data_8ZQ8
# 
_entry.id   8ZQ8 
# 
_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   8ZQ8         pdb_00008zq8 10.2210/pdb8zq8/pdb 
WWPDB D_1300048320 ?            ?                   
# 
_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       2025-06-11 
_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                        8ZQ8 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-01 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              xiubo.tang@curegene.com.cn 
_pdbx_contact_author.name_first         Xiubo 
_pdbx_contact_author.name_last          Tang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0009-0008-0782-0913 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chen, X.' 1 ? 
'Hou, K.'  2 ? 
'Tang, X.' 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                     'SARS-Cov-2 3CL protease in complex with macrocyclic inhibitor CG-1039' 
_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 'Chen, X.' 1 ? 
primary 'Hou, K.'  2 ? 
primary 'Tang, X.' 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 '3C-like proteinase nsp5' 34735.559 1   3.4.22.69 ? ? 
'The first 10-residues (GPLGSSAVLQ) is the linker between the protein of interest and fusion tag.' 
2 non-polymer syn CG-1039                   580.675   1   ?         ? ? ? 
3 water       nat water                     18.015    396 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '3CL-PRO,3CLp,Main protease,Mpro,Non-structural protein 5,nsp5,SARS coronavirus main proteinase' 
# 
_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       
;GPLGSSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQA
GNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGF
NIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDF
NLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPLGSSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQA
GNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGF
NIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDF
NLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 CG-1039 A1D8T 
3 water   HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   LEU n 
1 4   GLY n 
1 5   SER n 
1 6   SER n 
1 7   ALA n 
1 8   VAL n 
1 9   LEU n 
1 10  GLN n 
1 11  SER n 
1 12  GLY n 
1 13  PHE n 
1 14  ARG n 
1 15  LYS n 
1 16  MET n 
1 17  ALA n 
1 18  PHE n 
1 19  PRO n 
1 20  SER n 
1 21  GLY n 
1 22  LYS n 
1 23  VAL n 
1 24  GLU n 
1 25  GLY n 
1 26  CYS n 
1 27  MET n 
1 28  VAL n 
1 29  GLN n 
1 30  VAL n 
1 31  THR n 
1 32  CYS n 
1 33  GLY n 
1 34  THR n 
1 35  THR n 
1 36  THR n 
1 37  LEU n 
1 38  ASN n 
1 39  GLY n 
1 40  LEU n 
1 41  TRP n 
1 42  LEU n 
1 43  ASP n 
1 44  ASP n 
1 45  VAL n 
1 46  VAL n 
1 47  TYR n 
1 48  CYS n 
1 49  PRO n 
1 50  ARG n 
1 51  HIS n 
1 52  VAL n 
1 53  ILE n 
1 54  CYS n 
1 55  THR n 
1 56  SER n 
1 57  GLU n 
1 58  ASP n 
1 59  MET n 
1 60  LEU n 
1 61  ASN n 
1 62  PRO n 
1 63  ASN n 
1 64  TYR n 
1 65  GLU n 
1 66  ASP n 
1 67  LEU n 
1 68  LEU n 
1 69  ILE n 
1 70  ARG n 
1 71  LYS n 
1 72  SER n 
1 73  ASN n 
1 74  HIS n 
1 75  ASN n 
1 76  PHE n 
1 77  LEU n 
1 78  VAL n 
1 79  GLN n 
1 80  ALA n 
1 81  GLY n 
1 82  ASN n 
1 83  VAL n 
1 84  GLN n 
1 85  LEU n 
1 86  ARG n 
1 87  VAL n 
1 88  ILE n 
1 89  GLY n 
1 90  HIS n 
1 91  SER n 
1 92  MET n 
1 93  GLN n 
1 94  ASN n 
1 95  CYS n 
1 96  VAL n 
1 97  LEU n 
1 98  LYS n 
1 99  LEU n 
1 100 LYS n 
1 101 VAL n 
1 102 ASP n 
1 103 THR n 
1 104 ALA n 
1 105 ASN n 
1 106 PRO n 
1 107 LYS n 
1 108 THR n 
1 109 PRO n 
1 110 LYS n 
1 111 TYR n 
1 112 LYS n 
1 113 PHE n 
1 114 VAL n 
1 115 ARG n 
1 116 ILE n 
1 117 GLN n 
1 118 PRO n 
1 119 GLY n 
1 120 GLN n 
1 121 THR n 
1 122 PHE n 
1 123 SER n 
1 124 VAL n 
1 125 LEU n 
1 126 ALA n 
1 127 CYS n 
1 128 TYR n 
1 129 ASN n 
1 130 GLY n 
1 131 SER n 
1 132 PRO n 
1 133 SER n 
1 134 GLY n 
1 135 VAL n 
1 136 TYR n 
1 137 GLN n 
1 138 CYS n 
1 139 ALA n 
1 140 MET n 
1 141 ARG n 
1 142 PRO n 
1 143 ASN n 
1 144 PHE n 
1 145 THR n 
1 146 ILE n 
1 147 LYS n 
1 148 GLY n 
1 149 SER n 
1 150 PHE n 
1 151 LEU n 
1 152 ASN n 
1 153 GLY n 
1 154 SER n 
1 155 CYS n 
1 156 GLY n 
1 157 SER n 
1 158 VAL n 
1 159 GLY n 
1 160 PHE n 
1 161 ASN n 
1 162 ILE n 
1 163 ASP n 
1 164 TYR n 
1 165 ASP n 
1 166 CYS n 
1 167 VAL n 
1 168 SER n 
1 169 PHE n 
1 170 CYS n 
1 171 TYR n 
1 172 MET n 
1 173 HIS n 
1 174 HIS n 
1 175 MET n 
1 176 GLU n 
1 177 LEU n 
1 178 PRO n 
1 179 THR n 
1 180 GLY n 
1 181 VAL n 
1 182 HIS n 
1 183 ALA n 
1 184 GLY n 
1 185 THR n 
1 186 ASP n 
1 187 LEU n 
1 188 GLU n 
1 189 GLY n 
1 190 ASN n 
1 191 PHE n 
1 192 TYR n 
1 193 GLY n 
1 194 PRO n 
1 195 PHE n 
1 196 VAL n 
1 197 ASP n 
1 198 ARG n 
1 199 GLN n 
1 200 THR n 
1 201 ALA n 
1 202 GLN n 
1 203 ALA n 
1 204 ALA n 
1 205 GLY n 
1 206 THR n 
1 207 ASP n 
1 208 THR n 
1 209 THR n 
1 210 ILE n 
1 211 THR n 
1 212 VAL n 
1 213 ASN n 
1 214 VAL n 
1 215 LEU n 
1 216 ALA n 
1 217 TRP n 
1 218 LEU n 
1 219 TYR n 
1 220 ALA n 
1 221 ALA n 
1 222 VAL n 
1 223 ILE n 
1 224 ASN n 
1 225 GLY n 
1 226 ASP n 
1 227 ARG n 
1 228 TRP n 
1 229 PHE n 
1 230 LEU n 
1 231 ASN n 
1 232 ARG n 
1 233 PHE n 
1 234 THR n 
1 235 THR n 
1 236 THR n 
1 237 LEU n 
1 238 ASN n 
1 239 ASP n 
1 240 PHE n 
1 241 ASN n 
1 242 LEU n 
1 243 VAL n 
1 244 ALA n 
1 245 MET n 
1 246 LYS n 
1 247 TYR n 
1 248 ASN n 
1 249 TYR n 
1 250 GLU n 
1 251 PRO n 
1 252 LEU n 
1 253 THR n 
1 254 GLN n 
1 255 ASP n 
1 256 HIS n 
1 257 VAL n 
1 258 ASP n 
1 259 ILE n 
1 260 LEU n 
1 261 GLY n 
1 262 PRO n 
1 263 LEU n 
1 264 SER n 
1 265 ALA n 
1 266 GLN n 
1 267 THR n 
1 268 GLY n 
1 269 ILE n 
1 270 ALA n 
1 271 VAL n 
1 272 LEU n 
1 273 ASP n 
1 274 MET n 
1 275 CYS n 
1 276 ALA n 
1 277 SER n 
1 278 LEU n 
1 279 LYS n 
1 280 GLU n 
1 281 LEU n 
1 282 LEU n 
1 283 GLN n 
1 284 ASN n 
1 285 GLY n 
1 286 MET n 
1 287 ASN n 
1 288 GLY n 
1 289 ARG n 
1 290 THR n 
1 291 ILE n 
1 292 LEU n 
1 293 GLY n 
1 294 SER n 
1 295 ALA n 
1 296 LEU n 
1 297 LEU n 
1 298 GLU n 
1 299 ASP n 
1 300 GLU n 
1 301 PHE n 
1 302 THR n 
1 303 PRO n 
1 304 PHE n 
1 305 ASP n 
1 306 VAL n 
1 307 VAL n 
1 308 ARG n 
1 309 GLN n 
1 310 CYS n 
1 311 SER n 
1 312 GLY n 
1 313 VAL n 
1 314 THR n 
1 315 PHE n 
1 316 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   316 
_entity_src_gen.gene_src_common_name               '2019-nCoV, SARS-CoV-2' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_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      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_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 
A1D8T peptide-like        . CG-1039         ? 'C30 H40 N6 O6'  580.675 
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   GLY 1   -9  ?   ?   ?   A . n 
A 1 2   PRO 2   -8  ?   ?   ?   A . n 
A 1 3   LEU 3   -7  ?   ?   ?   A . n 
A 1 4   GLY 4   -6  ?   ?   ?   A . n 
A 1 5   SER 5   -5  ?   ?   ?   A . n 
A 1 6   SER 6   -4  ?   ?   ?   A . n 
A 1 7   ALA 7   -3  ?   ?   ?   A . n 
A 1 8   VAL 8   -2  ?   ?   ?   A . n 
A 1 9   LEU 9   -1  ?   ?   ?   A . n 
A 1 10  GLN 10  0   ?   ?   ?   A . n 
A 1 11  SER 11  1   1   SER SER A . n 
A 1 12  GLY 12  2   2   GLY GLY A . n 
A 1 13  PHE 13  3   3   PHE PHE A . n 
A 1 14  ARG 14  4   4   ARG ARG A . n 
A 1 15  LYS 15  5   5   LYS LYS A . n 
A 1 16  MET 16  6   6   MET MET A . n 
A 1 17  ALA 17  7   7   ALA ALA A . n 
A 1 18  PHE 18  8   8   PHE PHE A . n 
A 1 19  PRO 19  9   9   PRO PRO A . n 
A 1 20  SER 20  10  10  SER SER A . n 
A 1 21  GLY 21  11  11  GLY GLY A . n 
A 1 22  LYS 22  12  12  LYS LYS A . n 
A 1 23  VAL 23  13  13  VAL VAL A . n 
A 1 24  GLU 24  14  14  GLU GLU A . n 
A 1 25  GLY 25  15  15  GLY GLY A . n 
A 1 26  CYS 26  16  16  CYS CYS A . n 
A 1 27  MET 27  17  17  MET MET A . n 
A 1 28  VAL 28  18  18  VAL VAL A . n 
A 1 29  GLN 29  19  19  GLN GLN A . n 
A 1 30  VAL 30  20  20  VAL VAL A . n 
A 1 31  THR 31  21  21  THR THR A . n 
A 1 32  CYS 32  22  22  CYS CYS A . n 
A 1 33  GLY 33  23  23  GLY GLY A . n 
A 1 34  THR 34  24  24  THR THR A . n 
A 1 35  THR 35  25  25  THR THR A . n 
A 1 36  THR 36  26  26  THR THR A . n 
A 1 37  LEU 37  27  27  LEU LEU A . n 
A 1 38  ASN 38  28  28  ASN ASN A . n 
A 1 39  GLY 39  29  29  GLY GLY A . n 
A 1 40  LEU 40  30  30  LEU LEU A . n 
A 1 41  TRP 41  31  31  TRP TRP A . n 
A 1 42  LEU 42  32  32  LEU LEU A . n 
A 1 43  ASP 43  33  33  ASP ASP A . n 
A 1 44  ASP 44  34  34  ASP ASP A . n 
A 1 45  VAL 45  35  35  VAL VAL A . n 
A 1 46  VAL 46  36  36  VAL VAL A . n 
A 1 47  TYR 47  37  37  TYR TYR A . n 
A 1 48  CYS 48  38  38  CYS CYS A . n 
A 1 49  PRO 49  39  39  PRO PRO A . n 
A 1 50  ARG 50  40  40  ARG ARG A . n 
A 1 51  HIS 51  41  41  HIS HIS A . n 
A 1 52  VAL 52  42  42  VAL VAL A . n 
A 1 53  ILE 53  43  43  ILE ILE A . n 
A 1 54  CYS 54  44  44  CYS CYS A . n 
A 1 55  THR 55  45  45  THR THR A . n 
A 1 56  SER 56  46  46  SER SER A . n 
A 1 57  GLU 57  47  47  GLU GLU A . n 
A 1 58  ASP 58  48  48  ASP ASP A . n 
A 1 59  MET 59  49  49  MET MET A . n 
A 1 60  LEU 60  50  50  LEU LEU A . n 
A 1 61  ASN 61  51  51  ASN ASN A . n 
A 1 62  PRO 62  52  52  PRO PRO A . n 
A 1 63  ASN 63  53  53  ASN ASN A . n 
A 1 64  TYR 64  54  54  TYR TYR A . n 
A 1 65  GLU 65  55  55  GLU GLU A . n 
A 1 66  ASP 66  56  56  ASP ASP A . n 
A 1 67  LEU 67  57  57  LEU LEU A . n 
A 1 68  LEU 68  58  58  LEU LEU A . n 
A 1 69  ILE 69  59  59  ILE ILE A . n 
A 1 70  ARG 70  60  60  ARG ARG A . n 
A 1 71  LYS 71  61  61  LYS LYS A . n 
A 1 72  SER 72  62  62  SER SER A . n 
A 1 73  ASN 73  63  63  ASN ASN A . n 
A 1 74  HIS 74  64  64  HIS HIS A . n 
A 1 75  ASN 75  65  65  ASN ASN A . n 
A 1 76  PHE 76  66  66  PHE PHE A . n 
A 1 77  LEU 77  67  67  LEU LEU A . n 
A 1 78  VAL 78  68  68  VAL VAL A . n 
A 1 79  GLN 79  69  69  GLN GLN A . n 
A 1 80  ALA 80  70  70  ALA ALA A . n 
A 1 81  GLY 81  71  71  GLY GLY A . n 
A 1 82  ASN 82  72  72  ASN ASN A . n 
A 1 83  VAL 83  73  73  VAL VAL A . n 
A 1 84  GLN 84  74  74  GLN GLN A . n 
A 1 85  LEU 85  75  75  LEU LEU A . n 
A 1 86  ARG 86  76  76  ARG ARG A . n 
A 1 87  VAL 87  77  77  VAL VAL A . n 
A 1 88  ILE 88  78  78  ILE ILE A . n 
A 1 89  GLY 89  79  79  GLY GLY A . n 
A 1 90  HIS 90  80  80  HIS HIS A . n 
A 1 91  SER 91  81  81  SER SER A . n 
A 1 92  MET 92  82  82  MET MET A . n 
A 1 93  GLN 93  83  83  GLN GLN A . n 
A 1 94  ASN 94  84  84  ASN ASN A . n 
A 1 95  CYS 95  85  85  CYS CYS A . n 
A 1 96  VAL 96  86  86  VAL VAL A . n 
A 1 97  LEU 97  87  87  LEU LEU A . n 
A 1 98  LYS 98  88  88  LYS LYS A . n 
A 1 99  LEU 99  89  89  LEU LEU A . n 
A 1 100 LYS 100 90  90  LYS LYS A . n 
A 1 101 VAL 101 91  91  VAL VAL A . n 
A 1 102 ASP 102 92  92  ASP ASP A . n 
A 1 103 THR 103 93  93  THR THR A . n 
A 1 104 ALA 104 94  94  ALA ALA A . n 
A 1 105 ASN 105 95  95  ASN ASN A . n 
A 1 106 PRO 106 96  96  PRO PRO A . n 
A 1 107 LYS 107 97  97  LYS LYS A . n 
A 1 108 THR 108 98  98  THR THR A . n 
A 1 109 PRO 109 99  99  PRO PRO A . n 
A 1 110 LYS 110 100 100 LYS LYS A . n 
A 1 111 TYR 111 101 101 TYR TYR A . n 
A 1 112 LYS 112 102 102 LYS LYS A . n 
A 1 113 PHE 113 103 103 PHE PHE A . n 
A 1 114 VAL 114 104 104 VAL VAL A . n 
A 1 115 ARG 115 105 105 ARG ARG A . n 
A 1 116 ILE 116 106 106 ILE ILE A . n 
A 1 117 GLN 117 107 107 GLN GLN A . n 
A 1 118 PRO 118 108 108 PRO PRO A . n 
A 1 119 GLY 119 109 109 GLY GLY A . n 
A 1 120 GLN 120 110 110 GLN GLN A . n 
A 1 121 THR 121 111 111 THR THR A . n 
A 1 122 PHE 122 112 112 PHE PHE A . n 
A 1 123 SER 123 113 113 SER SER A . n 
A 1 124 VAL 124 114 114 VAL VAL A . n 
A 1 125 LEU 125 115 115 LEU LEU A . n 
A 1 126 ALA 126 116 116 ALA ALA A . n 
A 1 127 CYS 127 117 117 CYS CYS A . n 
A 1 128 TYR 128 118 118 TYR TYR A . n 
A 1 129 ASN 129 119 119 ASN ASN A . n 
A 1 130 GLY 130 120 120 GLY GLY A . n 
A 1 131 SER 131 121 121 SER SER A . n 
A 1 132 PRO 132 122 122 PRO PRO A . n 
A 1 133 SER 133 123 123 SER SER A . n 
A 1 134 GLY 134 124 124 GLY GLY A . n 
A 1 135 VAL 135 125 125 VAL VAL A . n 
A 1 136 TYR 136 126 126 TYR TYR A . n 
A 1 137 GLN 137 127 127 GLN GLN A . n 
A 1 138 CYS 138 128 128 CYS CYS A . n 
A 1 139 ALA 139 129 129 ALA ALA A . n 
A 1 140 MET 140 130 130 MET MET A . n 
A 1 141 ARG 141 131 131 ARG ARG A . n 
A 1 142 PRO 142 132 132 PRO PRO A . n 
A 1 143 ASN 143 133 133 ASN ASN A . n 
A 1 144 PHE 144 134 134 PHE PHE A . n 
A 1 145 THR 145 135 135 THR THR A . n 
A 1 146 ILE 146 136 136 ILE ILE A . n 
A 1 147 LYS 147 137 137 LYS LYS A . n 
A 1 148 GLY 148 138 138 GLY GLY A . n 
A 1 149 SER 149 139 139 SER SER A . n 
A 1 150 PHE 150 140 140 PHE PHE A . n 
A 1 151 LEU 151 141 141 LEU LEU A . n 
A 1 152 ASN 152 142 142 ASN ASN A . n 
A 1 153 GLY 153 143 143 GLY GLY A . n 
A 1 154 SER 154 144 144 SER SER A . n 
A 1 155 CYS 155 145 145 CYS CYS A . n 
A 1 156 GLY 156 146 146 GLY GLY A . n 
A 1 157 SER 157 147 147 SER SER A . n 
A 1 158 VAL 158 148 148 VAL VAL A . n 
A 1 159 GLY 159 149 149 GLY GLY A . n 
A 1 160 PHE 160 150 150 PHE PHE A . n 
A 1 161 ASN 161 151 151 ASN ASN A . n 
A 1 162 ILE 162 152 152 ILE ILE A . n 
A 1 163 ASP 163 153 153 ASP ASP A . n 
A 1 164 TYR 164 154 154 TYR TYR A . n 
A 1 165 ASP 165 155 155 ASP ASP A . n 
A 1 166 CYS 166 156 156 CYS CYS A . n 
A 1 167 VAL 167 157 157 VAL VAL A . n 
A 1 168 SER 168 158 158 SER SER A . n 
A 1 169 PHE 169 159 159 PHE PHE A . n 
A 1 170 CYS 170 160 160 CYS CYS A . n 
A 1 171 TYR 171 161 161 TYR TYR A . n 
A 1 172 MET 172 162 162 MET MET A . n 
A 1 173 HIS 173 163 163 HIS HIS A . n 
A 1 174 HIS 174 164 164 HIS HIS A . n 
A 1 175 MET 175 165 165 MET MET A . n 
A 1 176 GLU 176 166 166 GLU GLU A . n 
A 1 177 LEU 177 167 167 LEU LEU A . n 
A 1 178 PRO 178 168 168 PRO PRO A . n 
A 1 179 THR 179 169 169 THR THR A . n 
A 1 180 GLY 180 170 170 GLY GLY A . n 
A 1 181 VAL 181 171 171 VAL VAL A . n 
A 1 182 HIS 182 172 172 HIS HIS A . n 
A 1 183 ALA 183 173 173 ALA ALA A . n 
A 1 184 GLY 184 174 174 GLY GLY A . n 
A 1 185 THR 185 175 175 THR THR A . n 
A 1 186 ASP 186 176 176 ASP ASP A . n 
A 1 187 LEU 187 177 177 LEU LEU A . n 
A 1 188 GLU 188 178 178 GLU GLU A . n 
A 1 189 GLY 189 179 179 GLY GLY A . n 
A 1 190 ASN 190 180 180 ASN ASN A . n 
A 1 191 PHE 191 181 181 PHE PHE A . n 
A 1 192 TYR 192 182 182 TYR TYR A . n 
A 1 193 GLY 193 183 183 GLY GLY A . n 
A 1 194 PRO 194 184 184 PRO PRO A . n 
A 1 195 PHE 195 185 185 PHE PHE A . n 
A 1 196 VAL 196 186 186 VAL VAL A . n 
A 1 197 ASP 197 187 187 ASP ASP A . n 
A 1 198 ARG 198 188 188 ARG ARG A . n 
A 1 199 GLN 199 189 189 GLN GLN A . n 
A 1 200 THR 200 190 190 THR THR A . n 
A 1 201 ALA 201 191 191 ALA ALA A . n 
A 1 202 GLN 202 192 192 GLN GLN A . n 
A 1 203 ALA 203 193 193 ALA ALA A . n 
A 1 204 ALA 204 194 194 ALA ALA A . n 
A 1 205 GLY 205 195 195 GLY GLY A . n 
A 1 206 THR 206 196 196 THR THR A . n 
A 1 207 ASP 207 197 197 ASP ASP A . n 
A 1 208 THR 208 198 198 THR THR A . n 
A 1 209 THR 209 199 199 THR THR A . n 
A 1 210 ILE 210 200 200 ILE ILE A . n 
A 1 211 THR 211 201 201 THR THR A . n 
A 1 212 VAL 212 202 202 VAL VAL A . n 
A 1 213 ASN 213 203 203 ASN ASN A . n 
A 1 214 VAL 214 204 204 VAL VAL A . n 
A 1 215 LEU 215 205 205 LEU LEU A . n 
A 1 216 ALA 216 206 206 ALA ALA A . n 
A 1 217 TRP 217 207 207 TRP TRP A . n 
A 1 218 LEU 218 208 208 LEU LEU A . n 
A 1 219 TYR 219 209 209 TYR TYR A . n 
A 1 220 ALA 220 210 210 ALA ALA A . n 
A 1 221 ALA 221 211 211 ALA ALA A . n 
A 1 222 VAL 222 212 212 VAL VAL A . n 
A 1 223 ILE 223 213 213 ILE ILE A . n 
A 1 224 ASN 224 214 214 ASN ASN A . n 
A 1 225 GLY 225 215 215 GLY GLY A . n 
A 1 226 ASP 226 216 216 ASP ASP A . n 
A 1 227 ARG 227 217 217 ARG ARG A . n 
A 1 228 TRP 228 218 218 TRP TRP A . n 
A 1 229 PHE 229 219 219 PHE PHE A . n 
A 1 230 LEU 230 220 220 LEU LEU A . n 
A 1 231 ASN 231 221 221 ASN ASN A . n 
A 1 232 ARG 232 222 222 ARG ARG A . n 
A 1 233 PHE 233 223 223 PHE PHE A . n 
A 1 234 THR 234 224 224 THR THR A . n 
A 1 235 THR 235 225 225 THR THR A . n 
A 1 236 THR 236 226 226 THR THR A . n 
A 1 237 LEU 237 227 227 LEU LEU A . n 
A 1 238 ASN 238 228 228 ASN ASN A . n 
A 1 239 ASP 239 229 229 ASP ASP A . n 
A 1 240 PHE 240 230 230 PHE PHE A . n 
A 1 241 ASN 241 231 231 ASN ASN A . n 
A 1 242 LEU 242 232 232 LEU LEU A . n 
A 1 243 VAL 243 233 233 VAL VAL A . n 
A 1 244 ALA 244 234 234 ALA ALA A . n 
A 1 245 MET 245 235 235 MET MET A . n 
A 1 246 LYS 246 236 236 LYS LYS A . n 
A 1 247 TYR 247 237 237 TYR TYR A . n 
A 1 248 ASN 248 238 238 ASN ASN A . n 
A 1 249 TYR 249 239 239 TYR TYR A . n 
A 1 250 GLU 250 240 240 GLU GLU A . n 
A 1 251 PRO 251 241 241 PRO PRO A . n 
A 1 252 LEU 252 242 242 LEU LEU A . n 
A 1 253 THR 253 243 243 THR THR A . n 
A 1 254 GLN 254 244 244 GLN GLN A . n 
A 1 255 ASP 255 245 245 ASP ASP A . n 
A 1 256 HIS 256 246 246 HIS HIS A . n 
A 1 257 VAL 257 247 247 VAL VAL A . n 
A 1 258 ASP 258 248 248 ASP ASP A . n 
A 1 259 ILE 259 249 249 ILE ILE A . n 
A 1 260 LEU 260 250 250 LEU LEU A . n 
A 1 261 GLY 261 251 251 GLY GLY A . n 
A 1 262 PRO 262 252 252 PRO PRO A . n 
A 1 263 LEU 263 253 253 LEU LEU A . n 
A 1 264 SER 264 254 254 SER SER A . n 
A 1 265 ALA 265 255 255 ALA ALA A . n 
A 1 266 GLN 266 256 256 GLN GLN A . n 
A 1 267 THR 267 257 257 THR THR A . n 
A 1 268 GLY 268 258 258 GLY GLY A . n 
A 1 269 ILE 269 259 259 ILE ILE A . n 
A 1 270 ALA 270 260 260 ALA ALA A . n 
A 1 271 VAL 271 261 261 VAL VAL A . n 
A 1 272 LEU 272 262 262 LEU LEU A . n 
A 1 273 ASP 273 263 263 ASP ASP A . n 
A 1 274 MET 274 264 264 MET MET A . n 
A 1 275 CYS 275 265 265 CYS CYS A . n 
A 1 276 ALA 276 266 266 ALA ALA A . n 
A 1 277 SER 277 267 267 SER SER A . n 
A 1 278 LEU 278 268 268 LEU LEU A . n 
A 1 279 LYS 279 269 269 LYS LYS A . n 
A 1 280 GLU 280 270 270 GLU GLU A . n 
A 1 281 LEU 281 271 271 LEU LEU A . n 
A 1 282 LEU 282 272 272 LEU LEU A . n 
A 1 283 GLN 283 273 273 GLN GLN A . n 
A 1 284 ASN 284 274 274 ASN ASN A . n 
A 1 285 GLY 285 275 275 GLY GLY A . n 
A 1 286 MET 286 276 276 MET MET A . n 
A 1 287 ASN 287 277 277 ASN ASN A . n 
A 1 288 GLY 288 278 278 GLY GLY A . n 
A 1 289 ARG 289 279 279 ARG ARG A . n 
A 1 290 THR 290 280 280 THR THR A . n 
A 1 291 ILE 291 281 281 ILE ILE A . n 
A 1 292 LEU 292 282 282 LEU LEU A . n 
A 1 293 GLY 293 283 283 GLY GLY A . n 
A 1 294 SER 294 284 284 SER SER A . n 
A 1 295 ALA 295 285 285 ALA ALA A . n 
A 1 296 LEU 296 286 286 LEU LEU A . n 
A 1 297 LEU 297 287 287 LEU LEU A . n 
A 1 298 GLU 298 288 288 GLU GLU A . n 
A 1 299 ASP 299 289 289 ASP ASP A . n 
A 1 300 GLU 300 290 290 GLU GLU A . n 
A 1 301 PHE 301 291 291 PHE PHE A . n 
A 1 302 THR 302 292 292 THR THR A . n 
A 1 303 PRO 303 293 293 PRO PRO A . n 
A 1 304 PHE 304 294 294 PHE PHE A . n 
A 1 305 ASP 305 295 295 ASP ASP A . n 
A 1 306 VAL 306 296 296 VAL VAL A . n 
A 1 307 VAL 307 297 297 VAL VAL A . n 
A 1 308 ARG 308 298 298 ARG ARG A . n 
A 1 309 GLN 309 299 299 GLN GLN A . n 
A 1 310 CYS 310 300 300 CYS CYS A . n 
A 1 311 SER 311 301 301 SER SER A . n 
A 1 312 GLY 312 302 302 GLY GLY A . n 
A 1 313 VAL 313 303 303 VAL VAL A . n 
A 1 314 THR 314 304 304 THR THR A . n 
A 1 315 PHE 315 305 305 PHE PHE A . n 
A 1 316 GLN 316 306 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1D8T 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1D8T 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1D8T 1   401 310 A1D8T UNL A . 
C 3 HOH   1   501 113 HOH   HOH A . 
C 3 HOH   2   502 302 HOH   HOH A . 
C 3 HOH   3   503 382 HOH   HOH A . 
C 3 HOH   4   504 159 HOH   HOH A . 
C 3 HOH   5   505 14  HOH   HOH A . 
C 3 HOH   6   506 247 HOH   HOH A . 
C 3 HOH   7   507 43  HOH   HOH A . 
C 3 HOH   8   508 233 HOH   HOH A . 
C 3 HOH   9   509 117 HOH   HOH A . 
C 3 HOH   10  510 124 HOH   HOH A . 
C 3 HOH   11  511 375 HOH   HOH A . 
C 3 HOH   12  512 288 HOH   HOH A . 
C 3 HOH   13  513 381 HOH   HOH A . 
C 3 HOH   14  514 128 HOH   HOH A . 
C 3 HOH   15  515 220 HOH   HOH A . 
C 3 HOH   16  516 81  HOH   HOH A . 
C 3 HOH   17  517 85  HOH   HOH A . 
C 3 HOH   18  518 115 HOH   HOH A . 
C 3 HOH   19  519 258 HOH   HOH A . 
C 3 HOH   20  520 29  HOH   HOH A . 
C 3 HOH   21  521 289 HOH   HOH A . 
C 3 HOH   22  522 141 HOH   HOH A . 
C 3 HOH   23  523 92  HOH   HOH A . 
C 3 HOH   24  524 261 HOH   HOH A . 
C 3 HOH   25  525 178 HOH   HOH A . 
C 3 HOH   26  526 242 HOH   HOH A . 
C 3 HOH   27  527 219 HOH   HOH A . 
C 3 HOH   28  528 24  HOH   HOH A . 
C 3 HOH   29  529 192 HOH   HOH A . 
C 3 HOH   30  530 173 HOH   HOH A . 
C 3 HOH   31  531 11  HOH   HOH A . 
C 3 HOH   32  532 252 HOH   HOH A . 
C 3 HOH   33  533 213 HOH   HOH A . 
C 3 HOH   34  534 282 HOH   HOH A . 
C 3 HOH   35  535 217 HOH   HOH A . 
C 3 HOH   36  536 303 HOH   HOH A . 
C 3 HOH   37  537 276 HOH   HOH A . 
C 3 HOH   38  538 351 HOH   HOH A . 
C 3 HOH   39  539 106 HOH   HOH A . 
C 3 HOH   40  540 196 HOH   HOH A . 
C 3 HOH   41  541 372 HOH   HOH A . 
C 3 HOH   42  542 63  HOH   HOH A . 
C 3 HOH   43  543 2   HOH   HOH A . 
C 3 HOH   44  544 69  HOH   HOH A . 
C 3 HOH   45  545 245 HOH   HOH A . 
C 3 HOH   46  546 146 HOH   HOH A . 
C 3 HOH   47  547 374 HOH   HOH A . 
C 3 HOH   48  548 290 HOH   HOH A . 
C 3 HOH   49  549 283 HOH   HOH A . 
C 3 HOH   50  550 73  HOH   HOH A . 
C 3 HOH   51  551 256 HOH   HOH A . 
C 3 HOH   52  552 76  HOH   HOH A . 
C 3 HOH   53  553 201 HOH   HOH A . 
C 3 HOH   54  554 279 HOH   HOH A . 
C 3 HOH   55  555 305 HOH   HOH A . 
C 3 HOH   56  556 376 HOH   HOH A . 
C 3 HOH   57  557 227 HOH   HOH A . 
C 3 HOH   58  558 222 HOH   HOH A . 
C 3 HOH   59  559 40  HOH   HOH A . 
C 3 HOH   60  560 164 HOH   HOH A . 
C 3 HOH   61  561 80  HOH   HOH A . 
C 3 HOH   62  562 370 HOH   HOH A . 
C 3 HOH   63  563 264 HOH   HOH A . 
C 3 HOH   64  564 91  HOH   HOH A . 
C 3 HOH   65  565 248 HOH   HOH A . 
C 3 HOH   66  566 396 HOH   HOH A . 
C 3 HOH   67  567 265 HOH   HOH A . 
C 3 HOH   68  568 41  HOH   HOH A . 
C 3 HOH   69  569 26  HOH   HOH A . 
C 3 HOH   70  570 190 HOH   HOH A . 
C 3 HOH   71  571 327 HOH   HOH A . 
C 3 HOH   72  572 134 HOH   HOH A . 
C 3 HOH   73  573 65  HOH   HOH A . 
C 3 HOH   74  574 161 HOH   HOH A . 
C 3 HOH   75  575 5   HOH   HOH A . 
C 3 HOH   76  576 74  HOH   HOH A . 
C 3 HOH   77  577 163 HOH   HOH A . 
C 3 HOH   78  578 157 HOH   HOH A . 
C 3 HOH   79  579 160 HOH   HOH A . 
C 3 HOH   80  580 105 HOH   HOH A . 
C 3 HOH   81  581 114 HOH   HOH A . 
C 3 HOH   82  582 151 HOH   HOH A . 
C 3 HOH   83  583 149 HOH   HOH A . 
C 3 HOH   84  584 175 HOH   HOH A . 
C 3 HOH   85  585 127 HOH   HOH A . 
C 3 HOH   86  586 78  HOH   HOH A . 
C 3 HOH   87  587 150 HOH   HOH A . 
C 3 HOH   88  588 395 HOH   HOH A . 
C 3 HOH   89  589 262 HOH   HOH A . 
C 3 HOH   90  590 122 HOH   HOH A . 
C 3 HOH   91  591 154 HOH   HOH A . 
C 3 HOH   92  592 189 HOH   HOH A . 
C 3 HOH   93  593 199 HOH   HOH A . 
C 3 HOH   94  594 235 HOH   HOH A . 
C 3 HOH   95  595 55  HOH   HOH A . 
C 3 HOH   96  596 138 HOH   HOH A . 
C 3 HOH   97  597 67  HOH   HOH A . 
C 3 HOH   98  598 7   HOH   HOH A . 
C 3 HOH   99  599 236 HOH   HOH A . 
C 3 HOH   100 600 140 HOH   HOH A . 
C 3 HOH   101 601 96  HOH   HOH A . 
C 3 HOH   102 602 19  HOH   HOH A . 
C 3 HOH   103 603 95  HOH   HOH A . 
C 3 HOH   104 604 30  HOH   HOH A . 
C 3 HOH   105 605 6   HOH   HOH A . 
C 3 HOH   106 606 123 HOH   HOH A . 
C 3 HOH   107 607 270 HOH   HOH A . 
C 3 HOH   108 608 237 HOH   HOH A . 
C 3 HOH   109 609 142 HOH   HOH A . 
C 3 HOH   110 610 205 HOH   HOH A . 
C 3 HOH   111 611 156 HOH   HOH A . 
C 3 HOH   112 612 181 HOH   HOH A . 
C 3 HOH   113 613 215 HOH   HOH A . 
C 3 HOH   114 614 212 HOH   HOH A . 
C 3 HOH   115 615 232 HOH   HOH A . 
C 3 HOH   116 616 285 HOH   HOH A . 
C 3 HOH   117 617 179 HOH   HOH A . 
C 3 HOH   118 618 216 HOH   HOH A . 
C 3 HOH   119 619 137 HOH   HOH A . 
C 3 HOH   120 620 295 HOH   HOH A . 
C 3 HOH   121 621 52  HOH   HOH A . 
C 3 HOH   122 622 266 HOH   HOH A . 
C 3 HOH   123 623 31  HOH   HOH A . 
C 3 HOH   124 624 281 HOH   HOH A . 
C 3 HOH   125 625 278 HOH   HOH A . 
C 3 HOH   126 626 298 HOH   HOH A . 
C 3 HOH   127 627 21  HOH   HOH A . 
C 3 HOH   128 628 343 HOH   HOH A . 
C 3 HOH   129 629 25  HOH   HOH A . 
C 3 HOH   130 630 104 HOH   HOH A . 
C 3 HOH   131 631 244 HOH   HOH A . 
C 3 HOH   132 632 249 HOH   HOH A . 
C 3 HOH   133 633 378 HOH   HOH A . 
C 3 HOH   134 634 18  HOH   HOH A . 
C 3 HOH   135 635 94  HOH   HOH A . 
C 3 HOH   136 636 153 HOH   HOH A . 
C 3 HOH   137 637 57  HOH   HOH A . 
C 3 HOH   138 638 10  HOH   HOH A . 
C 3 HOH   139 639 72  HOH   HOH A . 
C 3 HOH   140 640 263 HOH   HOH A . 
C 3 HOH   141 641 206 HOH   HOH A . 
C 3 HOH   142 642 32  HOH   HOH A . 
C 3 HOH   143 643 47  HOH   HOH A . 
C 3 HOH   144 644 68  HOH   HOH A . 
C 3 HOH   145 645 139 HOH   HOH A . 
C 3 HOH   146 646 16  HOH   HOH A . 
C 3 HOH   147 647 203 HOH   HOH A . 
C 3 HOH   148 648 167 HOH   HOH A . 
C 3 HOH   149 649 228 HOH   HOH A . 
C 3 HOH   150 650 147 HOH   HOH A . 
C 3 HOH   151 651 391 HOH   HOH A . 
C 3 HOH   152 652 218 HOH   HOH A . 
C 3 HOH   153 653 280 HOH   HOH A . 
C 3 HOH   154 654 209 HOH   HOH A . 
C 3 HOH   155 655 148 HOH   HOH A . 
C 3 HOH   156 656 125 HOH   HOH A . 
C 3 HOH   157 657 61  HOH   HOH A . 
C 3 HOH   158 658 64  HOH   HOH A . 
C 3 HOH   159 659 89  HOH   HOH A . 
C 3 HOH   160 660 158 HOH   HOH A . 
C 3 HOH   161 661 28  HOH   HOH A . 
C 3 HOH   162 662 42  HOH   HOH A . 
C 3 HOH   163 663 116 HOH   HOH A . 
C 3 HOH   164 664 129 HOH   HOH A . 
C 3 HOH   165 665 75  HOH   HOH A . 
C 3 HOH   166 666 77  HOH   HOH A . 
C 3 HOH   167 667 45  HOH   HOH A . 
C 3 HOH   168 668 348 HOH   HOH A . 
C 3 HOH   169 669 229 HOH   HOH A . 
C 3 HOH   170 670 27  HOH   HOH A . 
C 3 HOH   171 671 176 HOH   HOH A . 
C 3 HOH   172 672 234 HOH   HOH A . 
C 3 HOH   173 673 15  HOH   HOH A . 
C 3 HOH   174 674 300 HOH   HOH A . 
C 3 HOH   175 675 385 HOH   HOH A . 
C 3 HOH   176 676 101 HOH   HOH A . 
C 3 HOH   177 677 231 HOH   HOH A . 
C 3 HOH   178 678 3   HOH   HOH A . 
C 3 HOH   179 679 37  HOH   HOH A . 
C 3 HOH   180 680 171 HOH   HOH A . 
C 3 HOH   181 681 143 HOH   HOH A . 
C 3 HOH   182 682 304 HOH   HOH A . 
C 3 HOH   183 683 257 HOH   HOH A . 
C 3 HOH   184 684 112 HOH   HOH A . 
C 3 HOH   185 685 22  HOH   HOH A . 
C 3 HOH   186 686 20  HOH   HOH A . 
C 3 HOH   187 687 328 HOH   HOH A . 
C 3 HOH   188 688 214 HOH   HOH A . 
C 3 HOH   189 689 4   HOH   HOH A . 
C 3 HOH   190 690 111 HOH   HOH A . 
C 3 HOH   191 691 13  HOH   HOH A . 
C 3 HOH   192 692 169 HOH   HOH A . 
C 3 HOH   193 693 98  HOH   HOH A . 
C 3 HOH   194 694 50  HOH   HOH A . 
C 3 HOH   195 695 135 HOH   HOH A . 
C 3 HOH   196 696 251 HOH   HOH A . 
C 3 HOH   197 697 392 HOH   HOH A . 
C 3 HOH   198 698 8   HOH   HOH A . 
C 3 HOH   199 699 191 HOH   HOH A . 
C 3 HOH   200 700 180 HOH   HOH A . 
C 3 HOH   201 701 297 HOH   HOH A . 
C 3 HOH   202 702 38  HOH   HOH A . 
C 3 HOH   203 703 340 HOH   HOH A . 
C 3 HOH   204 704 287 HOH   HOH A . 
C 3 HOH   205 705 225 HOH   HOH A . 
C 3 HOH   206 706 168 HOH   HOH A . 
C 3 HOH   207 707 53  HOH   HOH A . 
C 3 HOH   208 708 267 HOH   HOH A . 
C 3 HOH   209 709 70  HOH   HOH A . 
C 3 HOH   210 710 155 HOH   HOH A . 
C 3 HOH   211 711 250 HOH   HOH A . 
C 3 HOH   212 712 260 HOH   HOH A . 
C 3 HOH   213 713 271 HOH   HOH A . 
C 3 HOH   214 714 273 HOH   HOH A . 
C 3 HOH   215 715 239 HOH   HOH A . 
C 3 HOH   216 716 86  HOH   HOH A . 
C 3 HOH   217 717 44  HOH   HOH A . 
C 3 HOH   218 718 277 HOH   HOH A . 
C 3 HOH   219 719 230 HOH   HOH A . 
C 3 HOH   220 720 145 HOH   HOH A . 
C 3 HOH   221 721 17  HOH   HOH A . 
C 3 HOH   222 722 241 HOH   HOH A . 
C 3 HOH   223 723 221 HOH   HOH A . 
C 3 HOH   224 724 93  HOH   HOH A . 
C 3 HOH   225 725 99  HOH   HOH A . 
C 3 HOH   226 726 34  HOH   HOH A . 
C 3 HOH   227 727 210 HOH   HOH A . 
C 3 HOH   228 728 253 HOH   HOH A . 
C 3 HOH   229 729 294 HOH   HOH A . 
C 3 HOH   230 730 23  HOH   HOH A . 
C 3 HOH   231 731 240 HOH   HOH A . 
C 3 HOH   232 732 177 HOH   HOH A . 
C 3 HOH   233 733 136 HOH   HOH A . 
C 3 HOH   234 734 35  HOH   HOH A . 
C 3 HOH   235 735 224 HOH   HOH A . 
C 3 HOH   236 736 223 HOH   HOH A . 
C 3 HOH   237 737 133 HOH   HOH A . 
C 3 HOH   238 738 198 HOH   HOH A . 
C 3 HOH   239 739 62  HOH   HOH A . 
C 3 HOH   240 740 383 HOH   HOH A . 
C 3 HOH   241 741 284 HOH   HOH A . 
C 3 HOH   242 742 56  HOH   HOH A . 
C 3 HOH   243 743 46  HOH   HOH A . 
C 3 HOH   244 744 269 HOH   HOH A . 
C 3 HOH   245 745 131 HOH   HOH A . 
C 3 HOH   246 746 187 HOH   HOH A . 
C 3 HOH   247 747 259 HOH   HOH A . 
C 3 HOH   248 748 126 HOH   HOH A . 
C 3 HOH   249 749 211 HOH   HOH A . 
C 3 HOH   250 750 33  HOH   HOH A . 
C 3 HOH   251 751 12  HOH   HOH A . 
C 3 HOH   252 752 79  HOH   HOH A . 
C 3 HOH   253 753 197 HOH   HOH A . 
C 3 HOH   254 754 226 HOH   HOH A . 
C 3 HOH   255 755 311 HOH   HOH A . 
C 3 HOH   256 756 49  HOH   HOH A . 
C 3 HOH   257 757 59  HOH   HOH A . 
C 3 HOH   258 758 384 HOH   HOH A . 
C 3 HOH   259 759 316 HOH   HOH A . 
C 3 HOH   260 760 84  HOH   HOH A . 
C 3 HOH   261 761 286 HOH   HOH A . 
C 3 HOH   262 762 60  HOH   HOH A . 
C 3 HOH   263 763 202 HOH   HOH A . 
C 3 HOH   264 764 272 HOH   HOH A . 
C 3 HOH   265 765 292 HOH   HOH A . 
C 3 HOH   266 766 200 HOH   HOH A . 
C 3 HOH   267 767 254 HOH   HOH A . 
C 3 HOH   268 768 386 HOH   HOH A . 
C 3 HOH   269 769 275 HOH   HOH A . 
C 3 HOH   270 770 174 HOH   HOH A . 
C 3 HOH   271 771 325 HOH   HOH A . 
C 3 HOH   272 772 120 HOH   HOH A . 
C 3 HOH   273 773 130 HOH   HOH A . 
C 3 HOH   274 774 339 HOH   HOH A . 
C 3 HOH   275 775 119 HOH   HOH A . 
C 3 HOH   276 776 373 HOH   HOH A . 
C 3 HOH   277 777 1   HOH   HOH A . 
C 3 HOH   278 778 332 HOH   HOH A . 
C 3 HOH   279 779 97  HOH   HOH A . 
C 3 HOH   280 780 188 HOH   HOH A . 
C 3 HOH   281 781 357 HOH   HOH A . 
C 3 HOH   282 782 312 HOH   HOH A . 
C 3 HOH   283 783 132 HOH   HOH A . 
C 3 HOH   284 784 324 HOH   HOH A . 
C 3 HOH   285 785 36  HOH   HOH A . 
C 3 HOH   286 786 51  HOH   HOH A . 
C 3 HOH   287 787 83  HOH   HOH A . 
C 3 HOH   288 788 336 HOH   HOH A . 
C 3 HOH   289 789 301 HOH   HOH A . 
C 3 HOH   290 790 326 HOH   HOH A . 
C 3 HOH   291 791 320 HOH   HOH A . 
C 3 HOH   292 792 165 HOH   HOH A . 
C 3 HOH   293 793 317 HOH   HOH A . 
C 3 HOH   294 794 313 HOH   HOH A . 
C 3 HOH   295 795 334 HOH   HOH A . 
C 3 HOH   296 796 144 HOH   HOH A . 
C 3 HOH   297 797 204 HOH   HOH A . 
C 3 HOH   298 798 90  HOH   HOH A . 
C 3 HOH   299 799 314 HOH   HOH A . 
C 3 HOH   300 800 337 HOH   HOH A . 
C 3 HOH   301 801 310 HOH   HOH A . 
C 3 HOH   302 802 360 HOH   HOH A . 
C 3 HOH   303 803 318 HOH   HOH A . 
C 3 HOH   304 804 243 HOH   HOH A . 
C 3 HOH   305 805 331 HOH   HOH A . 
C 3 HOH   306 806 103 HOH   HOH A . 
C 3 HOH   307 807 394 HOH   HOH A . 
C 3 HOH   308 808 118 HOH   HOH A . 
C 3 HOH   309 809 315 HOH   HOH A . 
C 3 HOH   310 810 183 HOH   HOH A . 
C 3 HOH   311 811 330 HOH   HOH A . 
C 3 HOH   312 812 322 HOH   HOH A . 
C 3 HOH   313 813 238 HOH   HOH A . 
C 3 HOH   314 814 291 HOH   HOH A . 
C 3 HOH   315 815 323 HOH   HOH A . 
C 3 HOH   316 816 321 HOH   HOH A . 
C 3 HOH   317 817 329 HOH   HOH A . 
C 3 HOH   318 818 172 HOH   HOH A . 
C 3 HOH   319 819 170 HOH   HOH A . 
C 3 HOH   320 820 371 HOH   HOH A . 
C 3 HOH   321 821 335 HOH   HOH A . 
C 3 HOH   322 822 309 HOH   HOH A . 
C 3 HOH   323 823 195 HOH   HOH A . 
C 3 HOH   324 824 100 HOH   HOH A . 
C 3 HOH   325 825 308 HOH   HOH A . 
C 3 HOH   326 826 367 HOH   HOH A . 
C 3 HOH   327 827 87  HOH   HOH A . 
C 3 HOH   328 828 299 HOH   HOH A . 
C 3 HOH   329 829 359 HOH   HOH A . 
C 3 HOH   330 830 319 HOH   HOH A . 
C 3 HOH   331 831 390 HOH   HOH A . 
C 3 HOH   332 832 185 HOH   HOH A . 
C 3 HOH   333 833 306 HOH   HOH A . 
C 3 HOH   334 834 186 HOH   HOH A . 
C 3 HOH   335 835 54  HOH   HOH A . 
C 3 HOH   336 836 365 HOH   HOH A . 
C 3 HOH   337 837 341 HOH   HOH A . 
C 3 HOH   338 838 208 HOH   HOH A . 
C 3 HOH   339 839 108 HOH   HOH A . 
C 3 HOH   340 840 307 HOH   HOH A . 
C 3 HOH   341 841 207 HOH   HOH A . 
C 3 HOH   342 842 48  HOH   HOH A . 
C 3 HOH   343 843 58  HOH   HOH A . 
C 3 HOH   344 844 39  HOH   HOH A . 
C 3 HOH   345 845 193 HOH   HOH A . 
C 3 HOH   346 846 88  HOH   HOH A . 
C 3 HOH   347 847 380 HOH   HOH A . 
C 3 HOH   348 848 274 HOH   HOH A . 
C 3 HOH   349 849 152 HOH   HOH A . 
C 3 HOH   350 850 268 HOH   HOH A . 
C 3 HOH   351 851 345 HOH   HOH A . 
C 3 HOH   352 852 333 HOH   HOH A . 
C 3 HOH   353 853 364 HOH   HOH A . 
C 3 HOH   354 854 361 HOH   HOH A . 
C 3 HOH   355 855 66  HOH   HOH A . 
C 3 HOH   356 856 349 HOH   HOH A . 
C 3 HOH   357 857 102 HOH   HOH A . 
C 3 HOH   358 858 342 HOH   HOH A . 
C 3 HOH   359 859 107 HOH   HOH A . 
C 3 HOH   360 860 377 HOH   HOH A . 
C 3 HOH   361 861 389 HOH   HOH A . 
C 3 HOH   362 862 293 HOH   HOH A . 
C 3 HOH   363 863 344 HOH   HOH A . 
C 3 HOH   364 864 71  HOH   HOH A . 
C 3 HOH   365 865 363 HOH   HOH A . 
C 3 HOH   366 866 379 HOH   HOH A . 
C 3 HOH   367 867 162 HOH   HOH A . 
C 3 HOH   368 868 355 HOH   HOH A . 
C 3 HOH   369 869 347 HOH   HOH A . 
C 3 HOH   370 870 246 HOH   HOH A . 
C 3 HOH   371 871 184 HOH   HOH A . 
C 3 HOH   372 872 9   HOH   HOH A . 
C 3 HOH   373 873 353 HOH   HOH A . 
C 3 HOH   374 874 110 HOH   HOH A . 
C 3 HOH   375 875 296 HOH   HOH A . 
C 3 HOH   376 876 346 HOH   HOH A . 
C 3 HOH   377 877 388 HOH   HOH A . 
C 3 HOH   378 878 338 HOH   HOH A . 
C 3 HOH   379 879 362 HOH   HOH A . 
C 3 HOH   380 880 109 HOH   HOH A . 
C 3 HOH   381 881 356 HOH   HOH A . 
C 3 HOH   382 882 354 HOH   HOH A . 
C 3 HOH   383 883 194 HOH   HOH A . 
C 3 HOH   384 884 166 HOH   HOH A . 
C 3 HOH   385 885 121 HOH   HOH A . 
C 3 HOH   386 886 182 HOH   HOH A . 
C 3 HOH   387 887 352 HOH   HOH A . 
C 3 HOH   388 888 255 HOH   HOH A . 
C 3 HOH   389 889 82  HOH   HOH A . 
C 3 HOH   390 890 350 HOH   HOH A . 
C 3 HOH   391 891 393 HOH   HOH A . 
C 3 HOH   392 892 366 HOH   HOH A . 
C 3 HOH   393 893 369 HOH   HOH A . 
C 3 HOH   394 894 387 HOH   HOH A . 
C 3 HOH   395 895 358 HOH   HOH A . 
C 3 HOH   396 896 368 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       ? ? ? ? ? ? ? ? ? ? ? REFMAC    ? ? ? 5.8.0267 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? iMOSFLM   ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? pointless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   103.51 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZQ8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     114.390 
_cell.length_a_esd                 ? 
_cell.length_b                     52.950 
_cell.length_b_esd                 ? 
_cell.length_c                     45.420 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8ZQ8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZQ8 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             1.93 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          36.11 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M LiCl, 0.1 M Bis-Tris pH 6.5, 13%(w/v) polyethylene glycol 8000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             'nitrogen stream' 
_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                      'CCD MSC PAD200sk detector' 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         RIGAKU 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-11-08 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.54187 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        RIGAKU 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.54187 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ZQ8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.77 
_reflns.d_resolution_low                               26.50 
_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                                     23834 
_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                           91.63 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.89 
_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                                   0.995 
_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                                    1.77 
_reflns_shell.d_res_low                                     1.833 
_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                             2152 
_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                                  0.875 
_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]                            0.55 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.15 
_refine.aniso_B[2][2]                            0.00 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.56 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               15.926 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.960 
_refine.correlation_coeff_Fo_to_Fc_free          0.930 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8ZQ8 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.77 
_refine.ls_d_res_low                             26.50 
_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                     22662 
_refine.ls_number_reflns_R_free                  1190 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    91.60 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16960 
_refine.ls_R_factor_R_free                       0.22256 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16692 
_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                    MASK 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.153 
_refine.pdbx_overall_ESU_R_Free                  0.145 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             2.912 
_refine.overall_SU_ML                            0.091 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.77 
_refine_hist.d_res_low                        26.50 
_refine_hist.number_atoms_solvent             396 
_refine_hist.number_atoms_total               2796 
_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        2358 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         42 
_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' ? 0.010  0.013  2475 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  2286 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.648  1.645  3376 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.439  1.577  5254 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.441  5.000  308  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 33.030 22.698 126  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.177 15.000 389  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 10.507 15.000 11   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.096  0.200  325  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  2861 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  589  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.290  1.461  1229 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.287  1.459  1228 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.022  2.184  1538 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.023  2.187  1539 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.963  1.688  1246 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.963  1.688  1247 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.989  2.439  1836 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.125  19.341 2871 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 4.881  18.469 2756 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.77 
_refine_ls_shell.d_res_low                        1.813 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             94 
_refine_ls_shell.number_reflns_R_work             1480 
_refine_ls_shell.percent_reflns_obs               81.72 
_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                  0.230 
_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                  0.309 
# 
_struct.entry_id                     8ZQ8 
_struct.title                        'SARS-Cov-2 3CL protease in complex with macrocyclic inhibitor CG-1039' 
_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        8ZQ8 
_struct_keywords.text            'the main protease, 3C-like protease, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_struct_ref.pdbx_align_begin           3264 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8ZQ8 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 11 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 316 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P0DTD1 
_struct_ref_seq.db_align_beg                  3264 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  3569 
_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       306 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8ZQ8 GLY A 1  ? UNP P0DTD1 ? ? linker -9 1  
1 8ZQ8 PRO A 2  ? UNP P0DTD1 ? ? linker -8 2  
1 8ZQ8 LEU A 3  ? UNP P0DTD1 ? ? linker -7 3  
1 8ZQ8 GLY A 4  ? UNP P0DTD1 ? ? linker -6 4  
1 8ZQ8 SER A 5  ? UNP P0DTD1 ? ? linker -5 5  
1 8ZQ8 SER A 6  ? UNP P0DTD1 ? ? linker -4 6  
1 8ZQ8 ALA A 7  ? UNP P0DTD1 ? ? linker -3 7  
1 8ZQ8 VAL A 8  ? UNP P0DTD1 ? ? linker -2 8  
1 8ZQ8 LEU A 9  ? UNP P0DTD1 ? ? linker -1 9  
1 8ZQ8 GLN A 10 ? UNP P0DTD1 ? ? linker 0  10 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3060  ? 
1 MORE         -16   ? 
1 'SSA (A^2)'  25030 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
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_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 
# 
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 SER A 20  ? GLY A 25  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 51  ? CYS A 54  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 GLU A 57  ? ASN A 61  ? GLU A 47  ASN A 51  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 63  ? ARG A 70  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P5  AA5 LYS A 71  ? HIS A 74  ? LYS A 61  HIS A 64  5 ? 4  
HELX_P HELX_P6  AA6 ILE A 210 ? ASN A 224 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P7  AA7 THR A 236 ? TYR A 247 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P8  AA8 THR A 253 ? LEU A 260 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P9  AA9 LEU A 260 ? GLY A 268 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P10 AB1 ALA A 270 ? GLY A 285 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P11 AB2 THR A 302 ? GLY A 312 ? THR A 292 GLY A 302 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        none 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            155 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           A1D8T 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C26 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             145 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            A1D8T 
_struct_conn.ptnr2_auth_seq_id             401 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               1.728 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      A1D8T 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      155 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       A1D8T 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        401 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       145 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C26 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        A1D8T 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
# 
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 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 83  ? LEU A 85  ? VAL A 73  LEU A 75  
AA1 2 PHE A 76  ? ALA A 80  ? PHE A 66  ALA A 70  
AA1 3 MET A 27  ? CYS A 32  ? MET A 17  CYS A 22  
AA1 4 THR A 35  ? LEU A 42  ? THR A 25  LEU A 32  
AA1 5 VAL A 45  ? PRO A 49  ? VAL A 35  PRO A 39  
AA1 6 VAL A 96  ? VAL A 101 ? VAL A 86  VAL A 91  
AA1 7 VAL A 87  ? GLN A 93  ? VAL A 77  GLN A 83  
AA2 1 TYR A 111 ? PHE A 113 ? TYR A 101 PHE A 103 
AA2 2 CYS A 166 ? LEU A 177 ? CYS A 156 LEU A 167 
AA2 3 VAL A 158 ? ASP A 163 ? VAL A 148 ASP A 153 
AA2 4 THR A 121 ? TYR A 128 ? THR A 111 TYR A 118 
AA2 5 SER A 131 ? ALA A 139 ? SER A 121 ALA A 129 
AA3 1 TYR A 111 ? PHE A 113 ? TYR A 101 PHE A 103 
AA3 2 CYS A 166 ? LEU A 177 ? CYS A 156 LEU A 167 
AA3 3 VAL A 181 ? THR A 185 ? VAL A 171 THR A 175 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU A 85  ? O LEU A 75  N VAL A 78  ? N VAL A 68  
AA1 2 3 O LEU A 77  ? O LEU A 67  N THR A 31  ? N THR A 21  
AA1 3 4 N VAL A 28  ? N VAL A 18  O GLY A 39  ? O GLY A 29  
AA1 4 5 N LEU A 40  ? N LEU A 30  O TYR A 47  ? O TYR A 37  
AA1 5 6 N VAL A 46  ? N VAL A 36  O LEU A 99  ? O LEU A 89  
AA1 6 7 O LYS A 98  ? O LYS A 88  N SER A 91  ? N SER A 81  
AA2 1 2 N LYS A 112 ? N LYS A 102 O PHE A 169 ? O PHE A 159 
AA2 2 3 O SER A 168 ? O SER A 158 N ASN A 161 ? N ASN A 151 
AA2 3 4 O PHE A 160 ? O PHE A 150 N SER A 123 ? N SER A 113 
AA2 4 5 N VAL A 124 ? N VAL A 114 O TYR A 136 ? O TYR A 126 
AA3 1 2 N LYS A 112 ? N LYS A 102 O PHE A 169 ? O PHE A 159 
AA3 2 3 N LEU A 177 ? N LEU A 167 O VAL A 181 ? O VAL A 171 
# 
_pdbx_entry_details.entry_id                   8ZQ8 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 ASP A 33  ? ? 53.03   -133.71 
2 1 ASN A 51  ? ? -164.95 60.50   
3 1 ASN A 84  ? ? 54.88   -120.25 
4 1 TYR A 154 ? ? 44.40   -90.17  
5 1 THR A 169 ? ? 90.75   1.56    
# 
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 749 ? C HOH . 
2 1 A HOH 777 ? C HOH . 
3 1 A HOH 887 ? C HOH . 
# 
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 895 ? 6.07 . 
