data_8XRR
# 
_entry.id   8XRR 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8XRR         pdb_00008xrr 10.2210/pdb8xrr/pdb 
WWPDB D_1300044068 ?            ?                   
# 
_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       2025-01-15 
# 
_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                        8XRR 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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              zhusujie@qdu.edu.cn 
_pdbx_contact_author.name_first         Sujie 
_pdbx_contact_author.name_last          Zhu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6488-9644 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhu, S.J.' 1 ? 
'Bi, S.Z.'  2 ? 
# 
_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                     'A complex structure of PDGFRA with an inhibitor RH140' 
_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 'Zhu, S.J.' 1 ? 
primary 'Bi, S.Z.'  2 ? 
# 
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 'Platelet-derived growth factor receptor alpha' 40558.750 1  ? ? ? ? 
2 non-polymer syn RH140                                           399.488   1  ? ? ? ? 
3 water       nat water                                           18.015    55 ? ? ? ? 
# 
_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       
;GAMDKQKPRYEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRVLGSGAFGKVVEGTAYGLSRSQPVMKVA
VKMLKPTARSSSKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIIIEYCFYGDLVNYLHKNRDSFLSHKKKSMLDSE
VKNLLSDDNSEGLTLLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFL
PVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMMVDSTFYNKIKSGYRMAKPDHATSEVYEIMVKCWNSEP
EKRPSFYHLSEIVENLLPGQYKKSYEKIHLDFLKSD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GAMDKQKPRYEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRVLGSGAFGKVVEGTAYGLSRSQPVMKVA
VKMLKPTARSSSKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIIIEYCFYGDLVNYLHKNRDSFLSHKKKSMLDSE
VKNLLSDDNSEGLTLLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFL
PVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMMVDSTFYNKIKSGYRMAKPDHATSEVYEIMVKCWNSEP
EKRPSFYHLSEIVENLLPGQYKKSYEKIHLDFLKSD
;
_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 RH140 A1LV8 
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   ALA n 
1 3   MET n 
1 4   ASP n 
1 5   LYS n 
1 6   GLN n 
1 7   LYS n 
1 8   PRO n 
1 9   ARG n 
1 10  TYR n 
1 11  GLU n 
1 12  ILE n 
1 13  ARG n 
1 14  TRP n 
1 15  ARG n 
1 16  VAL n 
1 17  ILE n 
1 18  GLU n 
1 19  SER n 
1 20  ILE n 
1 21  SER n 
1 22  PRO n 
1 23  ASP n 
1 24  GLY n 
1 25  HIS n 
1 26  GLU n 
1 27  TYR n 
1 28  ILE n 
1 29  TYR n 
1 30  VAL n 
1 31  ASP n 
1 32  PRO n 
1 33  MET n 
1 34  GLN n 
1 35  LEU n 
1 36  PRO n 
1 37  TYR n 
1 38  ASP n 
1 39  SER n 
1 40  ARG n 
1 41  TRP n 
1 42  GLU n 
1 43  PHE n 
1 44  PRO n 
1 45  ARG n 
1 46  ASP n 
1 47  GLY n 
1 48  LEU n 
1 49  VAL n 
1 50  LEU n 
1 51  GLY n 
1 52  ARG n 
1 53  VAL n 
1 54  LEU n 
1 55  GLY n 
1 56  SER n 
1 57  GLY n 
1 58  ALA n 
1 59  PHE n 
1 60  GLY n 
1 61  LYS n 
1 62  VAL n 
1 63  VAL n 
1 64  GLU n 
1 65  GLY n 
1 66  THR n 
1 67  ALA n 
1 68  TYR n 
1 69  GLY n 
1 70  LEU n 
1 71  SER n 
1 72  ARG n 
1 73  SER n 
1 74  GLN n 
1 75  PRO n 
1 76  VAL n 
1 77  MET n 
1 78  LYS n 
1 79  VAL n 
1 80  ALA n 
1 81  VAL n 
1 82  LYS n 
1 83  MET n 
1 84  LEU n 
1 85  LYS n 
1 86  PRO n 
1 87  THR n 
1 88  ALA n 
1 89  ARG n 
1 90  SER n 
1 91  SER n 
1 92  SER n 
1 93  LYS n 
1 94  GLN n 
1 95  ALA n 
1 96  LEU n 
1 97  MET n 
1 98  SER n 
1 99  GLU n 
1 100 LEU n 
1 101 LYS n 
1 102 ILE n 
1 103 MET n 
1 104 THR n 
1 105 HIS n 
1 106 LEU n 
1 107 GLY n 
1 108 PRO n 
1 109 HIS n 
1 110 LEU n 
1 111 ASN n 
1 112 ILE n 
1 113 VAL n 
1 114 ASN n 
1 115 LEU n 
1 116 LEU n 
1 117 GLY n 
1 118 ALA n 
1 119 CYS n 
1 120 THR n 
1 121 LYS n 
1 122 SER n 
1 123 GLY n 
1 124 PRO n 
1 125 ILE n 
1 126 TYR n 
1 127 ILE n 
1 128 ILE n 
1 129 ILE n 
1 130 GLU n 
1 131 TYR n 
1 132 CYS n 
1 133 PHE n 
1 134 TYR n 
1 135 GLY n 
1 136 ASP n 
1 137 LEU n 
1 138 VAL n 
1 139 ASN n 
1 140 TYR n 
1 141 LEU n 
1 142 HIS n 
1 143 LYS n 
1 144 ASN n 
1 145 ARG n 
1 146 ASP n 
1 147 SER n 
1 148 PHE n 
1 149 LEU n 
1 150 SER n 
1 151 HIS n 
1 152 LYS n 
1 153 LYS n 
1 154 LYS n 
1 155 SER n 
1 156 MET n 
1 157 LEU n 
1 158 ASP n 
1 159 SER n 
1 160 GLU n 
1 161 VAL n 
1 162 LYS n 
1 163 ASN n 
1 164 LEU n 
1 165 LEU n 
1 166 SER n 
1 167 ASP n 
1 168 ASP n 
1 169 ASN n 
1 170 SER n 
1 171 GLU n 
1 172 GLY n 
1 173 LEU n 
1 174 THR n 
1 175 LEU n 
1 176 LEU n 
1 177 ASP n 
1 178 LEU n 
1 179 LEU n 
1 180 SER n 
1 181 PHE n 
1 182 THR n 
1 183 TYR n 
1 184 GLN n 
1 185 VAL n 
1 186 ALA n 
1 187 ARG n 
1 188 GLY n 
1 189 MET n 
1 190 GLU n 
1 191 PHE n 
1 192 LEU n 
1 193 ALA n 
1 194 SER n 
1 195 LYS n 
1 196 ASN n 
1 197 CYS n 
1 198 VAL n 
1 199 HIS n 
1 200 ARG n 
1 201 ASP n 
1 202 LEU n 
1 203 ALA n 
1 204 ALA n 
1 205 ARG n 
1 206 ASN n 
1 207 VAL n 
1 208 LEU n 
1 209 LEU n 
1 210 ALA n 
1 211 GLN n 
1 212 GLY n 
1 213 LYS n 
1 214 ILE n 
1 215 VAL n 
1 216 LYS n 
1 217 ILE n 
1 218 CYS n 
1 219 ASP n 
1 220 PHE n 
1 221 GLY n 
1 222 LEU n 
1 223 ALA n 
1 224 ARG n 
1 225 ASP n 
1 226 ILE n 
1 227 MET n 
1 228 HIS n 
1 229 ASP n 
1 230 SER n 
1 231 ASN n 
1 232 TYR n 
1 233 VAL n 
1 234 SER n 
1 235 LYS n 
1 236 GLY n 
1 237 SER n 
1 238 THR n 
1 239 PHE n 
1 240 LEU n 
1 241 PRO n 
1 242 VAL n 
1 243 LYS n 
1 244 TRP n 
1 245 MET n 
1 246 ALA n 
1 247 PRO n 
1 248 GLU n 
1 249 SER n 
1 250 ILE n 
1 251 PHE n 
1 252 ASP n 
1 253 ASN n 
1 254 LEU n 
1 255 TYR n 
1 256 THR n 
1 257 THR n 
1 258 LEU n 
1 259 SER n 
1 260 ASP n 
1 261 VAL n 
1 262 TRP n 
1 263 SER n 
1 264 TYR n 
1 265 GLY n 
1 266 ILE n 
1 267 LEU n 
1 268 LEU n 
1 269 TRP n 
1 270 GLU n 
1 271 ILE n 
1 272 PHE n 
1 273 SER n 
1 274 LEU n 
1 275 GLY n 
1 276 GLY n 
1 277 THR n 
1 278 PRO n 
1 279 TYR n 
1 280 PRO n 
1 281 GLY n 
1 282 MET n 
1 283 MET n 
1 284 VAL n 
1 285 ASP n 
1 286 SER n 
1 287 THR n 
1 288 PHE n 
1 289 TYR n 
1 290 ASN n 
1 291 LYS n 
1 292 ILE n 
1 293 LYS n 
1 294 SER n 
1 295 GLY n 
1 296 TYR n 
1 297 ARG n 
1 298 MET n 
1 299 ALA n 
1 300 LYS n 
1 301 PRO n 
1 302 ASP n 
1 303 HIS n 
1 304 ALA n 
1 305 THR n 
1 306 SER n 
1 307 GLU n 
1 308 VAL n 
1 309 TYR n 
1 310 GLU n 
1 311 ILE n 
1 312 MET n 
1 313 VAL n 
1 314 LYS n 
1 315 CYS n 
1 316 TRP n 
1 317 ASN n 
1 318 SER n 
1 319 GLU n 
1 320 PRO n 
1 321 GLU n 
1 322 LYS n 
1 323 ARG n 
1 324 PRO n 
1 325 SER n 
1 326 PHE n 
1 327 TYR n 
1 328 HIS n 
1 329 LEU n 
1 330 SER n 
1 331 GLU n 
1 332 ILE n 
1 333 VAL n 
1 334 GLU n 
1 335 ASN n 
1 336 LEU n 
1 337 LEU n 
1 338 PRO n 
1 339 GLY n 
1 340 GLN n 
1 341 TYR n 
1 342 LYS n 
1 343 LYS n 
1 344 SER n 
1 345 TYR n 
1 346 GLU n 
1 347 LYS n 
1 348 ILE n 
1 349 HIS n 
1 350 LEU n 
1 351 ASP n 
1 352 PHE n 
1 353 LEU n 
1 354 LYS n 
1 355 SER n 
1 356 ASP 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                   356 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_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 
A1LV8 non-polymer         . RH140           ? 'C24 H25 N5 O'   399.488 
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   546 ?   ?   ?   A . n 
A 1 2   ALA 2   547 ?   ?   ?   A . n 
A 1 3   MET 3   548 ?   ?   ?   A . n 
A 1 4   ASP 4   549 ?   ?   ?   A . n 
A 1 5   LYS 5   550 ?   ?   ?   A . n 
A 1 6   GLN 6   551 ?   ?   ?   A . n 
A 1 7   LYS 7   552 ?   ?   ?   A . n 
A 1 8   PRO 8   553 ?   ?   ?   A . n 
A 1 9   ARG 9   554 ?   ?   ?   A . n 
A 1 10  TYR 10  555 ?   ?   ?   A . n 
A 1 11  GLU 11  556 ?   ?   ?   A . n 
A 1 12  ILE 12  557 ?   ?   ?   A . n 
A 1 13  ARG 13  558 ?   ?   ?   A . n 
A 1 14  TRP 14  559 ?   ?   ?   A . n 
A 1 15  ARG 15  560 ?   ?   ?   A . n 
A 1 16  VAL 16  561 ?   ?   ?   A . n 
A 1 17  ILE 17  562 ?   ?   ?   A . n 
A 1 18  GLU 18  563 ?   ?   ?   A . n 
A 1 19  SER 19  564 ?   ?   ?   A . n 
A 1 20  ILE 20  565 ?   ?   ?   A . n 
A 1 21  SER 21  566 ?   ?   ?   A . n 
A 1 22  PRO 22  567 ?   ?   ?   A . n 
A 1 23  ASP 23  568 ?   ?   ?   A . n 
A 1 24  GLY 24  569 569 GLY GLY A . n 
A 1 25  HIS 25  570 570 HIS HIS A . n 
A 1 26  GLU 26  571 571 GLU GLU A . n 
A 1 27  TYR 27  572 572 TYR TYR A . n 
A 1 28  ILE 28  573 573 ILE ILE A . n 
A 1 29  TYR 29  574 574 TYR TYR A . n 
A 1 30  VAL 30  575 575 VAL VAL A . n 
A 1 31  ASP 31  576 576 ASP ASP A . n 
A 1 32  PRO 32  577 577 PRO PRO A . n 
A 1 33  MET 33  578 578 MET MET A . n 
A 1 34  GLN 34  579 579 GLN GLN A . n 
A 1 35  LEU 35  580 580 LEU LEU A . n 
A 1 36  PRO 36  581 581 PRO PRO A . n 
A 1 37  TYR 37  582 582 TYR TYR A . n 
A 1 38  ASP 38  583 583 ASP ASP A . n 
A 1 39  SER 39  584 584 SER SER A . n 
A 1 40  ARG 40  585 585 ARG ARG A . n 
A 1 41  TRP 41  586 586 TRP TRP A . n 
A 1 42  GLU 42  587 587 GLU GLU A . n 
A 1 43  PHE 43  588 588 PHE PHE A . n 
A 1 44  PRO 44  589 589 PRO PRO A . n 
A 1 45  ARG 45  590 590 ARG ARG A . n 
A 1 46  ASP 46  591 591 ASP ASP A . n 
A 1 47  GLY 47  592 592 GLY GLY A . n 
A 1 48  LEU 48  593 593 LEU LEU A . n 
A 1 49  VAL 49  594 594 VAL VAL A . n 
A 1 50  LEU 50  595 595 LEU LEU A . n 
A 1 51  GLY 51  596 596 GLY GLY A . n 
A 1 52  ARG 52  597 597 ARG ARG A . n 
A 1 53  VAL 53  598 598 VAL VAL A . n 
A 1 54  LEU 54  599 599 LEU LEU A . n 
A 1 55  GLY 55  600 600 GLY GLY A . n 
A 1 56  SER 56  601 601 SER SER A . n 
A 1 57  GLY 57  602 602 GLY GLY A . n 
A 1 58  ALA 58  603 603 ALA ALA A . n 
A 1 59  PHE 59  604 604 PHE PHE A . n 
A 1 60  GLY 60  605 605 GLY GLY A . n 
A 1 61  LYS 61  606 606 LYS LYS A . n 
A 1 62  VAL 62  607 607 VAL VAL A . n 
A 1 63  VAL 63  608 608 VAL VAL A . n 
A 1 64  GLU 64  609 609 GLU GLU A . n 
A 1 65  GLY 65  610 610 GLY GLY A . n 
A 1 66  THR 66  611 611 THR THR A . n 
A 1 67  ALA 67  612 612 ALA ALA A . n 
A 1 68  TYR 68  613 613 TYR TYR A . n 
A 1 69  GLY 69  614 614 GLY GLY A . n 
A 1 70  LEU 70  615 615 LEU LEU A . n 
A 1 71  SER 71  616 616 SER SER A . n 
A 1 72  ARG 72  617 617 ARG ARG A . n 
A 1 73  SER 73  618 618 SER SER A . n 
A 1 74  GLN 74  619 619 GLN GLN A . n 
A 1 75  PRO 75  620 620 PRO PRO A . n 
A 1 76  VAL 76  621 621 VAL VAL A . n 
A 1 77  MET 77  622 622 MET MET A . n 
A 1 78  LYS 78  623 623 LYS LYS A . n 
A 1 79  VAL 79  624 624 VAL VAL A . n 
A 1 80  ALA 80  625 625 ALA ALA A . n 
A 1 81  VAL 81  626 626 VAL VAL A . n 
A 1 82  LYS 82  627 627 LYS LYS A . n 
A 1 83  MET 83  628 628 MET MET A . n 
A 1 84  LEU 84  629 629 LEU LEU A . n 
A 1 85  LYS 85  630 630 LYS LYS A . n 
A 1 86  PRO 86  631 631 PRO PRO A . n 
A 1 87  THR 87  632 632 THR THR A . n 
A 1 88  ALA 88  633 ?   ?   ?   A . n 
A 1 89  ARG 89  634 ?   ?   ?   A . n 
A 1 90  SER 90  635 ?   ?   ?   A . n 
A 1 91  SER 91  636 636 SER SER A . n 
A 1 92  SER 92  637 637 SER SER A . n 
A 1 93  LYS 93  638 638 LYS LYS A . n 
A 1 94  GLN 94  639 639 GLN GLN A . n 
A 1 95  ALA 95  640 640 ALA ALA A . n 
A 1 96  LEU 96  641 641 LEU LEU A . n 
A 1 97  MET 97  642 642 MET MET A . n 
A 1 98  SER 98  643 643 SER SER A . n 
A 1 99  GLU 99  644 644 GLU GLU A . n 
A 1 100 LEU 100 645 645 LEU LEU A . n 
