.10355 33.61847 1.000 19.45683 ? 212 PHE A CD1 1 
ATOM   1724 C CD2 . PHE A 1 212 ? -16.36441 68.64003 33.74452 1.000 20.62575 ? 212 PHE A CD2 1 
ATOM   1725 C CE1 . PHE A 1 212 ? -14.24689 67.48097 32.39229 1.000 20.34401 ? 212 PHE A CE1 1 
ATOM   1726 C CE2 . PHE A 1 212 ? -16.57634 68.03106 32.51763 1.000 21.12885 ? 212 PHE A CE2 1 
ATOM   1727 C CZ  . PHE A 1 212 ? -15.51115 67.45188 31.83665 1.000 21.97260 ? 212 PHE A CZ  1 
ATOM   1728 N N   . ASN A 1 213 ? -13.24200 69.99877 38.45355 1.000 21.76135 ? 213 ASN A N   1 
ATOM   1729 C CA  . ASN A 1 213 ? -12.98323 70.86106 39.60225 1.000 21.28107 ? 213 ASN A CA  1 
ATOM   1730 C C   . ASN A 1 213 ? -11.60223 71.51059 39.56676 1.000 20.86027 ? 213 ASN A C   1 
ATOM   1731 O O   . ASN A 1 213 ? -11.41646 72.57939 40.13445 1.000 21.61490 ? 213 ASN A O   1 
ATOM   1732 C CB  . ASN A 1 213 ? -13.14501 70.08491 40.90810 1.000 21.05535 ? 213 ASN A CB  1 
ATOM   1733 C CG  . ASN A 1 213 ? -14.56046 70.14288 41.43777 1.000 24.83931 ? 213 ASN A CG  1 
ATOM   1734 O OD1 . ASN A 1 213 ? -15.45530 70.63834 40.76556 1.000 25.16311 ? 213 ASN A OD1 1 
ATOM   1735 N ND2 . ASN A 1 213 ? -14.76972 69.63297 42.64571 1.000 25.15966 ? 213 ASN A ND2 1 
ATOM   1736 N N   . TYR A 1 214 ? -10.64096 70.86876 38.90767 1.000 20.03459 ? 214 TYR A N   1 
ATOM   1737 C CA  . TYR A 1 214 ? -9.32724  71.48580 38.72303 1.000 21.24481 ? 214 TYR A CA  1 
ATOM   1738 C C   . TYR A 1 214 ? -9.46975  72.76257 37.90854 1.000 21.04970 ? 214 TYR A C   1 
ATOM   1739 O O   . TYR A 1 214 ? -8.82376  73.77024 38.20617 1.000 21.25446 ? 214 TYR A O   1 
ATOM   1740 C CB  . TYR A 1 214 ? -8.34115  70.53100 38.03837 1.000 19.25384 ? 214 TYR A CB  1 
ATOM   1741 C CG  . TYR A 1 214 ? -7.52693  69.67005 38.99740 1.000 21.58959 ? 214 TYR A CG  1 
ATOM   1742 C CD1 . TYR A 1 214 ? -8.14212  68.75727 39.83917 1.000 20.61844 ? 214 TYR A CD1 1 
ATOM   1743 C CD2 . TYR A 1 214 ? -6.13819  69.77227 39.04547 1.000 21.95338 ? 214 TYR A CD2 1 
ATOM   1744 C CE1 . TYR A 1 214 ? -7.40009  67.96880 40.71090 1.000 22.21016 ? 214 TYR A CE1 1 
ATOM   1745 C CE2 . TYR A 1 214 ? -5.38747  68.99106 39.89789 1.000 20.89670 ? 214 TYR A CE2 1 
ATOM   1746 C CZ  . TYR A 1 214 ? -6.01767  68.08864 40.73061 1.000 23.12720 ? 214 TYR A CZ  1 
ATOM   1747 O OH  . TYR A 1 214 ? -5.25924  67.31285 41.57852 1.000 20.14478 ? 214 TYR A OH  1 
ATOM   1748 N N   . TYR A 1 215 ? -10.32250 72.71302 36.88476 1.000 22.13762 ? 215 TYR A N   1 
ATOM   1749 C CA  . TYR A 1 215 ? -10.57595 73.87532 36.03321 1.000 20.86137 ? 215 TYR A CA  1 
ATOM   1750 C C   . TYR A 1 215 ? -11.34221 74.95167 36.78004 1.000 20.41246 ? 215 TYR A C   1 
ATOM   1751 O O   . TYR A 1 215 ? -11.05790 76.14330 36.62475 1.000 22.55591 ? 215 TYR A O   1 
ATOM   1752 C CB  . TYR A 1 215 ? -11.31800 73.44887 34.75443 1.000 19.22776 ? 215 TYR A CB  1 
ATOM   1753 C CG  . TYR A 1 215 ? -10.41483 72.58306 33.91576 1.000 21.26965 ? 215 TYR A CG  1 
ATOM   1754 C CD1 . TYR A 1 215 ? -9.52274  73.15140 33.01574 1.000 19.49496 ? 215 TYR A CD1 1 
ATOM   1755 C CD2 . TYR A 1 215 ? -10.39020 71.20964 34.08525 1.000 20.61222 ? 215 TYR A CD2 1 
ATOM   1756 C CE1 . TYR A 1 215 ? -8.66422  72.37164 32.28254 1.000 22.28187 ? 215 TYR A CE1 1 
ATOM   1757 C CE2 . TYR A 1 215 ? -9.53216  70.42177 33.35573 1.000 20.40777 ? 215 TYR A CE2 1 
ATOM   1758 C CZ  . TYR A 1 215 ? -8.67714  71.00468 32.45384 1.000 19.21416 ? 215 TYR A CZ  1 
ATOM   1759 O OH  . TYR A 1 215 ? -7.81640  70.21605 31.73940 1.000 20.22675 ? 215 TYR A OH  1 
ATOM   1760 N N   . ARG A 1 216 ? -12.28428 74.53504 37.62032 1.000 21.61747 ? 216 ARG A N   1 
ATOM   1761 C CA  . ARG A 1 216 ? -13.07761 75.48516 38.40298 1.000 23.49156 ? 216 ARG A CA  1 
ATOM   1762 C C   . ARG A 1 216 ? -12.24356 76.21072 39.45193 1.000 24.13931 ? 216 ARG A C   1 
ATOM   1763 O O   . ARG A 1 216 ? -12.42352 77.40284 39.67928 1.000 24.31637 ? 216 ARG A O   1 
ATOM   1764 C CB  . ARG A 1 216 ? -14.26015 74.77270 39.06781 1.000 22.12352 ? 216 ARG A CB  1 
ATOM   1765 C CG  . ARG A 1 216 ? -15.23675 74.21261 38.04130 1.000 22.61705 ? 216 ARG A CG  1 
ATOM   1766 C CD  . ARG A 1 216 ? -16.29490 73.31089 38.66513 1.000 21.41900 ? 216 ARG A CD  1 
ATOM   1767 N NE  . ARG A 1 216 ? -17.09732 72.69403 37.61857 1.000 24.12806 ? 216 ARG A NE  1 
ATOM   1768 C CZ  . ARG A 1 216 ? -18.11573 71.87246 37.82980 1.000 24.09432 ? 216 ARG A CZ  1 
ATOM   1769 N NH1 . ARG A 1 216 ? -18.47203 71.55442 39.06339 1.000 24.55522 ? 216 ARG A NH1 1 
ATOM   1770 N NH2 . ARG A 1 216 ? -18.77760 71.37744 36.79735 1.000 21.20872 ? 216 ARG A NH2 1 
ATOM   1771 N N   . SER A 1 217 ? -11.31996 75.48697 40.07427 1.000 22.50791 ? 217 SER A N   1 
ATOM   1772 C CA  . SER A 1 217 ? -10.49052 76.04831 41.13312 1.000 21.86522 ? 217 SER A CA  1 
ATOM   1773 C C   . SER A 1 217 ? -9.32257  76.87397 40.59456 1.000 25.44128 ? 217 SER A C   1 
ATOM   1774 O O   . SER A 1 217 ? -8.94269  77.89075 41.18297 1.000 24.45589 ? 217 SER A O   1 
ATOM   1775 C CB  . SER A 1 217 ? -9.95886  74.92079 42.02231 1.000 23.44471 ? 217 SER A CB  1 
ATOM   1776 O OG  . SER A 1 217 ? -9.25098  75.41587 43.13502 1.000 24.37639 ? 217 SER A OG  1 
ATOM   1777 N N   . ASN A 1 218 ? -8.74767  76.43354 39.47784 1.000 23.34849 ? 218 ASN A N   1 
ATOM   1778 C CA  . ASN A 1 218 ? -7.49542  77.01147 39.00887 1.000 23.49060 ? 218 ASN A CA  1 
ATOM   1779 C C   . ASN A 1 218 ? -7.57259  77.76100 37.67628 1.000 24.42713 ? 218 ASN A C   1 
ATOM   1780 O O   . ASN A 1 218 ? -6.62856  78.44109 37.29357 1.000 22.97549 ? 218 ASN A O   1 
ATOM   1781 C CB  . ASN A 1 218 ? -6.43637  75.91290 38.90158 1.000 24.21051 ? 218 ASN A CB  1 
ATOM   1782 C CG  . ASN A 1 218 ? -6.27619  75.12568 40.19795 1.000 21.59541 ? 218 ASN A CG  1 
ATOM   1783 O OD1 . ASN A 1 218 ? -5.68071  75.60586 41.16168 1.000 21.33502 ? 218 ASN A OD1 1 
ATOM   1784 N ND2 . ASN A 1 218 ? -6.80475  73.90879 40.21742 1.000 20.15818 ? 218 ASN A ND2 1 
ATOM   1785 N N   . LEU A 1 219 ? -8.69079  77.64203 36.96996 1.000 24.86165 ? 219 LEU A N   1 
ATOM   1786 C CA  . LEU A 1 219 ? -8.76033  78.20370 35.62724 1.000 23.12930 ? 219 LEU A CA  1 
ATOM   1787 C C   . LEU A 1 219 ? -10.08027 78.90474 35.30351 1.000 23.86145 ? 219 LEU A C   1 
ATOM   1788 O O   . LEU A 1 219 ? -10.39396 79.12516 34.13893 1.000 23.49150 ? 219 LEU A O   1 
ATOM   1789 C CB  . LEU A 1 219 ? -8.49150  77.10616 34.60304 1.000 21.22752 ? 219 LEU A CB  1 
ATOM   1790 C CG  . LEU A 1 219 ? -7.01686  76.85951 34.27265 1.000 28.54156 ? 219 LEU A CG  1 
ATOM   1791 C CD1 . LEU A 1 219 ? -6.83334  75.69186 33.30233 1.000 28.05358 ? 219 LEU A CD1 1 
ATOM   1792 C CD2 . LEU A 1 219 ? -6.39607  78.12375 33.70505 1.000 27.22095 ? 219 LEU A CD2 1 
ATOM   1793 N N   . SER A 1 220 ? -10.84895 79.24574 36.33269 1.000 23.56300 ? 220 SER A N   1 
ATOM   1794 C CA  . SER A 1 220 ? -11.99338 80.13085 36.15885 1.000 24.74113 ? 220 SER A CA  1 
ATOM   1795 C C   . SER A 1 220 ? -11.47500 81.52729 35.83311 1.000 24.47487 ? 220 SER A C   1 
ATOM   1796 O O   . SER A 1 220 ? -10.29838 81.81096 36.05188 1.000 21.88353 ? 220 SER A O   1 
ATOM   1797 C CB  . SER A 1 220 ? -12.86298 80.17138 37.41854 1.000 23.59516 ? 220 SER A CB  1 
ATOM   1798 O OG  . SER A 1 220 ? -12.37118 81.13365 38.34006 1.000 26.26473 ? 220 SER A OG  1 
ATOM   1799 N N   . VAL A 1 221 ? -12.34105 82.40250 35.32206 1.000 24.38672 ? 221 VAL A N   1 
ATOM   1800 C CA  . VAL A 1 221 ? -11.89409 83.75486 34.98785 1.000 25.38564 ? 221 VAL A CA  1 
ATOM   1801 C C   . VAL A 1 221 ? -11.59629 84.61956 36.22564 1.000 25.82479 ? 221 VAL A C   1 
ATOM   1802 O O   . VAL A 1 221 ? -11.13112 85.74039 36.09600 1.000 28.53826 ? 221 VAL A O   1 
ATOM   1803 C CB  . VAL A 1 221 ? -12.91982 84.49318 34.09192 1.000 25.24775 ? 221 VAL A CB  1 
ATOM   1804 C CG1 . VAL A 1 221 ? -12.98161 83.83671 32.70538 1.000 21.54179 ? 221 VAL A CG1 1 
ATOM   1805 C CG2 . VAL A 1 221 ? -14.28925 84.55479 34.75831 1.000 22.38911 ? 221 VAL A CG2 1 
ATOM   1806 N N   . THR A 1 222 ? -11.84177 84.09879 37.42041 1.000 25.45589 ? 222 THR A N   1 
ATOM   1807 C CA  . THR A 1 222 ? -11.44324 84.80568 38.63610 1.000 29.15520 ? 222 THR A CA  1 
ATOM   1808 C C   . THR A 1 222 ? -10.43558 84.00797 39.46105 1.000 30.68328 ? 222 THR A C   1 
ATOM   1809 O O   . THR A 1 222 ? -10.17950 84.34733 40.61149 1.000 28.85791 ? 222 THR A O   1 
ATOM   1810 C CB  . THR A 1 222 ? -12.64759 85.13242 39.54134 1.000 29.53898 ? 222 THR A CB  1 
ATOM   1811 O OG1 . THR A 1 222 ? -13.28825 83.91751 39.94461 1.000 34.07976 ? 222 THR A OG1 1 
ATOM   1812 C CG2 . THR A 1 222 ? -13.64194 86.01416 38.81507 1.000 28.89383 ? 222 THR A CG2 1 
ATOM   1813 N N   . SER A 1 223 ? -9.87165  82.95051 38.87772 1.000 27.61813 ? 223 SER A N   1 
ATOM   1814 C CA  . SER A 1 223 ? -8.89874  82.12042 39.58412 1.000 26.92196 ? 223 SER A CA  1 
ATOM   1815 C C   . SER A 1 223 ? -7.49737  82.71291 39.55716 1.000 30.74612 ? 223 SER A C   1 
ATOM   1816 O O   . SER A 1 223 ? -7.11142  83.38734 38.60145 1.000 29.52467 ? 223 SER A O   1 
ATOM   1817 C CB  . SER A 1 223 ? -8.84980  80.71789 38.98871 1.000 24.57631 ? 223 SER A CB  1 
ATOM   1818 O OG  . SER A 1 223 ? -10.08385 80.04950 39.14456 1.000 26.58836 ? 223 SER A OG  1 
ATOM   1819 N N   . ASP A 1 224 ? -6.73241  82.44232 40.60762 1.000 30.10160 ? 224 ASP A N   1 
ATOM   1820 C CA  . ASP A 1 224 ? -5.31061  82.76849 40.61091 1.000 32.44118 ? 224 ASP A CA  1 
ATOM   1821 C C   . ASP A 1 224 ? -4.54229  81.73072 41.41715 1.000 28.30051 ? 224 ASP A C   1 
ATOM   1822 O O   . ASP A 1 224 ? -4.41473  81.84580 42.63449 1.000 29.83797 ? 224 ASP A O   1 
ATOM   1823 C CB  . ASP A 1 224 ? -5.05926  84.17003 41.17050 1.000 34.54479 ? 224 ASP A CB  1 
ATOM   1824 C CG  . ASP A 1 224 ? -3.58070  84.54393 41.15778 1.000 42.14283 ? 224 ASP A CG  1 
ATOM   1825 O OD1 . ASP A 1 224 ? -2.81792  84.00824 40.30824 1.000 36.31244 ? 224 ASP A OD1 1 
ATOM   1826 O OD2 . ASP A 1 224 ? -3.17854  85.36697 42.00496 1.000 45.27768 ? 224 ASP A OD2 1 
ATOM   1827 N N   . PRO A 1 225 ? -4.02081  80.71288 40.72795 1.000 28.23668 ? 225 PRO A N   1 
ATOM   1828 C CA  . PRO A 1 225 ? -3.37170  79.56204 41.35484 1.000 26.71730 ? 225 PRO A CA  1 
ATOM   1829 C C   . PRO A 1 225 ? -1.91683  79.82061 41.73251 1.000 26.01717 ? 225 PRO A C   1 
ATOM   1830 O O   . PRO A 1 225 ? -1.30567  78.98612 42.39419 1.000 28.26171 ? 225 PRO A O   1 
ATOM   1831 C CB  . PRO A 1 225 ? -3.46458  78.49385 40.26569 1.000 25.14069 ? 225 PRO A CB  1 
ATOM   1832 C CG  . PRO A 1 225 ? -3.35496  79.28584 38.99657 1.000 26.73583 ? 225 PRO A CG  1 
ATOM   1833 C CD  . PRO A 1 225 ? -4.08310  80.57975 39.26153 1.000 26.92712 ? 225 PRO A CD  1 
ATOM   1834 N N   . TRP A 1 226 ? -1.37226  80.95563 41.31341 1.000 26.34360 ? 226 TRP A N   1 
ATOM   1835 C CA  . TRP A 1 226 ? 0.04218   81.25136 41.52426 1.000 26.33809 ? 226 TRP A CA  1 
ATOM   1836 C C   . TRP A 1 226 ? 0.30370   82.04356 42.81300 1.000 28.97481 ? 226 TRP A C   1 
ATOM   1837 O O   . TRP A 1 226 ? -0.47164  82.91872 43.17936 1.000 28.58378 ? 226 TRP A O   1 
ATOM   1838 C CB  . TRP A 1 226 ? 0.59679   82.03346 40.33455 1.000 24.87828 ? 226 TRP A CB  1 
ATOM   1839 C CG  . TRP A 1 226 ? 0.48151   81.33299 39.00638 1.000 26.50659 ? 226 TRP A CG  1 
ATOM   1840 C CD1 . TRP A 1 226 ? -0.35498  81.65851 37.97530 1.000 23.39475 ? 226 TRP A CD1 1 
ATOM   1841 C CD2 . TRP A 1 226 ? 1.23717   80.19720 38.56545 1.000 24.32990 ? 226 TRP A CD2 1 
ATOM   1842 N NE1 . TRP A 1 226 ? -0.16930  80.79237 36.92526 1.000 24.45098 ? 226 TRP A NE1 1 
ATOM   1843 C CE2 . TRP A 1 226 ? 0.80663   79.89033 37.25873 1.000 23.85022 ? 226 TRP A CE2 1 
ATOM   1844 C CE3 . TRP A 1 226 ? 2.23756   79.41653 39.14618 1.000 22.93047 ? 226 TRP A CE3 1 
ATOM   1845 C CZ2 . TRP A 1 226 ? 1.34328   78.83292 36.52121 1.000 22.56118 ? 226 TRP A CZ2 1 
ATOM   1846 C CZ3 . TRP A 1 226 ? 2.77720   78.37153 38.40946 1.000 23.93732 ? 226 TRP A CZ3 1 
ATOM   1847 C CH2 . TRP A 1 226 ? 2.32762   78.08976 37.11229 1.000 23.31921 ? 226 TRP A CH2 1 
ATOM   1848 N N   . THR A 1 227 ? 1.41055   81.73939 43.48239 1.000 28.05762 ? 227 THR A N   1 
ATOM   1849 C CA  . THR A 1 227 ? 1.82177   82.47306 44.67818 1.000 28.21189 ? 227 THR A CA  1 
ATOM   1850 C C   . THR A 1 227 ? 2.99877   83.39898 44.38982 1.000 27.90471 ? 227 THR A C   1 
ATOM   1851 O O   . THR A 1 227 ? 3.58127   83.34608 43.31050 1.000 26.97098 ? 227 THR A O   1 