2 1 O ? A HOH 896 ? 6.31 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY -9  ? A GLY 1   
2  1 Y 1 A PRO -8  ? A PRO 2   
3  1 Y 1 A LEU -7  ? A LEU 3   
4  1 Y 1 A GLY -6  ? A GLY 4   
5  1 Y 1 A SER -5  ? A SER 5   
6  1 Y 1 A SER -4  ? A SER 6   
7  1 Y 1 A ALA -3  ? A ALA 7   
8  1 Y 1 A VAL -2  ? A VAL 8   
9  1 Y 1 A LEU -1  ? A LEU 9   
10 1 Y 1 A GLN 0   ? A GLN 10  
11 1 Y 1 A GLN 306 ? A GLN 316 
# 
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 
A1D8T C7   C N N 1   
A1D8T C4   C Y N 2   
A1D8T C2   C Y N 3   
A1D8T C6   C Y N 4   
A1D8T C8   C N N 5   
A1D8T C3   C Y N 6   
A1D8T C1   C Y N 7   
A1D8T C5   C Y N 8   
A1D8T O1   O N N 9   
A1D8T O2   O N N 10  
A1D8T N1   N N N 11  
A1D8T C9   C N S 12  
A1D8T C10  C N N 13  
A1D8T C11  C N N 14  
A1D8T O3   O N N 15  
A1D8T C16  C N N 16  
A1D8T C17  C N N 17  
A1D8T C18  C N N 18  
A1D8T N3   N N N 19  
A1D8T N2   N N N 20  
A1D8T C15  C N N 21  
A1D8T C12  C N S 22  
A1D8T C13  C N R 23  
A1D8T C14  C N S 24  
A1D8T C28  C N N 25  
A1D8T C29  C N N 26  
A1D8T C30  C N N 27  
A1D8T C27  C N N 28  
A1D8T O5   O N N 29  
A1D8T C19  C N N 30  
A1D8T O4   O N N 31  
A1D8T C20  C N S 32  
A1D8T N4   N N N 33  
A1D8T C21  C N N 34  
A1D8T C22  C N S 35  
A1D8T C23  C N N 36  
A1D8T C24  C N N 37  
A1D8T C25  C N S 38  
A1D8T C26  C N N 39  
A1D8T N5   N N N 40  
A1D8T O6   O N N 41  
A1D8T N6   N N N 42  
A1D8T H6   H N N 43  
A1D8T H7   H N N 44  
A1D8T H2   H N N 45  
A1D8T H5   H N N 46  
A1D8T H3   H N N 47  
A1D8T H1   H N N 48  
A1D8T H4   H N N 49  
A1D8T H8   H N N 50  
A1D8T H9   H N N 51  
A1D8T H15  H N N 52  
A1D8T H16  H N N 53  
A1D8T H17  H N N 54  
A1D8T H18  H N N 55  
A1D8T H19  H N N 56  
A1D8T H20  H N N 57  
A1D8T H21  H N N 58  
A1D8T H22  H N N 59  
A1D8T H23  H N N 60  
A1D8T H13  H N N 61  
A1D8T H14  H N N 62  
A1D8T H10  H N N 63  
A1D8T H11  H N N 64  
A1D8T H12  H N N 65  
A1D8T H35  H N N 66  
A1D8T H36  H N N 67  
A1D8T H37  H N N 68  
A1D8T H38  H N N 69  
A1D8T H39  H N N 70  
A1D8T H40  H N N 71  
A1D8T H24  H N N 72  
A1D8T H25  H N N 73  
A1D8T H26  H N N 74  
A1D8T H27  H N N 75  
A1D8T H28  H N N 76  
A1D8T H29  H N N 77  
A1D8T H30  H N N 78  
A1D8T H31  H N N 79  
A1D8T H32  H N N 80  
A1D8T H33  H N N 81  
A1D8T H34  H N N 82  
ALA   N    N N N 83  
ALA   CA   C N S 84  
ALA   C    C N N 85  
ALA   O    O N N 86  
ALA   CB   C N N 87  
ALA   OXT  O N N 88  
ALA   H    H N N 89  
ALA   H2   H N N 90  
ALA   HA   H N N 91  
ALA   HB1  H N N 92  
ALA   HB2  H N N 93  
ALA   HB3  H N N 94  
ALA   HXT  H N N 95  
ARG   N    N N N 96  
ARG   CA   C N S 97  
ARG   C    C N N 98  
ARG   O    O N N 99  
ARG   CB   C N N 100 
ARG   CG   C N N 101 
ARG   CD   C N N 102 
ARG   NE   N N N 103 
ARG   CZ   C N N 104 
ARG   NH1  N N N 105 
ARG   NH2  N N N 106 
ARG   OXT  O N N 107 
ARG   H    H N N 108 
ARG   H2   H N N 109 
ARG   HA   H N N 110 
ARG   HB2  H N N 111 
ARG   HB3  H N N 112 
ARG   HG2  H N N 113 
ARG   HG3  H N N 114 
ARG   HD2  H N N 115 
ARG   HD3  H N N 116 
ARG   HE   H N N 117 
ARG   HH11 H N N 118 
ARG   HH12 H N N 119 
ARG   HH21 H N N 120 
ARG   HH22 H N N 121 
ARG   HXT  H N N 122 
ASN   N    N N N 123 
ASN   CA   C N S 124 
ASN   C    C N N 125 
ASN   O    O N N 126 
ASN   CB   C N N 127 
ASN   CG   C N N 128 
ASN   OD1  O N N 129 
ASN   ND2  N N N 130 
ASN   OXT  O N N 131 
ASN   H    H N N 132 
ASN   H2   H N N 133 
ASN   HA   H N N 134 
ASN   HB2  H N N 135 
ASN   HB3  H N N 136 
ASN   HD21 H N N 137 
ASN   HD22 H N N 138 
ASN   HXT  H N N 139 
ASP   N    N N N 140 
ASP   CA   C N S 141 
ASP   C    C N N 142 
ASP   O    O N N 143 
ASP   CB   C N N 144 
ASP   CG   C N N 145 
ASP   OD1  O N N 146 
ASP   OD2  O N N 147 
ASP   OXT  O N N 148 
ASP   H    H N N 149 
ASP   H2   H N N 150 
ASP   HA   H N N 151 
ASP   HB2  H N N 152 
ASP   HB3  H N N 153 
ASP   HD2  H N N 154 
ASP   HXT  H N N 155 
CYS   N    N N N 156 
CYS   CA   C N R 157 
CYS   C    C N N 158 
CYS   O    O N N 159 
CYS   CB   C N N 160 
CYS   SG   S N N 161 
CYS   OXT  O N N 162 
CYS   H    H N N 163 
CYS   H2   H N N 164 
CYS   HA   H N N 165 
CYS   HB2  H N N 166 
CYS   HB3  H N N 167 
CYS   HG   H N N 168 
CYS   HXT  H N N 169 
GLN   N    N N N 170 
GLN   CA   C N S 171 
GLN   C    C N N 172 
GLN   O    O N N 173 
GLN   CB   C N N 174 
GLN   CG   C N N 175 
GLN   CD   C N N 176 
GLN   OE1  O N N 177 
GLN   NE2  N N N 178 
GLN   OXT  O N N 179 
GLN   H    H N N 180 
GLN   H2   H N N 181 
GLN   HA   H N N 182 
GLN   HB2  H N N 183 
GLN   HB3  H N N 184 
GLN   HG2  H N N 185 
GLN   HG3  H N N 186 
GLN   HE21 H N N 187 
GLN   HE22 H N N 188 
GLN   HXT  H N N 189 
GLU   N    N N N 190 
GLU   CA   C N S 191 
GLU   C    C N N 192 
GLU   O    O N N 193 
GLU   CB   C N N 194 
GLU   CG   C N N 195 
GLU   CD   C N N 196 
GLU   OE1  O N N 197 
GLU   OE2  O N N 198 
GLU   OXT  O N N 199 
GLU   H    H N N 200 
GLU   H2   H N N 201 
GLU   HA   H N N 202 
GLU   HB2  H N N 203 
GLU   HB3  H N N 204 
GLU   HG2  H N N 205 
GLU   HG3  H N N 206 
GLU   HE2  H N N 207 
GLU   HXT  H N N 208 
GLY   N    N N N 209 
GLY   CA   C N N 210 
GLY   C    C N N 211 
GLY   O    O N N 212 
GLY   OXT  O N N 213 
GLY   H    H N N 214 
GLY   H2   H N N 215 
GLY   HA2  H N N 216 
GLY   HA3  H N N 217 
GLY   HXT  H N N 218 
HIS   N    N N N 219 
HIS   CA   C N S 220 
HIS   C    C N N 221 
HIS   O    O N N 222 
HIS   CB   C N N 223 
HIS   CG   C Y N 224 
HIS   ND1  N Y N 225 
HIS   CD2  C Y N 226 
HIS   CE1  C Y N 227 
HIS   NE2  N Y N 228 
HIS   OXT  O N N 229 
HIS   H    H N N 230 
HIS   H2   H N N 231 
HIS   HA   H N N 232 
HIS   HB2  H N N 233 
HIS   HB3  H N N 234 
HIS   HD1  H N N 235 
HIS   HD2  H N N 236 
HIS   HE1  H N N 237 
HIS   HE2  H N N 238 
HIS   HXT  H N N 239 
HOH   O    O N N 240 
HOH   H1   H N N 241 
HOH   H2   H N N 242 
ILE   N    N N N 243 
ILE   CA   C N S 244 
ILE   C    C N N 245 
ILE   O    O N N 246 
ILE   CB   C N S 247 
ILE   CG1  C N N 248 
ILE   CG2  C N N 249 
ILE   CD1  C N N 250 
ILE   OXT  O N N 251 
ILE   H    H N N 252 
ILE   H2   H N N 253 
ILE   HA   H N N 254 
ILE   HB   H N N 255 
ILE   HG12 H N N 256 
ILE   HG13 H N N 257 
ILE   HG21 H N N 258 
ILE   HG22 H N N 259 
ILE   HG23 H N N 260 
ILE   HD11 H N N 261 
ILE   HD12 H N N 262 
ILE   HD13 H N N 263 
ILE   HXT  H N N 264 
LEU   N    N N N 265 
LEU   CA   C N S 266 
LEU   C    C N N 267 
LEU   O    O N N 268 
LEU   CB   C N N 269 
LEU   CG   C N N 270 
LEU   CD1  C N N 271 
LEU   CD2  C N N 272 
LEU   OXT  O N N 273 
LEU   H    H N N 274 
LEU   H2   H N N 275 
LEU   HA   H N N 276 
LEU   HB2  H N N 277 
LEU   HB3  H N N 278 
LEU   HG   H N N 279 
LEU   HD11 H N N 280 
LEU   HD12 H N N 281 
LEU   HD13 H N N 282 
LEU   HD21 H N N 283 
LEU   HD22 H N N 284 
LEU   HD23 H N N 285 
LEU   HXT  H N N 286 
LYS   N    N N N 287 
LYS   CA   C N S 288 
LYS   C    C N N 289 
LYS   O    O N N 290 
LYS   CB   C N N 291 
LYS   CG   C N N 292 
LYS   CD   C N N 293 
LYS   CE   C N N 294 
LYS   NZ   N N N 295 
LYS   OXT  O N N 296 
LYS   H    H N N 297 
LYS   H2   H N N 298 
LYS   HA   H N N 299 
LYS   HB2  H N N 300 
LYS   HB3  H N N 301 
LYS   HG2  H N N 302 
LYS   HG3  H N N 303 
LYS   HD2  H N N 304 
LYS   HD3  H N N 305 
LYS   HE2  H N N 306 
LYS   HE3  H N N 307 
LYS   HZ1  H N N 308 
LYS   HZ2  H N N 309 
LYS   HZ3  H N N 310 
LYS   HXT  H N N 311 
MET   N    N N N 312 
MET   CA   C N S 313 
MET   C    C N N 314 
MET   O    O N N 315 
MET   CB   C N N 316 
MET   CG   C N N 317 
MET   SD   S N N 318 
MET   CE   C N N 319 
MET   OXT  O N N 320 
MET   H    H N N 321 
MET   H2   H N N 322 
MET   HA   H N N 323 
MET   HB2  H N N 324 
MET   HB3  H N N 325 
MET   HG2  H N N 326 
MET   HG3  H N N 327 
MET   HE1  H N N 328 
MET   HE2  H N N 329 
MET   HE3  H N N 330 
MET   HXT  H N N 331 
PHE   N    N N N 332 
PHE   CA   C N S 333 
PHE   C    C N N 334 
PHE   O    O N N 335 
PHE   CB   C N N 336 
PHE   CG   C Y N 337 
PHE   CD1  C Y N 338 
PHE   CD2  C Y N 339 
PHE   CE1  C Y N 340 
PHE   CE2  C Y N 341 
PHE   CZ   C Y N 342 
PHE   OXT  O N N 343 
PHE   H    H N N 344 
PHE   H2   H N N 345 
PHE   HA   H N N 346 
PHE   HB2  H N N 347 
PHE   HB3  H N N 348 
PHE   HD1  H N N 349 
PHE   HD2  H N N 350 
PHE   HE1  H N N 351 
PHE   HE2  H N N 352 
PHE   HZ   H N N 353 
PHE   HXT  H N N 354 
PRO   N    N N N 355 
PRO   CA   C N S 356 
PRO   C    C N N 357 
PRO   O    O N N 358 
PRO   CB   C N N 359 
PRO   CG   C N N 360 
PRO   CD   C N N 361 
PRO   OXT  O N N 362 
PRO   H    H N N 363 
PRO   HA   H N N 364 
PRO   HB2  H N N 365 
PRO   HB3  H N N 366 
PRO   HG2  H N N 367 
PRO   HG3  H N N 368 
PRO   HD2  H N N 369 
PRO   HD3  H N N 370 
PRO   HXT  H N N 371 
SER   N    N N N 372 
SER   CA   C N S 373 
SER   C    C N N 374 
SER   O    O N N 375 
SER   CB   C N N 376 
SER   OG   O N N 377 
SER   OXT  O N N 378 
SER   H    H N N 379 
SER   H2   H N N 380 
SER   HA   H N N 381 
SER   HB2  H N N 382 
SER   HB3  H N N 383 
SER   HG   H N N 384 
SER   HXT  H N N 385 
THR   N    N N N 386 
THR   CA   C N S 387 
THR   C    C N N 388 
THR   O    O N N 389 
THR   CB   C N R 390 
THR   OG1  O N N 391 
THR   CG2  C N N 392 
THR   OXT  O N N 393 
THR   H    H N N 394 
THR   H2   H N N 395 
THR   HA   H N N 396 
THR   HB   H N N 397 
THR   HG1  H N N 398 
THR   HG21 H N N 399 
THR   HG22 H N N 400 
THR   HG23 H N N 401 
THR   HXT  H N N 402 
TRP   N    N N N 403 
TRP   CA   C N S 404 
TRP   C    C N N 405 
TRP   O    O N N 406 
TRP   CB   C N N 407 
TRP   CG   C Y N 408 
TRP   CD1  C Y N 409 
TRP   CD2  C Y N 410 
TRP   NE1  N Y N 411 
TRP   CE2  C Y N 412 
TRP   CE3  C Y N 413 
TRP   CZ2  C Y N 414 
TRP   CZ3  C Y N 415 
TRP   CH2  C Y N 416 
TRP   OXT  O N N 417 
TRP   H    H N N 418 
TRP   H2   H N N 419 
TRP   HA   H N N 420 
TRP   HB2  H N N 421 
TRP   HB3  H N N 422 
TRP   HD1  H N N 423 
TRP   HE1  H N N 424 
TRP   HE3  H N N 425 
TRP   HZ2  H N N 426 
TRP   HZ3  H N N 427 
TRP   HH2  H N N 428 
TRP   HXT  H N N 429 
TYR   N    N N N 430 
TYR   CA   C N S 431 
TYR   C    C N N 432 
TYR   O    O N N 433 
TYR   CB   C N N 434 
TYR   CG   C Y N 435 
TYR   CD1  C Y N 436 
TYR   CD2  C Y N 437 
TYR   CE1  C Y N 438 
TYR   CE2  C Y N 439 
TYR   CZ   C Y N 440 
TYR   OH   O N N 441 
TYR   OXT  O N N 442 
TYR   H    H N N 443 
TYR   H2   H N N 444 
TYR   HA   H N N 445 
TYR   HB2  H N N 446 
TYR   HB3  H N N 447 
TYR   HD1  H N N 448 
TYR   HD2  H N N 449 
TYR   HE1  H N N 450 
TYR   HE2  H N N 451 
TYR   HH   H N N 452 
TYR   HXT  H N N 453 
VAL   N    N N N 454 
VAL   CA   C N S 455 
VAL   C    C N N 456 
VAL   O    O N N 457 
VAL   CB   C N N 458 
VAL   CG1  C N N 459 
VAL   CG2  C N N 460 
VAL   OXT  O N N 461 
VAL   H    H N N 462 
VAL   H2   H N N 463 
VAL   HA   H N N 464 
VAL   HB   H N N 465 
VAL   HG11 H N N 466 
VAL   HG12 H N N 467 
VAL   HG13 H N N 468 
VAL   HG21 H N N 469 
VAL   HG22 H N N 470 
VAL   HG23 H N N 471 
VAL   HXT  H N N 472 
# 
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 
A1D8T O6  C21  doub N N 1   
A1D8T C21 N4   sing N N 2   
A1D8T C21 C22  sing N N 3   
A1D8T N4  C20  sing N N 4   
A1D8T C24 C22  sing N N 5   
A1D8T C24 C25  sing N N 6   
A1D8T C22 C23  sing N N 7   
A1D8T C26 N6   doub N N 8   
A1D8T C26 C25  sing N N 9   
A1D8T C25 N5   sing N N 10  
A1D8T C20 C23  sing N N 11  
A1D8T C20 C19  sing N N 12  
A1D8T N5  C27  sing N N 13  
A1D8T O3  C10  doub N N 14  
A1D8T C19 N3   sing N N 15  
A1D8T C19 O4   doub N N 16  
A1D8T N3  C16  sing N N 17  
A1D8T C27 C12  sing N N 18  
A1D8T C27 O5   doub N N 19  
A1D8T C12 N2   sing N N 20  
A1D8T C12 C13  sing N N 21  
A1D8T C16 C11  sing N N 22  
A1D8T C10 N2   sing N N 23  
A1D8T C10 C9   sing N N 24  
A1D8T O1  C7   sing N N 25  
A1D8T O1  C8   sing N N 26  
A1D8T N1  C8   sing N N 27  
A1D8T N1  C9   sing N N 28  
A1D8T C29 C28  sing N N 29  
A1D8T N2  C15  sing N N 30  
A1D8T C7  C4   sing N N 31  
A1D8T C8  O2   doub N N 32  
A1D8T C13 C28  sing N N 33  
A1D8T C13 C14  sing N N 34  
A1D8T C9  C11  sing N N 35  
A1D8T C3  C4   doub Y N 36  
A1D8T C3  C2   sing Y N 37  
A1D8T C28 C30  sing N N 38  
A1D8T C28 C14  sing N N 39  
A1D8T C11 C18  sing N N 40  
A1D8T C11 C17  sing N N 41  
A1D8T C4  C5   sing Y N 42  
A1D8T C2  C1   doub Y N 43  
A1D8T C15 C14  sing N N 44  
A1D8T C5  C6   doub Y N 45  
A1D8T C1  C6   sing Y N 46  
A1D8T C1  H1   sing N N 47  
A1D8T C2  H2   sing N N 48  
A1D8T C3  H3   sing N N 49  
A1D8T C5  H4   sing N N 50  
A1D8T C6  H5   sing N N 51  
A1D8T C7  H6   sing N N 52  
A1D8T C7  H7   sing N N 53  
A1D8T N1  H8   sing N N 54  
A1D8T C9  H9   sing N N 55  
A1D8T C12 H10  sing N N 56  
A1D8T C13 H11  sing N N 57  
A1D8T C14 H12  sing N N 58  
A1D8T C15 H13  sing N N 59  
A1D8T C15 H14  sing N N 60  
A1D8T C16 H15  sing N N 61  
A1D8T C16 H16  sing N N 62  
A1D8T C17 H17  sing N N 63  
A1D8T C17 H18  sing N N 64  
A1D8T C17 H19  sing N N 65  
A1D8T C18 H20  sing N N 66  
A1D8T C18 H21  sing N N 67  
A1D8T C18 H22  sing N N 68  
A1D8T N3  H23  sing N N 69  
A1D8T C20 H24  sing N N 70  
A1D8T N4  H25  sing N N 71  
A1D8T C22 H26  sing N N 72  
A1D8T C23 H27  sing N N 73  
A1D8T C23 H28  sing N N 74  
A1D8T C24 H29  sing N N 75  
A1D8T C24 H30  sing N N 76  
A1D8T C25 H31  sing N N 77  
A1D8T C26 H32  sing N N 78  
A1D8T N5  H33  sing N N 79  
A1D8T N6  H34  sing N N 80  
A1D8T C29 H35  sing N N 81  
A1D8T C29 H36  sing N N 82  
A1D8T C29 H37  sing N N 83  
A1D8T C30 H38  sing N N 84  
A1D8T C30 H39  sing N N 85  
A1D8T C30 H40  sing N N 86  
ALA   N   CA   sing N N 87  
ALA   N   H    sing N N 88  
ALA   N   H2   sing N N 89  
ALA   CA  C    sing N N 90  
ALA   CA  CB   sing N N 91  
ALA   CA  HA   sing N N 92  
ALA   C   O    doub N N 93  
ALA   C   OXT  sing N N 94  
ALA   CB  HB1  sing N N 95  
ALA   CB  HB2  sing N N 96  
ALA   CB  HB3  sing N N 97  
ALA   OXT HXT  sing N N 98  
ARG   N   CA   sing N N 99  
ARG   N   H    sing N N 100 
ARG   N   H2   sing N N 101 
ARG   CA  C    sing N N 102 
ARG   CA  CB   sing N N 103 
ARG   CA  HA   sing N N 104 
ARG   C   O    doub N N 105 
ARG   C   OXT  sing N N 106 
ARG   CB  CG   sing N N 107 
ARG   CB  HB2  sing N N 108 
ARG   CB  HB3  sing N N 109 
ARG   CG  CD   sing N N 110 
ARG   CG  HG2  sing N N 111 
ARG   CG  HG3  sing N N 112 
ARG   CD  NE   sing N N 113 
ARG   CD  HD2  sing N N 114 
ARG   CD  HD3  sing N N 115 
ARG   NE  CZ   sing N N 116 
ARG   NE  HE   sing N N 117 
ARG   CZ  NH1  sing N N 118 
ARG   CZ  NH2  doub N N 119 
ARG   NH1 HH11 sing N N 120 
ARG   NH1 HH12 sing N N 121 
ARG   NH2 HH21 sing N N 122 
ARG   NH2 HH22 sing N N 123 
ARG   OXT HXT  sing N N 124 
ASN   N   CA   sing N N 125 
ASN   N   H    sing N N 126 
ASN   N   H2   sing N N 127 
ASN   CA  C    sing N N 128 
ASN   CA  CB   sing N N 129 
ASN   CA  HA   sing N N 130 
ASN   C   O    doub N N 131 
ASN   C   OXT  sing N N 132 
ASN   CB  CG   sing N N 133 
ASN   CB  HB2  sing N N 134 
ASN   CB  HB3  sing N N 135 
ASN   CG  OD1  doub N N 136 
ASN   CG  ND2  sing N N 137 
ASN   ND2 HD21 sing N N 138 
ASN   ND2 HD22 sing N N 139 
ASN   OXT HXT  sing N N 140 
ASP   N   CA   sing N N 141 
ASP   N   H    sing N N 142 
ASP   N   H2   sing N N 143 
ASP   CA  C    sing N N 144 
ASP   CA  CB   sing N N 145 
ASP   CA  HA   sing N N 146 
ASP   C   O    doub N N 147 
ASP   C   OXT  sing N N 148 
ASP   CB  CG   sing N N 149 
ASP   CB  HB2  sing N N 150 
ASP   CB  HB3  sing N N 151 
ASP   CG  OD1  doub N N 152 
ASP   CG  OD2  sing N N 153 
ASP   OD2 HD2  sing N N 154 
ASP   OXT HXT  sing N N 155 
CYS   N   CA   sing N N 156 
CYS   N   H    sing N N 157 
CYS   N   H2   sing N N 158 
CYS   CA  C    sing N N 159 
CYS   CA  CB   sing N N 160 
CYS   CA  HA   sing N N 161 
CYS   C   O    doub N N 162 
CYS   C   OXT  sing N N 163 
CYS   CB  SG   sing N N 164 
CYS   CB  HB2  sing N N 165 
CYS   CB  HB3  sing N N 166 
CYS   SG  HG   sing N N 167 
CYS   OXT HXT  sing N N 168 
GLN   N   CA   sing N N 169 
GLN   N   H    sing N N 170 
GLN   N   H2   sing N N 171 
GLN   CA  C    sing N N 172 
GLN   CA  CB   sing N N 173 
GLN   CA  HA   sing N N 174 
GLN   C   O    doub N N 175 
GLN   C   OXT  sing N N 176 
GLN   CB  CG   sing N N 177 
GLN   CB  HB2  sing N N 178 
GLN   CB  HB3  sing N N 179 
GLN   CG  CD   sing N N 180 
GLN   CG  HG2  sing N N 181 
GLN   CG  HG3  sing N N 182 
GLN   CD  OE1  doub N N 183 
GLN   CD  NE2  sing N N 184 
GLN   NE2 HE21 sing N N 185 
GLN   NE2 HE22 sing N N 186 
GLN   OXT HXT  sing N N 187 
GLU   N   CA   sing N N 188 
GLU   N   H    sing N N 189 
GLU   N   H2   sing N N 190 
GLU   CA  C    sing N N 191 
GLU   CA  CB   sing N N 192 
GLU   CA  HA   sing N N 193 
GLU   C   O    doub N N 194 
GLU   C   OXT  sing N N 195 
GLU   CB  CG   sing N N 196 
GLU   CB  HB2  sing N N 197 
GLU   CB  HB3  sing N N 198 
GLU   CG  CD   sing N N 199 
GLU   CG  HG2  sing N N 200 
GLU   CG  HG3  sing N N 201 
GLU   CD  OE1  doub N N 202 
GLU   CD  OE2  sing N N 203 
GLU   OE2 HE2  sing N N 204 
GLU   OXT HXT  sing N N 205 
GLY   N   CA   sing N N 206 
GLY   N   H    sing N N 207 
GLY   N   H2   sing N N 208 
GLY   CA  C    sing N N 209 
GLY   CA  HA2  sing N N 210 
GLY   CA  HA3  sing N N 211 
GLY   C   O    doub N N 212 
GLY   C   OXT  sing N N 213 
GLY   OXT HXT  sing N N 214 
HIS   N   CA   sing N N 215 
HIS   N   H    sing N N 216 
HIS   N   H2   sing N N 217 
HIS   CA  C    sing N N 218 
HIS   CA  CB   sing N N 219 
HIS   CA  HA   sing N N 220 
HIS   C   O    doub N N 221 
HIS   C   OXT  sing N N 222 
HIS   CB  CG   sing N N 223 
HIS   CB  HB2  sing N N 224 
HIS   CB  HB3  sing N N 225 
HIS   CG  ND1  sing Y N 226 
HIS   CG  CD2  doub Y N 227 
HIS   ND1 CE1  doub Y N 228 
HIS   ND1 HD1  sing N N 229 
HIS   CD2 NE2  sing Y N 230 
HIS   CD2 HD2  sing N N 231 
HIS   CE1 NE2  sing Y N 232 
HIS   CE1 HE1  sing N N 233 
HIS   NE2 HE2  sing N N 234 
HIS   OXT HXT  sing N N 235 
HOH   O   H1   sing N N 236 
HOH   O   H2   sing N N 237 
ILE   N   CA   sing N N 238 
ILE   N   H    sing N N 239 
ILE   N   H2   sing N N 240 
ILE   CA  C    sing N N 241 
ILE   CA  CB   sing N N 242 
ILE   CA  HA   sing N N 243 
ILE   C   O    doub N N 244 
ILE   C   OXT  sing N N 245 
ILE   CB  CG1  sing N N 246 
ILE   CB  CG2  sing N N 247 
ILE   CB  HB   sing N N 248 
ILE   CG1 CD1  sing N N 249 
ILE   CG1 HG12 sing N N 250 
ILE   CG1 HG13 sing N N 251 
ILE   CG2 HG21 sing N N 252 
ILE   CG2 HG22 sing N N 253 
ILE   CG2 HG23 sing N N 254 
ILE   CD1 HD11 sing N N 255 
ILE   CD1 HD12 sing N N 256 
ILE   CD1 HD13 sing N N 257 
ILE   OXT HXT  sing N N 258 
LEU   N   CA   sing N N 259 
LEU   N   H    sing N N 260 
LEU   N   H2   sing N N 261 
LEU   CA  C    sing N N 262 
LEU   CA  CB   sing N N 263 
LEU   CA  HA   sing N N 264 
LEU   C   O    doub N N 265 
LEU   C   OXT  sing N N 266 
LEU   CB  CG   sing N N 267 
LEU   CB  HB2  sing N N 268 
LEU   CB  HB3  sing N N 269 
LEU   CG  CD1  sing N N 270 
LEU   CG  CD2  sing N N 271 
LEU   CG  HG   sing N N 272 
LEU   CD1 HD11 sing N N 273 
LEU   CD1 HD12 sing N N 274 
LEU   CD1 HD13 sing N N 275 
LEU   CD2 HD21 sing N N 276 
LEU   CD2 HD22 sing N N 277 
LEU   CD2 HD23 sing N N 278 
LEU   OXT HXT  sing N N 279 
LYS   N   CA   sing N N 280 
LYS   N   H    sing N N 281 
LYS   N   H2   sing N N 282 
LYS   CA  C    sing N N 283 
LYS   CA  CB   sing N N 284 
LYS   CA  HA   sing N N 285 
LYS   C   O    doub N N 286 
LYS   C   OXT  sing N N 287 
LYS   CB  CG   sing N N 288 
LYS   CB  HB2  sing N N 289 
LYS   CB  HB3  sing N N 290 
LYS   CG  CD   sing N N 291 
LYS   CG  HG2  sing N N 292 
LYS   CG  HG3  sing N N 293 
LYS   CD  CE   sing N N 294 
LYS   CD  HD2  sing N N 295 
LYS   CD  HD3  sing N N 296 
LYS   CE  NZ   sing N N 297 
LYS   CE  HE2  sing N N 298 
LYS   CE  HE3  sing N N 299 
LYS   NZ  HZ1  sing N N 300 
LYS   NZ  HZ2  sing N N 301 
LYS   NZ  HZ3  sing N N 302 
LYS   OXT HXT  sing N N 303 
MET   N   CA   sing N N 304 
MET   N   H    sing N N 305 
MET   N   H2   sing N N 306 
MET   CA  C    sing N N 307 
MET   CA  CB   sing N N 308 
MET   CA  HA   sing N N 309 
MET   C   O    doub N N 310 
MET   C   OXT  sing N N 311 
MET   CB  CG   sing N N 312 
MET   CB  HB2  sing N N 313 
MET   CB  HB3  sing N N 314 
MET   CG  SD   sing N N 315 
MET   CG  HG2  sing N N 316 
MET   CG  HG3  sing N N 317 
MET   SD  CE   sing N N 318 
MET   CE  HE1  sing N N 319 
MET   CE  HE2  sing N N 320 
MET   CE  HE3  sing N N 321 
MET   OXT HXT  sing N N 322 
PHE   N   CA   sing N N 323 
PHE   N   H    sing N N 324 
PHE   N   H2   sing N N 325 
PHE   CA  C    sing N N 326 
PHE   CA  CB   sing N N 327 
PHE   CA  HA   sing N N 328 
PHE   C   O    doub N N 329 
PHE   C   OXT  sing N N 330 
PHE   CB  CG   sing N N 331 
PHE   CB  HB2  sing N N 332 
PHE   CB  HB3  sing N N 333 
PHE   CG  CD1  doub Y N 334 
PHE   CG  CD2  sing Y N 335 
PHE   CD1 CE1  sing Y N 336 
PHE   CD1 HD1  sing N N 337 
PHE   CD2 CE2  doub Y N 338 
PHE   CD2 HD2  sing N N 339 
PHE   CE1 CZ   doub Y N 340 
PHE   CE1 HE1  sing N N 341 
PHE   CE2 CZ   sing Y N 342 
PHE   CE2 HE2  sing N N 343 
PHE   CZ  HZ   sing N N 344 
PHE   OXT HXT  sing N N 345 
PRO   N   CA   sing N N 346 
PRO   N   CD   sing N N 347 
PRO   N   H    sing N N 348 
PRO   CA  C    sing N N 349 
PRO   CA  CB   sing N N 350 
PRO   CA  HA   sing N N 351 
PRO   C   O    doub N N 352 
PRO   C   OXT  sing N N 353 
PRO   CB  CG   sing N N 354 
PRO   CB  HB2  sing N N 355 
PRO   CB  HB3  sing N N 356 
PRO   CG  CD   sing N N 357 
PRO   CG  HG2  sing N N 358 
PRO   CG  HG3  sing N N 359 
PRO   CD  HD2  sing N N 360 
PRO   CD  HD3  sing N N 361 
PRO   OXT HXT  sing N N 362 
SER   N   CA   sing N N 363 
SER   N   H    sing N N 364 
SER   N   H2   sing N N 365 
SER   CA  C    sing N N 366 
SER   CA  CB   sing N N 367 
SER   CA  HA   sing N N 368 
SER   C   O    doub N N 369 
SER   C   OXT  sing N N 370 
SER   CB  OG   sing N N 371 
SER   CB  HB2  sing N N 372 
SER   CB  HB3  sing N N 373 
SER   OG  HG   sing N N 374 
SER   OXT HXT  sing N N 375 
THR   N   CA   sing N N 376 
THR   N   H    sing N N 377 
THR   N   H2   sing N N 378 
THR   CA  C    sing N N 379 
THR   CA  CB   sing N N 380 
THR   CA  HA   sing N N 381 
THR   C   O    doub N N 382 
THR   C   OXT  sing N N 383 
THR   CB  OG1  sing N N 384 
THR   CB  CG2  sing N N 385 
THR   CB  HB   sing N N 386 
THR   OG1 HG1  sing N N 387 
THR   CG2 HG21 sing N N 388 
THR   CG2 HG22 sing N N 389 
THR   CG2 HG23 sing N N 390 
THR   OXT HXT  sing N N 391 
TRP   N   CA   sing N N 392 
TRP   N   H    sing N N 393 
TRP   N   H2   sing N N 394 
TRP   CA  C    sing N N 395 
TRP   CA  CB   sing N N 396 
TRP   CA  HA   sing N N 397 
TRP   C   O    doub N N 398 
TRP   C   OXT  sing N N 399 
TRP   CB  CG   sing N N 400 
TRP   CB  HB2  sing N N 401 
TRP   CB  HB3  sing N N 402 
TRP   CG  CD1  doub Y N 403 
TRP   CG  CD2  sing Y N 404 
TRP   CD1 NE1  sing Y N 405 
TRP   CD1 HD1  sing N N 406 
TRP   CD2 CE2  doub Y N 407 
TRP   CD2 CE3  sing Y N 408 
TRP   NE1 CE2  sing Y N 409 
TRP   NE1 HE1  sing N N 410 
TRP   CE2 CZ2  sing Y N 411 
TRP   CE3 CZ3  doub Y N 412 
TRP   CE3 HE3  sing N N 413 
TRP   CZ2 CH2  doub Y N 414 
TRP   CZ2 HZ2  sing N N 415 
TRP   CZ3 CH2  sing Y N 416 
TRP   CZ3 HZ3  sing N N 417 
TRP   CH2 HH2  sing N N 418 
TRP   OXT HXT  sing N N 419 
TYR   N   CA   sing N N 420 
TYR   N   H    sing N N 421 
TYR   N   H2   sing N N 422 
TYR   CA  C    sing N N 423 
TYR   CA  CB   sing N N 424 
TYR   CA  HA   sing N N 425 
TYR   C   O    doub N N 426 
TYR   C   OXT  sing N N 427 
TYR   CB  CG   sing N N 428 
TYR   CB  HB2  sing N N 429 
TYR   CB  HB3  sing N N 430 
TYR   CG  CD1  doub Y N 431 
TYR   CG  CD2  sing Y N 432 
TYR   CD1 CE1  sing Y N 433 
TYR   CD1 HD1  sing N N 434 
TYR   CD2 CE2  doub Y N 435 
TYR   CD2 HD2  sing N N 436 
TYR   CE1 CZ   doub Y N 437 
TYR   CE1 HE1  sing N N 438 
TYR   CE2 CZ   sing Y N 439 
TYR   CE2 HE2  sing N N 440 
TYR   CZ  OH   sing N N 441 
TYR   OH  HH   sing N N 442 
TYR   OXT HXT  sing N N 443 
VAL   N   CA   sing N N 444 
VAL   N   H    sing N N 445 
VAL   N   H2   sing N N 446 
VAL   CA  C    sing N N 447 
VAL   CA  CB   sing N N 448 
VAL   CA  HA   sing N N 449 
VAL   C   O    doub N N 450 
VAL   C   OXT  sing N N 451 
VAL   CB  CG1  sing N N 452 
VAL   CB  CG2  sing N N 453 
VAL   CB  HB   sing N N 454 
VAL   CG1 HG11 sing N N 455 
VAL   CG1 HG12 sing N N 456 
VAL   CG1 HG13 sing N N 457 
VAL   CG2 HG21 sing N N 458 
VAL   CG2 HG22 sing N N 459 
VAL   CG2 HG23 sing N N 460 
VAL   OXT HXT  sing N N 461 
# 
_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             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5R7Y 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8ZQ8 
_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]   0.008742 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002100 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018886 
_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]   0.022643 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . SER   A 1 11  ? -2.818 4.802   -16.949 1.00 15.70 ? 1   SER   A N   1 
ATOM   2    C CA  . SER   A 1 11  ? -2.022 5.828   -16.253 1.00 16.37 ? 1   SER   A CA  1 
ATOM   3    C C   . SER   A 1 11  ? -2.454 5.908   -14.793 1.00 16.25 ? 1   SER   A C   1 
ATOM   4    O O   . SER   A 1 11  ? -3.255 5.063   -14.370 1.00 13.19 ? 1   SER   A O   1 
ATOM   5    C CB  . SER   A 1 11  ? -2.091 7.162   -16.962 1.00 18.30 ? 1   SER   A CB  1 
ATOM   6    O OG  . SER   A 1 11  ? -3.376 7.707   -16.946 1.00 20.69 ? 1   SER   A OG  1 
ATOM   7    N N   . GLY   A 1 12  ? -1.974 6.929   -14.084 1.00 16.07 ? 2   GLY   A N   1 
ATOM   8    C CA  . GLY   A 1 12  ? -2.170 7.082   -12.637 1.00 16.69 ? 2   GLY   A CA  1 
ATOM   9    C C   . GLY   A 1 12  ? -0.884 6.717   -11.936 1.00 16.08 ? 2   GLY   A C   1 
ATOM   10   O O   . GLY   A 1 12  ? -0.083 5.956   -12.486 1.00 17.87 ? 2   GLY   A O   1 
ATOM   11   N N   . PHE   A 1 13  ? -0.680 7.213   -10.739 1.00 17.55 ? 3   PHE   A N   1 
ATOM   12   C CA  . PHE   A 1 13  ? 0.581  6.973   -10.007 1.00 17.54 ? 3   PHE   A CA  1 
ATOM   13   C C   . PHE   A 1 13  ? 0.253  6.925   -8.539  1.00 17.76 ? 3   PHE   A C   1 
ATOM   14   O O   . PHE   A 1 13  ? -0.239 7.946   -8.024  1.00 18.87 ? 3   PHE   A O   1 
ATOM   15   C CB  . PHE   A 1 13  ? 1.643  8.037   -10.321 1.00 18.19 ? 3   PHE   A CB  1 
ATOM   16   C CG  . PHE   A 1 13  ? 3.025  7.541   -10.017 1.00 17.41 ? 3   PHE   A CG  1 
ATOM   17   C CD1 . PHE   A 1 13  ? 3.620  6.607   -10.851 1.00 18.60 ? 3   PHE   A CD1 1 
ATOM   18   C CD2 . PHE   A 1 13  ? 3.703  7.952   -8.875  1.00 18.33 ? 3   PHE   A CD2 1 
ATOM   19   C CE1 . PHE   A 1 13  ? 4.878  6.101   -10.562 1.00 20.17 ? 3   PHE   A CE1 1 
ATOM   20   C CE2 . PHE   A 1 13  ? 4.964  7.444   -8.591  1.00 19.19 ? 3   PHE   A CE2 1 
ATOM   21   C CZ  . PHE   A 1 13  ? 5.544  6.519   -9.424  1.00 19.22 ? 3   PHE   A CZ  1 
ATOM   22   N N   . ARG   A 1 14  ? 0.469  5.760   -7.928  1.00 16.38 ? 4   ARG   A N   1 
ATOM   23   C CA  . ARG   A 1 14  ? 0.073  5.468   -6.533  1.00 16.66 ? 4   ARG   A CA  1 
ATOM   24   C C   . ARG   A 1 14  ? 1.293  5.029   -5.730  1.00 14.31 ? 4   ARG   A C   1 
ATOM   25   O O   . ARG   A 1 14  ? 2.169  4.386   -6.278  1.00 15.07 ? 4   ARG   A O   1 
ATOM   26   C CB  . ARG   A 1 14  ? -1.011 4.387   -6.533  1.00 16.40 ? 4   ARG   A CB  1 
ATOM   27   C CG  . ARG   A 1 14  ? -2.314 4.859   -7.162  1.00 17.62 ? 4   ARG   A CG  1 
ATOM   28   C CD  . ARG   A 1 14  ? -2.811 6.127   -6.506  1.00 20.21 ? 4   ARG   A CD  1 
ATOM   29   N NE  . ARG   A 1 14  ? -2.740 5.884   -5.081  1.00 21.73 ? 4   ARG   A NE  1 
ATOM   30   C CZ  . ARG   A 1 14  ? -3.669 5.260   -4.381  1.00 23.62 ? 4   ARG   A CZ  1 
ATOM   31   N NH1 . ARG   A 1 14  ? -3.490 5.058   -3.079  1.00 21.75 ? 4   ARG   A NH1 1 
ATOM   32   N NH2 . ARG   A 1 14  ? -4.780 4.857   -4.979  1.00 25.01 ? 4   ARG   A NH2 1 
ATOM   33   N N   . LYS   A 1 15  ? 1.322  5.346   -4.438  1.00 15.25 ? 5   LYS   A N   1 
ATOM   34   C CA  . LYS   A 1 15  ? 2.315  4.718   -3.534  1.00 16.74 ? 5   LYS   A CA  1 
ATOM   35   C C   . LYS   A 1 15  ? 1.902  3.237   -3.462  1.00 16.29 ? 5   LYS   A C   1 
ATOM   36   O O   . LYS   A 1 15  ? 0.755  2.955   -3.094  1.00 15.71 ? 5   LYS   A O   1 
ATOM   37   C CB  . LYS   A 1 15  ? 2.354  5.459   -2.192  1.00 20.39 ? 5   LYS   A CB  1 
ATOM   38   C CG  . LYS   A 1 15  ? 3.504  5.084   -1.267  1.00 23.85 ? 5   LYS   A CG  1 
ATOM   39   C CD  . LYS   A 1 15  ? 4.900  5.432   -1.793  1.00 29.04 ? 5   LYS   A CD  1 
ATOM   40   C CE  . LYS   A 1 15  ? 5.214  6.918   -1.790  1.00 31.88 ? 5   LYS   A CE  1 
ATOM   41   N NZ  . LYS   A 1 15  ? 5.148  7.508   -0.428  1.00 32.63 ? 5   LYS   A NZ  1 
ATOM   42   N N   . MET   A 1 16  ? 2.757  2.343   -3.953  1.00 14.34 ? 6   MET   A N   1 
ATOM   43   C CA  . MET   A 1 16  ? 2.391  0.950   -4.292  1.00 15.73 ? 6   MET   A CA  1 
ATOM   44   C C   . MET   A 1 16  ? 3.321  0.016   -3.535  1.00 13.63 ? 6   MET   A C   1 
ATOM   45   O O   . MET   A 1 16  ? 4.558  0.219   -3.620  1.00 14.79 ? 6   MET   A O   1 
ATOM   46   C CB  . MET   A 1 16  ? 2.542  0.685   -5.792  1.00 16.77 ? 6   MET   A CB  1 
ATOM   47   C CG  . MET   A 1 16  ? 1.965  -0.636  -6.181  1.00 20.40 ? 6   MET   A CG  1 
ATOM   48   S SD  . MET   A 1 16  ? 1.714  -0.758  -7.955  1.00 24.01 ? 6   MET   A SD  1 
ATOM   49   C CE  . MET   A 1 16  ? 1.083  0.871   -8.349  1.00 24.16 ? 6   MET   A CE  1 
ATOM   50   N N   . ALA   A 1 17  ? 2.760  -0.906  -2.759  1.00 13.44 ? 7   ALA   A N   1 
ATOM   51   C CA  . ALA   A 1 17  ? 3.543  -1.908  -2.005  1.00 12.40 ? 7   ALA   A CA  1 
ATOM   52   C C   . ALA   A 1 17  ? 3.736  -3.138  -2.884  1.00 12.63 ? 7   ALA   A C   1 
ATOM   53   O O   . ALA   A 1 17  ? 2.936  -3.336  -3.811  1.00 12.50 ? 7   ALA   A O   1 
ATOM   54   C CB  . ALA   A 1 17  ? 2.838  -2.278  -0.735  1.00 12.34 ? 7   ALA   A CB  1 
ATOM   55   N N   . PHE   A 1 18  ? 4.735  -3.962  -2.586  1.00 12.27 ? 8   PHE   A N   1 
ATOM   56   C CA  . PHE   A 1 18  ? 4.804  -5.316  -3.176  1.00 12.43 ? 8   PHE   A CA  1 
ATOM   57   C C   . PHE   A 1 18  ? 3.664  -6.181  -2.649  1.00 12.73 ? 8   PHE   A C   1 
ATOM   58   O O   . PHE   A 1 18  ? 3.236  -6.088  -1.500  1.00 11.31 ? 8   PHE   A O   1 
ATOM   59   C CB  . PHE   A 1 18  ? 6.149  -5.974  -2.912  1.00 13.10 ? 8   PHE   A CB  1 
ATOM   60   C CG  . PHE   A 1 18  ? 7.291  -5.319  -3.643  1.00 13.99 ? 8   PHE   A CG  1 
ATOM   61   C CD1 . PHE   A 1 18  ? 7.527  -5.560  -4.985  1.00 16.18 ? 8   PHE   A CD1 1 
ATOM   62   C CD2 . PHE   A 1 18  ? 8.131  -4.452  -2.976  1.00 15.10 ? 8   PHE   A CD2 1 
ATOM   63   C CE1 . PHE   A 1 18  ? 8.588  -4.944  -5.639  1.00 16.89 ? 8   PHE   A CE1 1 
ATOM   64   C CE2 . PHE   A 1 18  ? 9.203  -3.867  -3.622  1.00 16.79 ? 8   PHE   A CE2 1 
ATOM   65   C CZ  . PHE   A 1 18  ? 9.430  -4.107  -4.961  1.00 16.14 ? 8   PHE   A CZ  1 
ATOM   66   N N   . PRO   A 1 19  ? 3.237  -7.157  -3.471  1.00 13.93 ? 9   PRO   A N   1 
ATOM   67   C CA  . PRO   A 1 19  ? 2.309  -8.186  -3.013  1.00 13.42 ? 9   PRO   A CA  1 
ATOM   68   C C   . PRO   A 1 19  ? 2.973  -8.864  -1.803  1.00 12.47 ? 9   PRO   A C   1 
ATOM   69   O O   . PRO   A 1 19  ? 4.153  -9.151  -1.895  1.00 12.36 ? 9   PRO   A O   1 
ATOM   70   C CB  . PRO   A 1 19  ? 2.169  -9.120  -4.203  1.00 14.08 ? 9   PRO   A CB  1 
ATOM   71   C CG  . PRO   A 1 19  ? 2.597  -8.240  -5.394  1.00 16.34 ? 9   PRO   A CG  1 
ATOM   72   C CD  . PRO   A 1 19  ? 3.707  -7.368  -4.846  1.00 14.13 ? 9   PRO   A CD  1 
ATOM   73   N N   . SER   A 1 20  ? 2.204  -9.098  -0.750  1.00 13.13 ? 10  SER   A N   1 
ATOM   74   C CA  . SER   A 1 20  ? 2.714  -9.465  0.589   1.00 13.18 ? 10  SER   A CA  1 
ATOM   75   C C   . SER   A 1 20  ? 2.651  -10.969 0.836   1.00 13.40 ? 10  SER   A C   1 
ATOM   76   O O   . SER   A 1 20  ? 3.165  -11.395 1.886   1.00 12.52 ? 10  SER   A O   1 
ATOM   77   C CB  . SER   A 1 20  ? 2.005  -8.701  1.667   1.00 12.46 ? 10  SER   A CB  1 
ATOM   78   O OG  . SER   A 1 20  ? 0.607  -8.964  1.732   1.00 12.25 ? 10  SER   A OG  1 
ATOM   79   N N   . GLY   A 1 21  ? 2.012  -11.746 -0.047  1.00 13.63 ? 11  GLY   A N   1 
ATOM   80   C CA  . GLY   A 1 21  ? 1.762  -13.187 0.181   1.00 13.66 ? 11  GLY   A CA  1 
ATOM   81   C C   . GLY   A 1 21  ? 3.004  -13.977 0.595   1.00 14.03 ? 11  GLY   A C   1 
ATOM   82   O O   . GLY   A 1 21  ? 2.904  -14.787 1.561   1.00 14.09 ? 11  GLY   A O   1 
ATOM   83   N N   . LYS   A 1 22  ? 4.127  -13.792 -0.106  1.00 13.38 ? 12  LYS   A N   1 
ATOM   84   C CA  . LYS   A 1 22  ? 5.359  -14.567 0.177   1.00 14.43 ? 12  LYS   A CA  1 
ATOM   85   C C   . LYS   A 1 22  ? 5.818  -14.286 1.615   1.00 14.03 ? 12  LYS   A C   1 
ATOM   86   O O   . LYS   A 1 22  ? 6.337  -15.202 2.235   1.00 14.07 ? 12  LYS   A O   1 
ATOM   87   C CB  . LYS   A 1 22  ? 6.422  -14.270 -0.870  1.00 15.98 ? 12  LYS   A CB  1 
ATOM   88   C CG  . LYS   A 1 22  ? 6.081  -14.845 -2.236  1.00 18.57 ? 12  LYS   A CG  1 
ATOM   89   C CD  . LYS   A 1 22  ? 7.056  -14.360 -3.301  1.00 21.24 ? 12  LYS   A CD  1 
ATOM   90   C CE  . LYS   A 1 22  ? 6.835  -15.015 -4.641  1.00 24.39 ? 12  LYS   A CE  1 
ATOM   91   N NZ  . LYS   A 1 22  ? 7.702  -16.200 -4.787  1.00 27.77 ? 12  LYS   A NZ  1 
ATOM   92   N N   . VAL   A 1 23  ? 5.595  -13.073 2.126   1.00 12.82 ? 13  VAL   A N   1 
ATOM   93   C CA  . VAL   A 1 23  ? 6.043  -12.718 3.508   1.00 12.55 ? 13  VAL   A CA  1 
ATOM   94   C C   . VAL   A 1 23  ? 4.991  -13.172 4.523   1.00 12.01 ? 13  VAL   A C   1 
ATOM   95   O O   . VAL   A 1 23  ? 5.364  -13.586 5.654   1.00 11.34 ? 13  VAL   A O   1 
ATOM   96   C CB  . VAL   A 1 23  ? 6.339  -11.215 3.583   1.00 12.05 ? 13  VAL   A CB  1 
ATOM   97   C CG1 . VAL   A 1 23  ? 6.787  -10.817 4.980   1.00 11.81 ? 13  VAL   A CG1 1 
ATOM   98   C CG2 . VAL   A 1 23  ? 7.386  -10.795 2.580   1.00 11.60 ? 13  VAL   A CG2 1 
ATOM   99   N N   . GLU   A 1 24  ? 3.710  -13.003 4.213   1.00 11.41 ? 14  GLU   A N   1 
ATOM   100  C CA  . GLU   A 1 24  ? 2.619  -13.433 5.117   1.00 11.74 ? 14  GLU   A CA  1 
ATOM   101  C C   . GLU   A 1 24  ? 2.875  -14.876 5.599   1.00 12.60 ? 14  GLU   A C   1 
ATOM   102  O O   . GLU   A 1 24  ? 2.660  -15.174 6.787   1.00 11.86 ? 14  GLU   A O   1 
ATOM   103  C CB  . GLU   A 1 24  ? 1.294  -13.371 4.362   1.00 11.61 ? 14  GLU   A CB  1 
ATOM   104  C CG  . GLU   A 1 24  ? 0.795  -11.965 4.133   1.00 11.59 ? 14  GLU   A CG  1 
ATOM   105  C CD  . GLU   A 1 24  ? -0.440 -11.971 3.273   1.00 11.30 ? 14  GLU   A CD  1 
ATOM   106  O OE1 . GLU   A 1 24  ? -1.325 -12.739 3.612   1.00 13.47 ? 14  GLU   A OE1 1 
ATOM   107  O OE2 . GLU   A 1 24  ? -0.475 -11.250 2.286   1.00 11.28 ? 14  GLU   A OE2 1 
ATOM   108  N N   . GLY   A 1 25  ? 3.314  -15.762 4.688   1.00 12.59 ? 15  GLY   A N   1 
ATOM   109  C CA  . GLY   A 1 25  ? 3.565  -17.184 4.995   1.00 12.35 ? 15  GLY   A CA  1 
ATOM   110  C C   . GLY   A 1 25  ? 4.753  -17.401 5.931   1.00 12.33 ? 15  GLY   A C   1 
ATOM   111  O O   . GLY   A 1 25  ? 4.946  -18.547 6.340   1.00 13.55 ? 15  GLY   A O   1 
ATOM   112  N N   . CYS   A 1 26  ? 5.539  -16.360 6.229   1.00 11.13 ? 16  CYS   A N   1 
ATOM   113  C CA  . CYS   A 1 26  ? 6.725  -16.455 7.106   1.00 11.53 ? 16  CYS   A CA  1 
ATOM   114  C C   . CYS   A 1 26  ? 6.426  -15.853 8.476   1.00 11.45 ? 16  CYS   A C   1 
ATOM   115  O O   . CYS   A 1 26  ? 7.330  -15.880 9.341   1.00 10.31 ? 16  CYS   A O   1 
ATOM   116  C CB  . CYS   A 1 26  ? 7.935  -15.753 6.506   1.00 11.08 ? 16  CYS   A CB  1 
ATOM   117  S SG  . CYS   A 1 26  ? 8.378  -16.354 4.848   1.00 13.28 ? 16  CYS   A SG  1 
ATOM   118  N N   . MET   A 1 27  ? 5.242  -15.291 8.691   1.00 10.57 ? 17  MET   A N   1 
ATOM   119  C CA  . MET   A 1 27  ? 5.034  -14.571 9.958   1.00 10.74 ? 17  MET   A CA  1 
ATOM   120  C C   . MET   A 1 27  ? 4.563  -15.546 11.026  1.00 10.65 ? 17  MET   A C   1 
ATOM   121  O O   . MET   A 1 27  ? 3.677  -16.377 10.778  1.00 10.52 ? 17  MET   A O   1 
ATOM   122  C CB  . MET   A 1 27  ? 4.061  -13.402 9.813   1.00 11.64 ? 17  MET   A CB  1 
ATOM   123  C CG  . MET   A 1 27  ? 4.560  -12.339 8.789   1.00 11.54 ? 17  MET   A CG  1 
ATOM   124  S SD  . MET   A 1 27  ? 6.256  -11.739 9.045   1.00 12.38 ? 17  MET   A SD  1 
ATOM   125  C CE  . MET   A 1 27  ? 6.180  -11.166 10.737  1.00 12.74 ? 17  MET   A CE  1 
ATOM   126  N N   . VAL   A 1 28  ? 5.160  -15.394 12.197  1.00 9.68  ? 18  VAL   A N   1 
ATOM   127  C CA  . VAL   A 1 28  ? 4.841  -16.193 13.398  1.00 9.72  ? 18  VAL   A CA  1 
ATOM   128  C C   . VAL   A 1 28  ? 4.809  -15.255 14.587  1.00 10.08 ? 18  VAL   A C   1 
ATOM   129  O O   . VAL   A 1 28  ? 5.286  -14.108 14.503  1.00 9.66  ? 18  VAL   A O   1 
ATOM   130  C CB  . VAL   A 1 28  ? 5.839  -17.345 13.636  1.00 9.55  ? 18  VAL   A CB  1 
ATOM   131  C CG1 . VAL   A 1 28  ? 5.930  -18.270 12.443  1.00 9.27  ? 18  VAL   A CG1 1 
ATOM   132  C CG2 . VAL   A 1 28  ? 7.226  -16.905 14.020  1.00 9.40  ? 18  VAL   A CG2 1 
ATOM   133  N N   A GLN   A 1 29  ? 4.292  -15.784 15.679  0.50 9.78  ? 19  GLN   A N   1 
ATOM   134  N N   B GLN   A 1 29  ? 4.282  -15.754 15.691  0.50 10.16 ? 19  GLN   A N   1 
ATOM   135  C CA  A GLN   A 1 29  ? 4.223  -15.097 16.980  0.50 10.46 ? 19  GLN   A CA  1 
ATOM   136  C CA  B GLN   A 1 29  ? 4.246  -15.002 16.960  0.50 11.16 ? 19  GLN   A CA  1 
ATOM   137  C C   A GLN   A 1 29  ? 5.309  -15.679 17.876  0.50 10.60 ? 19  GLN   A C   1 
ATOM   138  C C   B GLN   A 1 29  ? 5.230  -15.656 17.926  0.50 10.99 ? 19  GLN   A C   1 
ATOM   139  O O   A GLN   A 1 29  ? 5.549  -16.908 17.808  0.50 10.76 ? 19  GLN   A O   1 
ATOM   140  O O   B GLN   A 1 29  ? 5.330  -16.901 17.949  0.50 11.21 ? 19  GLN   A O   1 
ATOM   141  C CB  A GLN   A 1 29  ? 2.836  -15.268 17.574  0.50 10.84 ? 19  GLN   A CB  1 
ATOM   142  C CB  B GLN   A 1 29  ? 2.822  -14.903 17.488  0.50 12.03 ? 19  GLN   A CB  1 
ATOM   143  C CG  A GLN   A 1 29  ? 2.724  -14.730 18.986  0.50 11.06 ? 19  GLN   A CG  1 
ATOM   144  C CG  B GLN   A 1 29  ? 2.313  -16.179 18.123  0.50 12.93 ? 19  GLN   A CG  1 
ATOM   145  C CD  A GLN   A 1 29  ? 1.384  -15.149 19.517  0.50 11.91 ? 19  GLN   A CD  1 
ATOM   146  C CD  B GLN   A 1 29  ? 1.036  -15.894 18.869  0.50 13.74 ? 19  GLN   A CD  1 
ATOM   147  O OE1 A GLN   A 1 29  ? 0.373  -14.527 19.214  0.50 12.50 ? 19  GLN   A OE1 1 
ATOM   148  O OE1 B GLN   A 1 29  ? -0.048 -16.212 18.402  0.50 15.20 ? 19  GLN   A OE1 1 
ATOM   149  N NE2 A GLN   A 1 29  ? 1.368  -16.253 20.252  0.50 12.13 ? 19  GLN   A NE2 1 
ATOM   150  N NE2 B GLN   A 1 29  ? 1.155  -15.229 20.009  0.50 14.92 ? 19  GLN   A NE2 1 
ATOM   151  N N   . VAL   A 1 30  ? 5.956  -14.811 18.650  1.00 10.91 ? 20  VAL   A N   1 
ATOM   152  C CA  . VAL   A 1 30  ? 7.009  -15.211 19.608  1.00 10.51 ? 20  VAL   A CA  1 
ATOM   153  C C   . VAL   A 1 30  ? 6.621  -14.573 20.925  1.00 10.91 ? 20  VAL   A C   1 
ATOM   154  O O   . VAL   A 1 30  ? 6.476  -13.352 20.959  1.00 11.79 ? 20  VAL   A O   1 
ATOM   155  C CB  . VAL   A 1 30  ? 8.406  -14.752 19.164  1.00 10.16 ? 20  VAL   A CB  1 
ATOM   156  C CG1 . VAL   A 1 30  ? 9.451  -15.280 20.129  1.00 10.62 ? 20  VAL   A CG1 1 
ATOM   157  C CG2 . VAL   A 1 30  ? 8.719  -15.186 17.729  1.00 10.21 ? 20  VAL   A CG2 1 
ATOM   158  N N   . THR   A 1 31  ? 6.538  -15.387 21.961  1.00 11.67 ? 21  THR   A N   1 
ATOM   159  C CA  . THR   A 1 31  ? 6.321  -14.950 23.351  1.00 13.65 ? 21  THR   A CA  1 
ATOM   160  C C   . THR   A 1 31  ? 7.485  -15.452 24.198  1.00 13.83 ? 21  THR   A C   1 
ATOM   161  O O   . THR   A 1 31  ? 7.797  -16.664 24.110  1.00 13.14 ? 21  THR   A O   1 
ATOM   162  C CB  . THR   A 1 31  ? 4.994  -15.499 23.873  1.00 15.43 ? 21  THR   A CB  1 
ATOM   163  O OG1 . THR   A 1 31  ? 3.973  -15.133 22.947  1.00 15.27 ? 21  THR   A OG1 1 
ATOM   164  C CG2 . THR   A 1 31  ? 4.672  -15.019 25.270  1.00 16.43 ? 21  THR   A CG2 1 
ATOM   165  N N   . CYS   A 1 32  ? 8.021  -14.582 25.032  1.00 14.50 ? 22  CYS   A N   1 
ATOM   166  C CA  . CYS   A 1 32  ? 8.980  -14.927 26.095  1.00 17.74 ? 22  CYS   A CA  1 
ATOM   167  C C   . CYS   A 1 32  ? 8.477  -14.228 27.367  1.00 19.50 ? 22  CYS   A C   1 
ATOM   168  O O   . CYS   A 1 32  ? 8.249  -13.030 27.312  1.00 20.96 ? 22  CYS   A O   1 