A 1 101 LYS 101 646 646 LYS LYS A . n 
A 1 102 ILE 102 647 647 ILE ILE A . n 
A 1 103 MET 103 648 648 MET MET A . n 
A 1 104 THR 104 649 649 THR THR A . n 
A 1 105 HIS 105 650 650 HIS HIS A . n 
A 1 106 LEU 106 651 651 LEU LEU A . n 
A 1 107 GLY 107 652 652 GLY GLY A . n 
A 1 108 PRO 108 653 653 PRO PRO A . n 
A 1 109 HIS 109 654 654 HIS HIS A . n 
A 1 110 LEU 110 655 655 LEU LEU A . n 
A 1 111 ASN 111 656 656 ASN ASN A . n 
A 1 112 ILE 112 657 657 ILE ILE A . n 
A 1 113 VAL 113 658 658 VAL VAL A . n 
A 1 114 ASN 114 659 659 ASN ASN A . n 
A 1 115 LEU 115 660 660 LEU LEU A . n 
A 1 116 LEU 116 661 661 LEU LEU A . n 
A 1 117 GLY 117 662 662 GLY GLY A . n 
A 1 118 ALA 118 663 663 ALA ALA A . n 
A 1 119 CYS 119 664 664 CYS CYS A . n 
A 1 120 THR 120 665 665 THR THR A . n 
A 1 121 LYS 121 666 666 LYS LYS A . n 
A 1 122 SER 122 667 667 SER SER A . n 
A 1 123 GLY 123 668 668 GLY GLY A . n 
A 1 124 PRO 124 669 669 PRO PRO A . n 
A 1 125 ILE 125 670 670 ILE ILE A . n 
A 1 126 TYR 126 671 671 TYR TYR A . n 
A 1 127 ILE 127 672 672 ILE ILE A . n 
A 1 128 ILE 128 673 673 ILE ILE A . n 
A 1 129 ILE 129 674 674 ILE ILE A . n 
A 1 130 GLU 130 675 675 GLU GLU A . n 
A 1 131 TYR 131 676 676 TYR TYR A . n 
A 1 132 CYS 132 677 677 CYS CYS A . n 
A 1 133 PHE 133 678 678 PHE PHE A . n 
A 1 134 TYR 134 679 679 TYR TYR A . n 
A 1 135 GLY 135 680 680 GLY GLY A . n 
A 1 136 ASP 136 681 681 ASP ASP A . n 
A 1 137 LEU 137 682 682 LEU LEU A . n 
A 1 138 VAL 138 683 683 VAL VAL A . n 
A 1 139 ASN 139 684 684 ASN ASN A . n 
A 1 140 TYR 140 685 685 TYR TYR A . n 
A 1 141 LEU 141 686 686 LEU LEU A . n 
A 1 142 HIS 142 687 687 HIS HIS A . n 
A 1 143 LYS 143 688 688 LYS LYS A . n 
A 1 144 ASN 144 689 689 ASN ASN A . n 
A 1 145 ARG 145 690 690 ARG ARG A . n 
A 1 146 ASP 146 691 691 ASP ASP A . n 
A 1 147 SER 147 692 692 SER SER A . n 
A 1 148 PHE 148 693 693 PHE PHE A . n 
A 1 149 LEU 149 694 694 LEU LEU A . n 
A 1 150 SER 150 695 ?   ?   ?   A . n 
A 1 151 HIS 151 696 ?   ?   ?   A . n 
A 1 152 LYS 152 697 ?   ?   ?   A . n 
A 1 153 LYS 153 698 ?   ?   ?   A . n 
A 1 154 LYS 154 699 ?   ?   ?   A . n 
A 1 155 SER 155 700 ?   ?   ?   A . n 
A 1 156 MET 156 701 ?   ?   ?   A . n 
A 1 157 LEU 157 702 ?   ?   ?   A . n 
A 1 158 ASP 158 703 ?   ?   ?   A . n 
A 1 159 SER 159 704 ?   ?   ?   A . n 
A 1 160 GLU 160 705 ?   ?   ?   A . n 
A 1 161 VAL 161 706 ?   ?   ?   A . n 
A 1 162 LYS 162 707 ?   ?   ?   A . n 
A 1 163 ASN 163 708 ?   ?   ?   A . n 
A 1 164 LEU 164 709 ?   ?   ?   A . n 
A 1 165 LEU 165 710 ?   ?   ?   A . n 
A 1 166 SER 166 711 ?   ?   ?   A . n 
A 1 167 ASP 167 712 ?   ?   ?   A . n 
A 1 168 ASP 168 713 ?   ?   ?   A . n 
A 1 169 ASN 169 714 ?   ?   ?   A . n 
A 1 170 SER 170 715 ?   ?   ?   A . n 
A 1 171 GLU 171 716 ?   ?   ?   A . n 
A 1 172 GLY 172 717 717 GLY GLY A . n 
A 1 173 LEU 173 718 718 LEU LEU A . n 
A 1 174 THR 174 719 719 THR THR A . n 
A 1 175 LEU 175 720 720 LEU LEU A . n 
A 1 176 LEU 176 721 721 LEU LEU A . n 
A 1 177 ASP 177 722 722 ASP ASP A . n 
A 1 178 LEU 178 723 723 LEU LEU A . n 
A 1 179 LEU 179 724 724 LEU LEU A . n 
A 1 180 SER 180 725 725 SER SER A . n 
A 1 181 PHE 181 726 726 PHE PHE A . n 
A 1 182 THR 182 727 727 THR THR A . n 
A 1 183 TYR 183 728 728 TYR TYR A . n 
A 1 184 GLN 184 729 729 GLN GLN A . n 
A 1 185 VAL 185 730 730 VAL VAL A . n 
A 1 186 ALA 186 731 731 ALA ALA A . n 
A 1 187 ARG 187 732 732 ARG ARG A . n 
A 1 188 GLY 188 733 733 GLY GLY A . n 
A 1 189 MET 189 734 734 MET MET A . n 
A 1 190 GLU 190 735 735 GLU GLU A . n 
A 1 191 PHE 191 736 736 PHE PHE A . n 
A 1 192 LEU 192 737 737 LEU LEU A . n 
A 1 193 ALA 193 738 738 ALA ALA A . n 
A 1 194 SER 194 739 739 SER SER A . n 
A 1 195 LYS 195 740 740 LYS LYS A . n 
A 1 196 ASN 196 741 741 ASN ASN A . n 
A 1 197 CYS 197 742 742 CYS CYS A . n 
A 1 198 VAL 198 743 743 VAL VAL A . n 
A 1 199 HIS 199 744 744 HIS HIS A . n 
A 1 200 ARG 200 745 745 ARG ARG A . n 
A 1 201 ASP 201 746 746 ASP ASP A . n 
A 1 202 LEU 202 747 747 LEU LEU A . n 
A 1 203 ALA 203 748 748 ALA ALA A . n 
A 1 204 ALA 204 749 749 ALA ALA A . n 
A 1 205 ARG 205 750 750 ARG ARG A . n 
A 1 206 ASN 206 751 751 ASN ASN A . n 
A 1 207 VAL 207 752 752 VAL VAL A . n 
A 1 208 LEU 208 753 753 LEU LEU A . n 
A 1 209 LEU 209 754 754 LEU LEU A . n 
A 1 210 ALA 210 755 755 ALA ALA A . n 
A 1 211 GLN 211 756 756 GLN GLN A . n 
A 1 212 GLY 212 757 757 GLY GLY A . n 
A 1 213 LYS 213 758 758 LYS LYS A . n 
A 1 214 ILE 214 759 759 ILE ILE A . n 
A 1 215 VAL 215 760 760 VAL VAL A . n 
A 1 216 LYS 216 761 761 LYS LYS A . n 
A 1 217 ILE 217 762 762 ILE ILE A . n 
A 1 218 CYS 218 763 763 CYS CYS A . n 
A 1 219 ASP 219 764 764 ASP ASP A . n 
A 1 220 PHE 220 765 765 PHE PHE A . n 
A 1 221 GLY 221 766 766 GLY GLY A . n 
A 1 222 LEU 222 767 767 LEU LEU A . n 
A 1 223 ALA 223 768 768 ALA ALA A . n 
A 1 224 ARG 224 769 769 ARG ARG A . n 
A 1 225 ASP 225 770 770 ASP ASP A . n 
A 1 226 ILE 226 771 771 ILE ILE A . n 
A 1 227 MET 227 772 ?   ?   ?   A . n 
A 1 228 HIS 228 773 ?   ?   ?   A . n 
A 1 229 ASP 229 774 ?   ?   ?   A . n 
A 1 230 SER 230 775 ?   ?   ?   A . n 
A 1 231 ASN 231 776 ?   ?   ?   A . n 
A 1 232 TYR 232 777 ?   ?   ?   A . n 
A 1 233 VAL 233 778 ?   ?   ?   A . n 
A 1 234 SER 234 779 ?   ?   ?   A . n 
A 1 235 LYS 235 780 ?   ?   ?   A . n 
A 1 236 GLY 236 781 ?   ?   ?   A . n 
A 1 237 SER 237 782 ?   ?   ?   A . n 
A 1 238 THR 238 783 783 THR THR A . n 
A 1 239 PHE 239 784 784 PHE PHE A . n 
A 1 240 LEU 240 785 785 LEU LEU A . n 
A 1 241 PRO 241 786 786 PRO PRO A . n 
A 1 242 VAL 242 787 787 VAL VAL A . n 
A 1 243 LYS 243 788 788 LYS LYS A . n 
A 1 244 TRP 244 789 789 TRP TRP A . n 
A 1 245 MET 245 790 790 MET MET A . n 
A 1 246 ALA 246 791 791 ALA ALA A . n 
A 1 247 PRO 247 792 792 PRO PRO A . n 
A 1 248 GLU 248 793 793 GLU GLU A . n 
A 1 249 SER 249 794 794 SER SER A . n 
A 1 250 ILE 250 795 795 ILE ILE A . n 
A 1 251 PHE 251 796 796 PHE PHE A . n 
A 1 252 ASP 252 797 797 ASP ASP A . n 
A 1 253 ASN 253 798 798 ASN ASN A . n 
A 1 254 LEU 254 799 799 LEU LEU A . n 
A 1 255 TYR 255 800 800 TYR TYR A . n 
A 1 256 THR 256 801 801 THR THR A . n 
A 1 257 THR 257 802 802 THR THR A . n 
A 1 258 LEU 258 803 803 LEU LEU A . n 
A 1 259 SER 259 804 804 SER SER A . n 
A 1 260 ASP 260 805 805 ASP ASP A . n 
A 1 261 VAL 261 806 806 VAL VAL A . n 
A 1 262 TRP 262 807 807 TRP TRP A . n 
A 1 263 SER 263 808 808 SER SER A . n 
A 1 264 TYR 264 809 809 TYR TYR A . n 
A 1 265 GLY 265 810 810 GLY GLY A . n 
A 1 266 ILE 266 811 811 ILE ILE A . n 
A 1 267 LEU 267 812 812 LEU LEU A . n 
A 1 268 LEU 268 813 813 LEU LEU A . n 
A 1 269 TRP 269 814 814 TRP TRP A . n 
A 1 270 GLU 270 815 815 GLU GLU A . n 
A 1 271 ILE 271 816 816 ILE ILE A . n 
A 1 272 PHE 272 817 817 PHE PHE A . n 
A 1 273 SER 273 818 818 SER SER A . n 
A 1 274 LEU 274 819 819 LEU LEU A . n 
A 1 275 GLY 275 820 820 GLY GLY A . n 
A 1 276 GLY 276 821 821 GLY GLY A . n 
A 1 277 THR 277 822 822 THR THR A . n 
A 1 278 PRO 278 823 823 PRO PRO A . n 
A 1 279 TYR 279 824 824 TYR TYR A . n 
A 1 280 PRO 280 825 825 PRO PRO A . n 
A 1 281 GLY 281 826 826 GLY GLY A . n 
A 1 282 MET 282 827 827 MET MET A . n 
A 1 283 MET 283 828 828 MET MET A . n 
A 1 284 VAL 284 829 829 VAL VAL A . n 
A 1 285 ASP 285 830 830 ASP ASP A . n 
A 1 286 SER 286 831 831 SER SER A . n 
A 1 287 THR 287 832 832 THR THR A . n 
A 1 288 PHE 288 833 833 PHE PHE A . n 
A 1 289 TYR 289 834 834 TYR TYR A . n 
A 1 290 ASN 290 835 835 ASN ASN A . n 
A 1 291 LYS 291 836 836 LYS LYS A . n 
A 1 292 ILE 292 837 837 ILE ILE A . n 
A 1 293 LYS 293 838 838 LYS LYS A . n 
A 1 294 SER 294 839 839 SER SER A . n 
A 1 295 GLY 295 840 840 GLY GLY A . n 
A 1 296 TYR 296 841 841 TYR TYR A . n 
A 1 297 ARG 297 842 842 ARG ARG A . n 
A 1 298 MET 298 843 843 MET MET A . n 
A 1 299 ALA 299 844 844 ALA ALA A . n 
A 1 300 LYS 300 845 845 LYS LYS A . n 
A 1 301 PRO 301 846 846 PRO PRO A . n 
A 1 302 ASP 302 847 847 ASP ASP A . n 
A 1 303 HIS 303 848 848 HIS HIS A . n 
A 1 304 ALA 304 849 849 ALA ALA A . n 
A 1 305 THR 305 850 850 THR THR A . n 
A 1 306 SER 306 851 851 SER SER A . n 
A 1 307 GLU 307 852 852 GLU GLU A . n 
A 1 308 VAL 308 853 853 VAL VAL A . n 
A 1 309 TYR 309 854 854 TYR TYR A . n 
A 1 310 GLU 310 855 855 GLU GLU A . n 
A 1 311 ILE 311 856 856 ILE ILE A . n 
A 1 312 MET 312 857 857 MET MET A . n 
A 1 313 VAL 313 858 858 VAL VAL A . n 
A 1 314 LYS 314 859 859 LYS LYS A . n 
A 1 315 CYS 315 860 860 CYS CYS A . n 
A 1 316 TRP 316 861 861 TRP TRP A . n 
A 1 317 ASN 317 862 862 ASN ASN A . n 
A 1 318 SER 318 863 863 SER SER A . n 
A 1 319 GLU 319 864 864 GLU GLU A . n 
A 1 320 PRO 320 865 865 PRO PRO A . n 
A 1 321 GLU 321 866 866 GLU GLU A . n 
A 1 322 LYS 322 867 867 LYS LYS A . n 
A 1 323 ARG 323 868 868 ARG ARG A . n 
A 1 324 PRO 324 869 869 PRO PRO A . n 
A 1 325 SER 325 870 870 SER SER A . n 
A 1 326 PHE 326 871 871 PHE PHE A . n 
A 1 327 TYR 327 872 872 TYR TYR A . n 
A 1 328 HIS 328 873 873 HIS HIS A . n 
A 1 329 LEU 329 874 874 LEU LEU A . n 
A 1 330 SER 330 875 875 SER SER A . n 
A 1 331 GLU 331 876 876 GLU GLU A . n 
A 1 332 ILE 332 877 877 ILE ILE A . n 
A 1 333 VAL 333 878 878 VAL VAL A . n 
A 1 334 GLU 334 879 879 GLU GLU A . n 
A 1 335 ASN 335 880 880 ASN ASN A . n 
A 1 336 LEU 336 881 881 LEU LEU A . n 
A 1 337 LEU 337 882 882 LEU LEU A . n 
A 1 338 PRO 338 883 883 PRO PRO A . n 
A 1 339 GLY 339 884 884 GLY GLY A . n 
A 1 340 GLN 340 885 885 GLN GLN A . n 
A 1 341 TYR 341 886 886 TYR TYR A . n 
A 1 342 LYS 342 887 887 LYS LYS A . n 
A 1 343 LYS 343 888 888 LYS LYS A . n 
A 1 344 SER 344 889 889 SER SER A . n 
A 1 345 TYR 345 890 890 TYR TYR A . n 
A 1 346 GLU 346 891 891 GLU GLU A . n 
A 1 347 LYS 347 892 892 LYS LYS A . n 
A 1 348 ILE 348 893 893 ILE ILE A . n 
A 1 349 HIS 349 894 894 HIS HIS A . n 
A 1 350 LEU 350 895 895 LEU LEU A . n 
A 1 351 ASP 351 896 896 ASP ASP A . n 
A 1 352 PHE 352 897 897 PHE PHE A . n 
A 1 353 LEU 353 898 898 LEU LEU A . n 
A 1 354 LYS 354 899 ?   ?   ?   A . n 
A 1 355 SER 355 900 ?   ?   ?   A . n 
A 1 356 ASP 356 901 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1LV8 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1LV8 
_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 A1LV8 1  1001 1  A1LV8 DRG A . 
C 3 HOH   1  1101 41 HOH   HOH A . 
C 3 HOH   2  1102 11 HOH   HOH A . 
C 3 HOH   3  1103 8  HOH   HOH A . 
C 3 HOH   4  1104 42 HOH   HOH A . 
C 3 HOH   5  1105 6  HOH   HOH A . 
C 3 HOH   6  1106 44 HOH   HOH A . 
C 3 HOH   7  1107 19 HOH   HOH A . 
C 3 HOH   8  1108 55 HOH   HOH A . 
C 3 HOH   9  1109 40 HOH   HOH A . 
C 3 HOH   10 1110 24 HOH   HOH A . 
C 3 HOH   11 1111 5  HOH   HOH A . 
C 3 HOH   12 1112 26 HOH   HOH A . 
C 3 HOH   13 1113 31 HOH   HOH A . 
C 3 HOH   14 1114 22 HOH   HOH A . 
C 3 HOH   15 1115 39 HOH   HOH A . 
C 3 HOH   16 1116 4  HOH   HOH A . 
C 3 HOH   17 1117 27 HOH   HOH A . 
C 3 HOH   18 1118 23 HOH   HOH A . 
C 3 HOH   19 1119 18 HOH   HOH A . 
C 3 HOH   20 1120 25 HOH   HOH A . 
C 3 HOH   21 1121 20 HOH   HOH A . 
C 3 HOH   22 1122 30 HOH   HOH A . 
C 3 HOH   23 1123 37 HOH   HOH A . 
C 3 HOH   24 1124 21 HOH   HOH A . 
C 3 HOH   25 1125 13 HOH   HOH A . 