ATOM   1852 C CB  . THR A 1 227 ? 2.22872   81.52175 45.80913 1.000 27.71182 ? 227 THR A CB  1 
ATOM   1853 O OG1 . THR A 1 227 ? 3.37283   80.76288 45.39980 1.000 25.98009 ? 227 THR A OG1 1 
ATOM   1854 C CG2 . THR A 1 227 ? 1.09334   80.58315 46.15336 1.000 27.22646 ? 227 THR A CG2 1 
ATOM   1855 N N   . ASP A 1 228 ? 3.36653   84.23505 45.35706 1.000 28.21842 ? 228 ASP A N   1 
ATOM   1856 C CA  . ASP A 1 228 ? 4.54024   85.09240 45.18154 1.000 29.75596 ? 228 ASP A CA  1 
ATOM   1857 C C   . ASP A 1 228 ? 5.78283   84.24705 44.98182 1.000 27.85567 ? 228 ASP A C   1 
ATOM   1858 O O   . ASP A 1 228 ? 6.65388   84.58438 44.18649 1.000 28.59201 ? 228 ASP A O   1 
ATOM   1859 C CB  . ASP A 1 228 ? 4.73858   86.02235 46.37754 1.000 34.07000 ? 228 ASP A CB  1 
ATOM   1860 C CG  . ASP A 1 228 ? 3.66699   87.08470 46.47035 1.000 39.07237 ? 228 ASP A CG  1 
ATOM   1861 O OD1 . ASP A 1 228 ? 3.10402   87.44713 45.41865 1.000 40.90615 ? 228 ASP A OD1 1 
ATOM   1862 O OD2 . ASP A 1 228 ? 3.38924   87.55108 47.59450 1.000 41.35285 ? 228 ASP A OD2 1 
ATOM   1863 N N   . LEU A 1 229 ? 5.85356   83.14303 45.71073 1.000 26.92802 ? 229 LEU A N   1 
ATOM   1864 C CA  . LEU A 1 229 ? 7.00923   82.25823 45.64423 1.000 27.32203 ? 229 LEU A CA  1 
ATOM   1865 C C   . LEU A 1 229 ? 7.16259   81.66119 44.24854 1.000 25.30635 ? 229 LEU A C   1 
ATOM   1866 O O   . LEU A 1 229 ? 8.27916   81.47620 43.76845 1.000 27.18688 ? 229 LEU A O   1 
ATOM   1867 C CB  . LEU A 1 229 ? 6.88538   81.15342 46.68681 1.000 23.76894 ? 229 LEU A CB  1 
ATOM   1868 C CG  . LEU A 1 229 ? 8.02952   80.15281 46.80018 1.000 27.20822 ? 229 LEU A CG  1 
ATOM   1869 C CD1 . LEU A 1 229 ? 9.35532   80.86001 47.09845 1.000 27.52594 ? 229 LEU A CD1 1 
ATOM   1870 C CD2 . LEU A 1 229 ? 7.69955   79.12473 47.88190 1.000 25.29989 ? 229 LEU A CD2 1 
ATOM   1871 N N   . ASP A 1 230 ? 6.03749   81.37226 43.59939 1.000 24.67247 ? 230 ASP A N   1 
ATOM   1872 C CA  . ASP A 1 230 ? 6.04054   80.87577 42.21672 1.000 23.33882 ? 230 ASP A CA  1 
ATOM   1873 C C   . ASP A 1 230 ? 6.68032   81.84788 41.23334 1.000 24.79611 ? 230 ASP A C   1 
ATOM   1874 O O   . ASP A 1 230 ? 7.20122   81.44275 40.18497 1.000 26.07004 ? 230 ASP A O   1 
ATOM   1875 C CB  . ASP A 1 230 ? 4.61279   80.57925 41.75913 1.000 24.17057 ? 230 ASP A CB  1 
ATOM   1876 C CG  . ASP A 1 230 ? 4.01613   79.39872 42.46795 1.000 23.81896 ? 230 ASP A CG  1 
ATOM   1877 O OD1 . ASP A 1 230 ? 4.79633   78.50683 42.86770 1.000 23.81510 ? 230 ASP A OD1 1 
ATOM   1878 O OD2 . ASP A 1 230 ? 2.77397   79.35874 42.61686 1.000 23.96338 ? 230 ASP A OD2 1 
ATOM   1879 N N   . ARG A 1 231 ? 6.62156   83.13443 41.56156 1.000 27.57239 ? 231 ARG A N   1 
ATOM   1880 C CA  . ARG A 1 231 ? 7.18885   84.17096 40.70806 1.000 28.46296 ? 231 ARG A CA  1 
ATOM   1881 C C   . ARG A 1 231 ? 8.66225   84.45332 41.03758 1.000 30.33105 ? 231 ARG A C   1 
ATOM   1882 O O   . ARG A 1 231 ? 9.11444   85.59676 41.02978 1.000 38.52025 ? 231 ARG A O   1 
ATOM   1883 C CB  . ARG A 1 231 ? 6.35080   85.44734 40.82320 1.000 30.59429 ? 231 ARG A CB  1 
ATOM   1884 C CG  . ARG A 1 231 ? 5.01809   85.36783 40.07889 1.000 36.89317 ? 231 ARG A CG  1 
ATOM   1885 C CD  . ARG A 1 231 ? 4.28147   86.68878 40.13648 1.000 42.25476 ? 231 ARG A CD  1 
ATOM   1886 N NE  . ARG A 1 231 ? 3.58645   86.80135 41.39917 1.000 43.06728 ? 231 ARG A NE  1 
ATOM   1887 C CZ  . ARG A 1 231 ? 2.36711   86.32628 41.63828 1.000 42.87765 ? 231 ARG A CZ  1 
ATOM   1888 N NH1 . ARG A 1 231 ? 1.85140   86.50762 42.85596 1.000 38.41635 ? 231 ARG A NH1 1 
ATOM   1889 N NH2 . ARG A 1 231 ? 1.66777   85.67479 40.68696 1.000 39.18766 ? 231 ARG A NH2 1 
ATOM   1890 N N   . THR A 1 232 ? 9.39936   83.40226 41.35601 1.000 27.16962 ? 232 THR A N   1 
ATOM   1891 C CA  . THR A 1 232 ? 10.81048  83.53608 41.62130 1.000 27.29994 ? 232 THR A CA  1 
ATOM   1892 C C   . THR A 1 232 ? 11.58350  82.68694 40.62652 1.000 26.94251 ? 232 THR A C   1 
ATOM   1893 O O   . THR A 1 232 ? 11.05300  81.73204 40.05310 1.000 26.06137 ? 232 THR A O   1 
ATOM   1894 C CB  . THR A 1 232 ? 11.16645  83.11904 43.06732 1.000 30.14607 ? 232 THR A CB  1 
ATOM   1895 O OG1 . THR A 1 232 ? 10.75201  81.76743 43.28829 1.000 30.53905 ? 232 THR A OG1 1 
ATOM   1896 C CG2 . THR A 1 232 ? 10.47232  84.03309 44.07644 1.000 27.66227 ? 232 THR A CG2 1 
ATOM   1897 N N   . VAL A 1 233 ? 12.83811  83.05443 40.42070 1.000 26.09159 ? 233 VAL A N   1 
ATOM   1898 C CA  . VAL A 1 233 ? 13.72928  82.31493 39.55614 1.000 25.63481 ? 233 VAL A CA  1 
ATOM   1899 C C   . VAL A 1 233 ? 14.21740  81.08971 40.30323 1.000 26.27869 ? 233 VAL A C   1 
ATOM   1900 O O   . VAL A 1 233 ? 14.56685  81.18380 41.46775 1.000 29.87516 ? 233 VAL A O   1 
ATOM   1901 C CB  . VAL A 1 233 ? 14.93215  83.17471 39.11548 1.000 25.91923 ? 233 VAL A CB  1 
ATOM   1902 C CG1 . VAL A 1 233 ? 15.87902  82.35835 38.24092 1.000 27.12520 ? 233 VAL A CG1 1 
ATOM   1903 C CG2 . VAL A 1 233 ? 14.45216  84.43721 38.39359 1.000 24.17354 ? 233 VAL A CG2 1 
ATOM   1904 N N   . SER A 1 234 ? 14.21798  79.93775 39.64430 1.000 27.11218 ? 234 SER A N   1 
ATOM   1905 C CA  . SER A 1 234 ? 14.82453  78.75371 40.22449 1.000 26.28771 ? 234 SER A CA  1 
ATOM   1906 C C   . SER A 1 234 ? 16.13350  78.42176 39.52958 1.000 27.74987 ? 234 SER A C   1 
ATOM   1907 O O   . SER A 1 234 ? 16.19684  78.41516 38.30791 1.000 26.42690 ? 234 SER A O   1 
ATOM   1908 C CB  . SER A 1 234 ? 13.87955  77.56085 40.12781 1.000 24.54903 ? 234 SER A CB  1 
ATOM   1909 O OG  . SER A 1 234 ? 14.59112  76.37083 40.38546 1.000 27.34865 ? 234 SER A OG  1 
ATOM   1910 N N   . ASP A 1 235 ? 17.18025  78.12714 40.29011 1.000 30.26049 ? 235 ASP A N   1 
ATOM   1911 C CA  . ASP A 1 235 ? 18.40750  77.66846 39.65151 1.000 30.68834 ? 235 ASP A CA  1 
ATOM   1912 C C   . ASP A 1 235 ? 18.63979  76.17220 39.85335 1.000 29.76752 ? 235 ASP A C   1 
ATOM   1913 O O   . ASP A 1 235 ? 19.75746  75.69989 39.74735 1.000 29.43909 ? 235 ASP A O   1 
ATOM   1914 C CB  . ASP A 1 235 ? 19.61894  78.46943 40.14064 1.000 41.96433 ? 235 ASP A CB  1 
ATOM   1915 C CG  . ASP A 1 235 ? 19.65419  78.62913 41.63480 1.000 51.61151 ? 235 ASP A CG  1 
ATOM   1916 O OD1 . ASP A 1 235 ? 19.50914  77.61583 42.34983 1.000 58.09649 ? 235 ASP A OD1 1 
ATOM   1917 O OD2 . ASP A 1 235 ? 19.82564  79.78158 42.09202 1.000 57.50869 ? 235 ASP A OD2 1 
ATOM   1918 N N   . LEU A 1 236 ? 17.57480  75.42906 40.12656 1.000 30.00149 ? 236 LEU A N   1 
ATOM   1919 C CA  . LEU A 1 236 ? 17.64632  73.97043 40.09501 1.000 28.86120 ? 236 LEU A CA  1 
ATOM   1920 C C   . LEU A 1 236 ? 17.82276  73.50062 38.65923 1.000 25.90011 ? 236 LEU A C   1 
ATOM   1921 O O   . LEU A 1 236 ? 17.28728  74.11752 37.74955 1.000 27.31398 ? 236 LEU A O   1 
ATOM   1922 C CB  . LEU A 1 236 ? 16.38868  73.34790 40.70017 1.000 27.70496 ? 236 LEU A CB  1 
ATOM   1923 C CG  . LEU A 1 236 ? 16.44641  72.91188 42.16402 1.000 41.68288 ? 236 LEU A CG  1 
ATOM   1924 C CD1 . LEU A 1 236 ? 17.09980  71.53825 42.26964 1.000 39.69692 ? 236 LEU A CD1 1 
ATOM   1925 C CD2 . LEU A 1 236 ? 17.19226  73.93750 43.02592 1.000 42.73413 ? 236 LEU A CD2 1 
ATOM   1926 N N   . PRO A 1 237 ? 18.59029  72.41922 38.44995 1.000 25.30418 ? 237 PRO A N   1 
ATOM   1927 C CA  . PRO A 1 237 ? 18.73942  71.86351 37.10358 1.000 28.19222 ? 237 PRO A CA  1 
ATOM   1928 C C   . PRO A 1 237 ? 17.40806  71.32074 36.62431 1.000 27.76008 ? 237 PRO A C   1 
ATOM   1929 O O   . PRO A 1 237 ? 16.84253  70.45580 37.28831 1.000 25.95382 ? 237 PRO A O   1 
ATOM   1930 C CB  . PRO A 1 237 ? 19.76038  70.72446 37.28333 1.000 26.17197 ? 237 PRO A CB  1 
ATOM   1931 C CG  . PRO A 1 237 ? 20.41981  70.98548 38.59239 1.000 29.26018 ? 237 PRO A CG  1 
ATOM   1932 C CD  . PRO A 1 237 ? 19.39192  71.68037 39.44042 1.000 29.39509 ? 237 PRO A CD  1 
ATOM   1933 N N   . VAL A 1 238 ? 16.90582  71.83208 35.50683 1.000 25.49155 ? 238 VAL A N   1 
ATOM   1934 C CA  . VAL A 1 238 ? 15.63239  71.36622 34.98225 1.000 21.83787 ? 238 VAL A CA  1 
ATOM   1935 C C   . VAL A 1 238 ? 15.76457  70.97678 33.51955 1.000 24.46253 ? 238 VAL A C   1 
ATOM   1936 O O   . VAL A 1 238 ? 16.26324  71.75141 32.69656 1.000 21.86452 ? 238 VAL A O   1 
ATOM   1937 C CB  . VAL A 1 238 ? 14.53254  72.43182 35.12659 1.000 23.94666 ? 238 VAL A CB  1 
ATOM   1938 C CG1 . VAL A 1 238 ? 13.20242  71.88536 34.60660 1.000 21.77492 ? 238 VAL A CG1 1 
ATOM   1939 C CG2 . VAL A 1 238 ? 14.41148  72.89020 36.57520 1.000 21.61046 ? 238 VAL A CG2 1 
ATOM   1940 N N   . THR A 1 239 ? 15.33055  69.75936 33.21163 1.000 25.05603 ? 239 THR A N   1 
ATOM   1941 C CA  . THR A 1 239 ? 15.30589  69.25322 31.84539 1.000 21.57182 ? 239 THR A CA  1 
ATOM   1942 C C   . THR A 1 239 ? 13.92877  69.49559 31.23888 1.000 22.98285 ? 239 THR A C   1 
ATOM   1943 O O   . THR A 1 239 ? 12.91434  69.00983 31.75470 1.000 23.50821 ? 239 THR A O   1 
ATOM   1944 C CB  . THR A 1 239 ? 15.63858  67.74984 31.81008 1.000 24.43718 ? 239 THR A CB  1 
ATOM   1945 O OG1 . THR A 1 239 ? 16.89642  67.51963 32.46622 1.000 25.66266 ? 239 THR A OG1 1 
ATOM   1946 C CG2 . THR A 1 239 ? 15.68468  67.23282 30.38880 1.000 25.36072 ? 239 THR A CG2 1 
ATOM   1947 N N   . MET A 1 240 ? 13.87071  70.25916 30.15792 1.000 21.29957 ? 240 MET A N   1 
ATOM   1948 C CA  . MET A 1 240 ? 12.57654  70.56289 29.56229 1.000 23.20084 ? 240 MET A CA  1 
ATOM   1949 C C   . MET A 1 240 ? 12.46411  70.03090 28.14791 1.000 22.43485 ? 240 MET A C   1 
ATOM   1950 O O   . MET A 1 240 ? 13.40481  70.10069 27.37271 1.000 23.77587 ? 240 MET A O   1 
ATOM   1951 C CB  . MET A 1 240 ? 12.31709  72.06800 29.57763 1.000 21.37607 ? 240 MET A CB  1 
ATOM   1952 C CG  . MET A 1 240 ? 12.32902  72.66594 30.97612 1.000 22.65293 ? 240 MET A CG  1 
ATOM   1953 S SD  . MET A 1 240 ? 12.15790  74.44993 30.90689 1.000 24.61609 ? 240 MET A SD  1 
ATOM   1954 C CE  . MET A 1 240 ? 12.42259  74.90554 32.61708 1.000 23.90826 ? 240 MET A CE  1 
ATOM   1955 N N   . LEU A 1 241 ? 11.29771  69.49334 27.82969 1.000 22.73678 ? 241 LEU A N   1 
ATOM   1956 C CA  . LEU A 1 241 ? 10.99902  69.03570 26.48365 1.000 23.63030 ? 241 LEU A CA  1 
ATOM   1957 C C   . LEU A 1 241 ? 9.74315   69.73762 26.01868 1.000 22.26247 ? 241 LEU A C   1 
ATOM   1958 O O   . LEU A 1 241 ? 8.88109   70.06663 26.82803 1.000 23.19026 ? 241 LEU A O   1 
ATOM   1959 C CB  . LEU A 1 241 ? 10.79585  67.51342 26.43193 1.000 21.33320 ? 241 LEU A CB  1 
ATOM   1960 C CG  . LEU A 1 241 ? 11.88338  66.60935 27.00430 1.000 24.76355 ? 241 LEU A CG  1 
ATOM   1961 C CD1 . LEU A 1 241 ? 11.40855  65.15851 27.02657 1.000 26.24297 ? 241 LEU A CD1 1 
ATOM   1962 C CD2 . LEU A 1 241 ? 13.18052  66.74398 26.19728 1.000 25.15592 ? 241 LEU A CD2 1 
ATOM   1963 N N   . TRP A 1 242 ? 9.63643   69.95883 24.71713 1.000 21.12985 ? 242 TRP A N   1 
ATOM   1964 C CA  . TRP A 1 242 ? 8.39723   70.45064 24.14974 1.000 21.69947 ? 242 TRP A CA  1 
ATOM   1965 C C   . TRP A 1 242 ? 8.00743   69.59733 22.97405 1.000 23.02940 ? 242 TRP A C   1 
ATOM   1966 O O   . TRP A 1 242 ? 8.84048   69.29332 22.12431 1.000 23.71479 ? 242 TRP A O   1 
ATOM   1967 C CB  . TRP A 1 242 ? 8.51231   71.90723 23.69835 1.000 21.30828 ? 242 TRP A CB  1 
ATOM   1968 C CG  . TRP A 1 242 ? 7.32100   72.69791 24.07455 1.000 20.36089 ? 242 TRP A CG  1 
ATOM   1969 C CD1 . TRP A 1 242 ? 6.04398   72.53449 23.61286 1.000 22.77827 ? 242 TRP A CD1 1 
ATOM   1970 C CD2 . TRP A 1 242 ? 7.27355   73.76837 25.01771 1.000 22.32039 ? 242 TRP A CD2 1 
ATOM   1971 N NE1 . TRP A 1 242 ? 5.20461   73.43621 24.21880 1.000 22.65030 ? 242 TRP A NE1 1 
ATOM   1972 C CE2 . TRP A 1 242 ? 5.93580   74.20616 25.08689 1.000 21.78319 ? 242 TRP A CE2 1 
ATOM   1973 C CE3 . TRP A 1 242 ? 8.23088   74.39539 25.81894 1.000 22.20019 ? 242 TRP A CE3 1 
ATOM   1974 C CZ2 . TRP A 1 242 ? 5.53645   75.25137 25.91798 1.000 22.74983 ? 242 TRP A CZ2 1 
ATOM   1975 C CZ3 . TRP A 1 242 ? 7.83024   75.43533 26.63769 1.000 23.38962 ? 242 TRP A CZ3 1 
ATOM   1976 C CH2 . TRP A 1 242 ? 6.49796   75.85058 26.68172 1.000 20.54606 ? 242 TRP A CH2 1 
ATOM   1977 N N   . GLY A 1 243 ? 6.73867   69.21361 22.92033 1.000 21.43476 ? 243 GLY A N   1 
ATOM   1978 C CA  . GLY A 1 243 ? 6.20895   68.57908 21.72961 1.000 22.21515 ? 243 GLY A CA  1 
ATOM   1979 C C   . GLY A 1 243 ? 5.68596   69.66445 20.81859 1.000 23.37390 ? 243 GLY A C   1 