ATOM   169  C CB  . CYS   A 1 32  ? 10.388 -14.545 25.652  1.00 18.71 ? 22  CYS   A CB  1 
ATOM   170  S SG  . CYS   A 1 32  ? 11.693 -15.212 26.718  1.00 20.26 ? 22  CYS   A SG  1 
ATOM   171  N N   . GLY   A 1 33  ? 8.223  -14.965 28.443  1.00 24.28 ? 23  GLY   A N   1 
ATOM   172  C CA  . GLY   A 1 33  ? 7.524  -14.426 29.630  1.00 27.74 ? 23  GLY   A CA  1 
ATOM   173  C C   . GLY   A 1 33  ? 6.171  -13.855 29.234  1.00 30.05 ? 23  GLY   A C   1 
ATOM   174  O O   . GLY   A 1 33  ? 5.355  -14.611 28.658  1.00 34.50 ? 23  GLY   A O   1 
ATOM   175  N N   . THR   A 1 34  ? 5.947  -12.558 29.444  1.00 30.06 ? 24  THR   A N   1 
ATOM   176  C CA  . THR   A 1 34  ? 4.632  -11.908 29.156  1.00 33.35 ? 24  THR   A CA  1 
ATOM   177  C C   . THR   A 1 34  ? 4.708  -11.080 27.868  1.00 28.39 ? 24  THR   A C   1 
ATOM   178  O O   . THR   A 1 34  ? 3.683  -10.551 27.465  1.00 31.88 ? 24  THR   A O   1 
ATOM   179  C CB  . THR   A 1 34  ? 4.141  -11.026 30.320  1.00 34.10 ? 24  THR   A CB  1 
ATOM   180  O OG1 . THR   A 1 34  ? 5.274  -10.404 30.927  1.00 31.91 ? 24  THR   A OG1 1 
ATOM   181  C CG2 . THR   A 1 34  ? 3.329  -11.797 31.340  1.00 36.60 ? 24  THR   A CG2 1 
ATOM   182  N N   . THR   A 1 35  ? 5.878  -10.985 27.244  1.00 26.15 ? 25  THR   A N   1 
ATOM   183  C CA  . THR   A 1 35  ? 6.123  -10.119 26.059  1.00 23.43 ? 25  THR   A CA  1 
ATOM   184  C C   . THR   A 1 35  ? 5.800  -10.920 24.801  1.00 17.67 ? 25  THR   A C   1 
ATOM   185  O O   . THR   A 1 35  ? 6.365  -12.016 24.666  1.00 21.03 ? 25  THR   A O   1 
ATOM   186  C CB  . THR   A 1 35  ? 7.573  -9.611  26.080  1.00 24.56 ? 25  THR   A CB  1 
ATOM   187  O OG1 . THR   A 1 35  ? 7.769  -8.873  27.292  1.00 26.39 ? 25  THR   A OG1 1 
ATOM   188  C CG2 . THR   A 1 35  ? 7.940  -8.760  24.884  1.00 25.65 ? 25  THR   A CG2 1 
ATOM   189  N N   . THR   A 1 36  ? 4.910  -10.455 23.928  1.00 17.09 ? 26  THR   A N   1 
ATOM   190  C CA  . THR   A 1 36  ? 4.607  -11.127 22.622  1.00 14.76 ? 26  THR   A CA  1 
ATOM   191  C C   . THR   A 1 36  ? 4.960  -10.170 21.481  1.00 13.43 ? 26  THR   A C   1 
ATOM   192  O O   . THR   A 1 36  ? 4.633  -8.974  21.577  1.00 14.12 ? 26  THR   A O   1 
ATOM   193  C CB  . THR   A 1 36  ? 3.161  -11.622 22.488  1.00 15.34 ? 26  THR   A CB  1 
ATOM   194  O OG1 . THR   A 1 36  ? 2.992  -12.744 23.361  1.00 16.75 ? 26  THR   A OG1 1 
ATOM   195  C CG2 . THR   A 1 36  ? 2.837  -12.093 21.096  1.00 14.84 ? 26  THR   A CG2 1 
ATOM   196  N N   . LEU   A 1 37  ? 5.716  -10.640 20.504  1.00 11.81 ? 27  LEU   A N   1 
ATOM   197  C CA  . LEU   A 1 37  ? 5.926  -9.844  19.272  1.00 10.96 ? 27  LEU   A CA  1 
ATOM   198  C C   . LEU   A 1 37  ? 5.999  -10.821 18.101  1.00 9.62  ? 27  LEU   A C   1 
ATOM   199  O O   . LEU   A 1 37  ? 5.587  -11.956 18.269  1.00 9.71  ? 27  LEU   A O   1 
ATOM   200  C CB  . LEU   A 1 37  ? 7.126  -8.900  19.399  1.00 11.60 ? 27  LEU   A CB  1 
ATOM   201  C CG  . LEU   A 1 37  ? 8.386  -9.468  20.026  1.00 11.70 ? 27  LEU   A CG  1 
ATOM   202  C CD1 . LEU   A 1 37  ? 8.904  -10.633 19.213  1.00 12.87 ? 27  LEU   A CD1 1 
ATOM   203  C CD2 . LEU   A 1 37  ? 9.453  -8.398  20.199  1.00 11.80 ? 27  LEU   A CD2 1 
ATOM   204  N N   . ASN   A 1 38  ? 6.384  -10.329 16.928  1.00 9.50  ? 28  ASN   A N   1 
ATOM   205  C CA  . ASN   A 1 38  ? 6.352  -11.127 15.686  1.00 9.20  ? 28  ASN   A CA  1 
ATOM   206  C C   . ASN   A 1 38  ? 7.733  -11.704 15.411  1.00 9.20  ? 28  ASN   A C   1 
ATOM   207  O O   . ASN   A 1 38  ? 8.728  -11.083 15.762  1.00 8.84  ? 28  ASN   A O   1 
ATOM   208  C CB  . ASN   A 1 38  ? 5.915  -10.280 14.493  1.00 9.44  ? 28  ASN   A CB  1 
ATOM   209  C CG  . ASN   A 1 38  ? 4.596  -9.565  14.740  1.00 9.83  ? 28  ASN   A CG  1 
ATOM   210  O OD1 . ASN   A 1 38  ? 3.520  -10.174 14.656  1.00 9.23  ? 28  ASN   A OD1 1 
ATOM   211  N ND2 . ASN   A 1 38  ? 4.687  -8.304  15.146  1.00 9.92  ? 28  ASN   A ND2 1 
ATOM   212  N N   . GLY   A 1 39  ? 7.764  -12.824 14.706  1.00 8.91  ? 29  GLY   A N   1 
ATOM   213  C CA  . GLY   A 1 39  ? 9.026  -13.349 14.189  1.00 9.50  ? 29  GLY   A CA  1 
ATOM   214  C C   . GLY   A 1 39  ? 8.890  -13.663 12.711  1.00 9.14  ? 29  GLY   A C   1 
ATOM   215  O O   . GLY   A 1 39  ? 7.780  -13.766 12.233  1.00 8.50  ? 29  GLY   A O   1 
ATOM   216  N N   . LEU   A 1 40  ? 10.018 -13.846 12.046  1.00 9.60  ? 30  LEU   A N   1 
ATOM   217  C CA  . LEU   A 1 40  ? 10.069 -14.212 10.615  1.00 9.75  ? 30  LEU   A CA  1 
ATOM   218  C C   . LEU   A 1 40  ? 10.645 -15.629 10.519  1.00 9.70  ? 30  LEU   A C   1 
ATOM   219  O O   . LEU   A 1 40  ? 11.829 -15.821 10.951  1.00 9.19  ? 30  LEU   A O   1 
ATOM   220  C CB  . LEU   A 1 40  ? 10.972 -13.199 9.919   1.00 9.78  ? 30  LEU   A CB  1 
ATOM   221  C CG  . LEU   A 1 40  ? 11.065 -13.379 8.403   1.00 9.71  ? 30  LEU   A CG  1 
ATOM   222  C CD1 . LEU   A 1 40  ? 9.797  -12.890 7.745   1.00 10.54 ? 30  LEU   A CD1 1 
ATOM   223  C CD2 . LEU   A 1 40  ? 12.274 -12.652 7.857   1.00 10.03 ? 30  LEU   A CD2 1 
ATOM   224  N N   . TRP   A 1 41  ? 9.850  -16.591 10.038  1.00 9.23  ? 31  TRP   A N   1 
ATOM   225  C CA  . TRP   A 1 41  ? 10.233 -18.026 9.959   1.00 8.84  ? 31  TRP   A CA  1 
ATOM   226  C C   . TRP   A 1 41  ? 10.712 -18.333 8.529   1.00 8.83  ? 31  TRP   A C   1 
ATOM   227  O O   . TRP   A 1 41  ? 9.899  -18.214 7.581   1.00 8.24  ? 31  TRP   A O   1 
ATOM   228  C CB  . TRP   A 1 41  ? 9.055  -18.881 10.418  1.00 9.02  ? 31  TRP   A CB  1 
ATOM   229  C CG  . TRP   A 1 41  ? 9.236  -20.368 10.406  1.00 9.73  ? 31  TRP   A CG  1 
ATOM   230  C CD1 . TRP   A 1 41  ? 10.378 -21.101 10.478  1.00 9.21  ? 31  TRP   A CD1 1 
ATOM   231  C CD2 . TRP   A 1 41  ? 8.163  -21.318 10.332  1.00 9.96  ? 31  TRP   A CD2 1 
ATOM   232  N NE1 . TRP   A 1 41  ? 10.085 -22.436 10.496  1.00 9.46  ? 31  TRP   A NE1 1 
ATOM   233  C CE2 . TRP   A 1 41  ? 8.733  -22.607 10.443  1.00 10.10 ? 31  TRP   A CE2 1 
ATOM   234  C CE3 . TRP   A 1 41  ? 6.776  -21.201 10.279  1.00 11.18 ? 31  TRP   A CE3 1 
ATOM   235  C CZ2 . TRP   A 1 41  ? 7.961  -23.770 10.377  1.00 10.37 ? 31  TRP   A CZ2 1 
ATOM   236  C CZ3 . TRP   A 1 41  ? 6.005  -22.348 10.237  1.00 11.41 ? 31  TRP   A CZ3 1 
ATOM   237  C CH2 . TRP   A 1 41  ? 6.597  -23.617 10.274  1.00 11.22 ? 31  TRP   A CH2 1 
ATOM   238  N N   . LEU   A 1 42  ? 12.005 -18.588 8.382   1.00 8.78  ? 32  LEU   A N   1 
ATOM   239  C CA  . LEU   A 1 42  ? 12.656 -18.890 7.078   1.00 10.17 ? 32  LEU   A CA  1 
ATOM   240  C C   . LEU   A 1 42  ? 13.460 -20.168 7.265   1.00 10.53 ? 32  LEU   A C   1 
ATOM   241  O O   . LEU   A 1 42  ? 14.323 -20.176 8.158   1.00 10.81 ? 32  LEU   A O   1 
ATOM   242  C CB  . LEU   A 1 42  ? 13.581 -17.746 6.652   1.00 10.64 ? 32  LEU   A CB  1 
ATOM   243  C CG  . LEU   A 1 42  ? 12.938 -16.377 6.461   1.00 10.97 ? 32  LEU   A CG  1 
ATOM   244  C CD1 . LEU   A 1 42  ? 13.966 -15.333 6.076   1.00 10.11 ? 32  LEU   A CD1 1 
ATOM   245  C CD2 . LEU   A 1 42  ? 11.847 -16.427 5.411   1.00 10.36 ? 32  LEU   A CD2 1 
ATOM   246  N N   . ASP   A 1 43  ? 13.196 -21.202 6.454   1.00 11.91 ? 33  ASP   A N   1 
ATOM   247  C CA  . ASP   A 1 43  ? 13.842 -22.520 6.670   1.00 12.26 ? 33  ASP   A CA  1 
ATOM   248  C C   . ASP   A 1 43  ? 13.562 -22.878 8.132   1.00 11.30 ? 33  ASP   A C   1 
ATOM   249  O O   . ASP   A 1 43  ? 12.431 -22.720 8.551   1.00 11.67 ? 33  ASP   A O   1 
ATOM   250  C CB  . ASP   A 1 43  ? 15.335 -22.461 6.334   1.00 13.48 ? 33  ASP   A CB  1 
ATOM   251  C CG  . ASP   A 1 43  ? 15.623 -21.963 4.928   1.00 14.59 ? 33  ASP   A CG  1 
ATOM   252  O OD1 . ASP   A 1 43  ? 14.829 -22.278 4.044   1.00 16.35 ? 33  ASP   A OD1 1 
ATOM   253  O OD2 . ASP   A 1 43  ? 16.600 -21.202 4.762   1.00 15.14 ? 33  ASP   A OD2 1 
ATOM   254  N N   . ASP   A 1 44  ? 14.551 -23.331 8.891   1.00 10.78 ? 34  ASP   A N   1 
ATOM   255  C CA  . ASP   A 1 44  ? 14.304 -23.811 10.272  1.00 11.08 ? 34  ASP   A CA  1 
ATOM   256  C C   . ASP   A 1 44  ? 14.731 -22.753 11.296  1.00 10.60 ? 34  ASP   A C   1 
ATOM   257  O O   . ASP   A 1 44  ? 15.051 -23.124 12.414  1.00 10.46 ? 34  ASP   A O   1 
ATOM   258  C CB  . ASP   A 1 44  ? 14.987 -25.156 10.512  1.00 12.31 ? 34  ASP   A CB  1 
ATOM   259  C CG  . ASP   A 1 44  ? 16.494 -25.139 10.411  1.00 13.06 ? 34  ASP   A CG  1 
ATOM   260  O OD1 . ASP   A 1 44  ? 17.051 -24.134 9.944   1.00 12.82 ? 34  ASP   A OD1 1 
ATOM   261  O OD2 . ASP   A 1 44  ? 17.091 -26.147 10.813  1.00 15.36 ? 34  ASP   A OD2 1 
ATOM   262  N N   . VAL   A 1 45  ? 14.667 -21.474 10.956  1.00 10.02 ? 35  VAL   A N   1 
ATOM   263  C CA  . VAL   A 1 45  ? 15.062 -20.370 11.879  1.00 10.09 ? 35  VAL   A CA  1 
ATOM   264  C C   . VAL   A 1 45  ? 13.936 -19.337 11.992  1.00 9.82  ? 35  VAL   A C   1 
ATOM   265  O O   . VAL   A 1 45  ? 13.345 -18.948 10.977  1.00 9.02  ? 35  VAL   A O   1 
ATOM   266  C CB  . VAL   A 1 45  ? 16.372 -19.708 11.404  1.00 10.42 ? 35  VAL   A CB  1 
ATOM   267  C CG1 . VAL   A 1 45  ? 16.769 -18.544 12.293  1.00 10.86 ? 35  VAL   A CG1 1 
ATOM   268  C CG2 . VAL   A 1 45  ? 17.498 -20.715 11.285  1.00 11.33 ? 35  VAL   A CG2 1 
ATOM   269  N N   . VAL   A 1 46  ? 13.671 -18.888 13.218  1.00 9.84  ? 36  VAL   A N   1 
ATOM   270  C CA  . VAL   A 1 46  ? 12.765 -17.738 13.453  1.00 9.45  ? 36  VAL   A CA  1 
ATOM   271  C C   . VAL   A 1 46  ? 13.623 -16.569 13.927  1.00 9.21  ? 36  VAL   A C   1 
ATOM   272  O O   . VAL   A 1 46  ? 14.399 -16.705 14.925  1.00 9.56  ? 36  VAL   A O   1 
ATOM   273  C CB  . VAL   A 1 46  ? 11.653 -18.109 14.447  1.00 9.69  ? 36  VAL   A CB  1 
ATOM   274  C CG1 . VAL   A 1 46  ? 10.813 -16.882 14.794  1.00 9.05  ? 36  VAL   A CG1 1 
ATOM   275  C CG2 . VAL   A 1 46  ? 10.791 -19.233 13.892  1.00 10.26 ? 36  VAL   A CG2 1 
ATOM   276  N N   . TYR   A 1 47  ? 13.533 -15.447 13.225  1.00 9.07  ? 37  TYR   A N   1 
ATOM   277  C CA  . TYR   A 1 47  ? 14.283 -14.213 13.549  1.00 9.32  ? 37  TYR   A CA  1 
ATOM   278  C C   . TYR   A 1 47  ? 13.320 -13.296 14.293  1.00 8.90  ? 37  TYR   A C   1 
ATOM   279  O O   . TYR   A 1 47  ? 12.171 -13.139 13.830  1.00 9.11  ? 37  TYR   A O   1 
ATOM   280  C CB  . TYR   A 1 47  ? 14.793 -13.535 12.275  1.00 9.25  ? 37  TYR   A CB  1 
ATOM   281  C CG  . TYR   A 1 47  ? 15.666 -14.433 11.428  1.00 10.05 ? 37  TYR   A CG  1 
ATOM   282  C CD1 . TYR   A 1 47  ? 15.118 -15.411 10.632  1.00 10.39 ? 37  TYR   A CD1 1 
ATOM   283  C CD2 . TYR   A 1 47  ? 17.041 -14.332 11.470  1.00 10.18 ? 37  TYR   A CD2 1 
ATOM   284  C CE1 . TYR   A 1 47  ? 15.916 -16.253 9.872   1.00 10.75 ? 37  TYR   A CE1 1 
ATOM   285  C CE2 . TYR   A 1 47  ? 17.855 -15.142 10.700  1.00 10.51 ? 37  TYR   A CE2 1 
ATOM   286  C CZ  . TYR   A 1 47  ? 17.283 -16.073 9.861   1.00 10.12 ? 37  TYR   A CZ  1 
ATOM   287  O OH  . TYR   A 1 47  ? 18.068 -16.962 9.177   1.00 12.07 ? 37  TYR   A OH  1 
ATOM   288  N N   . CYS   A 1 48  ? 13.730 -12.717 15.412  1.00 9.25  ? 38  CYS   A N   1 
ATOM   289  C CA  . CYS   A 1 48  ? 12.841 -11.767 16.126  1.00 9.05  ? 38  CYS   A CA  1 
ATOM   290  C C   . CYS   A 1 48  ? 13.704 -10.776 16.902  1.00 8.80  ? 38  CYS   A C   1 
ATOM   291  O O   . CYS   A 1 48  ? 14.915 -11.000 17.102  1.00 9.02  ? 38  CYS   A O   1 
ATOM   292  C CB  . CYS   A 1 48  ? 11.812 -12.476 17.007  1.00 9.01  ? 38  CYS   A CB  1 
ATOM   293  S SG  . CYS   A 1 48  ? 12.530 -13.128 18.539  1.00 10.65 ? 38  CYS   A SG  1 
ATOM   294  N N   . PRO   A 1 49  ? 13.144 -9.610  17.300  1.00 8.10  ? 39  PRO   A N   1 
ATOM   295  C CA  . PRO   A 1 49  ? 13.885 -8.629  18.085  1.00 8.27  ? 39  PRO   A CA  1 
ATOM   296  C C   . PRO   A 1 49  ? 14.256 -9.236  19.440  1.00 8.43  ? 39  PRO   A C   1 
ATOM   297  O O   . PRO   A 1 49  ? 13.446 -9.928  20.011  1.00 8.81  ? 39  PRO   A O   1 
ATOM   298  C CB  . PRO   A 1 49  ? 12.904 -7.472  18.266  1.00 8.52  ? 39  PRO   A CB  1 
ATOM   299  C CG  . PRO   A 1 49  ? 11.949 -7.637  17.093  1.00 8.13  ? 39  PRO   A CG  1 
ATOM   300  C CD  . PRO   A 1 49  ? 11.783 -9.139  16.974  1.00 8.23  ? 39  PRO   A CD  1 
ATOM   301  N N   . ARG   A 1 50  ? 15.485 -8.995  19.878  1.00 8.61  ? 40  ARG   A N   1 
ATOM   302  C CA  . ARG   A 1 50  ? 16.010 -9.591  21.123  1.00 8.37  ? 40  ARG   A CA  1 
ATOM   303  C C   . ARG   A 1 50  ? 15.225 -9.039  22.321  1.00 8.88  ? 40  ARG   A C   1 
ATOM   304  O O   . ARG   A 1 50  ? 15.175 -9.782  23.353  1.00 8.57  ? 40  ARG   A O   1 
ATOM   305  C CB  . ARG   A 1 50  ? 17.523 -9.355  21.203  1.00 8.01  ? 40  ARG   A CB  1 
ATOM   306  C CG  . ARG   A 1 50  ? 17.928 -7.900  21.387  1.00 7.97  ? 40  ARG   A CG  1 
ATOM   307  C CD  . ARG   A 1 50  ? 19.415 -7.854  21.635  1.00 7.84  ? 40  ARG   A CD  1 
ATOM   308  N NE  . ARG   A 1 50  ? 19.905 -6.492  21.651  1.00 8.23  ? 40  ARG   A NE  1 
ATOM   309  C CZ  . ARG   A 1 50  ? 21.151 -6.128  21.964  1.00 9.17  ? 40  ARG   A CZ  1 
ATOM   310  N NH1 . ARG   A 1 50  ? 22.047 -7.060  22.265  1.00 9.09  ? 40  ARG   A NH1 1 
ATOM   311  N NH2 . ARG   A 1 50  ? 21.475 -4.840  21.999  1.00 9.08  ? 40  ARG   A NH2 1 
ATOM   312  N N   . HIS   A 1 51  ? 14.542 -7.878  22.215  1.00 8.85  ? 41  HIS   A N   1 
ATOM   313  C CA  . HIS   A 1 51  ? 13.839 -7.284  23.391  1.00 9.89  ? 41  HIS   A CA  1 
ATOM   314  C C   . HIS   A 1 51  ? 12.566 -8.066  23.720  1.00 10.04 ? 41  HIS   A C   1 
ATOM   315  O O   . HIS   A 1 51  ? 11.952 -7.779  24.772  1.00 11.31 ? 41  HIS   A O   1 
ATOM   316  C CB  . HIS   A 1 51  ? 13.566 -5.774  23.289  1.00 9.45  ? 41  HIS   A CB  1 
ATOM   317  C CG  . HIS   A 1 51  ? 12.489 -5.374  22.339  1.00 9.98  ? 41  HIS   A CG  1 
ATOM   318  N ND1 . HIS   A 1 51  ? 12.767 -4.772  21.149  1.00 10.17 ? 41  HIS   A ND1 1 
ATOM   319  C CD2 . HIS   A 1 51  ? 11.134 -5.435  22.431  1.00 10.50 ? 41  HIS   A CD2 1 
ATOM   320  C CE1 . HIS   A 1 51  ? 11.628 -4.490  20.518  1.00 10.36 ? 41  HIS   A CE1 1 
ATOM   321  N NE2 . HIS   A 1 51  ? 10.601 -4.865  21.308  1.00 10.44 ? 41  HIS   A NE2 1 
ATOM   322  N N   . VAL   A 1 52  ? 12.289 -9.148  22.989  1.00 10.16 ? 42  VAL   A N   1 
ATOM   323  C CA  . VAL   A 1 52  ? 11.230 -10.101 23.434  1.00 9.53  ? 42  VAL   A CA  1 
ATOM   324  C C   . VAL   A 1 52  ? 11.541 -10.642 24.840  1.00 10.56 ? 42  VAL   A C   1 
ATOM   325  O O   . VAL   A 1 52  ? 10.609 -11.079 25.522  1.00 10.19 ? 42  VAL   A O   1 
ATOM   326  C CB  . VAL   A 1 52  ? 11.003 -11.232 22.418  1.00 9.67  ? 42  VAL   A CB  1 
ATOM   327  C CG1 . VAL   A 1 52  ? 12.074 -12.313 22.446  1.00 9.52  ? 42  VAL   A CG1 1 
ATOM   328  C CG2 . VAL   A 1 52  ? 9.608  -11.832 22.600  1.00 9.50  ? 42  VAL   A CG2 1 
ATOM   329  N N   . ILE   A 1 53  ? 12.809 -10.709 25.256  1.00 10.23 ? 43  ILE   A N   1 
ATOM   330  C CA  . ILE   A 1 53  ? 13.192 -11.341 26.551  1.00 10.83 ? 43  ILE   A CA  1 
ATOM   331  C C   . ILE   A 1 53  ? 13.005 -10.337 27.685  1.00 12.01 ? 43  ILE   A C   1 
ATOM   332  O O   . ILE   A 1 53  ? 13.206 -10.734 28.844  1.00 14.17 ? 43  ILE   A O   1 
ATOM   333  C CB  . ILE   A 1 53  ? 14.654 -11.838 26.519  1.00 10.79 ? 43  ILE   A CB  1 
ATOM   334  C CG1 . ILE   A 1 53  ? 15.655 -10.687 26.401  1.00 10.80 ? 43  ILE   A CG1 1 
ATOM   335  C CG2 . ILE   A 1 53  ? 14.809 -12.859 25.418  1.00 11.35 ? 43  ILE   A CG2 1 
ATOM   336  C CD1 . ILE   A 1 53  ? 17.134 -11.117 26.356  1.00 11.24 ? 43  ILE   A CD1 1 
ATOM   337  N N   . CYS   A 1 54  ? 12.716 -9.081  27.387  1.00 12.80 ? 44  CYS   A N   1 
ATOM   338  C CA  . CYS   A 1 54  ? 12.676 -8.006  28.407  1.00 14.56 ? 44  CYS   A CA  1 
ATOM   339  C C   . CYS   A 1 54  ? 11.282 -7.861  29.014  1.00 16.68 ? 44  CYS   A C   1 
ATOM   340  O O   . CYS   A 1 54  ? 10.282 -7.940  28.266  1.00 18.32 ? 44  CYS   A O   1 
ATOM   341  C CB  . CYS   A 1 54  ? 13.041 -6.663  27.805  1.00 14.31 ? 44  CYS   A CB  1 
ATOM   342  S SG  . CYS   A 1 54  ? 14.750 -6.574  27.251  1.00 14.67 ? 44  CYS   A SG  1 
ATOM   343  N N   . THR   A 1 55  ? 11.261 -7.639  30.330  1.00 21.34 ? 45  THR   A N   1 
ATOM   344  C CA  . THR   A 1 55  ? 10.161 -6.990  31.085  1.00 24.51 ? 45  THR   A CA  1 
ATOM   345  C C   . THR   A 1 55  ? 10.136 -5.520  30.673  1.00 26.51 ? 45  THR   A C   1 
ATOM   346  O O   . THR   A 1 55  ? 11.202 -5.007  30.229  1.00 24.90 ? 45  THR   A O   1 
ATOM   347  C CB  . THR   A 1 55  ? 10.370 -7.132  32.601  1.00 26.45 ? 45  THR   A CB  1 
ATOM   348  O OG1 . THR   A 1 55  ? 11.470 -6.300  32.969  1.00 22.43 ? 45  THR   A OG1 1 
ATOM   349  C CG2 . THR   A 1 55  ? 10.662 -8.550  33.048  1.00 25.03 ? 45  THR   A CG2 1 
ATOM   350  N N   . SER   A 1 56  ? 8.992  -4.844  30.826  1.00 29.83 ? 46  SER   A N   1 
ATOM   351  C CA  . SER   A 1 56  ? 8.879  -3.377  30.592  1.00 32.35 ? 46  SER   A CA  1 
ATOM   352  C C   . SER   A 1 56  ? 10.015 -2.637  31.320  1.00 33.04 ? 46  SER   A C   1 
ATOM   353  O O   . SER   A 1 56  ? 10.631 -1.733  30.702  1.00 33.06 ? 46  SER   A O   1 
ATOM   354  C CB  . SER   A 1 56  ? 7.523  -2.852  31.002  1.00 31.84 ? 46  SER   A CB  1 
ATOM   355  O OG  . SER   A 1 56  ? 7.419  -2.875  32.415  1.00 38.50 ? 46  SER   A OG  1 
ATOM   356  N N   . GLU   A 1 57  ? 10.324 -3.035  32.563  1.00 32.36 ? 47  GLU   A N   1 
ATOM   357  C CA  . GLU   A 1 57  ? 11.378 -2.404  33.398  1.00 32.62 ? 47  GLU   A CA  1 
ATOM   358  C C   . GLU   A 1 57  ? 12.776 -2.645  32.805  1.00 30.46 ? 47  GLU   A C   1 
ATOM   359  O O   . GLU   A 1 57  ? 13.601 -1.702  32.811  1.00 29.53 ? 47  GLU   A O   1 
ATOM   360  C CB  . GLU   A 1 57  ? 11.337 -2.955  34.815  1.00 35.74 ? 47  GLU   A CB  1 
ATOM   361  C CG  . GLU   A 1 57  ? 12.515 -2.484  35.649  1.00 41.17 ? 47  GLU   A CG  1 
ATOM   362  C CD  . GLU   A 1 57  ? 12.341 -2.694  37.141  1.00 43.58 ? 47  GLU   A CD  1 
ATOM   363  O OE1 . GLU   A 1 57  ? 11.297 -3.264  37.528  1.00 42.47 ? 47  GLU   A OE1 1 
ATOM   364  O OE2 . GLU   A 1 57  ? 13.238 -2.270  37.907  1.00 44.55 ? 47  GLU   A OE2 1 
ATOM   365  N N   . ASP   A 1 58  ? 13.042 -3.870  32.350  1.00 25.96 ? 48  ASP   A N   1 
ATOM   366  C CA  . ASP   A 1 58  ? 14.317 -4.247  31.697  1.00 23.93 ? 48  ASP   A CA  1 
ATOM   367  C C   . ASP   A 1 58  ? 14.623 -3.275  30.560  1.00 22.09 ? 48  ASP   A C   1 
ATOM   368  O O   . ASP   A 1 58  ? 15.819 -2.975  30.343  1.00 21.05 ? 48  ASP   A O   1 
ATOM   369  C CB  . ASP   A 1 58  ? 14.238 -5.657  31.112  1.00 23.46 ? 48  ASP   A CB  1 
ATOM   370  C CG  . ASP   A 1 58  ? 14.312 -6.755  32.150  1.00 23.65 ? 48  ASP   A CG  1 
ATOM   371  O OD1 . ASP   A 1 58  ? 14.831 -6.490  33.253  1.00 26.06 ? 48  ASP   A OD1 1 
ATOM   372  O OD2 . ASP   A 1 58  ? 13.894 -7.858  31.834  1.00 21.84 ? 48  ASP   A OD2 1 
ATOM   373  N N   . MET   A 1 59  ? 13.583 -2.833  29.846  1.00 21.86 ? 49  MET   A N   1 
ATOM   374  C CA  . MET   A 1 59  ? 13.748 -2.056  28.591  1.00 22.03 ? 49  MET   A CA  1 
ATOM   375  C C   . MET   A 1 59  ? 14.376 -0.678  28.885  1.00 19.96 ? 49  MET   A C   1 
ATOM   376  O O   . MET   A 1 59  ? 15.001 -0.108  27.991  1.00 17.05 ? 49  MET   A O   1 
ATOM   377  C CB  . MET   A 1 59  ? 12.408 -1.958  27.848  1.00 24.84 ? 49  MET   A CB  1 
ATOM   378  C CG  . MET   A 1 59  ? 12.147 -3.186  26.979  1.00 24.45 ? 49  MET   A CG  1 
ATOM   379  S SD  . MET   A 1 59  ? 10.445 -3.360  26.485  1.00 37.78 ? 49  MET   A SD  1 
ATOM   380  C CE  . MET   A 1 59  ? 10.390 -5.115  26.118  1.00 37.87 ? 49  MET   A CE  1 
ATOM   381  N N   . LEU   A 1 60  ? 14.358 -0.189  30.129  1.00 20.80 ? 50  LEU   A N   1 
ATOM   382  C CA  . LEU   A 1 60  ? 14.960 1.129   30.461  1.00 20.44 ? 50  LEU   A CA  1 
ATOM   383  C C   . LEU   A 1 60  ? 16.498 1.087   30.339  1.00 20.19 ? 50  LEU   A C   1 
ATOM   384  O O   . LEU   A 1 60  ? 17.065 2.104   29.984  1.00 19.49 ? 50  LEU   A O   1 
ATOM   385  C CB  . LEU   A 1 60  ? 14.522 1.544   31.865  1.00 21.63 ? 50  LEU   A CB  1 
ATOM   386  C CG  . LEU   A 1 60  ? 13.029 1.791   32.050  1.00 24.81 ? 50  LEU   A CG  1 
ATOM   387  C CD1 . LEU   A 1 60  ? 12.750 2.122   33.513  1.00 23.76 ? 50  LEU   A CD1 1 
ATOM   388  C CD2 . LEU   A 1 60  ? 12.530 2.908   31.133  1.00 25.30 ? 50  LEU   A CD2 1 
ATOM   389  N N   . ASN   A 1 61  ? 17.141 -0.063  30.587  1.00 19.96 ? 51  ASN   A N   1 
ATOM   390  C CA  . ASN   A 1 61  ? 18.622 -0.200  30.631  1.00 20.01 ? 51  ASN   A CA  1 
ATOM   391  C C   . ASN   A 1 61  ? 19.024 -1.677  30.564  1.00 18.65 ? 51  ASN   A C   1 
ATOM   392  O O   . ASN   A 1 61  ? 19.661 -2.198  31.479  1.00 22.08 ? 51  ASN   A O   1 
ATOM   393  C CB  . ASN   A 1 61  ? 19.195 0.415   31.916  1.00 21.74 ? 51  ASN   A CB  1 
ATOM   394  C CG  . ASN   A 1 61  ? 20.708 0.528   31.890  1.00 24.25 ? 51  ASN   A CG  1 
ATOM   395  O OD1 . ASN   A 1 61  ? 21.329 0.511   30.825  1.00 26.35 ? 51  ASN   A OD1 1 
ATOM   396  N ND2 . ASN   A 1 61  ? 21.315 0.661   33.061  1.00 28.28 ? 51  ASN   A ND2 1 
ATOM   397  N N   . PRO   A 1 62  ? 18.682 -2.415  29.497  1.00 17.12 ? 52  PRO   A N   1 
ATOM   398  C CA  . PRO   A 1 62  ? 18.816 -3.877  29.498  1.00 16.59 ? 52  PRO   A CA  1 
ATOM   399  C C   . PRO   A 1 62  ? 20.263 -4.349  29.294  1.00 15.14 ? 52  PRO   A C   1 
ATOM   400  O O   . PRO   A 1 62  ? 20.988 -3.709  28.525  1.00 16.74 ? 52  PRO   A O   1 
ATOM   401  C CB  . PRO   A 1 62  ? 17.942 -4.317  28.320  1.00 16.20 ? 52  PRO   A CB  1 
ATOM   402  C CG  . PRO   A 1 62  ? 17.978 -3.121  27.378  1.00 17.38 ? 52  PRO   A CG  1 
ATOM   403  C CD  . PRO   A 1 62  ? 18.101 -1.896  28.249  1.00 17.67 ? 52  PRO   A CD  1 
ATOM   404  N N   . ASN   A 1 63  ? 20.665 -5.400  30.014  1.00 13.60 ? 53  ASN   A N   1 
ATOM   405  C CA  . ASN   A 1 63  ? 21.908 -6.159  29.715  1.00 13.97 ? 53  ASN   A CA  1 
ATOM   406  C C   . ASN   A 1 63  ? 21.458 -7.438  29.034  1.00 13.06 ? 53  ASN   A C   1 
ATOM   407  O O   . ASN   A 1 63  ? 21.120 -8.420  29.726  1.00 13.07 ? 53  ASN   A O   1 
ATOM   408  C CB  . ASN   A 1 63  ? 22.799 -6.433  30.933  1.00 14.39 ? 53  ASN   A CB  1 
ATOM   409  C CG  . ASN   A 1 63  ? 24.141 -7.012  30.547  1.00 14.77 ? 53  ASN   A CG  1 
ATOM   410  O OD1 . ASN   A 1 63  ? 24.227 -7.908  29.705  1.00 16.62 ? 53  ASN   A OD1 1 
ATOM   411  N ND2 . ASN   A 1 63  ? 25.208 -6.483  31.133  1.00 15.25 ? 53  ASN   A ND2 1 
ATOM   412  N N   . TYR   A 1 64  ? 21.414 -7.404  27.716  1.00 13.22 ? 54  TYR   A N   1 
ATOM   413  C CA  . TYR   A 1 64  ? 20.814 -8.498  26.928  1.00 14.38 ? 54  TYR   A CA  1 
ATOM   414  C C   . TYR   A 1 64  ? 21.569 -9.804  27.157  1.00 14.00 ? 54  TYR   A C   1 
ATOM   415  O O   . TYR   A 1 64  ? 20.943 -10.841 27.245  1.00 14.75 ? 54  TYR   A O   1 
ATOM   416  C CB  . TYR   A 1 64  ? 20.741 -8.109  25.455  1.00 13.55 ? 54  TYR   A CB  1 
ATOM   417  C CG  . TYR   A 1 64  ? 19.664 -7.101  25.147  1.00 13.06 ? 54  TYR   A CG  1 
ATOM   418  C CD1 . TYR   A 1 64  ? 18.338 -7.501  25.092  1.00 12.51 ? 54  TYR   A CD1 1 
ATOM   419  C CD2 . TYR   A 1 64  ? 19.935 -5.757  24.899  1.00 12.43 ? 54  TYR   A CD2 1 
ATOM   420  C CE1 . TYR   A 1 64  ? 17.316 -6.612  24.839  1.00 11.81 ? 54  TYR   A CE1 1 
ATOM   421  C CE2 . TYR   A 1 64  ? 18.918 -4.860  24.605  1.00 11.93 ? 54  TYR   A CE2 1 
ATOM   422  C CZ  . TYR   A 1 64  ? 17.595 -5.293  24.564  1.00 12.10 ? 54  TYR   A CZ  1 
ATOM   423  O OH  . TYR   A 1 64  ? 16.533 -4.467  24.292  1.00 11.29 ? 54  TYR   A OH  1 
ATOM   424  N N   . GLU   A 1 65  ? 22.896 -9.798  27.238  1.00 15.35 ? 55  GLU   A N   1 
ATOM   425  C CA  . GLU   A 1 65  ? 23.613 -11.082 27.445  1.00 14.68 ? 55  GLU   A CA  1 
ATOM   426  C C   . GLU   A 1 65  ? 23.200 -11.655 28.801  1.00 13.49 ? 55  GLU   A C   1 
ATOM   427  O O   . GLU   A 1 65  ? 22.942 -12.874 28.888  1.00 13.51 ? 55  GLU   A O   1 
ATOM   428  C CB  . GLU   A 1 65  ? 25.126 -10.886 27.278  1.00 17.06 ? 55  GLU   A CB  1 
ATOM   429  C CG  . GLU   A 1 65  ? 25.889 -12.201 27.083  1.00 19.31 ? 55  GLU   A CG  1 
ATOM   430  C CD  . GLU   A 1 65  ? 25.764 -12.903 25.736  1.00 21.46 ? 55  GLU   A CD  1 
ATOM   431  O OE1 . GLU   A 1 65  ? 25.432 -14.109 25.738  1.00 23.29 ? 55  GLU   A OE1 1 
ATOM   432  O OE2 . GLU   A 1 65  ? 26.093 -12.287 24.696  1.00 23.73 ? 55  GLU   A OE2 1 
ATOM   433  N N   . ASP   A 1 66  ? 23.157 -10.824 29.841  1.00 12.74 ? 56  ASP   A N   1 
ATOM   434  C CA  . ASP   A 1 66  ? 22.789 -11.252 31.216  1.00 14.27 ? 56  ASP   A CA  1 
ATOM   435  C C   . ASP   A 1 66  ? 21.343 -11.770 31.238  1.00 13.82 ? 56  ASP   A C   1 
ATOM   436  O O   . ASP   A 1 66  ? 21.080 -12.832 31.852  1.00 13.72 ? 56  ASP   A O   1 
ATOM   437  C CB  . ASP   A 1 66  ? 22.993 -10.106 32.202  1.00 14.71 ? 56  ASP   A CB  1 
ATOM   438  C CG  . ASP   A 1 66  ? 24.439 -9.879  32.594  1.00 16.68 ? 56  ASP   A CG  1 
ATOM   439  O OD1 . ASP   A 1 66  ? 25.353 -10.628 32.078  1.00 16.24 ? 56  ASP   A OD1 1 
ATOM   440  O OD2 . ASP   A 1 66  ? 24.650 -8.967  33.396  1.00 17.91 ? 56  ASP   A OD2 1 
ATOM   441  N N   . LEU   A 1 67  ? 20.419 -11.039 30.602  1.00 15.48 ? 57  LEU   A N   1 
ATOM   442  C CA  . LEU   A 1 67  ? 18.979 -11.426 30.541  1.00 15.33 ? 57  LEU   A CA  1 
ATOM   443  C C   . LEU   A 1 67  ? 18.837 -12.782 29.852  1.00 16.32 ? 57  LEU   A C   1 
ATOM   444  O O   . LEU   A 1 67  ? 18.006 -13.597 30.294  1.00 16.51 ? 57  LEU   A O   1 
ATOM   445  C CB  . LEU   A 1 67  ? 18.177 -10.328 29.845  1.00 15.69 ? 57  LEU   A CB  1 
ATOM   446  C CG  . LEU   A 1 67  ? 18.130 -9.001  30.614  1.00 16.79 ? 57  LEU   A CG  1 
ATOM   447  C CD1 . LEU   A 1 67  ? 17.415 -7.904  29.823  1.00 17.64 ? 57  LEU   A CD1 1 
ATOM   448  C CD2 . LEU   A 1 67  ? 17.505 -9.189  31.972  1.00 16.45 ? 57  LEU   A CD2 1 
ATOM   449  N N   . LEU   A 1 68  ? 19.629 -13.020 28.811  1.00 16.76 ? 58  LEU   A N   1 
ATOM   450  C CA  . LEU   A 1 68  ? 19.504 -14.239 27.967  1.00 18.37 ? 58  LEU   A CA  1 
ATOM   451  C C   . LEU   A 1 68  ? 19.963 -15.482 28.737  1.00 19.08 ? 58  LEU   A C   1 
ATOM   452  O O   . LEU   A 1 68  ? 19.394 -16.545 28.449  1.00 18.99 ? 58  LEU   A O   1 
ATOM   453  C CB  . LEU   A 1 68  ? 20.293 -14.001 26.676  1.00 18.43 ? 58  LEU   A CB  1 
ATOM   454  C CG  . LEU   A 1 68  ? 19.974 -14.875 25.470  1.00 18.54 ? 58  LEU   A CG  1 
ATOM   455  C CD1 . LEU   A 1 68  ? 18.497 -14.904 25.143  1.00 18.39 ? 58  LEU   A CD1 1 
ATOM   456  C CD2 . LEU   A 1 68  ? 20.773 -14.404 24.271  1.00 18.57 ? 58  LEU   A CD2 1 
ATOM   457  N N   . ILE   A 1 69  ? 20.906 -15.364 29.696  1.00 18.89 ? 59  ILE   A N   1 
ATOM   458  C CA  . ILE   A 1 69  ? 21.354 -16.473 30.596  1.00 19.45 ? 59  ILE   A CA  1 
ATOM   459  C C   . ILE   A 1 69  ? 20.115 -17.160 31.179  1.00 19.57 ? 59  ILE   A C   1 
ATOM   460  O O   . ILE   A 1 69  ? 20.097 -18.410 31.277  1.00 21.87 ? 59  ILE   A O   1 
ATOM   461  C CB  . ILE   A 1 69  ? 22.276 -15.977 31.734  1.00 19.92 ? 59  ILE   A CB  1 
ATOM   462  C CG1 . ILE   A 1 69  ? 23.696 -15.693 31.243  1.00 20.41 ? 59  ILE   A CG1 1 
ATOM   463  C CG2 . ILE   A 1 69  ? 22.275 -16.960 32.907  1.00 20.74 ? 59  ILE   A CG2 1 
ATOM   464  C CD1 . ILE   A 1 69  ? 24.566 -14.865 32.201  1.00 21.15 ? 59  ILE   A CD1 1 
ATOM   465  N N   . ARG   A 1 70  ? 19.126 -16.365 31.572  1.00 20.50 ? 60  ARG   A N   1 
ATOM   466  C CA  . ARG   A 1 70  ? 17.950 -16.863 32.298  1.00 23.08 ? 60  ARG   A CA  1 
ATOM   467  C C   . ARG   A 1 70  ? 16.962 -17.467 31.303  1.00 19.48 ? 60  ARG   A C   1 
ATOM   468  O O   . ARG   A 1 70  ? 15.930 -17.926 31.772  1.00 19.11 ? 60  ARG   A O   1 
ATOM   469  C CB  . ARG   A 1 70  ? 17.339 -15.727 33.113  1.00 29.53 ? 60  ARG   A CB  1 
ATOM   470  C CG  . ARG   A 1 70  ? 18.202 -15.332 34.303  1.00 38.77 ? 60  ARG   A CG  1 
ATOM   471  C CD  . ARG   A 1 70  ? 17.361 -14.731 35.401  1.00 45.81 ? 60  ARG   A CD  1 
ATOM   472  N NE  . ARG   A 1 70  ? 16.621 -13.563 34.932  1.00 52.81 ? 60  ARG   A NE  1 
ATOM   473  C CZ  . ARG   A 1 70  ? 17.150 -12.364 34.662  1.00 52.30 ? 60  ARG   A CZ  1 
ATOM   474  N NH1 . ARG   A 1 70  ? 18.453 -12.147 34.781  1.00 55.78 ? 60  ARG   A NH1 1 
ATOM   475  N NH2 . ARG   A 1 70  ? 16.358 -11.380 34.273  1.00 52.12 ? 60  ARG   A NH2 1 
ATOM   476  N N   . LYS   A 1 71  ? 17.262 -17.480 30.000  1.00 16.50 ? 61  LYS   A N   1 
ATOM   477  C CA  . LYS   A 1 71  ? 16.273 -17.994 29.007  1.00 16.36 ? 61  LYS   A CA  1 
ATOM   478  C C   . LYS   A 1 71  ? 16.800 -19.287 28.372  1.00 15.67 ? 61  LYS   A C   1 
ATOM   479  O O   . LYS   A 1 71  ? 17.965 -19.348 27.954  1.00 17.93 ? 61  LYS   A O   1 
ATOM   480  C CB  . LYS   A 1 71  ? 15.914 -16.962 27.935  1.00 16.55 ? 61  LYS   A CB  1 
ATOM   481  C CG  . LYS   A 1 71  ? 15.363 -15.648 28.461  1.00 16.13 ? 61  LYS   A CG  1 
ATOM   482  C CD  . LYS   A 1 71  ? 14.061 -15.765 29.177  1.00 17.86 ? 61  LYS   A CD  1 
ATOM   483  C CE  . LYS   A 1 71  ? 13.546 -14.406 29.596  1.00 19.63 ? 61  LYS   A CE  1 
ATOM   484  N NZ  . LYS   A 1 71  ? 12.407 -14.526 30.523  1.00 22.11 ? 61  LYS   A NZ  1 
ATOM   485  N N   . SER   A 1 72  ? 15.943 -20.293 28.317  1.00 14.10 ? 62  SER   A N   1 
ATOM   486  C CA  . SER   A 1 72  ? 16.201 -21.572 27.642  1.00 13.87 ? 62  SER   A CA  1 
ATOM   487  C C   . SER   A 1 72  ? 15.277 -21.690 26.431  1.00 12.98 ? 62  SER   A C   1 
ATOM   488  O O   . SER   A 1 72  ? 14.287 -20.957 26.319  1.00 12.35 ? 62  SER   A O   1 
ATOM   489  C CB  . SER   A 1 72  ? 16.006 -22.714 28.602  1.00 14.49 ? 62  SER   A CB  1 
ATOM   490  O OG  . SER   A 1 72  ? 16.934 -22.653 29.677  1.00 16.87 ? 62  SER   A OG  1 
ATOM   491  N N   . ASN   A 1 73  ? 15.557 -22.660 25.588  1.00 12.26 ? 63  ASN   A N   1 
ATOM   492  C CA  . ASN   A 1 73  ? 14.756 -22.916 24.370  1.00 12.01 ? 63  ASN   A CA  1 
ATOM   493  C C   . ASN   A 1 73  ? 13.261 -22.957 24.716  1.00 11.72 ? 63  ASN   A C   1 
ATOM   494  O O   . ASN   A 1 73  ? 12.478 -22.377 23.961  1.00 11.10 ? 63  ASN   A O   1 
ATOM   495  C CB  . ASN   A 1 73  ? 15.163 -24.220 23.723  1.00 11.60 ? 63  ASN   A CB  1 
ATOM   496  C CG  . ASN   A 1 73  ? 16.545 -24.194 23.114  1.00 12.47 ? 63  ASN   A CG  1 
ATOM   497  O OD1 . ASN   A 1 73  ? 17.042 -23.158 22.667  1.00 11.69 ? 63  ASN   A OD1 1 
ATOM   498  N ND2 . ASN   A 1 73  ? 17.122 -25.373 23.008  1.00 12.22 ? 63  ASN   A ND2 1 
ATOM   499  N N   . HIS   A 1 74  ? 12.869 -23.628 25.805  1.00 12.29 ? 64  HIS   A N   1 
ATOM   500  C CA  . HIS   A 1 74  ? 11.437 -23.834 26.166  1.00 13.11 ? 64  HIS   A CA  1 
ATOM   501  C C   . HIS   A 1 74  ? 10.763 -22.535 26.623  1.00 13.57 ? 64  HIS   A C   1 
ATOM   502  O O   . HIS   A 1 74  ? 9.505  -22.486 26.727  1.00 12.72 ? 64  HIS   A O   1 
ATOM   503  C CB  . HIS   A 1 74  ? 11.292 -24.970 27.192  1.00 13.70 ? 64  HIS   A CB  1 
ATOM   504  C CG  . HIS   A 1 74  ? 11.753 -24.645 28.566  1.00 15.03 ? 64  HIS   A CG  1 
ATOM   505  N ND1 . HIS   A 1 74  ? 13.022 -24.978 29.006  1.00 16.78 ? 64  HIS   A ND1 1 
ATOM   506  C CD2 . HIS   A 1 74  ? 11.122 -24.069 29.606  1.00 15.81 ? 64  HIS   A CD2 1 
ATOM   507  C CE1 . HIS   A 1 74  ? 13.151 -24.574 30.248  1.00 16.34 ? 64  HIS   A CE1 1 
ATOM   508  N NE2 . HIS   A 1 74  ? 12.008 -24.024 30.644  1.00 15.47 ? 64  HIS   A NE2 1 
ATOM   509  N N   . ASN   A 1 75  ? 11.548 -21.502 26.910  1.00 12.62 ? 65  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 75  ? 11.017 -20.201 27.372  1.00 13.16 ? 65  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 75  ? 10.561 -19.393 26.151  1.00 13.59 ? 65  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 75  ? 9.884  -18.357 26.341  1.00 13.28 ? 65  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 75  ? 12.061 -19.445 28.171  1.00 13.79 ? 65  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 75  ? 12.385 -20.093 29.490  1.00 15.43 ? 65  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 75  ? 13.551 -20.323 29.799  1.00 15.73 ? 65  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 75  ? 11.355 -20.397 30.252  1.00 14.21 ? 65  ASN   A ND2 1 
ATOM   517  N N   . PHE   A 1 76  ? 10.890 -19.862 24.951  1.00 12.05 ? 66  PHE   A N   1 
ATOM   518  C CA  . PHE   A 1 76  ? 10.491 -19.176 23.698  1.00 12.52 ? 66  PHE   A CA  1 
ATOM   519  C C   . PHE   A 1 76  ? 9.293  -19.900 23.096  1.00 12.41 ? 66  PHE   A C   1 
ATOM   520  O O   . PHE   A 1 76  ? 9.450  -20.948 22.461  1.00 12.54 ? 66  PHE   A O   1 
ATOM   521  C CB  . PHE   A 1 76  ? 11.638 -19.064 22.705  1.00 12.59 ? 66  PHE   A CB  1 
ATOM   522  C CG  . PHE   A 1 76  ? 12.762 -18.203 23.190  1.00 13.13 ? 66  PHE   A CG  1 
ATOM   523  C CD1 . PHE   A 1 76  ? 12.690 -16.825 23.099  1.00 14.46 ? 66  PHE   A CD1 1 
ATOM   524  C CD2 . PHE   A 1 76  ? 13.877 -18.771 23.781  1.00 14.24 ? 66  PHE   A CD2 1 
ATOM   525  C CE1 . PHE   A 1 76  ? 13.724 -16.035 23.565  1.00 13.95 ? 66  PHE   A CE1 1 
ATOM   526  C CE2 . PHE   A 1 76  ? 14.923 -17.975 24.221  1.00 13.63 ? 66  PHE   A CE2 1 
ATOM   527  C CZ  . PHE   A 1 76  ? 14.830 -16.611 24.136  1.00 13.21 ? 66  PHE   A CZ  1 
ATOM   528  N N   . LEU   A 1 77  ? 8.122  -19.309 23.267  1.00 12.96 ? 67  LEU   A N   1 
ATOM   529  C CA  . LEU   A 1 77  ? 6.869  -19.862 22.712  1.00 12.92 ? 67  LEU   A CA  1 
ATOM   530  C C   . LEU   A 1 77  ? 6.680  -19.293 21.314  1.00 13.00 ? 67  LEU   A C   1 
ATOM   531  O O   . LEU   A 1 77  ? 6.483  -18.063 21.187  1.00 12.92 ? 67  LEU   A O   1 
ATOM   532  C CB  . LEU   A 1 77  ? 5.704  -19.505 23.625  1.00 14.57 ? 67  LEU   A CB  1 
ATOM   533  C CG  . LEU   A 1 77  ? 5.837  -20.060 25.039  1.00 16.73 ? 67  LEU   A CG  1 
ATOM   534  C CD1 . LEU   A 1 77  ? 4.730  -19.532 25.947  1.00 17.63 ? 67  LEU   A CD1 1 
ATOM   535  C CD2 . LEU   A 1 77  ? 5.842  -21.576 25.005  1.00 17.88 ? 67  LEU   A CD2 1 
ATOM   536  N N   . VAL   A 1 78  ? 6.754  -20.168 20.323  1.00 12.75 ? 68  VAL   A N   1 
ATOM   537  C CA  . VAL   A 1 78  ? 6.654  -19.766 18.901  1.00 12.98 ? 68  VAL   A CA  1 
ATOM   538  C C   . VAL   A 1 78  ? 5.409  -20.401 18.308  1.00 13.62 ? 68  VAL   A C   1 
ATOM   539  O O   . VAL   A 1 78  ? 5.296  -21.633 18.361  1.00 12.26 ? 68  VAL   A O   1 
ATOM   540  C CB  . VAL   A 1 78  ? 7.910  -20.151 18.126  1.00 12.96 ? 68  VAL   A CB  1 
ATOM   541  C CG1 . VAL   A 1 78  ? 7.800  -19.662 16.688  1.00 13.64 ? 68  VAL   A CG1 1 
ATOM   542  C CG2 . VAL   A 1 78  ? 9.149  -19.611 18.841  1.00 13.67 ? 68  VAL   A CG2 1 
ATOM   543  N N   . GLN   A 1 79  ? 4.523  -19.583 17.751  1.00 15.49 ? 69  GLN   A N   1 
ATOM   544  C CA  . GLN   A 1 79  ? 3.239  -20.083 17.219  1.00 18.02 ? 69  GLN   A CA  1 
ATOM   545  C C   . GLN   A 1 79  ? 3.074  -19.585 15.788  1.00 17.74 ? 69  GLN   A C   1 
ATOM   546  O O   . GLN   A 1 79  ? 3.171  -18.383 15.584  1.00 16.48 ? 69  GLN   A O   1 
ATOM   547  C CB  . GLN   A 1 79  ? 2.148  -19.616 18.177  1.00 19.97 ? 69  GLN   A CB  1 
ATOM   548  C CG  . GLN   A 1 79  ? 0.846  -20.349 18.018  1.00 23.11 ? 69  GLN   A CG  1 
ATOM   549  C CD  . GLN   A 1 79  ? -0.111 -19.881 19.076  1.00 22.77 ? 69  GLN   A CD  1 
ATOM   550  O OE1 . GLN   A 1 79  ? 0.247  -19.733 20.250  1.00 24.49 ? 69  GLN   A OE1 1 
ATOM   551  N NE2 . GLN   A 1 79  ? -1.328 -19.591 18.648  1.00 27.80 ? 69  GLN   A NE2 1 
ATOM   552  N N   . ALA   A 1 80  ? 2.905  -20.524 14.853  1.00 19.45 ? 70  ALA   A N   1 
ATOM   553  C CA  . ALA   A 1 80  ? 2.629  -20.313 13.420  1.00 21.19 ? 70  ALA   A CA  1 
ATOM   554  C C   . ALA   A 1 80  ? 1.135  -20.590 13.206  1.00 24.38 ? 70  ALA   A C   1 
ATOM   555  O O   . ALA   A 1 80  ? 0.694  -21.752 13.377  1.00 21.37 ? 70  ALA   A O   1 
ATOM   556  C CB  . ALA   A 1 80  ? 3.504  -21.237 12.604  1.00 22.38 ? 70  ALA   A CB  1 
ATOM   557  N N   . GLY   A 1 81  ? 0.367  -19.541 12.938  1.00 26.65 ? 71  GLY   A N   1 
ATOM   558  C CA  . GLY   A 1 81  ? -1.092 -19.596 13.095  1.00 28.55 ? 71  GLY   A CA  1 
ATOM   559  C C   . GLY   A 1 81  ? -1.445 -20.272 14.403  1.00 27.51 ? 71  GLY   A C   1 
ATOM   560  O O   . GLY   A 1 81  ? -1.079 -19.756 15.465  1.00 29.02 ? 71  GLY   A O   1 
ATOM   561  N N   . ASN   A 1 82  ? -2.126 -21.409 14.353  1.00 32.10 ? 72  ASN   A N   1 
ATOM   562  C CA  . ASN   A 1 82  ? -2.715 -21.997 15.581  1.00 34.94 ? 72  ASN   A CA  1 
ATOM   563  C C   . ASN   A 1 82  ? -1.769 -23.052 16.165  1.00 33.05 ? 72  ASN   A C   1 
ATOM   564  O O   . ASN   A 1 82  ? -2.107 -23.571 17.237  1.00 32.82 ? 72  ASN   A O   1 
ATOM   565  C CB  . ASN   A 1 82  ? -4.122 -22.538 15.314  1.00 42.50 ? 72  ASN   A CB  1 
ATOM   566  C CG  . ASN   A 1 82  ? -4.897 -22.806 16.589  1.00 47.44 ? 72  ASN   A CG  1 
ATOM   567  O OD1 . ASN   A 1 82  ? -4.923 -21.979 17.504  1.00 54.66 ? 72  ASN   A OD1 1 
ATOM   568  N ND2 . ASN   A 1 82  ? -5.524 -23.968 16.666  1.00 53.12 ? 72  ASN   A ND2 1 
ATOM   569  N N   . VAL   A 1 83  ? -0.615 -23.320 15.528  1.00 30.71 ? 73  VAL   A N   1 
ATOM   570  C CA  . VAL   A 1 83  ? 0.235  -24.516 15.822  1.00 29.84 ? 73  VAL   A CA  1 
ATOM   571  C C   . VAL   A 1 83  ? 1.586  -24.086 16.414  1.00 28.47 ? 73  VAL   A C   1 
ATOM   572  O O   . VAL   A 1 83  ? 2.244  -23.227 15.830  1.00 23.97 ? 73  VAL   A O   1 
ATOM   573  C CB  . VAL   A 1 83  ? 0.393  -25.377 14.551  1.00 32.58 ? 73  VAL   A CB  1 
ATOM   574  C CG1 . VAL   A 1 83  ? 1.241  -26.621 14.790  1.00 33.29 ? 73  VAL   A CG1 1 
ATOM   575  C CG2 . VAL   A 1 83  ? -0.972 -25.766 13.991  1.00 31.18 ? 73  VAL   A CG2 1 
ATOM   576  N N   . GLN   A 1 84  ? 1.992  -24.730 17.517  1.00 26.51 ? 74  GLN   A N   1 
ATOM   577  C CA  . GLN   A 1 84  ? 3.244  -24.451 18.256  1.00 24.62 ? 74  GLN   A CA  1 
ATOM   578  C C   . GLN   A 1 84  ? 4.429  -25.041 17.484  1.00 23.58 ? 74  GLN   A C   1 
ATOM   579  O O   . GLN   A 1 84  ? 4.298  -26.189 17.014  1.00 26.57 ? 74  GLN   A O   1 
ATOM   580  C CB  . GLN   A 1 84  ? 3.111  -25.070 19.648  1.00 27.03 ? 74  GLN   A CB  1 
ATOM   581  C CG  . GLN   A 1 84  ? 3.786  -24.270 20.741  1.00 27.23 ? 74  GLN   A CG  1 
ATOM   582  C CD  . GLN   A 1 84  ? 3.116  -22.934 20.983  1.00 27.75 ? 74  GLN   A CD  1 
ATOM   583  O OE1 . GLN   A 1 84  ? 1.944  -22.718 20.648  1.00 32.18 ? 74  GLN   A OE1 1 
ATOM   584  N NE2 . GLN   A 1 84  ? 3.856  -22.031 21.599  1.00 26.84 ? 74  GLN   A NE2 1 
ATOM   585  N N   . LEU   A 1 85  ? 5.531  -24.290 17.326  1.00 19.45 ? 75  LEU   A N   1 
ATOM   586  C CA  . LEU   A 1 85  ? 6.827  -24.790 16.784  1.00 18.34 ? 75  LEU   A CA  1 
ATOM   587  C C   . LEU   A 1 85  ? 7.729  -25.165 17.959  1.00 18.76 ? 75  LEU   A C   1 
ATOM   588  O O   . LEU   A 1 85  ? 7.620  -24.529 19.023  1.00 20.98 ? 75  LEU   A O   1 
ATOM   589  C CB  . LEU   A 1 85  ? 7.519  -23.725 15.930  1.00 19.53 ? 75  LEU   A CB  1 
ATOM   590  C CG  . LEU   A 1 85  ? 6.650  -23.124 14.840  1.00 20.93 ? 75  LEU   A CG  1 
ATOM   591  C CD1 . LEU   A 1 85  ? 7.486  -22.330 13.854  1.00 20.47 ? 75  LEU   A CD1 1 
ATOM   592  C CD2 . LEU   A 1 85  ? 5.895  -24.225 14.122  1.00 23.39 ? 75  LEU   A CD2 1 
ATOM   593  N N   . ARG   A 1 86  ? 8.551  -26.192 17.788  1.00 16.36 ? 76  ARG   A N   1 
ATOM   594  C CA  . ARG   A 1 86  ? 9.422  -26.705 18.860  1.00 14.44 ? 76  ARG   A CA  1 
ATOM   595  C C   . ARG   A 1 86  ? 10.788 -26.004 18.701  1.00 13.92 ? 76  ARG   A C   1 
ATOM   596  O O   . ARG   A 1 86  ? 11.369 -26.086 17.632  1.00 15.01 ? 76  ARG   A O   1 
ATOM   597  C CB  . ARG   A 1 86  ? 9.455  -28.237 18.835  1.00 15.25 ? 76  ARG   A CB  1 
ATOM   598  C CG  . ARG   A 1 86  ? 10.249 -28.879 19.972  1.00 15.53 ? 76  ARG   A CG  1 
ATOM   599  C CD  . ARG   A 1 86  ? 10.220 -30.400 19.919  1.00 15.41 ? 76  ARG   A CD  1 
ATOM   600  N NE  . ARG   A 1 86  ? 8.852  -30.929 20.039  1.00 15.48 ? 76  ARG   A NE  1 
ATOM   601  C CZ  . ARG   A 1 86  ? 8.193  -31.076 21.185  1.00 15.55 ? 76  ARG   A CZ  1 
ATOM   602  N NH1 . ARG   A 1 86  ? 8.773  -30.783 22.336  1.00 14.85 ? 76  ARG   A NH1 1 
ATOM   603  N NH2 . ARG   A 1 86  ? 6.943  -31.505 21.168  1.00 16.11 ? 76  ARG   A NH2 1 
ATOM   604  N N   . VAL   A 1 87  ? 11.224 -25.266 19.719  1.00 12.67 ? 77  VAL   A N   1 
ATOM   605  C CA  . VAL   A 1 87  ? 12.508 -24.500 19.658  1.00 12.99 ? 77  VAL   A CA  1 
ATOM   606  C C   . VAL   A 1 87  ? 13.630 -25.415 20.144  1.00 13.58 ? 77  VAL   A C   1 
ATOM   607  O O   . VAL   A 1 87  ? 13.561 -25.907 21.310  1.00 12.38 ? 77  VAL   A O   1 
ATOM   608  C CB  . VAL   A 1 87  ? 12.391 -23.206 20.465  1.00 12.79 ? 77  VAL   A CB  1 