C 3 HOH   26 1126 54 HOH   HOH A . 
C 3 HOH   27 1127 7  HOH   HOH A . 
C 3 HOH   28 1128 15 HOH   HOH A . 
C 3 HOH   29 1129 1  HOH   HOH A . 
C 3 HOH   30 1130 2  HOH   HOH A . 
C 3 HOH   31 1131 29 HOH   HOH A . 
C 3 HOH   32 1132 32 HOH   HOH A . 
C 3 HOH   33 1133 12 HOH   HOH A . 
C 3 HOH   34 1134 59 HOH   HOH A . 
C 3 HOH   35 1135 34 HOH   HOH A . 
C 3 HOH   36 1136 33 HOH   HOH A . 
C 3 HOH   37 1137 53 HOH   HOH A . 
C 3 HOH   38 1138 47 HOH   HOH A . 
C 3 HOH   39 1139 38 HOH   HOH A . 
C 3 HOH   40 1140 61 HOH   HOH A . 
C 3 HOH   41 1141 56 HOH   HOH A . 
C 3 HOH   42 1142 43 HOH   HOH A . 
C 3 HOH   43 1143 48 HOH   HOH A . 
C 3 HOH   44 1144 28 HOH   HOH A . 
C 3 HOH   45 1145 14 HOH   HOH A . 
C 3 HOH   46 1146 57 HOH   HOH A . 
C 3 HOH   47 1147 10 HOH   HOH A . 
C 3 HOH   48 1148 35 HOH   HOH A . 
C 3 HOH   49 1149 45 HOH   HOH A . 
C 3 HOH   50 1150 16 HOH   HOH A . 
C 3 HOH   51 1151 60 HOH   HOH A . 
C 3 HOH   52 1152 49 HOH   HOH A . 
C 3 HOH   53 1153 50 HOH   HOH A . 
C 3 HOH   54 1154 46 HOH   HOH A . 
C 3 HOH   55 1155 51 HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XRR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     53.970 
_cell.length_a_esd                 ? 
_cell.length_b                     72.990 
_cell.length_b_esd                 ? 
_cell.length_c                     99.550 
_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                         8XRR 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8XRR 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.93 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          58.03 
_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    '0.1 M HEPES, pH 7.5, 20% PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 S 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-12-25 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9785 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9785 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          57.95 
_reflns.entry_id                                       8XRR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.57 
_reflns.d_resolution_low                               36.59 
_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                                     13017 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                25.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          1.3 
_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                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.57 
_reflns_shell.d_res_low                                     2.64 
_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                             948 
_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                                  0.729 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8XRR 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.57 
_refine.ls_d_res_low                             36.59 
_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                     13017 
_refine.ls_number_reflns_R_free                  1303 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.75 
_refine.ls_percent_reflns_R_free                 10.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2383 
_refine.ls_R_factor_R_free                       0.2595 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2360 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      6A32 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 29.44 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.37 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.57 
_refine_hist.d_res_low                        36.59 
_refine_hist.number_atoms_solvent             55 
_refine_hist.number_atoms_total               2437 
_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        2352 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_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' ? 0.008  ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.096  ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.245 ? 898 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.048  ? 358 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 407 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.57 2.67 . . 142 1275 100.00 . . . . 0.3473 . . . . . . . . . . . 0.3473 
'X-RAY DIFFRACTION' 2.67 2.79 . . 141 1271 100.00 . . . . 0.3121 . . . . . . . . . . . 0.3999 
'X-RAY DIFFRACTION' 2.79 2.94 . . 143 1274 100.00 . . . . 0.2970 . . . . . . . . . . . 0.3155 
'X-RAY DIFFRACTION' 2.94 3.13 . . 144 1287 100.00 . . . . 0.2811 . . . . . . . . . . . 0.3183 
'X-RAY DIFFRACTION' 3.13 3.37 . . 143 1285 100.00 . . . . 0.2859 . . . . . . . . . . . 0.2927 
'X-RAY DIFFRACTION' 3.37 3.71 . . 140 1283 100.00 . . . . 0.2497 . . . . . . . . . . . 0.2878 
'X-RAY DIFFRACTION' 3.71 4.24 . . 146 1309 100.00 . . . . 0.2089 . . . . . . . . . . . 0.2326 
'X-RAY DIFFRACTION' 4.24 5.34 . . 148 1331 100.00 . . . . 0.1987 . . . . . . . . . . . 0.2087 
'X-RAY DIFFRACTION' 5.34 10.0 . . 156 1399 100.00 . . . . 0.2076 . . . . . . . . . . . 0.2358 
# 
_struct.entry_id                     8XRR 
_struct.title                        'A complex structure of PDGFRA with an inhibitor RH140' 
_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        8XRR 
_struct_keywords.text            'inhibitor, TRANSFERASE, TRANSFERASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   TRANSFERASE/INHIBITOR 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8XRR 
_struct_ref.pdbx_db_accession          8XRR 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8XRR 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 356 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             8XRR 
_struct_ref_seq.db_align_beg                  546 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  901 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       546 
_struct_ref_seq.pdbx_auth_seq_align_end       901 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 38  ? GLU A 42  ? ASP A 583 GLU A 587 5 ? 5  
HELX_P HELX_P2  AA2 PRO A 44  ? ASP A 46  ? PRO A 589 ASP A 591 5 ? 3  
HELX_P HELX_P3  AA3 SER A 92  ? GLY A 107 ? SER A 637 GLY A 652 1 ? 16 
HELX_P HELX_P4  AA4 LEU A 137 ? ASN A 144 ? LEU A 682 ASN A 689 1 ? 8  
HELX_P HELX_P5  AA5 THR A 174 ? LYS A 195 ? THR A 719 LYS A 740 1 ? 22 
HELX_P HELX_P6  AA6 ALA A 203 ? ARG A 205 ? ALA A 748 ARG A 750 5 ? 3  
HELX_P HELX_P7  AA7 PRO A 241 ? MET A 245 ? PRO A 786 MET A 790 5 ? 5  
HELX_P HELX_P8  AA8 ALA A 246 ? ASN A 253 ? ALA A 791 ASN A 798 1 ? 8  
HELX_P HELX_P9  AA9 THR A 256 ? PHE A 272 ? THR A 801 PHE A 817 1 ? 17 
HELX_P HELX_P10 AB1 ASP A 285 ? GLY A 295 ? ASP A 830 GLY A 840 1 ? 11 
HELX_P HELX_P11 AB2 THR A 305 ? TRP A 316 ? THR A 850 TRP A 861 1 ? 12 
HELX_P HELX_P12 AB3 GLU A 319 ? ARG A 323 ? GLU A 864 ARG A 868 5 ? 5  
HELX_P HELX_P13 AB4 SER A 325 ? LEU A 336 ? SER A 870 LEU A 881 1 ? 12 
HELX_P HELX_P14 AB5 PRO A 338 ? PHE A 352 ? PRO A 883 PHE A 897 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? 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 LEU A 48  ? GLY A 55  ? LEU A 593 GLY A 600 
AA1 2 LYS A 61  ? TYR A 68  ? LYS A 606 TYR A 613 
AA1 3 VAL A 76  ? MET A 83  ? VAL A 621 MET A 628 
AA1 4 TYR A 126 ? GLU A 130 ? TYR A 671 GLU A 675 
AA1 5 LEU A 115 ? CYS A 119 ? LEU A 660 CYS A 664 
AA2 1 GLY A 135 ? ASP A 136 ? GLY A 680 ASP A 681 
AA2 2 VAL A 207 ? ALA A 210 ? VAL A 752 ALA A 755 
AA2 3 ILE A 214 ? ILE A 217 ? ILE A 759 ILE A 762 
AA3 1 CYS A 197 ? VAL A 198 ? CYS A 742 VAL A 743 
AA3 2 ARG A 224 ? ASP A 225 ? ARG A 769 ASP A 770 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLY A 55  ? N GLY A 600 O VAL A 62  ? O VAL A 607 
AA1 2 3 N GLY A 65  ? N GLY A 610 O VAL A 79  ? O VAL A 624 
AA1 3 4 N ALA A 80  ? N ALA A 625 O ILE A 129 ? O ILE A 674 
AA1 4 5 O ILE A 128 ? O ILE A 673 N LEU A 116 ? N LEU A 661 
AA2 1 2 N GLY A 135 ? N GLY A 680 O LEU A 209 ? O LEU A 754 
AA2 2 3 N LEU A 208 ? N LEU A 753 O LYS A 216 ? O LYS A 761 
AA3 1 2 N VAL A 198 ? N VAL A 743 O ARG A 224 ? O ARG A 769 
# 
_pdbx_entry_details.entry_id                   8XRR 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 746 ? ? -149.54 44.62 
2 1 ASP A 764 ? ? 60.75   77.27 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       1155 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.83 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 546 ? A GLY 1   
2  1 Y 1 A ALA 547 ? A ALA 2   
3  1 Y 1 A MET 548 ? A MET 3   
4  1 Y 1 A ASP 549 ? A ASP 4   
5  1 Y 1 A LYS 550 ? A LYS 5   
6  1 Y 1 A GLN 551 ? A GLN 6   
7  1 Y 1 A LYS 552 ? A LYS 7   
8  1 Y 1 A PRO 553 ? A PRO 8   
9  1 Y 1 A ARG 554 ? A ARG 9   
10 1 Y 1 A TYR 555 ? A TYR 10  
11 1 Y 1 A GLU 556 ? A GLU 11  
12 1 Y 1 A ILE 557 ? A ILE 12  
13 1 Y 1 A ARG 558 ? A ARG 13  
14 1 Y 1 A TRP 559 ? A TRP 14  
15 1 Y 1 A ARG 560 ? A ARG 15  
16 1 Y 1 A VAL 561 ? A VAL 16  
17 1 Y 1 A ILE 562 ? A ILE 17  
18 1 Y 1 A GLU 563 ? A GLU 18  
19 1 Y 1 A SER 564 ? A SER 19  
20 1 Y 1 A ILE 565 ? A ILE 20  
21 1 Y 1 A SER 566 ? A SER 21  
22 1 Y 1 A PRO 567 ? A PRO 22  
23 1 Y 1 A ASP 568 ? A ASP 23  
24 1 Y 1 A ALA 633 ? A ALA 88  
25 1 Y 1 A ARG 634 ? A ARG 89  
26 1 Y 1 A SER 635 ? A SER 90  
27 1 Y 1 A SER 695 ? A SER 150 
28 1 Y 1 A HIS 696 ? A HIS 151 
29 1 Y 1 A LYS 697 ? A LYS 152 
30 1 Y 1 A LYS 698 ? A LYS 153 
31 1 Y 1 A LYS 699 ? A LYS 154 
32 1 Y 1 A SER 700 ? A SER 155 
33 1 Y 1 A MET 701 ? A MET 156 
34 1 Y 1 A LEU 702 ? A LEU 157 
35 1 Y 1 A ASP 703 ? A ASP 158 
36 1 Y 1 A SER 704 ? A SER 159 
37 1 Y 1 A GLU 705 ? A GLU 160 
38 1 Y 1 A VAL 706 ? A VAL 161 
39 1 Y 1 A LYS 707 ? A LYS 162 
40 1 Y 1 A ASN 708 ? A ASN 163 
41 1 Y 1 A LEU 709 ? A LEU 164 
42 1 Y 1 A LEU 710 ? A LEU 165 
43 1 Y 1 A SER 711 ? A SER 166 
44 1 Y 1 A ASP 712 ? A ASP 167 
45 1 Y 1 A ASP 713 ? A ASP 168 
46 1 Y 1 A ASN 714 ? A ASN 169 
47 1 Y 1 A SER 715 ? A SER 170 
48 1 Y 1 A GLU 716 ? A GLU 171 
49 1 Y 1 A MET 772 ? A MET 227 
50 1 Y 1 A HIS 773 ? A HIS 228 
51 1 Y 1 A ASP 774 ? A ASP 229 
52 1 Y 1 A SER 775 ? A SER 230 
53 1 Y 1 A ASN 776 ? A ASN 231 
54 1 Y 1 A TYR 777 ? A TYR 232 
55 1 Y 1 A VAL 778 ? A VAL 233 
56 1 Y 1 A SER 779 ? A SER 234 
57 1 Y 1 A LYS 780 ? A LYS 235 
58 1 Y 1 A GLY 781 ? A GLY 236 
59 1 Y 1 A SER 782 ? A SER 237 
60 1 Y 1 A LYS 899 ? A LYS 354 
61 1 Y 1 A SER 900 ? A SER 355 
62 1 Y 1 A ASP 901 ? A ASP 356 
# 
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 
A1LV8 C14  C Y N 1   
A1LV8 C10  C Y N 2   
A1LV8 C12  C Y N 3   
A1LV8 C01  C Y N 4   
A1LV8 C02  C Y N 5   
A1LV8 C03  C Y N 6   
A1LV8 C04  C Y N 7   
A1LV8 C06  C Y N 8   
A1LV8 C07  C Y N 9   
A1LV8 C08  C Y N 10  
A1LV8 C09  C Y N 11  
A1LV8 C15  C Y N 12  
A1LV8 C16  C Y N 13  
A1LV8 C17  C Y N 14  
A1LV8 C18  C Y N 15  
A1LV8 C19  C Y N 16  
A1LV8 C21  C N N 17  
A1LV8 C22  C N N 18  
A1LV8 C23  C N N 19  
A1LV8 C25  C N N 20  
A1LV8 C26  C N N 21  
A1LV8 C27  C N N 22  
A1LV8 C29  C N N 23  
A1LV8 C30  C N N 24  
A1LV8 N05  N Y N 25  
A1LV8 N11  N Y N 26  
A1LV8 N13  N Y N 27  
A1LV8 N24  N N N 28  
A1LV8 N28  N N N 29  
A1LV8 O20  O N N 30  
A1LV8 H1   H N N 31  
A1LV8 H2   H N N 32  
A1LV8 H3   H N N 33  
A1LV8 H4   H N N 34  
A1LV8 H5   H N N 35  
A1LV8 H6   H N N 36  
A1LV8 H7   H N N 37  
A1LV8 H8   H N N 38  
A1LV8 H9   H N N 39  
A1LV8 H10  H N N 40  
A1LV8 H11  H N N 41  
A1LV8 H12  H N N 42  
A1LV8 H13  H N N 43  
A1LV8 H14  H N N 44  
A1LV8 H15  H N N 45  
A1LV8 H16  H N N 46  
A1LV8 H17  H N N 47  
A1LV8 H18  H N N 48  
A1LV8 H19  H N N 49  
A1LV8 H20  H N N 50  