ATOM   1980 O O   . GLY A 1 243 ? 4.74999   70.36741 21.17730 1.000 23.98650 ? 243 GLY A O   1 
ATOM   1981 N N   . VAL A 1 244 ? 6.28933   69.82168 19.64292 1.000 24.94318 ? 244 VAL A N   1 
ATOM   1982 C CA  . VAL A 1 244 ? 5.93694   70.94645 18.78897 1.000 24.04341 ? 244 VAL A CA  1 
ATOM   1983 C C   . VAL A 1 244 ? 4.52805   70.78926 18.23122 1.000 25.14039 ? 244 VAL A C   1 
ATOM   1984 O O   . VAL A 1 244 ? 3.92484   71.76645 17.81316 1.000 24.44913 ? 244 VAL A O   1 
ATOM   1985 C CB  . VAL A 1 244 ? 6.94751   71.14509 17.62459 1.000 26.37556 ? 244 VAL A CB  1 
ATOM   1986 C CG1 . VAL A 1 244 ? 8.36521   71.27929 18.17479 1.000 25.53956 ? 244 VAL A CG1 1 
ATOM   1987 C CG2 . VAL A 1 244 ? 6.87046   70.01115 16.63606 1.000 31.14975 ? 244 VAL A CG2 1 
ATOM   1988 N N   . GLY A 1 245 ? 3.99286   69.57156 18.26779 1.000 25.13724 ? 245 GLY A N   1 
ATOM   1989 C CA  . GLY A 1 245 ? 2.62175   69.33625 17.84723 1.000 25.46961 ? 245 GLY A CA  1 
ATOM   1990 C C   . GLY A 1 245 ? 1.53979   69.68763 18.87141 1.000 24.84204 ? 245 GLY A C   1 
ATOM   1991 O O   . GLY A 1 245 ? 0.35503   69.53578 18.58917 1.000 24.95185 ? 245 GLY A O   1 
ATOM   1992 N N   . ASP A 1 246 ? 1.94340   70.14877 20.05422 1.000 21.97621 ? 246 ASP A N   1 
ATOM   1993 C CA  . ASP A 1 246 ? 1.01003   70.54360 21.11533 1.000 21.82288 ? 246 ASP A CA  1 
ATOM   1994 C C   . ASP A 1 246 ? 0.31228   71.86113 20.75412 1.000 22.51358 ? 246 ASP A C   1 
ATOM   1995 O O   . ASP A 1 246 ? 0.95320   72.90406 20.70130 1.000 23.11966 ? 246 ASP A O   1 
ATOM   1996 C CB  . ASP A 1 246 ? 1.76187   70.68071 22.45091 1.000 22.15905 ? 246 ASP A CB  1 
ATOM   1997 C CG  . ASP A 1 246 ? 0.83502   70.88905 23.64902 1.000 21.88502 ? 246 ASP A CG  1 
ATOM   1998 O OD1 . ASP A 1 246 ? -0.34197  71.23596 23.46689 1.000 21.76049 ? 246 ASP A OD1 1 
ATOM   1999 O OD2 . ASP A 1 246 ? 1.29744   70.71223 24.79314 1.000 22.83777 ? 246 ASP A OD2 1 
ATOM   2000 N N   . PRO A 1 247 ? -1.00481  71.82185 20.51044 1.000 20.67655 ? 247 PRO A N   1 
ATOM   2001 C CA  . PRO A 1 247 ? -1.69363  73.06609 20.15183 1.000 20.49309 ? 247 PRO A CA  1 
ATOM   2002 C C   . PRO A 1 247 ? -2.21456  73.84414 21.36688 1.000 21.33672 ? 247 PRO A C   1 
ATOM   2003 O O   . PRO A 1 247 ? -2.49502  75.03088 21.23376 1.000 22.11330 ? 247 PRO A O   1 
ATOM   2004 C CB  . PRO A 1 247 ? -2.85303  72.57591 19.29113 1.000 21.14738 ? 247 PRO A CB  1 
ATOM   2005 C CG  . PRO A 1 247 ? -3.20714  71.23597 19.92762 1.000 22.41876 ? 247 PRO A CG  1 
ATOM   2006 C CD  . PRO A 1 247 ? -1.91877  70.66516 20.49897 1.000 21.77170 ? 247 PRO A CD  1 
ATOM   2007 N N   . VAL A 1 248 ? -2.33478  73.20086 22.52933 1.000 20.77465 ? 248 VAL A N   1 
ATOM   2008 C CA  . VAL A 1 248 ? -2.99861  73.84551 23.65303 1.000 18.76488 ? 248 VAL A CA  1 
ATOM   2009 C C   . VAL A 1 248 ? -1.98033  74.51314 24.57622 1.000 21.90909 ? 248 VAL A C   1 
ATOM   2010 O O   . VAL A 1 248 ? -2.25686  75.56537 25.15901 1.000 22.13489 ? 248 VAL A O   1 
ATOM   2011 C CB  . VAL A 1 248 ? -3.90382  72.84844 24.43223 1.000 21.22681 ? 248 VAL A CB  1 
ATOM   2012 C CG1 . VAL A 1 248 ? -3.09437  71.71101 25.07720 1.000 21.65498 ? 248 VAL A CG1 1 
ATOM   2013 C CG2 . VAL A 1 248 ? -4.71849  73.58879 25.46984 1.000 22.02412 ? 248 VAL A CG2 1 
ATOM   2014 N N   . VAL A 1 249 ? -0.79174  73.92638 24.67674 1.000 20.70634 ? 249 VAL A N   1 
ATOM   2015 C CA  . VAL A 1 249 ? 0.34780   74.58202 25.31304 1.000 20.23366 ? 249 VAL A CA  1 
ATOM   2016 C C   . VAL A 1 249 ? 1.50230   74.59861 24.29011 1.000 21.78338 ? 249 VAL A C   1 
ATOM   2017 O O   . VAL A 1 249 ? 2.41078   73.76832 24.35090 1.000 22.60958 ? 249 VAL A O   1 
ATOM   2018 C CB  . VAL A 1 249 ? 0.76028   73.86982 26.62794 1.000 20.48046 ? 249 VAL A CB  1 
ATOM   2019 C CG1 . VAL A 1 249 ? 1.81748   74.66703 27.37102 1.000 21.31210 ? 249 VAL A CG1 1 
ATOM   2020 C CG2 . VAL A 1 249 ? -0.46673  73.64716 27.53640 1.000 20.87100 ? 249 VAL A CG2 1 
ATOM   2021 N N   . PRO A 1 250 ? 1.43990   75.52821 23.31354 1.000 21.39175 ? 250 PRO A N   1 
ATOM   2022 C CA  . PRO A 1 250 ? 2.34043   75.53125 22.14875 1.000 22.66626 ? 250 PRO A CA  1 
ATOM   2023 C C   . PRO A 1 250 ? 3.77927   75.96223 22.43828 1.000 22.98771 ? 250 PRO A C   1 
ATOM   2024 O O   . PRO A 1 250 ? 4.04835   76.70682 23.38264 1.000 24.92577 ? 250 PRO A O   1 
ATOM   2025 C CB  . PRO A 1 250 ? 1.67330   76.52860 21.19446 1.000 21.78541 ? 250 PRO A CB  1 
ATOM   2026 C CG  . PRO A 1 250 ? 0.92515   77.45305 22.09448 1.000 24.66356 ? 250 PRO A CG  1 
ATOM   2027 C CD  . PRO A 1 250 ? 0.40160   76.56814 23.20062 1.000 20.42171 ? 250 PRO A CD  1 
ATOM   2028 N N   . SER A 1 251 ? 4.69172   75.50084 21.59017 1.000 22.70398 ? 251 SER A N   1 
ATOM   2029 C CA  . SER A 1 251 ? 6.12914   75.69210 21.79111 1.000 23.84341 ? 251 SER A CA  1 
ATOM   2030 C C   . SER A 1 251 ? 6.56438   77.16212 21.76699 1.000 25.60273 ? 251 SER A C   1 
ATOM   2031 O O   . SER A 1 251 ? 7.68594   77.48484 22.14773 1.000 28.24098 ? 251 SER A O   1 
ATOM   2032 C CB  . SER A 1 251 ? 6.91310   74.90296 20.73434 1.000 25.02950 ? 251 SER A CB  1 
ATOM   2033 O OG  . SER A 1 251 ? 6.52512   75.28224 19.42260 1.000 28.05350 ? 251 SER A OG  1 
ATOM   2034 N N   . SER A 1 252 ? 5.68364   78.04999 21.31905 1.000 25.49655 ? 252 SER A N   1 
ATOM   2035 C CA  . SER A 1 252 ? 5.95084   79.47975 21.40592 1.000 25.31955 ? 252 SER A CA  1 
ATOM   2036 C C   . SER A 1 252 ? 6.17504   79.91134 22.85362 1.000 25.35947 ? 252 SER A C   1 
ATOM   2037 O O   . SER A 1 252 ? 6.89487   80.87799 23.11538 1.000 24.87085 ? 252 SER A O   1 
ATOM   2038 C CB  . SER A 1 252 ? 4.80019   80.28098 20.79806 1.000 27.38660 ? 252 SER A CB  1 
ATOM   2039 O OG  . SER A 1 252 ? 3.58886   80.04558 21.49781 1.000 26.83321 ? 252 SER A OG  1 
ATOM   2040 N N   . LEU A 1 253 ? 5.57311   79.17891 23.78975 1.000 22.78186 ? 253 LEU A N   1 
ATOM   2041 C CA  . LEU A 1 253 ? 5.62867   79.53987 25.20569 1.000 22.17283 ? 253 LEU A CA  1 
ATOM   2042 C C   . LEU A 1 253 ? 7.00270   79.30726 25.84316 1.000 22.41334 ? 253 LEU A C   1 
ATOM   2043 O O   . LEU A 1 253 ? 7.20608   79.64249 27.00473 1.000 23.56861 ? 253 LEU A O   1 
ATOM   2044 C CB  . LEU A 1 253 ? 4.54566   78.79091 25.98310 1.000 22.73128 ? 253 LEU A CB  1 
ATOM   2045 C CG  . LEU A 1 253 ? 3.12237   79.28670 25.66568 1.000 23.64501 ? 253 LEU A CG  1 
ATOM   2046 C CD1 . LEU A 1 253 ? 2.07177   78.30821 26.15010 1.000 20.65936 ? 253 LEU A CD1 1 
ATOM   2047 C CD2 . LEU A 1 253 ? 2.87401   80.67105 26.25533 1.000 22.24307 ? 253 LEU A CD2 1 
ATOM   2048 N N   . VAL A 1 254 ? 7.95585   78.77871 25.08301 1.000 22.06253 ? 254 VAL A N   1 
ATOM   2049 C CA  . VAL A 1 254 ? 9.35188   78.78633 25.53426 1.000 24.74003 ? 254 VAL A CA  1 
ATOM   2050 C C   . VAL A 1 254 ? 9.77968   80.20418 25.93773 1.000 25.62953 ? 254 VAL A C   1 
ATOM   2051 O O   . VAL A 1 254 ? 10.59052  80.38299 26.84246 1.000 24.18236 ? 254 VAL A O   1 
ATOM   2052 C CB  . VAL A 1 254 ? 10.32292  78.24425 24.44698 1.000 23.38839 ? 254 VAL A CB  1 
ATOM   2053 C CG1 . VAL A 1 254 ? 11.78832  78.52903 24.80167 1.000 20.18147 ? 254 VAL A CG1 1 
ATOM   2054 C CG2 . VAL A 1 254 ? 10.11988  76.75770 24.26062 1.000 23.42627 ? 254 VAL A CG2 1 
ATOM   2055 N N   . HIS A 1 255 ? 9.20877   81.21834 25.30027 1.000 23.34747 ? 255 HIS A N   1 
ATOM   2056 C CA  . HIS A 1 255 ? 9.66828   82.57079 25.57892 1.000 26.69424 ? 255 HIS A CA  1 
ATOM   2057 C C   . HIS A 1 255 ? 9.33222   83.00951 27.00845 1.000 26.04928 ? 255 HIS A C   1 
ATOM   2058 O O   . HIS A 1 255 ? 9.92167   83.95750 27.51253 1.000 25.86840 ? 255 HIS A O   1 
ATOM   2059 C CB  . HIS A 1 255 ? 9.09314   83.55793 24.56181 1.000 28.04877 ? 255 HIS A CB  1 
ATOM   2060 C CG  . HIS A 1 255 ? 7.81215   84.19038 24.99109 1.000 28.03335 ? 255 HIS A CG  1 
ATOM   2061 N ND1 . HIS A 1 255 ? 6.58022   83.65030 24.69561 1.000 32.49782 ? 255 HIS A ND1 1 
ATOM   2062 C CD2 . HIS A 1 255 ? 7.56848   85.32819 25.68289 1.000 30.91194 ? 255 HIS A CD2 1 
ATOM   2063 C CE1 . HIS A 1 255 ? 5.63279   84.42131 25.19826 1.000 32.33428 ? 255 HIS A CE1 1 
ATOM   2064 N NE2 . HIS A 1 255 ? 6.20645   85.44814 25.80081 1.000 36.92509 ? 255 HIS A NE2 1 
ATOM   2065 N N   . GLN A 1 256 ? 8.42016   82.30128 27.67399 1.000 25.53977 ? 256 GLN A N   1 
ATOM   2066 C CA  . GLN A 1 256 ? 8.05807   82.63753 29.05313 1.000 26.16944 ? 256 GLN A CA  1 
ATOM   2067 C C   . GLN A 1 256 ? 8.96683   81.99353 30.09275 1.000 25.11978 ? 256 GLN A C   1 
ATOM   2068 O O   . GLN A 1 256 ? 8.90768   82.33932 31.27646 1.000 26.34089 ? 256 GLN A O   1 
ATOM   2069 C CB  . GLN A 1 256 ? 6.60691   82.23425 29.34857 1.000 23.81962 ? 256 GLN A CB  1 
ATOM   2070 C CG  . GLN A 1 256 ? 5.57849   82.99070 28.51790 1.000 28.42833 ? 256 GLN A CG  1 
ATOM   2071 C CD  . GLN A 1 256 ? 4.16776   82.82607 29.04024 1.000 25.76310 ? 256 GLN A CD  1 
ATOM   2072 O OE1 . GLN A 1 256 ? 3.90892   82.00215 29.91507 1.000 26.77170 ? 256 GLN A OE1 1 
ATOM   2073 N NE2 . GLN A 1 256 ? 3.24952   83.62135 28.51521 1.000 26.64250 ? 256 GLN A NE2 1 
ATOM   2074 N N   . VAL A 1 257 ? 9.79083   81.04869 29.65809 1.000 24.79495 ? 257 VAL A N   1 
ATOM   2075 C CA  . VAL A 1 257 ? 10.62255  80.26084 30.57520 1.000 21.80713 ? 257 VAL A CA  1 
ATOM   2076 C C   . VAL A 1 257 ? 11.83139  81.00589 31.18399 1.000 22.02657 ? 257 VAL A C   1 
ATOM   2077 O O   . VAL A 1 257 ? 12.05205  80.90533 32.39071 1.000 22.23619 ? 257 VAL A O   1 
ATOM   2078 C CB  . VAL A 1 257 ? 11.11079  78.97834 29.86897 1.000 23.10988 ? 257 VAL A CB  1 
ATOM   2079 C CG1 . VAL A 1 257 ? 12.25757  78.31705 30.62357 1.000 23.98057 ? 257 VAL A CG1 1 
ATOM   2080 C CG2 . VAL A 1 257 ? 9.95089   78.01181 29.68490 1.000 25.29389 ? 257 VAL A CG2 1 
ATOM   2081 N N   . PRO A 1 258 ? 12.60412  81.76757 30.37008 1.000 24.01236 ? 258 PRO A N   1 
ATOM   2082 C CA  . PRO A 1 258 ? 13.80325  82.42330 30.91767 1.000 22.07603 ? 258 PRO A CA  1 
ATOM   2083 C C   . PRO A 1 258 ? 13.57834  83.33576 32.12239 1.000 23.85095 ? 258 PRO A C   1 
ATOM   2084 O O   . PRO A 1 258 ? 14.50231  83.49924 32.91514 1.000 25.82166 ? 258 PRO A O   1 
ATOM   2085 C CB  . PRO A 1 258 ? 14.31440  83.24780 29.72962 1.000 25.48648 ? 258 PRO A CB  1 
ATOM   2086 C CG  . PRO A 1 258 ? 13.89810  82.46233 28.55970 1.000 23.39956 ? 258 PRO A CG  1 
ATOM   2087 C CD  . PRO A 1 258 ? 12.51132  81.99211 28.91306 1.000 21.58187 ? 258 PRO A CD  1 
ATOM   2088 N N   . ASN A 1 259 ? 12.38780  83.90212 32.28112 1.000 25.27181 ? 259 ASN A N   1 
ATOM   2089 C CA  . ASN A 1 259 ? 12.13947  84.73625 33.45099 1.000 24.42919 ? 259 ASN A CA  1 
ATOM   2090 C C   . ASN A 1 259 ? 12.06303  83.92651 34.74179 1.000 25.62140 ? 259 ASN A C   1 
ATOM   2091 O O   . ASN A 1 259 ? 12.12592  84.49729 35.81477 1.000 24.36899 ? 259 ASN A O   1 
ATOM   2092 C CB  . ASN A 1 259 ? 10.84943  85.54253 33.29338 1.000 24.70915 ? 259 ASN A CB  1 
ATOM   2093 C CG  . ASN A 1 259 ? 11.02312  86.76312 32.40863 1.000 30.82591 ? 259 ASN A CG  1 
ATOM   2094 O OD1 . ASN A 1 259 ? 12.12626  87.27529 32.24778 1.000 34.53294 ? 259 ASN A OD1 1 
ATOM   2095 N ND2 . ASN A 1 259 ? 9.93010   87.22891 31.82557 1.000 31.05517 ? 259 ASN A ND2 1 
ATOM   2096 N N   . TYR A 1 260 ? 11.92896  82.60378 34.64045 1.000 24.36010 ? 260 TYR A N   1 
ATOM   2097 C CA  . TYR A 1 260 ? 11.73247  81.78808 35.83565 1.000 22.25457 ? 260 TYR A CA  1 
ATOM   2098 C C   . TYR A 1 260 ? 12.82436  80.76696 36.08954 1.000 23.59544 ? 260 TYR A C   1 
ATOM   2099 O O   . TYR A 1 260 ? 12.85949  80.16953 37.15475 1.000 24.52319 ? 260 TYR A O   1 
ATOM   2100 C CB  . TYR A 1 260 ? 10.36916  81.07859 35.76363 1.000 21.21467 ? 260 TYR A CB  1 
ATOM   2101 C CG  . TYR A 1 260 ? 9.25615   82.08778 35.73446 1.000 22.24596 ? 260 TYR A CG  1 
ATOM   2102 C CD1 . TYR A 1 260 ? 8.90443   82.78603 36.88221 1.000 20.95290 ? 260 TYR A CD1 1 
ATOM   2103 C CD2 . TYR A 1 260 ? 8.59986   82.38816 34.55564 1.000 21.48000 ? 260 TYR A CD2 1 
ATOM   2104 C CE1 . TYR A 1 260 ? 7.90407   83.73985 36.86087 1.000 24.55898 ? 260 TYR A CE1 1 
ATOM   2105 C CE2 . TYR A 1 260 ? 7.59082   83.33804 34.52604 1.000 24.19104 ? 260 TYR A CE2 1 
ATOM   2106 C CZ  . TYR A 1 260 ? 7.25745   84.01491 35.67657 1.000 26.77599 ? 260 TYR A CZ  1 
ATOM   2107 O OH  . TYR A 1 260 ? 6.26850   84.96520 35.64470 1.000 29.40093 ? 260 TYR A OH  1 