ATOM   609  C CG1 . VAL   A 1 87  ? 13.686 -22.405 20.470  1.00 12.69 ? 77  VAL   A CG1 1 
ATOM   610  C CG2 . VAL   A 1 87  ? 11.225 -22.396 19.925  1.00 11.72 ? 77  VAL   A CG2 1 
ATOM   611  N N   . ILE   A 1 88  ? 14.585 -25.688 19.265  1.00 13.20 ? 78  ILE   A N   1 
ATOM   612  C CA  . ILE   A 1 88  ? 15.676 -26.659 19.544  1.00 14.84 ? 78  ILE   A CA  1 
ATOM   613  C C   . ILE   A 1 88  ? 17.008 -25.918 19.661  1.00 14.25 ? 78  ILE   A C   1 
ATOM   614  O O   . ILE   A 1 88  ? 18.044 -26.583 19.857  1.00 15.81 ? 78  ILE   A O   1 
ATOM   615  C CB  . ILE   A 1 88  ? 15.692 -27.750 18.459  1.00 15.12 ? 78  ILE   A CB  1 
ATOM   616  C CG1 . ILE   A 1 88  ? 15.912 -27.188 17.048  1.00 15.25 ? 78  ILE   A CG1 1 
ATOM   617  C CG2 . ILE   A 1 88  ? 14.418 -28.579 18.557  1.00 16.03 ? 78  ILE   A CG2 1 
ATOM   618  C CD1 . ILE   A 1 88  ? 16.400 -28.218 16.032  1.00 16.46 ? 78  ILE   A CD1 1 
ATOM   619  N N   . GLY   A 1 89  ? 17.009 -24.590 19.605  1.00 13.58 ? 79  GLY   A N   1 
ATOM   620  C CA  . GLY   A 1 89  ? 18.261 -23.820 19.736  1.00 13.13 ? 79  GLY   A CA  1 
ATOM   621  C C   . GLY   A 1 89  ? 17.971 -22.343 19.687  1.00 13.02 ? 79  GLY   A C   1 
ATOM   622  O O   . GLY   A 1 89  ? 16.911 -21.950 19.180  1.00 11.90 ? 79  GLY   A O   1 
ATOM   623  N N   . HIS   A 1 90  ? 18.804 -21.542 20.307  1.00 12.65 ? 80  HIS   A N   1 
ATOM   624  C CA  . HIS   A 1 90  ? 18.640 -20.075 20.240  1.00 11.85 ? 80  HIS   A CA  1 
ATOM   625  C C   . HIS   A 1 90  ? 20.012 -19.410 20.280  1.00 12.03 ? 80  HIS   A C   1 
ATOM   626  O O   . HIS   A 1 90  ? 20.945 -19.912 20.960  1.00 11.59 ? 80  HIS   A O   1 
ATOM   627  C CB  . HIS   A 1 90  ? 17.688 -19.566 21.322  1.00 11.30 ? 80  HIS   A CB  1 
ATOM   628  C CG  . HIS   A 1 90  ? 18.205 -19.692 22.702  1.00 11.53 ? 80  HIS   A CG  1 
ATOM   629  N ND1 . HIS   A 1 90  ? 18.081 -20.863 23.443  1.00 11.30 ? 80  HIS   A ND1 1 
ATOM   630  C CD2 . HIS   A 1 90  ? 18.908 -18.825 23.474  1.00 11.50 ? 80  HIS   A CD2 1 
ATOM   631  C CE1 . HIS   A 1 90  ? 18.625 -20.671 24.639  1.00 12.48 ? 80  HIS   A CE1 1 
ATOM   632  N NE2 . HIS   A 1 90  ? 19.119 -19.443 24.688  1.00 11.25 ? 80  HIS   A NE2 1 
ATOM   633  N N   . SER   A 1 91  ? 20.096 -18.231 19.688  1.00 13.07 ? 81  SER   A N   1 
ATOM   634  C CA  . SER   A 1 91  ? 21.342 -17.434 19.749  1.00 13.90 ? 81  SER   A CA  1 
ATOM   635  C C   . SER   A 1 91  ? 21.002 -15.980 19.468  1.00 15.09 ? 81  SER   A C   1 
ATOM   636  O O   . SER   A 1 91  ? 19.973 -15.748 18.753  1.00 14.97 ? 81  SER   A O   1 
ATOM   637  C CB  . SER   A 1 91  ? 22.350 -17.976 18.799  1.00 15.76 ? 81  SER   A CB  1 
ATOM   638  O OG  . SER   A 1 91  ? 21.930 -17.773 17.484  1.00 17.58 ? 81  SER   A OG  1 
ATOM   639  N N   . MET   A 1 92  ? 21.802 -15.063 20.019  1.00 13.66 ? 82  MET   A N   1 
ATOM   640  C CA  . MET   A 1 92  ? 21.691 -13.612 19.755  1.00 14.20 ? 82  MET   A CA  1 
ATOM   641  C C   . MET   A 1 92  ? 22.749 -13.215 18.713  1.00 14.59 ? 82  MET   A C   1 
ATOM   642  O O   . MET   A 1 92  ? 23.932 -13.579 18.887  1.00 13.52 ? 82  MET   A O   1 
ATOM   643  C CB  . MET   A 1 92  ? 21.867 -12.828 21.052  1.00 14.37 ? 82  MET   A CB  1 
ATOM   644  C CG  . MET   A 1 92  ? 21.717 -11.338 20.892  1.00 13.75 ? 82  MET   A CG  1 
ATOM   645  S SD  . MET   A 1 92  ? 21.566 -10.508 22.488  1.00 15.13 ? 82  MET   A SD  1 
ATOM   646  C CE  . MET   A 1 92  ? 23.145 -10.893 23.253  1.00 16.67 ? 82  MET   A CE  1 
ATOM   647  N N   . GLN   A 1 93  ? 22.323 -12.530 17.665  1.00 13.01 ? 83  GLN   A N   1 
ATOM   648  C CA  . GLN   A 1 93  ? 23.198 -11.880 16.659  1.00 13.78 ? 83  GLN   A CA  1 
ATOM   649  C C   . GLN   A 1 93  ? 22.846 -10.397 16.637  1.00 12.38 ? 83  GLN   A C   1 
ATOM   650  O O   . GLN   A 1 93  ? 21.735 -10.083 16.242  1.00 11.81 ? 83  GLN   A O   1 
ATOM   651  C CB  . GLN   A 1 93  ? 23.006 -12.492 15.286  1.00 14.85 ? 83  GLN   A CB  1 
ATOM   652  C CG  . GLN   A 1 93  ? 23.702 -11.692 14.193  1.00 15.97 ? 83  GLN   A CG  1 
ATOM   653  C CD  . GLN   A 1 93  ? 23.583 -12.381 12.858  1.00 18.00 ? 83  GLN   A CD  1 
ATOM   654  O OE1 . GLN   A 1 93  ? 22.692 -13.195 12.619  1.00 20.25 ? 83  GLN   A OE1 1 
ATOM   655  N NE2 . GLN   A 1 93  ? 24.479 -12.039 11.951  1.00 20.31 ? 83  GLN   A NE2 1 
ATOM   656  N N   . ASN   A 1 94  ? 23.726 -9.562  17.166  1.00 11.57 ? 84  ASN   A N   1 
ATOM   657  C CA  . ASN   A 1 94  ? 23.498 -8.107  17.286  1.00 10.53 ? 84  ASN   A CA  1 
ATOM   658  C C   . ASN   A 1 94  ? 22.171 -7.939  18.049  1.00 10.31 ? 84  ASN   A C   1 
ATOM   659  O O   . ASN   A 1 94  ? 22.051 -8.497  19.170  1.00 9.36  ? 84  ASN   A O   1 
ATOM   660  C CB  . ASN   A 1 94  ? 23.609 -7.488  15.899  1.00 10.58 ? 84  ASN   A CB  1 
ATOM   661  C CG  . ASN   A 1 94  ? 24.976 -7.756  15.286  1.00 10.42 ? 84  ASN   A CG  1 
ATOM   662  O OD1 . ASN   A 1 94  ? 26.002 -7.517  15.908  1.00 10.85 ? 84  ASN   A OD1 1 
ATOM   663  N ND2 . ASN   A 1 94  ? 25.016 -8.357  14.128  1.00 10.49 ? 84  ASN   A ND2 1 
ATOM   664  N N   . CYS   A 1 95  ? 21.183 -7.292  17.447  1.00 10.51 ? 85  CYS   A N   1 
ATOM   665  C CA  . CYS   A 1 95  ? 19.908 -6.932  18.097  1.00 10.34 ? 85  CYS   A CA  1 
ATOM   666  C C   . CYS   A 1 95  ? 18.799 -7.920  17.744  1.00 10.96 ? 85  CYS   A C   1 
ATOM   667  O O   . CYS   A 1 95  ? 17.631 -7.643  18.126  1.00 10.00 ? 85  CYS   A O   1 
ATOM   668  C CB  . CYS   A 1 95  ? 19.512 -5.500  17.773  1.00 11.17 ? 85  CYS   A CB  1 
ATOM   669  S SG  . CYS   A 1 95  ? 20.681 -4.313  18.501  1.00 11.59 ? 85  CYS   A SG  1 
ATOM   670  N N   . VAL   A 1 96  ? 19.127 -9.063  17.139  1.00 10.61 ? 86  VAL   A N   1 
ATOM   671  C CA  . VAL   A 1 96  ? 18.077 -10.072 16.830  1.00 10.30 ? 86  VAL   A CA  1 
ATOM   672  C C   . VAL   A 1 96  ? 18.405 -11.378 17.527  1.00 10.14 ? 86  VAL   A C   1 
ATOM   673  O O   . VAL   A 1 96  ? 19.605 -11.652 17.840  1.00 9.84  ? 86  VAL   A O   1 
ATOM   674  C CB  . VAL   A 1 96  ? 17.800 -10.277 15.332  1.00 9.77  ? 86  VAL   A CB  1 
ATOM   675  C CG1 . VAL   A 1 96  ? 17.192 -9.033  14.695  1.00 9.89  ? 86  VAL   A CG1 1 
ATOM   676  C CG2 . VAL   A 1 96  ? 18.989 -10.780 14.557  1.00 10.54 ? 86  VAL   A CG2 1 
ATOM   677  N N   . LEU   A 1 97  ? 17.342 -12.111 17.846  1.00 10.59 ? 87  LEU   A N   1 
ATOM   678  C CA  . LEU   A 1 97  ? 17.463 -13.533 18.230  1.00 11.85 ? 87  LEU   A CA  1 
ATOM   679  C C   . LEU   A 1 97  ? 17.127 -14.396 17.014  1.00 11.32 ? 87  LEU   A C   1 
ATOM   680  O O   . LEU   A 1 97  ? 16.221 -14.090 16.255  1.00 10.28 ? 87  LEU   A O   1 
ATOM   681  C CB  . LEU   A 1 97  ? 16.542 -13.879 19.389  1.00 12.36 ? 87  LEU   A CB  1 
ATOM   682  C CG  . LEU   A 1 97  ? 16.774 -13.079 20.662  1.00 13.85 ? 87  LEU   A CG  1 
ATOM   683  C CD1 . LEU   A 1 97  ? 15.825 -13.527 21.754  1.00 14.62 ? 87  LEU   A CD1 1 
ATOM   684  C CD2 . LEU   A 1 97  ? 18.217 -13.176 21.098  1.00 14.18 ? 87  LEU   A CD2 1 
ATOM   685  N N   . LYS   A 1 98  ? 17.853 -15.480 16.903  1.00 12.15 ? 88  LYS   A N   1 
ATOM   686  C CA  . LYS   A 1 98  ? 17.640 -16.574 15.950  1.00 11.13 ? 88  LYS   A CA  1 
ATOM   687  C C   . LYS   A 1 98  ? 17.197 -17.803 16.733  1.00 11.05 ? 88  LYS   A C   1 
ATOM   688  O O   . LYS   A 1 98  ? 18.054 -18.355 17.473  1.00 11.09 ? 88  LYS   A O   1 
ATOM   689  C CB  . LYS   A 1 98  ? 18.946 -16.823 15.213  1.00 12.47 ? 88  LYS   A CB  1 
ATOM   690  C CG  . LYS   A 1 98  ? 19.293 -15.699 14.269  1.00 13.63 ? 88  LYS   A CG  1 
ATOM   691  C CD  . LYS   A 1 98  ? 20.427 -15.997 13.355  1.00 15.85 ? 88  LYS   A CD  1 
ATOM   692  C CE  . LYS   A 1 98  ? 21.775 -15.942 14.012  1.00 16.93 ? 88  LYS   A CE  1 
ATOM   693  N NZ  . LYS   A 1 98  ? 22.836 -16.109 12.988  1.00 17.89 ? 88  LYS   A NZ  1 
ATOM   694  N N   . LEU   A 1 99  ? 15.936 -18.210 16.574  1.00 10.25 ? 89  LEU   A N   1 
ATOM   695  C CA  . LEU   A 1 99  ? 15.379 -19.411 17.263  1.00 10.40 ? 89  LEU   A CA  1 
ATOM   696  C C   . LEU   A 1 99  ? 15.375 -20.547 16.248  1.00 10.90 ? 89  LEU   A C   1 
ATOM   697  O O   . LEU   A 1 99  ? 14.681 -20.424 15.237  1.00 11.31 ? 89  LEU   A O   1 
ATOM   698  C CB  . LEU   A 1 99  ? 13.987 -19.091 17.811  1.00 10.35 ? 89  LEU   A CB  1 
ATOM   699  C CG  . LEU   A 1 99  ? 13.886 -17.782 18.592  1.00 10.07 ? 89  LEU   A CG  1 
ATOM   700  C CD1 . LEU   A 1 99  ? 12.438 -17.534 19.006  1.00 10.62 ? 89  LEU   A CD1 1 
ATOM   701  C CD2 . LEU   A 1 99  ? 14.805 -17.765 19.790  1.00 10.15 ? 89  LEU   A CD2 1 
ATOM   702  N N   . LYS   A 1 100 ? 16.186 -21.584 16.494  1.00 11.32 ? 90  LYS   A N   1 
ATOM   703  C CA  . LYS   A 1 100 ? 16.209 -22.777 15.621  1.00 11.87 ? 90  LYS   A CA  1 
ATOM   704  C C   . LYS   A 1 100 ? 15.000 -23.618 16.029  1.00 12.31 ? 90  LYS   A C   1 
ATOM   705  O O   . LYS   A 1 100 ? 14.791 -23.834 17.239  1.00 12.82 ? 90  LYS   A O   1 
ATOM   706  C CB  . LYS   A 1 100 ? 17.524 -23.557 15.753  1.00 13.61 ? 90  LYS   A CB  1 
ATOM   707  C CG  . LYS   A 1 100 ? 17.670 -24.613 14.673  1.00 16.35 ? 90  LYS   A CG  1 
ATOM   708  C CD  . LYS   A 1 100 ? 18.991 -25.297 14.667  1.00 20.17 ? 90  LYS   A CD  1 
ATOM   709  C CE  . LYS   A 1 100 ? 18.995 -26.490 13.742  1.00 22.15 ? 90  LYS   A CE  1 
ATOM   710  N NZ  . LYS   A 1 100 ? 20.285 -27.211 13.860  1.00 25.19 ? 90  LYS   A NZ  1 
ATOM   711  N N   . VAL   A 1 101 ? 14.184 -23.992 15.051  1.00 12.24 ? 91  VAL   A N   1 
ATOM   712  C CA  . VAL   A 1 101 ? 12.985 -24.829 15.287  1.00 11.83 ? 91  VAL   A CA  1 
ATOM   713  C C   . VAL   A 1 101 ? 13.153 -26.179 14.584  1.00 12.71 ? 91  VAL   A C   1 
ATOM   714  O O   . VAL   A 1 101 ? 14.013 -26.281 13.705  1.00 10.81 ? 91  VAL   A O   1 
ATOM   715  C CB  . VAL   A 1 101 ? 11.738 -24.076 14.832  1.00 11.59 ? 91  VAL   A CB  1 
ATOM   716  C CG1 . VAL   A 1 101 ? 11.434 -22.884 15.724  1.00 11.59 ? 91  VAL   A CG1 1 
ATOM   717  C CG2 . VAL   A 1 101 ? 11.809 -23.621 13.389  1.00 11.64 ? 91  VAL   A CG2 1 
ATOM   718  N N   . ASP   A 1 102 ? 12.347 -27.173 14.958  1.00 13.32 ? 92  ASP   A N   1 
ATOM   719  C CA  . ASP   A 1 102 ? 12.538 -28.563 14.458  1.00 15.88 ? 92  ASP   A CA  1 
ATOM   720  C C   . ASP   A 1 102 ? 11.877 -28.734 13.090  1.00 16.21 ? 92  ASP   A C   1 
ATOM   721  O O   . ASP   A 1 102 ? 12.002 -29.851 12.507  1.00 17.15 ? 92  ASP   A O   1 
ATOM   722  C CB  . ASP   A 1 102 ? 12.083 -29.593 15.494  1.00 17.34 ? 92  ASP   A CB  1 
ATOM   723  C CG  . ASP   A 1 102 ? 10.597 -29.779 15.613  1.00 20.32 ? 92  ASP   A CG  1 
ATOM   724  O OD1 . ASP   A 1 102 ? 9.867  -28.952 15.064  1.00 20.01 ? 92  ASP   A OD1 1 
ATOM   725  O OD2 . ASP   A 1 102 ? 10.187 -30.730 16.309  1.00 26.03 ? 92  ASP   A OD2 1 
ATOM   726  N N   . THR   A 1 103 ? 11.255 -27.688 12.540  1.00 14.95 ? 93  THR   A N   1 
ATOM   727  C CA  . THR   A 1 103 ? 10.521 -27.775 11.247  1.00 14.87 ? 93  THR   A CA  1 
ATOM   728  C C   . THR   A 1 103 ? 10.962 -26.618 10.347  1.00 14.23 ? 93  THR   A C   1 
ATOM   729  O O   . THR   A 1 103 ? 10.869 -25.441 10.762  1.00 12.32 ? 93  THR   A O   1 
ATOM   730  C CB  . THR   A 1 103 ? 8.997  -27.809 11.442  1.00 16.16 ? 93  THR   A CB  1 
ATOM   731  O OG1 . THR   A 1 103 ? 8.607  -28.841 12.358  1.00 18.11 ? 93  THR   A OG1 1 
ATOM   732  C CG2 . THR   A 1 103 ? 8.212  -28.015 10.161  1.00 16.03 ? 93  THR   A CG2 1 
ATOM   733  N N   . ALA   A 1 104 ? 11.383 -26.952 9.135   1.00 14.47 ? 94  ALA   A N   1 
ATOM   734  C CA  . ALA   A 1 104 ? 11.605 -25.979 8.051   1.00 14.34 ? 94  ALA   A CA  1 
ATOM   735  C C   . ALA   A 1 104 ? 10.242 -25.418 7.612   1.00 14.03 ? 94  ALA   A C   1 
ATOM   736  O O   . ALA   A 1 104 ? 9.266  -26.203 7.439   1.00 13.01 ? 94  ALA   A O   1 
ATOM   737  C CB  . ALA   A 1 104 ? 12.368 -26.636 6.905   1.00 15.89 ? 94  ALA   A CB  1 
ATOM   738  N N   . ASN   A 1 105 ? 10.141 -24.097 7.491   1.00 12.88 ? 95  ASN   A N   1 
ATOM   739  C CA  . ASN   A 1 105 ? 8.882  -23.436 7.063   1.00 12.93 ? 95  ASN   A CA  1 
ATOM   740  C C   . ASN   A 1 105 ? 8.567  -23.927 5.653   1.00 13.27 ? 95  ASN   A C   1 
ATOM   741  O O   . ASN   A 1 105 ? 9.315  -23.620 4.733   1.00 11.12 ? 95  ASN   A O   1 
ATOM   742  C CB  . ASN   A 1 105 ? 8.996  -21.907 7.061   1.00 13.09 ? 95  ASN   A CB  1 
ATOM   743  C CG  . ASN   A 1 105 ? 7.710  -21.224 6.652   1.00 14.06 ? 95  ASN   A CG  1 
ATOM   744  O OD1 . ASN   A 1 105 ? 6.720  -21.880 6.331   1.00 14.50 ? 95  ASN   A OD1 1 
ATOM   745  N ND2 . ASN   A 1 105 ? 7.687  -19.905 6.696   1.00 14.79 ? 95  ASN   A ND2 1 
ATOM   746  N N   . PRO   A 1 106 ? 7.454  -24.667 5.436   1.00 14.31 ? 96  PRO   A N   1 
ATOM   747  C CA  . PRO   A 1 106 ? 7.151  -25.207 4.112   1.00 15.51 ? 96  PRO   A CA  1 
ATOM   748  C C   . PRO   A 1 106 ? 6.824  -24.087 3.118   1.00 17.19 ? 96  PRO   A C   1 
ATOM   749  O O   . PRO   A 1 106 ? 6.884  -24.334 1.912   1.00 17.39 ? 96  PRO   A O   1 
ATOM   750  C CB  . PRO   A 1 106 ? 5.917  -26.072 4.338   1.00 14.17 ? 96  PRO   A CB  1 
ATOM   751  C CG  . PRO   A 1 106 ? 5.268  -25.488 5.578   1.00 14.64 ? 96  PRO   A CG  1 
ATOM   752  C CD  . PRO   A 1 106 ? 6.424  -25.018 6.430   1.00 14.93 ? 96  PRO   A CD  1 
ATOM   753  N N   . LYS   A 1 107 ? 6.461  -22.905 3.643   1.00 15.52 ? 97  LYS   A N   1 
ATOM   754  C CA  . LYS   A 1 107 ? 6.136  -21.715 2.830   1.00 16.74 ? 97  LYS   A CA  1 
ATOM   755  C C   . LYS   A 1 107 ? 7.365  -20.830 2.638   1.00 16.07 ? 97  LYS   A C   1 
ATOM   756  O O   . LYS   A 1 107 ? 7.170  -19.718 2.163   1.00 17.37 ? 97  LYS   A O   1 
ATOM   757  C CB  . LYS   A 1 107 ? 5.006  -20.918 3.482   1.00 16.87 ? 97  LYS   A CB  1 
ATOM   758  C CG  . LYS   A 1 107 ? 3.714  -21.688 3.668   1.00 20.35 ? 97  LYS   A CG  1 
ATOM   759  C CD  . LYS   A 1 107 ? 2.615  -20.875 4.316   1.00 22.15 ? 97  LYS   A CD  1 
ATOM   760  C CE  . LYS   A 1 107 ? 1.521  -21.729 4.925   1.00 26.79 ? 97  LYS   A CE  1 
ATOM   761  N NZ  . LYS   A 1 107 ? 0.458  -20.914 5.577   1.00 28.44 ? 97  LYS   A NZ  1 
ATOM   762  N N   . THR   A 1 108 ? 8.582  -21.276 2.959   1.00 15.79 ? 98  THR   A N   1 
ATOM   763  C CA  . THR   A 1 108 ? 9.773  -20.418 2.763   1.00 14.63 ? 98  THR   A CA  1 
ATOM   764  C C   . THR   A 1 108 ? 9.891  -20.052 1.285   1.00 17.33 ? 98  THR   A C   1 
ATOM   765  O O   . THR   A 1 108 ? 10.031 -20.943 0.443   1.00 16.95 ? 98  THR   A O   1 
ATOM   766  C CB  . THR   A 1 108 ? 11.081 -21.069 3.182   1.00 14.22 ? 98  THR   A CB  1 
ATOM   767  O OG1 . THR   A 1 108 ? 11.010 -21.536 4.528   1.00 13.67 ? 98  THR   A OG1 1 
ATOM   768  C CG2 . THR   A 1 108 ? 12.250 -20.125 3.025   1.00 13.40 ? 98  THR   A CG2 1 
ATOM   769  N N   . PRO   A 1 109 ? 9.889  -18.747 0.932   1.00 16.69 ? 99  PRO   A N   1 
ATOM   770  C CA  . PRO   A 1 109 ? 10.209 -18.336 -0.435  1.00 17.60 ? 99  PRO   A CA  1 
ATOM   771  C C   . PRO   A 1 109 ? 11.718 -18.295 -0.682  1.00 17.43 ? 99  PRO   A C   1 
ATOM   772  O O   . PRO   A 1 109 ? 12.502 -18.323 0.249   1.00 17.61 ? 99  PRO   A O   1 
ATOM   773  C CB  . PRO   A 1 109 ? 9.675  -16.902 -0.494  1.00 17.42 ? 99  PRO   A CB  1 
ATOM   774  C CG  . PRO   A 1 109 ? 9.999  -16.400 0.909   1.00 17.29 ? 99  PRO   A CG  1 
ATOM   775  C CD  . PRO   A 1 109 ? 9.634  -17.583 1.804   1.00 17.03 ? 99  PRO   A CD  1 
ATOM   776  N N   . LYS   A 1 110 ? 12.094 -18.196 -1.952  1.00 17.38 ? 100 LYS   A N   1 
ATOM   777  C CA  . LYS   A 1 110 ? 13.434 -17.743 -2.370  1.00 18.25 ? 100 LYS   A CA  1 
ATOM   778  C C   . LYS   A 1 110 ? 13.678 -16.388 -1.698  1.00 16.28 ? 100 LYS   A C   1 
ATOM   779  O O   . LYS   A 1 110 ? 12.844 -15.517 -1.836  1.00 15.03 ? 100 LYS   A O   1 
ATOM   780  C CB  . LYS   A 1 110 ? 13.468 -17.648 -3.898  1.00 22.43 ? 100 LYS   A CB  1 
ATOM   781  C CG  . LYS   A 1 110 ? 14.760 -18.081 -4.560  1.00 26.81 ? 100 LYS   A CG  1 
ATOM   782  C CD  . LYS   A 1 110 ? 14.642 -18.185 -6.084  1.00 28.38 ? 100 LYS   A CD  1 
ATOM   783  C CE  . LYS   A 1 110 ? 13.573 -19.162 -6.528  1.00 31.39 ? 100 LYS   A CE  1 
ATOM   784  N NZ  . LYS   A 1 110 ? 13.832 -19.663 -7.902  1.00 34.24 ? 100 LYS   A NZ  1 
ATOM   785  N N   . TYR   A 1 111 ? 14.756 -16.246 -0.945  1.00 15.64 ? 101 TYR   A N   1 
ATOM   786  C CA  . TYR   A 1 111 ? 15.015 -15.021 -0.145  1.00 15.98 ? 101 TYR   A CA  1 
ATOM   787  C C   . TYR   A 1 111 ? 16.508 -14.738 -0.038  1.00 15.99 ? 101 TYR   A C   1 
ATOM   788  O O   . TYR   A 1 111 ? 17.345 -15.695 -0.177  1.00 15.44 ? 101 TYR   A O   1 
ATOM   789  C CB  . TYR   A 1 111 ? 14.389 -15.139 1.246   1.00 15.93 ? 101 TYR   A CB  1 
ATOM   790  C CG  . TYR   A 1 111 ? 15.135 -16.009 2.216   1.00 17.07 ? 101 TYR   A CG  1 
ATOM   791  C CD1 . TYR   A 1 111 ? 14.859 -17.365 2.312   1.00 17.22 ? 101 TYR   A CD1 1 
ATOM   792  C CD2 . TYR   A 1 111 ? 16.117 -15.488 3.040   1.00 18.36 ? 101 TYR   A CD2 1 
ATOM   793  C CE1 . TYR   A 1 111 ? 15.534 -18.182 3.202   1.00 17.28 ? 101 TYR   A CE1 1 
ATOM   794  C CE2 . TYR   A 1 111 ? 16.789 -16.289 3.948   1.00 17.63 ? 101 TYR   A CE2 1 
ATOM   795  C CZ  . TYR   A 1 111 ? 16.493 -17.641 4.033   1.00 18.88 ? 101 TYR   A CZ  1 
ATOM   796  O OH  . TYR   A 1 111 ? 17.156 -18.428 4.934   1.00 19.49 ? 101 TYR   A OH  1 
ATOM   797  N N   . LYS   A 1 112 ? 16.798 -13.464 0.248   1.00 16.41 ? 102 LYS   A N   1 
ATOM   798  C CA  . LYS   A 1 112 ? 18.113 -12.906 0.615   1.00 17.18 ? 102 LYS   A CA  1 
ATOM   799  C C   . LYS   A 1 112 ? 17.920 -11.896 1.757   1.00 15.94 ? 102 LYS   A C   1 
ATOM   800  O O   . LYS   A 1 112 ? 16.818 -11.408 1.925   1.00 13.93 ? 102 LYS   A O   1 
ATOM   801  C CB  . LYS   A 1 112 ? 18.730 -12.207 -0.593  1.00 21.70 ? 102 LYS   A CB  1 
ATOM   802  C CG  . LYS   A 1 112 ? 19.377 -13.148 -1.591  1.00 27.01 ? 102 LYS   A CG  1 
ATOM   803  C CD  . LYS   A 1 112 ? 19.791 -12.502 -2.903  1.00 30.80 ? 102 LYS   A CD  1 
ATOM   804  C CE  . LYS   A 1 112 ? 19.815 -10.989 -2.860  1.00 31.71 ? 102 LYS   A CE  1 
ATOM   805  N NZ  . LYS   A 1 112 ? 20.733 -10.448 -3.892  1.00 37.80 ? 102 LYS   A NZ  1 
ATOM   806  N N   . PHE   A 1 113 ? 18.962 -11.667 2.542   1.00 14.12 ? 103 PHE   A N   1 
ATOM   807  C CA  . PHE   A 1 113 ? 19.070 -10.535 3.491   1.00 14.16 ? 103 PHE   A CA  1 
ATOM   808  C C   . PHE   A 1 113 ? 19.896 -9.438  2.834   1.00 14.67 ? 103 PHE   A C   1 
ATOM   809  O O   . PHE   A 1 113 ? 21.035 -9.710  2.350   1.00 15.32 ? 103 PHE   A O   1 
ATOM   810  C CB  . PHE   A 1 113 ? 19.676 -10.989 4.813   1.00 13.08 ? 103 PHE   A CB  1 
ATOM   811  C CG  . PHE   A 1 113 ? 18.847 -11.964 5.602   1.00 12.77 ? 103 PHE   A CG  1 
ATOM   812  C CD1 . PHE   A 1 113 ? 17.499 -12.135 5.339   1.00 12.61 ? 103 PHE   A CD1 1 
ATOM   813  C CD2 . PHE   A 1 113 ? 19.412 -12.649 6.672   1.00 13.68 ? 103 PHE   A CD2 1 
ATOM   814  C CE1 . PHE   A 1 113 ? 16.739 -12.996 6.113   1.00 12.76 ? 103 PHE   A CE1 1 
ATOM   815  C CE2 . PHE   A 1 113 ? 18.648 -13.513 7.442   1.00 13.93 ? 103 PHE   A CE2 1 
ATOM   816  C CZ  . PHE   A 1 113 ? 17.315 -13.669 7.164   1.00 13.80 ? 103 PHE   A CZ  1 
ATOM   817  N N   . VAL   A 1 114 ? 19.359 -8.222  2.798   1.00 13.64 ? 104 VAL   A N   1 
ATOM   818  C CA  . VAL   A 1 114 ? 20.127 -7.082  2.237   1.00 15.12 ? 104 VAL   A CA  1 
ATOM   819  C C   . VAL   A 1 114 ? 20.097 -5.934  3.233   1.00 14.97 ? 104 VAL   A C   1 
ATOM   820  O O   . VAL   A 1 114 ? 19.076 -5.736  3.881   1.00 16.06 ? 104 VAL   A O   1 
ATOM   821  C CB  . VAL   A 1 114 ? 19.649 -6.675  0.837   1.00 17.02 ? 104 VAL   A CB  1 
ATOM   822  C CG1 . VAL   A 1 114 ? 19.746 -7.864  -0.120  1.00 17.31 ? 104 VAL   A CG1 1 
ATOM   823  C CG2 . VAL   A 1 114 ? 18.246 -6.118  0.845   1.00 18.91 ? 104 VAL   A CG2 1 
ATOM   824  N N   . ARG   A 1 115 ? 21.205 -5.232  3.357   1.00 14.27 ? 105 ARG   A N   1 
ATOM   825  C CA  . ARG   A 1 115 ? 21.231 -3.983  4.150   1.00 13.59 ? 105 ARG   A CA  1 
ATOM   826  C C   . ARG   A 1 115 ? 21.061 -2.871  3.124   1.00 14.22 ? 105 ARG   A C   1 
ATOM   827  O O   . ARG   A 1 115 ? 21.977 -2.683  2.318   1.00 13.41 ? 105 ARG   A O   1 
ATOM   828  C CB  . ARG   A 1 115 ? 22.494 -3.891  5.007   1.00 12.80 ? 105 ARG   A CB  1 
ATOM   829  C CG  . ARG   A 1 115 ? 22.508 -2.694  5.936   1.00 12.65 ? 105 ARG   A CG  1 
ATOM   830  C CD  . ARG   A 1 115 ? 23.794 -2.607  6.737   1.00 12.94 ? 105 ARG   A CD  1 
ATOM   831  N NE  . ARG   A 1 115 ? 23.782 -1.379  7.506   1.00 13.04 ? 105 ARG   A NE  1 
ATOM   832  C CZ  . ARG   A 1 115 ? 23.129 -1.206  8.641   1.00 12.92 ? 105 ARG   A CZ  1 
ATOM   833  N NH1 . ARG   A 1 115 ? 22.453 -2.206  9.181   1.00 12.89 ? 105 ARG   A NH1 1 
ATOM   834  N NH2 . ARG   A 1 115 ? 23.207 -0.046  9.258   1.00 13.59 ? 105 ARG   A NH2 1 
ATOM   835  N N   . ILE   A 1 116 ? 19.892 -2.220  3.090   1.00 14.80 ? 106 ILE   A N   1 
ATOM   836  C CA  . ILE   A 1 116 ? 19.616 -1.166  2.069   1.00 16.29 ? 106 ILE   A CA  1 
ATOM   837  C C   . ILE   A 1 116 ? 20.351 0.128   2.406   1.00 15.90 ? 106 ILE   A C   1 
ATOM   838  O O   . ILE   A 1 116 ? 20.637 0.427   3.586   1.00 14.03 ? 106 ILE   A O   1 
ATOM   839  C CB  . ILE   A 1 116 ? 18.122 -0.871  1.834   1.00 17.75 ? 106 ILE   A CB  1 
ATOM   840  C CG1 . ILE   A 1 116 ? 17.392 -0.575  3.138   1.00 19.45 ? 106 ILE   A CG1 1 
ATOM   841  C CG2 . ILE   A 1 116 ? 17.457 -1.949  1.017   1.00 19.95 ? 106 ILE   A CG2 1 
ATOM   842  C CD1 . ILE   A 1 116 ? 16.128 0.186   2.928   1.00 22.24 ? 106 ILE   A CD1 1 
ATOM   843  N N   . GLN   A 1 117 ? 20.574 0.898   1.350   1.00 15.84 ? 107 GLN   A N   1 
ATOM   844  C CA  . GLN   A 1 117 ? 21.113 2.274   1.398   1.00 17.72 ? 107 GLN   A CA  1 
ATOM   845  C C   . GLN   A 1 117 ? 19.986 3.255   1.706   1.00 16.29 ? 107 GLN   A C   1 
ATOM   846  O O   . GLN   A 1 117 ? 18.834 3.080   1.281   1.00 15.71 ? 107 GLN   A O   1 
ATOM   847  C CB  . GLN   A 1 117 ? 21.796 2.601   0.070   1.00 19.02 ? 107 GLN   A CB  1 
ATOM   848  C CG  . GLN   A 1 117 ? 23.009 1.708   -0.189  1.00 23.42 ? 107 GLN   A CG  1 
ATOM   849  C CD  . GLN   A 1 117 ? 24.151 2.140   0.703   1.00 26.05 ? 107 GLN   A CD  1 
ATOM   850  O OE1 . GLN   A 1 117 ? 24.488 3.317   0.787   1.00 31.16 ? 107 GLN   A OE1 1 
ATOM   851  N NE2 . GLN   A 1 117 ? 24.746 1.198   1.409   1.00 29.21 ? 107 GLN   A NE2 1 
ATOM   852  N N   . PRO   A 1 118 ? 20.345 4.343   2.404   1.00 15.52 ? 108 PRO   A N   1 
ATOM   853  C CA  . PRO   A 1 118 ? 19.449 5.476   2.612   1.00 15.91 ? 108 PRO   A CA  1 
ATOM   854  C C   . PRO   A 1 118 ? 18.960 5.988   1.243   1.00 14.59 ? 108 PRO   A C   1 
ATOM   855  O O   . PRO   A 1 118 ? 19.747 6.051   0.296   1.00 14.56 ? 108 PRO   A O   1 
ATOM   856  C CB  . PRO   A 1 118 ? 20.292 6.513   3.371   1.00 16.42 ? 108 PRO   A CB  1 
ATOM   857  C CG  . PRO   A 1 118 ? 21.730 6.092   3.162   1.00 16.61 ? 108 PRO   A CG  1 
ATOM   858  C CD  . PRO   A 1 118 ? 21.699 4.593   2.927   1.00 16.59 ? 108 PRO   A CD  1 
ATOM   859  N N   . GLY   A 1 119 ? 17.662 6.216   1.119   1.00 14.14 ? 109 GLY   A N   1 
ATOM   860  C CA  . GLY   A 1 119 ? 17.022 6.735   -0.109  1.00 14.58 ? 109 GLY   A CA  1 
ATOM   861  C C   . GLY   A 1 119 ? 16.337 5.628   -0.887  1.00 15.73 ? 109 GLY   A C   1 
ATOM   862  O O   . GLY   A 1 119 ? 15.576 5.923   -1.831  1.00 15.64 ? 109 GLY   A O   1 
ATOM   863  N N   . GLN   A 1 120 ? 16.610 4.371   -0.537  1.00 14.13 ? 110 GLN   A N   1 
ATOM   864  C CA  . GLN   A 1 120 ? 15.892 3.204   -1.096  1.00 14.14 ? 110 GLN   A CA  1 
ATOM   865  C C   . GLN   A 1 120 ? 14.565 2.978   -0.362  1.00 13.01 ? 110 GLN   A C   1 
ATOM   866  O O   . GLN   A 1 120 ? 14.440 3.342   0.816   1.00 13.16 ? 110 GLN   A O   1 
ATOM   867  C CB  . GLN   A 1 120 ? 16.795 1.970   -1.057  1.00 16.09 ? 110 GLN   A CB  1 
ATOM   868  C CG  . GLN   A 1 120 ? 18.068 2.151   -1.865  1.00 18.77 ? 110 GLN   A CG  1 
ATOM   869  C CD  . GLN   A 1 120 ? 17.780 2.417   -3.320  1.00 22.79 ? 110 GLN   A CD  1 
ATOM   870  O OE1 . GLN   A 1 120 ? 18.152 3.457   -3.881  1.00 26.86 ? 110 GLN   A OE1 1 
ATOM   871  N NE2 . GLN   A 1 120 ? 17.106 1.466   -3.945  1.00 24.24 ? 110 GLN   A NE2 1 
ATOM   872  N N   . THR   A 1 121 ? 13.596 2.401   -1.075  1.00 12.64 ? 111 THR   A N   1 
ATOM   873  C CA  . THR   A 1 121 ? 12.221 2.117   -0.594  1.00 12.02 ? 111 THR   A CA  1 
ATOM   874  C C   . THR   A 1 121 ? 12.057 0.613   -0.364  1.00 11.42 ? 111 THR   A C   1 
ATOM   875  O O   . THR   A 1 121 ? 12.903 -0.185  -0.822  1.00 10.49 ? 111 THR   A O   1 
ATOM   876  C CB  . THR   A 1 121 ? 11.185 2.644   -1.584  1.00 12.46 ? 111 THR   A CB  1 
ATOM   877  O OG1 . THR   A 1 121 ? 11.483 2.010   -2.836  1.00 12.96 ? 111 THR   A OG1 1 
ATOM   878  C CG2 . THR   A 1 121 ? 11.257 4.149   -1.698  1.00 12.27 ? 111 THR   A CG2 1 
ATOM   879  N N   . PHE   A 1 122 ? 11.024 0.253   0.383   1.00 10.36 ? 112 PHE   A N   1 
ATOM   880  C CA  . PHE   A 1 122 ? 10.689 -1.155  0.659   1.00 10.91 ? 112 PHE   A CA  1 
ATOM   881  C C   . PHE   A 1 122 ? 9.262  -1.193  1.180   1.00 10.30 ? 112 PHE   A C   1 
ATOM   882  O O   . PHE   A 1 122 ? 8.774  -0.127  1.583   1.00 11.28 ? 112 PHE   A O   1 
ATOM   883  C CB  . PHE   A 1 122 ? 11.701 -1.778  1.616   1.00 11.20 ? 112 PHE   A CB  1 
ATOM   884  C CG  . PHE   A 1 122 ? 11.820 -1.106  2.969   1.00 11.51 ? 112 PHE   A CG  1 
ATOM   885  C CD1 . PHE   A 1 122 ? 10.965 -1.455  3.999   1.00 11.34 ? 112 PHE   A CD1 1 
ATOM   886  C CD2 . PHE   A 1 122 ? 12.830 -0.182  3.215   1.00 12.51 ? 112 PHE   A CD2 1 
ATOM   887  C CE1 . PHE   A 1 122 ? 11.085 -0.879  5.257   1.00 11.81 ? 112 PHE   A CE1 1 
ATOM   888  C CE2 . PHE   A 1 122 ? 12.932 0.428   4.465   1.00 12.56 ? 112 PHE   A CE2 1 
ATOM   889  C CZ  . PHE   A 1 122 ? 12.086 0.042   5.500   1.00 12.49 ? 112 PHE   A CZ  1 
ATOM   890  N N   . SER   A 1 123 ? 8.645  -2.372  1.148   1.00 10.27 ? 113 SER   A N   1 
ATOM   891  C CA  . SER   A 1 123 ? 7.267  -2.599  1.653   1.00 9.63  ? 113 SER   A CA  1 
ATOM   892  C C   . SER   A 1 123 ? 7.381  -3.100  3.088   1.00 9.72  ? 113 SER   A C   1 
ATOM   893  O O   . SER   A 1 123 ? 8.323  -3.857  3.372   1.00 9.13  ? 113 SER   A O   1 
ATOM   894  C CB  . SER   A 1 123 ? 6.520  -3.573  0.794   1.00 10.45 ? 113 SER   A CB  1 
ATOM   895  O OG  . SER   A 1 123 ? 6.358  -3.063  -0.510  1.00 10.96 ? 113 SER   A OG  1 
ATOM   896  N N   . VAL   A 1 124 ? 6.483  -2.643  3.947   1.00 9.50  ? 114 VAL   A N   1 
ATOM   897  C CA  . VAL   A 1 124 ? 6.362  -3.134  5.341   1.00 9.31  ? 114 VAL   A CA  1 
ATOM   898  C C   . VAL   A 1 124 ? 5.077  -3.931  5.435   1.00 9.14  ? 114 VAL   A C   1 
ATOM   899  O O   . VAL   A 1 124 ? 4.011  -3.430  5.024   1.00 9.60  ? 114 VAL   A O   1 
ATOM   900  C CB  . VAL   A 1 124 ? 6.371  -1.960  6.323   1.00 9.49  ? 114 VAL   A CB  1 
ATOM   901  C CG1 . VAL   A 1 124 ? 5.940  -2.402  7.717   1.00 8.88  ? 114 VAL   A CG1 1 
ATOM   902  C CG2 . VAL   A 1 124 ? 7.738  -1.308  6.328   1.00 10.07 ? 114 VAL   A CG2 1 
ATOM   903  N N   . LEU   A 1 125 ? 5.160  -5.128  5.984   1.00 8.95  ? 115 LEU   A N   1 
ATOM   904  C CA  . LEU   A 1 125 ? 3.957  -5.902  6.347   1.00 8.79  ? 115 LEU   A CA  1 
ATOM   905  C C   . LEU   A 1 125 ? 3.801  -5.749  7.859   1.00 8.81  ? 115 LEU   A C   1 
ATOM   906  O O   . LEU   A 1 125 ? 4.547  -6.403  8.637   1.00 8.81  ? 115 LEU   A O   1 
ATOM   907  C CB  . LEU   A 1 125 ? 4.145  -7.354  5.922   1.00 9.06  ? 115 LEU   A CB  1 
ATOM   908  C CG  . LEU   A 1 125 ? 2.965  -8.269  6.221   1.00 9.37  ? 115 LEU   A CG  1 
ATOM   909  C CD1 . LEU   A 1 125 ? 1.725  -7.904  5.407   1.00 9.36  ? 115 LEU   A CD1 1 
ATOM   910  C CD2 . LEU   A 1 125 ? 3.362  -9.712  5.998   1.00 9.22  ? 115 LEU   A CD2 1 
ATOM   911  N N   . ALA   A 1 126 ? 2.978  -4.790  8.270   1.00 9.09  ? 116 ALA   A N   1 
ATOM   912  C CA  . ALA   A 1 126 ? 2.686  -4.555  9.694   1.00 10.02 ? 116 ALA   A CA  1 
ATOM   913  C C   . ALA   A 1 126 ? 1.922  -5.776  10.223  1.00 10.58 ? 116 ALA   A C   1 
ATOM   914  O O   . ALA   A 1 126 ? 0.870  -6.159  9.609   1.00 12.19 ? 116 ALA   A O   1 
ATOM   915  C CB  . ALA   A 1 126 ? 1.897  -3.278  9.891   1.00 10.82 ? 116 ALA   A CB  1 
ATOM   916  N N   . CYS   A 1 127 ? 2.409  -6.338  11.327  1.00 10.06 ? 117 CYS   A N   1 
ATOM   917  C CA  . CYS   A 1 127 ? 1.841  -7.531  11.987  1.00 10.57 ? 117 CYS   A CA  1 
ATOM   918  C C   . CYS   A 1 127 ? 1.642  -7.309  13.478  1.00 9.30  ? 117 CYS   A C   1 
ATOM   919  O O   . CYS   A 1 127 ? 2.413  -6.592  14.074  1.00 8.62  ? 117 CYS   A O   1 
ATOM   920  C CB  . CYS   A 1 127 ? 2.751  -8.731  11.812  1.00 11.89 ? 117 CYS   A CB  1 
ATOM   921  S SG  . CYS   A 1 127 ? 2.875  -9.192  10.078  1.00 14.48 ? 117 CYS   A SG  1 
ATOM   922  N N   . TYR   A 1 128 ? 0.671  -8.019  14.039  1.00 10.10 ? 118 TYR   A N   1 
ATOM   923  C CA  . TYR   A 1 128 ? 0.427  -8.116  15.500  1.00 10.96 ? 118 TYR   A CA  1 
ATOM   924  C C   . TYR   A 1 128 ? 0.136  -9.583  15.826  1.00 11.80 ? 118 TYR   A C   1 
ATOM   925  O O   . TYR   A 1 128 ? -0.658 -10.225 15.094  1.00 11.16 ? 118 TYR   A O   1 
ATOM   926  C CB  . TYR   A 1 128 ? -0.680 -7.133  15.914  1.00 11.43 ? 118 TYR   A CB  1 
ATOM   927  C CG  . TYR   A 1 128 ? -0.335 -5.698  15.618  1.00 11.38 ? 118 TYR   A CG  1 
ATOM   928  C CD1 . TYR   A 1 128 ? 0.391  -4.932  16.519  1.00 11.61 ? 118 TYR   A CD1 1 
ATOM   929  C CD2 . TYR   A 1 128 ? -0.617 -5.151  14.372  1.00 11.71 ? 118 TYR   A CD2 1 
ATOM   930  C CE1 . TYR   A 1 128 ? 0.797  -3.655  16.200  1.00 11.74 ? 118 TYR   A CE1 1 
ATOM   931  C CE2 . TYR   A 1 128 ? -0.256 -3.855  14.059  1.00 11.39 ? 118 TYR   A CE2 1 
ATOM   932  C CZ  . TYR   A 1 128 ? 0.450  -3.107  14.988  1.00 11.89 ? 118 TYR   A CZ  1 
ATOM   933  O OH  . TYR   A 1 128 ? 0.889  -1.852  14.668  1.00 12.86 ? 118 TYR   A OH  1 
ATOM   934  N N   . ASN   A 1 129 ? 0.747  -10.115 16.891  1.00 14.18 ? 119 ASN   A N   1 
ATOM   935  C CA  . ASN   A 1 129 ? 0.486  -11.513 17.342  1.00 15.61 ? 119 ASN   A CA  1 
ATOM   936  C C   . ASN   A 1 129 ? 0.747  -12.494 16.188  1.00 15.32 ? 119 ASN   A C   1 
ATOM   937  O O   . ASN   A 1 129 ? 0.059  -13.528 16.095  1.00 13.82 ? 119 ASN   A O   1 
ATOM   938  C CB  . ASN   A 1 129 ? -0.950 -11.664 17.848  1.00 18.78 ? 119 ASN   A CB  1 
ATOM   939  C CG  . ASN   A 1 129 ? -1.174 -10.862 19.106  1.00 22.58 ? 119 ASN   A CG  1 
ATOM   940  O OD1 . ASN   A 1 129 ? -1.891 -9.872  19.105  1.00 29.32 ? 119 ASN   A OD1 1 
ATOM   941  N ND2 . ASN   A 1 129 ? -0.515 -11.254 20.181  1.00 27.42 ? 119 ASN   A ND2 1 
ATOM   942  N N   . GLY   A 1 130 ? 1.684  -12.169 15.301  1.00 14.97 ? 120 GLY   A N   1 
ATOM   943  C CA  . GLY   A 1 130 ? 2.088  -13.063 14.205  1.00 14.89 ? 120 GLY   A CA  1 
ATOM   944  C C   . GLY   A 1 130 ? 1.112  -12.993 13.037  1.00 15.23 ? 120 GLY   A C   1 
ATOM   945  O O   . GLY   A 1 130 ? 1.255  -13.817 12.120  1.00 13.68 ? 120 GLY   A O   1 
ATOM   946  N N   . SER   A 1 131 ? 0.147  -12.064 13.069  1.00 15.41 ? 121 SER   A N   1 
ATOM   947  C CA  . SER   A 1 131 ? -0.931 -11.955 12.061  1.00 15.56 ? 121 SER   A CA  1 
ATOM   948  C C   . SER   A 1 131 ? -0.808 -10.633 11.325  1.00 14.69 ? 121 SER   A C   1 
ATOM   949  O O   . SER   A 1 131 ? -0.740 -9.580  11.928  1.00 13.26 ? 121 SER   A O   1 
ATOM   950  C CB  . SER   A 1 131 ? -2.298 -12.073 12.664  1.00 17.56 ? 121 SER   A CB  1 
ATOM   951  O OG  . SER   A 1 131 ? -2.449 -13.352 13.260  1.00 20.58 ? 121 SER   A OG  1 
ATOM   952  N N   . PRO   A 1 132 ? -0.884 -10.638 9.990   1.00 17.17 ? 122 PRO   A N   1 
ATOM   953  C CA  . PRO   A 1 132 ? -0.757 -9.394  9.238   1.00 17.40 ? 122 PRO   A CA  1 
ATOM   954  C C   . PRO   A 1 132 ? -1.987 -8.497  9.374   1.00 17.89 ? 122 PRO   A C   1 
ATOM   955  O O   . PRO   A 1 132 ? -3.125 -8.956  9.289   1.00 17.18 ? 122 PRO   A O   1 
ATOM   956  C CB  . PRO   A 1 132 ? -0.523 -9.935  7.828   1.00 19.37 ? 122 PRO   A CB  1 
ATOM   957  C CG  . PRO   A 1 132 ? -1.426 -11.122 7.798   1.00 20.56 ? 122 PRO   A CG  1 
ATOM   958  C CD  . PRO   A 1 132 ? -1.130 -11.806 9.121   1.00 19.07 ? 122 PRO   A CD  1 
ATOM   959  N N   . SER   A 1 133 ? -1.707 -7.223  9.614   1.00 17.05 ? 123 SER   A N   1 
ATOM   960  C CA  . SER   A 1 133 ? -2.647 -6.094  9.681   1.00 18.01 ? 123 SER   A CA  1 
ATOM   961  C C   . SER   A 1 133 ? -2.706 -5.425  8.309   1.00 16.79 ? 123 SER   A C   1 
ATOM   962  O O   . SER   A 1 133 ? -3.800 -5.127  7.863   1.00 16.10 ? 123 SER   A O   1 
ATOM   963  C CB  . SER   A 1 133 ? -2.202 -5.131  10.746  1.00 20.63 ? 123 SER   A CB  1 
ATOM   964  O OG  . SER   A 1 133 ? -3.197 -4.155  11.031  1.00 27.53 ? 123 SER   A OG  1 
ATOM   965  N N   . GLY   A 1 134 ? -1.569 -5.141  7.680   1.00 14.15 ? 124 GLY   A N   1 
ATOM   966  C CA  . GLY   A 1 134 ? -1.590 -4.303  6.467   1.00 13.88 ? 124 GLY   A CA  1 
ATOM   967  C C   . GLY   A 1 134 ? -0.235 -4.141  5.848   1.00 13.62 ? 124 GLY   A C   1 
ATOM   968  O O   . GLY   A 1 134 ? 0.760  -4.587  6.429   1.00 12.30 ? 124 GLY   A O   1 
ATOM   969  N N   . VAL   A 1 135 ? -0.211 -3.510  4.682   1.00 14.19 ? 125 VAL   A N   1 
ATOM   970  C CA  . VAL   A 1 135 ? 1.029  -3.334  3.905   1.00 13.96 ? 125 VAL   A CA  1 
ATOM   971  C C   . VAL   A 1 135 ? 1.128  -1.884  3.415   1.00 13.85 ? 125 VAL   A C   1 
ATOM   972  O O   . VAL   A 1 135 ? 0.126  -1.301  2.961   1.00 13.80 ? 125 VAL   A O   1 
ATOM   973  C CB  . VAL   A 1 135 ? 1.119  -4.352  2.756   1.00 16.54 ? 125 VAL   A CB  1 
ATOM   974  C CG1 . VAL   A 1 135 ? 0.196  -4.020  1.608   1.00 19.07 ? 125 VAL   A CG1 1 
ATOM   975  C CG2 . VAL   A 1 135 ? 2.530  -4.490  2.273   1.00 17.68 ? 125 VAL   A CG2 1 
ATOM   976  N N   . TYR   A 1 136 ? 2.329  -1.317  3.510   1.00 12.63 ? 126 TYR   A N   1 
ATOM   977  C CA  . TYR   A 1 136 ? 2.583  0.045   3.017   1.00 12.46 ? 126 TYR   A CA  1 
ATOM   978  C C   . TYR   A 1 136 ? 4.040  0.154   2.622   1.00 12.37 ? 126 TYR   A C   1 
ATOM   979  O O   . TYR   A 1 136 ? 4.911  -0.603  3.078   1.00 10.39 ? 126 TYR   A O   1 
ATOM   980  C CB  . TYR   A 1 136 ? 2.140  1.090   4.040   1.00 12.82 ? 126 TYR   A CB  1 
ATOM   981  C CG  . TYR   A 1 136 ? 2.675  0.891   5.427   1.00 13.51 ? 126 TYR   A CG  1 
ATOM   982  C CD1 . TYR   A 1 136 ? 3.961  1.265   5.745   1.00 14.41 ? 126 TYR   A CD1 1 
ATOM   983  C CD2 . TYR   A 1 136 ? 1.883  0.355   6.425   1.00 14.11 ? 126 TYR   A CD2 1 
ATOM   984  C CE1 . TYR   A 1 136 ? 4.461  1.109   7.026   1.00 15.37 ? 126 TYR   A CE1 1 
ATOM   985  C CE2 . TYR   A 1 136 ? 2.377  0.164   7.708   1.00 15.08 ? 126 TYR   A CE2 1 
ATOM   986  C CZ  . TYR   A 1 136 ? 3.686  0.514   7.997   1.00 15.55 ? 126 TYR   A CZ  1 
ATOM   987  O OH  . TYR   A 1 136 ? 4.206  0.378   9.253   1.00 15.88 ? 126 TYR   A OH  1 
ATOM   988  N N   . GLN   A 1 137 ? 4.284  1.153   1.800   1.00 12.49 ? 127 GLN   A N   1 
ATOM   989  C CA  . GLN   A 1 137 ? 5.614  1.458   1.274   1.00 13.15 ? 127 GLN   A CA  1 
ATOM   990  C C   . GLN   A 1 137 ? 6.270  2.496   2.164   1.00 12.91 ? 127 GLN   A C   1 
ATOM   991  O O   . GLN   A 1 137 ? 5.584  3.471   2.542   1.00 14.84 ? 127 GLN   A O   1 
ATOM   992  C CB  . GLN   A 1 137 ? 5.403  1.944   -0.156  1.00 14.03 ? 127 GLN   A CB  1 
ATOM   993  C CG  . GLN   A 1 137 ? 6.644  1.965   -0.968  1.00 16.01 ? 127 GLN   A CG  1 
ATOM   994  C CD  . GLN   A 1 137 ? 7.082  0.595   -1.400  1.00 15.65 ? 127 GLN   A CD  1 
ATOM   995  O OE1 . GLN   A 1 137 ? 6.631  -0.432  -0.899  1.00 16.29 ? 127 GLN   A OE1 1 
ATOM   996  N NE2 . GLN   A 1 137 ? 8.047  0.598   -2.285  1.00 18.78 ? 127 GLN   A NE2 1 
ATOM   997  N N   . CYS   A 1 138 ? 7.579  2.356   2.388   1.00 12.65 ? 128 CYS   A N   1 
ATOM   998  C CA  . CYS   A 1 138 ? 8.427  3.258   3.204   1.00 13.32 ? 128 CYS   A CA  1 
ATOM   999  C C   . CYS   A 1 138 ? 9.713  3.514   2.420   1.00 12.82 ? 128 CYS   A C   1 
ATOM   1000 O O   . CYS   A 1 138 ? 10.050 2.709   1.532   1.00 13.39 ? 128 CYS   A O   1 
ATOM   1001 C CB  . CYS   A 1 138 ? 8.838  2.626   4.537   1.00 14.88 ? 128 CYS   A CB  1 
ATOM   1002 S SG  . CYS   A 1 138 ? 7.466  2.509   5.698   1.00 19.54 ? 128 CYS   A SG  1 
ATOM   1003 N N   . ALA   A 1 139 ? 10.430 4.565   2.770   1.00 12.04 ? 129 ALA   A N   1 
ATOM   1004 C CA  . ALA   A 1 139 ? 11.832 4.803   2.355   1.00 11.86 ? 129 ALA   A CA  1 
ATOM   1005 C C   . ALA   A 1 139 ? 12.713 4.678   3.601   1.00 11.85 ? 129 ALA   A C   1 
ATOM   1006 O O   . ALA   A 1 139 ? 12.315 5.203   4.688   1.00 10.62 ? 129 ALA   A O   1 
ATOM   1007 C CB  . ALA   A 1 139 ? 11.954 6.159   1.728   1.00 11.88 ? 129 ALA   A CB  1 
ATOM   1008 N N   . MET   A 1 140 ? 13.919 4.144   3.438   1.00 11.41 ? 130 MET   A N   1 
ATOM   1009 C CA  . MET   A 1 140 ? 15.006 4.410   4.424   1.00 12.05 ? 130 MET   A CA  1 
ATOM   1010 C C   . MET   A 1 140 ? 15.444 5.865   4.260   1.00 12.20 ? 130 MET   A C   1 
ATOM   1011 O O   . MET   A 1 140 ? 16.070 6.201   3.249   1.00 11.04 ? 130 MET   A O   1 
ATOM   1012 C CB  . MET   A 1 140 ? 16.203 3.481   4.240   1.00 12.15 ? 130 MET   A CB  1 
ATOM   1013 C CG  . MET   A 1 140 ? 17.271 3.536   5.317   1.00 12.13 ? 130 MET   A CG  1 
ATOM   1014 S SD  . MET   A 1 140 ? 16.685 3.473   7.025   1.00 11.08 ? 130 MET   A SD  1 
ATOM   1015 C CE  . MET   A 1 140 ? 15.961 1.844   7.096   1.00 11.24 ? 130 MET   A CE  1 
ATOM   1016 N N   . ARG   A 1 141 ? 15.129 6.690   5.246   1.00 12.50 ? 131 ARG   A N   1 
ATOM   1017 C CA  . ARG   A 1 141 ? 15.392 8.143   5.165   1.00 12.48 ? 131 ARG   A CA  1 
ATOM   1018 C C   . ARG   A 1 141 ? 16.889 8.374   5.352   1.00 12.57 ? 131 ARG   A C   1 
ATOM   1019 O O   . ARG   A 1 141 ? 17.592 7.552   5.950   1.00 11.42 ? 131 ARG   A O   1 
ATOM   1020 C CB  . ARG   A 1 141 ? 14.408 8.833   6.110   1.00 13.78 ? 131 ARG   A CB  1 
ATOM   1021 C CG  . ARG   A 1 141 ? 12.991 8.564   5.604   1.00 14.52 ? 131 ARG   A CG  1 
ATOM   1022 C CD  . ARG   A 1 141 ? 12.062 9.709   5.736   1.00 14.37 ? 131 ARG   A CD  1 
ATOM   1023 N NE  . ARG   A 1 141 ? 12.610 10.894  5.127   1.00 14.14 ? 131 ARG   A NE  1 
ATOM   1024 C CZ  . ARG   A 1 141 ? 12.348 11.297  3.896   1.00 13.43 ? 131 ARG   A CZ  1 
ATOM   1025 N NH1 . ARG   A 1 141 ? 11.554 10.575  3.124   1.00 13.17 ? 131 ARG   A NH1 1 
ATOM   1026 N NH2 . ARG   A 1 141 ? 12.864 12.441  3.476   1.00 13.23 ? 131 ARG   A NH2 1 
ATOM   1027 N N   . PRO   A 1 142 ? 17.435 9.475   4.776   1.00 12.66 ? 132 PRO   A N   1 
ATOM   1028 C CA  . PRO   A 1 142 ? 18.836 9.844   4.986   1.00 12.14 ? 132 PRO   A CA  1 
ATOM   1029 C C   . PRO   A 1 142 ? 19.276 9.812   6.453   1.00 11.96 ? 132 PRO   A C   1 
ATOM   1030 O O   . PRO   A 1 142 ? 20.477 9.548   6.717   1.00 10.54 ? 132 PRO   A O   1 
ATOM   1031 C CB  . PRO   A 1 142 ? 18.895 11.246  4.357   1.00 12.38 ? 132 PRO   A CB  1 
ATOM   1032 C CG  . PRO   A 1 142 ? 17.904 11.170  3.218   1.00 13.14 ? 132 PRO   A CG  1 
ATOM   1033 C CD  . PRO   A 1 142 ? 16.760 10.381  3.833   1.00 13.00 ? 132 PRO   A CD  1 
ATOM   1034 N N   . ASN   A 1 143 ? 18.353 10.077  7.388   1.00 11.58 ? 133 ASN   A N   1 
ATOM   1035 C CA  . ASN   A 1 143 ? 18.674 10.112  8.835   1.00 11.39 ? 133 ASN   A CA  1 
ATOM   1036 C C   . ASN   A 1 143 ? 18.470 8.724   9.446   1.00 11.51 ? 133 ASN   A C   1 
ATOM   1037 O O   . ASN   A 1 143 ? 18.463 8.652   10.675  1.00 11.44 ? 133 ASN   A O   1 
ATOM   1038 C CB  . ASN   A 1 143 ? 17.900 11.196  9.591   1.00 11.84 ? 133 ASN   A CB  1 
ATOM   1039 C CG  . ASN   A 1 143 ? 16.407 10.926  9.647   1.00 12.13 ? 133 ASN   A CG  1 
ATOM   1040 O OD1 . ASN   A 1 143 ? 15.948 9.894   9.178   1.00 11.33 ? 133 ASN   A OD1 1 
ATOM   1041 N ND2 . ASN   A 1 143 ? 15.651 11.853  10.208  1.00 12.27 ? 133 ASN   A ND2 1 
ATOM   1042 N N   . PHE   A 1 144 ? 18.248 7.687   8.629   1.00 11.78 ? 134 PHE   A N   1 
ATOM   1043 C CA  . PHE   A 1 144 ? 18.185 6.258   9.026   1.00 13.17 ? 134 PHE   A CA  1 
ATOM   1044 C C   . PHE   A 1 144 ? 16.951 5.945   9.873   1.00 12.40 ? 134 PHE   A C   1 
ATOM   1045 O O   . PHE   A 1 144 ? 16.976 4.974   10.677  1.00 13.88 ? 134 PHE   A O   1 
ATOM   1046 C CB  . PHE   A 1 144 ? 19.462 5.881   9.775   1.00 13.65 ? 134 PHE   A CB  1 
ATOM   1047 C CG  . PHE   A 1 144 ? 20.694 6.015   8.930   1.00 16.70 ? 134 PHE   A CG  1 
ATOM   1048 C CD1 . PHE   A 1 144 ? 20.917 5.126   7.891   1.00 17.89 ? 134 PHE   A CD1 1 
ATOM   1049 C CD2 . PHE   A 1 144 ? 21.607 7.040   9.139   1.00 19.73 ? 134 PHE   A CD2 1 