A1LV8 H21  H N N 51  
A1LV8 H22  H N N 52  
A1LV8 H23  H N N 53  
A1LV8 H24  H N N 54  
A1LV8 H25  H N N 55  
ALA   N    N N N 56  
ALA   CA   C N S 57  
ALA   C    C N N 58  
ALA   O    O N N 59  
ALA   CB   C N N 60  
ALA   OXT  O N N 61  
ALA   H    H N N 62  
ALA   H2   H N N 63  
ALA   HA   H N N 64  
ALA   HB1  H N N 65  
ALA   HB2  H N N 66  
ALA   HB3  H N N 67  
ALA   HXT  H N N 68  
ARG   N    N N N 69  
ARG   CA   C N S 70  
ARG   C    C N N 71  
ARG   O    O N N 72  
ARG   CB   C N N 73  
ARG   CG   C N N 74  
ARG   CD   C N N 75  
ARG   NE   N N N 76  
ARG   CZ   C N N 77  
ARG   NH1  N N N 78  
ARG   NH2  N N N 79  
ARG   OXT  O N N 80  
ARG   H    H N N 81  
ARG   H2   H N N 82  
ARG   HA   H N N 83  
ARG   HB2  H N N 84  
ARG   HB3  H N N 85  
ARG   HG2  H N N 86  
ARG   HG3  H N N 87  
ARG   HD2  H N N 88  
ARG   HD3  H N N 89  
ARG   HE   H N N 90  
ARG   HH11 H N N 91  
ARG   HH12 H N N 92  
ARG   HH21 H N N 93  
ARG   HH22 H N N 94  
ARG   HXT  H N N 95  
ASN   N    N N N 96  
ASN   CA   C N S 97  
ASN   C    C N N 98  
ASN   O    O N N 99  
ASN   CB   C N N 100 
ASN   CG   C N N 101 
ASN   OD1  O N N 102 
ASN   ND2  N N N 103 
ASN   OXT  O N N 104 
ASN   H    H N N 105 
ASN   H2   H N N 106 
ASN   HA   H N N 107 
ASN   HB2  H N N 108 
ASN   HB3  H N N 109 
ASN   HD21 H N N 110 
ASN   HD22 H N N 111 
ASN   HXT  H N N 112 
ASP   N    N N N 113 
ASP   CA   C N S 114 
ASP   C    C N N 115 
ASP   O    O N N 116 
ASP   CB   C N N 117 
ASP   CG   C N N 118 
ASP   OD1  O N N 119 
ASP   OD2  O N N 120 
ASP   OXT  O N N 121 
ASP   H    H N N 122 
ASP   H2   H N N 123 
ASP   HA   H N N 124 
ASP   HB2  H N N 125 
ASP   HB3  H N N 126 
ASP   HD2  H N N 127 
ASP   HXT  H N N 128 
CYS   N    N N N 129 
CYS   CA   C N R 130 
CYS   C    C N N 131 
CYS   O    O N N 132 
CYS   CB   C N N 133 
CYS   SG   S N N 134 
CYS   OXT  O N N 135 
CYS   H    H N N 136 
CYS   H2   H N N 137 
CYS   HA   H N N 138 
CYS   HB2  H N N 139 
CYS   HB3  H N N 140 
CYS   HG   H N N 141 
CYS   HXT  H N N 142 
GLN   N    N N N 143 
GLN   CA   C N S 144 
GLN   C    C N N 145 
GLN   O    O N N 146 
GLN   CB   C N N 147 
GLN   CG   C N N 148 
GLN   CD   C N N 149 
GLN   OE1  O N N 150 
GLN   NE2  N N N 151 
GLN   OXT  O N N 152 
GLN   H    H N N 153 
GLN   H2   H N N 154 
GLN   HA   H N N 155 
GLN   HB2  H N N 156 
GLN   HB3  H N N 157 
GLN   HG2  H N N 158 
GLN   HG3  H N N 159 
GLN   HE21 H N N 160 
GLN   HE22 H N N 161 
GLN   HXT  H N N 162 
GLU   N    N N N 163 
GLU   CA   C N S 164 
GLU   C    C N N 165 
GLU   O    O N N 166 
GLU   CB   C N N 167 
GLU   CG   C N N 168 
GLU   CD   C N N 169 
GLU   OE1  O N N 170 
GLU   OE2  O N N 171 
GLU   OXT  O N N 172 
GLU   H    H N N 173 
GLU   H2   H N N 174 
GLU   HA   H N N 175 
GLU   HB2  H N N 176 
GLU   HB3  H N N 177 
GLU   HG2  H N N 178 
GLU   HG3  H N N 179 
GLU   HE2  H N N 180 
GLU   HXT  H N N 181 
GLY   N    N N N 182 
GLY   CA   C N N 183 
GLY   C    C N N 184 
GLY   O    O N N 185 
GLY   OXT  O N N 186 
GLY   H    H N N 187 
GLY   H2   H N N 188 
GLY   HA2  H N N 189 
GLY   HA3  H N N 190 
GLY   HXT  H N N 191 
HIS   N    N N N 192 
HIS   CA   C N S 193 
HIS   C    C N N 194 
HIS   O    O N N 195 
HIS   CB   C N N 196 
HIS   CG   C Y N 197 
HIS   ND1  N Y N 198 
HIS   CD2  C Y N 199 
HIS   CE1  C Y N 200 
HIS   NE2  N Y N 201 
HIS   OXT  O N N 202 
HIS   H    H N N 203 
HIS   H2   H N N 204 
HIS   HA   H N N 205 
HIS   HB2  H N N 206 
HIS   HB3  H N N 207 
HIS   HD1  H N N 208 
HIS   HD2  H N N 209 
HIS   HE1  H N N 210 
HIS   HE2  H N N 211 
HIS   HXT  H N N 212 
HOH   O    O N N 213 
HOH   H1   H N N 214 
HOH   H2   H N N 215 
ILE   N    N N N 216 
ILE   CA   C N S 217 
ILE   C    C N N 218 
ILE   O    O N N 219 
ILE   CB   C N S 220 
ILE   CG1  C N N 221 
ILE   CG2  C N N 222 
ILE   CD1  C N N 223 
ILE   OXT  O N N 224 
ILE   H    H N N 225 
ILE   H2   H N N 226 
ILE   HA   H N N 227 
ILE   HB   H N N 228 
ILE   HG12 H N N 229 
ILE   HG13 H N N 230 
ILE   HG21 H N N 231 
ILE   HG22 H N N 232 
ILE   HG23 H N N 233 
ILE   HD11 H N N 234 
ILE   HD12 H N N 235 
ILE   HD13 H N N 236 
ILE   HXT  H N N 237 
LEU   N    N N N 238 
LEU   CA   C N S 239 
LEU   C    C N N 240 
LEU   O    O N N 241 
LEU   CB   C N N 242 
LEU   CG   C N N 243 
LEU   CD1  C N N 244 
LEU   CD2  C N N 245 
LEU   OXT  O N N 246 
LEU   H    H N N 247 
LEU   H2   H N N 248 
LEU   HA   H N N 249 
LEU   HB2  H N N 250 
LEU   HB3  H N N 251 
LEU   HG   H N N 252 
LEU   HD11 H N N 253 
LEU   HD12 H N N 254 
LEU   HD13 H N N 255 
LEU   HD21 H N N 256 
LEU   HD22 H N N 257 
LEU   HD23 H N N 258 
LEU   HXT  H N N 259 
LYS   N    N N N 260 
LYS   CA   C N S 261 
LYS   C    C N N 262 
LYS   O    O N N 263 
LYS   CB   C N N 264 
LYS   CG   C N N 265 
LYS   CD   C N N 266 
LYS   CE   C N N 267 
LYS   NZ   N N N 268 
LYS   OXT  O N N 269 
LYS   H    H N N 270 
LYS   H2   H N N 271 
LYS   HA   H N N 272 
LYS   HB2  H N N 273 
LYS   HB3  H N N 274 
LYS   HG2  H N N 275 
LYS   HG3  H N N 276 
LYS   HD2  H N N 277 
LYS   HD3  H N N 278 
LYS   HE2  H N N 279 
LYS   HE3  H N N 280 
LYS   HZ1  H N N 281 
LYS   HZ2  H N N 282 
LYS   HZ3  H N N 283 
LYS   HXT  H N N 284 
MET   N    N N N 285 
MET   CA   C N S 286 
MET   C    C N N 287 
MET   O    O N N 288 
MET   CB   C N N 289 
MET   CG   C N N 290 
MET   SD   S N N 291 
MET   CE   C N N 292 
MET   OXT  O N N 293 
MET   H    H N N 294 
MET   H2   H N N 295 
MET   HA   H N N 296 
MET   HB2  H N N 297 
MET   HB3  H N N 298 
MET   HG2  H N N 299 
MET   HG3  H N N 300 
MET   HE1  H N N 301 
MET   HE2  H N N 302 
MET   HE3  H N N 303 
MET   HXT  H N N 304 
PHE   N    N N N 305 
PHE   CA   C N S 306 
PHE   C    C N N 307 
PHE   O    O N N 308 
PHE   CB   C N N 309 
PHE   CG   C Y N 310 
PHE   CD1  C Y N 311 
PHE   CD2  C Y N 312 
PHE   CE1  C Y N 313 
PHE   CE2  C Y N 314 
PHE   CZ   C Y N 315 
PHE   OXT  O N N 316 
PHE   H    H N N 317 
PHE   H2   H N N 318 
PHE   HA   H N N 319 
PHE   HB2  H N N 320 
PHE   HB3  H N N 321 
PHE   HD1  H N N 322 
PHE   HD2  H N N 323 
PHE   HE1  H N N 324 
PHE   HE2  H N N 325 
PHE   HZ   H N N 326 
PHE   HXT  H N N 327 
PRO   N    N N N 328 
PRO   CA   C N S 329 
PRO   C    C N N 330 
PRO   O    O N N 331 
PRO   CB   C N N 332 
PRO   CG   C N N 333 
PRO   CD   C N N 334 
PRO   OXT  O N N 335 
PRO   H    H N N 336 
PRO   HA   H N N 337 
PRO   HB2  H N N 338 
PRO   HB3  H N N 339 
PRO   HG2  H N N 340 
PRO   HG3  H N N 341 
PRO   HD2  H N N 342 
PRO   HD3  H N N 343 
PRO   HXT  H N N 344 
SER   N    N N N 345 
SER   CA   C N S 346 
SER   C    C N N 347 
SER   O    O N N 348 
SER   CB   C N N 349 
SER   OG   O N N 350 
SER   OXT  O N N 351 
SER   H    H N N 352 
SER   H2   H N N 353 
SER   HA   H N N 354 
SER   HB2  H N N 355 
SER   HB3  H N N 356 
SER   HG   H N N 357 
SER   HXT  H N N 358 
THR   N    N N N 359 
THR   CA   C N S 360 
THR   C    C N N 361 
THR   O    O N N 362 
THR   CB   C N R 363 
THR   OG1  O N N 364 
THR   CG2  C N N 365 
THR   OXT  O N N 366 
THR   H    H N N 367 
THR   H2   H N N 368 
THR   HA   H N N 369 
THR   HB   H N N 370 
THR   HG1  H N N 371 
THR   HG21 H N N 372 
THR   HG22 H N N 373 
THR   HG23 H N N 374 
THR   HXT  H N N 375 
TRP   N    N N N 376 
TRP   CA   C N S 377 
TRP   C    C N N 378 
TRP   O    O N N 379 
TRP   CB   C N N 380 
TRP   CG   C Y N 381 
TRP   CD1  C Y N 382 
TRP   CD2  C Y N 383 
TRP   NE1  N Y N 384 
TRP   CE2  C Y N 385 
TRP   CE3  C Y N 386 
TRP   CZ2  C Y N 387 
TRP   CZ3  C Y N 388 
TRP   CH2  C Y N 389 
TRP   OXT  O N N 390 
TRP   H    H N N 391 
TRP   H2   H N N 392 
TRP   HA   H N N 393 
TRP   HB2  H N N 394 
TRP   HB3  H N N 395 
TRP   HD1  H N N 396 
TRP   HE1  H N N 397 
TRP   HE3  H N N 398 
TRP   HZ2  H N N 399 
TRP   HZ3  H N N 400 
TRP   HH2  H N N 401 
TRP   HXT  H N N 402 
TYR   N    N N N 403 
TYR   CA   C N S 404 
TYR   C    C N N 405 
TYR   O    O N N 406 
TYR   CB   C N N 407 
TYR   CG   C Y N 408 
TYR   CD1  C Y N 409 
TYR   CD2  C Y N 410 
TYR   CE1  C Y N 411 
TYR   CE2  C Y N 412 
TYR   CZ   C Y N 413 
TYR   OH   O N N 414 
TYR   OXT  O N N 415 
TYR   H    H N N 416 
TYR   H2   H N N 417 
TYR   HA   H N N 418 
TYR   HB2  H N N 419 
TYR   HB3  H N N 420 
TYR   HD1  H N N 421 
TYR   HD2  H N N 422 
TYR   HE1  H N N 423 
TYR   HE2  H N N 424 
TYR   HH   H N N 425 
TYR   HXT  H N N 426 
VAL   N    N N N 427 
VAL   CA   C N S 428 
VAL   C    C N N 429 
VAL   O    O N N 430 
VAL   CB   C N N 431 
VAL   CG1  C N N 432 
VAL   CG2  C N N 433 
VAL   OXT  O N N 434 
VAL   H    H N N 435 
VAL   H2   H N N 436 
VAL   HA   H N N 437 
VAL   HB   H N N 438 
VAL   HG11 H N N 439 
VAL   HG12 H N N 440 
VAL   HG13 H N N 441 
VAL   HG21 H N N 442 
VAL   HG22 H N N 443 
VAL   HG23 H N N 444 
VAL   HXT  H N N 445 
# 
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 
A1LV8 N13 C12  doub Y N 1   
A1LV8 N13 C14  sing Y N 2   
A1LV8 C07 C08  doub Y N 3   
A1LV8 C07 C06  sing Y N 4   
A1LV8 C12 N11  sing Y N 5   
A1LV8 C08 C09  sing Y N 6   
A1LV8 C14 C15  doub Y N 7   
A1LV8 C14 C19  sing Y N 8   
A1LV8 C15 C16  sing Y N 9   
A1LV8 N11 C19  sing Y N 10  
A1LV8 N11 C06  sing N N 11  
A1LV8 C19 C18  doub Y N 12  
A1LV8 C06 N05  doub Y N 13  
A1LV8 C16 C17  doub Y N 14  
A1LV8 C18 C17  sing Y N 15  
A1LV8 C09 C10  doub Y N 16  
A1LV8 C09 C04  sing Y N 17  
A1LV8 C17 O20  sing N N 18  
A1LV8 C10 C01  sing Y N 19  
A1LV8 N05 C04  sing Y N 20  
A1LV8 O20 C21  sing N N 21  
A1LV8 C04 C03  doub Y N 22  
A1LV8 C01 C02  doub Y N 23  
A1LV8 C21 C22  sing N N 24  
A1LV8 C03 C02  sing Y N 25  
A1LV8 C03 N28  sing N N 26  
A1LV8 C27 N28  sing N N 27  
A1LV8 C27 C26  sing N N 28  
A1LV8 N28 C29  sing N N 29  
A1LV8 C26 C25  sing N N 30  
A1LV8 C23 C22  sing N N 31  
A1LV8 C23 N24  sing N N 32  
A1LV8 C29 C30  sing N N 33  
A1LV8 C30 C25  sing N N 34  
A1LV8 C25 N24  sing N N 35  
A1LV8 C10 H1   sing N N 36  
A1LV8 C12 H2   sing N N 37  
A1LV8 C01 H3   sing N N 38  
A1LV8 C02 H4   sing N N 39  
A1LV8 C07 H5   sing N N 40  
A1LV8 C08 H6   sing N N 41  
A1LV8 C15 H7   sing N N 42  
A1LV8 C16 H8   sing N N 43  
A1LV8 C18 H9   sing N N 44  
A1LV8 C21 H10  sing N N 45  
A1LV8 C21 H11  sing N N 46  
A1LV8 C22 H12  sing N N 47  
A1LV8 C22 H13  sing N N 48  
A1LV8 C23 H14  sing N N 49  
A1LV8 C23 H15  sing N N 50  
A1LV8 C25 H16  sing N N 51  
A1LV8 C26 H17  sing N N 52  
A1LV8 C26 H18  sing N N 53  
A1LV8 C27 H19  sing N N 54  
A1LV8 C27 H20  sing N N 55  
A1LV8 C29 H21  sing N N 56  
A1LV8 C29 H22  sing N N 57  
A1LV8 C30 H23  sing N N 58  
A1LV8 C30 H24  sing N N 59  
A1LV8 N24 H25  sing N N 60  
ALA   N   CA   sing N N 61  
ALA   N   H    sing N N 62  
ALA   N   H2   sing N N 63  
ALA   CA  C    sing N N 64  
ALA   CA  CB   sing N N 65  
ALA   CA  HA   sing N N 66  
ALA   C   O    doub N N 67  
ALA   C   OXT  sing N N 68  
ALA   CB  HB1  sing N N 69  
ALA   CB  HB2  sing N N 70  
ALA   CB  HB3  sing N N 71  
ALA   OXT HXT  sing N N 72  
ARG   N   CA   sing N N 73  
ARG   N   H    sing N N 74  
ARG   N   H2   sing N N 75  
ARG   CA  C    sing N N 76  
ARG   CA  CB   sing N N 77  
ARG   CA  HA   sing N N 78  
ARG   C   O    doub N N 79  
ARG   C   OXT  sing N N 80  
ARG   CB  CG   sing N N 81  
ARG   CB  HB2  sing N N 82  
ARG   CB  HB3  sing N N 83  
ARG   CG  CD   sing N N 84  
ARG   CG  HG2  sing N N 85  
ARG   CG  HG3  sing N N 86  
ARG   CD  NE   sing N N 87  
ARG   CD  HD2  sing N N 88  
ARG   CD  HD3  sing N N 89  
ARG   NE  CZ   sing N N 90  
ARG   NE  HE   sing N N 91  
ARG   CZ  NH1  sing N N 92  
ARG   CZ  NH2  doub N N 93  
ARG   NH1 HH11 sing N N 94  
ARG   NH1 HH12 sing N N 95  
ARG   NH2 HH21 sing N N 96  
ARG   NH2 HH22 sing N N 97  