ATOM   2108 N N   . TYR A 1 261 ? 13.71482  80.56719 35.12319 1.000 25.34751 ? 261 TYR A N   1 
ATOM   2109 C CA  . TYR A 1 261 ? 14.73984  79.53337 35.25038 1.000 24.64420 ? 261 TYR A CA  1 
ATOM   2110 C C   . TYR A 1 261 ? 16.09452  80.02089 34.75738 1.000 25.03844 ? 261 TYR A C   1 
ATOM   2111 O O   . TYR A 1 261 ? 16.18264  80.70716 33.74450 1.000 26.41265 ? 261 TYR A O   1 
ATOM   2112 C CB  . TYR A 1 261 ? 14.31726  78.27144 34.48453 1.000 23.93554 ? 261 TYR A CB  1 
ATOM   2113 C CG  . TYR A 1 261 ? 13.08671  77.61045 35.07143 1.000 22.72488 ? 261 TYR A CG  1 
ATOM   2114 C CD1 . TYR A 1 261 ? 11.81458  77.98308 34.66946 1.000 22.19865 ? 261 TYR A CD1 1 
ATOM   2115 C CD2 . TYR A 1 261 ? 13.20479  76.63459 36.05433 1.000 24.75359 ? 261 TYR A CD2 1 
ATOM   2116 C CE1 . TYR A 1 261 ? 10.68377  77.39306 35.22821 1.000 22.86482 ? 261 TYR A CE1 1 
ATOM   2117 C CE2 . TYR A 1 261 ? 12.08903  76.03022 36.61119 1.000 22.48707 ? 261 TYR A CE2 1 
ATOM   2118 C CZ  . TYR A 1 261 ? 10.83369  76.41163 36.20205 1.000 23.35116 ? 261 TYR A CZ  1 
ATOM   2119 O OH  . TYR A 1 261 ? 9.72911   75.81428 36.77241 1.000 23.91831 ? 261 TYR A OH  1 
ATOM   2120 N N   . SER A 1 262 ? 17.14965  79.65255 35.47363 1.000 27.46552 ? 262 SER A N   1 
ATOM   2121 C CA  . SER A 1 262 ? 18.49986  80.05413 35.10494 1.000 27.39415 ? 262 SER A CA  1 
ATOM   2122 C C   . SER A 1 262 ? 19.40233  78.85611 34.83749 1.000 26.37846 ? 262 SER A C   1 
ATOM   2123 O O   . SER A 1 262 ? 20.56571  79.01908 34.50310 1.000 28.04406 ? 262 SER A O   1 
ATOM   2124 C CB  . SER A 1 262 ? 19.10978  80.91105 36.20841 1.000 28.09617 ? 262 SER A CB  1 
ATOM   2125 O OG  . SER A 1 262 ? 19.24161  80.14099 37.39274 1.000 31.74112 ? 262 SER A OG  1 
ATOM   2126 N N   . ASN A 1 263 ? 18.86864  77.65009 34.98426 1.000 24.81548 ? 263 ASN A N   1 
ATOM   2127 C CA  . ASN A 1 263 ? 19.69093  76.44757 34.87566 1.000 26.52143 ? 263 ASN A CA  1 
ATOM   2128 C C   . ASN A 1 263 ? 18.86781  75.31812 34.26807 1.000 25.39738 ? 263 ASN A C   1 
ATOM   2129 O O   . ASN A 1 263 ? 18.45579  74.39243 34.96188 1.000 27.79522 ? 263 ASN A O   1 
ATOM   2130 C CB  . ASN A 1 263 ? 20.24320  76.05702 36.26207 1.000 24.69611 ? 263 ASN A CB  1 
ATOM   2131 C CG  . ASN A 1 263 ? 21.20201  74.86595 36.21422 1.000 27.15796 ? 263 ASN A CG  1 
ATOM   2132 O OD1 . ASN A 1 263 ? 21.52518  74.35840 35.15550 1.000 28.40130 ? 263 ASN A OD1 1 
ATOM   2133 N ND2 . ASN A 1 263 ? 21.66505  74.43641 37.37425 1.000 28.15752 ? 263 ASN A ND2 1 
ATOM   2134 N N   . TYR A 1 264 ? 18.61809  75.40800 32.96883 1.000 24.06093 ? 264 TYR A N   1 
ATOM   2135 C CA  . TYR A 1 264 ? 17.75641  74.45453 32.29858 1.000 20.93692 ? 264 TYR A CA  1 
ATOM   2136 C C   . TYR A 1 264 ? 18.28416  74.05000 30.92921 1.000 24.30075 ? 264 TYR A C   1 
ATOM   2137 O O   . TYR A 1 264 ? 19.17350  74.70056 30.36358 1.000 24.91858 ? 264 TYR A O   1 
ATOM   2138 C CB  . TYR A 1 264 ? 16.33601  75.03444 32.15187 1.000 23.58068 ? 264 TYR A CB  1 
ATOM   2139 C CG  . TYR A 1 264 ? 16.27223  76.25341 31.26107 1.000 22.60984 ? 264 TYR A CG  1 
ATOM   2140 C CD1 . TYR A 1 264 ? 16.48856  77.52523 31.77723 1.000 23.20638 ? 264 TYR A CD1 1 
ATOM   2141 C CD2 . TYR A 1 264 ? 16.01474  76.13204 29.90019 1.000 23.81716 ? 264 TYR A CD2 1 
ATOM   2142 C CE1 . TYR A 1 264 ? 16.44833  78.64649 30.96779 1.000 22.43329 ? 264 TYR A CE1 1 
ATOM   2143 C CE2 . TYR A 1 264 ? 15.97416  77.24700 29.08047 1.000 24.60247 ? 264 TYR A CE2 1 
ATOM   2144 C CZ  . TYR A 1 264 ? 16.19056  78.49886 29.62101 1.000 23.90376 ? 264 TYR A CZ  1 
ATOM   2145 O OH  . TYR A 1 264 ? 16.15047  79.60112 28.80491 1.000 26.38920 ? 264 TYR A OH  1 
ATOM   2146 N N   . THR A 1 265 ? 17.72624  72.96583 30.40318 1.000 22.93102 ? 265 THR A N   1 
ATOM   2147 C CA  . THR A 1 265 ? 17.85823  72.64653 28.99123 1.000 22.60751 ? 265 THR A CA  1 
ATOM   2148 C C   . THR A 1 265 ? 16.46375  72.61158 28.36824 1.000 24.25518 ? 265 THR A C   1 
ATOM   2149 O O   . THR A 1 265 ? 15.46170  72.39291 29.06260 1.000 22.49615 ? 265 THR A O   1 
ATOM   2150 C CB  . THR A 1 265 ? 18.58103  71.30256 28.75305 1.000 25.64766 ? 265 THR A CB  1 
ATOM   2151 O OG1 . THR A 1 265 ? 17.77788  70.21764 29.23957 1.000 25.34155 ? 265 THR A OG1 1 
ATOM   2152 C CG2 . THR A 1 265 ? 19.94053  71.29299 29.45624 1.000 24.96971 ? 265 THR A CG2 1 
ATOM   2153 N N   . MET A 1 266 ? 16.40740  72.84085 27.06530 1.000 21.84901 ? 266 MET A N   1 
ATOM   2154 C CA  . MET A 1 266 ? 15.15422  72.79178 26.31697 1.000 22.00569 ? 266 MET A CA  1 
ATOM   2155 C C   . MET A 1 266 ? 15.38191  72.04725 25.01675 1.000 25.51281 ? 266 MET A C   1 
ATOM   2156 O O   . MET A 1 266 ? 16.37679  72.27973 24.33526 1.000 25.05052 ? 266 MET A O   1 
ATOM   2157 C CB  . MET A 1 266 ? 14.62261  74.19909 26.03844 1.000 23.58928 ? 266 MET A CB  1 
ATOM   2158 C CG  . MET A 1 266 ? 13.37547  74.22545 25.16187 1.000 24.59336 ? 266 MET A CG  1 
ATOM   2159 S SD  . MET A 1 266 ? 11.93296  73.54147 25.99657 1.000 25.32538 ? 266 MET A SD  1 
ATOM   2160 C CE  . MET A 1 266 ? 11.61569  74.82206 27.20415 1.000 26.73507 ? 266 MET A CE  1 
ATOM   2161 N N   . GLU A 1 267 ? 14.47751  71.13411 24.67992 1.000 24.22022 ? 267 GLU A N   1 
ATOM   2162 C CA  . GLU A 1 267 ? 14.56563  70.42567 23.41193 1.000 23.87746 ? 267 GLU A CA  1 
ATOM   2163 C C   . GLU A 1 267 ? 13.18324  70.33127 22.77450 1.000 23.83943 ? 267 GLU A C   1 
ATOM   2164 O O   . GLU A 1 267 ? 12.24108  69.83936 23.39129 1.000 25.36150 ? 267 GLU A O   1 
ATOM   2165 C CB  . GLU A 1 267 ? 15.17933  69.03102 23.61129 1.000 22.24912 ? 267 GLU A CB  1 
ATOM   2166 C CG  . GLU A 1 267 ? 15.16342  68.16392 22.35094 1.000 28.12604 ? 267 GLU A CG  1 
ATOM   2167 C CD  . GLU A 1 267 ? 15.80302  66.78928 22.55000 1.000 29.28483 ? 267 GLU A CD  1 
ATOM   2168 O OE1 . GLU A 1 267 ? 15.84429  66.01281 21.57434 1.000 34.58736 ? 267 GLU A OE1 1 
ATOM   2169 O OE2 . GLU A 1 267 ? 16.25150  66.48384 23.67187 1.000 28.84764 ? 267 GLU A OE2 1 
ATOM   2170 N N   . LEU A 1 268 ? 13.04950  70.82420 21.54867 1.000 24.87208 ? 268 LEU A N   1 
ATOM   2171 C CA  . LEU A 1 268 ? 11.77402  70.71715 20.84339 1.000 24.81134 ? 268 LEU A CA  1 
ATOM   2172 C C   . LEU A 1 268 ? 11.72209  69.39571 20.07769 1.000 27.98179 ? 268 LEU A C   1 
ATOM   2173 O O   . LEU A 1 268 ? 12.50346  69.17131 19.15154 1.000 29.24806 ? 268 LEU A O   1 
ATOM   2174 C CB  . LEU A 1 268 ? 11.55264  71.88297 19.87182 1.000 23.69684 ? 268 LEU A CB  1 
ATOM   2175 C CG  . LEU A 1 268 ? 11.60346  73.36341 20.27921 1.000 25.13179 ? 268 LEU A CG  1 
ATOM   2176 C CD1 . LEU A 1 268 ? 10.61536  74.18120 19.46482 1.000 26.03886 ? 268 LEU A CD1 1 
ATOM   2177 C CD2 . LEU A 1 268 ? 11.40267  73.59994 21.73475 1.000 24.55967 ? 268 LEU A CD2 1 
ATOM   2178 N N   . ILE A 1 269 ? 10.80187  68.52607 20.47368 1.000 25.41317 ? 269 ILE A N   1 
ATOM   2179 C CA  . ILE A 1 269 ? 10.60780  67.25055 19.80580 1.000 25.71825 ? 269 ILE A CA  1 
ATOM   2180 C C   . ILE A 1 269 ? 9.66096   67.40844 18.61536 1.000 25.87642 ? 269 ILE A C   1 
ATOM   2181 O O   . ILE A 1 269 ? 8.50589   67.79732 18.78136 1.000 23.59116 ? 269 ILE A O   1 
ATOM   2182 C CB  . ILE A 1 269 ? 10.05078  66.20669 20.78127 1.000 28.46827 ? 269 ILE A CB  1 
ATOM   2183 C CG1 . ILE A 1 269 ? 10.92892  66.14090 22.03464 1.000 26.77506 ? 269 ILE A CG1 1 
ATOM   2184 C CG2 . ILE A 1 269 ? 9.93005   64.85656 20.10510 1.000 28.82297 ? 269 ILE A CG2 1 
ATOM   2185 C CD1 . ILE A 1 269 ? 12.36992  65.83396 21.75460 1.000 27.52026 ? 269 ILE A CD1 1 
ATOM   2186 N N   . GLN A 1 270 ? 10.14829  67.08445 17.42058 1.000 25.65767 ? 270 GLN A N   1 
ATOM   2187 C CA  . GLN A 1 270 ? 9.44456   67.41931 16.18246 1.000 27.61638 ? 270 GLN A CA  1 
ATOM   2188 C C   . GLN A 1 270 ? 8.19569   66.59502 15.89984 1.000 30.40590 ? 270 GLN A C   1 
ATOM   2189 O O   . GLN A 1 270 ? 7.30127   67.05950 15.20695 1.000 34.15352 ? 270 GLN A O   1 
ATOM   2190 C CB  . GLN A 1 270 ? 10.40294  67.29763 14.98726 1.000 29.26235 ? 270 GLN A CB  1 
ATOM   2191 C CG  . GLN A 1 270 ? 11.56255  68.28402 15.05316 1.000 30.81989 ? 270 GLN A CG  1 
ATOM   2192 C CD  . GLN A 1 270 ? 11.09500  69.72605 15.11133 1.000 31.18552 ? 270 GLN A CD  1 
ATOM   2193 O OE1 . GLN A 1 270 ? 10.40422  70.19666 14.21504 1.000 38.21355 ? 270 GLN A OE1 1 
ATOM   2194 N NE2 . GLN A 1 270 ? 11.44931  70.42471 16.17984 1.000 29.17082 ? 270 GLN A NE2 1 
ATOM   2195 N N   . ASP A 1 271 ? 8.12393   65.37434 16.41277 1.000 28.81083 ? 271 ASP A N   1 
ATOM   2196 C CA  . ASP A 1 271 ? 6.97485   64.52958 16.09712 1.000 30.59136 ? 271 ASP A CA  1 
ATOM   2197 C C   . ASP A 1 271 ? 6.19506   64.13962 17.34307 1.000 28.62014 ? 271 ASP A C   1 
ATOM   2198 O O   . ASP A 1 271 ? 5.71406   63.01591 17.45296 1.000 27.45847 ? 271 ASP A O   1 
ATOM   2199 C CB  . ASP A 1 271 ? 7.42539   63.27205 15.34305 1.000 30.77030 ? 271 ASP A CB  1 
ATOM   2200 C CG  . ASP A 1 271 ? 8.47292   62.47466 16.10607 1.000 36.51239 ? 271 ASP A CG  1 
ATOM   2201 O OD1 . ASP A 1 271 ? 9.03381   62.99846 17.09382 1.000 36.39862 ? 271 ASP A OD1 1 
ATOM   2202 O OD2 . ASP A 1 271 ? 8.74492   61.31755 15.71570 1.000 40.90850 ? 271 ASP A OD2 1 
ATOM   2203 N N   . ALA A 1 272 ? 6.07803   65.07161 18.28329 1.000 27.18439 ? 272 ALA A N   1 
ATOM   2204 C CA  . ALA A 1 272 ? 5.28514   64.84035 19.47991 1.000 25.23607 ? 272 ALA A CA  1 
ATOM   2205 C C   . ALA A 1 272 ? 4.38171   66.02886 19.76447 1.000 23.56460 ? 272 ALA A C   1 
ATOM   2206 O O   . ALA A 1 272 ? 4.69681   67.16269 19.40982 1.000 27.12374 ? 272 ALA A O   1 
ATOM   2207 C CB  . ALA A 1 272 ? 6.18114   64.55484 20.67837 1.000 26.79402 ? 272 ALA A CB  1 
ATOM   2208 N N   . GLY A 1 273 ? 3.24477   65.74630 20.38339 1.000 23.14312 ? 273 GLY A N   1 
ATOM   2209 C CA  . GLY A 1 273 ? 2.32492   66.76960 20.83495 1.000 22.30952 ? 273 GLY A CA  1 
ATOM   2210 C C   . GLY A 1 273 ? 2.33002   66.82951 22.35078 1.000 22.78265 ? 273 GLY A C   1 
ATOM   2211 O O   . GLY A 1 273 ? 3.38237   66.75099 22.97269 1.000 24.66738 ? 273 GLY A O   1 
ATOM   2212 N N   . HIS A 1 274 ? 1.14054   66.91616 22.93921 1.000 22.69591 ? 274 HIS A N   1 
ATOM   2213 C CA  . HIS A 1 274 ? 0.96718   67.19264 24.35917 1.000 21.64952 ? 274 HIS A CA  1 
ATOM   2214 C C   . HIS A 1 274 ? 1.27065   66.00489 25.29564 1.000 25.05894 ? 274 HIS A C   1 
ATOM   2215 O O   . HIS A 1 274 ? 1.50618   66.20612 26.48697 1.000 25.13032 ? 274 HIS A O   1 
ATOM   2216 C CB  . HIS A 1 274 ? -0.47303  67.67502 24.58591 1.000 22.87564 ? 274 HIS A CB  1 
ATOM   2217 C CG  . HIS A 1 274 ? -0.73680  68.20992 25.95541 1.000 20.95439 ? 274 HIS A CG  1 
ATOM   2218 N ND1 . HIS A 1 274 ? -0.31980  69.46093 26.36031 1.000 21.38232 ? 274 HIS A ND1 1 
ATOM   2219 C CD2 . HIS A 1 274 ? -1.39491  67.67299 27.01059 1.000 22.84200 ? 274 HIS A CD2 1 
ATOM   2220 C CE1 . HIS A 1 274 ? -0.70571  69.66853 27.60542 1.000 23.41984 ? 274 HIS A CE1 1 
ATOM   2221 N NE2 . HIS A 1 274 ? -1.35769  68.59713 28.02459 1.000 24.88364 ? 274 HIS A NE2 1 
ATOM   2222 N N   . PHE A 1 275 ? 1.25072   64.78270 24.76483 1.000 22.85710 ? 275 PHE A N   1 
ATOM   2223 C CA  . PHE A 1 275 ? 1.41540   63.57335 25.58345 1.000 23.10327 ? 275 PHE A CA  1 
ATOM   2224 C C   . PHE A 1 275 ? 2.71197   62.86281 25.23481 1.000 23.42148 ? 275 PHE A C   1 
ATOM   2225 O O   . PHE A 1 275 ? 2.69941   61.81319 24.57757 1.000 22.68665 ? 275 PHE A O   1 
ATOM   2226 C CB  . PHE A 1 275 ? 0.24000   62.60349 25.38735 1.000 22.11518 ? 275 PHE A CB  1 
ATOM   2227 C CG  . PHE A 1 275 ? -1.10938  63.21786 25.62285 1.000 20.38931 ? 275 PHE A CG  1 
ATOM   2228 C CD1 . PHE A 1 275 ? -1.64225  63.27820 26.89355 1.000 22.48335 ? 275 PHE A CD1 1 
ATOM   2229 C CD2 . PHE A 1 275 ? -1.85659  63.71003 24.56223 1.000 22.79358 ? 275 PHE A CD2 1 
ATOM   2230 C CE1 . PHE A 1 275 ? -2.88133  63.83252 27.11053 1.000 24.88392 ? 275 PHE A CE1 1 
ATOM   2231 C CE2 . PHE A 1 275 ? -3.10080  64.25613 24.77210 1.000 21.76464 ? 275 PHE A CE2 1 
ATOM   2232 C CZ  . PHE A 1 275 ? -3.61400  64.32622 26.04426 1.000 22.58320 ? 275 PHE A CZ  1 
ATOM   2233 N N   . MET A 1 276 ? 3.82531   63.44921 25.66146 1.000 22.37908 ? 276 MET A N   1 
ATOM   2234 C CA  . MET A 1 276 ? 5.15442   62.97964 25.27243 1.000 24.32801 ? 276 MET A CA  1 
ATOM   2235 C C   . MET A 1 276 ? 5.39660   61.53169 25.70212 1.000 24.17510 ? 276 MET A C   1 
ATOM   2236 O O   . MET A 1 276 ? 5.98103   60.75013 24.95547 1.000 24.14432 ? 276 MET A O   1 