ATOM   1050 C CE1 . PHE   A 1 144 ? 22.059 5.230   7.110   1.00 20.07 ? 134 PHE   A CE1 1 
ATOM   1051 C CE2 . PHE   A 1 144 ? 22.758 7.127   8.363   1.00 19.40 ? 134 PHE   A CE2 1 
ATOM   1052 C CZ  . PHE   A 1 144 ? 22.981 6.209   7.360   1.00 19.32 ? 134 PHE   A CZ  1 
ATOM   1053 N N   . THR   A 1 145 ? 15.892 6.719   9.684   1.00 12.57 ? 135 THR   A N   1 
ATOM   1054 C CA  . THR   A 1 145 ? 14.541 6.413   10.218  1.00 12.78 ? 135 THR   A CA  1 
ATOM   1055 C C   . THR   A 1 145 ? 13.612 6.096   9.054   1.00 13.20 ? 135 THR   A C   1 
ATOM   1056 O O   . THR   A 1 145 ? 13.988 6.359   7.882   1.00 14.23 ? 135 THR   A O   1 
ATOM   1057 C CB  . THR   A 1 145 ? 14.029 7.593   11.040  1.00 12.63 ? 135 THR   A CB  1 
ATOM   1058 O OG1 . THR   A 1 145 ? 13.818 8.678   10.143  1.00 13.43 ? 135 THR   A OG1 1 
ATOM   1059 C CG2 . THR   A 1 145 ? 15.013 7.985   12.130  1.00 12.37 ? 135 THR   A CG2 1 
ATOM   1060 N N   . ILE   A 1 146 ? 12.438 5.565   9.371   1.00 12.12 ? 136 ILE   A N   1 
ATOM   1061 C CA  . ILE   A 1 146 ? 11.331 5.406   8.400   1.00 12.09 ? 136 ILE   A CA  1 
ATOM   1062 C C   . ILE   A 1 146 ? 10.079 6.037   8.992   1.00 13.26 ? 136 ILE   A C   1 
ATOM   1063 O O   . ILE   A 1 146 ? 9.986  6.140   10.226  1.00 11.64 ? 136 ILE   A O   1 
ATOM   1064 C CB  . ILE   A 1 146 ? 11.147 3.923   8.019   1.00 11.72 ? 136 ILE   A CB  1 
ATOM   1065 C CG1 . ILE   A 1 146 ? 10.502 3.068   9.109   1.00 11.64 ? 136 ILE   A CG1 1 
ATOM   1066 C CG2 . ILE   A 1 146 ? 12.488 3.337   7.608   1.00 11.61 ? 136 ILE   A CG2 1 
ATOM   1067 C CD1 . ILE   A 1 146 ? 10.065 1.718   8.610   1.00 12.94 ? 136 ILE   A CD1 1 
ATOM   1068 N N   . LYS   A 1 147 ? 9.168  6.460   8.122   1.00 14.71 ? 137 LYS   A N   1 
ATOM   1069 C CA  . LYS   A 1 147 ? 7.863  7.025   8.529   1.00 16.00 ? 137 LYS   A CA  1 
ATOM   1070 C C   . LYS   A 1 147 ? 6.854  5.896   8.366   1.00 13.82 ? 137 LYS   A C   1 
ATOM   1071 O O   . LYS   A 1 147 ? 6.329  5.693   7.251   1.00 13.43 ? 137 LYS   A O   1 
ATOM   1072 C CB  . LYS   A 1 147 ? 7.597  8.300   7.728   1.00 19.44 ? 137 LYS   A CB  1 
ATOM   1073 C CG  . LYS   A 1 147 ? 8.664  9.378   7.863   1.00 21.83 ? 137 LYS   A CG  1 
ATOM   1074 C CD  . LYS   A 1 147 ? 8.373  10.651  7.028   1.00 25.20 ? 137 LYS   A CD  1 
ATOM   1075 C CE  . LYS   A 1 147 ? 8.313  10.409  5.528   1.00 27.32 ? 137 LYS   A CE  1 
ATOM   1076 N NZ  . LYS   A 1 147 ? 8.536  11.667  4.759   1.00 30.83 ? 137 LYS   A NZ  1 
ATOM   1077 N N   . GLY   A 1 148 ? 6.686  5.100   9.421   1.00 11.89 ? 138 GLY   A N   1 
ATOM   1078 C CA  . GLY   A 1 148 ? 5.788  3.947   9.380   1.00 12.68 ? 138 GLY   A CA  1 
ATOM   1079 C C   . GLY   A 1 148 ? 4.527  4.172   10.185  1.00 12.38 ? 138 GLY   A C   1 
ATOM   1080 O O   . GLY   A 1 148 ? 4.157  5.337   10.504  1.00 12.19 ? 138 GLY   A O   1 
ATOM   1081 N N   . SER   A 1 149 ? 3.888  3.057   10.496  1.00 11.90 ? 139 SER   A N   1 
ATOM   1082 C CA  . SER   A 1 149 ? 2.619  2.967   11.244  1.00 11.73 ? 139 SER   A CA  1 
ATOM   1083 C C   . SER   A 1 149 ? 2.711  1.715   12.085  1.00 10.51 ? 139 SER   A C   1 
ATOM   1084 O O   . SER   A 1 149 ? 2.546  0.615   11.526  1.00 11.05 ? 139 SER   A O   1 
ATOM   1085 C CB  . SER   A 1 149 ? 1.421  2.970   10.357  1.00 12.28 ? 139 SER   A CB  1 
ATOM   1086 O OG  . SER   A 1 149 ? 0.247  2.786   11.108  1.00 12.65 ? 139 SER   A OG  1 
ATOM   1087 N N   . PHE   A 1 150 ? 3.071  1.910   13.352  1.00 9.98  ? 140 PHE   A N   1 
ATOM   1088 C CA  . PHE   A 1 150 ? 3.450  0.816   14.255  1.00 9.91  ? 140 PHE   A CA  1 
ATOM   1089 C C   . PHE   A 1 150 ? 2.922  1.127   15.650  1.00 9.90  ? 140 PHE   A C   1 
ATOM   1090 O O   . PHE   A 1 150 ? 3.165  2.230   16.176  1.00 10.09 ? 140 PHE   A O   1 
ATOM   1091 C CB  . PHE   A 1 150 ? 4.966  0.663   14.291  1.00 9.72  ? 140 PHE   A CB  1 
ATOM   1092 C CG  . PHE   A 1 150 ? 5.653  0.211   13.021  1.00 10.13 ? 140 PHE   A CG  1 
ATOM   1093 C CD1 . PHE   A 1 150 ? 5.551  -1.087  12.566  1.00 10.98 ? 140 PHE   A CD1 1 
ATOM   1094 C CD2 . PHE   A 1 150 ? 6.459  1.084   12.309  1.00 10.29 ? 140 PHE   A CD2 1 
ATOM   1095 C CE1 . PHE   A 1 150 ? 6.237  -1.502  11.435  1.00 10.41 ? 140 PHE   A CE1 1 
ATOM   1096 C CE2 . PHE   A 1 150 ? 7.155  0.674   11.194  1.00 10.05 ? 140 PHE   A CE2 1 
ATOM   1097 C CZ  . PHE   A 1 150 ? 7.054  -0.624  10.763  1.00 10.70 ? 140 PHE   A CZ  1 
ATOM   1098 N N   . LEU   A 1 151 ? 2.304  0.127   16.249  1.00 11.17 ? 141 LEU   A N   1 
ATOM   1099 C CA  . LEU   A 1 151 ? 1.757  0.199   17.633  1.00 12.58 ? 141 LEU   A CA  1 
ATOM   1100 C C   . LEU   A 1 151 ? 2.509  -0.787  18.510  1.00 12.55 ? 141 LEU   A C   1 
ATOM   1101 O O   . LEU   A 1 151 ? 3.408  -1.514  18.002  1.00 11.14 ? 141 LEU   A O   1 
ATOM   1102 C CB  . LEU   A 1 151 ? 0.266  -0.142  17.625  1.00 13.41 ? 141 LEU   A CB  1 
ATOM   1103 C CG  . LEU   A 1 151 ? -0.609 0.655   16.663  1.00 14.46 ? 141 LEU   A CG  1 
ATOM   1104 C CD1 . LEU   A 1 151 ? -1.976 -0.030  16.519  1.00 15.90 ? 141 LEU   A CD1 1 
ATOM   1105 C CD2 . LEU   A 1 151 ? -0.769 2.094   17.174  1.00 14.97 ? 141 LEU   A CD2 1 
ATOM   1106 N N   . ASN   A 1 152 ? 2.093  -0.879  19.766  1.00 13.21 ? 142 ASN   A N   1 
ATOM   1107 C CA  . ASN   A 1 152 ? 2.557  -1.956  20.666  1.00 14.49 ? 142 ASN   A CA  1 
ATOM   1108 C C   . ASN   A 1 152 ? 2.302  -3.294  19.972  1.00 12.67 ? 142 ASN   A C   1 
ATOM   1109 O O   . ASN   A 1 152 ? 1.254  -3.461  19.333  1.00 13.29 ? 142 ASN   A O   1 
ATOM   1110 C CB  . ASN   A 1 152 ? 1.875  -1.870  22.034  1.00 16.45 ? 142 ASN   A CB  1 
ATOM   1111 C CG  . ASN   A 1 152 ? 2.366  -0.673  22.818  1.00 20.63 ? 142 ASN   A CG  1 
ATOM   1112 O OD1 . ASN   A 1 152 ? 3.432  -0.133  22.548  1.00 23.75 ? 142 ASN   A OD1 1 
ATOM   1113 N ND2 . ASN   A 1 152 ? 1.608  -0.269  23.819  1.00 23.92 ? 142 ASN   A ND2 1 
ATOM   1114 N N   . GLY   A 1 153 ? 3.272  -4.205  20.079  1.00 12.86 ? 143 GLY   A N   1 
ATOM   1115 C CA  . GLY   A 1 153 ? 3.182  -5.559  19.522  1.00 11.13 ? 143 GLY   A CA  1 
ATOM   1116 C C   . GLY   A 1 153 ? 3.652  -5.660  18.083  1.00 10.86 ? 143 GLY   A C   1 
ATOM   1117 O O   . GLY   A 1 153 ? 3.649  -6.789  17.583  1.00 10.48 ? 143 GLY   A O   1 
ATOM   1118 N N   . SER   A 1 154 ? 3.989  -4.550  17.416  1.00 10.28 ? 144 SER   A N   1 
ATOM   1119 C CA  . SER   A 1 154 ? 4.368  -4.538  15.968  1.00 9.72  ? 144 SER   A CA  1 
ATOM   1120 C C   . SER   A 1 154 ? 5.799  -4.997  15.741  1.00 9.50  ? 144 SER   A C   1 
ATOM   1121 O O   . SER   A 1 154 ? 6.117  -5.362  14.587  1.00 9.74  ? 144 SER   A O   1 
ATOM   1122 C CB  . SER   A 1 154 ? 4.175  -3.188  15.324  1.00 9.65  ? 144 SER   A CB  1 
ATOM   1123 O OG  . SER   A 1 154 ? 4.959  -2.210  15.956  1.00 9.17  ? 144 SER   A OG  1 
ATOM   1124 N N   . CYS   A 1 155 ? 6.655  -4.973  16.755  1.00 9.18  ? 145 CYS   A N   1 
ATOM   1125 C CA  . CYS   A 1 155 ? 8.096  -5.263  16.538  1.00 9.03  ? 145 CYS   A CA  1 
ATOM   1126 C C   . CYS   A 1 155 ? 8.237  -6.648  15.902  1.00 8.49  ? 145 CYS   A C   1 
ATOM   1127 O O   . CYS   A 1 155 ? 7.397  -7.551  16.200  1.00 8.77  ? 145 CYS   A O   1 
ATOM   1128 C CB  . CYS   A 1 155 ? 8.939  -5.132  17.787  1.00 9.64  ? 145 CYS   A CB  1 
ATOM   1129 S SG  . CYS   A 1 155 ? 9.030  -3.450  18.251  1.00 11.17 ? 145 CYS   A SG  1 
ATOM   1130 N N   . GLY   A 1 156 ? 9.236  -6.815  15.048  1.00 7.93  ? 146 GLY   A N   1 
ATOM   1131 C CA  . GLY   A 1 156 ? 9.422  -8.050  14.259  1.00 7.71  ? 146 GLY   A CA  1 
ATOM   1132 C C   . GLY   A 1 156 ? 8.716  -8.038  12.931  1.00 8.21  ? 146 GLY   A C   1 
ATOM   1133 O O   . GLY   A 1 156 ? 8.999  -8.967  12.137  1.00 7.67  ? 146 GLY   A O   1 
ATOM   1134 N N   . SER   A 1 157 ? 7.748  -7.127  12.722  1.00 8.96  ? 147 SER   A N   1 
ATOM   1135 C CA  . SER   A 1 157 ? 7.254  -6.779  11.369  1.00 8.79  ? 147 SER   A CA  1 
ATOM   1136 C C   . SER   A 1 157 ? 8.486  -6.470  10.509  1.00 9.09  ? 147 SER   A C   1 
ATOM   1137 O O   . SER   A 1 157 ? 9.437  -5.818  10.991  1.00 7.65  ? 147 SER   A O   1 
ATOM   1138 C CB  . SER   A 1 157 ? 6.298  -5.613  11.371  1.00 9.08  ? 147 SER   A CB  1 
ATOM   1139 O OG  . SER   A 1 157 ? 5.137  -5.883  12.162  1.00 9.42  ? 147 SER   A OG  1 
ATOM   1140 N N   . VAL   A 1 158 ? 8.480  -6.929  9.259   1.00 9.21  ? 148 VAL   A N   1 
ATOM   1141 C CA  . VAL   A 1 158 ? 9.664  -6.770  8.394   1.00 9.17  ? 148 VAL   A CA  1 
ATOM   1142 C C   . VAL   A 1 158 ? 9.341  -5.915  7.176   1.00 8.59  ? 148 VAL   A C   1 
ATOM   1143 O O   . VAL   A 1 158 ? 8.172  -5.779  6.769   1.00 9.96  ? 148 VAL   A O   1 
ATOM   1144 C CB  . VAL   A 1 158 ? 10.270 -8.108  7.958   1.00 9.32  ? 148 VAL   A CB  1 
ATOM   1145 C CG1 . VAL   A 1 158 ? 10.805 -8.850  9.166   1.00 9.23  ? 148 VAL   A CG1 1 
ATOM   1146 C CG2 . VAL   A 1 158 ? 9.261  -8.923  7.183   1.00 9.69  ? 148 VAL   A CG2 1 
ATOM   1147 N N   . GLY   A 1 159 ? 10.402 -5.403  6.608   1.00 9.04  ? 149 GLY   A N   1 
ATOM   1148 C CA  . GLY   A 1 159 ? 10.394 -4.660  5.350   1.00 8.71  ? 149 GLY   A CA  1 
ATOM   1149 C C   . GLY   A 1 159 ? 11.133 -5.459  4.308   1.00 9.15  ? 149 GLY   A C   1 
ATOM   1150 O O   . GLY   A 1 159 ? 12.103 -6.173  4.649   1.00 8.44  ? 149 GLY   A O   1 
ATOM   1151 N N   . PHE   A 1 160 ? 10.697 -5.361  3.061   1.00 9.81  ? 150 PHE   A N   1 
ATOM   1152 C CA  . PHE   A 1 160 ? 11.243 -6.237  2.003   1.00 11.26 ? 150 PHE   A CA  1 
ATOM   1153 C C   . PHE   A 1 160 ? 11.040 -5.581  0.637   1.00 11.95 ? 150 PHE   A C   1 
ATOM   1154 O O   . PHE   A 1 160 ? 10.205 -4.708  0.464   1.00 12.53 ? 150 PHE   A O   1 
ATOM   1155 C CB  . PHE   A 1 160 ? 10.541 -7.593  2.059   1.00 11.38 ? 150 PHE   A CB  1 
ATOM   1156 C CG  . PHE   A 1 160 ? 9.045  -7.535  1.861   1.00 11.65 ? 150 PHE   A CG  1 
ATOM   1157 C CD1 . PHE   A 1 160 ? 8.209  -7.190  2.914   1.00 11.51 ? 150 PHE   A CD1 1 
ATOM   1158 C CD2 . PHE   A 1 160 ? 8.487  -7.798  0.631   1.00 11.89 ? 150 PHE   A CD2 1 
ATOM   1159 C CE1 . PHE   A 1 160 ? 6.847  -7.081  2.725   1.00 12.21 ? 150 PHE   A CE1 1 
ATOM   1160 C CE2 . PHE   A 1 160 ? 7.115  -7.719  0.445   1.00 11.98 ? 150 PHE   A CE2 1 
ATOM   1161 C CZ  . PHE   A 1 160 ? 6.297  -7.371  1.492   1.00 12.14 ? 150 PHE   A CZ  1 
ATOM   1162 N N   . ASN   A 1 161 ? 11.739 -6.145  -0.330  1.00 13.41 ? 151 ASN   A N   1 
ATOM   1163 C CA  . ASN   A 1 161 ? 11.608 -5.890  -1.775  1.00 14.64 ? 151 ASN   A CA  1 
ATOM   1164 C C   . ASN   A 1 161 ? 11.455 -7.264  -2.426  1.00 16.91 ? 151 ASN   A C   1 
ATOM   1165 O O   . ASN   A 1 161 ? 11.861 -8.284  -1.815  1.00 13.82 ? 151 ASN   A O   1 
ATOM   1166 C CB  . ASN   A 1 161 ? 12.818 -5.153  -2.340  1.00 15.67 ? 151 ASN   A CB  1 
ATOM   1167 C CG  . ASN   A 1 161 ? 12.760 -3.665  -2.076  1.00 16.02 ? 151 ASN   A CG  1 
ATOM   1168 O OD1 . ASN   A 1 161 ? 12.016 -2.939  -2.742  1.00 18.23 ? 151 ASN   A OD1 1 
ATOM   1169 N ND2 . ASN   A 1 161 ? 13.463 -3.219  -1.049  1.00 15.96 ? 151 ASN   A ND2 1 
ATOM   1170 N N   . ILE   A 1 162 ? 10.830 -7.308  -3.592  1.00 19.07 ? 152 ILE   A N   1 
ATOM   1171 C CA  . ILE   A 1 162 ? 10.784 -8.562  -4.386  1.00 21.07 ? 152 ILE   A CA  1 
ATOM   1172 C C   . ILE   A 1 162 ? 11.426 -8.248  -5.736  1.00 23.30 ? 152 ILE   A C   1 
ATOM   1173 O O   . ILE   A 1 162 ? 11.190 -7.144  -6.267  1.00 20.32 ? 152 ILE   A O   1 
ATOM   1174 C CB  . ILE   A 1 162 ? 9.366  -9.136  -4.477  1.00 21.40 ? 152 ILE   A CB  1 
ATOM   1175 C CG1 . ILE   A 1 162 ? 8.667  -9.143  -3.120  1.00 21.78 ? 152 ILE   A CG1 1 
ATOM   1176 C CG2 . ILE   A 1 162 ? 9.399  -10.539 -5.074  1.00 23.57 ? 152 ILE   A CG2 1 
ATOM   1177 C CD1 . ILE   A 1 162 ? 7.285  -9.723  -3.134  1.00 24.21 ? 152 ILE   A CD1 1 
ATOM   1178 N N   . ASP   A 1 163 ? 12.344 -9.114  -6.151  1.00 27.32 ? 153 ASP   A N   1 
ATOM   1179 C CA  . ASP   A 1 163 ? 12.898 -9.154  -7.525  1.00 31.25 ? 153 ASP   A CA  1 
ATOM   1180 C C   . ASP   A 1 163 ? 12.424 -10.482 -8.134  1.00 30.70 ? 153 ASP   A C   1 
ATOM   1181 O O   . ASP   A 1 163 ? 12.961 -11.525 -7.768  1.00 28.59 ? 153 ASP   A O   1 
ATOM   1182 C CB  . ASP   A 1 163 ? 14.416 -8.987  -7.533  1.00 36.02 ? 153 ASP   A CB  1 
ATOM   1183 C CG  . ASP   A 1 163 ? 14.985 -8.908  -8.941  1.00 38.76 ? 153 ASP   A CG  1 
ATOM   1184 O OD1 . ASP   A 1 163 ? 14.974 -7.806  -9.507  1.00 43.79 ? 153 ASP   A OD1 1 
ATOM   1185 O OD2 . ASP   A 1 163 ? 15.384 -9.962  -9.475  1.00 47.79 ? 153 ASP   A OD2 1 
ATOM   1186 N N   . TYR   A 1 164 ? 11.443 -10.403 -9.030  1.00 32.64 ? 154 TYR   A N   1 
ATOM   1187 C CA  . TYR   A 1 164 ? 10.639 -11.516 -9.590  1.00 35.01 ? 154 TYR   A CA  1 
ATOM   1188 C C   . TYR   A 1 164 ? 10.206 -12.477 -8.478  1.00 34.24 ? 154 TYR   A C   1 
ATOM   1189 O O   . TYR   A 1 164 ? 9.100  -12.287 -7.926  1.00 37.00 ? 154 TYR   A O   1 
ATOM   1190 C CB  . TYR   A 1 164 ? 11.350 -12.241 -10.739 1.00 41.32 ? 154 TYR   A CB  1 
ATOM   1191 C CG  . TYR   A 1 164 ? 10.505 -13.354 -11.318 1.00 50.82 ? 154 TYR   A CG  1 
ATOM   1192 C CD1 . TYR   A 1 164 ? 9.138  -13.183 -11.524 1.00 54.24 ? 154 TYR   A CD1 1 
ATOM   1193 C CD2 . TYR   A 1 164 ? 11.048 -14.597 -11.615 1.00 57.19 ? 154 TYR   A CD2 1 
ATOM   1194 C CE1 . TYR   A 1 164 ? 8.341  -14.205 -12.022 1.00 58.62 ? 154 TYR   A CE1 1 
ATOM   1195 C CE2 . TYR   A 1 164 ? 10.266 -15.627 -12.122 1.00 60.59 ? 154 TYR   A CE2 1 
ATOM   1196 C CZ  . TYR   A 1 164 ? 8.909  -15.432 -12.325 1.00 61.21 ? 154 TYR   A CZ  1 
ATOM   1197 O OH  . TYR   A 1 164 ? 8.140  -16.443 -12.827 1.00 65.11 ? 154 TYR   A OH  1 
ATOM   1198 N N   . ASP   A 1 165 ? 11.009 -13.502 -8.185  1.00 30.38 ? 155 ASP   A N   1 
ATOM   1199 C CA  . ASP   A 1 165 ? 10.570 -14.597 -7.281  1.00 31.10 ? 155 ASP   A CA  1 
ATOM   1200 C C   . ASP   A 1 165 ? 11.313 -14.507 -5.948  1.00 26.41 ? 155 ASP   A C   1 
ATOM   1201 O O   . ASP   A 1 165 ? 10.947 -15.277 -5.034  1.00 26.10 ? 155 ASP   A O   1 
ATOM   1202 C CB  . ASP   A 1 165 ? 10.766 -15.976 -7.915  1.00 32.90 ? 155 ASP   A CB  1 
ATOM   1203 C CG  . ASP   A 1 165 ? 12.188 -16.286 -8.364  1.00 35.38 ? 155 ASP   A CG  1 
ATOM   1204 O OD1 . ASP   A 1 165 ? 13.021 -15.354 -8.430  1.00 37.84 ? 155 ASP   A OD1 1 
ATOM   1205 O OD2 . ASP   A 1 165 ? 12.429 -17.456 -8.695  1.00 38.35 ? 155 ASP   A OD2 1 
ATOM   1206 N N   . CYS   A 1 166 ? 12.310 -13.617 -5.852  1.00 22.91 ? 156 CYS   A N   1 
ATOM   1207 C CA  . CYS   A 1 166 ? 13.240 -13.538 -4.703  1.00 21.78 ? 156 CYS   A CA  1 
ATOM   1208 C C   . CYS   A 1 166 ? 12.833 -12.391 -3.766  1.00 19.49 ? 156 CYS   A C   1 
ATOM   1209 O O   . CYS   A 1 166 ? 12.765 -11.226 -4.215  1.00 19.43 ? 156 CYS   A O   1 
ATOM   1210 C CB  . CYS   A 1 166 ? 14.680 -13.369 -5.155  1.00 22.46 ? 156 CYS   A CB  1 
ATOM   1211 S SG  . CYS   A 1 166 ? 15.855 -13.451 -3.778  1.00 23.88 ? 156 CYS   A SG  1 
ATOM   1212 N N   . VAL   A 1 167 ? 12.617 -12.718 -2.499  1.00 15.72 ? 157 VAL   A N   1 
ATOM   1213 C CA  . VAL   A 1 167 ? 12.251 -11.681 -1.483  1.00 14.95 ? 157 VAL   A CA  1 
ATOM   1214 C C   . VAL   A 1 167 ? 13.550 -11.207 -0.844  1.00 13.31 ? 157 VAL   A C   1 
ATOM   1215 O O   . VAL   A 1 167 ? 14.224 -12.041 -0.260  1.00 12.56 ? 157 VAL   A O   1 
ATOM   1216 C CB  . VAL   A 1 167 ? 11.308 -12.229 -0.404  1.00 12.93 ? 157 VAL   A CB  1 
ATOM   1217 C CG1 . VAL   A 1 167 ? 11.055 -11.184 0.670   1.00 12.90 ? 157 VAL   A CG1 1 
ATOM   1218 C CG2 . VAL   A 1 167 ? 10.010 -12.769 -0.975  1.00 13.32 ? 157 VAL   A CG2 1 
ATOM   1219 N N   . SER   A 1 168 ? 13.862 -9.910  -0.903  1.00 13.04 ? 158 SER   A N   1 
ATOM   1220 C CA  . SER   A 1 168 ? 15.036 -9.323  -0.224  1.00 12.48 ? 158 SER   A CA  1 
ATOM   1221 C C   . SER   A 1 168 ? 14.533 -8.661  1.042   1.00 11.01 ? 158 SER   A C   1 
ATOM   1222 O O   . SER   A 1 168 ? 13.928 -7.631  0.942   1.00 10.12 ? 158 SER   A O   1 
ATOM   1223 C CB  . SER   A 1 168 ? 15.802 -8.328  -1.065  1.00 13.54 ? 158 SER   A CB  1 
ATOM   1224 O OG  . SER   A 1 168 ? 16.443 -8.971  -2.132  1.00 15.39 ? 158 SER   A OG  1 
ATOM   1225 N N   . PHE   A 1 169 ? 14.736 -9.297  2.184   1.00 10.99 ? 159 PHE   A N   1 
ATOM   1226 C CA  . PHE   A 1 169 ? 14.380 -8.704  3.498   1.00 11.09 ? 159 PHE   A CA  1 
ATOM   1227 C C   . PHE   A 1 169 ? 15.449 -7.698  3.881   1.00 10.78 ? 159 PHE   A C   1 
ATOM   1228 O O   . PHE   A 1 169 ? 16.623 -8.056  3.877   1.00 10.77 ? 159 PHE   A O   1 
ATOM   1229 C CB  . PHE   A 1 169 ? 14.306 -9.774  4.592   1.00 10.73 ? 159 PHE   A CB  1 
ATOM   1230 C CG  . PHE   A 1 169 ? 13.185 -10.747 4.368   1.00 10.43 ? 159 PHE   A CG  1 
ATOM   1231 C CD1 . PHE   A 1 169 ? 11.877 -10.385 4.652   1.00 9.40  ? 159 PHE   A CD1 1 
ATOM   1232 C CD2 . PHE   A 1 169 ? 13.426 -11.998 3.835   1.00 10.28 ? 159 PHE   A CD2 1 
ATOM   1233 C CE1 . PHE   A 1 169 ? 10.846 -11.285 4.455   1.00 9.76  ? 159 PHE   A CE1 1 
ATOM   1234 C CE2 . PHE   A 1 169 ? 12.395 -12.890 3.629   1.00 9.73  ? 159 PHE   A CE2 1 
ATOM   1235 C CZ  . PHE   A 1 169 ? 11.099 -12.533 3.929   1.00 9.44  ? 159 PHE   A CZ  1 
ATOM   1236 N N   . CYS   A 1 170 ? 15.053 -6.479  4.223   1.00 10.47 ? 160 CYS   A N   1 
ATOM   1237 C CA  . CYS   A 1 170 ? 16.014 -5.398  4.534   1.00 10.80 ? 160 CYS   A CA  1 
ATOM   1238 C C   . CYS   A 1 170 ? 15.735 -4.770  5.891   1.00 10.53 ? 160 CYS   A C   1 
ATOM   1239 O O   . CYS   A 1 170 ? 16.577 -4.012  6.324   1.00 11.19 ? 160 CYS   A O   1 
ATOM   1240 C CB  . CYS   A 1 170 ? 15.976 -4.286  3.493   1.00 10.83 ? 160 CYS   A CB  1 
ATOM   1241 S SG  . CYS   A 1 170 ? 14.335 -3.584  3.189   1.00 11.51 ? 160 CYS   A SG  1 
ATOM   1242 N N   . TYR   A 1 171 ? 14.580 -5.023  6.509   1.00 9.78  ? 161 TYR   A N   1 
ATOM   1243 C CA  . TYR   A 1 171 ? 14.202 -4.266  7.737   1.00 9.45  ? 161 TYR   A CA  1 
ATOM   1244 C C   . TYR   A 1 171 ? 13.455 -5.167  8.712   1.00 8.66  ? 161 TYR   A C   1 
ATOM   1245 O O   . TYR   A 1 171 ? 12.574 -5.946  8.266   1.00 7.52  ? 161 TYR   A O   1 
ATOM   1246 C CB  . TYR   A 1 171 ? 13.348 -3.046  7.400   1.00 9.67  ? 161 TYR   A CB  1 
ATOM   1247 C CG  . TYR   A 1 171 ? 12.924 -2.193  8.568   1.00 9.45  ? 161 TYR   A CG  1 
ATOM   1248 C CD1 . TYR   A 1 171 ? 13.758 -1.222  9.077   1.00 9.63  ? 161 TYR   A CD1 1 
ATOM   1249 C CD2 . TYR   A 1 171 ? 11.639 -2.282  9.109   1.00 9.76  ? 161 TYR   A CD2 1 
ATOM   1250 C CE1 . TYR   A 1 171 ? 13.373 -0.431  10.149  1.00 9.72  ? 161 TYR   A CE1 1 
ATOM   1251 C CE2 . TYR   A 1 171 ? 11.229 -1.478  10.163  1.00 9.13  ? 161 TYR   A CE2 1 
ATOM   1252 C CZ  . TYR   A 1 171 ? 12.095 -0.536  10.679  1.00 9.79  ? 161 TYR   A CZ  1 
ATOM   1253 O OH  . TYR   A 1 171 ? 11.771 0.282   11.731  1.00 9.20  ? 161 TYR   A OH  1 
ATOM   1254 N N   . MET   A 1 172 ? 13.750 -4.977  10.007  1.00 8.54  ? 162 MET   A N   1 
ATOM   1255 C CA  . MET   A 1 172 ? 12.955 -5.580  11.108  1.00 8.64  ? 162 MET   A CA  1 
ATOM   1256 C C   . MET   A 1 172 ? 12.629 -4.461  12.090  1.00 8.05  ? 162 MET   A C   1 
ATOM   1257 O O   . MET   A 1 172 ? 13.520 -3.678  12.355  1.00 7.34  ? 162 MET   A O   1 
ATOM   1258 C CB  . MET   A 1 172 ? 13.662 -6.716  11.837  1.00 8.91  ? 162 MET   A CB  1 
ATOM   1259 C CG  . MET   A 1 172 ? 12.747 -7.296  12.876  1.00 9.20  ? 162 MET   A CG  1 
ATOM   1260 S SD  . MET   A 1 172 ? 13.202 -8.897  13.495  1.00 11.50 ? 162 MET   A SD  1 
ATOM   1261 C CE  . MET   A 1 172 ? 12.465 -9.906  12.219  1.00 10.90 ? 162 MET   A CE  1 
ATOM   1262 N N   . HIS   A 1 173 ? 11.361 -4.318  12.488  1.00 7.96  ? 163 HIS   A N   1 
ATOM   1263 C CA  . HIS   A 1 173 ? 10.908 -3.143  13.271  1.00 7.43  ? 163 HIS   A CA  1 
ATOM   1264 C C   . HIS   A 1 173 ? 11.302 -3.326  14.739  1.00 8.06  ? 163 HIS   A C   1 
ATOM   1265 O O   . HIS   A 1 173 ? 10.983 -4.366  15.282  1.00 7.91  ? 163 HIS   A O   1 
ATOM   1266 C CB  . HIS   A 1 173 ? 9.398  -2.898  13.157  1.00 7.39  ? 163 HIS   A CB  1 
ATOM   1267 C CG  . HIS   A 1 173 ? 9.023  -1.637  13.856  1.00 7.37  ? 163 HIS   A CG  1 
ATOM   1268 N ND1 . HIS   A 1 173 ? 9.671  -0.470  13.583  1.00 6.83  ? 163 HIS   A ND1 1 
ATOM   1269 C CD2 . HIS   A 1 173 ? 8.235  -1.417  14.934  1.00 6.87  ? 163 HIS   A CD2 1 
ATOM   1270 C CE1 . HIS   A 1 173 ? 9.215  0.454   14.399  1.00 7.45  ? 163 HIS   A CE1 1 
ATOM   1271 N NE2 . HIS   A 1 173 ? 8.311  -0.092  15.223  1.00 6.63  ? 163 HIS   A NE2 1 
ATOM   1272 N N   . HIS   A 1 174 ? 11.903 -2.308  15.353  1.00 7.92  ? 164 HIS   A N   1 
ATOM   1273 C CA  . HIS   A 1 174 ? 12.262 -2.379  16.797  1.00 8.36  ? 164 HIS   A CA  1 
ATOM   1274 C C   . HIS   A 1 174 ? 11.671 -1.251  17.634  1.00 8.16  ? 164 HIS   A C   1 
ATOM   1275 O O   . HIS   A 1 174 ? 11.421 -1.507  18.825  1.00 7.68  ? 164 HIS   A O   1 
ATOM   1276 C CB  . HIS   A 1 174 ? 13.776 -2.397  17.020  1.00 7.84  ? 164 HIS   A CB  1 
ATOM   1277 C CG  . HIS   A 1 174 ? 14.439 -3.666  16.567  1.00 8.55  ? 164 HIS   A CG  1 
ATOM   1278 N ND1 . HIS   A 1 174 ? 15.019 -4.546  17.446  1.00 8.08  ? 164 HIS   A ND1 1 
ATOM   1279 C CD2 . HIS   A 1 174 ? 14.643 -4.156  15.331  1.00 8.04  ? 164 HIS   A CD2 1 
ATOM   1280 C CE1 . HIS   A 1 174 ? 15.577 -5.541  16.785  1.00 8.49  ? 164 HIS   A CE1 1 
ATOM   1281 N NE2 . HIS   A 1 174 ? 15.355 -5.333  15.452  1.00 8.80  ? 164 HIS   A NE2 1 
ATOM   1282 N N   . MET   A 1 175 ? 11.560 -0.037  17.134  1.00 8.72  ? 165 MET   A N   1 
ATOM   1283 C CA  . MET   A 1 175 ? 11.237 1.075   18.062  1.00 9.56  ? 165 MET   A CA  1 
ATOM   1284 C C   . MET   A 1 175 ? 10.688 2.329   17.364  1.00 9.77  ? 165 MET   A C   1 
ATOM   1285 O O   . MET   A 1 175 ? 10.855 2.505   16.154  1.00 9.10  ? 165 MET   A O   1 
ATOM   1286 C CB  . MET   A 1 175 ? 12.475 1.481   18.881  1.00 10.23 ? 165 MET   A CB  1 
ATOM   1287 C CG  . MET   A 1 175 ? 13.616 2.039   18.054  1.00 11.84 ? 165 MET   A CG  1 
ATOM   1288 S SD  . MET   A 1 175 ? 15.174 2.120   19.038  1.00 13.95 ? 165 MET   A SD  1 
ATOM   1289 C CE  . MET   A 1 175 ? 14.690 3.275   20.321  1.00 11.85 ? 165 MET   A CE  1 
ATOM   1290 N N   . GLU   A 1 176 ? 10.179 3.241   18.194  1.00 10.66 ? 166 GLU   A N   1 
ATOM   1291 C CA  . GLU   A 1 176 ? 9.658  4.558   17.766  1.00 11.13 ? 166 GLU   A CA  1 
ATOM   1292 C C   . GLU   A 1 176 ? 10.399 5.686   18.497  1.00 12.39 ? 166 GLU   A C   1 
ATOM   1293 O O   . GLU   A 1 176 ? 10.570 5.616   19.748  1.00 12.22 ? 166 GLU   A O   1 
ATOM   1294 C CB  . GLU   A 1 176 ? 8.153  4.602   17.972  1.00 11.10 ? 166 GLU   A CB  1 
ATOM   1295 C CG  . GLU   A 1 176 ? 7.516  5.879   17.428  1.00 11.30 ? 166 GLU   A CG  1 
ATOM   1296 C CD  . GLU   A 1 176 ? 6.005  5.915   17.655  1.00 11.35 ? 166 GLU   A CD  1 
ATOM   1297 O OE1 . GLU   A 1 176 ? 5.498  6.873   18.348  1.00 12.34 ? 166 GLU   A OE1 1 
ATOM   1298 O OE2 . GLU   A 1 176 ? 5.331  4.953   17.248  1.00 10.42 ? 166 GLU   A OE2 1 
ATOM   1299 N N   . LEU   A 1 177 ? 10.773 6.711   17.736  1.00 13.25 ? 167 LEU   A N   1 
ATOM   1300 C CA  . LEU   A 1 177 ? 11.445 7.949   18.205  1.00 14.85 ? 167 LEU   A CA  1 
ATOM   1301 C C   . LEU   A 1 177 ? 10.444 9.097   18.177  1.00 16.69 ? 167 LEU   A C   1 
ATOM   1302 O O   . LEU   A 1 177 ? 9.402  8.987   17.543  1.00 17.65 ? 167 LEU   A O   1 
ATOM   1303 C CB  . LEU   A 1 177 ? 12.623 8.250   17.272  1.00 15.94 ? 167 LEU   A CB  1 
ATOM   1304 C CG  . LEU   A 1 177 ? 13.631 7.112   17.232  1.00 16.99 ? 167 LEU   A CG  1 
ATOM   1305 C CD1 . LEU   A 1 177 ? 14.560 7.226   16.064  1.00 19.91 ? 167 LEU   A CD1 1 
ATOM   1306 C CD2 . LEU   A 1 177 ? 14.393 7.072   18.554  1.00 16.79 ? 167 LEU   A CD2 1 
ATOM   1307 N N   . PRO   A 1 178 ? 10.735 10.226  18.861  1.00 19.40 ? 168 PRO   A N   1 
ATOM   1308 C CA  . PRO   A 1 178 ? 9.887  11.415  18.769  1.00 22.98 ? 168 PRO   A CA  1 
ATOM   1309 C C   . PRO   A 1 178 ? 9.815  11.961  17.336  1.00 26.27 ? 168 PRO   A C   1 
ATOM   1310 O O   . PRO   A 1 178 ? 10.780 11.871  16.616  1.00 30.31 ? 168 PRO   A O   1 
ATOM   1311 C CB  . PRO   A 1 178 ? 10.570 12.423  19.715  1.00 21.79 ? 168 PRO   A CB  1 
ATOM   1312 C CG  . PRO   A 1 178 ? 11.400 11.577  20.622  1.00 21.32 ? 168 PRO   A CG  1 
ATOM   1313 C CD  . PRO   A 1 178 ? 11.892 10.435  19.742  1.00 20.92 ? 168 PRO   A CD  1 
ATOM   1314 N N   . THR   A 1 179 ? 8.667  12.540  17.001  1.00 34.51 ? 169 THR   A N   1 
ATOM   1315 C CA  . THR   A 1 179 ? 8.173  12.867  15.641  1.00 35.69 ? 169 THR   A CA  1 
ATOM   1316 C C   . THR   A 1 179 ? 7.364  11.649  15.152  1.00 31.22 ? 169 THR   A C   1 
ATOM   1317 O O   . THR   A 1 179 ? 6.827  11.725  14.055  1.00 31.03 ? 169 THR   A O   1 
ATOM   1318 C CB  . THR   A 1 179 ? 9.274  13.439  14.710  1.00 41.12 ? 169 THR   A CB  1 
ATOM   1319 O OG1 . THR   A 1 179 ? 10.409 12.599  14.476  1.00 42.73 ? 169 THR   A OG1 1 
ATOM   1320 C CG2 . THR   A 1 179 ? 9.835  14.750  15.228  1.00 44.37 ? 169 THR   A CG2 1 
ATOM   1321 N N   . GLY   A 1 180 ? 7.215  10.594  15.966  1.00 26.36 ? 170 GLY   A N   1 
ATOM   1322 C CA  . GLY   A 1 180 ? 6.520  9.353   15.572  1.00 21.36 ? 170 GLY   A CA  1 
ATOM   1323 C C   . GLY   A 1 180 ? 7.147  8.752   14.320  1.00 18.39 ? 170 GLY   A C   1 
ATOM   1324 O O   . GLY   A 1 180 ? 6.434  8.537   13.331  1.00 17.49 ? 170 GLY   A O   1 
ATOM   1325 N N   . VAL   A 1 181 ? 8.470  8.637   14.318  1.00 16.64 ? 171 VAL   A N   1 
ATOM   1326 C CA  . VAL   A 1 181 ? 9.253  7.954   13.255  1.00 16.28 ? 171 VAL   A CA  1 
ATOM   1327 C C   . VAL   A 1 181 ? 9.851  6.688   13.858  1.00 13.67 ? 171 VAL   A C   1 
ATOM   1328 O O   . VAL   A 1 181 ? 9.936  6.546   15.115  1.00 12.96 ? 171 VAL   A O   1 
ATOM   1329 C CB  . VAL   A 1 181 ? 10.352 8.820   12.608  1.00 17.41 ? 171 VAL   A CB  1 
ATOM   1330 C CG1 . VAL   A 1 181 ? 9.781  9.998   11.832  1.00 18.18 ? 171 VAL   A CG1 1 
ATOM   1331 C CG2 . VAL   A 1 181 ? 11.390 9.293   13.599  1.00 17.82 ? 171 VAL   A CG2 1 
ATOM   1332 N N   . HIS   A 1 182 ? 10.342 5.830   12.981  1.00 11.61 ? 172 HIS   A N   1 
ATOM   1333 C CA  . HIS   A 1 182 ? 10.575 4.411   13.329  1.00 10.89 ? 172 HIS   A CA  1 
ATOM   1334 C C   . HIS   A 1 182 ? 12.010 4.011   13.005  1.00 10.51 ? 172 HIS   A C   1 
ATOM   1335 O O   . HIS   A 1 182 ? 12.580 4.536   12.040  1.00 11.06 ? 172 HIS   A O   1 
ATOM   1336 C CB  . HIS   A 1 182 ? 9.490  3.599   12.664  1.00 10.31 ? 172 HIS   A CB  1 
ATOM   1337 C CG  . HIS   A 1 182 ? 8.148  3.987   13.167  1.00 10.33 ? 172 HIS   A CG  1 
ATOM   1338 N ND1 . HIS   A 1 182 ? 7.207  4.589   12.344  1.00 9.42  ? 172 HIS   A ND1 1 
ATOM   1339 C CD2 . HIS   A 1 182 ? 7.597  3.870   14.401  1.00 10.83 ? 172 HIS   A CD2 1 
ATOM   1340 C CE1 . HIS   A 1 182 ? 6.107  4.803   13.060  1.00 11.20 ? 172 HIS   A CE1 1 
ATOM   1341 N NE2 . HIS   A 1 182 ? 6.325  4.384   14.343  1.00 10.67 ? 172 HIS   A NE2 1 
ATOM   1342 N N   . ALA   A 1 183 ? 12.575 3.187   13.876  1.00 10.07 ? 173 ALA   A N   1 
ATOM   1343 C CA  . ALA   A 1 183 ? 13.961 2.698   13.765  1.00 9.19  ? 173 ALA   A CA  1 
ATOM   1344 C C   . ALA   A 1 183 ? 13.923 1.182   13.888  1.00 9.15  ? 173 ALA   A C   1 
ATOM   1345 O O   . ALA   A 1 183 ? 13.063 0.633   14.628  1.00 7.79  ? 173 ALA   A O   1 
ATOM   1346 C CB  . ALA   A 1 183 ? 14.835 3.317   14.799  1.00 9.68  ? 173 ALA   A CB  1 
ATOM   1347 N N   . GLY   A 1 184 ? 14.874 0.537   13.233  1.00 8.36  ? 174 GLY   A N   1 
ATOM   1348 C CA  . GLY   A 1 184 ? 14.999 -0.910  13.329  1.00 7.83  ? 174 GLY   A CA  1 
ATOM   1349 C C   . GLY   A 1 184 ? 16.267 -1.369  12.704  1.00 8.21  ? 174 GLY   A C   1 
ATOM   1350 O O   . GLY   A 1 184 ? 17.189 -0.530  12.481  1.00 7.97  ? 174 GLY   A O   1 
ATOM   1351 N N   . THR   A 1 185 ? 16.304 -2.661  12.411  1.00 8.61  ? 175 THR   A N   1 
ATOM   1352 C CA  . THR   A 1 185 ? 17.569 -3.324  12.042  1.00 8.29  ? 175 THR   A CA  1 
ATOM   1353 C C   . THR   A 1 185 ? 17.416 -3.941  10.658  1.00 8.37  ? 175 THR   A C   1 
ATOM   1354 O O   . THR   A 1 185 ? 16.285 -4.129  10.188  1.00 7.78  ? 175 THR   A O   1 
ATOM   1355 C CB  . THR   A 1 185 ? 17.991 -4.370  13.079  1.00 8.11  ? 175 THR   A CB  1 
ATOM   1356 O OG1 . THR   A 1 185 ? 17.085 -5.478  13.026  1.00 7.81  ? 175 THR   A OG1 1 
ATOM   1357 C CG2 . THR   A 1 185 ? 18.068 -3.858  14.498  1.00 8.13  ? 175 THR   A CG2 1 
ATOM   1358 N N   . ASP   A 1 186 ? 18.545 -4.265  10.059  1.00 9.05  ? 176 ASP   A N   1 
ATOM   1359 C CA  . ASP   A 1 186 ? 18.582 -5.269  8.965   1.00 9.38  ? 176 ASP   A CA  1 
ATOM   1360 C C   . ASP   A 1 186 ? 18.356 -6.664  9.591   1.00 9.59  ? 176 ASP   A C   1 
ATOM   1361 O O   . ASP   A 1 186 ? 18.221 -6.776  10.826  1.00 9.39  ? 176 ASP   A O   1 
ATOM   1362 C CB  . ASP   A 1 186 ? 19.901 -5.143  8.201   1.00 9.51  ? 176 ASP   A CB  1 
ATOM   1363 C CG  . ASP   A 1 186 ? 21.155 -5.539  8.945   1.00 9.62  ? 176 ASP   A CG  1 
ATOM   1364 O OD1 . ASP   A 1 186 ? 21.058 -6.209  9.994   1.00 9.16  ? 176 ASP   A OD1 1 
ATOM   1365 O OD2 . ASP   A 1 186 ? 22.273 -5.100  8.485   1.00 9.23  ? 176 ASP   A OD2 1 
ATOM   1366 N N   . LEU   A 1 187 ? 18.366 -7.729  8.792   1.00 10.38 ? 177 LEU   A N   1 
ATOM   1367 C CA  . LEU   A 1 187 ? 18.043 -9.079  9.319   1.00 11.65 ? 177 LEU   A CA  1 
ATOM   1368 C C   . LEU   A 1 187 ? 19.269 -9.736  9.975   1.00 13.13 ? 177 LEU   A C   1 
ATOM   1369 O O   . LEU   A 1 187 ? 19.127 -10.891 10.447  1.00 13.50 ? 177 LEU   A O   1 
ATOM   1370 C CB  . LEU   A 1 187 ? 17.473 -9.906  8.166   1.00 12.24 ? 177 LEU   A CB  1 
ATOM   1371 C CG  . LEU   A 1 187 ? 15.956 -9.868  8.072   1.00 12.65 ? 177 LEU   A CG  1 
ATOM   1372 C CD1 . LEU   A 1 187 ? 15.348 -10.619 9.247   1.00 13.30 ? 177 LEU   A CD1 1 
ATOM   1373 C CD2 . LEU   A 1 187 ? 15.428 -8.437  7.997   1.00 13.71 ? 177 LEU   A CD2 1 
ATOM   1374 N N   . GLU   A 1 188 ? 20.427 -9.056  10.003  1.00 12.27 ? 178 GLU   A N   1 
ATOM   1375 C CA  . GLU   A 1 188 ? 21.596 -9.458  10.824  1.00 12.51 ? 178 GLU   A CA  1 
ATOM   1376 C C   . GLU   A 1 188 ? 21.513 -8.771  12.186  1.00 11.66 ? 178 GLU   A C   1 
ATOM   1377 O O   . GLU   A 1 188 ? 22.444 -8.915  12.988  1.00 13.15 ? 178 GLU   A O   1 
ATOM   1378 C CB  . GLU   A 1 188 ? 22.923 -9.120  10.138  1.00 13.02 ? 178 GLU   A CB  1 
ATOM   1379 C CG  . GLU   A 1 188 ? 23.061 -9.802  8.800   1.00 14.49 ? 178 GLU   A CG  1 
ATOM   1380 C CD  . GLU   A 1 188 ? 24.433 -9.716  8.135   1.00 17.15 ? 178 GLU   A CD  1 
ATOM   1381 O OE1 . GLU   A 1 188 ? 25.168 -8.735  8.383   1.00 16.76 ? 178 GLU   A OE1 1 
ATOM   1382 O OE2 . GLU   A 1 188 ? 24.774 -10.677 7.400   1.00 17.64 ? 178 GLU   A OE2 1 
ATOM   1383 N N   . GLY   A 1 189 ? 20.454 -8.000  12.433  1.00 10.49 ? 179 GLY   A N   1 
ATOM   1384 C CA  . GLY   A 1 189 ? 20.239 -7.371  13.742  1.00 9.92  ? 179 GLY   A CA  1 
ATOM   1385 C C   . GLY   A 1 189 ? 21.045 -6.105  13.953  1.00 10.44 ? 179 GLY   A C   1 
ATOM   1386 O O   . GLY   A 1 189 ? 21.141 -5.699  15.095  1.00 10.47 ? 179 GLY   A O   1 
ATOM   1387 N N   . ASN   A 1 190 ? 21.602 -5.504  12.901  1.00 10.15 ? 180 ASN   A N   1 
ATOM   1388 C CA  . ASN   A 1 190 ? 22.367 -4.236  12.983  1.00 10.69 ? 180 ASN   A CA  1 
ATOM   1389 C C   . ASN   A 1 190 ? 21.385 -3.084  12.730  1.00 9.89  ? 180 ASN   A C   1 
ATOM   1390 O O   . ASN   A 1 190 ? 20.778 -3.045  11.645  1.00 8.87  ? 180 ASN   A O   1 
ATOM   1391 C CB  . ASN   A 1 190 ? 23.553 -4.246  12.004  1.00 11.48 ? 180 ASN   A CB  1 
ATOM   1392 C CG  . ASN   A 1 190 ? 24.720 -5.082  12.496  1.00 12.49 ? 180 ASN   A CG  1 
ATOM   1393 O OD1 . ASN   A 1 190 ? 25.268 -5.888  11.756  1.00 15.41 ? 180 ASN   A OD1 1 
ATOM   1394 N ND2 . ASN   A 1 190 ? 25.089 -4.949  13.754  1.00 12.77 ? 180 ASN   A ND2 1 
ATOM   1395 N N   . PHE   A 1 191 ? 21.279 -2.140  13.673  1.00 9.32  ? 181 PHE   A N   1 
ATOM   1396 C CA  . PHE   A 1 191 ? 20.425 -0.944  13.463  1.00 9.53  ? 181 PHE   A CA  1 
ATOM   1397 C C   . PHE   A 1 191 ? 20.844 -0.228  12.177  1.00 9.59  ? 181 PHE   A C   1 
ATOM   1398 O O   . PHE   A 1 191 ? 22.059 -0.153  11.879  1.00 8.08  ? 181 PHE   A O   1 
ATOM   1399 C CB  . PHE   A 1 191 ? 20.423 -0.002  14.666  1.00 9.07  ? 181 PHE   A CB  1 
ATOM   1400 C CG  . PHE   A 1 191 ? 19.269 -0.267  15.597  1.00 8.87  ? 181 PHE   A CG  1 
ATOM   1401 C CD1 . PHE   A 1 191 ? 18.008 0.319   15.402  1.00 9.49  ? 181 PHE   A CD1 1 
ATOM   1402 C CD2 . PHE   A 1 191 ? 19.409 -1.195  16.612  1.00 9.21  ? 181 PHE   A CD2 1 
ATOM   1403 C CE1 . PHE   A 1 191 ? 16.947 -0.006  16.233  1.00 9.51  ? 181 PHE   A CE1 1 
ATOM   1404 C CE2 . PHE   A 1 191 ? 18.371 -1.467  17.486  1.00 9.36  ? 181 PHE   A CE2 1 
ATOM   1405 C CZ  . PHE   A 1 191 ? 17.129 -0.897  17.275  1.00 9.38  ? 181 PHE   A CZ  1 
ATOM   1406 N N   . TYR   A 1 192 ? 19.856 0.319   11.478  1.00 9.84  ? 182 TYR   A N   1 
ATOM   1407 C CA  . TYR   A 1 192 ? 20.044 1.499   10.611  1.00 10.58 ? 182 TYR   A CA  1 
ATOM   1408 C C   . TYR   A 1 192 ? 20.252 2.702   11.529  1.00 11.48 ? 182 TYR   A C   1 
ATOM   1409 O O   . TYR   A 1 192 ? 19.459 2.922   12.448  1.00 11.53 ? 182 TYR   A O   1 
ATOM   1410 C CB  . TYR   A 1 192 ? 18.859 1.653   9.660   1.00 10.79 ? 182 TYR   A CB  1 
ATOM   1411 C CG  . TYR   A 1 192 ? 18.784 0.533   8.665   1.00 10.78 ? 182 TYR   A CG  1 
ATOM   1412 C CD1 . TYR   A 1 192 ? 19.596 0.554   7.537   1.00 11.05 ? 182 TYR   A CD1 1 
ATOM   1413 C CD2 . TYR   A 1 192 ? 17.923 -0.543  8.832   1.00 10.86 ? 182 TYR   A CD2 1 
ATOM   1414 C CE1 . TYR   A 1 192 ? 19.568 -0.482  6.621   1.00 10.38 ? 182 TYR   A CE1 1 
ATOM   1415 C CE2 . TYR   A 1 192 ? 17.898 -1.597  7.931   1.00 10.14 ? 182 TYR   A CE2 1 
ATOM   1416 C CZ  . TYR   A 1 192 ? 18.692 -1.542  6.793   1.00 9.40  ? 182 TYR   A CZ  1 
ATOM   1417 O OH  . TYR   A 1 192 ? 18.665 -2.571  5.886   1.00 9.56  ? 182 TYR   A OH  1 
ATOM   1418 N N   . GLY   A 1 193 ? 21.282 3.496   11.256  1.00 12.12 ? 183 GLY   A N   1 
ATOM   1419 C CA  . GLY   A 1 193 ? 21.592 4.689   12.058  1.00 12.38 ? 183 GLY   A CA  1 
ATOM   1420 C C   . GLY   A 1 193 ? 22.221 4.311   13.395  1.00 13.77 ? 183 GLY   A C   1 
ATOM   1421 O O   . GLY   A 1 193 ? 22.651 3.178   13.608  1.00 12.92 ? 183 GLY   A O   1 
ATOM   1422 N N   . PRO   A 1 194 ? 22.282 5.289   14.322  1.00 12.06 ? 184 PRO   A N   1 
ATOM   1423 C CA  . PRO   A 1 194 ? 22.989 5.143   15.587  1.00 12.85 ? 184 PRO   A CA  1 
ATOM   1424 C C   . PRO   A 1 194 ? 22.112 4.648   16.746  1.00 11.62 ? 184 PRO   A C   1 
ATOM   1425 O O   . PRO   A 1 194 ? 22.581 4.686   17.874  1.00 12.04 ? 184 PRO   A O   1 
ATOM   1426 C CB  . PRO   A 1 194 ? 23.386 6.614   15.821  1.00 12.32 ? 184 PRO   A CB  1 
ATOM   1427 C CG  . PRO   A 1 194 ? 22.172 7.371   15.396  1.00 13.17 ? 184 PRO   A CG  1 
ATOM   1428 C CD  . PRO   A 1 194 ? 21.735 6.636   14.143  1.00 13.58 ? 184 PRO   A CD  1 
ATOM   1429 N N   . PHE   A 1 195 ? 20.866 4.250   16.455  1.00 11.32 ? 185 PHE   A N   1 
ATOM   1430 C CA  . PHE   A 1 195 ? 19.864 3.887   17.474  1.00 11.48 ? 185 PHE   A CA  1 
ATOM   1431 C C   . PHE   A 1 195 ? 20.307 2.608   18.196  1.00 10.99 ? 185 PHE   A C   1 
ATOM   1432 O O   . PHE   A 1 195 ? 21.028 1.723   17.636  1.00 10.89 ? 185 PHE   A O   1 
ATOM   1433 C CB  . PHE   A 1 195 ? 18.461 3.854   16.861  1.00 11.26 ? 185 PHE   A CB  1 
ATOM   1434 C CG  . PHE   A 1 195 ? 18.202 5.093   16.039  1.00 11.26 ? 185 PHE   A CG  1 
ATOM   1435 C CD1 . PHE   A 1 195 ? 18.174 6.350   16.649  1.00 11.63 ? 185 PHE   A CD1 1 
ATOM   1436 C CD2 . PHE   A 1 195 ? 18.074 5.004   14.668  1.00 10.71 ? 185 PHE   A CD2 1 
ATOM   1437 C CE1 . PHE   A 1 195 ? 17.986 7.495   15.878  1.00 11.90 ? 185 PHE   A CE1 1 
ATOM   1438 C CE2 . PHE   A 1 195 ? 17.900 6.150   13.906  1.00 11.14 ? 185 PHE   A CE2 1 
ATOM   1439 C CZ  . PHE   A 1 195 ? 17.857 7.393   14.511  1.00 12.13 ? 185 PHE   A CZ  1 
ATOM   1440 N N   . VAL   A 1 196 ? 19.901 2.562   19.461  1.00 10.39 ? 186 VAL   A N   1 
ATOM   1441 C CA  . VAL   A 1 196 ? 20.003 1.351   20.312  1.00 11.01 ? 186 VAL   A CA  1 
ATOM   1442 C C   . VAL   A 1 196 ? 18.625 0.962   20.860  1.00 10.56 ? 186 VAL   A C   1 
ATOM   1443 O O   . VAL   A 1 196 ? 17.768 1.859   21.119  1.00 10.61 ? 186 VAL   A O   1 
ATOM   1444 C CB  . VAL   A 1 196 ? 21.022 1.575   21.429  1.00 12.13 ? 186 VAL   A CB  1 
ATOM   1445 C CG1 . VAL   A 1 196 ? 22.389 1.782   20.804  1.00 13.03 ? 186 VAL   A CG1 1 
ATOM   1446 C CG2 . VAL   A 1 196 ? 20.606 2.722   22.339  1.00 13.35 ? 186 VAL   A CG2 1 
ATOM   1447 N N   . ASP   A 1 197 ? 18.494 -0.328  21.148  1.00 10.86 ? 187 ASP   A N   1 
ATOM   1448 C CA  . ASP   A 1 197 ? 17.231 -0.962  21.603  1.00 10.56 ? 187 ASP   A CA  1 
ATOM   1449 C C   . ASP   A 1 197 ? 17.165 -0.845  23.123  1.00 11.42 ? 187 ASP   A C   1 
ATOM   1450 O O   . ASP   A 1 197 ? 17.234 -1.862  23.840  1.00 10.89 ? 187 ASP   A O   1 
ATOM   1451 C CB  . ASP   A 1 197 ? 17.079 -2.377  21.052  1.00 10.96 ? 187 ASP   A CB  1 
ATOM   1452 C CG  . ASP   A 1 197 ? 18.230 -3.332  21.266  1.00 11.82 ? 187 ASP   A CG  1 
ATOM   1453 O OD1 . ASP   A 1 197 ? 19.387 -2.883  21.615  1.00 12.26 ? 187 ASP   A OD1 1 
ATOM   1454 O OD2 . ASP   A 1 197 ? 17.988 -4.532  21.043  1.00 12.92 ? 187 ASP   A OD2 1 
ATOM   1455 N N   . ARG   A 1 198 ? 17.032 0.395   23.573  1.00 12.07 ? 188 ARG   A N   1 
ATOM   1456 C CA  . ARG   A 1 198 ? 16.912 0.738   25.000  1.00 13.75 ? 188 ARG   A CA  1 
ATOM   1457 C C   . ARG   A 1 198 ? 15.975 1.940   25.072  1.00 13.17 ? 188 ARG   A C   1 
ATOM   1458 O O   . ARG   A 1 198 ? 16.090 2.819   24.221  1.00 11.34 ? 188 ARG   A O   1 
ATOM   1459 C CB  . ARG   A 1 198 ? 18.296 1.044   25.586  1.00 15.90 ? 188 ARG   A CB  1 
ATOM   1460 C CG  . ARG   A 1 198 ? 18.245 1.668   26.971  1.00 19.44 ? 188 ARG   A CG  1 
ATOM   1461 C CD  . ARG   A 1 198 ? 19.596 2.110   27.482  1.00 22.88 ? 188 ARG   A CD  1 
ATOM   1462 N NE  . ARG   A 1 198 ? 19.475 2.737   28.788  1.00 24.84 ? 188 ARG   A NE  1 
ATOM   1463 C CZ  . ARG   A 1 198 ? 20.477 3.304   29.445  1.00 28.07 ? 188 ARG   A CZ  1 
ATOM   1464 N NH1 . ARG   A 1 198 ? 21.692 3.329   28.914  1.00 29.14 ? 188 ARG   A NH1 1 
ATOM   1465 N NH2 . ARG   A 1 198 ? 20.259 3.844   30.631  1.00 28.30 ? 188 ARG   A NH2 1 
ATOM   1466 N N   . GLN   A 1 199 ? 15.072 1.934   26.057  1.00 12.51 ? 189 GLN   A N   1 
ATOM   1467 C CA  . GLN   A 1 199 ? 14.127 3.050   26.269  1.00 13.69 ? 189 GLN   A CA  1 
ATOM   1468 C C   . GLN   A 1 199 ? 14.848 4.191   26.971  1.00 14.44 ? 189 GLN   A C   1 
ATOM   1469 O O   . GLN   A 1 199 ? 14.669 4.424   28.204  1.00 13.41 ? 189 GLN   A O   1 
ATOM   1470 C CB  . GLN   A 1 199 ? 12.886 2.560   26.992  1.00 13.55 ? 189 GLN   A CB  1 
ATOM   1471 C CG  . GLN   A 1 199 ? 11.824 3.629   27.072  1.00 14.52 ? 189 GLN   A CG  1 
ATOM   1472 C CD  . GLN   A 1 199 ? 10.594 3.004   27.667  1.00 14.35 ? 189 GLN   A CD  1 
ATOM   1473 O OE1 . GLN   A 1 199 ? 10.151 1.974   27.184  1.00 17.15 ? 189 GLN   A OE1 1 
ATOM   1474 N NE2 . GLN   A 1 199 ? 10.036 3.619   28.700  1.00 14.79 ? 189 GLN   A NE2 1 
ATOM   1475 N N   . THR   A 1 200 ? 15.674 4.897   26.214  1.00 15.42 ? 190 THR   A N   1 
ATOM   1476 C CA  . THR   A 1 200 ? 16.337 6.113   26.735  1.00 17.26 ? 190 THR   A CA  1 
ATOM   1477 C C   . THR   A 1 200 ? 16.247 7.140   25.625  1.00 18.02 ? 190 THR   A C   1 
ATOM   1478 O O   . THR   A 1 200 ? 16.142 6.721   24.453  1.00 18.73 ? 190 THR   A O   1 
ATOM   1479 C CB  . THR   A 1 200 ? 17.756 5.836   27.243  1.00 18.96 ? 190 THR   A CB  1 
ATOM   1480 O OG1 . THR   A 1 200 ? 18.083 6.939   28.102  1.00 19.13 ? 190 THR   A OG1 1 
ATOM   1481 C CG2 . THR   A 1 200 ? 18.746 5.684   26.115  1.00 21.62 ? 190 THR   A CG2 1 
ATOM   1482 N N   . ALA   A 1 201 ? 16.356 8.408   25.990  1.00 18.15 ? 191 ALA   A N   1 
ATOM   1483 C CA  . ALA   A 1 201 ? 16.191 9.546   25.067  1.00 19.21 ? 191 ALA   A CA  1 
ATOM   1484 C C   . ALA   A 1 201 ? 17.138 9.319   23.894  1.00 19.24 ? 191 ALA   A C   1 
ATOM   1485 O O   . ALA   A 1 201 ? 18.329 9.157   24.144  1.00 20.62 ? 191 ALA   A O   1 
ATOM   1486 C CB  . ALA   A 1 201 ? 16.471 10.851  25.777  1.00 20.72 ? 191 ALA   A CB  1 
ATOM   1487 N N   . GLN   A 1 202 ? 16.576 9.205   22.694  1.00 17.51 ? 192 GLN   A N   1 
ATOM   1488 C CA  . GLN   A 1 202 ? 17.308 9.228   21.407  1.00 17.37 ? 192 GLN   A CA  1 
ATOM   1489 C C   . GLN   A 1 202 ? 16.508 10.111  20.462  1.00 17.98 ? 192 GLN   A C   1 