ARG   OXT HXT  sing N N 98  
ASN   N   CA   sing N N 99  
ASN   N   H    sing N N 100 
ASN   N   H2   sing N N 101 
ASN   CA  C    sing N N 102 
ASN   CA  CB   sing N N 103 
ASN   CA  HA   sing N N 104 
ASN   C   O    doub N N 105 
ASN   C   OXT  sing N N 106 
ASN   CB  CG   sing N N 107 
ASN   CB  HB2  sing N N 108 
ASN   CB  HB3  sing N N 109 
ASN   CG  OD1  doub N N 110 
ASN   CG  ND2  sing N N 111 
ASN   ND2 HD21 sing N N 112 
ASN   ND2 HD22 sing N N 113 
ASN   OXT HXT  sing N N 114 
ASP   N   CA   sing N N 115 
ASP   N   H    sing N N 116 
ASP   N   H2   sing N N 117 
ASP   CA  C    sing N N 118 
ASP   CA  CB   sing N N 119 
ASP   CA  HA   sing N N 120 
ASP   C   O    doub N N 121 
ASP   C   OXT  sing N N 122 
ASP   CB  CG   sing N N 123 
ASP   CB  HB2  sing N N 124 
ASP   CB  HB3  sing N N 125 
ASP   CG  OD1  doub N N 126 
ASP   CG  OD2  sing N N 127 
ASP   OD2 HD2  sing N N 128 
ASP   OXT HXT  sing N N 129 
CYS   N   CA   sing N N 130 
CYS   N   H    sing N N 131 
CYS   N   H2   sing N N 132 
CYS   CA  C    sing N N 133 
CYS   CA  CB   sing N N 134 
CYS   CA  HA   sing N N 135 
CYS   C   O    doub N N 136 
CYS   C   OXT  sing N N 137 
CYS   CB  SG   sing N N 138 
CYS   CB  HB2  sing N N 139 
CYS   CB  HB3  sing N N 140 
CYS   SG  HG   sing N N 141 
CYS   OXT HXT  sing N N 142 
GLN   N   CA   sing N N 143 
GLN   N   H    sing N N 144 
GLN   N   H2   sing N N 145 
GLN   CA  C    sing N N 146 
GLN   CA  CB   sing N N 147 
GLN   CA  HA   sing N N 148 
GLN   C   O    doub N N 149 
GLN   C   OXT  sing N N 150 
GLN   CB  CG   sing N N 151 
GLN   CB  HB2  sing N N 152 
GLN   CB  HB3  sing N N 153 
GLN   CG  CD   sing N N 154 
GLN   CG  HG2  sing N N 155 
GLN   CG  HG3  sing N N 156 
GLN   CD  OE1  doub N N 157 
GLN   CD  NE2  sing N N 158 
GLN   NE2 HE21 sing N N 159 
GLN   NE2 HE22 sing N N 160 
GLN   OXT HXT  sing N N 161 
GLU   N   CA   sing N N 162 
GLU   N   H    sing N N 163 
GLU   N   H2   sing N N 164 
GLU   CA  C    sing N N 165 
GLU   CA  CB   sing N N 166 
GLU   CA  HA   sing N N 167 
GLU   C   O    doub N N 168 
GLU   C   OXT  sing N N 169 
GLU   CB  CG   sing N N 170 
GLU   CB  HB2  sing N N 171 
GLU   CB  HB3  sing N N 172 
GLU   CG  CD   sing N N 173 
GLU   CG  HG2  sing N N 174 
GLU   CG  HG3  sing N N 175 
GLU   CD  OE1  doub N N 176 
GLU   CD  OE2  sing N N 177 
GLU   OE2 HE2  sing N N 178 
GLU   OXT HXT  sing N N 179 
GLY   N   CA   sing N N 180 
GLY   N   H    sing N N 181 
GLY   N   H2   sing N N 182 
GLY   CA  C    sing N N 183 
GLY   CA  HA2  sing N N 184 
GLY   CA  HA3  sing N N 185 
GLY   C   O    doub N N 186 
GLY   C   OXT  sing N N 187 
GLY   OXT HXT  sing N N 188 
HIS   N   CA   sing N N 189 
HIS   N   H    sing N N 190 
HIS   N   H2   sing N N 191 
HIS   CA  C    sing N N 192 
HIS   CA  CB   sing N N 193 
HIS   CA  HA   sing N N 194 
HIS   C   O    doub N N 195 
HIS   C   OXT  sing N N 196 
HIS   CB  CG   sing N N 197 
HIS   CB  HB2  sing N N 198 
HIS   CB  HB3  sing N N 199 
HIS   CG  ND1  sing Y N 200 
HIS   CG  CD2  doub Y N 201 
HIS   ND1 CE1  doub Y N 202 
HIS   ND1 HD1  sing N N 203 
HIS   CD2 NE2  sing Y N 204 
HIS   CD2 HD2  sing N N 205 
HIS   CE1 NE2  sing Y N 206 
HIS   CE1 HE1  sing N N 207 
HIS   NE2 HE2  sing N N 208 
HIS   OXT HXT  sing N N 209 
HOH   O   H1   sing N N 210 
HOH   O   H2   sing N N 211 
ILE   N   CA   sing N N 212 
ILE   N   H    sing N N 213 
ILE   N   H2   sing N N 214 
ILE   CA  C    sing N N 215 
ILE   CA  CB   sing N N 216 
ILE   CA  HA   sing N N 217 
ILE   C   O    doub N N 218 
ILE   C   OXT  sing N N 219 
ILE   CB  CG1  sing N N 220 
ILE   CB  CG2  sing N N 221 
ILE   CB  HB   sing N N 222 
ILE   CG1 CD1  sing N N 223 
ILE   CG1 HG12 sing N N 224 
ILE   CG1 HG13 sing N N 225 
ILE   CG2 HG21 sing N N 226 
ILE   CG2 HG22 sing N N 227 
ILE   CG2 HG23 sing N N 228 
ILE   CD1 HD11 sing N N 229 
ILE   CD1 HD12 sing N N 230 
ILE   CD1 HD13 sing N N 231 
ILE   OXT HXT  sing N N 232 
LEU   N   CA   sing N N 233 
LEU   N   H    sing N N 234 
LEU   N   H2   sing N N 235 
LEU   CA  C    sing N N 236 
LEU   CA  CB   sing N N 237 
LEU   CA  HA   sing N N 238 
LEU   C   O    doub N N 239 
LEU   C   OXT  sing N N 240 
LEU   CB  CG   sing N N 241 
LEU   CB  HB2  sing N N 242 
LEU   CB  HB3  sing N N 243 
LEU   CG  CD1  sing N N 244 
LEU   CG  CD2  sing N N 245 
LEU   CG  HG   sing N N 246 
LEU   CD1 HD11 sing N N 247 
LEU   CD1 HD12 sing N N 248 
LEU   CD1 HD13 sing N N 249 
LEU   CD2 HD21 sing N N 250 
LEU   CD2 HD22 sing N N 251 
LEU   CD2 HD23 sing N N 252 
LEU   OXT HXT  sing N N 253 
LYS   N   CA   sing N N 254 
LYS   N   H    sing N N 255 
LYS   N   H2   sing N N 256 
LYS   CA  C    sing N N 257 
LYS   CA  CB   sing N N 258 
LYS   CA  HA   sing N N 259 
LYS   C   O    doub N N 260 
LYS   C   OXT  sing N N 261 
LYS   CB  CG   sing N N 262 
LYS   CB  HB2  sing N N 263 
LYS   CB  HB3  sing N N 264 
LYS   CG  CD   sing N N 265 
LYS   CG  HG2  sing N N 266 
LYS   CG  HG3  sing N N 267 
LYS   CD  CE   sing N N 268 
LYS   CD  HD2  sing N N 269 
LYS   CD  HD3  sing N N 270 
LYS   CE  NZ   sing N N 271 
LYS   CE  HE2  sing N N 272 
LYS   CE  HE3  sing N N 273 
LYS   NZ  HZ1  sing N N 274 
LYS   NZ  HZ2  sing N N 275 
LYS   NZ  HZ3  sing N N 276 
LYS   OXT HXT  sing N N 277 
MET   N   CA   sing N N 278 
MET   N   H    sing N N 279 
MET   N   H2   sing N N 280 
MET   CA  C    sing N N 281 
MET   CA  CB   sing N N 282 
MET   CA  HA   sing N N 283 
MET   C   O    doub N N 284 
MET   C   OXT  sing N N 285 
MET   CB  CG   sing N N 286 
MET   CB  HB2  sing N N 287 
MET   CB  HB3  sing N N 288 
MET   CG  SD   sing N N 289 
MET   CG  HG2  sing N N 290 
MET   CG  HG3  sing N N 291 
MET   SD  CE   sing N N 292 
MET   CE  HE1  sing N N 293 
MET   CE  HE2  sing N N 294 
MET   CE  HE3  sing N N 295 
MET   OXT HXT  sing N N 296 
PHE   N   CA   sing N N 297 
PHE   N   H    sing N N 298 
PHE   N   H2   sing N N 299 
PHE   CA  C    sing N N 300 
PHE   CA  CB   sing N N 301 
PHE   CA  HA   sing N N 302 
PHE   C   O    doub N N 303 
PHE   C   OXT  sing N N 304 
PHE   CB  CG   sing N N 305 
PHE   CB  HB2  sing N N 306 
PHE   CB  HB3  sing N N 307 
PHE   CG  CD1  doub Y N 308 
PHE   CG  CD2  sing Y N 309 
PHE   CD1 CE1  sing Y N 310 
PHE   CD1 HD1  sing N N 311 
PHE   CD2 CE2  doub Y N 312 
PHE   CD2 HD2  sing N N 313 
PHE   CE1 CZ   doub Y N 314 
PHE   CE1 HE1  sing N N 315 
PHE   CE2 CZ   sing Y N 316 
PHE   CE2 HE2  sing N N 317 
PHE   CZ  HZ   sing N N 318 
PHE   OXT HXT  sing N N 319 
PRO   N   CA   sing N N 320 
PRO   N   CD   sing N N 321 
PRO   N   H    sing N N 322 
PRO   CA  C    sing N N 323 
PRO   CA  CB   sing N N 324 
PRO   CA  HA   sing N N 325 
PRO   C   O    doub N N 326 
PRO   C   OXT  sing N N 327 
PRO   CB  CG   sing N N 328 
PRO   CB  HB2  sing N N 329 
PRO   CB  HB3  sing N N 330 
PRO   CG  CD   sing N N 331 
PRO   CG  HG2  sing N N 332 
PRO   CG  HG3  sing N N 333 
PRO   CD  HD2  sing N N 334 
PRO   CD  HD3  sing N N 335 
PRO   OXT HXT  sing N N 336 
SER   N   CA   sing N N 337 
SER   N   H    sing N N 338 
SER   N   H2   sing N N 339 
SER   CA  C    sing N N 340 
SER   CA  CB   sing N N 341 
SER   CA  HA   sing N N 342 
SER   C   O    doub N N 343 
SER   C   OXT  sing N N 344 
SER   CB  OG   sing N N 345 
SER   CB  HB2  sing N N 346 
SER   CB  HB3  sing N N 347 
SER   OG  HG   sing N N 348 
SER   OXT HXT  sing N N 349 
THR   N   CA   sing N N 350 
THR   N   H    sing N N 351 
THR   N   H2   sing N N 352 
THR   CA  C    sing N N 353 
THR   CA  CB   sing N N 354 
THR   CA  HA   sing N N 355 
THR   C   O    doub N N 356 
THR   C   OXT  sing N N 357 
THR   CB  OG1  sing N N 358 
THR   CB  CG2  sing N N 359 
THR   CB  HB   sing N N 360 
THR   OG1 HG1  sing N N 361 
THR   CG2 HG21 sing N N 362 
THR   CG2 HG22 sing N N 363 
THR   CG2 HG23 sing N N 364 
THR   OXT HXT  sing N N 365 
TRP   N   CA   sing N N 366 
TRP   N   H    sing N N 367 
TRP   N   H2   sing N N 368 
TRP   CA  C    sing N N 369 
TRP   CA  CB   sing N N 370 
TRP   CA  HA   sing N N 371 
TRP   C   O    doub N N 372 
TRP   C   OXT  sing N N 373 
TRP   CB  CG   sing N N 374 
TRP   CB  HB2  sing N N 375 
TRP   CB  HB3  sing N N 376 
TRP   CG  CD1  doub Y N 377 
TRP   CG  CD2  sing Y N 378 
TRP   CD1 NE1  sing Y N 379 
TRP   CD1 HD1  sing N N 380 
TRP   CD2 CE2  doub Y N 381 
TRP   CD2 CE3  sing Y N 382 
TRP   NE1 CE2  sing Y N 383 
TRP   NE1 HE1  sing N N 384 
TRP   CE2 CZ2  sing Y N 385 
TRP   CE3 CZ3  doub Y N 386 
TRP   CE3 HE3  sing N N 387 
TRP   CZ2 CH2  doub Y N 388 
TRP   CZ2 HZ2  sing N N 389 
TRP   CZ3 CH2  sing Y N 390 
TRP   CZ3 HZ3  sing N N 391 
TRP   CH2 HH2  sing N N 392 
TRP   OXT HXT  sing N N 393 
TYR   N   CA   sing N N 394 
TYR   N   H    sing N N 395 
TYR   N   H2   sing N N 396 
TYR   CA  C    sing N N 397 
TYR   CA  CB   sing N N 398 
TYR   CA  HA   sing N N 399 
TYR   C   O    doub N N 400 
TYR   C   OXT  sing N N 401 
TYR   CB  CG   sing N N 402 
TYR   CB  HB2  sing N N 403 
TYR   CB  HB3  sing N N 404 
TYR   CG  CD1  doub Y N 405 
TYR   CG  CD2  sing Y N 406 
TYR   CD1 CE1  sing Y N 407 
TYR   CD1 HD1  sing N N 408 
TYR   CD2 CE2  doub Y N 409 
TYR   CD2 HD2  sing N N 410 
TYR   CE1 CZ   doub Y N 411 
TYR   CE1 HE1  sing N N 412 
TYR   CE2 CZ   sing Y N 413 
TYR   CE2 HE2  sing N N 414 
TYR   CZ  OH   sing N N 415 
TYR   OH  HH   sing N N 416 
TYR   OXT HXT  sing N N 417 
VAL   N   CA   sing N N 418 
VAL   N   H    sing N N 419 
VAL   N   H2   sing N N 420 
VAL   CA  C    sing N N 421 
VAL   CA  CB   sing N N 422 
VAL   CA  HA   sing N N 423 
VAL   C   O    doub N N 424 
VAL   C   OXT  sing N N 425 
VAL   CB  CG1  sing N N 426 
VAL   CB  CG2  sing N N 427 
VAL   CB  HB   sing N N 428 
VAL   CG1 HG11 sing N N 429 
VAL   CG1 HG12 sing N N 430 
VAL   CG1 HG13 sing N N 431 
VAL   CG2 HG21 sing N N 432 
VAL   CG2 HG22 sing N N 433 
VAL   CG2 HG23 sing N N 434 
VAL   OXT HXT  sing N N 435 
# 
_pdbx_audit_support.funding_organization   'National Science Foundation (NSF, China)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           81903539 
_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   6A32 
_pdbx_initial_refinement_model.details          6A32 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8XRR 
_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]   0.018529 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013701 
_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]   0.010045 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLY   A 1 24  ? 32.994 37.353  3.828   1.00 78.16  ? 569  GLY   A N   1 
ATOM   2    C CA  . GLY   A 1 24  ? 33.744 36.404  3.031   1.00 66.90  ? 569  GLY   A CA  1 
ATOM   3    C C   . GLY   A 1 24  ? 33.065 36.100  1.722   1.00 69.80  ? 569  GLY   A C   1 
ATOM   4    O O   . GLY   A 1 24  ? 32.807 34.941  1.414   1.00 73.47  ? 569  GLY   A O   1 
ATOM   5    N N   . HIS   A 1 25  ? 32.776 37.134  0.944   1.00 71.50  ? 570  HIS   A N   1 
ATOM   6    C CA  . HIS   A 1 25  ? 32.137 36.946  -0.348  1.00 66.39  ? 570  HIS   A CA  1 
ATOM   7    C C   . HIS   A 1 25  ? 33.038 36.164  -1.276  1.00 62.49  ? 570  HIS   A C   1 
ATOM   8    O O   . HIS   A 1 25  ? 32.566 35.543  -2.220  1.00 62.42  ? 570  HIS   A O   1 
ATOM   9    C CB  . HIS   A 1 25  ? 31.820 38.299  -0.966  1.00 72.63  ? 570  HIS   A CB  1 
ATOM   10   C CG  . HIS   A 1 25  ? 33.033 39.081  -1.358  1.00 77.95  ? 570  HIS   A CG  1 
ATOM   11   N ND1 . HIS   A 1 25  ? 33.717 39.887  -0.475  1.00 78.86  ? 570  HIS   A ND1 1 
ATOM   12   C CD2 . HIS   A 1 25  ? 33.686 39.180  -2.540  1.00 76.03  ? 570  HIS   A CD2 1 
ATOM   13   C CE1 . HIS   A 1 25  ? 34.739 40.449  -1.095  1.00 73.78  ? 570  HIS   A CE1 1 