ATOM   2237 C CB  . MET A 1 276 ? 6.22388   63.89600 25.87332 1.000 23.55120 ? 276 MET A CB  1 
ATOM   2238 C CG  . MET A 1 276 ? 7.64592   63.59477 25.46587 1.000 30.43289 ? 276 MET A CG  1 
ATOM   2239 S SD  . MET A 1 276 ? 8.14569   64.35435 23.92673 1.000 35.74023 ? 276 MET A SD  1 
ATOM   2240 C CE  . MET A 1 276 ? 7.92637   66.10860 24.28032 1.000 26.30354 ? 276 MET A CE  1 
ATOM   2241 N N   . MET A 1 277 ? 4.92858   61.17624 26.89674 1.000 21.95404 ? 277 MET A N   1 
ATOM   2242 C CA  . MET A 1 277 ? 5.18747   59.85154 27.44916 1.000 22.13634 ? 277 MET A CA  1 
ATOM   2243 C C   . MET A 1 277 ? 4.34705   58.78027 26.75095 1.000 24.84902 ? 277 MET A C   1 
ATOM   2244 O O   . MET A 1 277 ? 4.67139   57.59120 26.80436 1.000 23.66308 ? 277 MET A O   1 
ATOM   2245 C CB  . MET A 1 277 ? 4.93379   59.83322 28.96651 1.000 23.64749 ? 277 MET A CB  1 
ATOM   2246 C CG  . MET A 1 277 ? 3.47190   59.97998 29.38773 1.000 21.75497 ? 277 MET A CG  1 
ATOM   2247 S SD  . MET A 1 277 ? 2.74551   61.57341 28.96721 1.000 23.61605 ? 277 MET A SD  1 
ATOM   2248 C CE  . MET A 1 277 ? 3.71653   62.65397 30.01575 1.000 22.94671 ? 277 MET A CE  1 
ATOM   2249 N N   . VAL A 1 278 ? 3.27611   59.20783 26.08591 1.000 23.49954 ? 278 VAL A N   1 
ATOM   2250 C CA  . VAL A 1 278 ? 2.42931   58.29453 25.33043 1.000 22.37158 ? 278 VAL A CA  1 
ATOM   2251 C C   . VAL A 1 278 ? 2.86839   58.20290 23.86179 1.000 25.63985 ? 278 VAL A C   1 
ATOM   2252 O O   . VAL A 1 278 ? 2.96694   57.10970 23.29110 1.000 24.11541 ? 278 VAL A O   1 
ATOM   2253 C CB  . VAL A 1 278 ? 0.94324   58.72266 25.38428 1.000 25.28841 ? 278 VAL A CB  1 
ATOM   2254 C CG1 . VAL A 1 278 ? 0.09868   57.75165 24.58547 1.000 23.55016 ? 278 VAL A CG1 1 
ATOM   2255 C CG2 . VAL A 1 278 ? 0.44448   58.80077 26.84291 1.000 22.70961 ? 278 VAL A CG2 1 
ATOM   2256 N N   . GLU A 1 279 ? 3.13631   59.35442 23.25581 1.000 23.63131 ? 279 GLU A N   1 
ATOM   2257 C CA  . GLU A 1 279 ? 3.42408   59.40783 21.82778 1.000 24.30175 ? 279 GLU A CA  1 
ATOM   2258 C C   . GLU A 1 279 ? 4.89731   59.07969 21.53068 1.000 24.73603 ? 279 GLU A C   1 
ATOM   2259 O O   . GLU A 1 279 ? 5.19572   58.42709 20.54879 1.000 26.50083 ? 279 GLU A O   1 
ATOM   2260 C CB  . GLU A 1 279 ? 3.04207   60.78858 21.26007 1.000 25.56568 ? 279 GLU A CB  1 
ATOM   2261 C CG  . GLU A 1 279 ? 3.07329   60.85417 19.73550 1.000 30.74040 ? 279 GLU A CG  1 
ATOM   2262 C CD  . GLU A 1 279 ? 2.24629   61.99708 19.14925 1.000 30.04720 ? 279 GLU A CD  1 
ATOM   2263 O OE1 . GLU A 1 279 ? 1.72696   61.80965 18.01688 1.000 28.78808 ? 279 GLU A OE1 1 
ATOM   2264 O OE2 . GLU A 1 279 ? 2.12250   63.06841 19.80724 1.000 26.02746 ? 279 GLU A OE2 1 
ATOM   2265 N N   . LYS A 1 280 ? 5.81409   59.53172 22.37932 1.000 26.13014 ? 280 LYS A N   1 
ATOM   2266 C CA  . LYS A 1 280 ? 7.23734   59.26147 22.17226 1.000 26.94206 ? 280 LYS A CA  1 
ATOM   2267 C C   . LYS A 1 280 ? 7.88998   58.72226 23.43776 1.000 25.17973 ? 280 LYS A C   1 
ATOM   2268 O O   . LYS A 1 280 ? 8.76737   59.36646 24.00232 1.000 25.00446 ? 280 LYS A O   1 
ATOM   2269 C CB  . LYS A 1 280 ? 7.97424   60.52701 21.72008 1.000 26.59547 ? 280 LYS A CB  1 
ATOM   2270 C CG  . LYS A 1 280 ? 7.46460   61.11775 20.41364 1.000 27.20353 ? 280 LYS A CG  1 
ATOM   2271 C CD  . LYS A 1 280 ? 7.77633   60.23093 19.22039 1.000 30.23383 ? 280 LYS A CD  1 
ATOM   2272 C CE  . LYS A 1 280 ? 9.25237   60.24206 18.88916 1.000 36.07236 ? 280 LYS A CE  1 
ATOM   2273 N NZ  . LYS A 1 280 ? 9.53539   59.47097 17.64429 1.000 43.65742 ? 280 LYS A NZ  1 
ATOM   2274 N N   . PRO A 1 281 ? 7.47049   57.52963 23.88099 1.000 24.14350 ? 281 PRO A N   1 
ATOM   2275 C CA  . PRO A 1 281 ? 7.95607   57.00678 25.16237 1.000 24.27900 ? 281 PRO A CA  1 
ATOM   2276 C C   . PRO A 1 281 ? 9.47404   56.79581 25.18971 1.000 25.95229 ? 281 PRO A C   1 
ATOM   2277 O O   . PRO A 1 281 ? 10.09768  57.02430 26.22766 1.000 27.08125 ? 281 PRO A O   1 
ATOM   2278 C CB  . PRO A 1 281 ? 7.21227   55.67372 25.30005 1.000 25.72490 ? 281 PRO A CB  1 
ATOM   2279 C CG  . PRO A 1 281 ? 6.88206   55.27401 23.89680 1.000 27.07981 ? 281 PRO A CG  1 
ATOM   2280 C CD  . PRO A 1 281 ? 6.59899   56.56828 23.18198 1.000 23.83791 ? 281 PRO A CD  1 
ATOM   2281 N N   . GLU A 1 282 ? 10.06279  56.38551 24.07097 1.000 27.53016 ? 282 GLU A N   1 
ATOM   2282 C CA  . GLU A 1 282 ? 11.50512  56.15433 24.03182 1.000 30.52416 ? 282 GLU A CA  1 
ATOM   2283 C C   . GLU A 1 282 ? 12.30128  57.45121 24.18656 1.000 28.37186 ? 282 GLU A C   1 
ATOM   2284 O O   . GLU A 1 282 ? 13.37206  57.45474 24.78531 1.000 27.14327 ? 282 GLU A O   1 
ATOM   2285 C CB  . GLU A 1 282 ? 11.89731  55.43633 22.73998 1.000 39.75215 ? 282 GLU A CB  1 
ATOM   2286 C CG  . GLU A 1 282 ? 11.28492  54.04243 22.62212 1.000 49.80339 ? 282 GLU A CG  1 
ATOM   2287 C CD  . GLU A 1 282 ? 12.14796  53.07607 21.82429 1.000 70.20584 ? 282 GLU A CD  1 
ATOM   2288 O OE1 . GLU A 1 282 ? 13.26573  53.46506 21.41639 1.000 78.15943 ? 282 GLU A OE1 1 
ATOM   2289 O OE2 . GLU A 1 282 ? 11.71034  51.92297 21.60908 1.000 78.21548 ? 282 GLU A OE2 1 
ATOM   2290 N N   . VAL A 1 283 ? 11.77372  58.55217 23.65977 1.000 28.30366 ? 283 VAL A N   1 
ATOM   2291 C CA  . VAL A 1 283 ? 12.37555  59.86268 23.89573 1.000 25.45717 ? 283 VAL A CA  1 
ATOM   2292 C C   . VAL A 1 283 ? 12.35028  60.20293 25.37895 1.000 25.00849 ? 283 VAL A C   1 
ATOM   2293 O O   . VAL A 1 283 ? 13.36152  60.61784 25.94510 1.000 28.08628 ? 283 VAL A O   1 
ATOM   2294 C CB  . VAL A 1 283 ? 11.65905  60.97730 23.09755 1.000 26.96417 ? 283 VAL A CB  1 
ATOM   2295 C CG1 . VAL A 1 283 ? 12.16268  62.34881 23.51735 1.000 26.59032 ? 283 VAL A CG1 1 
ATOM   2296 C CG2 . VAL A 1 283 ? 11.87055  60.77249 21.60649 1.000 30.59274 ? 283 VAL A CG2 1 
ATOM   2297 N N   . VAL A 1 284 ? 11.19995  60.01209 26.01794 1.000 24.86120 ? 284 VAL A N   1 
ATOM   2298 C CA  . VAL A 1 284 ? 11.08054  60.29345 27.44338 1.000 26.93555 ? 284 VAL A CA  1 
ATOM   2299 C C   . VAL A 1 284 ? 12.08905  59.47433 28.25654 1.000 26.00554 ? 284 VAL A C   1 
ATOM   2300 O O   . VAL A 1 284 ? 12.79788  60.01200 29.09791 1.000 25.97312 ? 284 VAL A O   1 
ATOM   2301 C CB  . VAL A 1 284 ? 9.65866   60.00025 27.97493 1.000 24.25645 ? 284 VAL A CB  1 
ATOM   2302 C CG1 . VAL A 1 284 ? 9.63810   60.05832 29.49565 1.000 22.27133 ? 284 VAL A CG1 1 
ATOM   2303 C CG2 . VAL A 1 284 ? 8.66580   60.98027 27.39773 1.000 24.12412 ? 284 VAL A CG2 1 
ATOM   2304 N N   . ILE A 1 285 ? 12.15048  58.17673 27.99468 1.000 25.13933 ? 285 ILE A N   1 
ATOM   2305 C CA  . ILE A 1 285 ? 13.06336  57.30740 28.73117 1.000 27.81702 ? 285 ILE A CA  1 
ATOM   2306 C C   . ILE A 1 285 ? 14.51295  57.75621 28.54540 1.000 28.09491 ? 285 ILE A C   1 
ATOM   2307 O O   . ILE A 1 285 ? 15.26982  57.86327 29.50846 1.000 27.07851 ? 285 ILE A O   1 
ATOM   2308 C CB  . ILE A 1 285 ? 12.91647  55.82924 28.28848 1.000 28.65803 ? 285 ILE A CB  1 
ATOM   2309 C CG1 . ILE A 1 285 ? 11.50954  55.31474 28.62187 1.000 26.35659 ? 285 ILE A CG1 1 
ATOM   2310 C CG2 . ILE A 1 285 ? 13.98975  54.95631 28.95420 1.000 27.50495 ? 285 ILE A CG2 1 
ATOM   2311 C CD1 . ILE A 1 285 ? 11.05859  54.13283 27.77616 1.000 25.08771 ? 285 ILE A CD1 1 
ATOM   2312 N N   . ASP A 1 286 ? 14.87714  58.04248 27.30060 1.000 28.44000 ? 286 ASP A N   1 
ATOM   2313 C CA  . ASP A 1 286 ? 16.23810  58.43381 26.97437 1.000 27.14474 ? 286 ASP A CA  1 
ATOM   2314 C C   . ASP A 1 286 ? 16.61585  59.76998 27.60515 1.000 29.83079 ? 286 ASP A C   1 
ATOM   2315 O O   . ASP A 1 286 ? 17.67827  59.89398 28.22781 1.000 30.05216 ? 286 ASP A O   1 
ATOM   2316 C CB  . ASP A 1 286 ? 16.41923  58.50573 25.45579 1.000 27.74436 ? 286 ASP A CB  1 
ATOM   2317 C CG  . ASP A 1 286 ? 17.81886  58.95912 25.05825 1.000 34.46939 ? 286 ASP A CG  1 
ATOM   2318 O OD1 . ASP A 1 286 ? 18.74160  58.11722 25.06351 1.000 37.26469 ? 286 ASP A OD1 1 
ATOM   2319 O OD2 . ASP A 1 286 ? 17.99849  60.15791 24.75274 1.000 35.18662 ? 286 ASP A OD2 1 
ATOM   2320 N N   . ARG A 1 287 ? 15.75094  60.77026 27.44994 1.000 27.39231 ? 287 ARG A N   1 
ATOM   2321 C CA  . ARG A 1 287 ? 16.07494  62.11288 27.93137 1.000 27.36600 ? 287 ARG A CA  1 
ATOM   2322 C C   . ARG A 1 287 ? 16.10670  62.20102 29.45997 1.000 28.28882 ? 287 ARG A C   1 
ATOM   2323 O O   . ARG A 1 287 ? 16.87723  62.98511 30.00515 1.000 27.91794 ? 287 ARG A O   1 
ATOM   2324 C CB  . ARG A 1 287 ? 15.08614  63.14942 27.38275 1.000 28.19615 ? 287 ARG A CB  1 
ATOM   2325 C CG  . ARG A 1 287 ? 15.05250  63.29418 25.86718 1.000 27.44622 ? 287 ARG A CG  1 
ATOM   2326 C CD  . ARG A 1 287 ? 16.42734  63.48242 25.22133 1.000 26.48983 ? 287 ARG A CD  1 
ATOM   2327 N NE  . ARG A 1 287 ? 16.25002  63.77079 23.79960 1.000 29.29984 ? 287 ARG A NE  1 
ATOM   2328 C CZ  . ARG A 1 287 ? 16.11851  62.84967 22.84932 1.000 30.72252 ? 287 ARG A CZ  1 
ATOM   2329 N NH1 . ARG A 1 287 ? 16.18405  61.56116 23.14702 1.000 33.08943 ? 287 ARG A NH1 1 
ATOM   2330 N NH2 . ARG A 1 287 ? 15.92840  63.21810 21.59454 1.000 32.03077 ? 287 ARG A NH2 1 
ATOM   2331 N N   . LEU A 1 288 ? 15.26648  61.42335 30.14794 1.000 25.64953 ? 288 LEU A N   1 
ATOM   2332 C CA  . LEU A 1 288 ? 15.26628  61.42612 31.61485 1.000 25.87790 ? 288 LEU A CA  1 
ATOM   2333 C C   . LEU A 1 288 ? 16.48157  60.66841 32.14761 1.000 28.68402 ? 288 LEU A C   1 
ATOM   2334 O O   . LEU A 1 288 ? 17.13991  61.12547 33.07282 1.000 30.41784 ? 288 LEU A O   1 
ATOM   2335 C CB  . LEU A 1 288 ? 13.97473  60.82048 32.19144 1.000 24.84313 ? 288 LEU A CB  1 
ATOM   2336 C CG  . LEU A 1 288 ? 12.65126  61.57564 31.97971 1.000 26.04631 ? 288 LEU A CG  1 
ATOM   2337 C CD1 . LEU A 1 288 ? 11.54224  60.88976 32.74327 1.000 27.24082 ? 288 LEU A CD1 1 
ATOM   2338 C CD2 . LEU A 1 288 ? 12.76573  63.03926 32.40162 1.000 21.56804 ? 288 LEU A CD2 1 
ATOM   2339 N N   . LYS A 1 289 ? 16.77077  59.50872 31.57095 1.000 28.72335 ? 289 LYS A N   1 
ATOM   2340 C CA  . LYS A 1 289 ? 17.98236  58.77467 31.93484 1.000 32.48107 ? 289 LYS A CA  1 
ATOM   2341 C C   . LYS A 1 289 ? 19.22945  59.63063 31.71750 1.000 36.13602 ? 289 LYS A C   1 
ATOM   2342 O O   . LYS A 1 289 ? 20.12666  59.64104 32.55457 1.000 39.60777 ? 289 LYS A O   1 
ATOM   2343 C CB  . LYS A 1 289 ? 18.09061  57.46491 31.14500 1.000 30.16261 ? 289 LYS A CB  1 
ATOM   2344 C CG  . LYS A 1 289 ? 17.31348  56.32565 31.78680 1.000 33.54296 ? 289 LYS A CG  1 
ATOM   2345 C CD  . LYS A 1 289 ? 17.33127  55.04756 30.95582 1.000 35.81386 ? 289 LYS A CD  1 
ATOM   2346 C CE  . LYS A 1 289 ? 16.59666  53.93278 31.69806 1.000 38.12286 ? 289 LYS A CE  1 
ATOM   2347 N NZ  . LYS A 1 289 ? 16.64735  52.61658 30.99944 1.000 42.87121 ? 289 LYS A NZ  1 
ATOM   2348 N N   . ALA A 1 290 ? 19.27027  60.36453 30.60759 1.000 33.45015 ? 290 ALA A N   1 
ATOM   2349 C CA  . ALA A 1 290 ? 20.40262  61.23620 30.31112 1.000 36.75600 ? 290 ALA A CA  1 
ATOM   2350 C C   . ALA A 1 290 ? 20.43807  62.44798 31.23567 1.000 38.13761 ? 290 ALA A C   1 
ATOM   2351 O O   . ALA A 1 290 ? 21.46837  62.74329 31.83859 1.000 38.19092 ? 290 ALA A O   1 
ATOM   2352 C CB  . ALA A 1 290 ? 20.36163  61.68516 28.85846 1.000 36.59251 ? 290 ALA A CB  1 
ATOM   2353 N N   . GLY A 1 291 ? 19.31132  63.14641 31.34518 1.000 35.01108 ? 291 GLY A N   1 
ATOM   2354 C CA  . GLY A 1 291 ? 19.23465  64.33533 32.17236 1.000 31.11145 ? 291 GLY A CA  1 
ATOM   2355 C C   . GLY A 1 291 ? 19.49639  64.07633 33.64675 1.000 32.25774 ? 291 GLY A C   1 
ATOM   2356 O O   . GLY A 1 291 ? 20.05114  64.92179 34.33897 1.000 30.33709 ? 291 GLY A O   1 
ATOM   2357 N N   . PHE A 1 292 ? 19.09647  62.90507 34.12972 1.000 31.18817 ? 292 PHE A N   1 
ATOM   2358 C CA  . PHE A 1 292 ? 19.19004  62.59640 35.55518 1.000 36.07917 ? 292 PHE A CA  1 
ATOM   2359 C C   . PHE A 1 292 ? 20.33249  61.63154 35.87776 1.000 41.11915 ? 292 PHE A C   1 
ATOM   2360 O O   . PHE A 1 292 ? 20.29369  60.94536 36.90325 1.000 44.53783 ? 292 PHE A O   1 
ATOM   2361 C CB  . PHE A 1 292 ? 17.87516  61.98830 36.06685 1.000 32.05221 ? 292 PHE A CB  1 
ATOM   2362 C CG  . PHE A 1 292 ? 16.70081  62.93115 36.04457 1.000 28.95001 ? 292 PHE A CG  1 
ATOM   2363 C CD1 . PHE A 1 292 ? 16.88248  64.30288 35.94966 1.000 27.37838 ? 292 PHE A CD1 1 
ATOM   2364 C CD2 . PHE A 1 292 ? 15.40798  62.43746 36.13714 1.000 25.75449 ? 292 PHE A CD2 1 