ATOM   1490 O O   . GLN   A 1 202 ? 15.262 10.216  20.618  1.00 17.59 ? 192 GLN   A O   1 
ATOM   1491 C CB  . GLN   A 1 202 ? 17.509 7.816   20.859  1.00 16.51 ? 192 GLN   A CB  1 
ATOM   1492 C CG  . GLN   A 1 202 ? 18.243 6.905   21.825  1.00 15.57 ? 192 GLN   A CG  1 
ATOM   1493 C CD  . GLN   A 1 202 ? 18.213 5.472   21.358  1.00 15.15 ? 192 GLN   A CD  1 
ATOM   1494 O OE1 . GLN   A 1 202 ? 18.772 5.137   20.315  1.00 16.37 ? 192 GLN   A OE1 1 
ATOM   1495 N NE2 . GLN   A 1 202 ? 17.582 4.623   22.140  1.00 14.38 ? 192 GLN   A NE2 1 
ATOM   1496 N N   . ALA   A 1 203 ? 17.205 10.765  19.548  1.00 17.32 ? 193 ALA   A N   1 
ATOM   1497 C CA  . ALA   A 1 203 ? 16.598 11.765  18.656  1.00 18.49 ? 193 ALA   A CA  1 
ATOM   1498 C C   . ALA   A 1 203 ? 17.110 11.497  17.247  1.00 18.82 ? 193 ALA   A C   1 
ATOM   1499 O O   . ALA   A 1 203 ? 18.305 11.118  17.114  1.00 18.89 ? 193 ALA   A O   1 
ATOM   1500 C CB  . ALA   A 1 203 ? 16.936 13.149  19.125  1.00 17.53 ? 193 ALA   A CB  1 
ATOM   1501 N N   . ALA   A 1 204 ? 16.212 11.633  16.271  1.00 19.21 ? 194 ALA   A N   1 
ATOM   1502 C CA  . ALA   A 1 204 ? 16.540 11.606  14.828  1.00 18.54 ? 194 ALA   A CA  1 
ATOM   1503 C C   . ALA   A 1 204 ? 17.307 12.888  14.489  1.00 17.81 ? 194 ALA   A C   1 
ATOM   1504 O O   . ALA   A 1 204 ? 16.947 13.960  15.036  1.00 16.78 ? 194 ALA   A O   1 
ATOM   1505 C CB  . ALA   A 1 204 ? 15.273 11.479  13.998  1.00 18.17 ? 194 ALA   A CB  1 
ATOM   1506 N N   . GLY   A 1 205 ? 18.290 12.784  13.602  1.00 17.18 ? 195 GLY   A N   1 
ATOM   1507 C CA  . GLY   A 1 205 ? 18.947 13.935  12.956  1.00 16.54 ? 195 GLY   A CA  1 
ATOM   1508 C C   . GLY   A 1 205 ? 18.042 14.625  11.953  1.00 16.17 ? 195 GLY   A C   1 
ATOM   1509 O O   . GLY   A 1 205 ? 16.867 14.214  11.779  1.00 14.63 ? 195 GLY   A O   1 
ATOM   1510 N N   . THR   A 1 206 ? 18.586 15.635  11.274  1.00 14.33 ? 196 THR   A N   1 
ATOM   1511 C CA  . THR   A 1 206 ? 17.882 16.407  10.222  1.00 15.17 ? 196 THR   A CA  1 
ATOM   1512 C C   . THR   A 1 206 ? 17.231 15.454  9.216   1.00 15.58 ? 196 THR   A C   1 
ATOM   1513 O O   . THR   A 1 206 ? 17.931 14.609  8.655   1.00 14.93 ? 196 THR   A O   1 
ATOM   1514 C CB  . THR   A 1 206 ? 18.858 17.355  9.519   1.00 16.18 ? 196 THR   A CB  1 
ATOM   1515 O OG1 . THR   A 1 206 ? 19.394 18.203  10.534  1.00 16.69 ? 196 THR   A OG1 1 
ATOM   1516 C CG2 . THR   A 1 206 ? 18.203 18.190  8.443   1.00 16.31 ? 196 THR   A CG2 1 
ATOM   1517 N N   . ASP   A 1 207 ? 15.959 15.690  8.903   1.00 16.65 ? 197 ASP   A N   1 
ATOM   1518 C CA  . ASP   A 1 207 ? 15.255 14.864  7.900   1.00 17.54 ? 197 ASP   A CA  1 
ATOM   1519 C C   . ASP   A 1 207 ? 15.456 15.460  6.507   1.00 16.54 ? 197 ASP   A C   1 
ATOM   1520 O O   . ASP   A 1 207 ? 14.583 16.176  6.039   1.00 19.81 ? 197 ASP   A O   1 
ATOM   1521 C CB  . ASP   A 1 207 ? 13.788 14.712  8.242   1.00 19.37 ? 197 ASP   A CB  1 
ATOM   1522 C CG  . ASP   A 1 207 ? 13.135 13.620  7.421   1.00 21.13 ? 197 ASP   A CG  1 
ATOM   1523 O OD1 . ASP   A 1 207 ? 13.872 12.755  6.827   1.00 18.50 ? 197 ASP   A OD1 1 
ATOM   1524 O OD2 . ASP   A 1 207 ? 11.902 13.665  7.378   1.00 22.13 ? 197 ASP   A OD2 1 
ATOM   1525 N N   . THR   A 1 208 ? 16.590 15.134  5.908   1.00 15.67 ? 198 THR   A N   1 
ATOM   1526 C CA  . THR   A 1 208 ? 17.022 15.523  4.554   1.00 15.13 ? 198 THR   A CA  1 
ATOM   1527 C C   . THR   A 1 208 ? 16.070 14.912  3.527   1.00 14.70 ? 198 THR   A C   1 
ATOM   1528 O O   . THR   A 1 208 ? 15.592 13.789  3.766   1.00 15.35 ? 198 THR   A O   1 
ATOM   1529 C CB  . THR   A 1 208 ? 18.484 15.080  4.391   1.00 17.13 ? 198 THR   A CB  1 
ATOM   1530 O OG1 . THR   A 1 208 ? 19.150 15.739  5.476   1.00 19.76 ? 198 THR   A OG1 1 
ATOM   1531 C CG2 . THR   A 1 208 ? 19.102 15.472  3.076   1.00 17.22 ? 198 THR   A CG2 1 
ATOM   1532 N N   . THR   A 1 209 ? 15.795 15.644  2.446   1.00 14.27 ? 199 THR   A N   1 
ATOM   1533 C CA  . THR   A 1 209 ? 14.928 15.200  1.327   1.00 12.77 ? 199 THR   A CA  1 
ATOM   1534 C C   . THR   A 1 209 ? 15.775 14.448  0.304   1.00 12.69 ? 199 THR   A C   1 
ATOM   1535 O O   . THR   A 1 209 ? 16.933 14.911  -0.030  1.00 12.35 ? 199 THR   A O   1 
ATOM   1536 C CB  . THR   A 1 209 ? 14.172 16.377  0.717   1.00 13.12 ? 199 THR   A CB  1 
ATOM   1537 O OG1 . THR   A 1 209 ? 13.371 16.902  1.771   1.00 13.21 ? 199 THR   A OG1 1 
ATOM   1538 C CG2 . THR   A 1 209 ? 13.311 16.012  -0.472  1.00 13.30 ? 199 THR   A CG2 1 
ATOM   1539 N N   . ILE   A 1 210 ? 15.239 13.326  -0.192  1.00 10.78 ? 200 ILE   A N   1 
ATOM   1540 C CA  . ILE   A 1 210 ? 15.953 12.437  -1.149  1.00 9.92  ? 200 ILE   A CA  1 
ATOM   1541 C C   . ILE   A 1 210 ? 15.775 13.029  -2.554  1.00 10.02 ? 200 ILE   A C   1 
ATOM   1542 O O   . ILE   A 1 210 ? 14.806 12.680  -3.261  1.00 9.99  ? 200 ILE   A O   1 
ATOM   1543 C CB  . ILE   A 1 210 ? 15.478 10.985  -1.036  1.00 9.59  ? 200 ILE   A CB  1 
ATOM   1544 C CG1 . ILE   A 1 210 ? 15.558 10.465  0.414   1.00 9.98  ? 200 ILE   A CG1 1 
ATOM   1545 C CG2 . ILE   A 1 210 ? 16.271 10.117  -1.986  1.00 10.04 ? 200 ILE   A CG2 1 
ATOM   1546 C CD1 . ILE   A 1 210 ? 14.501 9.445   0.709   1.00 10.62 ? 200 ILE   A CD1 1 
ATOM   1547 N N   . THR   A 1 211 ? 16.678 13.937  -2.916  1.00 9.89  ? 201 THR   A N   1 
ATOM   1548 C CA  . THR   A 1 211 ? 16.643 14.745  -4.163  1.00 9.46  ? 201 THR   A CA  1 
ATOM   1549 C C   . THR   A 1 211 ? 16.408 13.889  -5.417  1.00 9.49  ? 201 THR   A C   1 
ATOM   1550 O O   . THR   A 1 211 ? 15.534 14.265  -6.228  1.00 9.83  ? 201 THR   A O   1 
ATOM   1551 C CB  . THR   A 1 211 ? 17.958 15.507  -4.356  1.00 9.25  ? 201 THR   A CB  1 
ATOM   1552 O OG1 . THR   A 1 211 ? 18.146 16.230  -3.145  1.00 9.82  ? 201 THR   A OG1 1 
ATOM   1553 C CG2 . THR   A 1 211 ? 17.928 16.448  -5.544  1.00 9.58  ? 201 THR   A CG2 1 
ATOM   1554 N N   . VAL   A 1 212 ? 17.159 12.807  -5.598  1.00 9.09  ? 202 VAL   A N   1 
ATOM   1555 C CA  . VAL   A 1 212 ? 17.033 11.930  -6.799  1.00 8.56  ? 202 VAL   A CA  1 
ATOM   1556 C C   . VAL   A 1 212 ? 15.605 11.366  -6.857  1.00 8.33  ? 202 VAL   A C   1 
ATOM   1557 O O   . VAL   A 1 212 ? 15.060 11.204  -7.958  1.00 6.97  ? 202 VAL   A O   1 
ATOM   1558 C CB  . VAL   A 1 212 ? 18.090 10.810  -6.836  1.00 8.94  ? 202 VAL   A CB  1 
ATOM   1559 C CG1 . VAL   A 1 212 ? 17.945 9.804   -5.714  1.00 9.40  ? 202 VAL   A CG1 1 
ATOM   1560 C CG2 . VAL   A 1 212 ? 18.084 10.082  -8.160  1.00 9.53  ? 202 VAL   A CG2 1 
ATOM   1561 N N   . ASN   A 1 213 ? 15.023 11.026  -5.707  1.00 7.86  ? 203 ASN   A N   1 
ATOM   1562 C CA  . ASN   A 1 213 ? 13.629 10.514  -5.667  1.00 8.00  ? 203 ASN   A CA  1 
ATOM   1563 C C   . ASN   A 1 213 ? 12.607 11.587  -6.087  1.00 7.96  ? 203 ASN   A C   1 
ATOM   1564 O O   . ASN   A 1 213 ? 11.616 11.263  -6.767  1.00 7.80  ? 203 ASN   A O   1 
ATOM   1565 C CB  . ASN   A 1 213 ? 13.318 9.970   -4.282  1.00 8.09  ? 203 ASN   A CB  1 
ATOM   1566 C CG  . ASN   A 1 213 ? 13.990 8.656   -4.007  1.00 8.18  ? 203 ASN   A CG  1 
ATOM   1567 O OD1 . ASN   A 1 213 ? 14.828 8.174   -4.778  1.00 7.77  ? 203 ASN   A OD1 1 
ATOM   1568 N ND2 . ASN   A 1 213 ? 13.662 8.095   -2.859  1.00 8.51  ? 203 ASN   A ND2 1 
ATOM   1569 N N   . VAL   A 1 214 ? 12.768 12.830  -5.640  1.00 7.79  ? 204 VAL   A N   1 
ATOM   1570 C CA  . VAL   A 1 214 ? 11.859 13.935  -6.049  1.00 8.29  ? 204 VAL   A CA  1 
ATOM   1571 C C   . VAL   A 1 214 ? 11.922 14.070  -7.581  1.00 7.88  ? 204 VAL   A C   1 
ATOM   1572 O O   . VAL   A 1 214 ? 10.873 14.196  -8.199  1.00 8.26  ? 204 VAL   A O   1 
ATOM   1573 C CB  . VAL   A 1 214 ? 12.194 15.233  -5.311  1.00 8.20  ? 204 VAL   A CB  1 
ATOM   1574 C CG1 . VAL   A 1 214 ? 11.402 16.416  -5.818  1.00 8.57  ? 204 VAL   A CG1 1 
ATOM   1575 C CG2 . VAL   A 1 214 ? 12.029 15.065  -3.796  1.00 8.49  ? 204 VAL   A CG2 1 
ATOM   1576 N N   . LEU   A 1 215 ? 13.109 13.991  -8.164  1.00 8.26  ? 205 LEU   A N   1 
ATOM   1577 C CA  . LEU   A 1 215 ? 13.268 14.121  -9.634  1.00 8.17  ? 205 LEU   A CA  1 
ATOM   1578 C C   . LEU   A 1 215 ? 12.599 12.932  -10.306 1.00 7.68  ? 205 LEU   A C   1 
ATOM   1579 O O   . LEU   A 1 215 ? 11.880 13.119  -11.292 1.00 8.22  ? 205 LEU   A O   1 
ATOM   1580 C CB  . LEU   A 1 215 ? 14.759 14.196  -9.973  1.00 8.24  ? 205 LEU   A CB  1 
ATOM   1581 C CG  . LEU   A 1 215 ? 15.404 15.499  -9.562  1.00 8.56  ? 205 LEU   A CG  1 
ATOM   1582 C CD1 . LEU   A 1 215 ? 16.911 15.354  -9.576  1.00 8.81  ? 205 LEU   A CD1 1 
ATOM   1583 C CD2 . LEU   A 1 215 ? 14.943 16.638  -10.470 1.00 8.75  ? 205 LEU   A CD2 1 
ATOM   1584 N N   . ALA   A 1 216 ? 12.767 11.732  -9.765  1.00 7.70  ? 206 ALA   A N   1 
ATOM   1585 C CA  . ALA   A 1 216 ? 12.130 10.535  -10.345 1.00 7.53  ? 206 ALA   A CA  1 
ATOM   1586 C C   . ALA   A 1 216 ? 10.606 10.762  -10.368 1.00 7.55  ? 206 ALA   A C   1 
ATOM   1587 O O   . ALA   A 1 216 ? 9.959  10.447  -11.344 1.00 7.37  ? 206 ALA   A O   1 
ATOM   1588 C CB  . ALA   A 1 216 ? 12.488 9.295   -9.566  1.00 7.81  ? 206 ALA   A CB  1 
ATOM   1589 N N   . TRP   A 1 217 ? 10.046 11.307  -9.296  1.00 7.55  ? 207 TRP   A N   1 
ATOM   1590 C CA  . TRP   A 1 217 ? 8.590  11.510  -9.166  1.00 7.68  ? 207 TRP   A CA  1 
ATOM   1591 C C   . TRP   A 1 217 ? 8.135  12.619  -10.120 1.00 7.47  ? 207 TRP   A C   1 
ATOM   1592 O O   . TRP   A 1 217 ? 7.055  12.537  -10.722 1.00 7.22  ? 207 TRP   A O   1 
ATOM   1593 C CB  . TRP   A 1 217 ? 8.265  11.801  -7.699  1.00 8.09  ? 207 TRP   A CB  1 
ATOM   1594 C CG  . TRP   A 1 217 ? 6.882  12.270  -7.399  1.00 8.42  ? 207 TRP   A CG  1 
ATOM   1595 C CD1 . TRP   A 1 217 ? 5.756  11.522  -7.207  1.00 8.70  ? 207 TRP   A CD1 1 
ATOM   1596 C CD2 . TRP   A 1 217 ? 6.523  13.627  -7.097  1.00 8.56  ? 207 TRP   A CD2 1 
ATOM   1597 N NE1 . TRP   A 1 217 ? 4.708  12.322  -6.834  1.00 8.89  ? 207 TRP   A NE1 1 
ATOM   1598 C CE2 . TRP   A 1 217 ? 5.144  13.626  -6.788  1.00 8.96  ? 207 TRP   A CE2 1 
ATOM   1599 C CE3 . TRP   A 1 217 ? 7.236  14.830  -7.062  1.00 9.14  ? 207 TRP   A CE3 1 
ATOM   1600 C CZ2 . TRP   A 1 217 ? 4.485  14.784  -6.384  1.00 9.27  ? 207 TRP   A CZ2 1 
ATOM   1601 C CZ3 . TRP   A 1 217 ? 6.552  15.994  -6.755  1.00 9.72  ? 207 TRP   A CZ3 1 
ATOM   1602 C CH2 . TRP   A 1 217 ? 5.197  15.961  -6.422  1.00 9.32  ? 207 TRP   A CH2 1 
ATOM   1603 N N   . LEU   A 1 218 ? 8.942  13.648  -10.308 1.00 7.39  ? 208 LEU   A N   1 
ATOM   1604 C CA  . LEU   A 1 218 ? 8.634  14.677  -11.320 1.00 7.19  ? 208 LEU   A CA  1 
ATOM   1605 C C   . LEU   A 1 218 ? 8.588  14.031  -12.714 1.00 7.05  ? 208 LEU   A C   1 
ATOM   1606 O O   . LEU   A 1 218 ? 7.743  14.472  -13.542 1.00 6.63  ? 208 LEU   A O   1 
ATOM   1607 C CB  . LEU   A 1 218 ? 9.683  15.793  -11.241 1.00 7.43  ? 208 LEU   A CB  1 
ATOM   1608 C CG  . LEU   A 1 218 ? 9.564  16.738  -10.046 1.00 8.14  ? 208 LEU   A CG  1 
ATOM   1609 C CD1 . LEU   A 1 218 ? 10.681 17.769  -10.083 1.00 8.62  ? 208 LEU   A CD1 1 
ATOM   1610 C CD2 . LEU   A 1 218 ? 8.196  17.432  -9.996  1.00 8.19  ? 208 LEU   A CD2 1 
ATOM   1611 N N   . TYR   A 1 219 ? 9.479  13.075  -13.011 1.00 7.05  ? 209 TYR   A N   1 
ATOM   1612 C CA  . TYR   A 1 219 ? 9.429  12.286  -14.266 1.00 7.53  ? 209 TYR   A CA  1 
ATOM   1613 C C   . TYR   A 1 219 ? 8.112  11.474  -14.327 1.00 7.48  ? 209 TYR   A C   1 
ATOM   1614 O O   . TYR   A 1 219 ? 7.511  11.474  -15.401 1.00 7.33  ? 209 TYR   A O   1 
ATOM   1615 C CB  . TYR   A 1 219 ? 10.653 11.410  -14.484 1.00 8.21  ? 209 TYR   A CB  1 
ATOM   1616 C CG  . TYR   A 1 219 ? 11.864 12.164  -14.969 1.00 8.72  ? 209 TYR   A CG  1 
ATOM   1617 C CD1 . TYR   A 1 219 ? 11.969 12.574  -16.295 1.00 8.88  ? 209 TYR   A CD1 1 
ATOM   1618 C CD2 . TYR   A 1 219 ? 12.936 12.407  -14.131 1.00 8.78  ? 209 TYR   A CD2 1 
ATOM   1619 C CE1 . TYR   A 1 219 ? 13.099 13.230  -16.766 1.00 9.02  ? 209 TYR   A CE1 1 
ATOM   1620 C CE2 . TYR   A 1 219 ? 14.053 13.076  -14.581 1.00 9.38  ? 209 TYR   A CE2 1 
ATOM   1621 C CZ  . TYR   A 1 219 ? 14.141 13.503  -15.898 1.00 9.26  ? 209 TYR   A CZ  1 
ATOM   1622 O OH  . TYR   A 1 219 ? 15.252 14.171  -16.351 1.00 10.22 ? 209 TYR   A OH  1 
ATOM   1623 N N   . ALA   A 1 220 ? 7.679  10.837  -13.231 1.00 7.61  ? 210 ALA   A N   1 
ATOM   1624 C CA  . ALA   A 1 220 ? 6.388  10.102  -13.189 1.00 7.86  ? 210 ALA   A CA  1 
ATOM   1625 C C   . ALA   A 1 220 ? 5.246  11.051  -13.564 1.00 8.04  ? 210 ALA   A C   1 
ATOM   1626 O O   . ALA   A 1 220 ? 4.333  10.630  -14.295 1.00 9.15  ? 210 ALA   A O   1 
ATOM   1627 C CB  . ALA   A 1 220 ? 6.167  9.486   -11.829 1.00 7.97  ? 210 ALA   A CB  1 
ATOM   1628 N N   . ALA   A 1 221 ? 5.292  12.283  -13.076 1.00 8.44  ? 211 ALA   A N   1 
ATOM   1629 C CA  . ALA   A 1 221 ? 4.227  13.286  -13.256 1.00 8.72  ? 211 ALA   A CA  1 
ATOM   1630 C C   . ALA   A 1 221 ? 4.179  13.586  -14.747 1.00 9.26  ? 211 ALA   A C   1 
ATOM   1631 O O   . ALA   A 1 221 ? 3.098  13.521  -15.320 1.00 10.49 ? 211 ALA   A O   1 
ATOM   1632 C CB  . ALA   A 1 221 ? 4.483  14.506  -12.419 1.00 8.08  ? 211 ALA   A CB  1 
ATOM   1633 N N   . VAL   A 1 222 ? 5.339  13.766  -15.370 1.00 9.82  ? 212 VAL   A N   1 
ATOM   1634 C CA  . VAL   A 1 222 ? 5.394  14.101  -16.824 1.00 11.08 ? 212 VAL   A CA  1 
ATOM   1635 C C   . VAL   A 1 222 ? 4.811  12.931  -17.602 1.00 11.70 ? 212 VAL   A C   1 
ATOM   1636 O O   . VAL   A 1 222 ? 3.997  13.176  -18.543 1.00 13.50 ? 212 VAL   A O   1 
ATOM   1637 C CB  . VAL   A 1 222 ? 6.821  14.441  -17.304 1.00 10.86 ? 212 VAL   A CB  1 
ATOM   1638 C CG1 . VAL   A 1 222 ? 6.872  14.529  -18.828 1.00 10.85 ? 212 VAL   A CG1 1 
ATOM   1639 C CG2 . VAL   A 1 222 ? 7.279  15.740  -16.687 1.00 10.32 ? 212 VAL   A CG2 1 
ATOM   1640 N N   . ILE   A 1 223 ? 5.209  11.707  -17.250 1.00 13.52 ? 213 ILE   A N   1 
ATOM   1641 C CA  . ILE   A 1 223 ? 4.756  10.476  -17.953 1.00 13.64 ? 213 ILE   A CA  1 
ATOM   1642 C C   . ILE   A 1 223 ? 3.219  10.439  -17.876 1.00 15.50 ? 213 ILE   A C   1 
ATOM   1643 O O   . ILE   A 1 223 ? 2.579  10.042  -18.854 1.00 15.86 ? 213 ILE   A O   1 
ATOM   1644 C CB  . ILE   A 1 223 ? 5.431  9.227   -17.379 1.00 14.17 ? 213 ILE   A CB  1 
ATOM   1645 C CG1 . ILE   A 1 223 ? 6.906  9.195   -17.821 1.00 14.29 ? 213 ILE   A CG1 1 
ATOM   1646 C CG2 . ILE   A 1 223 ? 4.658  7.981   -17.782 1.00 15.70 ? 213 ILE   A CG2 1 
ATOM   1647 C CD1 . ILE   A 1 223 ? 7.786  8.239   -17.042 1.00 14.60 ? 213 ILE   A CD1 1 
ATOM   1648 N N   . ASN   A 1 224 ? 2.671  10.958  -16.783 1.00 15.68 ? 214 ASN   A N   1 
ATOM   1649 C CA  . ASN   A 1 224 ? 1.214  10.997  -16.504 1.00 17.83 ? 214 ASN   A CA  1 
ATOM   1650 C C   . ASN   A 1 224 ? 0.521  12.251  -17.046 1.00 17.88 ? 214 ASN   A C   1 
ATOM   1651 O O   . ASN   A 1 224 ? -0.702 12.403  -16.776 1.00 21.53 ? 214 ASN   A O   1 
ATOM   1652 C CB  . ASN   A 1 224 ? 1.020  10.817  -15.008 1.00 20.14 ? 214 ASN   A CB  1 
ATOM   1653 C CG  . ASN   A 1 224 ? 0.833  9.357   -14.700 1.00 22.84 ? 214 ASN   A CG  1 
ATOM   1654 O OD1 . ASN   A 1 224 ? -0.313 8.921   -14.643 1.00 27.11 ? 214 ASN   A OD1 1 
ATOM   1655 N ND2 . ASN   A 1 224 ? 1.918  8.606   -14.575 1.00 27.31 ? 214 ASN   A ND2 1 
ATOM   1656 N N   . GLY   A 1 225 ? 1.221  13.135  -17.742 1.00 17.31 ? 215 GLY   A N   1 
ATOM   1657 C CA  . GLY   A 1 225 ? 0.620  14.350  -18.315 1.00 17.28 ? 215 GLY   A CA  1 
ATOM   1658 C C   . GLY   A 1 225 ? 0.455  15.491  -17.321 1.00 17.44 ? 215 GLY   A C   1 
ATOM   1659 O O   . GLY   A 1 225 ? -0.150 16.503  -17.718 1.00 17.29 ? 215 GLY   A O   1 
ATOM   1660 N N   . ASP   A 1 226 ? 1.034  15.411  -16.117 1.00 17.10 ? 216 ASP   A N   1 
ATOM   1661 C CA  . ASP   A 1 226 ? 1.056  16.551  -15.168 1.00 18.33 ? 216 ASP   A CA  1 
ATOM   1662 C C   . ASP   A 1 226 ? 2.322  17.362  -15.473 1.00 19.42 ? 216 ASP   A C   1 
ATOM   1663 O O   . ASP   A 1 226 ? 3.393  16.977  -14.971 1.00 23.00 ? 216 ASP   A O   1 
ATOM   1664 C CB  . ASP   A 1 226 ? 0.920  16.038  -13.731 1.00 20.35 ? 216 ASP   A CB  1 
ATOM   1665 C CG  . ASP   A 1 226 ? 0.039  16.856  -12.815 1.00 22.59 ? 216 ASP   A CG  1 
ATOM   1666 O OD1 . ASP   A 1 226 ? -0.354 18.011  -13.192 1.00 26.74 ? 216 ASP   A OD1 1 
ATOM   1667 O OD2 . ASP   A 1 226 ? -0.240 16.342  -11.718 1.00 21.51 ? 216 ASP   A OD2 1 
ATOM   1668 N N   . ARG   A 1 227 ? 2.212  18.412  -16.297 1.00 18.35 ? 217 ARG   A N   1 
ATOM   1669 C CA  . ARG   A 1 227 ? 3.368  19.013  -17.022 1.00 20.48 ? 217 ARG   A CA  1 
ATOM   1670 C C   . ARG   A 1 227 ? 3.554  20.482  -16.650 1.00 17.73 ? 217 ARG   A C   1 
ATOM   1671 O O   . ARG   A 1 227 ? 4.554  21.095  -17.103 1.00 17.16 ? 217 ARG   A O   1 
ATOM   1672 C CB  . ARG   A 1 227 ? 3.140  18.894  -18.537 1.00 24.34 ? 217 ARG   A CB  1 
ATOM   1673 C CG  . ARG   A 1 227 ? 3.911  17.780  -19.232 1.00 30.09 ? 217 ARG   A CG  1 
ATOM   1674 C CD  . ARG   A 1 227 ? 3.579  17.705  -20.732 1.00 32.61 ? 217 ARG   A CD  1 
ATOM   1675 N NE  . ARG   A 1 227 ? 2.145  17.932  -20.992 1.00 34.96 ? 217 ARG   A NE  1 
ATOM   1676 C CZ  . ARG   A 1 227 ? 1.572  19.073  -21.434 1.00 38.12 ? 217 ARG   A CZ  1 
ATOM   1677 N NH1 . ARG   A 1 227 ? 2.289  20.153  -21.706 1.00 39.58 ? 217 ARG   A NH1 1 
ATOM   1678 N NH2 . ARG   A 1 227 ? 0.261  19.126  -21.616 1.00 36.55 ? 217 ARG   A NH2 1 
ATOM   1679 N N   . TRP   A 1 228 ? 2.655  21.054  -15.850 1.00 16.83 ? 218 TRP   A N   1 
ATOM   1680 C CA  . TRP   A 1 228 ? 2.593  22.527  -15.660 1.00 16.15 ? 218 TRP   A CA  1 
ATOM   1681 C C   . TRP   A 1 228 ? 3.930  23.060  -15.131 1.00 15.94 ? 218 TRP   A C   1 
ATOM   1682 O O   . TRP   A 1 228 ? 4.274  24.210  -15.427 1.00 16.16 ? 218 TRP   A O   1 
ATOM   1683 C CB  . TRP   A 1 228 ? 1.434  22.927  -14.749 1.00 15.80 ? 218 TRP   A CB  1 
ATOM   1684 C CG  . TRP   A 1 228 ? 1.506  22.388  -13.350 1.00 15.76 ? 218 TRP   A CG  1 
ATOM   1685 C CD1 . TRP   A 1 228 ? 0.858  21.294  -12.851 1.00 15.31 ? 218 TRP   A CD1 1 
ATOM   1686 C CD2 . TRP   A 1 228 ? 2.231  22.948  -12.240 1.00 15.97 ? 218 TRP   A CD2 1 
ATOM   1687 N NE1 . TRP   A 1 228 ? 1.150  21.122  -11.527 1.00 15.27 ? 218 TRP   A NE1 1 
ATOM   1688 C CE2 . TRP   A 1 228 ? 1.990  22.110  -11.122 1.00 15.34 ? 218 TRP   A CE2 1 
ATOM   1689 C CE3 . TRP   A 1 228 ? 3.064  24.052  -12.081 1.00 15.32 ? 218 TRP   A CE3 1 
ATOM   1690 C CZ2 . TRP   A 1 228 ? 2.559  22.356  -9.874  1.00 16.08 ? 218 TRP   A CZ2 1 
ATOM   1691 C CZ3 . TRP   A 1 228 ? 3.625  24.293  -10.846 1.00 15.39 ? 218 TRP   A CZ3 1 
ATOM   1692 C CH2 . TRP   A 1 228 ? 3.387  23.445  -9.768  1.00 15.45 ? 218 TRP   A CH2 1 
ATOM   1693 N N   . PHE   A 1 229 ? 4.678  22.284  -14.366 1.00 15.50 ? 219 PHE   A N   1 
ATOM   1694 C CA  . PHE   A 1 229 ? 5.877  22.794  -13.651 1.00 15.29 ? 219 PHE   A CA  1 
ATOM   1695 C C   . PHE   A 1 229 ? 7.108  22.767  -14.569 1.00 16.65 ? 219 PHE   A C   1 
ATOM   1696 O O   . PHE   A 1 229 ? 8.122  23.287  -14.137 1.00 16.87 ? 219 PHE   A O   1 
ATOM   1697 C CB  . PHE   A 1 229 ? 6.112  21.962  -12.391 1.00 14.97 ? 219 PHE   A CB  1 
ATOM   1698 C CG  . PHE   A 1 229 ? 6.232  20.502  -12.710 1.00 14.30 ? 219 PHE   A CG  1 
ATOM   1699 C CD1 . PHE   A 1 229 ? 7.428  19.982  -13.162 1.00 14.05 ? 219 PHE   A CD1 1 
ATOM   1700 C CD2 . PHE   A 1 229 ? 5.109  19.675  -12.660 1.00 13.82 ? 219 PHE   A CD2 1 
ATOM   1701 C CE1 . PHE   A 1 229 ? 7.503  18.652  -13.538 1.00 13.82 ? 219 PHE   A CE1 1 
ATOM   1702 C CE2 . PHE   A 1 229 ? 5.211  18.344  -13.008 1.00 13.45 ? 219 PHE   A CE2 1 
ATOM   1703 C CZ  . PHE   A 1 229 ? 6.404  17.844  -13.476 1.00 13.23 ? 219 PHE   A CZ  1 
ATOM   1704 N N   . LEU   A 1 230 ? 7.041  22.160  -15.763 1.00 16.92 ? 220 LEU   A N   1 
ATOM   1705 C CA  . LEU   A 1 230 ? 8.179  22.210  -16.719 1.00 17.98 ? 220 LEU   A CA  1 
ATOM   1706 C C   . LEU   A 1 230 ? 8.418  23.667  -17.133 1.00 20.69 ? 220 LEU   A C   1 
ATOM   1707 O O   . LEU   A 1 230 ? 7.449  24.333  -17.528 1.00 22.42 ? 220 LEU   A O   1 
ATOM   1708 C CB  . LEU   A 1 230 ? 7.901  21.351  -17.945 1.00 17.50 ? 220 LEU   A CB  1 
ATOM   1709 C CG  . LEU   A 1 230 ? 7.863  19.835  -17.740 1.00 16.85 ? 220 LEU   A CG  1 
ATOM   1710 C CD1 . LEU   A 1 230 ? 7.472  19.160  -19.047 1.00 17.01 ? 220 LEU   A CD1 1 
ATOM   1711 C CD2 . LEU   A 1 230 ? 9.188  19.293  -17.224 1.00 17.35 ? 220 LEU   A CD2 1 
ATOM   1712 N N   . ASN   A 1 231 ? 9.658  24.142  -17.101 1.00 21.56 ? 221 ASN   A N   1 
ATOM   1713 C CA  . ASN   A 1 231 ? 9.938  25.572  -17.411 1.00 22.51 ? 221 ASN   A CA  1 
ATOM   1714 C C   . ASN   A 1 231 ? 10.928 25.681  -18.582 1.00 22.76 ? 221 ASN   A C   1 
ATOM   1715 O O   . ASN   A 1 231 ? 11.270 24.642  -19.193 1.00 21.64 ? 221 ASN   A O   1 
ATOM   1716 C CB  . ASN   A 1 231 ? 10.349 26.338  -16.155 1.00 21.73 ? 221 ASN   A CB  1 
ATOM   1717 C CG  . ASN   A 1 231 ? 11.637 25.827  -15.551 1.00 22.90 ? 221 ASN   A CG  1 
ATOM   1718 O OD1 . ASN   A 1 231 ? 12.553 25.369  -16.258 1.00 21.49 ? 221 ASN   A OD1 1 
ATOM   1719 N ND2 . ASN   A 1 231 ? 11.739 25.943  -14.236 1.00 23.72 ? 221 ASN   A ND2 1 
ATOM   1720 N N   . ARG   A 1 232 ? 11.296 26.922  -18.920 1.00 23.78 ? 222 ARG   A N   1 
ATOM   1721 C CA  . ARG   A 1 232 ? 12.187 27.293  -20.050 1.00 24.80 ? 222 ARG   A CA  1 
ATOM   1722 C C   . ARG   A 1 232 ? 13.652 27.306  -19.596 1.00 22.11 ? 222 ARG   A C   1 
ATOM   1723 O O   . ARG   A 1 232 ? 14.509 27.774  -20.381 1.00 18.44 ? 222 ARG   A O   1 
ATOM   1724 C CB  . ARG   A 1 232 ? 11.825 28.680  -20.590 1.00 26.38 ? 222 ARG   A CB  1 
ATOM   1725 C CG  . ARG   A 1 232 ? 10.350 28.863  -20.930 1.00 30.86 ? 222 ARG   A CG  1 
ATOM   1726 C CD  . ARG   A 1 232 ? 10.023 30.219  -21.531 1.00 33.38 ? 222 ARG   A CD  1 
ATOM   1727 N NE  . ARG   A 1 232 ? 8.811  30.200  -22.361 1.00 36.45 ? 222 ARG   A NE  1 
ATOM   1728 C CZ  . ARG   A 1 232 ? 8.752  29.940  -23.677 1.00 38.76 ? 222 ARG   A CZ  1 
ATOM   1729 N NH1 . ARG   A 1 232 ? 9.848  29.664  -24.374 1.00 38.61 ? 222 ARG   A NH1 1 
ATOM   1730 N NH2 . ARG   A 1 232 ? 7.578  29.965  -24.298 1.00 37.81 ? 222 ARG   A NH2 1 
ATOM   1731 N N   . PHE   A 1 233 ? 13.957 26.810  -18.394 1.00 19.75 ? 223 PHE   A N   1 
ATOM   1732 C CA  . PHE   A 1 233 ? 15.287 27.014  -17.768 1.00 19.73 ? 223 PHE   A CA  1 
ATOM   1733 C C   . PHE   A 1 233 ? 16.075 25.695  -17.685 1.00 17.64 ? 223 PHE   A C   1 
ATOM   1734 O O   . PHE   A 1 233 ? 15.529 24.563  -17.788 1.00 16.41 ? 223 PHE   A O   1 
ATOM   1735 C CB  . PHE   A 1 233 ? 15.150 27.663  -16.389 1.00 23.66 ? 223 PHE   A CB  1 
ATOM   1736 C CG  . PHE   A 1 233 ? 14.093 28.735  -16.269 1.00 27.69 ? 223 PHE   A CG  1 
ATOM   1737 C CD1 . PHE   A 1 233 ? 14.067 29.817  -17.133 1.00 30.97 ? 223 PHE   A CD1 1 
ATOM   1738 C CD2 . PHE   A 1 233 ? 13.139 28.680  -15.264 1.00 31.12 ? 223 PHE   A CD2 1 
ATOM   1739 C CE1 . PHE   A 1 233 ? 13.087 30.794  -17.018 1.00 31.70 ? 223 PHE   A CE1 1 
ATOM   1740 C CE2 . PHE   A 1 233 ? 12.161 29.654  -15.144 1.00 32.72 ? 223 PHE   A CE2 1 
ATOM   1741 C CZ  . PHE   A 1 233 ? 12.135 30.712  -16.024 1.00 33.01 ? 223 PHE   A CZ  1 
ATOM   1742 N N   . THR   A 1 234 ? 17.389 25.838  -17.553 1.00 14.36 ? 224 THR   A N   1 
ATOM   1743 C CA  . THR   A 1 234 ? 18.291 24.734  -17.163 1.00 13.53 ? 224 THR   A CA  1 
ATOM   1744 C C   . THR   A 1 234 ? 19.188 25.224  -16.030 1.00 13.30 ? 224 THR   A C   1 
ATOM   1745 O O   . THR   A 1 234 ? 19.124 26.422  -15.653 1.00 13.64 ? 224 THR   A O   1 
ATOM   1746 C CB  . THR   A 1 234 ? 19.016 24.155  -18.385 1.00 12.69 ? 224 THR   A CB  1 
ATOM   1747 O OG1 . THR   A 1 234 ? 19.557 22.894  -17.987 1.00 12.45 ? 224 THR   A OG1 1 
ATOM   1748 C CG2 . THR   A 1 234 ? 20.128 25.046  -18.910 1.00 13.57 ? 224 THR   A CG2 1 
ATOM   1749 N N   . THR   A 1 235 ? 20.005 24.332  -15.488 1.00 12.94 ? 225 THR   A N   1 
ATOM   1750 C CA  . THR   A 1 235 ? 20.946 24.692  -14.417 1.00 13.07 ? 225 THR   A CA  1 
ATOM   1751 C C   . THR   A 1 235 ? 22.154 23.776  -14.556 1.00 12.36 ? 225 THR   A C   1 
ATOM   1752 O O   . THR   A 1 235 ? 22.214 23.038  -15.536 1.00 11.79 ? 225 THR   A O   1 
ATOM   1753 C CB  . THR   A 1 235 ? 20.235 24.657  -13.061 1.00 13.71 ? 225 THR   A CB  1 
ATOM   1754 O OG1 . THR   A 1 235 ? 21.112 25.167  -12.057 1.00 14.21 ? 225 THR   A OG1 1 
ATOM   1755 C CG2 . THR   A 1 235 ? 19.828 23.263  -12.655 1.00 14.31 ? 225 THR   A CG2 1 
ATOM   1756 N N   . THR   A 1 236 ? 23.069 23.864  -13.601 1.00 13.70 ? 226 THR   A N   1 
ATOM   1757 C CA  . THR   A 1 236 ? 24.213 22.945  -13.447 1.00 13.80 ? 226 THR   A CA  1 
ATOM   1758 C C   . THR   A 1 236 ? 24.061 22.186  -12.131 1.00 13.30 ? 226 THR   A C   1 
ATOM   1759 O O   . THR   A 1 236 ? 23.323 22.657  -11.261 1.00 13.09 ? 226 THR   A O   1 
ATOM   1760 C CB  . THR   A 1 236 ? 25.552 23.695  -13.493 1.00 14.45 ? 226 THR   A CB  1 
ATOM   1761 O OG1 . THR   A 1 236 ? 25.561 24.519  -12.327 1.00 15.64 ? 226 THR   A OG1 1 
ATOM   1762 C CG2 . THR   A 1 236 ? 25.739 24.494  -14.765 1.00 14.95 ? 226 THR   A CG2 1 
ATOM   1763 N N   . LEU   A 1 237 ? 24.806 21.094  -11.979 1.00 15.06 ? 227 LEU   A N   1 
ATOM   1764 C CA  . LEU   A 1 237 ? 24.827 20.349  -10.693 1.00 15.71 ? 227 LEU   A CA  1 
ATOM   1765 C C   . LEU   A 1 237 ? 25.203 21.305  -9.571  1.00 15.84 ? 227 LEU   A C   1 
ATOM   1766 O O   . LEU   A 1 237 ? 24.486 21.356  -8.569  1.00 15.08 ? 227 LEU   A O   1 
ATOM   1767 C CB  . LEU   A 1 237 ? 25.817 19.190  -10.759 1.00 17.76 ? 227 LEU   A CB  1 
ATOM   1768 C CG  . LEU   A 1 237 ? 25.272 17.864  -11.286 1.00 18.67 ? 227 LEU   A CG  1 
ATOM   1769 C CD1 . LEU   A 1 237 ? 26.295 16.745  -11.082 1.00 18.99 ? 227 LEU   A CD1 1 
ATOM   1770 C CD2 . LEU   A 1 237 ? 23.964 17.496  -10.605 1.00 18.82 ? 227 LEU   A CD2 1 
ATOM   1771 N N   . ASN   A 1 238 ? 26.326 22.019  -9.716  1.00 16.07 ? 228 ASN   A N   1 
ATOM   1772 C CA  . ASN   A 1 238 ? 26.819 22.900  -8.634  1.00 17.11 ? 228 ASN   A CA  1 
ATOM   1773 C C   . ASN   A 1 238 ? 25.756 23.970  -8.358  1.00 16.05 ? 228 ASN   A C   1 
ATOM   1774 O O   . ASN   A 1 238 ? 25.475 24.268  -7.172  1.00 16.67 ? 228 ASN   A O   1 
ATOM   1775 C CB  . ASN   A 1 238 ? 28.235 23.379  -8.957  1.00 20.59 ? 228 ASN   A CB  1 
ATOM   1776 C CG  . ASN   A 1 238 ? 29.280 22.286  -8.784  1.00 21.57 ? 228 ASN   A CG  1 
ATOM   1777 O OD1 . ASN   A 1 238 ? 28.993 21.225  -8.223  1.00 24.18 ? 228 ASN   A OD1 1 
ATOM   1778 N ND2 . ASN   A 1 238 ? 30.519 22.539  -9.203  1.00 19.39 ? 228 ASN   A ND2 1 
ATOM   1779 N N   . ASP   A 1 239 ? 25.160 24.540  -9.395  1.00 15.94 ? 229 ASP   A N   1 
ATOM   1780 C CA  . ASP   A 1 239 ? 24.169 25.627  -9.206  1.00 17.74 ? 229 ASP   A CA  1 
ATOM   1781 C C   . ASP   A 1 239 ? 22.927 25.085  -8.474  1.00 16.74 ? 229 ASP   A C   1 
ATOM   1782 O O   . ASP   A 1 239 ? 22.437 25.724  -7.516  1.00 15.44 ? 229 ASP   A O   1 
ATOM   1783 C CB  . ASP   A 1 239 ? 23.714 26.222  -10.531 1.00 21.66 ? 229 ASP   A CB  1 
ATOM   1784 C CG  . ASP   A 1 239 ? 22.698 27.329  -10.322 1.00 27.18 ? 229 ASP   A CG  1 
ATOM   1785 O OD1 . ASP   A 1 239 ? 23.129 28.392  -9.830  1.00 36.21 ? 229 ASP   A OD1 1 
ATOM   1786 O OD2 . ASP   A 1 239 ? 21.470 27.106  -10.594 1.00 31.85 ? 229 ASP   A OD2 1 
ATOM   1787 N N   . PHE   A 1 240 ? 22.415 23.961  -8.941  1.00 14.42 ? 230 PHE   A N   1 
ATOM   1788 C CA  . PHE   A 1 240 ? 21.238 23.314  -8.328  1.00 14.63 ? 230 PHE   A CA  1 
ATOM   1789 C C   . PHE   A 1 240 ? 21.532 23.017  -6.846  1.00 14.01 ? 230 PHE   A C   1 
ATOM   1790 O O   . PHE   A 1 240 ? 20.670 23.307  -5.958  1.00 13.24 ? 230 PHE   A O   1 
ATOM   1791 C CB  . PHE   A 1 240 ? 20.911 22.018  -9.063  1.00 14.02 ? 230 PHE   A CB  1 
ATOM   1792 C CG  . PHE   A 1 240 ? 19.802 21.304  -8.343  1.00 15.22 ? 230 PHE   A CG  1 
ATOM   1793 C CD1 . PHE   A 1 240 ? 18.500 21.771  -8.439  1.00 15.98 ? 230 PHE   A CD1 1 
ATOM   1794 C CD2 . PHE   A 1 240 ? 20.066 20.257  -7.479  1.00 15.46 ? 230 PHE   A CD2 1 
ATOM   1795 C CE1 . PHE   A 1 240 ? 17.466 21.178  -7.722  1.00 16.44 ? 230 PHE   A CE1 1 
ATOM   1796 C CE2 . PHE   A 1 240 ? 19.032 19.661  -6.765  1.00 16.32 ? 230 PHE   A CE2 1 
ATOM   1797 C CZ  . PHE   A 1 240 ? 17.737 20.127  -6.878  1.00 15.82 ? 230 PHE   A CZ  1 
ATOM   1798 N N   . ASN   A 1 241 ? 22.728 22.465  -6.592  1.00 14.69 ? 231 ASN   A N   1 
ATOM   1799 C CA  . ASN   A 1 241 ? 23.139 21.976  -5.247  1.00 15.52 ? 231 ASN   A CA  1 
ATOM   1800 C C   . ASN   A 1 241 ? 23.211 23.168  -4.293  1.00 17.04 ? 231 ASN   A C   1 
ATOM   1801 O O   . ASN   A 1 241 ? 22.796 22.989  -3.117  1.00 17.38 ? 231 ASN   A O   1 
ATOM   1802 C CB  . ASN   A 1 241 ? 24.406 21.121  -5.302  1.00 15.06 ? 231 ASN   A CB  1 
ATOM   1803 C CG  . ASN   A 1 241 ? 24.136 19.689  -5.717  1.00 15.41 ? 231 ASN   A CG  1 
ATOM   1804 O OD1 . ASN   A 1 241 ? 23.017 19.179  -5.580  1.00 15.33 ? 231 ASN   A OD1 1 
ATOM   1805 N ND2 . ASN   A 1 241 ? 25.158 19.019  -6.217  1.00 15.27 ? 231 ASN   A ND2 1 
ATOM   1806 N N   . LEU   A 1 242 ? 23.615 24.357  -4.757  1.00 17.80 ? 232 LEU   A N   1 
ATOM   1807 C CA  . LEU   A 1 242 ? 23.574 25.567  -3.876  1.00 20.43 ? 232 LEU   A CA  1 
ATOM   1808 C C   . LEU   A 1 242 ? 22.129 25.824  -3.415  1.00 23.25 ? 232 LEU   A C   1 
ATOM   1809 O O   . LEU   A 1 242 ? 21.925 26.141  -2.191  1.00 23.82 ? 232 LEU   A O   1 
ATOM   1810 C CB  . LEU   A 1 242 ? 24.185 26.756  -4.614  1.00 20.93 ? 232 LEU   A CB  1 
ATOM   1811 C CG  . LEU   A 1 242 ? 25.705 26.674  -4.721  1.00 22.13 ? 232 LEU   A CG  1 
ATOM   1812 C CD1 . LEU   A 1 242 ? 26.258 27.736  -5.661  1.00 24.37 ? 232 LEU   A CD1 1 
ATOM   1813 C CD2 . LEU   A 1 242 ? 26.349 26.809  -3.336  1.00 22.52 ? 232 LEU   A CD2 1 
ATOM   1814 N N   . VAL   A 1 243 ? 21.143 25.594  -4.289  1.00 23.23 ? 233 VAL   A N   1 
ATOM   1815 C CA  . VAL   A 1 243 ? 19.682 25.636  -3.925  1.00 25.08 ? 233 VAL   A CA  1 
ATOM   1816 C C   . VAL   A 1 243 ? 19.277 24.425  -3.067  1.00 24.25 ? 233 VAL   A C   1 
ATOM   1817 O O   . VAL   A 1 243 ? 18.616 24.616  -2.032  1.00 27.59 ? 233 VAL   A O   1 
ATOM   1818 C CB  . VAL   A 1 243 ? 18.797 25.730  -5.183  1.00 25.85 ? 233 VAL   A CB  1 
ATOM   1819 C CG1 . VAL   A 1 243 ? 17.316 25.728  -4.831  1.00 28.99 ? 233 VAL   A CG1 1 
ATOM   1820 C CG2 . VAL   A 1 243 ? 19.141 26.957  -6.005  1.00 27.03 ? 233 VAL   A CG2 1 
ATOM   1821 N N   . ALA   A 1 244 ? 19.588 23.203  -3.484  1.00 25.94 ? 234 ALA   A N   1 
ATOM   1822 C CA  . ALA   A 1 244 ? 19.338 21.999  -2.658  1.00 28.19 ? 234 ALA   A CA  1 
ATOM   1823 C C   . ALA   A 1 244 ? 19.673 22.322  -1.192  1.00 27.92 ? 234 ALA   A C   1 
ATOM   1824 O O   . ALA   A 1 244 ? 18.809 22.138  -0.325  1.00 28.51 ? 234 ALA   A O   1 
ATOM   1825 C CB  . ALA   A 1 244 ? 20.135 20.816  -3.161  1.00 28.61 ? 234 ALA   A CB  1 
ATOM   1826 N N   . MET   A 1 245 ? 20.883 22.811  -0.937  1.00 28.08 ? 235 MET   A N   1 
ATOM   1827 C CA  . MET   A 1 245 ? 21.457 22.907  0.429   1.00 29.17 ? 235 MET   A CA  1 
ATOM   1828 C C   . MET   A 1 245 ? 20.540 23.751  1.319   1.00 24.22 ? 235 MET   A C   1 
ATOM   1829 O O   . MET   A 1 245 ? 20.351 23.351  2.460   1.00 21.28 ? 235 MET   A O   1 
ATOM   1830 C CB  . MET   A 1 245 ? 22.858 23.519  0.427   1.00 34.49 ? 235 MET   A CB  1 
ATOM   1831 C CG  . MET   A 1 245 ? 23.676 23.058  1.622   1.00 40.28 ? 235 MET   A CG  1 
ATOM   1832 S SD  . MET   A 1 245 ? 25.269 23.913  1.829   1.00 52.89 ? 235 MET   A SD  1 
ATOM   1833 C CE  . MET   A 1 245 ? 24.800 25.189  3.001   1.00 53.08 ? 235 MET   A CE  1 
ATOM   1834 N N   . LYS   A 1 246 ? 19.982 24.854  0.807   1.00 22.20 ? 236 LYS   A N   1 
ATOM   1835 C CA  . LYS   A 1 246 ? 19.145 25.785  1.601   1.00 22.40 ? 236 LYS   A CA  1 
ATOM   1836 C C   . LYS   A 1 246 ? 17.874 25.065  2.089   1.00 21.32 ? 236 LYS   A C   1 
ATOM   1837 O O   . LYS   A 1 246 ? 17.383 25.380  3.175   1.00 22.05 ? 236 LYS   A O   1 
ATOM   1838 C CB  . LYS   A 1 246 ? 18.821 27.054  0.803   1.00 26.51 ? 236 LYS   A CB  1 
ATOM   1839 C CG  . LYS   A 1 246 ? 17.970 28.057  1.579   1.00 29.86 ? 236 LYS   A CG  1 
ATOM   1840 C CD  . LYS   A 1 246 ? 17.914 29.472  0.980   1.00 33.10 ? 236 LYS   A CD  1 
ATOM   1841 C CE  . LYS   A 1 246 ? 16.502 29.949  0.667   1.00 33.38 ? 236 LYS   A CE  1 
ATOM   1842 N NZ  . LYS   A 1 246 ? 15.937 30.812  1.739   1.00 32.41 ? 236 LYS   A NZ  1 
ATOM   1843 N N   . TYR   A 1 247 ? 17.392 24.087  1.321   1.00 17.75 ? 237 TYR   A N   1 
ATOM   1844 C CA  . TYR   A 1 247 ? 16.090 23.399  1.508   1.00 16.05 ? 237 TYR   A CA  1 
ATOM   1845 C C   . TYR   A 1 247 ? 16.262 22.009  2.136   1.00 14.86 ? 237 TYR   A C   1 
ATOM   1846 O O   . TYR   A 1 247 ? 15.259 21.268  2.254   1.00 14.65 ? 237 TYR   A O   1 
ATOM   1847 C CB  . TYR   A 1 247 ? 15.386 23.353  0.155   1.00 15.57 ? 237 TYR   A CB  1 
ATOM   1848 C CG  . TYR   A 1 247 ? 14.930 24.717  -0.262  1.00 16.80 ? 237 TYR   A CG  1 
ATOM   1849 C CD1 . TYR   A 1 247 ? 13.804 25.284  0.331   1.00 17.19 ? 237 TYR   A CD1 1 
ATOM   1850 C CD2 . TYR   A 1 247 ? 15.645 25.458  -1.186  1.00 15.76 ? 237 TYR   A CD2 1 
ATOM   1851 C CE1 . TYR   A 1 247 ? 13.395 26.566  0.007   1.00 17.29 ? 237 TYR   A CE1 1 
ATOM   1852 C CE2 . TYR   A 1 247 ? 15.243 26.736  -1.522  1.00 17.53 ? 237 TYR   A CE2 1 
ATOM   1853 C CZ  . TYR   A 1 247 ? 14.117 27.286  -0.927  1.00 18.10 ? 237 TYR   A CZ  1 
ATOM   1854 O OH  . TYR   A 1 247 ? 13.686 28.534  -1.267  1.00 20.86 ? 237 TYR   A OH  1 
ATOM   1855 N N   . ASN   A 1 248 ? 17.462 21.714  2.615   1.00 14.04 ? 238 ASN   A N   1 
ATOM   1856 C CA  . ASN   A 1 248 ? 17.840 20.429  3.249   1.00 15.30 ? 238 ASN   A CA  1 
ATOM   1857 C C   . ASN   A 1 248 ? 17.560 19.289  2.276   1.00 14.89 ? 238 ASN   A C   1 
ATOM   1858 O O   . ASN   A 1 248 ? 17.067 18.241  2.714   1.00 15.63 ? 238 ASN   A O   1 
ATOM   1859 C CB  . ASN   A 1 248 ? 17.160 20.223  4.598   1.00 17.92 ? 238 ASN   A CB  1 
ATOM   1860 C CG  . ASN   A 1 248 ? 17.724 21.193  5.618   1.00 20.29 ? 238 ASN   A CG  1 
ATOM   1861 O OD1 . ASN   A 1 248 ? 18.930 21.396  5.669   1.00 21.83 ? 238 ASN   A OD1 1 
ATOM   1862 N ND2 . ASN   A 1 248 ? 16.863 21.841  6.362   1.00 21.81 ? 238 ASN   A ND2 1 
ATOM   1863 N N   . TYR   A 1 249 ? 17.916 19.487  1.012   1.00 15.09 ? 239 TYR   A N   1 
ATOM   1864 C CA  . TYR   A 1 249 ? 17.940 18.415  -0.015  1.00 14.08 ? 239 TYR   A CA  1 
ATOM   1865 C C   . TYR   A 1 249 ? 19.343 17.789  -0.022  1.00 15.99 ? 239 TYR   A C   1 
ATOM   1866 O O   . TYR   A 1 249 ? 20.339 18.517  0.184   1.00 14.79 ? 239 TYR   A O   1 
ATOM   1867 C CB  . TYR   A 1 249 ? 17.511 18.989  -1.369  1.00 14.28 ? 239 TYR   A CB  1 
ATOM   1868 C CG  . TYR   A 1 249 ? 16.032 18.946  -1.670  1.00 13.82 ? 239 TYR   A CG  1 
ATOM   1869 C CD1 . TYR   A 1 249 ? 15.097 19.533  -0.832  1.00 12.60 ? 239 TYR   A CD1 1 
ATOM   1870 C CD2 . TYR   A 1 249 ? 15.555 18.351  -2.824  1.00 14.14 ? 239 TYR   A CD2 1 
ATOM   1871 C CE1 . TYR   A 1 249 ? 13.742 19.500  -1.109  1.00 12.14 ? 239 TYR   A CE1 1 
ATOM   1872 C CE2 . TYR   A 1 249 ? 14.201 18.299  -3.111  1.00 12.97 ? 239 TYR   A CE2 1 
ATOM   1873 C CZ  . TYR   A 1 249 ? 13.283 18.870  -2.255  1.00 12.64 ? 239 TYR   A CZ  1 
ATOM   1874 O OH  . TYR   A 1 249 ? 11.954 18.791  -2.574  1.00 11.74 ? 239 TYR   A OH  1 
ATOM   1875 N N   . GLU   A 1 250 ? 19.426 16.477  -0.253  1.00 15.57 ? 240 GLU   A N   1 
ATOM   1876 C CA  . GLU   A 1 250 ? 20.696 15.744  -0.462  1.00 16.99 ? 240 GLU   A CA  1 
ATOM   1877 C C   . GLU   A 1 250 ? 21.350 16.358  -1.680  1.00 15.76 ? 240 GLU   A C   1 
ATOM   1878 O O   . GLU   A 1 250 ? 20.646 16.714  -2.623  1.00 13.43 ? 240 GLU   A O   1 
ATOM   1879 C CB  . GLU   A 1 250 ? 20.514 14.278  -0.865  1.00 20.47 ? 240 GLU   A CB  1 
ATOM   1880 C CG  . GLU   A 1 250 ? 19.893 13.392  0.183   1.00 25.76 ? 240 GLU   A CG  1 
ATOM   1881 C CD  . GLU   A 1 250 ? 19.870 11.924  -0.233  1.00 30.36 ? 240 GLU   A CD  1 
ATOM   1882 O OE1 . GLU   A 1 250 ? 19.836 11.617  -1.493  1.00 28.88 ? 240 GLU   A OE1 1 
ATOM   1883 O OE2 . GLU   A 1 250 ? 19.900 11.069  0.693   1.00 41.79 ? 240 GLU   A OE2 1 
ATOM   1884 N N   . PRO   A 1 251 ? 22.692 16.490  -1.687  1.00 17.02 ? 241 PRO   A N   1 
ATOM   1885 C CA  . PRO   A 1 251 ? 23.404 16.869  -2.896  1.00 15.97 ? 241 PRO   A CA  1 
ATOM   1886 C C   . PRO   A 1 251 ? 23.143 15.873  -4.030  1.00 15.60 ? 241 PRO   A C   1 
ATOM   1887 O O   . PRO   A 1 251 ? 23.122 14.677  -3.808  1.00 16.35 ? 241 PRO   A O   1 
ATOM   1888 C CB  . PRO   A 1 251 ? 24.893 16.842  -2.501  1.00 16.49 ? 241 PRO   A CB  1 
ATOM   1889 C CG  . PRO   A 1 251 ? 24.888 16.933  -1.000  1.00 17.38 ? 241 PRO   A CG  1 
ATOM   1890 C CD  . PRO   A 1 251 ? 23.600 16.243  -0.552  1.00 16.79 ? 241 PRO   A CD  1 
ATOM   1891 N N   . LEU   A 1 252 ? 22.979 16.384  -5.239  1.00 13.25 ? 242 LEU   A N   1 
ATOM   1892 C CA  . LEU   A 1 252 ? 22.838 15.526  -6.430  1.00 13.86 ? 242 LEU   A CA  1 
ATOM   1893 C C   . LEU   A 1 252 ? 24.234 15.310  -7.037  1.00 14.43 ? 242 LEU   A C   1 
ATOM   1894 O O   . LEU   A 1 252 ? 24.965 16.285  -7.184  1.00 14.49 ? 242 LEU   A O   1 
ATOM   1895 C CB  . LEU   A 1 252 ? 21.897 16.211  -7.419  1.00 14.06 ? 242 LEU   A CB  1 
ATOM   1896 C CG  . LEU   A 1 252 ? 21.314 15.295  -8.497  1.00 14.52 ? 242 LEU   A CG  1 
ATOM   1897 C CD1 . LEU   A 1 252 ? 20.314 14.303  -7.916  1.00 14.48 ? 242 LEU   A CD1 1 
ATOM   1898 C CD2 . LEU   A 1 252 ? 20.662 16.122  -9.586  1.00 14.99 ? 242 LEU   A CD2 1 
ATOM   1899 N N   . THR   A 1 253 ? 24.548 14.073  -7.406  1.00 15.02 ? 243 THR   A N   1 
ATOM   1900 C CA  . THR   A 1 253 ? 25.830 13.673  -8.041  1.00 16.77 ? 243 THR   A CA  1 
ATOM   1901 C C   . THR   A 1 253 ? 25.561 13.113  -9.446  1.00 16.65 ? 243 THR   A C   1 
ATOM   1902 O O   . THR   A 1 253 ? 24.401 12.783  -9.763  1.00 15.05 ? 243 THR   A O   1 
ATOM   1903 C CB  . THR   A 1 253 ? 26.522 12.633  -7.159  1.00 15.92 ? 243 THR   A CB  1 
ATOM   1904 O OG1 . THR   A 1 253 ? 25.770 11.424  -7.285  1.00 16.40 ? 243 THR   A OG1 1 
ATOM   1905 C CG2 . THR   A 1 253 ? 26.603 13.058  -5.706  1.00 17.41 ? 243 THR   A CG2 1 
ATOM   1906 N N   . GLN   A 1 254 ? 26.607 12.976  -10.254 1.00 16.43 ? 244 GLN   A N   1 
ATOM   1907 C CA  . GLN   A 1 254 ? 26.556 12.319  -11.570 1.00 16.38 ? 244 GLN   A CA  1 
ATOM   1908 C C   . GLN   A 1 254 ? 26.004 10.893  -11.448 1.00 15.50 ? 244 GLN   A C   1 
ATOM   1909 O O   . GLN   A 1 254 ? 25.284 10.485  -12.372 1.00 15.69 ? 244 GLN   A O   1 
ATOM   1910 C CB  . GLN   A 1 254 ? 27.930 12.326  -12.244 1.00 18.76 ? 244 GLN   A CB  1 
ATOM   1911 C CG  . GLN   A 1 254 ? 27.872 11.844  -13.690 1.00 19.05 ? 244 GLN   A CG  1 
ATOM   1912 C CD  . GLN   A 1 254 ? 26.931 12.647  -14.561 1.00 20.75 ? 244 GLN   A CD  1 
ATOM   1913 O OE1 . GLN   A 1 254 ? 26.946 13.867  -14.549 1.00 24.06 ? 244 GLN   A OE1 1 
ATOM   1914 N NE2 . GLN   A 1 254 ? 26.102 11.966  -15.325 1.00 20.78 ? 244 GLN   A NE2 1 
ATOM   1915 N N   . ASP   A 1 255 ? 26.284 10.161  -10.364 1.00 15.07 ? 245 ASP   A N   1 
ATOM   1916 C CA  . ASP   A 1 255 ? 25.729 8.792   -10.170 1.00 15.51 ? 245 ASP   A CA  1 
ATOM   1917 C C   . ASP   A 1 255 ? 24.190 8.877   -10.174 1.00 13.95 ? 245 ASP   A C   1 
ATOM   1918 O O   . ASP   A 1 255 ? 23.545 8.000   -10.780 1.00 14.08 ? 245 ASP   A O   1 
ATOM   1919 C CB  . ASP   A 1 255 ? 26.173 8.146   -8.858  1.00 17.16 ? 245 ASP   A CB  1 
ATOM   1920 C CG  . ASP   A 1 255 ? 27.618 7.691   -8.793  1.00 22.01 ? 245 ASP   A CG  1 
ATOM   1921 O OD1 . ASP   A 1 255 ? 28.295 7.685   -9.839  1.00 19.76 ? 245 ASP   A OD1 1 
ATOM   1922 O OD2 . ASP   A 1 255 ? 28.026 7.305   -7.670  1.00 26.07 ? 245 ASP   A OD2 1 
ATOM   1923 N N   . HIS   A 1 256 ? 23.623 9.891   -9.509  1.00 12.62 ? 246 HIS   A N   1 
ATOM   1924 C CA  . HIS   A 1 256 ? 22.146 10.123  -9.459  1.00 12.25 ? 246 HIS   A CA  1 
ATOM   1925 C C   . HIS   A 1 256 ? 21.630 10.390  -10.888 1.00 12.05 ? 246 HIS   A C   1 
ATOM   1926 O O   . HIS   A 1 256 ? 20.566 9.838   -11.296 1.00 11.84 ? 246 HIS   A O   1 
ATOM   1927 C CB  . HIS   A 1 256 ? 21.818 11.278  -8.506  1.00 11.64 ? 246 HIS   A CB  1 
ATOM   1928 C CG  . HIS   A 1 256 ? 22.103 10.995  -7.071  1.00 12.40 ? 246 HIS   A CG  1 
ATOM   1929 N ND1 . HIS   A 1 256 ? 22.498 11.986  -6.196  1.00 12.86 ? 246 HIS   A ND1 1 
ATOM   1930 C CD2 . HIS   A 1 256 ? 21.990 9.865   -6.343  1.00 12.89 ? 246 HIS   A CD2 1 