ATOM   14   N NE2 . HIS   A 1 25  ? 34.743 40.037  -2.350  1.00 75.13  ? 570  HIS   A NE2 1 
ATOM   15   N N   . GLU   A 1 26  ? 34.336 36.197  -1.015  1.00 59.68  ? 571  GLU   A N   1 
ATOM   16   C CA  . GLU   A 1 26  ? 35.287 35.508  -1.861  1.00 52.15  ? 571  GLU   A CA  1 
ATOM   17   C C   . GLU   A 1 26  ? 35.249 34.015  -1.645  1.00 52.68  ? 571  GLU   A C   1 
ATOM   18   O O   . GLU   A 1 26  ? 35.754 33.257  -2.462  1.00 50.52  ? 571  GLU   A O   1 
ATOM   19   C CB  . GLU   A 1 26  ? 36.689 36.015  -1.567  1.00 55.65  ? 571  GLU   A CB  1 
ATOM   20   C CG  . GLU   A 1 26  ? 36.825 37.523  -1.495  1.00 63.01  ? 571  GLU   A CG  1 
ATOM   21   C CD  . GLU   A 1 26  ? 36.722 38.042  -0.079  1.00 68.07  ? 571  GLU   A CD  1 
ATOM   22   O OE1 . GLU   A 1 26  ? 36.009 37.420  0.735   1.00 69.62  ? 571  GLU   A OE1 1 
ATOM   23   O OE2 . GLU   A 1 26  ? 37.354 39.075  0.219   1.00 76.92  ? 571  GLU   A OE2 1 
ATOM   24   N N   . TYR   A 1 27  ? 34.665 33.589  -0.538  1.00 56.80  ? 572  TYR   A N   1 
ATOM   25   C CA  . TYR   A 1 27  ? 34.597 32.174  -0.229  1.00 51.28  ? 572  TYR   A CA  1 
ATOM   26   C C   . TYR   A 1 27  ? 33.175 31.706  -0.363  1.00 51.38  ? 572  TYR   A C   1 
ATOM   27   O O   . TYR   A 1 27  ? 32.301 32.168  0.355   1.00 56.69  ? 572  TYR   A O   1 
ATOM   28   C CB  . TYR   A 1 27  ? 35.126 31.920  1.171   1.00 51.46  ? 572  TYR   A CB  1 
ATOM   29   C CG  . TYR   A 1 27  ? 36.579 32.281  1.340   1.00 51.13  ? 572  TYR   A CG  1 
ATOM   30   C CD1 . TYR   A 1 27  ? 37.578 31.407  0.942   1.00 45.02  ? 572  TYR   A CD1 1 
ATOM   31   C CD2 . TYR   A 1 27  ? 36.953 33.494  1.895   1.00 49.93  ? 572  TYR   A CD2 1 
ATOM   32   C CE1 . TYR   A 1 27  ? 38.909 31.731  1.094   1.00 46.64  ? 572  TYR   A CE1 1 
ATOM   33   C CE2 . TYR   A 1 27  ? 38.282 33.826  2.050   1.00 46.07  ? 572  TYR   A CE2 1 
ATOM   34   C CZ  . TYR   A 1 27  ? 39.255 32.939  1.647   1.00 51.24  ? 572  TYR   A CZ  1 
ATOM   35   O OH  . TYR   A 1 27  ? 40.580 33.261  1.798   1.00 48.70  ? 572  TYR   A OH  1 
ATOM   36   N N   . ILE   A 1 28  ? 32.933 30.794  -1.290  1.00 55.68  ? 573  ILE   A N   1 
ATOM   37   C CA  . ILE   A 1 28  ? 31.573 30.347  -1.537  1.00 56.78  ? 573  ILE   A CA  1 
ATOM   38   C C   . ILE   A 1 28  ? 31.433 28.840  -1.590  1.00 59.50  ? 573  ILE   A C   1 
ATOM   39   O O   . ILE   A 1 28  ? 32.420 28.118  -1.674  1.00 58.83  ? 573  ILE   A O   1 
ATOM   40   C CB  . ILE   A 1 28  ? 31.038 30.911  -2.865  1.00 61.62  ? 573  ILE   A CB  1 
ATOM   41   C CG1 . ILE   A 1 28  ? 31.652 30.164  -4.046  1.00 51.07  ? 573  ILE   A CG1 1 
ATOM   42   C CG2 . ILE   A 1 28  ? 31.319 32.403  -2.965  1.00 57.52  ? 573  ILE   A CG2 1 
ATOM   43   C CD1 . ILE   A 1 28  ? 31.056 30.553  -5.378  1.00 65.15  ? 573  ILE   A CD1 1 
ATOM   44   N N   . TYR   A 1 29  ? 30.199 28.365  -1.543  1.00 60.08  ? 574  TYR   A N   1 
ATOM   45   C CA  . TYR   A 1 29  ? 29.945 26.938  -1.614  1.00 62.61  ? 574  TYR   A CA  1 
ATOM   46   C C   . TYR   A 1 29  ? 29.741 26.511  -3.044  1.00 59.37  ? 574  TYR   A C   1 
ATOM   47   O O   . TYR   A 1 29  ? 28.909 27.070  -3.748  1.00 60.38  ? 574  TYR   A O   1 
ATOM   48   C CB  . TYR   A 1 29  ? 28.709 26.593  -0.792  1.00 62.07  ? 574  TYR   A CB  1 
ATOM   49   C CG  . TYR   A 1 29  ? 27.949 25.373  -1.262  1.00 64.62  ? 574  TYR   A CG  1 
ATOM   50   C CD1 . TYR   A 1 29  ? 28.490 24.102  -1.144  1.00 72.54  ? 574  TYR   A CD1 1 
ATOM   51   C CD2 . TYR   A 1 29  ? 26.679 25.495  -1.804  1.00 69.61  ? 574  TYR   A CD2 1 
ATOM   52   C CE1 . TYR   A 1 29  ? 27.792 22.989  -1.569  1.00 74.92  ? 574  TYR   A CE1 1 
ATOM   53   C CE2 . TYR   A 1 29  ? 25.974 24.387  -2.228  1.00 73.31  ? 574  TYR   A CE2 1 
ATOM   54   C CZ  . TYR   A 1 29  ? 26.535 23.137  -2.108  1.00 74.39  ? 574  TYR   A CZ  1 
ATOM   55   O OH  . TYR   A 1 29  ? 25.833 22.034  -2.530  1.00 73.92  ? 574  TYR   A OH  1 
ATOM   56   N N   . VAL   A 1 30  ? 30.505 25.522  -3.478  1.00 54.05  ? 575  VAL   A N   1 
ATOM   57   C CA  . VAL   A 1 30  ? 30.355 25.013  -4.826  1.00 54.85  ? 575  VAL   A CA  1 
ATOM   58   C C   . VAL   A 1 30  ? 29.216 24.010  -4.894  1.00 61.66  ? 575  VAL   A C   1 
ATOM   59   O O   . VAL   A 1 30  ? 29.362 22.874  -4.457  1.00 63.19  ? 575  VAL   A O   1 
ATOM   60   C CB  . VAL   A 1 30  ? 31.648 24.342  -5.311  1.00 54.40  ? 575  VAL   A CB  1 
ATOM   61   C CG1 . VAL   A 1 30  ? 31.486 23.848  -6.738  1.00 55.15  ? 575  VAL   A CG1 1 
ATOM   62   C CG2 . VAL   A 1 30  ? 32.818 25.304  -5.199  1.00 43.20  ? 575  VAL   A CG2 1 
ATOM   63   N N   . ASP   A 1 31  ? 28.081 24.427  -5.437  1.00 58.04  ? 576  ASP   A N   1 
ATOM   64   C CA  . ASP   A 1 31  ? 26.953 23.528  -5.577  1.00 61.16  ? 576  ASP   A CA  1 
ATOM   65   C C   . ASP   A 1 31  ? 27.189 22.624  -6.764  1.00 59.65  ? 576  ASP   A C   1 
ATOM   66   O O   . ASP   A 1 31  ? 27.386 23.095  -7.876  1.00 61.42  ? 576  ASP   A O   1 
ATOM   67   C CB  . ASP   A 1 31  ? 25.665 24.317  -5.769  1.00 60.72  ? 576  ASP   A CB  1 
ATOM   68   C CG  . ASP   A 1 31  ? 24.435 23.441  -5.777  1.00 69.00  ? 576  ASP   A CG  1 
ATOM   69   O OD1 . ASP   A 1 31  ? 24.561 22.223  -5.549  1.00 73.79  ? 576  ASP   A OD1 1 
ATOM   70   O OD2 . ASP   A 1 31  ? 23.333 23.976  -6.007  1.00 70.62  ? 576  ASP   A OD2 1 
ATOM   71   N N   . PRO   A 1 32  ? 27.173 21.312  -6.530  1.00 61.48  ? 577  PRO   A N   1 
ATOM   72   C CA  . PRO   A 1 32  ? 27.380 20.361  -7.619  1.00 62.45  ? 577  PRO   A CA  1 
ATOM   73   C C   . PRO   A 1 32  ? 26.226 20.400  -8.604  1.00 61.39  ? 577  PRO   A C   1 
ATOM   74   O O   . PRO   A 1 32  ? 26.333 19.851  -9.694  1.00 61.84  ? 577  PRO   A O   1 
ATOM   75   C CB  . PRO   A 1 32  ? 27.432 19.014  -6.896  1.00 62.21  ? 577  PRO   A CB  1 
ATOM   76   C CG  . PRO   A 1 32  ? 27.792 19.342  -5.488  1.00 64.88  ? 577  PRO   A CG  1 
ATOM   77   C CD  . PRO   A 1 32  ? 27.117 20.649  -5.219  1.00 60.94  ? 577  PRO   A CD  1 
ATOM   78   N N   . MET   A 1 33  ? 25.136 21.046  -8.226  1.00 60.49  ? 578  MET   A N   1 
ATOM   79   C CA  . MET   A 1 33  ? 23.985 21.146  -9.102  1.00 62.89  ? 578  MET   A CA  1 
ATOM   80   C C   . MET   A 1 33  ? 24.158 22.264  -10.106 1.00 65.06  ? 578  MET   A C   1 
ATOM   81   O O   . MET   A 1 33  ? 23.420 22.349  -11.080 1.00 61.45  ? 578  MET   A O   1 
ATOM   82   C CB  . MET   A 1 33  ? 22.727 21.400  -8.283  1.00 64.04  ? 578  MET   A CB  1 
ATOM   83   C CG  . MET   A 1 33  ? 22.441 20.371  -7.205  1.00 71.55  ? 578  MET   A CG  1 
ATOM   84   S SD  . MET   A 1 33  ? 22.081 18.733  -7.855  1.00 67.00  ? 578  MET   A SD  1 
ATOM   85   C CE  . MET   A 1 33  ? 23.711 17.996  -7.850  1.00 61.23  ? 578  MET   A CE  1 
ATOM   86   N N   . GLN   A 1 34  ? 25.125 23.133  -9.866  1.00 65.53  ? 579  GLN   A N   1 
ATOM   87   C CA  . GLN   A 1 34  ? 25.340 24.260  -10.750 1.00 59.83  ? 579  GLN   A CA  1 
ATOM   88   C C   . GLN   A 1 34  ? 26.575 24.026  -11.575 1.00 56.28  ? 579  GLN   A C   1 
ATOM   89   O O   . GLN   A 1 34  ? 26.939 24.849  -12.407 1.00 57.80  ? 579  GLN   A O   1 
ATOM   90   C CB  . GLN   A 1 34  ? 25.466 25.537  -9.930  1.00 58.26  ? 579  GLN   A CB  1 
ATOM   91   C CG  . GLN   A 1 34  ? 24.255 25.808  -9.056  1.00 58.93  ? 579  GLN   A CG  1 
ATOM   92   C CD  . GLN   A 1 34  ? 24.421 27.037  -8.190  1.00 75.99  ? 579  GLN   A CD  1 
ATOM   93   O OE1 . GLN   A 1 34  ? 25.407 27.763  -8.304  1.00 73.59  ? 579  GLN   A OE1 1 
ATOM   94   N NE2 . GLN   A 1 34  ? 23.455 27.276  -7.314  1.00 86.45  ? 579  GLN   A NE2 1 
ATOM   95   N N   . LEU   A 1 35  ? 27.221 22.898  -11.351 1.00 52.13  ? 580  LEU   A N   1 
ATOM   96   C CA  . LEU   A 1 35  ? 28.401 22.568  -12.112 1.00 49.96  ? 580  LEU   A CA  1 
ATOM   97   C C   . LEU   A 1 35  ? 27.984 21.966  -13.436 1.00 58.50  ? 580  LEU   A C   1 
ATOM   98   O O   . LEU   A 1 35  ? 26.930 21.352  -13.542 1.00 56.89  ? 580  LEU   A O   1 
ATOM   99   C CB  . LEU   A 1 35  ? 29.279 21.596  -11.335 1.00 55.22  ? 580  LEU   A CB  1 
ATOM   100  C CG  . LEU   A 1 35  ? 29.921 22.110  -10.052 1.00 59.53  ? 580  LEU   A CG  1 
ATOM   101  C CD1 . LEU   A 1 35  ? 30.699 20.993  -9.378  1.00 54.48  ? 580  LEU   A CD1 1 
ATOM   102  C CD2 . LEU   A 1 35  ? 30.831 23.285  -10.365 1.00 51.03  ? 580  LEU   A CD2 1 
ATOM   103  N N   . PRO   A 1 36  ? 28.808 22.151  -14.462 1.00 61.31  ? 581  PRO   A N   1 
ATOM   104  C CA  . PRO   A 1 36  ? 28.483 21.619  -15.782 1.00 58.53  ? 581  PRO   A CA  1 
ATOM   105  C C   . PRO   A 1 36  ? 28.617 20.114  -15.840 1.00 56.11  ? 581  PRO   A C   1 
ATOM   106  O O   . PRO   A 1 36  ? 29.324 19.539  -15.022 1.00 59.19  ? 581  PRO   A O   1 
ATOM   107  C CB  . PRO   A 1 36  ? 29.543 22.255  -16.674 1.00 56.29  ? 581  PRO   A CB  1 
ATOM   108  C CG  . PRO   A 1 36  ? 30.688 22.531  -15.767 1.00 61.48  ? 581  PRO   A CG  1 
ATOM   109  C CD  . PRO   A 1 36  ? 30.067 22.912  -14.460 1.00 55.19  ? 581  PRO   A CD  1 
ATOM   110  N N   . TYR   A 1 37  ? 27.946 19.482  -16.792 1.00 61.75  ? 582  TYR   A N   1 
ATOM   111  C CA  . TYR   A 1 37  ? 28.049 18.038  -16.961 1.00 60.36  ? 582  TYR   A CA  1 
ATOM   112  C C   . TYR   A 1 37  ? 29.177 17.704  -17.917 1.00 51.60  ? 582  TYR   A C   1 
ATOM   113  O O   . TYR   A 1 37  ? 29.194 18.172  -19.048 1.00 55.74  ? 582  TYR   A O   1 
ATOM   114  C CB  . TYR   A 1 37  ? 26.720 17.481  -17.469 1.00 55.37  ? 582  TYR   A CB  1 
ATOM   115  C CG  . TYR   A 1 37  ? 26.775 16.104  -18.086 1.00 58.43  ? 582  TYR   A CG  1 
ATOM   116  C CD1 . TYR   A 1 37  ? 26.791 14.967  -17.294 1.00 57.61  ? 582  TYR   A CD1 1 
ATOM   117  C CD2 . TYR   A 1 37  ? 26.776 15.941  -19.463 1.00 58.84  ? 582  TYR   A CD2 1 
ATOM   118  C CE1 . TYR   A 1 37  ? 26.827 13.707  -17.857 1.00 57.64  ? 582  TYR   A CE1 1 
ATOM   119  C CE2 . TYR   A 1 37  ? 26.813 14.686  -20.034 1.00 57.09  ? 582  TYR   A CE2 1 
ATOM   120  C CZ  . TYR   A 1 37  ? 26.837 13.573  -19.226 1.00 54.59  ? 582  TYR   A CZ  1 
ATOM   121  O OH  . TYR   A 1 37  ? 26.871 12.322  -19.792 1.00 56.28  ? 582  TYR   A OH  1 
ATOM   122  N N   . ASP   A 1 38  ? 30.128 16.906  -17.459 1.00 53.02  ? 583  ASP   A N   1 
ATOM   123  C CA  . ASP   A 1 38  ? 31.221 16.509  -18.320 1.00 56.25  ? 583  ASP   A CA  1 
ATOM   124  C C   . ASP   A 1 38  ? 30.688 15.531  -19.335 1.00 62.05  ? 583  ASP   A C   1 
ATOM   125  O O   . ASP   A 1 38  ? 30.108 14.512  -18.977 1.00 58.26  ? 583  ASP   A O   1 
ATOM   126  C CB  . ASP   A 1 38  ? 32.356 15.882  -17.519 1.00 53.87  ? 583  ASP   A CB  1 
ATOM   127  C CG  . ASP   A 1 38  ? 33.606 15.670  -18.346 1.00 70.59  ? 583  ASP   A CG  1 
ATOM   128  O OD1 . ASP   A 1 38  ? 33.520 15.703  -19.590 1.00 66.63  ? 583  ASP   A OD1 1 
ATOM   129  O OD2 . ASP   A 1 38  ? 34.682 15.468  -17.751 1.00 74.01  ? 583  ASP   A OD2 1 
ATOM   130  N N   . SER   A 1 39  ? 30.895 15.831  -20.606 1.00 59.52  ? 584  SER   A N   1 
ATOM   131  C CA  . SER   A 1 39  ? 30.372 14.981  -21.655 1.00 59.33  ? 584  SER   A CA  1 
ATOM   132  C C   . SER   A 1 39  ? 31.176 13.708  -21.743 1.00 58.35  ? 584  SER   A C   1 
ATOM   133  O O   . SER   A 1 39  ? 30.854 12.823  -22.526 1.00 63.60  ? 584  SER   A O   1 
ATOM   134  C CB  . SER   A 1 39  ? 30.392 15.718  -22.986 1.00 58.80  ? 584  SER   A CB  1 
ATOM   135  O OG  . SER   A 1 39  ? 29.842 14.917  -24.014 1.00 85.00  ? 584  SER   A OG  1 
ATOM   136  N N   . ARG   A 1 40  ? 32.218 13.604  -20.934 1.00 55.30  ? 585  ARG   A N   1 
ATOM   137  C CA  . ARG   A 1 40  ? 33.013 12.396  -20.914 1.00 54.39  ? 585  ARG   A CA  1 