ATOM   2365 C CE1 . PHE A 1 292 ? 15.79306  65.17176 35.94695 1.000 24.37134 ? 292 PHE A CE1 1 
ATOM   2366 C CE2 . PHE A 1 292 ? 14.31348  63.29809 36.12925 1.000 24.56901 ? 292 PHE A CE2 1 
ATOM   2367 C CZ  . PHE A 1 292 ? 14.51364  64.67214 36.02903 1.000 23.57179 ? 292 PHE A CZ  1 
ATOM   2368 N N   . ARG A 1 293 ? 21.33723  61.56520 35.00861 1.000 42.65881 ? 293 ARG A N   1 
ATOM   2369 C CA  . ARG A 1 293 ? 22.41978  60.58946 35.17418 1.000 52.35814 ? 293 ARG A CA  1 
ATOM   2370 C C   . ARG A 1 293 ? 23.17498  60.79199 36.48513 1.000 53.00701 ? 293 ARG A C   1 
ATOM   2371 O O   . ARG A 1 293 ? 23.51753  61.91855 36.84698 1.000 49.93421 ? 293 ARG A O   1 
ATOM   2372 C CB  . ARG A 1 293 ? 23.39473  60.66214 33.99497 1.000 55.41073 ? 293 ARG A CB  1 
ATOM   2373 C CG  . ARG A 1 293 ? 23.38043  59.43793 33.08319 1.000 60.39414 ? 293 ARG A CG  1 
ATOM   2374 C CD  . ARG A 1 293 ? 24.54355  58.49455 33.37338 1.000 70.43845 ? 293 ARG A CD  1 
ATOM   2375 N NE  . ARG A 1 293 ? 24.21742  57.45765 34.35142 1.000 76.10961 ? 293 ARG A NE  1 
ATOM   2376 C CZ  . ARG A 1 293 ? 24.31907  56.15084 34.11669 1.000 82.32998 ? 293 ARG A CZ  1 
ATOM   2377 N NH1 . ARG A 1 293 ? 24.73945  55.71728 32.93347 1.000 84.66467 ? 293 ARG A NH1 1 
ATOM   2378 N NH2 . ARG A 1 293 ? 24.00391  55.27513 35.06475 1.000 81.74670 ? 293 ARG A NH2 1 
ATOM   2379 O OXT . ARG A 1 293 ? 23.45203  59.83251 37.20899 1.000 55.63055 ? 293 ARG A OXT 1 
HETATM 2380 O O   . HOH B 2 .   ? -24.58706 57.09304 19.45235 1.000 49.49099 ? 301 HOH A O   1 
HETATM 2381 O O   . HOH B 2 .   ? 13.42383  69.85873 54.65844 1.000 55.03980 ? 302 HOH A O   1 
HETATM 2382 O O   . HOH B 2 .   ? -11.23725 47.50755 25.12989 1.000 40.46100 ? 303 HOH A O   1 
HETATM 2383 O O   . HOH B 2 .   ? 2.67723   44.58257 24.74579 1.000 58.23687 ? 304 HOH A O   1 
HETATM 2384 O O   . HOH B 2 .   ? 6.723     54.776   54.991   1.000 37.31255 ? 305 HOH A O   1 
HETATM 2385 O O   . HOH B 2 .   ? 0.48321   59.34253 17.44835 1.000 33.34666 ? 306 HOH A O   1 
HETATM 2386 O O   . HOH B 2 .   ? -3.00842  65.74499 52.02432 1.000 32.99654 ? 307 HOH A O   1 
HETATM 2387 O O   . HOH B 2 .   ? -2.77522  63.49776 30.60519 1.000 27.98850 ? 308 HOH A O   1 
HETATM 2388 O O   . HOH B 2 .   ? 3.58276   79.64765 30.40225 1.000 24.08727 ? 309 HOH A O   1 
HETATM 2389 O O   . HOH B 2 .   ? -7.56642  70.02742 51.12302 1.000 38.12809 ? 310 HOH A O   1 
HETATM 2390 O O   . HOH B 2 .   ? -11.26688 53.99671 42.80446 1.000 35.91917 ? 311 HOH A O   1 
HETATM 2391 O O   . HOH B 2 .   ? -14.59705 70.98488 52.63735 1.000 51.48406 ? 312 HOH A O   1 
HETATM 2392 O O   . HOH B 2 .   ? 15.25661  66.80540 19.30976 1.000 49.18392 ? 313 HOH A O   1 
HETATM 2393 O O   . HOH B 2 .   ? -0.73710  85.65357 42.38604 1.000 42.19706 ? 314 HOH A O   1 
HETATM 2394 O O   . HOH B 2 .   ? -29.33735 63.89372 32.75436 1.000 35.33471 ? 315 HOH A O   1 
HETATM 2395 O O   . HOH B 2 .   ? 16.60588  52.56279 28.49659 1.000 43.90641 ? 316 HOH A O   1 
HETATM 2396 O O   . HOH B 2 .   ? -9.02496  58.04024 17.89634 1.000 36.52101 ? 317 HOH A O   1 
HETATM 2397 O O   . HOH B 2 .   ? -20.94842 70.16936 38.43597 1.000 26.17852 ? 318 HOH A O   1 
HETATM 2398 O O   . HOH B 2 .   ? -8.23931  73.96205 16.96415 1.000 33.72076 ? 319 HOH A O   1 
HETATM 2399 O O   . HOH B 2 .   ? -10.25355 61.94941 16.82409 1.000 32.33338 ? 320 HOH A O   1 
HETATM 2400 O O   . HOH B 2 .   ? -8.84356  53.66247 52.06881 1.000 47.80032 ? 321 HOH A O   1 
HETATM 2401 O O   . HOH B 2 .   ? 7.50918   60.18100 13.80020 1.000 41.84968 ? 322 HOH A O   1 
HETATM 2402 O O   . HOH B 2 .   ? 8.17184   75.47343 17.46492 1.000 32.99119 ? 323 HOH A O   1 
HETATM 2403 O O   . HOH B 2 .   ? -8.42594  54.30188 37.62601 1.000 30.11738 ? 324 HOH A O   1 
HETATM 2404 O O   . HOH B 2 .   ? -10.42965 62.96785 37.79466 1.000 20.50338 ? 325 HOH A O   1 
HETATM 2405 O O   . HOH B 2 .   ? -15.41131 59.17499 18.52877 1.000 39.64137 ? 326 HOH A O   1 
HETATM 2406 O O   . HOH B 2 .   ? 6.28887   49.80246 31.79002 1.000 30.94828 ? 327 HOH A O   1 
HETATM 2407 O O   . HOH B 2 .   ? 19.66177  62.76028 47.32707 1.000 45.07369 ? 328 HOH A O   1 
HETATM 2408 O O   . HOH B 2 .   ? 1.30463   86.42519 29.43305 1.000 35.04548 ? 329 HOH A O   1 
HETATM 2409 O O   . HOH B 2 .   ? 16.14937  69.39734 27.40922 1.000 24.21657 ? 330 HOH A O   1 
HETATM 2410 O O   . HOH B 2 .   ? 0.91922   63.63733 22.02169 1.000 26.53545 ? 331 HOH A O   1 
HETATM 2411 O O   . HOH B 2 .   ? -1.49477  68.35157 51.05966 1.000 31.82673 ? 332 HOH A O   1 
HETATM 2412 O O   . HOH B 2 .   ? -0.37579  51.85947 26.45159 1.000 36.57014 ? 333 HOH A O   1 
HETATM 2413 O O   . HOH B 2 .   ? -0.96800  82.76486 34.71928 1.000 31.70638 ? 334 HOH A O   1 
HETATM 2414 O O   . HOH B 2 .   ? -25.24680 59.85863 26.58301 1.000 25.41694 ? 335 HOH A O   1 
HETATM 2415 O O   . HOH B 2 .   ? -17.09309 59.90956 36.61297 1.000 20.89140 ? 336 HOH A O   1 
HETATM 2416 O O   . HOH B 2 .   ? 7.81296   76.19388 35.05680 1.000 28.87078 ? 337 HOH A O   1 
HETATM 2417 O O   . HOH B 2 .   ? 4.02540   78.55811 46.61703 1.000 31.34032 ? 338 HOH A O   1 
HETATM 2418 O O   . HOH B 2 .   ? -14.53438 61.98743 19.53737 1.000 29.11205 ? 339 HOH A O   1 
HETATM 2419 O O   . HOH B 2 .   ? 9.31791   53.74347 51.29949 1.000 32.69794 ? 340 HOH A O   1 
HETATM 2420 O O   . HOH B 2 .   ? 21.64127  63.77681 38.64420 1.000 44.19311 ? 341 HOH A O   1 
HETATM 2421 O O   . HOH B 2 .   ? -0.34560  67.55211 14.27763 1.000 46.93548 ? 342 HOH A O   1 
HETATM 2422 O O   . HOH B 2 .   ? 10.44076  50.90808 43.95953 1.000 30.51643 ? 343 HOH A O   1 
HETATM 2423 O O   . HOH B 2 .   ? 7.77684   85.11654 31.45797 1.000 30.34268 ? 344 HOH A O   1 
HETATM 2424 O O   . HOH B 2 .   ? -26.52583 69.86193 34.56815 1.000 30.98202 ? 345 HOH A O   1 
HETATM 2425 O O   . HOH B 2 .   ? 16.58943  76.50296 36.52798 1.000 27.18246 ? 346 HOH A O   1 
HETATM 2426 O O   . HOH B 2 .   ? 1.37193   60.46394 37.91008 1.000 21.34155 ? 347 HOH A O   1 
HETATM 2427 O O   . HOH B 2 .   ? -12.13167 75.58058 18.54413 1.000 27.61506 ? 348 HOH A O   1 
HETATM 2428 O O   . HOH B 2 .   ? 5.252     55.521   56.543   1.000 32.72819 ? 349 HOH A O   1 
HETATM 2429 O O   . HOH B 2 .   ? -1.10547  75.08440 51.06550 1.000 38.71479 ? 350 HOH A O   1 
HETATM 2430 O O   . HOH B 2 .   ? 17.51397  81.75693 29.54202 1.000 24.34321 ? 351 HOH A O   1 
HETATM 2431 O O   . HOH B 2 .   ? 2.08300   70.88274 29.53343 1.000 25.24051 ? 352 HOH A O   1 
HETATM 2432 O O   . HOH B 2 .   ? -10.60349 64.58185 51.56684 1.000 37.92530 ? 353 HOH A O   1 
HETATM 2433 O O   . HOH B 2 .   ? -4.94222  44.71105 26.48529 1.000 44.14298 ? 354 HOH A O   1 
HETATM 2434 O O   . HOH B 2 .   ? -8.65466  61.82114 34.04729 1.000 27.45360 ? 355 HOH A O   1 
HETATM 2435 O O   . HOH B 2 .   ? -4.49810  45.85611 23.51181 1.000 43.39111 ? 356 HOH A O   1 
HETATM 2436 O O   . HOH B 2 .   ? 17.37552  82.57285 32.25078 1.000 28.72204 ? 357 HOH A O   1 
HETATM 2437 O O   . HOH B 2 .   ? 1.47806   53.10246 50.67149 1.000 25.51210 ? 358 HOH A O   1 
HETATM 2438 O O   . HOH B 2 .   ? -13.61626 62.52307 49.99583 1.000 32.60808 ? 359 HOH A O   1 
HETATM 2439 O O   . HOH B 2 .   ? -15.28427 52.46128 35.26236 1.000 33.57977 ? 360 HOH A O   1 
HETATM 2440 O O   . HOH B 2 .   ? -7.84526  72.40618 22.52887 1.000 24.34637 ? 361 HOH A O   1 
HETATM 2441 O O   . HOH B 2 .   ? 4.40236   48.56356 40.01951 1.000 30.45620 ? 362 HOH A O   1 
HETATM 2442 O O   . HOH B 2 .   ? 16.88350  66.86608 26.25546 1.000 34.46925 ? 363 HOH A O   1 
HETATM 2443 O O   . HOH B 2 .   ? -1.91423  76.51854 19.07213 1.000 28.14542 ? 364 HOH A O   1 
HETATM 2444 O O   . HOH B 2 .   ? -0.56968  54.64338 22.21365 1.000 34.13890 ? 365 HOH A O   1 
HETATM 2445 O O   . HOH B 2 .   ? 3.43010   73.69593 19.63134 1.000 27.75978 ? 366 HOH A O   1 
HETATM 2446 O O   . HOH B 2 .   ? 11.68092  62.76906 17.55738 1.000 42.36324 ? 367 HOH A O   1 
HETATM 2447 O O   . HOH B 2 .   ? -2.33431  65.18998 44.79517 1.000 23.50615 ? 368 HOH A O   1 
HETATM 2448 O O   . HOH B 2 .   ? 5.90281   74.55384 34.59261 1.000 23.20533 ? 369 HOH A O   1 
HETATM 2449 O O   . HOH B 2 .   ? -8.07620  46.97467 33.01051 1.000 34.83785 ? 370 HOH A O   1 
HETATM 2450 O O   . HOH B 2 .   ? 6.11230   87.02175 37.40497 1.000 45.82153 ? 371 HOH A O   1 
HETATM 2451 O O   . HOH B 2 .   ? 9.64631   46.87482 36.37176 1.000 43.32500 ? 372 HOH A O   1 
HETATM 2452 O O   . HOH B 2 .   ? 18.99241  68.31876 30.74918 1.000 32.77576 ? 373 HOH A O   1 
HETATM 2453 O O   . HOH B 2 .   ? -3.24160  69.35759 55.63191 1.000 39.41289 ? 374 HOH A O   1 
HETATM 2454 O O   . HOH B 2 .   ? 16.31106  59.72046 45.76703 1.000 34.95068 ? 375 HOH A O   1 
HETATM 2455 O O   . HOH B 2 .   ? -5.96350  54.73874 39.07820 1.000 28.92010 ? 376 HOH A O   1 
HETATM 2456 O O   . HOH B 2 .   ? 3.99480   56.04715 28.99443 1.000 27.11184 ? 377 HOH A O   1 
HETATM 2457 O O   . HOH B 2 .   ? 11.19842  71.70343 52.66936 1.000 52.70251 ? 378 HOH A O   1 
HETATM 2458 O O   . HOH B 2 .   ? -14.66310 80.89777 34.37595 1.000 20.76618 ? 379 HOH A O   1 
HETATM 2459 O O   . HOH B 2 .   ? -8.56710  61.30125 53.70626 1.000 31.27486 ? 380 HOH A O   1 
HETATM 2460 O O   . HOH B 2 .   ? 5.90076   77.60705 45.20444 1.000 27.82589 ? 381 HOH A O   1 
HETATM 2461 O O   . HOH B 2 .   ? 0.50603   51.28368 21.93159 1.000 39.07536 ? 382 HOH A O   1 
HETATM 2462 O O   . HOH B 2 .   ? -13.72244 68.46759 53.55974 1.000 54.65172 ? 383 HOH A O   1 
HETATM 2463 O O   . HOH B 2 .   ? -9.58504  49.39379 33.00625 1.000 36.28727 ? 384 HOH A O   1 
HETATM 2464 O O   . HOH B 2 .   ? 1.50392   80.08325 19.70287 1.000 29.22098 ? 385 HOH A O   1 
HETATM 2465 O O   . HOH B 2 .   ? -11.93606 56.72464 43.42189 1.000 30.84744 ? 386 HOH A O   1 
HETATM 2466 O O   . HOH B 2 .   ? -1.92198  71.44686 51.81977 1.000 38.27821 ? 387 HOH A O   1 
HETATM 2467 O O   . HOH B 2 .   ? 9.621     72.411   12.734   1.000 39.59705 ? 388 HOH A O   1 
HETATM 2468 O O   . HOH B 2 .   ? -16.90915 78.51118 38.09580 1.000 43.01719 ? 389 HOH A O   1 
HETATM 2469 O O   . HOH B 2 .   ? 12.98099  78.35663 46.78680 1.000 32.87533 ? 390 HOH A O   1 
HETATM 2470 O O   . HOH B 2 .   ? 1.16030   62.67344 46.19826 1.000 23.40725 ? 391 HOH A O   1 
HETATM 2471 O O   . HOH B 2 .   ? -12.24786 65.26358 34.02034 1.000 20.08805 ? 392 HOH A O   1 
HETATM 2472 O O   . HOH B 2 .   ? -2.17968  66.03814 29.88585 1.000 25.92686 ? 393 HOH A O   1 
HETATM 2473 O O   . HOH B 2 .   ? 3.63114   46.17673 23.58869 1.000 51.09125 ? 394 HOH A O   1 
HETATM 2474 O O   . HOH B 2 .   ? 10.07751  69.25158 53.42295 1.000 39.72598 ? 395 HOH A O   1 
HETATM 2475 O O   . HOH B 2 .   ? -19.81952 56.19734 20.04031 1.000 47.73028 ? 396 HOH A O   1 
HETATM 2476 O O   . HOH B 2 .   ? -4.67435  76.23137 48.75448 1.000 41.75912 ? 397 HOH A O   1 
HETATM 2477 O O   . HOH B 2 .   ? 14.83319  86.84498 31.70373 1.000 32.62962 ? 398 HOH A O   1 
HETATM 2478 O O   . HOH B 2 .   ? 21.49442  67.40628 34.34578 1.000 50.28279 ? 399 HOH A O   1 
HETATM 2479 O O   . HOH B 2 .   ? 3.28245   62.67802 55.13874 1.000 37.08479 ? 400 HOH A O   1 
HETATM 2480 O O   . HOH B 2 .   ? -14.26703 57.00949 42.85686 1.000 34.08117 ? 401 HOH A O   1 
HETATM 2481 O O   . HOH B 2 .   ? -7.01760  79.73535 42.04899 1.000 34.85095 ? 402 HOH A O   1 
HETATM 2482 O O   . HOH B 2 .   ? 5.49032   51.81240 49.34872 1.000 29.25238 ? 403 HOH A O   1 
HETATM 2483 O O   . HOH B 2 .   ? -8.87214  47.83002 27.16705 1.000 35.28279 ? 404 HOH A O   1 
HETATM 2484 O O   . HOH B 2 .   ? -4.30852  69.89960 51.51227 1.000 43.45048 ? 405 HOH A O   1 
HETATM 2485 O O   . HOH B 2 .   ? -12.15771 82.06848 41.72731 1.000 40.96840 ? 406 HOH A O   1 
HETATM 2486 O O   . HOH B 2 .   ? -6.81887  58.01396 20.43682 1.000 27.01977 ? 407 HOH A O   1 
HETATM 2487 O O   . HOH B 2 .   ? -3.15178  80.28142 19.95813 1.000 31.32031 ? 408 HOH A O   1 
HETATM 2488 O O   . HOH B 2 .   ? 1.13063   50.47745 28.34820 1.000 34.09342 ? 409 HOH A O   1 
HETATM 2489 O O   . HOH B 2 .   ? 4.12049   65.17061 55.91376 1.000 39.97038 ? 410 HOH A O   1 
HETATM 2490 O O   . HOH B 2 .   ? 4.70940   58.30158 17.77320 1.000 38.36171 ? 411 HOH A O   1 
HETATM 2491 O O   . HOH B 2 .   ? -11.13914 47.94608 29.25760 1.000 36.62537 ? 412 HOH A O   1 
HETATM 2492 O O   . HOH B 2 .   ? 1.31533   43.30719 41.87409 1.000 42.36728 ? 413 HOH A O   1 