ATOM   1931 C CE1 . HIS   A 1 256 ? 22.675 11.475  -4.996  1.00 12.80 ? 246 HIS   A CE1 1 
ATOM   1932 N NE2 . HIS   A 1 256 ? 22.365 10.171  -5.047  1.00 13.75 ? 246 HIS   A NE2 1 
ATOM   1933 N N   . VAL   A 1 257 ? 22.320 11.263  -11.605 1.00 12.74 ? 247 VAL   A N   1 
ATOM   1934 C CA  . VAL   A 1 257 ? 21.980 11.654  -12.999 1.00 12.75 ? 247 VAL   A CA  1 
ATOM   1935 C C   . VAL   A 1 257 ? 21.933 10.381  -13.844 1.00 12.96 ? 247 VAL   A C   1 
ATOM   1936 O O   . VAL   A 1 257 ? 20.990 10.232  -14.634 1.00 12.57 ? 247 VAL   A O   1 
ATOM   1937 C CB  . VAL   A 1 257 ? 22.967 12.682  -13.584 1.00 13.82 ? 247 VAL   A CB  1 
ATOM   1938 C CG1 . VAL   A 1 257 ? 22.687 12.934  -15.060 1.00 15.19 ? 247 VAL   A CG1 1 
ATOM   1939 C CG2 . VAL   A 1 257 ? 22.951 13.984  -12.825 1.00 14.65 ? 247 VAL   A CG2 1 
ATOM   1940 N N   . ASP   A 1 258 ? 22.914 9.498   -13.672 1.00 13.00 ? 248 ASP   A N   1 
ATOM   1941 C CA  . ASP   A 1 258 ? 23.042 8.246   -14.454 1.00 13.78 ? 248 ASP   A CA  1 
ATOM   1942 C C   . ASP   A 1 258 ? 21.884 7.299   -14.125 1.00 12.81 ? 248 ASP   A C   1 
ATOM   1943 O O   . ASP   A 1 258 ? 21.348 6.646   -15.043 1.00 12.17 ? 248 ASP   A O   1 
ATOM   1944 C CB  . ASP   A 1 258 ? 24.376 7.564   -14.158 1.00 14.91 ? 248 ASP   A CB  1 
ATOM   1945 C CG  . ASP   A 1 258 ? 25.594 8.259   -14.734 1.00 16.47 ? 248 ASP   A CG  1 
ATOM   1946 O OD1 . ASP   A 1 258 ? 25.420 9.168   -15.583 1.00 16.01 ? 248 ASP   A OD1 1 
ATOM   1947 O OD2 . ASP   A 1 258 ? 26.707 7.859   -14.329 1.00 18.55 ? 248 ASP   A OD2 1 
ATOM   1948 N N   . ILE   A 1 259 ? 21.504 7.208   -12.858 1.00 11.86 ? 249 ILE   A N   1 
ATOM   1949 C CA  . ILE   A 1 259 ? 20.370 6.344   -12.429 1.00 11.25 ? 249 ILE   A CA  1 
ATOM   1950 C C   . ILE   A 1 259 ? 19.059 6.896   -13.014 1.00 10.52 ? 249 ILE   A C   1 
ATOM   1951 O O   . ILE   A 1 259 ? 18.150 6.094   -13.271 1.00 9.33  ? 249 ILE   A O   1 
ATOM   1952 C CB  . ILE   A 1 259 ? 20.377 6.221   -10.893 1.00 12.64 ? 249 ILE   A CB  1 
ATOM   1953 C CG1 . ILE   A 1 259 ? 21.492 5.282   -10.436 1.00 13.27 ? 249 ILE   A CG1 1 
ATOM   1954 C CG2 . ILE   A 1 259 ? 19.036 5.781   -10.347 1.00 13.45 ? 249 ILE   A CG2 1 
ATOM   1955 C CD1 . ILE   A 1 259 ? 21.926 5.479   -9.010  1.00 14.21 ? 249 ILE   A CD1 1 
ATOM   1956 N N   . LEU   A 1 260 ? 18.973 8.212   -13.256 1.00 9.07  ? 250 LEU   A N   1 
ATOM   1957 C CA  . LEU   A 1 260 ? 17.740 8.842   -13.819 1.00 9.53  ? 250 LEU   A CA  1 
ATOM   1958 C C   . LEU   A 1 260 ? 17.749 8.681   -15.355 1.00 9.81  ? 250 LEU   A C   1 
ATOM   1959 O O   . LEU   A 1 260 ? 16.765 9.019   -15.990 1.00 10.05 ? 250 LEU   A O   1 
ATOM   1960 C CB  . LEU   A 1 260 ? 17.678 10.312  -13.392 1.00 8.78  ? 250 LEU   A CB  1 
ATOM   1961 C CG  . LEU   A 1 260 ? 17.346 10.580  -11.932 1.00 8.38  ? 250 LEU   A CG  1 
ATOM   1962 C CD1 . LEU   A 1 260 ? 17.647 12.033  -11.549 1.00 8.19  ? 250 LEU   A CD1 1 
ATOM   1963 C CD2 . LEU   A 1 260 ? 15.864 10.252  -11.696 1.00 8.67  ? 250 LEU   A CD2 1 
ATOM   1964 N N   . GLY   A 1 261 ? 18.805 8.105   -15.935 1.00 10.61 ? 251 GLY   A N   1 
ATOM   1965 C CA  . GLY   A 1 261 ? 18.944 7.929   -17.396 1.00 10.90 ? 251 GLY   A CA  1 
ATOM   1966 C C   . GLY   A 1 261 ? 17.723 7.300   -18.063 1.00 11.23 ? 251 GLY   A C   1 
ATOM   1967 O O   . GLY   A 1 261 ? 17.277 7.761   -19.106 1.00 11.74 ? 251 GLY   A O   1 
ATOM   1968 N N   . PRO   A 1 262 ? 17.167 6.169   -17.578 1.00 11.29 ? 252 PRO   A N   1 
ATOM   1969 C CA  . PRO   A 1 262 ? 15.957 5.621   -18.183 1.00 11.22 ? 252 PRO   A CA  1 
ATOM   1970 C C   . PRO   A 1 262 ? 14.804 6.638   -18.257 1.00 11.13 ? 252 PRO   A C   1 
ATOM   1971 O O   . PRO   A 1 262 ? 14.114 6.722   -19.253 1.00 10.65 ? 252 PRO   A O   1 
ATOM   1972 C CB  . PRO   A 1 262 ? 15.651 4.420   -17.268 1.00 11.67 ? 252 PRO   A CB  1 
ATOM   1973 C CG  . PRO   A 1 262 ? 17.016 4.016   -16.752 1.00 12.25 ? 252 PRO   A CG  1 
ATOM   1974 C CD  . PRO   A 1 262 ? 17.727 5.312   -16.529 1.00 11.37 ? 252 PRO   A CD  1 
ATOM   1975 N N   . LEU   A 1 263 ? 14.574 7.401   -17.195 1.00 9.97  ? 253 LEU   A N   1 
ATOM   1976 C CA  . LEU   A 1 263 ? 13.409 8.328   -17.154 1.00 9.70  ? 253 LEU   A CA  1 
ATOM   1977 C C   . LEU   A 1 263 ? 13.675 9.555   -18.045 1.00 9.47  ? 253 LEU   A C   1 
ATOM   1978 O O   . LEU   A 1 263 ? 12.743 10.013  -18.717 1.00 9.64  ? 253 LEU   A O   1 
ATOM   1979 C CB  . LEU   A 1 263 ? 13.144 8.702   -15.687 1.00 9.89  ? 253 LEU   A CB  1 
ATOM   1980 C CG  . LEU   A 1 263 ? 12.575 7.558   -14.847 1.00 10.59 ? 253 LEU   A CG  1 
ATOM   1981 C CD1 . LEU   A 1 263 ? 12.478 7.988   -13.384 1.00 10.60 ? 253 LEU   A CD1 1 
ATOM   1982 C CD2 . LEU   A 1 263 ? 11.193 7.144   -15.361 1.00 11.08 ? 253 LEU   A CD2 1 
ATOM   1983 N N   A SER   A 1 264 ? 14.923 10.039  -18.075 0.50 9.34  ? 254 SER   A N   1 
ATOM   1984 N N   B SER   A 1 264 ? 14.916 10.045  -18.104 0.50 9.11  ? 254 SER   A N   1 
ATOM   1985 C CA  A SER   A 1 264 ? 15.373 11.135  -18.970 0.50 9.98  ? 254 SER   A CA  1 
ATOM   1986 C CA  B SER   A 1 264 ? 15.307 11.178  -18.982 0.50 9.60  ? 254 SER   A CA  1 
ATOM   1987 C C   A SER   A 1 264 ? 15.178 10.699  -20.421 0.50 9.82  ? 254 SER   A C   1 
ATOM   1988 C C   B SER   A 1 264 ? 15.249 10.736  -20.450 0.50 9.64  ? 254 SER   A C   1 
ATOM   1989 O O   A SER   A 1 264 ? 14.646 11.487  -21.196 0.50 10.06 ? 254 SER   A O   1 
ATOM   1990 O O   B SER   A 1 264 ? 14.881 11.569  -21.288 0.50 9.84  ? 254 SER   A O   1 
ATOM   1991 C CB  A SER   A 1 264 ? 16.815 11.559  -18.715 0.50 10.36 ? 254 SER   A CB  1 
ATOM   1992 C CB  B SER   A 1 264 ? 16.664 11.757  -18.598 0.50 9.76  ? 254 SER   A CB  1 
ATOM   1993 O OG  A SER   A 1 264 ? 17.076 12.788  -19.378 0.50 10.58 ? 254 SER   A OG  1 
ATOM   1994 O OG  B SER   A 1 264 ? 17.661 10.757  -18.659 0.50 9.37  ? 254 SER   A OG  1 
ATOM   1995 N N   . ALA   A 1 265 ? 15.597 9.484   -20.766 1.00 10.08 ? 255 ALA   A N   1 
ATOM   1996 C CA  . ALA   A 1 265 ? 15.493 8.940   -22.139 1.00 10.85 ? 255 ALA   A CA  1 
ATOM   1997 C C   . ALA   A 1 265 ? 14.016 8.765   -22.546 1.00 12.77 ? 255 ALA   A C   1 
ATOM   1998 O O   . ALA   A 1 265 ? 13.643 9.065   -23.710 1.00 12.87 ? 255 ALA   A O   1 
ATOM   1999 C CB  . ALA   A 1 265 ? 16.215 7.626   -22.194 1.00 11.16 ? 255 ALA   A CB  1 
ATOM   2000 N N   . GLN   A 1 266 ? 13.201 8.178   -21.672 1.00 13.73 ? 256 GLN   A N   1 
ATOM   2001 C CA  . GLN   A 1 266 ? 11.756 7.971   -21.960 1.00 14.18 ? 256 GLN   A CA  1 
ATOM   2002 C C   . GLN   A 1 266 ? 11.072 9.322   -22.238 1.00 14.17 ? 256 GLN   A C   1 
ATOM   2003 O O   . GLN   A 1 266 ? 10.161 9.388   -23.130 1.00 16.21 ? 256 GLN   A O   1 
ATOM   2004 C CB  . GLN   A 1 266 ? 11.058 7.261   -20.797 1.00 16.41 ? 256 GLN   A CB  1 
ATOM   2005 C CG  . GLN   A 1 266 ? 9.564  7.112   -21.029 1.00 19.92 ? 256 GLN   A CG  1 
ATOM   2006 C CD  . GLN   A 1 266 ? 8.894  6.284   -19.960 1.00 21.75 ? 256 GLN   A CD  1 
ATOM   2007 O OE1 . GLN   A 1 266 ? 9.552  5.705   -19.096 1.00 24.18 ? 256 GLN   A OE1 1 
ATOM   2008 N NE2 . GLN   A 1 266 ? 7.575  6.222   -20.023 1.00 22.88 ? 256 GLN   A NE2 1 
ATOM   2009 N N   . THR   A 1 267 ? 11.408 10.385  -21.500 1.00 12.93 ? 257 THR   A N   1 
ATOM   2010 C CA  . THR   A 1 267 ? 10.650 11.656  -21.574 1.00 12.40 ? 257 THR   A CA  1 
ATOM   2011 C C   . THR   A 1 267 ? 11.308 12.654  -22.528 1.00 12.78 ? 257 THR   A C   1 
ATOM   2012 O O   . THR   A 1 267 ? 10.623 13.604  -22.920 1.00 13.69 ? 257 THR   A O   1 
ATOM   2013 C CB  . THR   A 1 267 ? 10.467 12.282  -20.189 1.00 11.66 ? 257 THR   A CB  1 
ATOM   2014 O OG1 . THR   A 1 267 ? 11.752 12.595  -19.649 1.00 12.13 ? 257 THR   A OG1 1 
ATOM   2015 C CG2 . THR   A 1 267 ? 9.682  11.353  -19.284 1.00 12.45 ? 257 THR   A CG2 1 
ATOM   2016 N N   . GLY   A 1 268 ? 12.586 12.484  -22.849 1.00 13.00 ? 258 GLY   A N   1 
ATOM   2017 C CA  . GLY   A 1 268 ? 13.337 13.485  -23.630 1.00 12.80 ? 258 GLY   A CA  1 
ATOM   2018 C C   . GLY   A 1 268 ? 13.672 14.726  -22.820 1.00 13.91 ? 258 GLY   A C   1 
ATOM   2019 O O   . GLY   A 1 268 ? 14.104 15.724  -23.423 1.00 18.88 ? 258 GLY   A O   1 
ATOM   2020 N N   . ILE   A 1 269 ? 13.511 14.698  -21.485 1.00 12.53 ? 259 ILE   A N   1 
ATOM   2021 C CA  . ILE   A 1 269 ? 13.876 15.846  -20.617 1.00 12.74 ? 259 ILE   A CA  1 
ATOM   2022 C C   . ILE   A 1 269 ? 15.182 15.519  -19.902 1.00 11.75 ? 259 ILE   A C   1 
ATOM   2023 O O   . ILE   A 1 269 ? 15.210 14.579  -19.061 1.00 10.69 ? 259 ILE   A O   1 
ATOM   2024 C CB  . ILE   A 1 269 ? 12.746 16.178  -19.620 1.00 13.08 ? 259 ILE   A CB  1 
ATOM   2025 C CG1 . ILE   A 1 269 ? 11.424 16.406  -20.346 1.00 14.84 ? 259 ILE   A CG1 1 
ATOM   2026 C CG2 . ILE   A 1 269 ? 13.126 17.376  -18.763 1.00 13.13 ? 259 ILE   A CG2 1 
ATOM   2027 C CD1 . ILE   A 1 269 ? 10.212 16.289  -19.484 1.00 15.28 ? 259 ILE   A CD1 1 
ATOM   2028 N N   . ALA   A 1 270 ? 16.209 16.298  -20.199 1.00 11.89 ? 260 ALA   A N   1 
ATOM   2029 C CA  . ALA   A 1 270 ? 17.534 16.226  -19.547 1.00 11.96 ? 260 ALA   A CA  1 
ATOM   2030 C C   . ALA   A 1 270 ? 17.359 16.385  -18.021 1.00 11.58 ? 260 ALA   A C   1 
ATOM   2031 O O   . ALA   A 1 270 ? 16.559 17.241  -17.568 1.00 10.30 ? 260 ALA   A O   1 
ATOM   2032 C CB  . ALA   A 1 270 ? 18.431 17.278  -20.142 1.00 12.11 ? 260 ALA   A CB  1 
ATOM   2033 N N   . VAL   A 1 271 ? 18.117 15.618  -17.249 1.00 11.89 ? 261 VAL   A N   1 
ATOM   2034 C CA  . VAL   A 1 271 ? 18.051 15.704  -15.767 1.00 11.37 ? 261 VAL   A CA  1 
ATOM   2035 C C   . VAL   A 1 271 ? 18.311 17.153  -15.323 1.00 10.93 ? 261 VAL   A C   1 
ATOM   2036 O O   . VAL   A 1 271 ? 17.576 17.637  -14.461 1.00 9.87  ? 261 VAL   A O   1 
ATOM   2037 C CB  . VAL   A 1 271 ? 18.987 14.694  -15.097 1.00 11.85 ? 261 VAL   A CB  1 
ATOM   2038 C CG1 . VAL   A 1 271 ? 19.098 14.968  -13.618 1.00 12.81 ? 261 VAL   A CG1 1 
ATOM   2039 C CG2 . VAL   A 1 271 ? 18.533 13.263  -15.344 1.00 13.66 ? 261 VAL   A CG2 1 
ATOM   2040 N N   . LEU   A 1 272 ? 19.289 17.845  -15.905 1.00 10.70 ? 262 LEU   A N   1 
ATOM   2041 C CA  . LEU   A 1 272 ? 19.572 19.242  -15.498 1.00 11.55 ? 262 LEU   A CA  1 
ATOM   2042 C C   . LEU   A 1 272 ? 18.378 20.170  -15.820 1.00 10.16 ? 262 LEU   A C   1 
ATOM   2043 O O   . LEU   A 1 272 ? 18.162 21.139  -15.057 1.00 9.06  ? 262 LEU   A O   1 
ATOM   2044 C CB  . LEU   A 1 272 ? 20.892 19.695  -16.140 1.00 12.45 ? 262 LEU   A CB  1 
ATOM   2045 C CG  . LEU   A 1 272 ? 22.145 19.052  -15.548 1.00 13.51 ? 262 LEU   A CG  1 
ATOM   2046 C CD1 . LEU   A 1 272 ? 23.413 19.636  -16.163 1.00 14.05 ? 262 LEU   A CD1 1 
ATOM   2047 C CD2 . LEU   A 1 272 ? 22.201 19.184  -14.043 1.00 14.86 ? 262 LEU   A CD2 1 
ATOM   2048 N N   . ASP   A 1 273 ? 17.644 19.963  -16.906 1.00 10.16 ? 263 ASP   A N   1 
ATOM   2049 C CA  . ASP   A 1 273 ? 16.405 20.761  -17.146 1.00 10.84 ? 263 ASP   A CA  1 
ATOM   2050 C C   . ASP   A 1 273 ? 15.375 20.449  -16.053 1.00 10.38 ? 263 ASP   A C   1 
ATOM   2051 O O   . ASP   A 1 273 ? 14.702 21.397  -15.558 1.00 10.26 ? 263 ASP   A O   1 
ATOM   2052 C CB  . ASP   A 1 273 ? 15.786 20.488  -18.503 1.00 11.65 ? 263 ASP   A CB  1 
ATOM   2053 C CG  . ASP   A 1 273 ? 16.674 20.914  -19.656 1.00 12.72 ? 263 ASP   A CG  1 
ATOM   2054 O OD1 . ASP   A 1 273 ? 17.836 21.374  -19.398 1.00 11.97 ? 263 ASP   A OD1 1 
ATOM   2055 O OD2 . ASP   A 1 273 ? 16.181 20.797  -20.801 1.00 12.49 ? 263 ASP   A OD2 1 
ATOM   2056 N N   . MET   A 1 274 ? 15.249 19.180  -15.667 1.00 9.79  ? 264 MET   A N   1 
ATOM   2057 C CA  . MET   A 1 274 ? 14.284 18.852  -14.599 1.00 10.27 ? 264 MET   A CA  1 
ATOM   2058 C C   . MET   A 1 274 ? 14.769 19.483  -13.288 1.00 10.20 ? 264 MET   A C   1 
ATOM   2059 O O   . MET   A 1 274 ? 13.944 19.934  -12.498 1.00 10.81 ? 264 MET   A O   1 
ATOM   2060 C CB  . MET   A 1 274 ? 14.104 17.346  -14.460 1.00 10.89 ? 264 MET   A CB  1 
ATOM   2061 C CG  . MET   A 1 274 ? 12.909 17.011  -13.602 1.00 10.79 ? 264 MET   A CG  1 
ATOM   2062 S SD  . MET   A 1 274 ? 11.320 17.416  -14.343 1.00 11.72 ? 264 MET   A SD  1 
ATOM   2063 C CE  . MET   A 1 274 ? 11.028 15.908  -15.258 1.00 11.60 ? 264 MET   A CE  1 
ATOM   2064 N N   . CYS   A 1 275 ? 16.078 19.524  -13.040 1.00 11.25 ? 265 CYS   A N   1 
ATOM   2065 C CA  . CYS   A 1 275 ? 16.631 20.202  -11.837 1.00 11.52 ? 265 CYS   A CA  1 
ATOM   2066 C C   . CYS   A 1 275 ? 16.240 21.672  -11.827 1.00 10.96 ? 265 CYS   A C   1 
ATOM   2067 O O   . CYS   A 1 275 ? 15.957 22.176  -10.765 1.00 9.73  ? 265 CYS   A O   1 
ATOM   2068 C CB  . CYS   A 1 275 ? 18.149 20.120  -11.754 1.00 11.42 ? 265 CYS   A CB  1 
ATOM   2069 S SG  . CYS   A 1 275 ? 18.724 18.473  -11.316 1.00 12.41 ? 265 CYS   A SG  1 
ATOM   2070 N N   . ALA   A 1 276 ? 16.211 22.326  -12.986 1.00 12.07 ? 266 ALA   A N   1 
ATOM   2071 C CA  . ALA   A 1 276 ? 15.808 23.748  -13.107 1.00 12.63 ? 266 ALA   A CA  1 
ATOM   2072 C C   . ALA   A 1 276 ? 14.325 23.905  -12.751 1.00 13.26 ? 266 ALA   A C   1 
ATOM   2073 O O   . ALA   A 1 276 ? 13.985 24.884  -12.006 1.00 14.51 ? 266 ALA   A O   1 
ATOM   2074 C CB  . ALA   A 1 276 ? 16.091 24.268  -14.494 1.00 13.37 ? 266 ALA   A CB  1 
ATOM   2075 N N   . SER   A 1 277 ? 13.499 22.924  -13.107 1.00 13.42 ? 267 SER   A N   1 
ATOM   2076 C CA  . SER   A 1 277 ? 12.064 22.902  -12.726 1.00 12.65 ? 267 SER   A CA  1 
ATOM   2077 C C   . SER   A 1 277 ? 11.958 22.716  -11.216 1.00 11.63 ? 267 SER   A C   1 
ATOM   2078 O O   . SER   A 1 277 ? 11.146 23.440  -10.596 1.00 10.41 ? 267 SER   A O   1 
ATOM   2079 C CB  . SER   A 1 277 ? 11.269 21.859  -13.467 1.00 14.26 ? 267 SER   A CB  1 
ATOM   2080 O OG  . SER   A 1 277 ? 11.079 22.275  -14.814 1.00 17.28 ? 267 SER   A OG  1 
ATOM   2081 N N   . LEU   A 1 278 ? 12.702 21.754  -10.669 1.00 11.58 ? 268 LEU   A N   1 
ATOM   2082 C CA  . LEU   A 1 278 ? 12.705 21.508  -9.207  1.00 11.89 ? 268 LEU   A CA  1 
ATOM   2083 C C   . LEU   A 1 278 ? 13.128 22.803  -8.493  1.00 12.41 ? 268 LEU   A C   1 
ATOM   2084 O O   . LEU   A 1 278 ? 12.441 23.226  -7.566  1.00 11.77 ? 268 LEU   A O   1 
ATOM   2085 C CB  . LEU   A 1 278 ? 13.623 20.334  -8.860  1.00 11.91 ? 268 LEU   A CB  1 
ATOM   2086 C CG  . LEU   A 1 278 ? 13.698 19.969  -7.379  1.00 12.01 ? 268 LEU   A CG  1 
ATOM   2087 C CD1 . LEU   A 1 278 ? 12.315 19.875  -6.735  1.00 13.29 ? 268 LEU   A CD1 1 
ATOM   2088 C CD2 . LEU   A 1 278 ? 14.438 18.660  -7.196  1.00 11.91 ? 268 LEU   A CD2 1 
ATOM   2089 N N   . LYS   A 1 279 ? 14.207 23.445  -8.936  1.00 13.06 ? 269 LYS   A N   1 
ATOM   2090 C CA  . LYS   A 1 279 ? 14.699 24.714  -8.335  1.00 14.27 ? 269 LYS   A CA  1 
ATOM   2091 C C   . LYS   A 1 279 ? 13.557 25.739  -8.252  1.00 14.35 ? 269 LYS   A C   1 
ATOM   2092 O O   . LYS   A 1 279 ? 13.374 26.355  -7.155  1.00 12.88 ? 269 LYS   A O   1 
ATOM   2093 C CB  . LYS   A 1 279 ? 15.887 25.240  -9.135  1.00 15.92 ? 269 LYS   A CB  1 
ATOM   2094 C CG  . LYS   A 1 279 ? 16.343 26.662  -8.815  1.00 18.29 ? 269 LYS   A CG  1 
ATOM   2095 C CD  . LYS   A 1 279 ? 17.661 26.972  -9.489  1.00 21.56 ? 269 LYS   A CD  1 
ATOM   2096 C CE  . LYS   A 1 279 ? 17.966 28.445  -9.689  1.00 24.27 ? 269 LYS   A CE  1 
ATOM   2097 N NZ  . LYS   A 1 279 ? 19.019 28.620  -10.730 1.00 25.39 ? 269 LYS   A NZ  1 
ATOM   2098 N N   . GLU   A 1 280 ? 12.776 25.902  -9.324  1.00 13.45 ? 270 GLU   A N   1 
ATOM   2099 C CA  . GLU   A 1 280 ? 11.666 26.894  -9.319  1.00 16.05 ? 270 GLU   A CA  1 
ATOM   2100 C C   . GLU   A 1 280 ? 10.621 26.481  -8.283  1.00 13.40 ? 270 GLU   A C   1 
ATOM   2101 O O   . GLU   A 1 280 ? 10.124 27.367  -7.557  1.00 13.48 ? 270 GLU   A O   1 
ATOM   2102 C CB  . GLU   A 1 280 ? 11.086 27.076  -10.719 1.00 17.87 ? 270 GLU   A CB  1 
ATOM   2103 C CG  . GLU   A 1 280 ? 12.068 27.707  -11.691 1.00 21.52 ? 270 GLU   A CG  1 
ATOM   2104 C CD  . GLU   A 1 280 ? 12.687 29.035  -11.272 1.00 26.18 ? 270 GLU   A CD  1 
ATOM   2105 O OE1 . GLU   A 1 280 ? 11.918 29.929  -10.871 1.00 28.30 ? 270 GLU   A OE1 1 
ATOM   2106 O OE2 . GLU   A 1 280 ? 13.937 29.166  -11.336 1.00 28.62 ? 270 GLU   A OE2 1 
ATOM   2107 N N   . LEU   A 1 281 ? 10.299 25.193  -8.205  1.00 13.05 ? 271 LEU   A N   1 
ATOM   2108 C CA  . LEU   A 1 281 ? 9.307  24.664  -7.231  1.00 14.10 ? 271 LEU   A CA  1 
ATOM   2109 C C   . LEU   A 1 281 ? 9.828  24.911  -5.802  1.00 14.03 ? 271 LEU   A C   1 
ATOM   2110 O O   . LEU   A 1 281 ? 9.008  25.252  -4.925  1.00 16.13 ? 271 LEU   A O   1 
ATOM   2111 C CB  . LEU   A 1 281 ? 9.071  23.168  -7.478  1.00 13.71 ? 271 LEU   A CB  1 
ATOM   2112 C CG  . LEU   A 1 281 ? 8.276  22.766  -8.726  1.00 14.18 ? 271 LEU   A CG  1 
ATOM   2113 C CD1 . LEU   A 1 281 ? 8.308  21.252  -8.892  1.00 14.21 ? 271 LEU   A CD1 1 
ATOM   2114 C CD2 . LEU   A 1 281 ? 6.858  23.244  -8.650  1.00 14.86 ? 271 LEU   A CD2 1 
ATOM   2115 N N   . LEU   A 1 282 ? 11.132 24.763  -5.550  1.00 13.46 ? 272 LEU   A N   1 
ATOM   2116 C CA  . LEU   A 1 282 ? 11.655 24.947  -4.163  1.00 14.17 ? 272 LEU   A CA  1 
ATOM   2117 C C   . LEU   A 1 282 ? 11.594 26.427  -3.801  1.00 15.28 ? 272 LEU   A C   1 
ATOM   2118 O O   . LEU   A 1 282 ? 11.239 26.749  -2.632  1.00 16.31 ? 272 LEU   A O   1 
ATOM   2119 C CB  . LEU   A 1 282 ? 13.081 24.430  -4.054  1.00 13.96 ? 272 LEU   A CB  1 
ATOM   2120 C CG  . LEU   A 1 282 ? 13.206 22.917  -4.094  1.00 14.24 ? 272 LEU   A CG  1 
ATOM   2121 C CD1 . LEU   A 1 282 ? 14.666 22.481  -4.065  1.00 15.52 ? 272 LEU   A CD1 1 
ATOM   2122 C CD2 . LEU   A 1 282 ? 12.461 22.303  -2.937  1.00 14.94 ? 272 LEU   A CD2 1 
ATOM   2123 N N   . GLN   A 1 283 ? 11.995 27.282  -4.747  1.00 16.75 ? 273 GLN   A N   1 
ATOM   2124 C CA  . GLN   A 1 283 ? 12.064 28.747  -4.519  1.00 18.57 ? 273 GLN   A CA  1 
ATOM   2125 C C   . GLN   A 1 283 ? 10.666 29.369  -4.508  1.00 19.36 ? 273 GLN   A C   1 
ATOM   2126 O O   . GLN   A 1 283 ? 10.478 30.269  -3.700  1.00 19.39 ? 273 GLN   A O   1 
ATOM   2127 C CB  . GLN   A 1 283 ? 12.957 29.416  -5.557  1.00 18.86 ? 273 GLN   A CB  1 
ATOM   2128 C CG  . GLN   A 1 283 ? 14.431 29.146  -5.288  1.00 19.78 ? 273 GLN   A CG  1 
ATOM   2129 C CD  . GLN   A 1 283 ? 15.359 29.638  -6.374  1.00 22.12 ? 273 GLN   A CD  1 
ATOM   2130 O OE1 . GLN   A 1 283 ? 14.959 29.949  -7.487  1.00 23.34 ? 273 GLN   A OE1 1 
ATOM   2131 N NE2 . GLN   A 1 283 ? 16.641 29.658  -6.060  1.00 26.08 ? 273 GLN   A NE2 1 
ATOM   2132 N N   . ASN   A 1 284 ? 9.722  28.906  -5.330  1.00 19.95 ? 274 ASN   A N   1 
ATOM   2133 C CA  . ASN   A 1 284 ? 8.421  29.608  -5.541  1.00 22.13 ? 274 ASN   A CA  1 
ATOM   2134 C C   . ASN   A 1 284 ? 7.262  28.868  -4.885  1.00 22.56 ? 274 ASN   A C   1 
ATOM   2135 O O   . ASN   A 1 284 ? 6.187  29.471  -4.736  1.00 21.44 ? 274 ASN   A O   1 
ATOM   2136 C CB  . ASN   A 1 284 ? 8.190  29.852  -7.028  1.00 24.16 ? 274 ASN   A CB  1 
ATOM   2137 C CG  . ASN   A 1 284 ? 9.341  30.662  -7.574  1.00 26.27 ? 274 ASN   A CG  1 
ATOM   2138 O OD1 . ASN   A 1 284 ? 9.513  31.815  -7.191  1.00 29.60 ? 274 ASN   A OD1 1 
ATOM   2139 N ND2 . ASN   A 1 284 ? 10.188 30.044  -8.375  1.00 27.13 ? 274 ASN   A ND2 1 
ATOM   2140 N N   . GLY   A 1 285 ? 7.470  27.622  -4.476  1.00 21.75 ? 275 GLY   A N   1 
ATOM   2141 C CA  . GLY   A 1 285 ? 6.381  26.753  -4.023  1.00 22.30 ? 275 GLY   A CA  1 
ATOM   2142 C C   . GLY   A 1 285 ? 5.487  26.378  -5.183  1.00 20.44 ? 275 GLY   A C   1 
ATOM   2143 O O   . GLY   A 1 285 ? 5.856  26.611  -6.349  1.00 21.60 ? 275 GLY   A O   1 
ATOM   2144 N N   . MET   A 1 286 ? 4.347  25.787  -4.877  1.00 22.10 ? 276 MET   A N   1 
ATOM   2145 C CA  . MET   A 1 286 ? 3.475  25.176  -5.901  1.00 23.93 ? 276 MET   A CA  1 
ATOM   2146 C C   . MET   A 1 286 ? 2.272  26.088  -6.171  1.00 24.13 ? 276 MET   A C   1 
ATOM   2147 O O   . MET   A 1 286 ? 1.519  25.795  -7.115  1.00 21.95 ? 276 MET   A O   1 
ATOM   2148 C CB  . MET   A 1 286 ? 3.081  23.767  -5.461  1.00 27.63 ? 276 MET   A CB  1 
ATOM   2149 C CG  . MET   A 1 286 ? 4.317  22.861  -5.426  1.00 28.66 ? 276 MET   A CG  1 
ATOM   2150 S SD  . MET   A 1 286 ? 4.015  21.183  -4.874  1.00 37.47 ? 276 MET   A SD  1 
ATOM   2151 C CE  . MET   A 1 286 ? 2.610  20.817  -5.903  1.00 25.82 ? 276 MET   A CE  1 
ATOM   2152 N N   . ASN   A 1 287 ? 2.171  27.214  -5.459  1.00 23.54 ? 277 ASN   A N   1 
ATOM   2153 C CA  . ASN   A 1 287 ? 1.159  28.257  -5.770  1.00 23.73 ? 277 ASN   A CA  1 
ATOM   2154 C C   . ASN   A 1 287 ? -0.220 27.601  -5.693  1.00 23.17 ? 277 ASN   A C   1 
ATOM   2155 O O   . ASN   A 1 287 ? -1.072 27.953  -6.524  1.00 24.83 ? 277 ASN   A O   1 
ATOM   2156 C CB  . ASN   A 1 287 ? 1.408  28.860  -7.152  1.00 26.60 ? 277 ASN   A CB  1 
ATOM   2157 C CG  . ASN   A 1 287 ? 2.495  29.908  -7.153  1.00 30.34 ? 277 ASN   A CG  1 
ATOM   2158 O OD1 . ASN   A 1 287 ? 3.575  29.714  -7.721  1.00 34.93 ? 277 ASN   A OD1 1 
ATOM   2159 N ND2 . ASN   A 1 287 ? 2.209  31.034  -6.520  1.00 33.06 ? 277 ASN   A ND2 1 
ATOM   2160 N N   . GLY   A 1 288 ? -0.407 26.664  -4.754  1.00 22.64 ? 278 GLY   A N   1 
ATOM   2161 C CA  . GLY   A 1 288 ? -1.693 25.975  -4.495  1.00 23.50 ? 278 GLY   A CA  1 
ATOM   2162 C C   . GLY   A 1 288 ? -2.059 24.961  -5.578  1.00 22.08 ? 278 GLY   A C   1 
ATOM   2163 O O   . GLY   A 1 288 ? -3.202 24.450  -5.540  1.00 24.44 ? 278 GLY   A O   1 
ATOM   2164 N N   . ARG   A 1 289 ? -1.146 24.656  -6.502  1.00 20.80 ? 279 ARG   A N   1 
ATOM   2165 C CA  . ARG   A 1 289 ? -1.306 23.601  -7.543  1.00 21.03 ? 279 ARG   A CA  1 
ATOM   2166 C C   . ARG   A 1 289 ? -0.889 22.255  -6.951  1.00 18.85 ? 279 ARG   A C   1 
ATOM   2167 O O   . ARG   A 1 289 ? -0.275 22.239  -5.892  1.00 18.46 ? 279 ARG   A O   1 
ATOM   2168 C CB  . ARG   A 1 289 ? -0.436 23.878  -8.776  1.00 24.45 ? 279 ARG   A CB  1 
ATOM   2169 C CG  . ARG   A 1 289 ? -1.072 24.744  -9.852  1.00 29.87 ? 279 ARG   A CG  1 
ATOM   2170 C CD  . ARG   A 1 289 ? -0.563 26.170  -9.863  1.00 31.99 ? 279 ARG   A CD  1 
ATOM   2171 N NE  . ARG   A 1 289 ? 0.836  26.273  -10.250 1.00 38.63 ? 279 ARG   A NE  1 
ATOM   2172 C CZ  . ARG   A 1 289 ? 1.422  27.384  -10.711 1.00 40.89 ? 279 ARG   A CZ  1 
ATOM   2173 N NH1 . ARG   A 1 289 ? 2.698  27.351  -11.042 1.00 38.99 ? 279 ARG   A NH1 1 
ATOM   2174 N NH2 . ARG   A 1 289 ? 0.741  28.512  -10.880 1.00 40.60 ? 279 ARG   A NH2 1 
ATOM   2175 N N   . THR   A 1 290 ? -1.182 21.164  -7.649  1.00 17.13 ? 280 THR   A N   1 
ATOM   2176 C CA  . THR   A 1 290 ? -0.810 19.788  -7.241  1.00 14.77 ? 280 THR   A CA  1 
ATOM   2177 C C   . THR   A 1 290 ? -0.008 19.105  -8.347  1.00 13.84 ? 280 THR   A C   1 
ATOM   2178 O O   . THR   A 1 290 ? -0.086 19.508  -9.513  1.00 14.12 ? 280 THR   A O   1 
ATOM   2179 C CB  . THR   A 1 290 ? -2.028 18.937  -6.877  1.00 15.28 ? 280 THR   A CB  1 
ATOM   2180 O OG1 . THR   A 1 290 ? -2.881 18.882  -8.020  1.00 13.64 ? 280 THR   A OG1 1 
ATOM   2181 C CG2 . THR   A 1 290 ? -2.754 19.476  -5.672  1.00 15.23 ? 280 THR   A CG2 1 
ATOM   2182 N N   . ILE   A 1 291 ? 0.765  18.099  -7.952  1.00 12.74 ? 281 ILE   A N   1 
ATOM   2183 C CA  . ILE   A 1 291 ? 1.526  17.220  -8.873  1.00 12.80 ? 281 ILE   A CA  1 
ATOM   2184 C C   . ILE   A 1 291 ? 1.189  15.795  -8.443  1.00 12.33 ? 281 ILE   A C   1 
ATOM   2185 O O   . ILE   A 1 291 ? 1.381  15.461  -7.247  1.00 10.44 ? 281 ILE   A O   1 
ATOM   2186 C CB  . ILE   A 1 291 ? 3.028  17.517  -8.803  1.00 12.47 ? 281 ILE   A CB  1 
ATOM   2187 C CG1 . ILE   A 1 291 ? 3.362  18.966  -9.163  1.00 13.25 ? 281 ILE   A CG1 1 
ATOM   2188 C CG2 . ILE   A 1 291 ? 3.800  16.524  -9.672  1.00 13.19 ? 281 ILE   A CG2 1 
ATOM   2189 C CD1 . ILE   A 1 291 ? 4.804  19.306  -8.947  1.00 13.96 ? 281 ILE   A CD1 1 
ATOM   2190 N N   . LEU   A 1 292 ? 0.615  15.017  -9.351  1.00 12.84 ? 282 LEU   A N   1 
ATOM   2191 C CA  . LEU   A 1 292 ? 0.136  13.649  -9.046  1.00 13.14 ? 282 LEU   A CA  1 
ATOM   2192 C C   . LEU   A 1 292 ? -0.709 13.661  -7.761  1.00 13.23 ? 282 LEU   A C   1 
ATOM   2193 O O   . LEU   A 1 292 ? -0.567 12.759  -6.934  1.00 13.11 ? 282 LEU   A O   1 
ATOM   2194 C CB  . LEU   A 1 292 ? 1.373  12.752  -8.959  1.00 13.34 ? 282 LEU   A CB  1 
ATOM   2195 C CG  . LEU   A 1 292 ? 2.061  12.531  -10.308 1.00 14.46 ? 282 LEU   A CG  1 
ATOM   2196 C CD1 . LEU   A 1 292 ? 3.386  11.802  -10.124 1.00 13.23 ? 282 LEU   A CD1 1 
ATOM   2197 C CD2 . LEU   A 1 292 ? 1.156  11.775  -11.262 1.00 14.65 ? 282 LEU   A CD2 1 
ATOM   2198 N N   . GLY   A 1 293 ? -1.547 14.686  -7.616  1.00 14.86 ? 283 GLY   A N   1 
ATOM   2199 C CA  . GLY   A 1 293 ? -2.541 14.858  -6.534  1.00 15.34 ? 283 GLY   A CA  1 
ATOM   2200 C C   . GLY   A 1 293 ? -1.911 15.252  -5.216  1.00 15.54 ? 283 GLY   A C   1 
ATOM   2201 O O   . GLY   A 1 293 ? -2.653 15.271  -4.194  1.00 17.26 ? 283 GLY   A O   1 
ATOM   2202 N N   . SER   A 1 294 ? -0.603 15.530  -5.197  1.00 14.19 ? 284 SER   A N   1 
ATOM   2203 C CA  . SER   A 1 294 ? 0.102  15.984  -3.969  1.00 14.12 ? 284 SER   A CA  1 
ATOM   2204 C C   . SER   A 1 294 ? 0.390  17.491  -4.021  1.00 12.83 ? 284 SER   A C   1 
ATOM   2205 O O   . SER   A 1 294 ? 0.778  17.991  -5.066  1.00 11.77 ? 284 SER   A O   1 
ATOM   2206 C CB  . SER   A 1 294 ? 1.375  15.201  -3.730  1.00 15.05 ? 284 SER   A CB  1 
ATOM   2207 O OG  . SER   A 1 294 ? 2.090  15.768  -2.637  1.00 18.40 ? 284 SER   A OG  1 
ATOM   2208 N N   . ALA   A 1 295 ? 0.314  18.152  -2.861  1.00 12.61 ? 285 ALA   A N   1 
ATOM   2209 C CA  . ALA   A 1 295 ? 0.590  19.590  -2.684  1.00 13.86 ? 285 ALA   A CA  1 
ATOM   2210 C C   . ALA   A 1 295 ? 1.969  19.797  -2.052  1.00 13.97 ? 285 ALA   A C   1 
ATOM   2211 O O   . ALA   A 1 295 ? 2.303  20.954  -1.737  1.00 15.32 ? 285 ALA   A O   1 
ATOM   2212 C CB  . ALA   A 1 295 ? -0.500 20.179  -1.848  1.00 14.50 ? 285 ALA   A CB  1 
ATOM   2213 N N   . LEU   A 1 296 ? 2.756  18.729  -1.939  1.00 13.37 ? 286 LEU   A N   1 
ATOM   2214 C CA  . LEU   A 1 296 ? 4.171  18.735  -1.495  1.00 14.12 ? 286 LEU   A CA  1 
ATOM   2215 C C   . LEU   A 1 296 ? 4.998  17.933  -2.503  1.00 12.66 ? 286 LEU   A C   1 
ATOM   2216 O O   . LEU   A 1 296 ? 4.412  17.134  -3.261  1.00 11.87 ? 286 LEU   A O   1 
ATOM   2217 C CB  . LEU   A 1 296 ? 4.343  18.032  -0.146  1.00 14.92 ? 286 LEU   A CB  1 
ATOM   2218 C CG  . LEU   A 1 296 ? 3.614  18.597  1.046   1.00 17.81 ? 286 LEU   A CG  1 
ATOM   2219 C CD1 . LEU   A 1 296 ? 3.767  17.614  2.191   1.00 17.21 ? 286 LEU   A CD1 1 
ATOM   2220 C CD2 . LEU   A 1 296 ? 4.144  19.982  1.419   1.00 18.96 ? 286 LEU   A CD2 1 
ATOM   2221 N N   . LEU   A 1 297 ? 6.320  18.107  -2.479  1.00 12.95 ? 287 LEU   A N   1 
ATOM   2222 C CA  . LEU   A 1 297 ? 7.217  17.317  -3.361  1.00 13.14 ? 287 LEU   A CA  1 
ATOM   2223 C C   . LEU   A 1 297 ? 7.479  15.966  -2.682  1.00 13.16 ? 287 LEU   A C   1 
ATOM   2224 O O   . LEU   A 1 297 ? 7.834  15.958  -1.513  1.00 14.72 ? 287 LEU   A O   1 
ATOM   2225 C CB  . LEU   A 1 297 ? 8.490  18.131  -3.616  1.00 14.09 ? 287 LEU   A CB  1 
ATOM   2226 C CG  . LEU   A 1 297 ? 8.248  19.544  -4.159  1.00 14.48 ? 287 LEU   A CG  1 
ATOM   2227 C CD1 . LEU   A 1 297 ? 9.534  20.347  -4.163  1.00 15.43 ? 287 LEU   A CD1 1 
ATOM   2228 C CD2 . LEU   A 1 297 ? 7.633  19.497  -5.544  1.00 14.34 ? 287 LEU   A CD2 1 
ATOM   2229 N N   . GLU   A 1 298 ? 7.175  14.867  -3.356  1.00 14.13 ? 288 GLU   A N   1 
ATOM   2230 C CA  . GLU   A 1 298 ? 7.261  13.482  -2.819  1.00 13.06 ? 288 GLU   A CA  1 
ATOM   2231 C C   . GLU   A 1 298 ? 8.649  12.917  -3.052  1.00 11.15 ? 288 GLU   A C   1 
ATOM   2232 O O   . GLU   A 1 298 ? 9.113  12.957  -4.174  1.00 9.33  ? 288 GLU   A O   1 
ATOM   2233 C CB  . GLU   A 1 298 ? 6.277  12.557  -3.525  1.00 15.16 ? 288 GLU   A CB  1 
ATOM   2234 C CG  . GLU   A 1 298 ? 4.842  12.977  -3.312  1.00 19.31 ? 288 GLU   A CG  1 
ATOM   2235 C CD  . GLU   A 1 298 ? 4.244  12.652  -1.947  1.00 22.83 ? 288 GLU   A CD  1 
ATOM   2236 O OE1 . GLU   A 1 298 ? 4.808  11.782  -1.246  1.00 21.32 ? 288 GLU   A OE1 1 
ATOM   2237 O OE2 . GLU   A 1 298 ? 3.139  13.206  -1.639  1.00 23.59 ? 288 GLU   A OE2 1 
ATOM   2238 N N   . ASP   A 1 299 ? 9.273  12.382  -2.012  1.00 9.70  ? 289 ASP   A N   1 
ATOM   2239 C CA  . ASP   A 1 299 ? 10.639 11.849  -2.145  1.00 9.36  ? 289 ASP   A CA  1 
ATOM   2240 C C   . ASP   A 1 299 ? 10.682 10.374  -1.729  1.00 9.69  ? 289 ASP   A C   1 
ATOM   2241 O O   . ASP   A 1 299 ? 11.797 9.919   -1.540  1.00 9.10  ? 289 ASP   A O   1 
ATOM   2242 C CB  . ASP   A 1 299 ? 11.652 12.671  -1.346  1.00 9.42  ? 289 ASP   A CB  1 
ATOM   2243 C CG  . ASP   A 1 299 ? 11.625 12.414  0.146   1.00 9.37  ? 289 ASP   A CG  1 
ATOM   2244 O OD1 . ASP   A 1 299 ? 10.587 11.954  0.631   1.00 9.02  ? 289 ASP   A OD1 1 
ATOM   2245 O OD2 . ASP   A 1 299 ? 12.669 12.658  0.795   1.00 10.48 ? 289 ASP   A OD2 1 
ATOM   2246 N N   . GLU   A 1 300 ? 9.563  9.650   -1.637  1.00 9.80  ? 290 GLU   A N   1 
ATOM   2247 C CA  . GLU   A 1 300 ? 9.641  8.204   -1.309  1.00 10.61 ? 290 GLU   A CA  1 
ATOM   2248 C C   . GLU   A 1 300 ? 9.294  7.331   -2.514  1.00 10.90 ? 290 GLU   A C   1 
ATOM   2249 O O   . GLU   A 1 300 ? 8.935  6.185   -2.304  1.00 12.00 ? 290 GLU   A O   1 
ATOM   2250 C CB  . GLU   A 1 300 ? 8.857  7.895   -0.034  1.00 11.59 ? 290 GLU   A CB  1 
ATOM   2251 C CG  . GLU   A 1 300 ? 9.443  8.623   1.164   1.00 12.12 ? 290 GLU   A CG  1 
ATOM   2252 C CD  . GLU   A 1 300 ? 9.121  7.991   2.502   1.00 12.85 ? 290 GLU   A CD  1 
ATOM   2253 O OE1 . GLU   A 1 300 ? 8.330  7.035   2.514   1.00 13.52 ? 290 GLU   A OE1 1 
ATOM   2254 O OE2 . GLU   A 1 300 ? 9.714  8.409   3.506   1.00 13.58 ? 290 GLU   A OE2 1 
ATOM   2255 N N   . PHE   A 1 301 ? 9.559  7.797   -3.740  1.00 10.47 ? 291 PHE   A N   1 
ATOM   2256 C CA  . PHE   A 1 301 ? 9.611  6.919   -4.928  1.00 10.46 ? 291 PHE   A CA  1 
ATOM   2257 C C   . PHE   A 1 301 ? 11.036 6.932   -5.486  1.00 10.07 ? 291 PHE   A C   1 
ATOM   2258 O O   . PHE   A 1 301 ? 11.472 8.004   -5.888  1.00 9.12  ? 291 PHE   A O   1 
ATOM   2259 C CB  . PHE   A 1 301 ? 8.630  7.365   -6.017  1.00 11.56 ? 291 PHE   A CB  1 
ATOM   2260 C CG  . PHE   A 1 301 ? 7.166  7.342   -5.629  1.00 11.86 ? 291 PHE   A CG  1 
ATOM   2261 C CD1 . PHE   A 1 301 ? 6.421  6.184   -5.739  1.00 14.93 ? 291 PHE   A CD1 1 
ATOM   2262 C CD2 . PHE   A 1 301 ? 6.516  8.489   -5.233  1.00 12.86 ? 291 PHE   A CD2 1 
ATOM   2263 C CE1 . PHE   A 1 301 ? 5.072  6.164   -5.404  1.00 14.39 ? 291 PHE   A CE1 1 
ATOM   2264 C CE2 . PHE   A 1 301 ? 5.159  8.479   -4.932  1.00 14.98 ? 291 PHE   A CE2 1 
ATOM   2265 C CZ  . PHE   A 1 301 ? 4.448  7.306   -4.993  1.00 14.76 ? 291 PHE   A CZ  1 
ATOM   2266 N N   . THR   A 1 302 ? 11.691 5.778   -5.627  1.00 10.81 ? 292 THR   A N   1 
ATOM   2267 C CA  . THR   A 1 302 ? 13.019 5.696   -6.290  1.00 10.05 ? 292 THR   A CA  1 
ATOM   2268 C C   . THR   A 1 302 ? 12.833 5.715   -7.815  1.00 9.62  ? 292 THR   A C   1 
ATOM   2269 O O   . THR   A 1 302 ? 11.719 5.537   -8.325  1.00 8.59  ? 292 THR   A O   1 
ATOM   2270 C CB  . THR   A 1 302 ? 13.804 4.428   -5.947  1.00 10.81 ? 292 THR   A CB  1 
ATOM   2271 O OG1 . THR   A 1 302 ? 13.044 3.399   -6.564  1.00 10.95 ? 292 THR   A OG1 1 
ATOM   2272 C CG2 . THR   A 1 302 ? 14.038 4.249   -4.452  1.00 10.05 ? 292 THR   A CG2 1 
ATOM   2273 N N   . PRO   A 1 303 ? 13.892 6.013   -8.583  1.00 9.90  ? 293 PRO   A N   1 
ATOM   2274 C CA  . PRO   A 1 303 ? 13.829 5.869   -10.036 1.00 11.57 ? 293 PRO   A CA  1 
ATOM   2275 C C   . PRO   A 1 303 ? 13.270 4.500   -10.446 1.00 13.93 ? 293 PRO   A C   1 
ATOM   2276 O O   . PRO   A 1 303 ? 12.489 4.431   -11.372 1.00 12.96 ? 293 PRO   A O   1 
ATOM   2277 C CB  . PRO   A 1 303 ? 15.288 6.107   -10.454 1.00 11.20 ? 293 PRO   A CB  1 
ATOM   2278 C CG  . PRO   A 1 303 ? 15.711 7.156   -9.473  1.00 10.57 ? 293 PRO   A CG  1 
ATOM   2279 C CD  . PRO   A 1 303 ? 15.153 6.657   -8.154  1.00 10.24 ? 293 PRO   A CD  1 
ATOM   2280 N N   . PHE   A 1 304 ? 13.718 3.452   -9.766  1.00 16.85 ? 294 PHE   A N   1 
ATOM   2281 C CA  . PHE   A 1 304 ? 13.300 2.066   -10.059 1.00 19.18 ? 294 PHE   A CA  1 
ATOM   2282 C C   . PHE   A 1 304 ? 11.809 1.929   -9.745  1.00 16.36 ? 294 PHE   A C   1 
ATOM   2283 O O   . PHE   A 1 304 ? 11.140 1.316   -10.571 1.00 15.01 ? 294 PHE   A O   1 
ATOM   2284 C CB  . PHE   A 1 304 ? 14.194 1.015   -9.394  1.00 23.79 ? 294 PHE   A CB  1 
ATOM   2285 C CG  . PHE   A 1 304 ? 13.733 -0.360  -9.786  1.00 30.98 ? 294 PHE   A CG  1 
ATOM   2286 C CD1 . PHE   A 1 304 ? 14.043 -0.869  -11.039 1.00 35.90 ? 294 PHE   A CD1 1 
ATOM   2287 C CD2 . PHE   A 1 304 ? 12.854 -1.069  -8.981  1.00 33.71 ? 294 PHE   A CD2 1 
ATOM   2288 C CE1 . PHE   A 1 304 ? 13.562 -2.109  -11.431 1.00 39.42 ? 294 PHE   A CE1 1 
ATOM   2289 C CE2 . PHE   A 1 304 ? 12.374 -2.308  -9.377  1.00 38.89 ? 294 PHE   A CE2 1 
ATOM   2290 C CZ  . PHE   A 1 304 ? 12.729 -2.825  -10.599 1.00 39.39 ? 294 PHE   A CZ  1 
ATOM   2291 N N   . ASP   A 1 305 ? 11.290 2.533   -8.663  1.00 15.56 ? 295 ASP   A N   1 
ATOM   2292 C CA  . ASP   A 1 305 ? 9.840  2.504   -8.342  1.00 15.16 ? 295 ASP   A CA  1 
ATOM   2293 C C   . ASP   A 1 305 ? 9.007  3.116   -9.478  1.00 16.49 ? 295 ASP   A C   1 
ATOM   2294 O O   . ASP   A 1 305 ? 7.894  2.581   -9.802  1.00 15.57 ? 295 ASP   A O   1 
ATOM   2295 C CB  . ASP   A 1 305 ? 9.504  3.250   -7.051  1.00 15.52 ? 295 ASP   A CB  1 
ATOM   2296 C CG  . ASP   A 1 305 ? 10.087 2.581   -5.819  1.00 14.61 ? 295 ASP   A CG  1 
ATOM   2297 O OD1 . ASP   A 1 305 ? 10.396 1.363   -5.911  1.00 14.54 ? 295 ASP   A OD1 1 
ATOM   2298 O OD2 . ASP   A 1 305 ? 10.289 3.286   -4.810  1.00 12.52 ? 295 ASP   A OD2 1 
ATOM   2299 N N   . VAL   A 1 306 ? 9.505  4.201   -10.068 1.00 14.71 ? 296 VAL   A N   1 
ATOM   2300 C CA  . VAL   A 1 306 ? 8.761  4.934   -11.109 1.00 13.99 ? 296 VAL   A CA  1 
ATOM   2301 C C   . VAL   A 1 306 ? 8.706  4.042   -12.353 1.00 15.79 ? 296 VAL   A C   1 
ATOM   2302 O O   . VAL   A 1 306 ? 7.595  3.912   -12.888 1.00 16.83 ? 296 VAL   A O   1 
ATOM   2303 C CB  . VAL   A 1 306 ? 9.391  6.302   -11.397 1.00 12.90 ? 296 VAL   A CB  1 
ATOM   2304 C CG1 . VAL   A 1 306 ? 8.720  6.975   -12.582 1.00 12.03 ? 296 VAL   A CG1 1 
ATOM   2305 C CG2 . VAL   A 1 306 ? 9.324  7.186   -10.147 1.00 12.31 ? 296 VAL   A CG2 1 
ATOM   2306 N N   . VAL   A 1 307 ? 9.850  3.516   -12.786 1.00 16.29 ? 297 VAL   A N   1 
ATOM   2307 C CA  . VAL   A 1 307 ? 9.974  2.606   -13.968 1.00 18.69 ? 297 VAL   A CA  1 
ATOM   2308 C C   . VAL   A 1 307 ? 9.106  1.357   -13.729 1.00 20.89 ? 297 VAL   A C   1 
ATOM   2309 O O   . VAL   A 1 307 ? 8.318  1.035   -14.649 1.00 22.51 ? 297 VAL   A O   1 
ATOM   2310 C CB  . VAL   A 1 307 ? 11.442 2.249   -14.259 1.00 20.01 ? 297 VAL   A CB  1 
ATOM   2311 C CG1 . VAL   A 1 307 ? 11.576 1.085   -15.238 1.00 20.53 ? 297 VAL   A CG1 1 
ATOM   2312 C CG2 . VAL   A 1 307 ? 12.231 3.457   -14.742 1.00 18.75 ? 297 VAL   A CG2 1 
ATOM   2313 N N   . ARG   A 1 308 ? 9.233  0.709   -12.557 1.00 21.60 ? 298 ARG   A N   1 
ATOM   2314 C CA  . ARG   A 1 308 ? 8.449  -0.495  -12.173 1.00 25.06 ? 298 ARG   A CA  1 
ATOM   2315 C C   . ARG   A 1 308 ? 6.968  -0.177  -12.373 1.00 22.57 ? 298 ARG   A C   1 
ATOM   2316 O O   . ARG   A 1 308 ? 6.268  -0.911  -13.101 1.00 26.53 ? 298 ARG   A O   1 
ATOM   2317 C CB  . ARG   A 1 308 ? 8.697  -0.928  -10.720 1.00 28.03 ? 298 ARG   A CB  1 
ATOM   2318 C CG  . ARG   A 1 308 ? 7.470  -1.562  -10.071 1.00 31.56 ? 298 ARG   A CG  1 
ATOM   2319 C CD  . ARG   A 1 308 ? 7.706  -2.566  -8.949  1.00 34.49 ? 298 ARG   A CD  1 
ATOM   2320 N NE  . ARG   A 1 308 ? 7.783  -1.997  -7.604  1.00 33.02 ? 298 ARG   A NE  1 
ATOM   2321 C CZ  . ARG   A 1 308 ? 8.887  -1.455  -7.068  1.00 36.36 ? 298 ARG   A CZ  1 
ATOM   2322 N NH1 . ARG   A 1 308 ? 8.875  -0.976  -5.833  1.00 32.33 ? 298 ARG   A NH1 1 
ATOM   2323 N NH2 . ARG   A 1 308 ? 10.010 -1.396  -7.771  1.00 36.98 ? 298 ARG   A NH2 1 
ATOM   2324 N N   . GLN   A 1 309 ? 6.498  0.909   -11.781 1.00 22.05 ? 299 GLN   A N   1 
ATOM   2325 C CA  . GLN   A 1 309 ? 5.053  1.226   -11.775 1.00 22.04 ? 299 GLN   A CA  1 
ATOM   2326 C C   . GLN   A 1 309 ? 4.608  1.611   -13.184 1.00 22.37 ? 299 GLN   A C   1 
ATOM   2327 O O   . GLN   A 1 309 ? 3.485  1.202   -13.573 1.00 21.03 ? 299 GLN   A O   1 
ATOM   2328 C CB  . GLN   A 1 309 ? 4.695  2.312   -10.759 1.00 20.18 ? 299 GLN   A CB  1 
ATOM   2329 C CG  . GLN   A 1 309 ? 3.198  2.535   -10.685 1.00 18.45 ? 299 GLN   A CG  1 
ATOM   2330 C CD  . GLN   A 1 309 ? 2.700  3.337   -9.514  1.00 16.99 ? 299 GLN   A CD  1 
ATOM   2331 O OE1 . GLN   A 1 309 ? 1.580  3.828   -9.533  1.00 15.11 ? 299 GLN   A OE1 1 
ATOM   2332 N NE2 . GLN   A 1 309 ? 3.508  3.470   -8.480  1.00 17.97 ? 299 GLN   A NE2 1 
ATOM   2333 N N   . CYS   A 1 310 ? 5.413  2.394   -13.904 1.00 23.82 ? 300 CYS   A N   1 
ATOM   2334 C CA  . CYS   A 1 310 ? 5.012  2.979   -15.212 1.00 23.33 ? 300 CYS   A CA  1 
ATOM   2335 C C   . CYS   A 1 310 ? 5.169  1.925   -16.340 1.00 24.33 ? 300 CYS   A C   1 
ATOM   2336 O O   . CYS   A 1 310 ? 4.531  2.114   -17.416 1.00 22.48 ? 300 CYS   A O   1 
ATOM   2337 C CB  . CYS   A 1 310 ? 5.739  4.300   -15.471 1.00 22.66 ? 300 CYS   A CB  1 
ATOM   2338 S SG  . CYS   A 1 310 ? 5.243  5.658   -14.357 1.00 23.67 ? 300 CYS   A SG  1 
ATOM   2339 N N   . SER   A 1 311 ? 5.900  0.815   -16.116 1.00 25.15 ? 301 SER   A N   1 
ATOM   2340 C CA  . SER   A 1 311 ? 6.093  -0.289  -17.110 1.00 24.25 ? 301 SER   A CA  1 
ATOM   2341 C C   . SER   A 1 311 ? 5.335  -1.576  -16.717 1.00 25.59 ? 301 SER   A C   1 
ATOM   2342 O O   . SER   A 1 311 ? 5.305  -2.496  -17.553 1.00 25.88 ? 301 SER   A O   1 
ATOM   2343 C CB  . SER   A 1 311 ? 7.560  -0.589  -17.309 1.00 25.40 ? 301 SER   A CB  1 
ATOM   2344 O OG  . SER   A 1 311 ? 8.098  -1.230  -16.163 1.00 24.67 ? 301 SER   A OG  1 
ATOM   2345 N N   . GLY   A 1 312 ? 4.760  -1.672  -15.505 1.00 24.80 ? 302 GLY   A N   1 
ATOM   2346 C CA  . GLY   A 1 312 ? 3.934  -2.823  -15.065 1.00 24.98 ? 302 GLY   A CA  1 
ATOM   2347 C C   . GLY   A 1 312 ? 4.750  -4.100  -14.836 1.00 25.39 ? 302 GLY   A C   1 
ATOM   2348 O O   . GLY   A 1 312 ? 4.252  -5.215  -15.178 1.00 24.91 ? 302 GLY   A O   1 
ATOM   2349 N N   . VAL   A 1 313 ? 5.933  -3.971  -14.228 1.00 25.72 ? 303 VAL   A N   1 
ATOM   2350 C CA  . VAL   A 1 313 ? 6.816  -5.103  -13.798 1.00 25.44 ? 303 VAL   A CA  1 
ATOM   2351 C C   . VAL   A 1 313 ? 6.055  -5.967  -12.776 1.00 26.19 ? 303 VAL   A C   1 
ATOM   2352 O O   . VAL   A 1 313 ? 5.482  -5.367  -11.857 1.00 24.22 ? 303 VAL   A O   1 
ATOM   2353 C CB  . VAL   A 1 313 ? 8.127  -4.573  -13.180 1.00 27.33 ? 303 VAL   A CB  1 
ATOM   2354 C CG1 . VAL   A 1 313 ? 8.952  -5.689  -12.536 1.00 27.44 ? 303 VAL   A CG1 1 
ATOM   2355 C CG2 . VAL   A 1 313 ? 8.959  -3.801  -14.202 1.00 28.14 ? 303 VAL   A CG2 1 
ATOM   2356 N N   . THR   A 1 314 ? 6.104  -7.301  -12.917 1.00 25.59 ? 304 THR   A N   1 
ATOM   2357 C CA  . THR   A 1 314 ? 5.396  -8.300  -12.058 1.00 28.78 ? 304 THR   A CA  1 
ATOM   2358 C C   . THR   A 1 314 ? 6.397  -9.243  -11.362 1.00 32.69 ? 304 THR   A C   1 
ATOM   2359 O O   . THR   A 1 314 ? 7.622  -9.209  -11.703 1.00 31.43 ? 304 THR   A O   1 
ATOM   2360 C CB  . THR   A 1 314 ? 4.356  -9.096  -12.857 1.00 27.98 ? 304 THR   A CB  1 
ATOM   2361 O OG1 . THR   A 1 314 ? 5.046  -9.771  -13.912 1.00 26.75 ? 304 THR   A OG1 1 
ATOM   2362 C CG2 . THR   A 1 314 ? 3.257  -8.232  -13.427 1.00 26.85 ? 304 THR   A CG2 1 
ATOM   2363 N N   . PHE   A 1 315 ? 5.884  -10.045 -10.415 1.00 34.81 ? 305 PHE   A N   1 
ATOM   2364 C CA  . PHE   A 1 315 ? 6.664  -10.854 -9.433  1.00 36.47 ? 305 PHE   A CA  1 
ATOM   2365 C C   . PHE   A 1 315 ? 6.111  -12.292 -9.388  1.00 39.70 ? 305 PHE   A C   1 
ATOM   2366 O O   . PHE   A 1 315 ? 4.975  -12.571 -9.790  1.00 40.44 ? 305 PHE   A O   1 
ATOM   2367 C CB  . PHE   A 1 315 ? 6.683  -10.126 -8.075  1.00 35.07 ? 305 PHE   A CB  1 
ATOM   2368 C CG  . PHE   A 1 315 ? 7.250  -8.734  -8.190  1.00 32.08 ? 305 PHE   A CG  1 
ATOM   2369 C CD1 . PHE   A 1 315 ? 8.601  -8.546  -8.452  1.00 35.53 ? 305 PHE   A CD1 1 
ATOM   2370 C CD2 . PHE   A 1 315 ? 6.422  -7.621  -8.174  1.00 36.01 ? 305 PHE   A CD2 1 