ATOM   138  C C   . ARG   A 1 40  ? 32.143 11.234  -20.521 1.00 52.63  ? 585  ARG   A C   1 
ATOM   139  O O   . ARG   A 1 40  ? 32.491 10.087  -20.766 1.00 62.39  ? 585  ARG   A O   1 
ATOM   140  C CB  . ARG   A 1 40  ? 34.146 12.526  -19.914 1.00 61.14  ? 585  ARG   A CB  1 
ATOM   141  C CG  . ARG   A 1 40  ? 33.699 12.406  -18.466 1.00 70.20  ? 585  ARG   A CG  1 
ATOM   142  C CD  . ARG   A 1 40  ? 34.857 12.021  -17.563 1.00 73.15  ? 585  ARG   A CD  1 
ATOM   143  N NE  . ARG   A 1 40  ? 34.449 11.904  -16.168 1.00 64.46  ? 585  ARG   A NE  1 
ATOM   144  C CZ  . ARG   A 1 40  ? 34.557 12.881  -15.275 1.00 78.07  ? 585  ARG   A CZ  1 
ATOM   145  N NH1 . ARG   A 1 40  ? 35.067 14.050  -15.630 1.00 77.48  ? 585  ARG   A NH1 1 
ATOM   146  N NH2 . ARG   A 1 40  ? 34.161 12.689  -14.025 1.00 72.67  ? 585  ARG   A NH2 1 
ATOM   147  N N   . TRP   A 1 41  ? 30.993 11.529  -19.936 1.00 54.50  ? 586  TRP   A N   1 
ATOM   148  C CA  . TRP   A 1 41  ? 30.106 10.478  -19.468 1.00 53.60  ? 586  TRP   A CA  1 
ATOM   149  C C   . TRP   A 1 41  ? 29.061 10.071  -20.490 1.00 55.25  ? 586  TRP   A C   1 
ATOM   150  O O   . TRP   A 1 41  ? 28.319 9.123   -20.260 1.00 52.23  ? 586  TRP   A O   1 
ATOM   151  C CB  . TRP   A 1 41  ? 29.388 10.935  -18.199 1.00 53.22  ? 586  TRP   A CB  1 
ATOM   152  C CG  . TRP   A 1 41  ? 30.236 11.009  -16.985 1.00 58.63  ? 586  TRP   A CG  1 
ATOM   153  C CD1 . TRP   A 1 41  ? 30.730 12.134  -16.400 1.00 62.14  ? 586  TRP   A CD1 1 
ATOM   154  C CD2 . TRP   A 1 41  ? 30.677 9.912   -16.185 1.00 49.19  ? 586  TRP   A CD2 1 
ATOM   155  N NE1 . TRP   A 1 41  ? 31.459 11.805  -15.287 1.00 56.13  ? 586  TRP   A NE1 1 
ATOM   156  C CE2 . TRP   A 1 41  ? 31.442 10.445  -15.133 1.00 53.85  ? 586  TRP   A CE2 1 
ATOM   157  C CE3 . TRP   A 1 41  ? 30.503 8.529   -16.259 1.00 53.46  ? 586  TRP   A CE3 1 
ATOM   158  C CZ2 . TRP   A 1 41  ? 32.032 9.645   -14.164 1.00 53.12  ? 586  TRP   A CZ2 1 
ATOM   159  C CZ3 . TRP   A 1 41  ? 31.089 7.738   -15.297 1.00 61.92  ? 586  TRP   A CZ3 1 
ATOM   160  C CH2 . TRP   A 1 41  ? 31.845 8.296   -14.263 1.00 56.30  ? 586  TRP   A CH2 1 
ATOM   161  N N   . GLU   A 1 42  ? 28.986 10.775  -21.612 1.00 54.33  ? 587  GLU   A N   1 
ATOM   162  C CA  . GLU   A 1 42  ? 27.929 10.485  -22.582 1.00 53.35  ? 587  GLU   A CA  1 
ATOM   163  C C   . GLU   A 1 42  ? 28.126 9.173   -23.313 1.00 52.37  ? 587  GLU   A C   1 
ATOM   164  O O   . GLU   A 1 42  ? 29.222 8.862   -23.761 1.00 52.45  ? 587  GLU   A O   1 
ATOM   165  C CB  . GLU   A 1 42  ? 27.777 11.629  -23.583 1.00 54.87  ? 587  GLU   A CB  1 
ATOM   166  C CG  . GLU   A 1 42  ? 26.553 12.492  -23.347 1.00 59.98  ? 587  GLU   A CG  1 
ATOM   167  C CD  . GLU   A 1 42  ? 25.272 11.798  -23.754 1.00 61.24  ? 587  GLU   A CD  1 
ATOM   168  O OE1 . GLU   A 1 42  ? 25.342 10.810  -24.513 1.00 64.48  ? 587  GLU   A OE1 1 
ATOM   169  O OE2 . GLU   A 1 42  ? 24.194 12.246  -23.326 1.00 60.61  ? 587  GLU   A OE2 1 
ATOM   170  N N   . PHE   A 1 43  ? 27.058 8.396   -23.419 1.00 52.38  ? 588  PHE   A N   1 
ATOM   171  C CA  . PHE   A 1 43  ? 27.125 7.132   -24.125 1.00 52.18  ? 588  PHE   A CA  1 
ATOM   172  C C   . PHE   A 1 43  ? 26.060 7.130   -25.193 1.00 47.75  ? 588  PHE   A C   1 
ATOM   173  O O   . PHE   A 1 43  ? 24.938 7.561   -24.959 1.00 48.02  ? 588  PHE   A O   1 
ATOM   174  C CB  . PHE   A 1 43  ? 26.922 5.962   -23.170 1.00 49.16  ? 588  PHE   A CB  1 
ATOM   175  C CG  . PHE   A 1 43  ? 27.140 4.619   -23.797 1.00 48.36  ? 588  PHE   A CG  1 
ATOM   176  C CD1 . PHE   A 1 43  ? 28.418 4.164   -24.062 1.00 50.17  ? 588  PHE   A CD1 1 
ATOM   177  C CD2 . PHE   A 1 43  ? 26.068 3.803   -24.104 1.00 48.07  ? 588  PHE   A CD2 1 
ATOM   178  C CE1 . PHE   A 1 43  ? 28.623 2.926   -24.635 1.00 54.13  ? 588  PHE   A CE1 1 
ATOM   179  C CE2 . PHE   A 1 43  ? 26.265 2.564   -24.675 1.00 47.90  ? 588  PHE   A CE2 1 
ATOM   180  C CZ  . PHE   A 1 43  ? 27.544 2.124   -24.942 1.00 52.18  ? 588  PHE   A CZ  1 
ATOM   181  N N   . PRO   A 1 44  ? 26.418 6.661   -26.398 1.00 49.54  ? 589  PRO   A N   1 
ATOM   182  C CA  . PRO   A 1 44  ? 25.413 6.585   -27.452 1.00 49.16  ? 589  PRO   A CA  1 
ATOM   183  C C   . PRO   A 1 44  ? 24.242 5.719   -27.032 1.00 49.30  ? 589  PRO   A C   1 
ATOM   184  O O   . PRO   A 1 44  ? 24.440 4.615   -26.544 1.00 49.38  ? 589  PRO   A O   1 
ATOM   185  C CB  . PRO   A 1 44  ? 26.171 5.930   -28.600 1.00 43.09  ? 589  PRO   A CB  1 
ATOM   186  C CG  . PRO   A 1 44  ? 27.597 6.251   -28.354 1.00 49.64  ? 589  PRO   A CG  1 
ATOM   187  C CD  . PRO   A 1 44  ? 27.734 6.188   -26.870 1.00 48.12  ? 589  PRO   A CD  1 
ATOM   188  N N   . ARG   A 1 45  ? 23.031 6.209   -27.230 1.00 44.40  ? 590  ARG   A N   1 
ATOM   189  C CA  . ARG   A 1 45  ? 21.851 5.459   -26.849 1.00 46.97  ? 590  ARG   A CA  1 
ATOM   190  C C   . ARG   A 1 45  ? 21.711 4.216   -27.707 1.00 52.50  ? 590  ARG   A C   1 
ATOM   191  O O   . ARG   A 1 45  ? 21.042 3.266   -27.319 1.00 55.22  ? 590  ARG   A O   1 
ATOM   192  C CB  . ARG   A 1 45  ? 20.622 6.348   -26.975 1.00 45.09  ? 590  ARG   A CB  1 
ATOM   193  C CG  . ARG   A 1 45  ? 19.485 6.005   -26.033 1.00 58.40  ? 590  ARG   A CG  1 
ATOM   194  C CD  . ARG   A 1 45  ? 18.302 6.923   -26.282 1.00 62.97  ? 590  ARG   A CD  1 
ATOM   195  N NE  . ARG   A 1 45  ? 18.625 8.318   -26.003 1.00 56.89  ? 590  ARG   A NE  1 
ATOM   196  C CZ  . ARG   A 1 45  ? 18.328 8.935   -24.867 1.00 60.81  ? 590  ARG   A CZ  1 
ATOM   197  N NH1 . ARG   A 1 45  ? 17.690 8.281   -23.909 1.00 59.19  ? 590  ARG   A NH1 1 
ATOM   198  N NH2 . ARG   A 1 45  ? 18.660 10.206  -24.691 1.00 56.00  ? 590  ARG   A NH2 1 
ATOM   199  N N   . ASP   A 1 46  ? 22.346 4.216   -28.870 1.00 49.16  ? 591  ASP   A N   1 
ATOM   200  C CA  . ASP   A 1 46  ? 22.289 3.069   -29.759 1.00 50.82  ? 591  ASP   A CA  1 
ATOM   201  C C   . ASP   A 1 46  ? 23.237 1.976   -29.318 1.00 52.82  ? 591  ASP   A C   1 
ATOM   202  O O   . ASP   A 1 46  ? 23.228 0.888   -29.879 1.00 54.13  ? 591  ASP   A O   1 
ATOM   203  C CB  . ASP   A 1 46  ? 22.623 3.487   -31.189 1.00 57.75  ? 591  ASP   A CB  1 
ATOM   204  C CG  . ASP   A 1 46  ? 23.919 4.253   -31.282 1.00 68.08  ? 591  ASP   A CG  1 
ATOM   205  O OD1 . ASP   A 1 46  ? 24.003 5.349   -30.694 1.00 68.61  ? 591  ASP   A OD1 1 
ATOM   206  O OD2 . ASP   A 1 46  ? 24.848 3.767   -31.955 1.00 69.06  ? 591  ASP   A OD2 1 
ATOM   207  N N   . GLY   A 1 47  ? 24.066 2.258   -28.324 1.00 52.66  ? 592  GLY   A N   1 
ATOM   208  C CA  . GLY   A 1 47  ? 24.968 1.254   -27.811 1.00 44.06  ? 592  GLY   A CA  1 
ATOM   209  C C   . GLY   A 1 47  ? 24.400 0.569   -26.596 1.00 45.96  ? 592  GLY   A C   1 
ATOM   210  O O   . GLY   A 1 47  ? 25.048 -0.288  -26.012 1.00 48.63  ? 592  GLY   A O   1 
ATOM   211  N N   . LEU   A 1 48  ? 23.186 0.935   -26.212 1.00 42.07  ? 593  LEU   A N   1 
ATOM   212  C CA  . LEU   A 1 48  ? 22.599 0.377   -25.006 1.00 51.26  ? 593  LEU   A CA  1 
ATOM   213  C C   . LEU   A 1 48  ? 21.335 -0.421  -25.260 1.00 53.11  ? 593  LEU   A C   1 
ATOM   214  O O   . LEU   A 1 48  ? 20.358 0.105   -25.775 1.00 50.18  ? 593  LEU   A O   1 
ATOM   215  C CB  . LEU   A 1 48  ? 22.298 1.491   -24.003 1.00 48.01  ? 593  LEU   A CB  1 
ATOM   216  C CG  . LEU   A 1 48  ? 21.760 1.054   -22.645 1.00 47.54  ? 593  LEU   A CG  1 
ATOM   217  C CD1 . LEU   A 1 48  ? 22.805 0.225   -21.917 1.00 48.79  ? 593  LEU   A CD1 1 
ATOM   218  C CD2 . LEU   A 1 48  ? 21.374 2.275   -21.827 1.00 51.63  ? 593  LEU   A CD2 1 
ATOM   219  N N   . VAL   A 1 49  ? 21.351 -1.691  -24.878 1.00 49.25  ? 594  VAL   A N   1 
ATOM   220  C CA  . VAL   A 1 49  ? 20.179 -2.523  -25.033 1.00 47.46  ? 594  VAL   A CA  1 
ATOM   221  C C   . VAL   A 1 49  ? 19.510 -2.642  -23.692 1.00 54.48  ? 594  VAL   A C   1 
ATOM   222  O O   . VAL   A 1 49  ? 20.150 -2.976  -22.706 1.00 52.99  ? 594  VAL   A O   1 
ATOM   223  C CB  . VAL   A 1 49  ? 20.536 -3.921  -25.545 1.00 51.41  ? 594  VAL   A CB  1 
ATOM   224  C CG1 . VAL   A 1 49  ? 19.309 -4.817  -25.542 1.00 51.58  ? 594  VAL   A CG1 1 
ATOM   225  C CG2 . VAL   A 1 49  ? 21.151 -3.839  -26.931 1.00 52.68  ? 594  VAL   A CG2 1 
ATOM   226  N N   . LEU   A 1 50  ? 18.220 -2.361  -23.651 1.00 55.44  ? 595  LEU   A N   1 
ATOM   227  C CA  . LEU   A 1 50  ? 17.505 -2.385  -22.395 1.00 50.46  ? 595  LEU   A CA  1 
ATOM   228  C C   . LEU   A 1 50  ? 16.738 -3.674  -22.234 1.00 50.48  ? 595  LEU   A C   1 
ATOM   229  O O   . LEU   A 1 50  ? 16.239 -4.229  -23.205 1.00 56.46  ? 595  LEU   A O   1 
ATOM   230  C CB  . LEU   A 1 50  ? 16.558 -1.191  -22.321 1.00 48.92  ? 595  LEU   A CB  1 
ATOM   231  C CG  . LEU   A 1 50  ? 17.215 0.183   -22.422 1.00 59.78  ? 595  LEU   A CG  1 
ATOM   232  C CD1 . LEU   A 1 50  ? 16.162 1.276   -22.492 1.00 65.38  ? 595  LEU   A CD1 1 
ATOM   233  C CD2 . LEU   A 1 50  ? 18.154 0.410   -21.250 1.00 52.40  ? 595  LEU   A CD2 1 
ATOM   234  N N   . GLY   A 1 51  ? 16.640 -4.152  -21.005 1.00 52.68  ? 596  GLY   A N   1 
ATOM   235  C CA  . GLY   A 1 51  ? 15.949 -5.395  -20.756 1.00 50.66  ? 596  GLY   A CA  1 
ATOM   236  C C   . GLY   A 1 51  ? 14.943 -5.389  -19.635 1.00 53.49  ? 596  GLY   A C   1 
ATOM   237  O O   . GLY   A 1 51  ? 14.115 -4.494  -19.548 1.00 58.90  ? 596  GLY   A O   1 
ATOM   238  N N   . ARG   A 1 52  ? 15.016 -6.382  -18.766 1.00 52.20  ? 597  ARG   A N   1 
ATOM   239  C CA  . ARG   A 1 52  ? 14.032 -6.517  -17.699 1.00 65.28  ? 597  ARG   A CA  1 
ATOM   240  C C   . ARG   A 1 52  ? 14.076 -5.432  -16.648 1.00 61.55  ? 597  ARG   A C   1 
ATOM   241  O O   . ARG   A 1 52  ? 15.102 -4.794  -16.446 1.00 58.93  ? 597  ARG   A O   1 
ATOM   242  C CB  . ARG   A 1 52  ? 14.230 -7.858  -17.000 1.00 69.13  ? 597  ARG   A CB  1 
ATOM   243  C CG  . ARG   A 1 52  ? 14.276 -9.057  -17.925 1.00 78.47  ? 597  ARG   A CG  1 
ATOM   244  C CD  . ARG   A 1 52  ? 14.525 -10.334 -17.138 1.00 91.71  ? 597  ARG   A CD  1 
ATOM   245  N NE  . ARG   A 1 52  ? 15.823 -10.329 -16.468 1.00 87.88  ? 597  ARG   A NE  1 
ATOM   246  C CZ  . ARG   A 1 52  ? 16.024 -9.921  -15.219 1.00 79.79  ? 597  ARG   A CZ  1 
ATOM   247  N NH1 . ARG   A 1 52  ? 15.010 -9.481  -14.490 1.00 83.01  ? 597  ARG   A NH1 1 
ATOM   248  N NH2 . ARG   A 1 52  ? 17.240 -9.957  -14.697 1.00 83.00  ? 597  ARG   A NH2 1 
ATOM   249  N N   . VAL   A 1 53  ? 12.958 -5.232  -15.965 1.00 55.95  ? 598  VAL   A N   1 
ATOM   250  C CA  . VAL   A 1 53  ? 12.927 -4.260  -14.897 1.00 58.78  ? 598  VAL   A CA  1 
ATOM   251  C C   . VAL   A 1 53  ? 13.489 -4.893  -13.653 1.00 60.18  ? 598  VAL   A C   1 
ATOM   252  O O   . VAL   A 1 53  ? 12.872 -5.778  -13.076 1.00 63.92  ? 598  VAL   A O   1 
ATOM   253  C CB  . VAL   A 1 53  ? 11.504 -3.796  -14.596 1.00 59.76  ? 598  VAL   A CB  1 
ATOM   254  C CG1 . VAL   A 1 53  ? 11.515 -2.757  -13.487 1.00 52.23  ? 598  VAL   A CG1 1 
ATOM   255  C CG2 . VAL   A 1 53  ? 10.858 -3.236  -15.852 1.00 62.59  ? 598  VAL   A CG2 1 
ATOM   256  N N   . LEU   A 1 54  ? 14.667 -4.452  -13.239 1.00 58.95  ? 599  LEU   A N   1 
ATOM   257  C CA  . LEU   A 1 54  ? 15.273 -4.982  -12.039 1.00 55.43  ? 599  LEU   A CA  1 
ATOM   258  C C   . LEU   A 1 54  ? 14.448 -4.552  -10.852 1.00 59.45  ? 599  LEU   A C   1 
ATOM   259  O O   . LEU   A 1 54  ? 14.217 -5.329  -9.934  1.00 55.68  ? 599  LEU   A O   1 
ATOM   260  C CB  . LEU   A 1 54  ? 16.705 -4.489  -11.909 1.00 54.72  ? 599  LEU   A CB  1 
ATOM   261  C CG  . LEU   A 1 54  ? 17.668 -4.899  -13.017 1.00 60.23  ? 599  LEU   A CG  1 