HETATM 2493 O O   . HOH B 2 .   ? 5.95580   78.42816 29.38406 1.000 23.09856 ? 414 HOH A O   1 
HETATM 2494 O O   . HOH B 2 .   ? 23.71512  72.53938 37.81701 1.000 39.02186 ? 415 HOH A O   1 
HETATM 2495 O O   . HOH B 2 .   ? -2.64731  81.56836 44.82975 1.000 38.22709 ? 416 HOH A O   1 
HETATM 2496 O O   . HOH B 2 .   ? -10.08831 71.74924 21.20760 1.000 26.10783 ? 417 HOH A O   1 
HETATM 2497 O O   . HOH B 2 .   ? -3.52094  48.01546 22.42927 1.000 39.62982 ? 418 HOH A O   1 
HETATM 2498 O O   . HOH B 2 .   ? 12.76156  46.11118 32.13186 1.000 55.17741 ? 419 HOH A O   1 
HETATM 2499 O O   . HOH B 2 .   ? 10.93824  84.94418 29.97898 1.000 29.61611 ? 420 HOH A O   1 
HETATM 2500 O O   . HOH B 2 .   ? -15.21638 83.01912 38.05326 1.000 34.16216 ? 421 HOH A O   1 
HETATM 2501 O O   . HOH B 2 .   ? 16.12560  51.79357 45.77164 1.000 43.43548 ? 422 HOH A O   1 
HETATM 2502 O O   . HOH B 2 .   ? 20.37021  57.19554 34.00079 1.000 46.83609 ? 423 HOH A O   1 
HETATM 2503 O O   . HOH B 2 .   ? -25.32159 62.08133 33.44349 1.000 32.37426 ? 424 HOH A O   1 
HETATM 2504 O O   . HOH B 2 .   ? -3.65285  65.90723 15.80780 1.000 32.35474 ? 425 HOH A O   1 
HETATM 2505 O O   . HOH B 2 .   ? -5.72843  77.71997 43.07676 1.000 29.59540 ? 426 HOH A O   1 
HETATM 2506 O O   . HOH B 2 .   ? 17.63712  68.49332 35.04549 1.000 29.84732 ? 427 HOH A O   1 
HETATM 2507 O O   . HOH B 2 .   ? 19.03109  51.31288 31.87677 1.000 53.54106 ? 428 HOH A O   1 
HETATM 2508 O O   . HOH B 2 .   ? -9.95814  86.26513 25.22500 0.50  30.35966 ? 429 HOH A O   1 
HETATM 2509 O O   . HOH B 2 .   ? 7.47459   57.53870 17.20883 1.000 49.13783 ? 430 HOH A O   1 
HETATM 2510 O O   . HOH B 2 .   ? -4.21033  84.12975 23.02525 1.000 24.33067 ? 431 HOH A O   1 
HETATM 2511 O O   . HOH B 2 .   ? -15.63986 76.12764 46.73856 1.000 31.89444 ? 432 HOH A O   1 
HETATM 2512 O O   . HOH B 2 .   ? -23.99116 67.96348 36.74001 1.000 29.89603 ? 433 HOH A O   1 
HETATM 2513 O O   . HOH B 2 .   ? 0.81567   57.29788 19.92462 1.000 34.02099 ? 434 HOH A O   1 
HETATM 2514 O O   . HOH B 2 .   ? 7.26745   83.21727 21.50253 1.000 33.05670 ? 435 HOH A O   1 
HETATM 2515 O O   . HOH B 2 .   ? -11.59349 59.77663 53.24161 1.000 51.04819 ? 436 HOH A O   1 
HETATM 2516 O O   . HOH B 2 .   ? 4.18288   42.92832 43.66927 1.000 42.08574 ? 437 HOH A O   1 
HETATM 2517 O O   . HOH B 2 .   ? 1.27116   69.63162 54.01620 1.000 35.38107 ? 438 HOH A O   1 
HETATM 2518 O O   . HOH B 2 .   ? -8.85969  52.06578 33.78221 1.000 28.19646 ? 439 HOH A O   1 
HETATM 2519 O O   . HOH B 2 .   ? 4.73952   67.07905 25.48671 1.000 27.73839 ? 440 HOH A O   1 
HETATM 2520 O O   . HOH B 2 .   ? 1.46921   79.04547 49.95450 1.000 41.73460 ? 441 HOH A O   1 
HETATM 2521 O O   . HOH B 2 .   ? 10.13408  60.78729 56.47680 1.000 42.31401 ? 442 HOH A O   1 
HETATM 2522 O O   . HOH B 2 .   ? 2.10102   68.54653 28.08380 1.000 24.11776 ? 443 HOH A O   1 
HETATM 2523 O O   . HOH B 2 .   ? -0.94886  55.28555 27.69117 1.000 46.98509 ? 444 HOH A O   1 
HETATM 2524 O O   . HOH B 2 .   ? -17.80794 62.48331 37.68692 1.000 23.47244 ? 445 HOH A O   1 
HETATM 2525 O O   . HOH B 2 .   ? 16.01641  84.78156 35.03533 1.000 35.79163 ? 446 HOH A O   1 
HETATM 2526 O O   . HOH B 2 .   ? 15.29860  68.59314 18.60259 1.000 33.90102 ? 447 HOH A O   1 
HETATM 2527 O O   . HOH B 2 .   ? -5.83736  79.80292 18.30388 1.000 30.74252 ? 448 HOH A O   1 
HETATM 2528 O O   . HOH B 2 .   ? -9.83956  53.16573 48.55977 1.000 59.91635 ? 449 HOH A O   1 
HETATM 2529 O O   . HOH B 2 .   ? -3.09696  77.07736 43.70260 1.000 24.98263 ? 450 HOH A O   1 
HETATM 2530 O O   . HOH B 2 .   ? 14.27758  54.27822 46.99845 1.000 42.96930 ? 451 HOH A O   1 
HETATM 2531 O O   . HOH B 2 .   ? -1.72108  68.90967 16.61704 1.000 33.18076 ? 452 HOH A O   1 
HETATM 2532 O O   . HOH B 2 .   ? -13.19724 59.62466 46.62829 1.000 27.11230 ? 453 HOH A O   1 
HETATM 2533 O O   . HOH B 2 .   ? 13.73013  85.37551 41.97658 1.000 32.00726 ? 454 HOH A O   1 
HETATM 2534 O O   . HOH B 2 .   ? 10.32046  46.85114 42.17162 1.000 40.65076 ? 455 HOH A O   1 
HETATM 2535 O O   . HOH B 2 .   ? -8.50908  55.72555 19.53629 1.000 35.02631 ? 456 HOH A O   1 
HETATM 2536 O O   . HOH B 2 .   ? -0.51467  85.43395 38.73887 1.000 44.73571 ? 457 HOH A O   1 
HETATM 2537 O O   . HOH B 2 .   ? 14.07661  76.28141 43.27506 1.000 31.94677 ? 458 HOH A O   1 
HETATM 2538 O O   . HOH B 2 .   ? 2.87380   49.47768 27.54938 1.000 45.26894 ? 459 HOH A O   1 
HETATM 2539 O O   . HOH B 2 .   ? -12.97239 88.02307 35.82209 1.000 32.19424 ? 460 HOH A O   1 
HETATM 2540 O O   . HOH B 2 .   ? -8.41351  58.75924 32.10750 1.000 28.02799 ? 461 HOH A O   1 
HETATM 2541 O O   . HOH B 2 .   ? 18.03172  65.15033 28.37403 1.000 36.12798 ? 462 HOH A O   1 
HETATM 2542 O O   . HOH B 2 .   ? -6.12666  88.56306 24.10488 1.000 28.76257 ? 463 HOH A O   1 
HETATM 2543 O O   . HOH B 2 .   ? 4.18067   65.54612 27.70717 1.000 19.97405 ? 464 HOH A O   1 
HETATM 2544 O O   . HOH B 2 .   ? -25.01812 55.02051 25.02479 1.000 42.47551 ? 465 HOH A O   1 
HETATM 2545 O O   . HOH B 2 .   ? 12.48705  59.42660 17.47966 1.000 51.95544 ? 466 HOH A O   1 
HETATM 2546 O O   . HOH B 2 .   ? -0.92412  62.86253 44.27932 1.000 20.95863 ? 467 HOH A O   1 
HETATM 2547 O O   . HOH B 2 .   ? -15.30569 59.17699 44.96987 1.000 29.85663 ? 468 HOH A O   1 
HETATM 2548 O O   . HOH B 2 .   ? -6.61202  55.66853 56.30355 1.000 47.59582 ? 469 HOH A O   1 
HETATM 2549 O O   . HOH B 2 .   ? 7.80734   87.31327 44.19645 1.000 38.46420 ? 470 HOH A O   1 
HETATM 2550 O O   . HOH B 2 .   ? -22.59666 53.89038 25.86919 1.000 34.04092 ? 471 HOH A O   1 
HETATM 2551 O O   . HOH B 2 .   ? -19.97324 59.97574 38.98916 1.000 30.54401 ? 472 HOH A O   1 
HETATM 2552 O O   . HOH B 2 .   ? 4.27797   60.68300 16.31615 1.000 34.92667 ? 473 HOH A O   1 
HETATM 2553 O O   . HOH B 2 .   ? 12.22199  54.04139 50.14441 1.000 42.17308 ? 474 HOH A O   1 
HETATM 2554 O O   . HOH B 2 .   ? -9.22374  60.68005 36.63301 1.000 23.65001 ? 475 HOH A O   1 
HETATM 2555 O O   . HOH B 2 .   ? -12.74417 66.33723 51.67098 1.000 32.35940 ? 476 HOH A O   1 
HETATM 2556 O O   . HOH B 2 .   ? 3.58786   43.67200 33.29389 1.000 45.72497 ? 477 HOH A O   1 
HETATM 2557 O O   . HOH B 2 .   ? 14.80071  54.84713 24.78456 1.000 38.80922 ? 478 HOH A O   1 
HETATM 2558 O O   . HOH B 2 .   ? 15.52306  47.60603 39.28206 1.000 46.54065 ? 479 HOH A O   1 
HETATM 2559 O O   . HOH B 2 .   ? -23.62158 75.57001 35.70586 1.000 31.60272 ? 480 HOH A O   1 
HETATM 2560 O O   . HOH B 2 .   ? 19.45817  69.74579 44.09611 1.000 45.47236 ? 481 HOH A O   1 
HETATM 2561 O O   . HOH B 2 .   ? 1.16694   63.18064 55.82836 1.000 39.46327 ? 482 HOH A O   1 
HETATM 2562 O O   . HOH B 2 .   ? -12.41781 53.06386 22.46908 1.000 43.28887 ? 483 HOH A O   1 
HETATM 2563 O O   . HOH B 2 .   ? -12.87569 66.87807 16.90203 1.000 25.24900 ? 484 HOH A O   1 
HETATM 2564 O O   . HOH B 2 .   ? -14.87869 78.92337 40.44211 1.000 39.20613 ? 485 HOH A O   1 
HETATM 2565 O O   . HOH B 2 .   ? -23.06165 53.80050 29.68835 1.000 35.19701 ? 486 HOH A O   1 
HETATM 2566 O O   . HOH B 2 .   ? -14.68295 49.60684 22.68238 1.000 53.67054 ? 487 HOH A O   1 
HETATM 2567 O O   . HOH B 2 .   ? 12.85597  65.81010 17.35885 1.000 36.06157 ? 488 HOH A O   1 
HETATM 2568 O O   . HOH B 2 .   ? 24.96645  66.32376 38.08129 1.000 55.05316 ? 489 HOH A O   1 
HETATM 2569 O O   . HOH B 2 .   ? 1.31275   84.79548 47.47003 1.000 36.30728 ? 490 HOH A O   1 
HETATM 2570 O O   . HOH B 2 .   ? 12.88551  81.04121 45.26969 1.000 44.15463 ? 491 HOH A O   1 
HETATM 2571 O O   . HOH B 2 .   ? 10.10727  89.62205 30.02197 1.000 43.72351 ? 492 HOH A O   1 
HETATM 2572 O O   . HOH B 2 .   ? 7.12197   88.30251 33.68316 1.000 45.34740 ? 493 HOH A O   1 
HETATM 2573 O O   . HOH B 2 .   ? -22.76340 62.80460 37.04536 1.000 32.41390 ? 494 HOH A O   1 
HETATM 2574 O O   . HOH B 2 .   ? 24.65497  60.83402 39.78231 1.000 55.47305 ? 495 HOH A O   1 
HETATM 2575 O O   . HOH B 2 .   ? 18.35490  70.71015 45.82855 1.000 49.06148 ? 496 HOH A O   1 
HETATM 2576 O O   . HOH B 2 .   ? -6.31879  50.78869 42.65611 1.000 37.72229 ? 497 HOH A O   1 
HETATM 2577 O O   . HOH B 2 .   ? 0.97705   64.44462 11.69109 1.000 43.03594 ? 498 HOH A O   1 
HETATM 2578 O O   . HOH B 2 .   ? -17.68640 64.84563 47.55891 1.000 31.05615 ? 499 HOH A O   1 
HETATM 2579 O O   . HOH B 2 .   ? 9.42217   56.68685 21.12631 1.000 33.36009 ? 500 HOH A O   1 
HETATM 2580 O O   . HOH B 2 .   ? -7.13865  47.93075 20.37300 1.000 35.71741 ? 501 HOH A O   1 
HETATM 2581 O O   . HOH B 2 .   ? -20.11030 63.88861 40.74716 1.000 35.25629 ? 502 HOH A O   1 
HETATM 2582 O O   . HOH B 2 .   ? 20.41956  58.71680 38.95425 1.000 43.87402 ? 503 HOH A O   1 
HETATM 2583 O O   . HOH B 2 .   ? 16.74198  78.12307 43.48398 1.000 37.31111 ? 504 HOH A O   1 
HETATM 2584 O O   . HOH B 2 .   ? -18.46071 71.56400 42.10233 1.000 37.00873 ? 505 HOH A O   1 
HETATM 2585 O O   . HOH B 2 .   ? 3.42968   82.43103 23.40656 1.000 30.16161 ? 506 HOH A O   1 
HETATM 2586 O O   . HOH B 2 .   ? 15.43398  57.30595 47.59091 1.000 42.06856 ? 507 HOH A O   1 
HETATM 2587 O O   . HOH B 2 .   ? -10.76467 80.10964 42.24729 1.000 47.21996 ? 508 HOH A O   1 
HETATM 2588 O O   . HOH B 2 .   ? 16.91448  85.30371 32.34483 1.000 36.26883 ? 509 HOH A O   1 
HETATM 2589 O O   . HOH B 2 .   ? 22.59514  75.14527 40.77010 1.000 49.74505 ? 510 HOH A O   1 
HETATM 2590 O O   . HOH B 2 .   ? -7.67628  83.28075 35.44309 1.000 39.88879 ? 511 HOH A O   1 
HETATM 2591 O O   . HOH B 2 .   ? -0.73873  61.39047 57.32747 1.000 56.07892 ? 512 HOH A O   1 
HETATM 2592 O O   . HOH B 2 .   ? -5.43838  51.64165 37.96212 1.000 31.20591 ? 513 HOH A O   1 
HETATM 2593 O O   . HOH B 2 .   ? -5.98959  77.60027 17.17885 1.000 32.73035 ? 514 HOH A O   1 
HETATM 2594 O O   . HOH B 2 .   ? 20.09208  57.99183 28.02587 1.000 44.70212 ? 515 HOH A O   1 
HETATM 2595 O O   . HOH B 2 .   ? 20.21028  56.24491 38.53839 1.000 40.57715 ? 516 HOH A O   1 
HETATM 2596 O O   . HOH B 2 .   ? -18.62202 74.36976 44.35387 1.000 44.81862 ? 517 HOH A O   1 
HETATM 2597 O O   . HOH B 2 .   ? -8.12488  63.38339 56.73892 1.000 55.30025 ? 518 HOH A O   1 
HETATM 2598 O O   . HOH B 2 .   ? -5.21538  61.82897 57.94232 1.000 41.63380 ? 519 HOH A O   1 
HETATM 2599 O O   . HOH B 2 .   ? 4.07511   77.53293 18.69960 1.000 37.44351 ? 520 HOH A O   1 
HETATM 2600 O O   . HOH B 2 .   ? -3.27453  64.41577 13.49880 1.000 39.20224 ? 521 HOH A O   1 
HETATM 2601 O O   . HOH B 2 .   ? 1.16986   88.06555 33.06230 1.000 41.28455 ? 522 HOH A O   1 
HETATM 2602 O O   . HOH B 2 .   ? 5.17318   88.65545 43.39880 1.000 44.21679 ? 523 HOH A O   1 
HETATM 2603 O O   . HOH B 2 .   ? 3.88758   86.63371 27.90860 1.000 47.71909 ? 524 HOH A O   1 
HETATM 2604 O O   . HOH B 2 .   ? -2.64867  62.64572 12.02965 1.000 42.98809 ? 525 HOH A O   1 
HETATM 2605 O O   . HOH B 2 .   ? -17.79377 73.60325 50.44639 1.000 40.37140 ? 526 HOH A O   1 
HETATM 2606 O O   . HOH B 2 .   ? -18.12216 52.43612 32.02576 1.000 40.86139 ? 527 HOH A O   1 
HETATM 2607 O O   . HOH B 2 .   ? 11.76379  61.98034 54.77351 1.000 40.94222 ? 528 HOH A O   1 
HETATM 2608 O O   . HOH B 2 .   ? 9.348     87.009   26.897   1.000 37.90107 ? 529 HOH A O   1 
HETATM 2609 O O   . HOH B 2 .   ? 4.37883   82.73778 48.49620 1.000 32.22697 ? 530 HOH A O   1 
HETATM 2610 O O   . HOH B 2 .   ? 11.08357  77.89213 50.14362 1.000 39.09534 ? 531 HOH A O   1 
HETATM 2611 O O   . HOH B 2 .   ? -17.12855 67.74229 53.81068 1.000 55.02144 ? 532 HOH A O   1 
HETATM 2612 O O   . HOH B 2 .   ? 16.84666  60.51490 49.25539 1.000 41.76703 ? 533 HOH A O   1 
HETATM 2613 O O   . HOH B 2 .   ? 9.71542   73.64897 52.99155 1.000 48.95448 ? 534 HOH A O   1 
HETATM 2614 O O   . HOH B 2 .   ? -23.61325 56.56083 32.95130 1.000 45.86524 ? 535 HOH A O   1 
HETATM 2615 O O   . HOH B 2 .   ? 2.87593   84.13616 25.38764 1.000 38.34463 ? 536 HOH A O   1 
HETATM 2616 O O   . HOH B 2 .   ? -18.99282 53.43388 37.27296 1.000 54.54778 ? 537 HOH A O   1 
HETATM 2617 O O   . HOH B 2 .   ? 3.70058   69.63633 53.40084 1.000 36.06495 ? 538 HOH A O   1 
HETATM 2618 O O   . HOH B 2 .   ? 7.90856   68.55960 54.34820 1.000 46.97330 ? 539 HOH A O   1 
HETATM 2619 O O   . HOH B 2 .   ? -5.00082  68.24488 15.21731 1.000 45.86653 ? 540 HOH A O   1 
HETATM 2620 O O   . HOH B 2 .   ? 21.62555  68.38498 41.56229 1.000 49.90353 ? 541 HOH A O   1 
HETATM 2621 O O   . HOH B 2 .   ? 15.93998  58.89322 51.80053 1.000 56.70902 ? 542 HOH A O   1 