ATOM   2371 C CE1 . PHE   A 1 315 ? 9.123  -7.273  -8.642  1.00 34.00 ? 305 PHE   A CE1 1 
ATOM   2372 C CE2 . PHE   A 1 315 ? 6.941  -6.344  -8.361  1.00 35.33 ? 305 PHE   A CE2 1 
ATOM   2373 C CZ  . PHE   A 1 315 ? 8.287  -6.175  -8.599  1.00 36.71 ? 305 PHE   A CZ  1 
HETATM 2374 C C7  . A1D8T B 2 .   ? 13.834 6.201   22.726  1.00 21.87 ? 401 A1D8T A C7  1 
HETATM 2375 C C4  . A1D8T B 2 .   ? 13.162 7.263   23.544  1.00 22.69 ? 401 A1D8T A C4  1 
HETATM 2376 C C2  . A1D8T B 2 .   ? 12.051 9.384   23.700  1.00 25.84 ? 401 A1D8T A C2  1 
HETATM 2377 C C6  . A1D8T B 2 .   ? 12.374 8.085   25.673  1.00 25.80 ? 401 A1D8T A C6  1 
HETATM 2378 C C8  . A1D8T B 2 .   ? 12.090 4.622   22.794  1.00 16.28 ? 401 A1D8T A C8  1 
HETATM 2379 C C3  . A1D8T B 2 .   ? 12.693 8.411   22.944  1.00 25.56 ? 401 A1D8T A C3  1 
HETATM 2380 C C1  . A1D8T B 2 .   ? 11.896 9.218   25.059  1.00 26.25 ? 401 A1D8T A C1  1 
HETATM 2381 C C5  . A1D8T B 2 .   ? 13.000 7.105   24.918  1.00 25.09 ? 401 A1D8T A C5  1 
HETATM 2382 O O1  . A1D8T B 2 .   ? 12.792 5.467   22.028  1.00 19.08 ? 401 A1D8T A O1  1 
HETATM 2383 O O2  . A1D8T B 2 .   ? 12.429 4.257   23.903  1.00 18.24 ? 401 A1D8T A O2  1 
HETATM 2384 N N1  . A1D8T B 2 .   ? 10.937 4.298   22.200  1.00 13.98 ? 401 A1D8T A N1  1 
HETATM 2385 C C9  . A1D8T B 2 .   ? 10.065 3.326   22.833  1.00 12.40 ? 401 A1D8T A C9  1 
HETATM 2386 C C10 . A1D8T B 2 .   ? 10.100 2.049   21.988  1.00 12.27 ? 401 A1D8T A C10 1 
HETATM 2387 C C11 . A1D8T B 2 .   ? 8.662  3.885   23.138  1.00 12.03 ? 401 A1D8T A C11 1 
HETATM 2388 O O3  . A1D8T B 2 .   ? 9.714  2.014   20.809  1.00 11.38 ? 401 A1D8T A O3  1 
HETATM 2389 C C16 . A1D8T B 2 .   ? 7.933  4.410   21.876  1.00 12.53 ? 401 A1D8T A C16 1 
HETATM 2390 C C17 . A1D8T B 2 .   ? 8.802  5.009   24.180  1.00 12.37 ? 401 A1D8T A C17 1 
HETATM 2391 C C18 . A1D8T B 2 .   ? 7.813  2.779   23.757  1.00 12.41 ? 401 A1D8T A C18 1 
HETATM 2392 N N3  . A1D8T B 2 .   ? 7.230  3.407   21.071  1.00 12.31 ? 401 A1D8T A N3  1 
HETATM 2393 N N2  . A1D8T B 2 .   ? 10.551 0.933   22.593  1.00 12.35 ? 401 A1D8T A N2  1 
HETATM 2394 C C15 . A1D8T B 2 .   ? 11.088 0.860   23.963  1.00 13.47 ? 401 A1D8T A C15 1 
HETATM 2395 C C12 . A1D8T B 2 .   ? 10.550 -0.342  21.866  1.00 12.08 ? 401 A1D8T A C12 1 
HETATM 2396 C C13 . A1D8T B 2 .   ? 11.249 -1.294  22.798  1.00 13.07 ? 401 A1D8T A C13 1 
HETATM 2397 C C14 . A1D8T B 2 .   ? 11.605 -0.557  24.075  1.00 13.47 ? 401 A1D8T A C14 1 
HETATM 2398 C C28 . A1D8T B 2 .   ? 12.704 -1.009  23.124  1.00 14.28 ? 401 A1D8T A C28 1 
HETATM 2399 C C29 . A1D8T B 2 .   ? 13.518 0.097   22.488  1.00 14.10 ? 401 A1D8T A C29 1 
HETATM 2400 C C30 . A1D8T B 2 .   ? 13.571 -2.140  23.627  1.00 14.73 ? 401 A1D8T A C30 1 
HETATM 2401 C C27 . A1D8T B 2 .   ? 9.129  -0.829  21.578  1.00 12.14 ? 401 A1D8T A C27 1 
HETATM 2402 O O5  . A1D8T B 2 .   ? 8.185  -0.589  22.343  1.00 12.14 ? 401 A1D8T A O5  1 
HETATM 2403 C C19 . A1D8T B 2 .   ? 5.894  3.378   20.944  1.00 13.69 ? 401 A1D8T A C19 1 
HETATM 2404 O O4  . A1D8T B 2 .   ? 5.125  4.116   21.586  1.00 14.69 ? 401 A1D8T A O4  1 
HETATM 2405 C C20 . A1D8T B 2 .   ? 5.316  2.305   20.024  1.00 13.10 ? 401 A1D8T A C20 1 
HETATM 2406 N N4  . A1D8T B 2 .   ? 5.662  2.445   18.609  1.00 13.20 ? 401 A1D8T A N4  1 
HETATM 2407 C C21 . A1D8T B 2 .   ? 6.458  1.477   18.146  1.00 13.79 ? 401 A1D8T A C21 1 
HETATM 2408 C C22 . A1D8T B 2 .   ? 6.303  0.286   19.079  1.00 14.10 ? 401 A1D8T A C22 1 
HETATM 2409 C C23 . A1D8T B 2 .   ? 5.869  0.913   20.398  1.00 12.88 ? 401 A1D8T A C23 1 
HETATM 2410 C C24 . A1D8T B 2 .   ? 7.296  -0.823  18.810  1.00 11.60 ? 401 A1D8T A C24 1 
HETATM 2411 C C25 . A1D8T B 2 .   ? 7.655  -1.828  19.912  1.00 10.96 ? 401 A1D8T A C25 1 
HETATM 2412 C C26 . A1D8T B 2 .   ? 7.688  -3.221  19.316  1.00 10.14 ? 401 A1D8T A C26 1 
HETATM 2413 N N5  . A1D8T B 2 .   ? 8.968  -1.474  20.422  1.00 10.56 ? 401 A1D8T A N5  1 
HETATM 2414 O O6  . A1D8T B 2 .   ? 7.071  1.467   17.083  1.00 11.97 ? 401 A1D8T A O6  1 
HETATM 2415 N N6  . A1D8T B 2 .   ? 6.779  -4.111  19.642  1.00 9.98  ? 401 A1D8T A N6  1 
HETATM 2416 O O   . HOH   C 3 .   ? 6.520  10.276  -1.093  1.00 21.49 ? 501 HOH   A O   1 
HETATM 2417 O O   . HOH   C 3 .   ? 18.707 18.859  12.695  1.00 36.43 ? 502 HOH   A O   1 
HETATM 2418 O O   . HOH   C 3 .   ? 5.417  24.537  -18.770 1.00 33.03 ? 503 HOH   A O   1 
HETATM 2419 O O   . HOH   C 3 .   ? 24.514 -5.821  9.016   1.00 20.35 ? 504 HOH   A O   1 
HETATM 2420 O O   . HOH   C 3 .   ? 21.417 21.536  3.665   1.00 29.09 ? 505 HOH   A O   1 
HETATM 2421 O O   . HOH   C 3 .   ? 12.860 30.959  -8.871  1.00 27.37 ? 506 HOH   A O   1 
HETATM 2422 O O   . HOH   C 3 .   ? 24.849 4.749   18.821  1.00 24.44 ? 507 HOH   A O   1 
HETATM 2423 O O   . HOH   C 3 .   ? 26.440 -15.941 24.444  1.00 20.03 ? 508 HOH   A O   1 
HETATM 2424 O O   . HOH   C 3 .   ? 15.326 31.198  -11.522 1.00 37.42 ? 509 HOH   A O   1 
HETATM 2425 O O   . HOH   C 3 .   ? 18.915 26.463  4.780   1.00 30.56 ? 510 HOH   A O   1 
HETATM 2426 O O   . HOH   C 3 .   ? 25.639 -12.870 22.332  1.00 37.80 ? 511 HOH   A O   1 
HETATM 2427 O O   . HOH   C 3 .   ? 26.302 -5.715  17.584  1.00 26.52 ? 512 HOH   A O   1 
HETATM 2428 O O   . HOH   C 3 .   ? 12.461 -32.277 12.774  1.00 47.49 ? 513 HOH   A O   1 
HETATM 2429 O O   . HOH   C 3 .   ? 7.053  -23.044 20.940  1.00 17.84 ? 514 HOH   A O   1 
HETATM 2430 O O   . HOH   C 3 .   ? 16.241 12.078  6.414   1.00 11.50 ? 515 HOH   A O   1 
HETATM 2431 O O   . HOH   C 3 .   ? 23.358 27.042  -0.343  1.00 27.93 ? 516 HOH   A O   1 
HETATM 2432 O O   . HOH   C 3 .   ? 23.001 -7.519  34.607  1.00 23.79 ? 517 HOH   A O   1 
HETATM 2433 O O   . HOH   C 3 .   ? 12.013 31.265  -1.983  1.00 41.79 ? 518 HOH   A O   1 
HETATM 2434 O O   . HOH   C 3 .   ? 16.933 28.208  -20.888 1.00 26.52 ? 519 HOH   A O   1 
HETATM 2435 O O   . HOH   C 3 .   ? 8.278  -28.284 6.430   1.00 25.37 ? 520 HOH   A O   1 
HETATM 2436 O O   . HOH   C 3 .   ? 27.377 -10.214 24.078  1.00 28.20 ? 521 HOH   A O   1 
HETATM 2437 O O   . HOH   C 3 .   ? 6.468  5.870   1.282   1.00 13.84 ? 522 HOH   A O   1 
HETATM 2438 O O   . HOH   C 3 .   ? 17.100 -5.425  33.534  1.00 34.15 ? 523 HOH   A O   1 
HETATM 2439 O O   . HOH   C 3 .   ? 7.885  -31.070 17.290  1.00 36.17 ? 524 HOH   A O   1 
HETATM 2440 O O   . HOH   C 3 .   ? 14.051 -10.970 31.220  1.00 19.18 ? 525 HOH   A O   1 
HETATM 2441 O O   . HOH   C 3 .   ? 8.163  0.407   27.086  1.00 25.76 ? 526 HOH   A O   1 
HETATM 2442 O O   . HOH   C 3 .   ? 9.220  -23.394 23.087  1.00 26.99 ? 527 HOH   A O   1 
HETATM 2443 O O   . HOH   C 3 .   ? 9.884  6.574   5.258   1.00 9.43  ? 528 HOH   A O   1 
HETATM 2444 O O   . HOH   C 3 .   ? 29.842 5.766   -10.465 1.00 31.83 ? 529 HOH   A O   1 
HETATM 2445 O O   . HOH   C 3 .   ? 21.561 -0.576  28.537  1.00 34.96 ? 530 HOH   A O   1 
HETATM 2446 O O   . HOH   C 3 .   ? 15.181 -9.623  -4.243  1.00 23.15 ? 531 HOH   A O   1 
HETATM 2447 O O   . HOH   C 3 .   ? 18.139 -28.899 20.932  1.00 25.39 ? 532 HOH   A O   1 
HETATM 2448 O O   . HOH   C 3 .   ? 12.051 -26.910 23.117  1.00 18.68 ? 533 HOH   A O   1 
HETATM 2449 O O   . HOH   C 3 .   ? 8.614  -26.752 14.651  1.00 36.18 ? 534 HOH   A O   1 
HETATM 2450 O O   . HOH   C 3 .   ? 24.479 -0.353  12.709  1.00 19.34 ? 535 HOH   A O   1 
HETATM 2451 O O   . HOH   C 3 .   ? 15.174 15.044  16.544  1.00 32.16 ? 536 HOH   A O   1 
HETATM 2452 O O   . HOH   C 3 .   ? 3.437  4.359   -18.019 1.00 32.90 ? 537 HOH   A O   1 
HETATM 2453 O O   . HOH   C 3 .   ? 20.867 8.742   24.053  1.00 32.59 ? 538 HOH   A O   1 
HETATM 2454 O O   . HOH   C 3 .   ? 24.224 13.031  -2.146  1.00 23.38 ? 539 HOH   A O   1 
HETATM 2455 O O   . HOH   C 3 .   ? 11.637 21.933  -17.318 1.00 29.69 ? 540 HOH   A O   1 
HETATM 2456 O O   . HOH   C 3 .   ? 0.165  -17.503 15.761  1.00 35.61 ? 541 HOH   A O   1 
HETATM 2457 O O   . HOH   C 3 .   ? -1.988 19.366  -11.701 1.00 19.99 ? 542 HOH   A O   1 
HETATM 2458 O O   . HOH   C 3 .   ? -1.643 -15.167 2.752   1.00 29.34 ? 543 HOH   A O   1 
HETATM 2459 O O   . HOH   C 3 .   ? 26.817 -9.454  30.280  1.00 45.61 ? 544 HOH   A O   1 
HETATM 2460 O O   . HOH   C 3 .   ? -0.845 16.552  -20.224 1.00 25.18 ? 545 HOH   A O   1 
HETATM 2461 O O   . HOH   C 3 .   ? 22.356 9.550   4.915   1.00 27.06 ? 546 HOH   A O   1 
HETATM 2462 O O   . HOH   C 3 .   ? 21.731 28.664  -7.649  1.00 31.73 ? 547 HOH   A O   1 
HETATM 2463 O O   . HOH   C 3 .   ? 10.841 16.022  7.702   1.00 36.92 ? 548 HOH   A O   1 
HETATM 2464 O O   . HOH   C 3 .   ? 8.178  14.272  -22.311 1.00 29.43 ? 549 HOH   A O   1 
HETATM 2465 O O   . HOH   C 3 .   ? 29.516 18.759  -8.889  1.00 38.64 ? 550 HOH   A O   1 
HETATM 2466 O O   . HOH   C 3 .   ? 25.729 28.140  -9.739  1.00 18.87 ? 551 HOH   A O   1 
HETATM 2467 O O   . HOH   C 3 .   ? 6.156  -8.464  8.571   1.00 12.88 ? 552 HOH   A O   1 
HETATM 2468 O O   . HOH   C 3 .   ? -0.013 -15.098 10.224  1.00 25.91 ? 553 HOH   A O   1 
HETATM 2469 O O   . HOH   C 3 .   ? 6.784  -4.632  -17.864 1.00 44.84 ? 554 HOH   A O   1 
HETATM 2470 O O   . HOH   C 3 .   ? -1.663 -13.511 6.090   1.00 32.80 ? 555 HOH   A O   1 
HETATM 2471 O O   . HOH   C 3 .   ? 27.097 -11.883 7.393   1.00 31.71 ? 556 HOH   A O   1 
HETATM 2472 O O   . HOH   C 3 .   ? -2.252 16.840  -9.536  1.00 18.71 ? 557 HOH   A O   1 
HETATM 2473 O O   . HOH   C 3 .   ? -6.669 6.643   -4.638  1.00 20.80 ? 558 HOH   A O   1 
HETATM 2474 O O   . HOH   C 3 .   ? 15.570 -27.885 12.315  1.00 26.02 ? 559 HOH   A O   1 
HETATM 2475 O O   . HOH   C 3 .   ? 12.658 21.627  2.442   1.00 25.43 ? 560 HOH   A O   1 
HETATM 2476 O O   . HOH   C 3 .   ? 11.084 -12.251 30.611  1.00 27.56 ? 561 HOH   A O   1 
HETATM 2477 O O   . HOH   C 3 .   ? 24.300 -8.834  20.509  1.00 14.10 ? 562 HOH   A O   1 
HETATM 2478 O O   . HOH   C 3 .   ? 22.410 -2.613  -0.285  1.00 29.77 ? 563 HOH   A O   1 
HETATM 2479 O O   . HOH   C 3 .   ? 19.974 5.097   -2.155  1.00 18.27 ? 564 HOH   A O   1 
HETATM 2480 O O   . HOH   C 3 .   ? 6.672  9.144   19.010  1.00 17.47 ? 565 HOH   A O   1 
HETATM 2481 O O   . HOH   C 3 .   ? 19.509 12.422  -3.987  1.00 13.38 ? 566 HOH   A O   1 
HETATM 2482 O O   . HOH   C 3 .   ? 13.339 12.254  17.153  1.00 24.55 ? 567 HOH   A O   1 
HETATM 2483 O O   . HOH   C 3 .   ? 10.638 -23.515 0.458   1.00 22.81 ? 568 HOH   A O   1 
HETATM 2484 O O   . HOH   C 3 .   ? 9.789  -17.578 -3.920  1.00 25.47 ? 569 HOH   A O   1 
HETATM 2485 O O   . HOH   C 3 .   ? 3.703  -8.366  25.019  1.00 29.40 ? 570 HOH   A O   1 
HETATM 2486 O O   . HOH   C 3 .   ? 1.842  -19.685 7.476   1.00 41.01 ? 571 HOH   A O   1 
HETATM 2487 O O   . HOH   C 3 .   ? 0.192  23.214  -3.470  1.00 40.16 ? 572 HOH   A O   1 
HETATM 2488 O O   . HOH   C 3 .   ? 1.086  25.570  -2.853  1.00 35.29 ? 573 HOH   A O   1 
HETATM 2489 O O   . HOH   C 3 .   ? 0.366  -1.063  12.188  1.00 16.17 ? 574 HOH   A O   1 
HETATM 2490 O O   . HOH   C 3 .   ? 2.248  -19.481 21.976  1.00 27.30 ? 575 HOH   A O   1 
HETATM 2491 O O   . HOH   C 3 .   ? 23.779 -15.166 27.841  1.00 19.53 ? 576 HOH   A O   1 
HETATM 2492 O O   . HOH   C 3 .   ? 13.505 -24.572 3.822   1.00 19.79 ? 577 HOH   A O   1 
HETATM 2493 O O   . HOH   C 3 .   ? 25.511 16.105  -14.504 1.00 22.41 ? 578 HOH   A O   1 
HETATM 2494 O O   . HOH   C 3 .   ? -1.370 -3.135  19.620  1.00 25.15 ? 579 HOH   A O   1 
HETATM 2495 O O   . HOH   C 3 .   ? 28.512 8.487   -12.367 1.00 20.99 ? 580 HOH   A O   1 
HETATM 2496 O O   . HOH   C 3 .   ? 8.609  -4.391  34.251  1.00 36.65 ? 581 HOH   A O   1 
HETATM 2497 O O   . HOH   C 3 .   ? 18.999 10.340  12.819  1.00 19.60 ? 582 HOH   A O   1 
HETATM 2498 O O   . HOH   C 3 .   ? 25.862 9.659   -5.288  1.00 23.55 ? 583 HOH   A O   1 
HETATM 2499 O O   . HOH   C 3 .   ? 2.497  -9.034  18.589  1.00 13.16 ? 584 HOH   A O   1 
HETATM 2500 O O   . HOH   C 3 .   ? 3.391  4.005   23.610  1.00 32.39 ? 585 HOH   A O   1 
HETATM 2501 O O   . HOH   C 3 .   ? 15.028 26.169  4.152   1.00 23.26 ? 586 HOH   A O   1 
HETATM 2502 O O   . HOH   C 3 .   ? 11.711 -6.615  35.609  1.00 34.11 ? 587 HOH   A O   1 
HETATM 2503 O O   . HOH   C 3 .   ? 21.293 -13.315 34.469  1.00 28.77 ? 588 HOH   A O   1 
HETATM 2504 O O   . HOH   C 3 .   ? 18.433 3.481   -13.751 1.00 33.54 ? 589 HOH   A O   1 
HETATM 2505 O O   . HOH   C 3 .   ? 13.543 21.143  -21.050 1.00 30.25 ? 590 HOH   A O   1 
HETATM 2506 O O   . HOH   C 3 .   ? 27.551 16.878  -7.518  1.00 18.32 ? 591 HOH   A O   1 
HETATM 2507 O O   . HOH   C 3 .   ? -0.577 1.748   13.432  1.00 17.97 ? 592 HOH   A O   1 
HETATM 2508 O O   . HOH   C 3 .   ? 8.184  24.256  -2.577  1.00 31.05 ? 593 HOH   A O   1 
HETATM 2509 O O   . HOH   C 3 .   ? 4.495  7.827   9.564   1.00 31.53 ? 594 HOH   A O   1 
HETATM 2510 O O   . HOH   C 3 .   ? 22.815 19.550  0.242   1.00 32.72 ? 595 HOH   A O   1 
HETATM 2511 O O   . HOH   C 3 .   ? 20.268 11.047  -17.090 1.00 18.52 ? 596 HOH   A O   1 
HETATM 2512 O O   . HOH   C 3 .   ? 9.242  28.061  -1.402  1.00 28.61 ? 597 HOH   A O   1 
HETATM 2513 O O   . HOH   C 3 .   ? 16.983 6.617   -4.381  1.00 11.71 ? 598 HOH   A O   1 
HETATM 2514 O O   . HOH   C 3 .   ? 8.656  -17.757 28.657  1.00 32.29 ? 599 HOH   A O   1 
HETATM 2515 O O   . HOH   C 3 .   ? 26.844 -10.809 12.326  1.00 27.41 ? 600 HOH   A O   1 
HETATM 2516 O O   . HOH   C 3 .   ? 8.935  24.750  -12.028 1.00 23.59 ? 601 HOH   A O   1 
HETATM 2517 O O   . HOH   C 3 .   ? 10.491 -0.764  -3.190  1.00 18.84 ? 602 HOH   A O   1 
HETATM 2518 O O   . HOH   C 3 .   ? 20.228 10.368  15.377  1.00 18.08 ? 603 HOH   A O   1 
HETATM 2519 O O   . HOH   C 3 .   ? 4.001  -10.180 -16.367 1.00 38.59 ? 604 HOH   A O   1 
HETATM 2520 O O   . HOH   C 3 .   ? 20.534 -18.408 26.743  1.00 15.44 ? 605 HOH   A O   1 
HETATM 2521 O O   . HOH   C 3 .   ? 17.947 27.771  -13.627 1.00 16.87 ? 606 HOH   A O   1 
HETATM 2522 O O   . HOH   C 3 .   ? 21.012 18.797  2.790   1.00 33.60 ? 607 HOH   A O   1 
HETATM 2523 O O   . HOH   C 3 .   ? 13.635 23.260  -19.219 1.00 31.46 ? 608 HOH   A O   1 
HETATM 2524 O O   . HOH   C 3 .   ? 16.830 -18.897 7.742   1.00 14.69 ? 609 HOH   A O   1 
HETATM 2525 O O   . HOH   C 3 .   ? 6.821  -6.052  31.905  1.00 41.40 ? 610 HOH   A O   1 
HETATM 2526 O O   . HOH   C 3 .   ? 22.769 1.354   4.976   1.00 33.95 ? 611 HOH   A O   1 
HETATM 2527 O O   . HOH   C 3 .   ? 7.674  -26.476 0.449   1.00 45.78 ? 612 HOH   A O   1 
HETATM 2528 O O   . HOH   C 3 .   ? 22.541 -0.472  18.139  1.00 12.03 ? 613 HOH   A O   1 
HETATM 2529 O O   . HOH   C 3 .   ? 27.784 26.026  -11.940 1.00 29.22 ? 614 HOH   A O   1 
HETATM 2530 O O   . HOH   C 3 .   ? 14.534 12.358  22.120  1.00 27.33 ? 615 HOH   A O   1 
HETATM 2531 O O   . HOH   C 3 .   ? 4.496  27.175  -8.633  1.00 31.67 ? 616 HOH   A O   1 
HETATM 2532 O O   . HOH   C 3 .   ? 21.734 21.788  -19.180 1.00 11.73 ? 617 HOH   A O   1 
HETATM 2533 O O   . HOH   C 3 .   ? 20.728 -13.076 10.744  1.00 18.69 ? 618 HOH   A O   1 
HETATM 2534 O O   . HOH   C 3 .   ? 15.086 -4.993  0.224   1.00 15.89 ? 619 HOH   A O   1 
HETATM 2535 O O   . HOH   C 3 .   ? 2.325  -17.454 8.677   1.00 29.32 ? 620 HOH   A O   1 
HETATM 2536 O O   . HOH   C 3 .   ? 20.474 -17.900 10.034  1.00 27.44 ? 621 HOH   A O   1 
HETATM 2537 O O   . HOH   C 3 .   ? 3.021  5.376   20.403  1.00 22.16 ? 622 HOH   A O   1 
HETATM 2538 O O   . HOH   C 3 .   ? 14.119 18.498  3.849   1.00 23.99 ? 623 HOH   A O   1 
HETATM 2539 O O   . HOH   C 3 .   ? 14.357 14.923  12.582  1.00 27.86 ? 624 HOH   A O   1 
HETATM 2540 O O   . HOH   C 3 .   ? 10.194 7.829   -25.372 1.00 33.31 ? 625 HOH   A O   1 
HETATM 2541 O O   . HOH   C 3 .   ? 17.964 4.077   32.103  1.00 26.15 ? 626 HOH   A O   1 
HETATM 2542 O O   . HOH   C 3 .   ? -3.226 -22.531 12.112  1.00 35.79 ? 627 HOH   A O   1 
HETATM 2543 O O   . HOH   C 3 .   ? 14.238 15.937  -26.150 1.00 31.44 ? 628 HOH   A O   1 
HETATM 2544 O O   . HOH   C 3 .   ? 14.376 0.068   -3.117  1.00 17.28 ? 629 HOH   A O   1 
HETATM 2545 O O   . HOH   C 3 .   ? 23.963 22.791  -17.632 1.00 14.80 ? 630 HOH   A O   1 
HETATM 2546 O O   . HOH   C 3 .   ? 21.691 -20.606 31.701  1.00 27.91 ? 631 HOH   A O   1 
HETATM 2547 O O   . HOH   C 3 .   ? 15.559 6.280   -14.169 1.00 19.91 ? 632 HOH   A O   1 
HETATM 2548 O O   . HOH   C 3 .   ? 0.705  -16.263 2.308   1.00 32.68 ? 633 HOH   A O   1 
HETATM 2549 O O   . HOH   C 3 .   ? 9.752  10.385  -4.943  1.00 7.02  ? 634 HOH   A O   1 
HETATM 2550 O O   . HOH   C 3 .   ? 3.510  28.780  -3.634  1.00 26.38 ? 635 HOH   A O   1 
HETATM 2551 O O   . HOH   C 3 .   ? 6.193  2.019   -7.711  1.00 21.96 ? 636 HOH   A O   1 
HETATM 2552 O O   . HOH   C 3 .   ? 16.600 2.616   12.049  1.00 9.90  ? 637 HOH   A O   1 
HETATM 2553 O O   . HOH   C 3 .   ? 10.270 19.728  -0.606  1.00 13.49 ? 638 HOH   A O   1 
HETATM 2554 O O   . HOH   C 3 .   ? 9.884  -11.103 28.414  1.00 22.10 ? 639 HOH   A O   1 
HETATM 2555 O O   . HOH   C 3 .   ? 7.947  -1.161  25.032  1.00 23.36 ? 640 HOH   A O   1 
HETATM 2556 O O   . HOH   C 3 .   ? 11.580 -29.612 8.427   1.00 24.33 ? 641 HOH   A O   1 
HETATM 2557 O O   . HOH   C 3 .   ? 15.469 -5.344  20.256  1.00 10.53 ? 642 HOH   A O   1 
HETATM 2558 O O   . HOH   C 3 .   ? 23.174 1.672   15.899  1.00 13.56 ? 643 HOH   A O   1 
HETATM 2559 O O   . HOH   C 3 .   ? 3.797  25.285  -2.213  1.00 22.17 ? 644 HOH   A O   1 
HETATM 2560 O O   . HOH   C 3 .   ? 5.182  -17.790 2.070   1.00 19.33 ? 645 HOH   A O   1 
HETATM 2561 O O   . HOH   C 3 .   ? 9.126  16.124  0.934   1.00 47.51 ? 646 HOH   A O   1 
HETATM 2562 O O   . HOH   C 3 .   ? 3.800  -17.387 20.960  1.00 22.40 ? 647 HOH   A O   1 
HETATM 2563 O O   . HOH   C 3 .   ? 0.008  19.954  -15.600 1.00 27.99 ? 648 HOH   A O   1 
HETATM 2564 O O   . HOH   C 3 .   ? 20.005 -20.112 16.561  1.00 21.14 ? 649 HOH   A O   1 
HETATM 2565 O O   . HOH   C 3 .   ? 20.782 6.787   19.321  1.00 37.07 ? 650 HOH   A O   1 
HETATM 2566 O O   . HOH   C 3 .   ? 6.301  -1.752  -4.538  1.00 22.96 ? 651 HOH   A O   1 
HETATM 2567 O O   . HOH   C 3 .   ? 22.386 -20.060 23.342  1.00 23.85 ? 652 HOH   A O   1 
HETATM 2568 O O   . HOH   C 3 .   ? -2.429 9.327   -10.239 1.00 24.72 ? 653 HOH   A O   1 
HETATM 2569 O O   . HOH   C 3 .   ? 11.550 9.942   -25.485 1.00 36.72 ? 654 HOH   A O   1 
HETATM 2570 O O   . HOH   C 3 .   ? 10.873 -24.924 2.821   1.00 17.11 ? 655 HOH   A O   1 
HETATM 2571 O O   . HOH   C 3 .   ? 15.522 27.189  -12.506 1.00 22.39 ? 656 HOH   A O   1 
HETATM 2572 O O   . HOH   C 3 .   ? 14.729 -25.886 26.993  1.00 13.34 ? 657 HOH   A O   1 
HETATM 2573 O O   . HOH   C 3 .   ? 21.576 -1.646  20.403  1.00 14.58 ? 658 HOH   A O   1 
HETATM 2574 O O   . HOH   C 3 .   ? 15.447 -21.598 31.791  1.00 32.14 ? 659 HOH   A O   1 
HETATM 2575 O O   . HOH   C 3 .   ? 29.085 14.177  -9.792  1.00 25.09 ? 660 HOH   A O   1 
HETATM 2576 O O   . HOH   C 3 .   ? 12.919 11.310  10.451  1.00 22.16 ? 661 HOH   A O   1 
HETATM 2577 O O   . HOH   C 3 .   ? 10.369 24.970  -0.658  1.00 24.65 ? 662 HOH   A O   1 
HETATM 2578 O O   . HOH   C 3 .   ? 23.355 2.965   9.451   1.00 17.01 ? 663 HOH   A O   1 
HETATM 2579 O O   . HOH   C 3 .   ? 15.821 18.307  -22.114 1.00 17.31 ? 664 HOH   A O   1 
HETATM 2580 O O   . HOH   C 3 .   ? 16.030 -27.809 23.871  1.00 14.11 ? 665 HOH   A O   1 
HETATM 2581 O O   . HOH   C 3 .   ? 15.825 -12.875 31.921  1.00 21.44 ? 666 HOH   A O   1 
HETATM 2582 O O   . HOH   C 3 .   ? 7.905  3.604   -3.346  1.00 9.35  ? 667 HOH   A O   1 
HETATM 2583 O O   . HOH   C 3 .   ? -1.226 4.412   -19.239 1.00 24.27 ? 668 HOH   A O   1 
HETATM 2584 O O   . HOH   C 3 .   ? -3.256 28.353  -8.257  1.00 19.80 ? 669 HOH   A O   1 
HETATM 2585 O O   . HOH   C 3 .   ? 13.481 0.868   -5.408  1.00 17.23 ? 670 HOH   A O   1 
HETATM 2586 O O   . HOH   C 3 .   ? 16.932 13.174  -22.366 1.00 25.02 ? 671 HOH   A O   1 
HETATM 2587 O O   . HOH   C 3 .   ? 31.030 24.810  -10.793 1.00 25.79 ? 672 HOH   A O   1 
HETATM 2588 O O   . HOH   C 3 .   ? 7.668  -24.469 25.918  1.00 19.30 ? 673 HOH   A O   1 
HETATM 2589 O O   . HOH   C 3 .   ? -2.956 -8.319  21.207  1.00 33.74 ? 674 HOH   A O   1 
HETATM 2590 O O   . HOH   C 3 .   ? 22.232 -10.235 -0.157  1.00 38.34 ? 675 HOH   A O   1 
HETATM 2591 O O   . HOH   C 3 .   ? 27.209 23.346  -5.136  1.00 16.09 ? 676 HOH   A O   1 
HETATM 2592 O O   . HOH   C 3 .   ? 20.581 13.811  9.258   1.00 26.08 ? 677 HOH   A O   1 
HETATM 2593 O O   . HOH   C 3 .   ? 24.583 -7.773  26.195  1.00 22.59 ? 678 HOH   A O   1 
HETATM 2594 O O   . HOH   C 3 .   ? -3.869 -12.056 2.561   1.00 18.31 ? 679 HOH   A O   1 
HETATM 2595 O O   . HOH   C 3 .   ? 26.139 -10.578 18.260  1.00 17.57 ? 680 HOH   A O   1 
HETATM 2596 O O   . HOH   C 3 .   ? 21.212 -13.363 2.192   1.00 20.93 ? 681 HOH   A O   1 
HETATM 2597 O O   . HOH   C 3 .   ? 20.535 -26.410 18.501  1.00 26.50 ? 682 HOH   A O   1 
HETATM 2598 O O   . HOH   C 3 .   ? 15.767 1.362   -6.455  1.00 31.18 ? 683 HOH   A O   1 
HETATM 2599 O O   . HOH   C 3 .   ? 23.857 -15.976 21.781  1.00 11.06 ? 684 HOH   A O   1 
HETATM 2600 O O   . HOH   C 3 .   ? 19.458 -6.337  32.430  1.00 15.97 ? 685 HOH   A O   1 
HETATM 2601 O O   . HOH   C 3 .   ? 27.506 -7.665  11.834  1.00 24.96 ? 686 HOH   A O   1 
HETATM 2602 O O   . HOH   C 3 .   ? -0.062 3.988   -14.562 1.00 31.06 ? 687 HOH   A O   1 
HETATM 2603 O O   . HOH   C 3 .   ? 22.975 -2.141  15.989  1.00 12.04 ? 688 HOH   A O   1 
HETATM 2604 O O   . HOH   C 3 .   ? 19.169 -7.696  6.033   1.00 13.46 ? 689 HOH   A O   1 
HETATM 2605 O O   . HOH   C 3 .   ? 20.327 -0.526  -1.140  1.00 25.06 ? 690 HOH   A O   1 
HETATM 2606 O O   . HOH   C 3 .   ? 7.720  12.224  0.548   1.00 29.52 ? 691 HOH   A O   1 
HETATM 2607 O O   . HOH   C 3 .   ? 29.615 14.928  -14.307 1.00 22.95 ? 692 HOH   A O   1 
HETATM 2608 O O   . HOH   C 3 .   ? 2.070  11.845  -5.765  1.00 17.23 ? 693 HOH   A O   1 
HETATM 2609 O O   . HOH   C 3 .   ? 27.759 20.984  -5.623  1.00 25.18 ? 694 HOH   A O   1 
HETATM 2610 O O   . HOH   C 3 .   ? 14.769 -20.107 -0.013  1.00 33.64 ? 695 HOH   A O   1 
HETATM 2611 O O   . HOH   C 3 .   ? 15.148 -8.645  35.163  1.00 35.51 ? 696 HOH   A O   1 
HETATM 2612 O O   . HOH   C 3 .   ? 5.271  -2.911  -6.469  1.00 19.72 ? 697 HOH   A O   1 
HETATM 2613 O O   . HOH   C 3 .   ? 7.591  19.886  -0.562  1.00 12.87 ? 698 HOH   A O   1 
HETATM 2614 O O   . HOH   C 3 .   ? -1.894 10.509  -8.217  1.00 35.72 ? 699 HOH   A O   1 
HETATM 2615 O O   . HOH   C 3 .   ? 3.948  -22.109 7.201   1.00 17.79 ? 700 HOH   A O   1 
HETATM 2616 O O   . HOH   C 3 .   ? 3.380  11.062  -21.470 1.00 33.14 ? 701 HOH   A O   1 
HETATM 2617 O O   . HOH   C 3 .   ? 23.462 -6.172  1.748   1.00 14.60 ? 702 HOH   A O   1 
HETATM 2618 O O   . HOH   C 3 .   ? 4.560  -13.984 -7.257  1.00 37.18 ? 703 HOH   A O   1 
HETATM 2619 O O   . HOH   C 3 .   ? 21.177 -1.682  26.417  1.00 37.18 ? 704 HOH   A O   1 
HETATM 2620 O O   . HOH   C 3 .   ? 0.700  1.531   20.691  1.00 20.38 ? 705 HOH   A O   1 
HETATM 2621 O O   . HOH   C 3 .   ? 18.185 -16.264 -2.930  1.00 29.94 ? 706 HOH   A O   1 
HETATM 2622 O O   . HOH   C 3 .   ? 16.193 3.292   -8.192  1.00 15.75 ? 707 HOH   A O   1 
HETATM 2623 O O   . HOH   C 3 .   ? 24.940 2.095   12.113  1.00 31.89 ? 708 HOH   A O   1 
HETATM 2624 O O   . HOH   C 3 .   ? 16.056 4.949   30.751  1.00 29.52 ? 709 HOH   A O   1 
HETATM 2625 O O   . HOH   C 3 .   ? 1.214  -16.689 12.781  1.00 23.41 ? 710 HOH   A O   1 
HETATM 2626 O O   . HOH   C 3 .   ? 11.425 -22.210 32.893  1.00 27.86 ? 711 HOH   A O   1 
HETATM 2627 O O   . HOH   C 3 .   ? 19.086 11.608  -21.186 1.00 27.03 ? 712 HOH   A O   1 
HETATM 2628 O O   . HOH   C 3 .   ? 14.797 17.958  10.390  1.00 30.41 ? 713 HOH   A O   1 
HETATM 2629 O O   . HOH   C 3 .   ? -2.586 18.677  -20.984 1.00 25.15 ? 714 HOH   A O   1 
HETATM 2630 O O   . HOH   C 3 .   ? 25.052 5.469   -10.996 1.00 25.80 ? 715 HOH   A O   1 
HETATM 2631 O O   . HOH   C 3 .   ? 11.681 32.645  -12.019 1.00 37.96 ? 716 HOH   A O   1 
HETATM 2632 O O   . HOH   C 3 .   ? 20.763 -1.579  23.891  1.00 20.36 ? 717 HOH   A O   1 
HETATM 2633 O O   . HOH   C 3 .   ? 4.305  22.140  -19.864 1.00 34.86 ? 718 HOH   A O   1 
HETATM 2634 O O   . HOH   C 3 .   ? 5.434  -3.107  22.088  1.00 17.34 ? 719 HOH   A O   1 
HETATM 2635 O O   . HOH   C 3 .   ? 23.798 -4.039  23.661  1.00 30.72 ? 720 HOH   A O   1 
HETATM 2636 O O   . HOH   C 3 .   ? 18.190 -23.963 26.000  1.00 14.51 ? 721 HOH   A O   1 
HETATM 2637 O O   . HOH   C 3 .   ? -5.196 24.321  -7.733  1.00 20.75 ? 722 HOH   A O   1 
HETATM 2638 O O   . HOH   C 3 .   ? 9.886  -25.878 22.297  1.00 16.36 ? 723 HOH   A O   1 
HETATM 2639 O O   . HOH   C 3 .   ? 10.573 -16.859 30.380  1.00 26.36 ? 724 HOH   A O   1 
HETATM 2640 O O   . HOH   C 3 .   ? 26.527 20.387  -14.296 1.00 18.55 ? 725 HOH   A O   1 
HETATM 2641 O O   . HOH   C 3 .   ? 1.641  14.393  0.637   1.00 33.51 ? 726 HOH   A O   1 
HETATM 2642 O O   . HOH   C 3 .   ? 11.905 15.714  4.081   1.00 36.67 ? 727 HOH   A O   1 
HETATM 2643 O O   . HOH   C 3 .   ? -2.364 21.945  -10.274 1.00 23.75 ? 728 HOH   A O   1 
HETATM 2644 O O   . HOH   C 3 .   ? -3.578 -12.715 15.949  1.00 39.33 ? 729 HOH   A O   1 
HETATM 2645 O O   . HOH   C 3 .   ? 28.265 21.787  -11.983 1.00 21.06 ? 730 HOH   A O   1 
HETATM 2646 O O   . HOH   C 3 .   ? 7.893  -4.728  22.575  1.00 21.79 ? 731 HOH   A O   1 
HETATM 2647 O O   . HOH   C 3 .   ? 10.819 18.304  1.076   1.00 21.47 ? 732 HOH   A O   1 
HETATM 2648 O O   . HOH   C 3 .   ? 20.147 13.668  -18.268 1.00 22.74 ? 733 HOH   A O   1 
HETATM 2649 O O   . HOH   C 3 .   ? 5.588  2.736   -4.879  1.00 13.91 ? 734 HOH   A O   1 
HETATM 2650 O O   . HOH   C 3 .   ? -0.531 -15.840 14.281  1.00 26.78 ? 735 HOH   A O   1 
HETATM 2651 O O   . HOH   C 3 .   ? 11.587 -29.822 22.728  1.00 17.85 ? 736 HOH   A O   1 
HETATM 2652 O O   . HOH   C 3 .   ? 17.920 5.004   -6.442  1.00 24.68 ? 737 HOH   A O   1 
HETATM 2653 O O   . HOH   C 3 .   ? 1.769  5.776   -15.571 1.00 28.38 ? 738 HOH   A O   1 
HETATM 2654 O O   . HOH   C 3 .   ? 20.065 -21.456 27.507  1.00 22.51 ? 739 HOH   A O   1 
HETATM 2655 O O   . HOH   C 3 .   ? 21.937 12.841  2.030   1.00 33.47 ? 740 HOH   A O   1 
HETATM 2656 O O   . HOH   C 3 .   ? 20.383 6.961   30.077  1.00 38.13 ? 741 HOH   A O   1 
HETATM 2657 O O   . HOH   C 3 .   ? 21.308 16.491  -17.718 1.00 15.57 ? 742 HOH   A O   1 
HETATM 2658 O O   . HOH   C 3 .   ? 20.109 -25.514 22.503  1.00 21.65 ? 743 HOH   A O   1 
HETATM 2659 O O   . HOH   C 3 .   ? 5.555  12.840  17.164  1.00 30.93 ? 744 HOH   A O   1 
HETATM 2660 O O   . HOH   C 3 .   ? 22.685 9.490   -2.097  1.00 29.41 ? 745 HOH   A O   1 
HETATM 2661 O O   . HOH   C 3 .   ? 28.763 10.619  -8.657  1.00 23.05 ? 746 HOH   A O   1 
HETATM 2662 O O   . HOH   C 3 .   ? 20.516 13.227  6.530   1.00 25.63 ? 747 HOH   A O   1 
HETATM 2663 O O   . HOH   C 3 .   ? -0.463 7.683   -3.618  1.00 22.95 ? 748 HOH   A O   1 
HETATM 2664 O O   . HOH   C 3 .   ? 5.305  20.497  -22.082 0.50 20.44 ? 749 HOH   A O   1 
HETATM 2665 O O   . HOH   C 3 .   ? 25.082 13.662  -17.660 1.00 14.16 ? 750 HOH   A O   1 
HETATM 2666 O O   . HOH   C 3 .   ? 23.189 -5.257  26.441  1.00 18.33 ? 751 HOH   A O   1 
HETATM 2667 O O   . HOH   C 3 .   ? -1.899 13.759  -11.765 1.00 30.92 ? 752 HOH   A O   1 
HETATM 2668 O O   . HOH   C 3 .   ? 24.438 1.873   7.189   1.00 37.64 ? 753 HOH   A O   1 
HETATM 2669 O O   . HOH   C 3 .   ? 2.255  -1.228  -12.127 1.00 26.55 ? 754 HOH   A O   1 
HETATM 2670 O O   . HOH   C 3 .   ? 21.092 -4.014  33.522  1.00 28.41 ? 755 HOH   A O   1 
HETATM 2671 O O   . HOH   C 3 .   ? 6.909  26.207  -15.103 1.00 34.34 ? 756 HOH   A O   1 
HETATM 2672 O O   . HOH   C 3 .   ? 6.900  -18.072 27.213  1.00 37.15 ? 757 HOH   A O   1 
HETATM 2673 O O   . HOH   C 3 .   ? 19.710 -17.066 6.112   1.00 39.31 ? 758 HOH   A O   1 
HETATM 2674 O O   . HOH   C 3 .   ? -5.464 16.295  -5.099  1.00 32.38 ? 759 HOH   A O   1 
HETATM 2675 O O   . HOH   C 3 .   ? 19.294 9.256   -20.986 1.00 33.06 ? 760 HOH   A O   1 
HETATM 2676 O O   . HOH   C 3 .   ? 8.456  3.100   -17.725 1.00 44.26 ? 761 HOH   A O   1 
HETATM 2677 O O   . HOH   C 3 .   ? 8.279  -20.520 29.623  1.00 38.84 ? 762 HOH   A O   1 
HETATM 2678 O O   . HOH   C 3 .   ? 17.783 -2.910  33.910  1.00 29.80 ? 763 HOH   A O   1 
HETATM 2679 O O   . HOH   C 3 .   ? -2.819 -14.841 10.505  1.00 44.47 ? 764 HOH   A O   1 
HETATM 2680 O O   . HOH   C 3 .   ? 7.821  -22.002 -1.546  1.00 35.98 ? 765 HOH   A O   1 
HETATM 2681 O O   . HOH   C 3 .   ? 16.618 -18.803 -0.768  1.00 30.77 ? 766 HOH   A O   1 
HETATM 2682 O O   . HOH   C 3 .   ? 24.213 -13.429 9.110   1.00 25.02 ? 767 HOH   A O   1 
HETATM 2683 O O   . HOH   C 3 .   ? -2.337 28.367  -11.673 1.00 43.58 ? 768 HOH   A O   1 
HETATM 2684 O O   . HOH   C 3 .   ? 15.392 11.200  -25.297 1.00 21.82 ? 769 HOH   A O   1 
HETATM 2685 O O   . HOH   C 3 .   ? 19.879 -16.223 1.682   1.00 43.25 ? 770 HOH   A O   1 
HETATM 2686 O O   . HOH   C 3 .   ? 24.162 -3.495  28.152  1.00 26.91 ? 771 HOH   A O   1 
HETATM 2687 O O   . HOH   C 3 .   ? 12.688 -3.167  -5.874  1.00 34.79 ? 772 HOH   A O   1 
HETATM 2688 O O   . HOH   C 3 .   ? 1.885  2.417   25.562  1.00 37.28 ? 773 HOH   A O   1 
HETATM 2689 O O   . HOH   C 3 .   ? 19.842 -23.727 28.819  1.00 40.00 ? 774 HOH   A O   1 
HETATM 2690 O O   . HOH   C 3 .   ? 7.028  -22.521 28.828  1.00 31.75 ? 775 HOH   A O   1 
HETATM 2691 O O   . HOH   C 3 .   ? 22.714 2.324   25.998  1.00 30.20 ? 776 HOH   A O   1 
HETATM 2692 O O   . HOH   C 3 .   ? -0.000 16.591  0.000   0.50 6.05  ? 777 HOH   A O   1 
HETATM 2693 O O   . HOH   C 3 .   ? 14.411 -6.978  -4.744  1.00 39.25 ? 778 HOH   A O   1 
HETATM 2694 O O   . HOH   C 3 .   ? 17.912 -24.780 6.828   1.00 36.02 ? 779 HOH   A O   1 
HETATM 2695 O O   . HOH   C 3 .   ? 16.394 30.288  -2.806  1.00 28.74 ? 780 HOH   A O   1 
HETATM 2696 O O   . HOH   C 3 .   ? 31.310 21.174  -5.840  1.00 34.65 ? 781 HOH   A O   1 
HETATM 2697 O O   . HOH   C 3 .   ? 11.526 21.337  -19.450 1.00 32.01 ? 782 HOH   A O   1 
HETATM 2698 O O   . HOH   C 3 .   ? 25.588 -11.243 20.607  1.00 26.68 ? 783 HOH   A O   1 
HETATM 2699 O O   . HOH   C 3 .   ? 26.118 23.306  -2.663  1.00 33.43 ? 784 HOH   A O   1 
HETATM 2700 O O   . HOH   C 3 .   ? 20.949 -22.198 17.786  1.00 29.44 ? 785 HOH   A O   1 
HETATM 2701 O O   . HOH   C 3 .   ? 23.725 19.993  -1.839  1.00 33.86 ? 786 HOH   A O   1 
HETATM 2702 O O   . HOH   C 3 .   ? 6.320  9.708   1.939   1.00 24.99 ? 787 HOH   A O   1 
HETATM 2703 O O   . HOH   C 3 .   ? 9.614  -0.351  38.199  1.00 27.05 ? 788 HOH   A O   1 
HETATM 2704 O O   . HOH   C 3 .   ? -0.133 -7.040  19.985  1.00 27.25 ? 789 HOH   A O   1 
HETATM 2705 O O   . HOH   C 3 .   ? 15.960 21.174  9.632   1.00 35.01 ? 790 HOH   A O   1 
HETATM 2706 O O   . HOH   C 3 .   ? 14.318 19.506  7.071   1.00 51.81 ? 791 HOH   A O   1 
HETATM 2707 O O   . HOH   C 3 .   ? 24.294 -19.792 21.961  1.00 43.45 ? 792 HOH   A O   1 
HETATM 2708 O O   . HOH   C 3 .   ? 25.104 10.332  -2.870  1.00 31.76 ? 793 HOH   A O   1 
HETATM 2709 O O   . HOH   C 3 .   ? 14.603 -29.339 10.201  1.00 38.86 ? 794 HOH   A O   1 
HETATM 2710 O O   . HOH   C 3 .   ? 5.805  13.393  6.154   1.00 35.66 ? 795 HOH   A O   1 
HETATM 2711 O O   . HOH   C 3 .   ? 25.677 -17.618 25.973  1.00 24.61 ? 796 HOH   A O   1 
HETATM 2712 O O   . HOH   C 3 .   ? 19.186 12.015  22.239  1.00 31.87 ? 797 HOH   A O   1 
HETATM 2713 O O   . HOH   C 3 .   ? 15.623 -26.015 6.821   1.00 30.33 ? 798 HOH   A O   1 
HETATM 2714 O O   . HOH   C 3 .   ? 18.759 -20.942 7.599   1.00 41.03 ? 799 HOH   A O   1 
HETATM 2715 O O   . HOH   C 3 .   ? 5.299  1.089   25.341  1.00 30.37 ? 800 HOH   A O   1 
HETATM 2716 O O   . HOH   C 3 .   ? 9.668  -34.160 21.540  1.00 31.74 ? 801 HOH   A O   1 
HETATM 2717 O O   . HOH   C 3 .   ? 5.347  -22.511 -0.764  1.00 43.76 ? 802 HOH   A O   1 
HETATM 2718 O O   . HOH   C 3 .   ? 3.378  -18.222 0.562   1.00 25.48 ? 803 HOH   A O   1 
HETATM 2719 O O   . HOH   C 3 .   ? 6.965  -15.195 -8.220  1.00 40.17 ? 804 HOH   A O   1 
HETATM 2720 O O   . HOH   C 3 .   ? 2.927  -16.878 -1.594  1.00 27.68 ? 805 HOH   A O   1 
HETATM 2721 O O   . HOH   C 3 .   ? 21.418 6.704   -5.585  1.00 26.85 ? 806 HOH   A O   1 
HETATM 2722 O O   . HOH   C 3 .   ? 0.964  -5.786  22.404  1.00 30.28 ? 807 HOH   A O   1 
HETATM 2723 O O   . HOH   C 3 .   ? 24.237 -4.379  17.254  1.00 25.61 ? 808 HOH   A O   1 
HETATM 2724 O O   . HOH   C 3 .   ? 24.731 7.409   -5.571  1.00 44.38 ? 809 HOH   A O   1 
HETATM 2725 O O   . HOH   C 3 .   ? 21.667 -7.804  5.945   1.00 19.37 ? 810 HOH   A O   1 
HETATM 2726 O O   . HOH   C 3 .   ? -4.721 -12.082 4.974   1.00 30.74 ? 811 HOH   A O   1 
HETATM 2727 O O   . HOH   C 3 .   ? 3.401  -25.650 1.898   1.00 29.48 ? 812 HOH   A O   1 
HETATM 2728 O O   . HOH   C 3 .   ? 29.265 24.234  -12.737 1.00 35.06 ? 813 HOH   A O   1 
HETATM 2729 O O   . HOH   C 3 .   ? 24.476 -3.893  19.975  1.00 34.45 ? 814 HOH   A O   1 
HETATM 2730 O O   . HOH   C 3 .   ? 7.218  -19.121 -2.494  1.00 37.40 ? 815 HOH   A O   1 
HETATM 2731 O O   . HOH   C 3 .   ? 17.862 -30.005 13.194  1.00 38.66 ? 816 HOH   A O   1 
HETATM 2732 O O   . HOH   C 3 .   ? 3.459  0.915   26.887  1.00 29.19 ? 817 HOH   A O   1 
HETATM 2733 O O   . HOH   C 3 .   ? 16.695 -4.919  -2.021  1.00 19.56 ? 818 HOH   A O   1 
HETATM 2734 O O   . HOH   C 3 .   ? 29.359 13.135  -17.373 1.00 30.25 ? 819 HOH   A O   1 
HETATM 2735 O O   . HOH   C 3 .   ? 22.199 -17.502 23.605  1.00 24.81 ? 820 HOH   A O   1 
HETATM 2736 O O   . HOH   C 3 .   ? 7.268  -35.175 20.217  1.00 30.88 ? 821 HOH   A O   1 
HETATM 2737 O O   . HOH   C 3 .   ? 17.841 14.952  -23.553 1.00 26.63 ? 822 HOH   A O   1 
HETATM 2738 O O   . HOH   C 3 .   ? 25.389 -8.493  23.508  1.00 27.63 ? 823 HOH   A O   1 
HETATM 2739 O O   . HOH   C 3 .   ? 23.061 -1.421  22.815  1.00 34.83 ? 824 HOH   A O   1 
HETATM 2740 O O   . HOH   C 3 .   ? 20.452 -23.979 24.380  1.00 16.26 ? 825 HOH   A O   1 
HETATM 2741 O O   . HOH   C 3 .   ? 28.720 -9.735  26.015  1.00 41.49 ? 826 HOH   A O   1 
HETATM 2742 O O   . HOH   C 3 .   ? 16.918 -17.267 -7.850  1.00 41.89 ? 827 HOH   A O   1 
HETATM 2743 O O   . HOH   C 3 .   ? 23.446 12.681  0.136   1.00 38.85 ? 828 HOH   A O   1 
HETATM 2744 O O   . HOH   C 3 .   ? 24.183 -7.901  37.156  1.00 39.39 ? 829 HOH   A O   1 
HETATM 2745 O O   . HOH   C 3 .   ? 17.214 -10.466 -5.993  1.00 30.37 ? 830 HOH   A O   1 
HETATM 2746 O O   . HOH   C 3 .   ? 20.996 6.223   24.288  1.00 37.27 ? 831 HOH   A O   1 
HETATM 2747 O O   . HOH   C 3 .   ? 22.803 -17.058 26.170  1.00 13.96 ? 832 HOH   A O   1 
HETATM 2748 O O   . HOH   C 3 .   ? 16.918 1.705   34.186  1.00 28.13 ? 833 HOH   A O   1 
HETATM 2749 O O   . HOH   C 3 .   ? 12.895 24.160  3.749   1.00 25.89 ? 834 HOH   A O   1 
HETATM 2750 O O   . HOH   C 3 .   ? 21.870 -25.671 20.760  1.00 30.51 ? 835 HOH   A O   1 
HETATM 2751 O O   . HOH   C 3 .   ? 6.840  -28.404 1.778   1.00 40.06 ? 836 HOH   A O   1 
HETATM 2752 O O   . HOH   C 3 .   ? 22.112 3.049   -3.022  1.00 40.95 ? 837 HOH   A O   1 
HETATM 2753 O O   . HOH   C 3 .   ? 12.918 22.870  6.052   1.00 33.06 ? 838 HOH   A O   1 
HETATM 2754 O O   . HOH   C 3 .   ? 27.272 17.940  -14.371 1.00 26.30 ? 839 HOH   A O   1 
HETATM 2755 O O   . HOH   C 3 .   ? 25.127 1.974   27.134  1.00 36.76 ? 840 HOH   A O   1 
HETATM 2756 O O   . HOH   C 3 .   ? 6.639  22.096  -1.548  1.00 24.84 ? 841 HOH   A O   1 
HETATM 2757 O O   . HOH   C 3 .   ? 21.952 -14.541 8.808   1.00 25.43 ? 842 HOH   A O   1 
HETATM 2758 O O   . HOH   C 3 .   ? 17.384 -26.157 27.558  1.00 15.94 ? 843 HOH   A O   1 
HETATM 2759 O O   . HOH   C 3 .   ? 19.452 7.594   -3.559  1.00 21.86 ? 844 HOH   A O   1 
HETATM 2760 O O   . HOH   C 3 .   ? 4.186  9.263   7.342   1.00 33.00 ? 845 HOH   A O   1 
HETATM 2761 O O   . HOH   C 3 .   ? 27.400 14.096  -18.694 1.00 25.16 ? 846 HOH   A O   1 
HETATM 2762 O O   . HOH   C 3 .   ? 15.725 2.684   -13.352 1.00 43.22 ? 847 HOH   A O   1 
HETATM 2763 O O   . HOH   C 3 .   ? 21.079 13.168  -20.615 1.00 21.19 ? 848 HOH   A O   1 
HETATM 2764 O O   . HOH   C 3 .   ? 18.035 28.784  -1.817  1.00 36.90 ? 849 HOH   A O   1 
HETATM 2765 O O   . HOH   C 3 .   ? 22.644 16.397  3.214   1.00 26.19 ? 850 HOH   A O   1 
HETATM 2766 O O   . HOH   C 3 .   ? 13.677 -27.769 25.432  1.00 13.40 ? 851 HOH   A O   1 
HETATM 2767 O O   . HOH   C 3 .   ? 11.083 -33.792 24.221  1.00 24.29 ? 852 HOH   A O   1 
HETATM 2768 O O   . HOH   C 3 .   ? -2.023 -0.922  20.815  1.00 38.94 ? 853 HOH   A O   1 
HETATM 2769 O O   . HOH   C 3 .   ? 7.426  17.287  2.502   1.00 42.34 ? 854 HOH   A O   1 
HETATM 2770 O O   . HOH   C 3 .   ? 26.132 20.553  -2.009  1.00 25.81 ? 855 HOH   A O   1 
HETATM 2771 O O   . HOH   C 3 .   ? 18.003 -28.397 25.905  1.00 23.05 ? 856 HOH   A O   1 
HETATM 2772 O O   . HOH   C 3 .   ? 20.569 -15.899 4.319   1.00 35.07 ? 857 HOH   A O   1 
HETATM 2773 O O   . HOH   C 3 .   ? 3.515  -16.864 -4.076  1.00 34.36 ? 858 HOH   A O   1 
HETATM 2774 O O   . HOH   C 3 .   ? 20.317 -8.323  33.948  1.00 24.74 ? 859 HOH   A O   1 
HETATM 2775 O O   . HOH   C 3 .   ? -5.192 22.251  -9.384  1.00 27.48 ? 860 HOH   A O   1 
HETATM 2776 O O   . HOH   C 3 .   ? 20.824 -20.158 14.052  1.00 33.65 ? 861 HOH   A O   1 
HETATM 2777 O O   . HOH   C 3 .   ? 28.999 -10.362 22.127  1.00 35.05 ? 862 HOH   A O   1 
HETATM 2778 O O   . HOH   C 3 .   ? 28.526 -4.154  16.976  1.00 21.68 ? 863 HOH   A O   1 
HETATM 2779 O O   . HOH   C 3 .   ? 22.442 13.016  4.635   1.00 34.06 ? 864 HOH   A O   1 
HETATM 2780 O O   . HOH   C 3 .   ? 6.933  26.315  -11.169 1.00 32.24 ? 865 HOH   A O   1 
HETATM 2781 O O   . HOH   C 3 .   ? 21.022 -27.953 22.743  1.00 49.54 ? 866 HOH   A O   1 
HETATM 2782 O O   . HOH   C 3 .   ? 23.917 16.054  -16.834 1.00 22.62 ? 867 HOH   A O   1 
HETATM 2783 O O   . HOH   C 3 .   ? 24.984 5.612   4.501   1.00 39.08 ? 868 HOH   A O   1 
HETATM 2784 O O   . HOH   C 3 .   ? 27.232 -13.877 5.559   1.00 30.24 ? 869 HOH   A O   1 
HETATM 2785 O O   . HOH   C 3 .   ? -4.676 26.412  -9.243  1.00 19.27 ? 870 HOH   A O   1 
HETATM 2786 O O   . HOH   C 3 .   ? 10.735 -27.423 2.843   1.00 24.64 ? 871 HOH   A O   1 
HETATM 2787 O O   . HOH   C 3 .   ? 25.147 0.233   18.586  1.00 21.84 ? 872 HOH   A O   1 
HETATM 2788 O O   . HOH   C 3 .   ? 16.014 -29.943 22.044  1.00 33.04 ? 873 HOH   A O   1 
HETATM 2789 O O   . HOH   C 3 .   ? 27.314 13.884  -2.329  1.00 35.54 ? 874 HOH   A O   1 
HETATM 2790 O O   . HOH   C 3 .   ? 17.121 13.674  23.130  1.00 14.48 ? 875 HOH   A O   1 
HETATM 2791 O O   . HOH   C 3 .   ? 26.219 21.365  -16.854 1.00 20.74 ? 876 HOH   A O   1 
HETATM 2792 O O   . HOH   C 3 .   ? 22.629 -12.927 -0.576  1.00 28.44 ? 877 HOH   A O   1 
HETATM 2793 O O   . HOH   C 3 .   ? 25.511 0.994   16.453  1.00 32.78 ? 878 HOH   A O   1 
HETATM 2794 O O   . HOH   C 3 .   ? 9.622  31.864  -18.094 1.00 32.81 ? 879 HOH   A O   1 
HETATM 2795 O O   . HOH   C 3 .   ? 26.882 2.768   9.784   1.00 38.01 ? 880 HOH   A O   1 
HETATM 2796 O O   . HOH   C 3 .   ? 6.644  -15.406 33.090  1.00 37.37 ? 881 HOH   A O   1 
HETATM 2797 O O   . HOH   C 3 .   ? 18.751 -2.653  -2.306  1.00 29.72 ? 882 HOH   A O   1 
HETATM 2798 O O   . HOH   C 3 .   ? 20.420 31.051  0.228   1.00 36.82 ? 883 HOH   A O   1 
HETATM 2799 O O   . HOH   C 3 .   ? 24.701 8.219   4.968   1.00 28.85 ? 884 HOH   A O   1 
HETATM 2800 O O   . HOH   C 3 .   ? 24.633 19.043  2.203   1.00 35.80 ? 885 HOH   A O   1 
HETATM 2801 O O   . HOH   C 3 .   ? 10.889 22.305  0.480   1.00 18.08 ? 886 HOH   A O   1 
HETATM 2802 O O   . HOH   C 3 .   ? -0.000 6.674   -0.000  0.50 18.25 ? 887 HOH   A O   1 
HETATM 2803 O O   . HOH   C 3 .   ? 25.199 10.219  7.596   1.00 33.56 ? 888 HOH   A O   1 
HETATM 2804 O O   . HOH   C 3 .   ? 18.701 -7.122  36.162  1.00 36.59 ? 889 HOH   A O   1 
HETATM 2805 O O   . HOH   C 3 .   ? 13.679 -30.978 21.429  1.00 26.95 ? 890 HOH   A O   1 
HETATM 2806 O O   . HOH   C 3 .   ? 13.138 12.710  24.438  1.00 28.26 ? 891 HOH   A O   1 
HETATM 2807 O O   . HOH   C 3 .   ? 7.548  19.874  2.112   1.00 41.41 ? 892 HOH   A O   1 
HETATM 2808 O O   . HOH   C 3 .   ? 21.550 -13.686 38.516  1.00 35.23 ? 893 HOH   A O   1 
HETATM 2809 O O   . HOH   C 3 .   ? 15.272 -31.954 16.242  1.00 48.70 ? 894 HOH   A O   1 
HETATM 2810 O O   . HOH   C 3 .   ? 25.193 17.965  -18.675 1.00 31.65 ? 895 HOH   A O   1 
HETATM 2811 O O   . HOH   C 3 .   ? 28.662 29.658  -6.369  1.00 32.37 ? 896 HOH   A O   1 
# 