HETATM 2622 O O   . HOH B 2 .   ? 10.81623  86.15086 38.28196 1.000 37.54051 ? 543 HOH A O   1 
HETATM 2623 O O   . HOH B 2 .   ? -8.21681  86.51809 37.32867 1.000 46.46482 ? 544 HOH A O   1 
HETATM 2624 O O   . HOH B 2 .   ? 5.94863   68.75683 54.54604 1.000 54.86171 ? 545 HOH A O   1 
HETATM 2625 O O   . HOH B 2 .   ? 19.13986  82.41914 39.76778 1.000 47.22445 ? 546 HOH A O   1 
HETATM 2626 O O   . HOH B 2 .   ? 9.26474   77.54699 51.41928 1.000 51.39725 ? 547 HOH A O   1 
HETATM 2627 O O   . HOH B 2 .   ? 11.32978  57.23070 19.29796 1.000 51.26109 ? 548 HOH A O   1 
HETATM 2628 O O   . HOH B 2 .   ? -17.47239 75.99280 49.27076 1.000 54.85332 ? 549 HOH A O   1 
HETATM 2629 O O   . HOH B 2 .   ? -24.49231 60.30781 35.24929 1.000 48.20874 ? 550 HOH A O   1 
HETATM 2630 O O   . HOH B 2 .   ? -12.02336 50.91058 40.84646 1.000 51.77356 ? 551 HOH A O   1 
HETATM 2631 O O   . HOH B 2 .   ? 10.54767  47.29739 31.08870 1.000 46.70559 ? 552 HOH A O   1 
HETATM 2632 O O   . HOH B 2 .   ? -5.39746  81.17677 35.77778 1.000 43.95002 ? 553 HOH A O   1 
HETATM 2633 O O   . HOH B 2 .   ? -14.69182 59.95135 15.63950 1.000 57.52022 ? 554 HOH A O   1 
HETATM 2634 O O   . HOH B 2 .   ? 21.22369  54.81914 32.16782 1.000 51.86986 ? 555 HOH A O   1 
HETATM 2635 O O   . HOH B 2 .   ? -9.81297  87.67788 40.01419 1.000 58.06108 ? 556 HOH A O   1 
HETATM 2636 O O   . HOH B 2 .   ? 21.33365  56.81182 36.53209 1.000 47.79777 ? 557 HOH A O   1 
HETATM 2637 O O   . HOH B 2 .   ? 2.23517   62.53086 10.64515 1.000 50.63415 ? 558 HOH A O   1 
HETATM 2638 O O   . HOH B 2 .   ? -10.32242 83.18167 43.82881 1.000 56.76178 ? 559 HOH A O   1 
HETATM 2639 O O   . HOH B 2 .   ? 6.20032   69.71772 13.32922 1.000 45.38888 ? 560 HOH A O   1 
HETATM 2640 O O   . HOH B 2 .   ? 11.585    87.132   28.804   1.000 34.99392 ? 561 HOH A O   1 
HETATM 2641 O O   . HOH B 2 .   ? -10.19747 63.78759 35.13932 1.000 23.87599 ? 562 HOH A O   1 
HETATM 2642 O O   . HOH B 2 .   ? -6.43830  87.74937 28.75581 1.000 34.11685 ? 563 HOH A O   1 
HETATM 2643 O O   . HOH B 2 .   ? -12.11273 63.11127 18.22937 1.000 28.96956 ? 564 HOH A O   1 
HETATM 2644 O O   . HOH B 2 .   ? -22.08311 67.74608 39.06724 1.000 34.18978 ? 565 HOH A O   1 
HETATM 2645 O O   . HOH B 2 .   ? -20.72196 71.10087 42.05525 1.000 51.69282 ? 566 HOH A O   1 
HETATM 2646 O O   . HOH B 2 .   ? -25.80322 55.19512 31.49610 1.000 53.96702 ? 567 HOH A O   1 
HETATM 2647 O O   . HOH B 2 .   ? -3.16860  75.81344 50.81911 1.000 52.62454 ? 568 HOH A O   1 
HETATM 2648 O O   . HOH B 2 .   ? 21.24696  53.61147 39.86773 1.000 43.02698 ? 569 HOH A O   1 
HETATM 2649 O O   . HOH B 2 .   ? -4.396    53.883   53.380   1.000 40.49948 ? 570 HOH A O   1 
HETATM 2650 O O   . HOH B 2 .   ? 3.00875   55.51794 20.11024 1.000 48.81504 ? 571 HOH A O   1 
HETATM 2651 O O   . HOH B 2 .   ? 4.84513   84.45065 21.69221 1.000 42.47725 ? 572 HOH A O   1 
HETATM 2652 O O   . HOH B 2 .   ? 6.853     58.150   57.994   1.000 47.03982 ? 573 HOH A O   1 
HETATM 2653 O O   . HOH B 2 .   ? 8.52704   84.61364 47.58156 1.000 36.77225 ? 574 HOH A O   1 
HETATM 2654 O O   . HOH B 2 .   ? 9.106     54.835   55.572   1.000 38.71131 ? 575 HOH A O   1 
HETATM 2655 O O   . HOH B 2 .   ? -10.21283 72.77921 18.64026 1.000 29.13720 ? 576 HOH A O   1 
HETATM 2656 O O   . HOH B 2 .   ? -15.34411 64.35896 51.75289 1.000 47.16380 ? 577 HOH A O   1 
HETATM 2657 O O   . HOH B 2 .   ? 6.679     53.543   53.311   1.000 31.77519 ? 578 HOH A O   1 
HETATM 2658 O O   . HOH B 2 .   ? -6.95629  65.17151 15.40851 1.000 37.81281 ? 579 HOH A O   1 
HETATM 2659 O O   . HOH B 2 .   ? 3.98802   80.11269 48.94435 1.000 37.39434 ? 580 HOH A O   1 
HETATM 2660 O O   . HOH B 2 .   ? 11.733    50.662   48.424   1.000 40.51739 ? 581 HOH A O   1 
HETATM 2661 O O   . HOH B 2 .   ? -8.59442  88.62715 25.22500 0.50  30.88284 ? 582 HOH A O   1 
HETATM 2662 O O   . HOH B 2 .   ? -5.87360  86.22031 32.39042 1.000 42.95650 ? 583 HOH A O   1 
HETATM 2663 O O   . HOH B 2 .   ? 7.22675   88.61884 24.21476 1.000 48.12992 ? 584 HOH A O   1 
HETATM 2664 O O   . HOH B 2 .   ? -24.36441 65.36080 36.68411 1.000 33.41677 ? 585 HOH A O   1 
HETATM 2665 O O   . HOH B 2 .   ? -0.69678  87.06669 34.89360 1.000 45.81791 ? 586 HOH A O   1 
HETATM 2666 O O   . HOH B 2 .   ? -2.58395  61.38514 58.63662 1.000 49.55666 ? 587 HOH A O   1 
HETATM 2667 O O   . HOH B 2 .   ? -3.66423  73.19695 30.35911 1.000 34.12753 ? 588 HOH A O   1 
HETATM 2668 O O   . HOH B 2 .   ? 12.751    46.177   43.636   1.000 44.33129 ? 589 HOH A O   1 
HETATM 2669 O O   . HOH B 2 .   ? 8.86320   87.53601 36.64837 1.000 43.08232 ? 590 HOH A O   1 
HETATM 2670 O O   . HOH B 2 .   ? 8.415     56.871   57.178   1.000 44.82136 ? 591 HOH A O   1 
HETATM 2671 O O   . HOH B 2 .   ? 13.24484  53.06899 25.19539 1.000 49.86893 ? 592 HOH A O   1 
HETATM 2672 O O   . HOH B 2 .   ? 20.42167  52.48364 30.46121 1.000 55.32331 ? 593 HOH A O   1 
HETATM 2673 O O   . HOH B 2 .   ? -1.85658  62.76735 9.37582  1.000 58.35064 ? 594 HOH A O   1 
HETATM 2674 O O   . HOH B 2 .   ? -12.79505 60.45011 15.14127 1.000 51.06948 ? 595 HOH A O   1 
HETATM 2675 O O   . HOH B 2 .   ? 6.69952   84.08542 49.33273 1.000 39.75565 ? 596 HOH A O   1 
HETATM 2676 O O   . HOH B 2 .   ? 8.75957   86.39387 46.84002 1.000 47.02165 ? 597 HOH A O   1 
HETATM 2677 O O   . HOH B 2 .   ? 19.78282  69.75672 33.67290 1.000 34.49288 ? 598 HOH A O   1 
HETATM 2678 O O   . HOH B 2 .   ? 2.90601   58.07308 13.91551 1.000 52.30059 ? 599 HOH A O   1 
HETATM 2679 O O   . HOH B 2 .   ? 3.36171   70.04315 14.40798 1.000 42.44200 ? 600 HOH A O   1 
HETATM 2680 O O   . HOH B 2 .   ? -9.98572  56.89615 48.26194 1.000 42.27188 ? 601 HOH A O   1 
HETATM 2681 O O   . HOH B 2 .   ? -7.56334  51.85076 36.06441 1.000 29.92652 ? 602 HOH A O   1 
HETATM 2682 O O   . HOH B 2 .   ? 20.43374  66.45289 29.63465 1.000 41.68519 ? 603 HOH A O   1 
HETATM 2683 O O   . HOH B 2 .   ? 16.82747  54.69194 26.99004 1.000 42.75806 ? 604 HOH A O   1 
HETATM 2684 O O   . HOH B 2 .   ? -18.06213 73.47077 42.43908 1.000 45.48526 ? 605 HOH A O   1 
HETATM 2685 O O   . HOH B 2 .   ? -21.913   58.447   17.644   1.000 40.41427 ? 606 HOH A O   1 
HETATM 2686 O O   . HOH B 2 .   ? 22.29671  58.02087 29.62174 1.000 54.65038 ? 607 HOH A O   1 
HETATM 2687 O O   . HOH B 2 .   ? -10.13695 54.29644 19.25448 1.000 38.73040 ? 608 HOH A O   1 
HETATM 2688 O O   . HOH B 2 .   ? -1.59572  64.56478 11.04457 1.000 53.57134 ? 609 HOH A O   1 
HETATM 2689 O O   . HOH B 2 .   ? -27.23245 72.75281 34.46683 1.000 32.86705 ? 610 HOH A O   1 
HETATM 2690 O O   . HOH B 2 .   ? -22.47079 65.46689 40.81709 1.000 56.63319 ? 611 HOH A O   1 
HETATM 2691 O O   . HOH B 2 .   ? -10.524   70.709   16.339   1.000 37.20636 ? 612 HOH A O   1 
HETATM 2692 O O   . HOH B 2 .   ? 15.44967  89.52049 32.84525 1.000 49.38798 ? 613 HOH A O   1 
HETATM 2693 O O   . HOH B 2 .   ? 6.857     89.438   26.219   1.000 52.64625 ? 614 HOH A O   1 
HETATM 2694 O O   . HOH B 2 .   ? -2.37226  83.14536 20.42989 1.000 52.30998 ? 615 HOH A O   1 
HETATM 2695 O O   . HOH B 2 .   ? -7.53694  60.60793 58.45198 1.000 53.55856 ? 616 HOH A O   1 
HETATM 2696 O O   . HOH B 2 .   ? 7.05210   72.29366 13.18392 1.000 48.24499 ? 617 HOH A O   1 
HETATM 2697 O O   . HOH B 2 .   ? -16.64591 52.28927 37.58825 1.000 38.23400 ? 618 HOH A O   1 
HETATM 2698 O O   . HOH B 2 .   ? -6.91742  87.25066 40.02759 1.000 57.03664 ? 619 HOH A O   1 
HETATM 2699 O O   . HOH B 2 .   ? -10.74400 75.20195 16.29840 1.000 32.61307 ? 620 HOH A O   1 
HETATM 2700 O O   . HOH B 2 .   ? 20.170    67.715   23.207   1.000 56.14621 ? 621 HOH A O   1 
HETATM 2701 O O   . HOH B 2 .   ? -14.15727 59.72822 49.33970 1.000 40.22131 ? 622 HOH A O   1 
HETATM 2702 O O   . HOH B 2 .   ? 21.13060  71.24057 42.33267 1.000 46.80816 ? 623 HOH A O   1 
HETATM 2703 O O   . HOH B 2 .   ? 0.17441   52.79937 19.78219 1.000 39.75578 ? 624 HOH A O   1 
HETATM 2704 O O   . HOH B 2 .   ? -11.222   66.470   15.487   1.000 42.46597 ? 625 HOH A O   1 
HETATM 2705 O O   . HOH B 2 .   ? -6.08939  84.40532 33.89824 1.000 44.78196 ? 626 HOH A O   1 
HETATM 2706 O O   . HOH B 2 .   ? -4.77170  87.42814 38.73204 1.000 54.13332 ? 627 HOH A O   1 
HETATM 2707 O O   . HOH B 2 .   ? -11.86360 56.86862 46.30751 1.000 35.00946 ? 628 HOH A O   1 
HETATM 2708 O O   . HOH B 2 .   ? -21.11798 51.90459 25.13823 1.000 46.08758 ? 629 HOH A O   1 
HETATM 2709 O O   . HOH B 2 .   ? -9.68911  62.01041 55.84026 1.000 56.02234 ? 630 HOH A O   1 
HETATM 2710 O O   . HOH B 2 .   ? -0.78291  79.15842 19.19989 1.000 35.33927 ? 631 HOH A O   1 
HETATM 2711 O O   . HOH B 2 .   ? -12.10515 57.67531 50.63531 1.000 47.79363 ? 632 HOH A O   1 
HETATM 2712 O O   . HOH B 2 .   ? -16.82690 80.93072 38.10365 1.000 39.09273 ? 633 HOH A O   1 
HETATM 2713 O O   . HOH B 2 .   ? -4.66139  46.80817 19.63553 1.000 43.73292 ? 634 HOH A O   1 
HETATM 2714 O O   . HOH B 2 .   ? 2.45806   75.79385 17.60415 1.000 39.85971 ? 635 HOH A O   1 
HETATM 2715 O O   . HOH B 2 .   ? -13.61864 50.06635 35.87963 1.000 50.10687 ? 636 HOH A O   1 
HETATM 2716 O O   . HOH B 2 .   ? 5.39532   78.70099 17.02246 1.000 39.93158 ? 637 HOH A O   1 
HETATM 2717 O O   . HOH B 2 .   ? -6.44546  87.38557 30.65866 1.000 45.05872 ? 638 HOH A O   1 
HETATM 2718 O O   . HOH B 2 .   ? -23.63071 59.17168 36.83790 1.000 59.77956 ? 639 HOH A O   1 
HETATM 2719 O O   . HOH B 2 .   ? 13.27695  61.63282 18.47853 1.000 55.22959 ? 640 HOH A O   1 
HETATM 2720 O O   . HOH B 2 .   ? -20.65762 62.60712 38.54719 1.000 28.63406 ? 641 HOH A O   1 
HETATM 2721 O O   . HOH B 2 .   ? -5.29929  50.26642 45.50867 1.000 35.08938 ? 642 HOH A O   1 
HETATM 2722 O O   . HOH B 2 .   ? 1.13931   86.40503 25.71735 1.000 41.43820 ? 643 HOH A O   1 
HETATM 2723 O O   . HOH B 2 .   ? -26.46090 68.67703 37.34824 1.000 37.02963 ? 644 HOH A O   1 
HETATM 2724 O O   . HOH B 2 .   ? 12.69024  77.19034 51.56073 1.000 46.45131 ? 645 HOH A O   1 
HETATM 2725 O O   . HOH B 2 .   ? -17.48860 76.79238 40.20465 1.000 41.90697 ? 646 HOH A O   1 
HETATM 2726 O O   . HOH B 2 .   ? 1.49408   69.87136 14.12600 1.000 55.35822 ? 647 HOH A O   1 
HETATM 2727 O O   . HOH B 2 .   ? 1.15996   88.89784 30.71491 1.000 42.09812 ? 648 HOH A O   1 
HETATM 2728 O O   . HOH B 2 .   ? 18.95355  60.30647 45.48117 1.000 39.62712 ? 649 HOH A O   1 
HETATM 2729 O O   . HOH B 2 .   ? -13.70001 49.99714 39.11413 1.000 50.79356 ? 650 HOH A O   1 
HETATM 2730 O O   . HOH B 2 .   ? -3.34306  73.61140 32.38761 1.000 48.22449 ? 651 HOH A O   1 
HETATM 2731 O O   . HOH B 2 .   ? 19.99848  68.87475 25.22500 0.50  54.48163 ? 652 HOH A O   1 
HETATM 2732 O O   . HOH B 2 .   ? 11.47801  59.61081 57.94775 1.000 62.43522 ? 653 HOH A O   1 
HETATM 2733 O O   . HOH B 2 .   ? -7.953    78.023   15.293   1.000 32.67364 ? 654 HOH A O   1 
HETATM 2734 O O   . HOH B 2 .   ? -16.84282 85.18893 37.01681 1.000 37.95804 ? 655 HOH A O   1 
HETATM 2735 O O   . HOH B 2 .   ? 4.32745   60.21535 13.79739 1.000 43.32730 ? 656 HOH A O   1 
HETATM 2736 O O   . HOH B 2 .   ? -15.59944 87.61440 36.17533 1.000 32.42358 ? 657 HOH A O   1 
HETATM 2737 O O   . HOH B 2 .   ? -17.34123 81.52780 35.26885 1.000 31.85407 ? 658 HOH A O   1 
HETATM 2738 O O   . HOH B 2 .   ? 18.49578  84.74557 38.89395 1.000 45.27505 ? 659 HOH A O   1 
HETATM 2739 O O   . HOH B 2 .   ? -5.82595  88.33876 32.81920 1.000 47.13379 ? 660 HOH A O   1 
HETATM 2740 O O   . HOH B 2 .   ? 22.36637  62.98360 44.57016 1.000 46.38086 ? 661 HOH A O   1 
HETATM 2741 O O   . HOH B 2 .   ? -4.826    81.285   15.734   1.000 39.31715 ? 662 HOH A O   1 
HETATM 2742 O O   . HOH B 2 .   ? -15.67563 54.44759 44.04871 1.000 45.87117 ? 663 HOH A O   1 
HETATM 2743 O O   . HOH B 2 .   ? -6.29929  64.45571 12.71779 1.000 51.19039 ? 664 HOH A O   1 
HETATM 2744 O O   . HOH B 2 .   ? -15.19798 51.84243 40.04455 1.000 46.10391 ? 665 HOH A O   1 
HETATM 2745 O O   . HOH B 2 .   ? -17.90953 86.18933 39.14244 1.000 49.61708 ? 666 HOH A O   1 
HETATM 2746 O O   . HOH B 2 .   ? -16.59323 78.49137 45.25899 1.000 49.27646 ? 667 HOH A O   1 
HETATM 2747 O O   . HOH B 2 .   ? 11.20618  84.03115 48.19054 1.000 42.32541 ? 668 HOH A O   1 
HETATM 2748 O O   . HOH B 2 .   ? -1.15850  90.56775 30.36216 1.000 49.35490 ? 669 HOH A O   1 
HETATM 2749 O O   . HOH B 2 .   ? -14.30547 55.29967 47.31723 1.000 46.22056 ? 670 HOH A O   1 
# 