ATOM   262  C CD1 . LEU   A 1 54  ? 19.015 -4.222  -12.822 1.00 60.30  ? 599  LEU   A CD1 1 
ATOM   263  C CD2 . LEU   A 1 54  ? 17.819 -6.410  -13.042 1.00 59.80  ? 599  LEU   A CD2 1 
ATOM   264  N N   . GLY   A 1 55  ? 13.992 -3.310  -10.874 1.00 59.00  ? 600  GLY   A N   1 
ATOM   265  C CA  . GLY   A 1 55  ? 13.182 -2.808  -9.788  1.00 50.52  ? 600  GLY   A CA  1 
ATOM   266  C C   . GLY   A 1 55  ? 12.943 -1.321  -9.813  1.00 49.01  ? 600  GLY   A C   1 
ATOM   267  O O   . GLY   A 1 55  ? 13.330 -0.641  -10.752 1.00 52.04  ? 600  GLY   A O   1 
ATOM   268  N N   . SER   A 1 56  ? 12.301 -0.810  -8.774  1.00 62.80  ? 601  SER   A N   1 
ATOM   269  C CA  . SER   A 1 56  ? 12.023 0.616   -8.685  1.00 63.78  ? 601  SER   A CA  1 
ATOM   270  C C   . SER   A 1 56  ? 12.250 1.129   -7.277  1.00 60.25  ? 601  SER   A C   1 
ATOM   271  O O   . SER   A 1 56  ? 12.046 0.404   -6.311  1.00 57.84  ? 601  SER   A O   1 
ATOM   272  C CB  . SER   A 1 56  ? 10.581 0.909   -9.112  1.00 57.96  ? 601  SER   A CB  1 
ATOM   273  O OG  . SER   A 1 56  ? 9.653  0.321   -8.223  1.00 68.97  ? 601  SER   A OG  1 
ATOM   274  N N   . GLY   A 1 57  ? 12.681 2.375   -7.154  1.00 66.57  ? 602  GLY   A N   1 
ATOM   275  C CA  . GLY   A 1 57  ? 12.853 2.973   -5.843  1.00 61.38  ? 602  GLY   A CA  1 
ATOM   276  C C   . GLY   A 1 57  ? 11.711 3.919   -5.541  1.00 65.99  ? 602  GLY   A C   1 
ATOM   277  O O   . GLY   A 1 57  ? 10.550 3.563   -5.710  1.00 68.09  ? 602  GLY   A O   1 
ATOM   278  N N   . ALA   A 1 58  ? 12.027 5.121   -5.081  1.00 63.92  ? 603  ALA   A N   1 
ATOM   279  C CA  . ALA   A 1 58  ? 10.992 6.109   -4.817  1.00 62.46  ? 603  ALA   A CA  1 
ATOM   280  C C   . ALA   A 1 58  ? 10.426 6.630   -6.112  1.00 68.88  ? 603  ALA   A C   1 
ATOM   281  O O   . ALA   A 1 58  ? 9.224  6.842   -6.234  1.00 68.81  ? 603  ALA   A O   1 
ATOM   282  C CB  . ALA   A 1 58  ? 11.553 7.254   -4.004  1.00 63.73  ? 603  ALA   A CB  1 
ATOM   283  N N   . PHE   A 1 59  ? 11.299 6.847   -7.083  1.00 68.45  ? 604  PHE   A N   1 
ATOM   284  C CA  . PHE   A 1 59  ? 10.853 7.335   -8.372  1.00 69.03  ? 604  PHE   A CA  1 
ATOM   285  C C   . PHE   A 1 59  ? 11.586 6.634   -9.492  1.00 68.84  ? 604  PHE   A C   1 
ATOM   286  O O   . PHE   A 1 59  ? 12.755 6.290   -9.353  1.00 68.55  ? 604  PHE   A O   1 
ATOM   287  C CB  . PHE   A 1 59  ? 11.057 8.848   -8.478  1.00 71.62  ? 604  PHE   A CB  1 
ATOM   288  C CG  . PHE   A 1 59  ? 12.457 9.252   -8.841  1.00 70.41  ? 604  PHE   A CG  1 
ATOM   289  C CD1 . PHE   A 1 59  ? 13.476 9.183   -7.910  1.00 75.57  ? 604  PHE   A CD1 1 
ATOM   290  C CD2 . PHE   A 1 59  ? 12.747 9.717   -10.112 1.00 69.33  ? 604  PHE   A CD2 1 
ATOM   291  C CE1 . PHE   A 1 59  ? 14.763 9.559   -8.243  1.00 74.92  ? 604  PHE   A CE1 1 
ATOM   292  C CE2 . PHE   A 1 59  ? 14.029 10.096  -10.450 1.00 73.90  ? 604  PHE   A CE2 1 
ATOM   293  C CZ  . PHE   A 1 59  ? 15.040 10.017  -9.515  1.00 70.90  ? 604  PHE   A CZ  1 
ATOM   294  N N   . GLY   A 1 60  ? 10.896 6.412   -10.602 1.00 71.10  ? 605  GLY   A N   1 
ATOM   295  C CA  . GLY   A 1 60  ? 11.524 5.796   -11.749 1.00 63.83  ? 605  GLY   A CA  1 
ATOM   296  C C   . GLY   A 1 60  ? 11.674 4.306   -11.657 1.00 62.19  ? 605  GLY   A C   1 
ATOM   297  O O   . GLY   A 1 60  ? 11.002 3.657   -10.867 1.00 59.32  ? 605  GLY   A O   1 
ATOM   298  N N   . LYS   A 1 61  ? 12.557 3.760   -12.477 1.00 57.96  ? 606  LYS   A N   1 
ATOM   299  C CA  . LYS   A 1 61  ? 12.784 2.335   -12.466 1.00 52.32  ? 606  LYS   A CA  1 
ATOM   300  C C   . LYS   A 1 61  ? 14.202 2.010   -12.840 1.00 51.45  ? 606  LYS   A C   1 
ATOM   301  O O   . LYS   A 1 61  ? 14.884 2.812   -13.462 1.00 54.76  ? 606  LYS   A O   1 
ATOM   302  C CB  . LYS   A 1 61  ? 11.838 1.645   -13.441 1.00 54.64  ? 606  LYS   A CB  1 
ATOM   303  C CG  . LYS   A 1 61  ? 11.910 2.168   -14.862 1.00 62.55  ? 606  LYS   A CG  1 
ATOM   304  C CD  . LYS   A 1 61  ? 10.936 1.421   -15.754 1.00 65.37  ? 606  LYS   A CD  1 
ATOM   305  C CE  . LYS   A 1 61  ? 10.984 1.940   -17.179 1.00 67.09  ? 606  LYS   A CE  1 
ATOM   306  N NZ  . LYS   A 1 61  ? 10.102 1.148   -18.077 1.00 77.31  ? 606  LYS   A NZ  1 
ATOM   307  N N   . VAL   A 1 62  ? 14.657 0.836   -12.443 1.00 50.25  ? 607  VAL   A N   1 
ATOM   308  C CA  . VAL   A 1 62  ? 15.981 0.402   -12.813 1.00 50.54  ? 607  VAL   A CA  1 
ATOM   309  C C   . VAL   A 1 62  ? 15.801 -0.825  -13.665 1.00 53.23  ? 607  VAL   A C   1 
ATOM   310  O O   . VAL   A 1 62  ? 15.098 -1.753  -13.286 1.00 53.13  ? 607  VAL   A O   1 
ATOM   311  C CB  . VAL   A 1 62  ? 16.841 0.077   -11.587 1.00 50.00  ? 607  VAL   A CB  1 
ATOM   312  C CG1 . VAL   A 1 62  ? 18.251 -0.292  -12.016 1.00 51.19  ? 607  VAL   A CG1 1 
ATOM   313  C CG2 . VAL   A 1 62  ? 16.864 1.265   -10.645 1.00 54.02  ? 607  VAL   A CG2 1 
ATOM   314  N N   . VAL   A 1 63  ? 16.422 -0.826  -14.830 1.00 48.23  ? 608  VAL   A N   1 
ATOM   315  C CA  . VAL   A 1 63  ? 16.277 -1.945  -15.735 1.00 53.55  ? 608  VAL   A CA  1 
ATOM   316  C C   . VAL   A 1 63  ? 17.615 -2.573  -16.034 1.00 56.15  ? 608  VAL   A C   1 
ATOM   317  O O   . VAL   A 1 63  ? 18.652 -1.936  -15.900 1.00 53.85  ? 608  VAL   A O   1 
ATOM   318  C CB  . VAL   A 1 63  ? 15.628 -1.512  -17.059 1.00 48.44  ? 608  VAL   A CB  1 
ATOM   319  C CG1 . VAL   A 1 63  ? 14.280 -0.862  -16.796 1.00 54.12  ? 608  VAL   A CG1 1 
ATOM   320  C CG2 . VAL   A 1 63  ? 16.544 -0.571  -17.821 1.00 46.77  ? 608  VAL   A CG2 1 
ATOM   321  N N   . GLU   A 1 64  ? 17.596 -3.835  -16.421 1.00 56.75  ? 609  GLU   A N   1 
ATOM   322  C CA  . GLU   A 1 64  ? 18.820 -4.498  -16.795 1.00 54.61  ? 609  GLU   A CA  1 
ATOM   323  C C   . GLU   A 1 64  ? 19.138 -4.090  -18.202 1.00 50.26  ? 609  GLU   A C   1 
ATOM   324  O O   . GLU   A 1 64  ? 18.243 -3.819  -18.988 1.00 53.19  ? 609  GLU   A O   1 
ATOM   325  C CB  . GLU   A 1 64  ? 18.648 -6.004  -16.709 1.00 59.95  ? 609  GLU   A CB  1 
ATOM   326  C CG  . GLU   A 1 64  ? 19.788 -6.804  -17.310 1.00 70.50  ? 609  GLU   A CG  1 
ATOM   327  C CD  . GLU   A 1 64  ? 19.662 -8.289  -17.040 1.00 80.04  ? 609  GLU   A CD  1 
ATOM   328  O OE1 . GLU   A 1 64  ? 18.954 -8.662  -16.084 1.00 73.28  ? 609  GLU   A OE1 1 
ATOM   329  O OE2 . GLU   A 1 64  ? 20.281 -9.082  -17.777 1.00 83.69  ? 609  GLU   A OE2 1 
ATOM   330  N N   . GLY   A 1 65  ? 20.416 -4.034  -18.527 1.00 48.96  ? 610  GLY   A N   1 
ATOM   331  C CA  . GLY   A 1 65  ? 20.810 -3.675  -19.864 1.00 52.30  ? 610  GLY   A CA  1 
ATOM   332  C C   . GLY   A 1 65  ? 22.159 -4.173  -20.297 1.00 53.97  ? 610  GLY   A C   1 
ATOM   333  O O   . GLY   A 1 65  ? 22.990 -4.526  -19.469 1.00 53.36  ? 610  GLY   A O   1 
ATOM   334  N N   . THR   A 1 66  ? 22.379 -4.214  -21.601 1.00 47.14  ? 611  THR   A N   1 
ATOM   335  C CA  . THR   A 1 66  ? 23.677 -4.612  -22.115 1.00 48.46  ? 611  THR   A CA  1 
ATOM   336  C C   . THR   A 1 66  ? 24.273 -3.436  -22.852 1.00 48.94  ? 611  THR   A C   1 
ATOM   337  O O   . THR   A 1 66  ? 23.601 -2.791  -23.646 1.00 48.19  ? 611  THR   A O   1 
ATOM   338  C CB  . THR   A 1 66  ? 23.587 -5.836  -23.040 1.00 49.53  ? 611  THR   A CB  1 
ATOM   339  O OG1 . THR   A 1 66  ? 22.847 -5.497  -24.216 1.00 64.54  ? 611  THR   A OG1 1 
ATOM   340  C CG2 . THR   A 1 66  ? 22.899 -6.985  -22.327 1.00 53.68  ? 611  THR   A CG2 1 
ATOM   341  N N   . ALA   A 1 67  ? 25.532 -3.146  -22.582 1.00 47.69  ? 612  ALA   A N   1 
ATOM   342  C CA  . ALA   A 1 67  ? 26.173 -2.004  -23.197 1.00 48.92  ? 612  ALA   A CA  1 
ATOM   343  C C   . ALA   A 1 67  ? 27.318 -2.412  -24.089 1.00 48.13  ? 612  ALA   A C   1 
ATOM   344  O O   . ALA   A 1 67  ? 28.176 -3.191  -23.693 1.00 48.05  ? 612  ALA   A O   1 
ATOM   345  C CB  . ALA   A 1 67  ? 26.667 -1.063  -22.123 1.00 45.50  ? 612  ALA   A CB  1 
ATOM   346  N N   . TYR   A 1 68  ? 27.338 -1.870  -25.294 1.00 46.90  ? 613  TYR   A N   1 
ATOM   347  C CA  . TYR   A 1 68  ? 28.382 -2.201  -26.240 1.00 48.97  ? 613  TYR   A CA  1 
ATOM   348  C C   . TYR   A 1 68  ? 29.278 -1.006  -26.469 1.00 47.51  ? 613  TYR   A C   1 
ATOM   349  O O   . TYR   A 1 68  ? 28.836 0.015   -26.977 1.00 47.11  ? 613  TYR   A O   1 
ATOM   350  C CB  . TYR   A 1 68  ? 27.763 -2.643  -27.561 1.00 49.04  ? 613  TYR   A CB  1 
ATOM   351  C CG  . TYR   A 1 68  ? 26.810 -3.814  -27.463 1.00 57.08  ? 613  TYR   A CG  1 
ATOM   352  C CD1 . TYR   A 1 68  ? 25.569 -3.680  -26.855 1.00 57.61  ? 613  TYR   A CD1 1 
ATOM   353  C CD2 . TYR   A 1 68  ? 27.140 -5.046  -28.005 1.00 53.88  ? 613  TYR   A CD2 1 
ATOM   354  C CE1 . TYR   A 1 68  ? 24.696 -4.745  -26.771 1.00 53.99  ? 613  TYR   A CE1 1 
ATOM   355  C CE2 . TYR   A 1 68  ? 26.272 -6.116  -27.929 1.00 49.39  ? 613  TYR   A CE2 1 
ATOM   356  C CZ  . TYR   A 1 68  ? 25.053 -5.960  -27.311 1.00 57.06  ? 613  TYR   A CZ  1 
ATOM   357  O OH  . TYR   A 1 68  ? 24.189 -7.026  -27.234 1.00 56.14  ? 613  TYR   A OH  1 
ATOM   358  N N   . GLY   A 1 69  ? 30.542 -1.128  -26.099 1.00 48.31  ? 614  GLY   A N   1 
ATOM   359  C CA  . GLY   A 1 69  ? 31.480 -0.043  -26.289 1.00 47.50  ? 614  GLY   A CA  1 
ATOM   360  C C   . GLY   A 1 69  ? 31.743 0.844   -25.091 1.00 54.86  ? 614  GLY   A C   1 
ATOM   361  O O   . GLY   A 1 69  ? 32.452 1.835   -25.211 1.00 53.99  ? 614  GLY   A O   1 
ATOM   362  N N   . LEU   A 1 70  ? 31.177 0.504   -23.939 1.00 52.35  ? 615  LEU   A N   1 
ATOM   363  C CA  . LEU   A 1 70  ? 31.416 1.286   -22.730 1.00 60.76  ? 615  LEU   A CA  1 
ATOM   364  C C   . LEU   A 1 70  ? 32.727 0.900   -22.060 1.00 60.50  ? 615  LEU   A C   1 
ATOM   365  O O   . LEU   A 1 70  ? 33.475 1.766   -21.626 1.00 69.01  ? 615  LEU   A O   1 
ATOM   366  C CB  . LEU   A 1 70  ? 30.248 1.146   -21.755 1.00 57.67  ? 615  LEU   A CB  1 
ATOM   367  C CG  . LEU   A 1 70  ? 30.215 2.078   -20.547 1.00 56.05  ? 615  LEU   A CG  1 
ATOM   368  C CD1 . LEU   A 1 70  ? 28.785 2.474   -20.218 1.00 55.83  ? 615  LEU   A CD1 1 
ATOM   369  C CD2 . LEU   A 1 70  ? 30.893 1.437   -19.348 1.00 73.10  ? 615  LEU   A CD2 1 
ATOM   370  N N   . SER   A 1 71  ? 33.012 -0.393  -21.982 1.00 60.89  ? 616  SER   A N   1 
ATOM   371  C CA  . SER   A 1 71  ? 34.258 -0.857  -21.380 1.00 67.08  ? 616  SER   A CA  1 
ATOM   372  C C   . SER   A 1 71  ? 35.163 -1.477  -22.409 1.00 70.49  ? 616  SER   A C   1 
ATOM   373  O O   . SER   A 1 71  ? 34.706 -2.212  -23.278 1.00 73.79  ? 616  SER   A O   1 
ATOM   374  C CB  . SER   A 1 71  ? 33.992 -1.891  -20.295 1.00 67.78  ? 616  SER   A CB  1 
ATOM   375  O OG  . SER   A 1 71  ? 35.173 -2.597  -19.968 1.00 70.18  ? 616  SER   A OG  1 
ATOM   376  N N   . ARG   A 1 72  ? 36.450 -1.184  -22.323 1.00 71.76  ? 617  ARG   A N   1 
ATOM   377  C CA  . ARG   A 1 72  ? 37.396 -1.794  -23.233 1.00 77.69  ? 617  ARG   A CA  1 
ATOM   378  C C   . ARG   A 1 72  ? 37.588 -3.246  -22.861 1.00 77.00  ? 617  ARG   A C   1 
ATOM   379  O O   . ARG   A 1 72  ? 37.649 -4.112  -23.729 1.00 76.30  ? 617  ARG   A O   1 
ATOM   380  C CB  . ARG   A 1 72  ? 38.725 -1.055  -23.187 1.00 80.44  ? 617  ARG   A CB  1 
ATOM   381  C CG  . ARG   A 1 72  ? 38.650 0.391   -23.639 1.00 85.88  ? 617  ARG   A CG  1 
ATOM   382  C CD  . ARG   A 1 72  ? 40.024 1.034   -23.597 1.00 90.41  ? 617  ARG   A CD  1 
ATOM   383  N NE  . ARG   A 1 72  ? 40.609 0.962   -22.262 1.00 95.29  ? 617  ARG   A NE  1 
ATOM   384  C CZ  . ARG   A 1 72  ? 41.840 1.361   -21.963 1.00 99.68  ? 617  ARG   A CZ  1 
ATOM   385  N NH1 . ARG   A 1 72  ? 42.627 1.858   -22.906 1.00 90.75  ? 617  ARG   A NH1 1 
ATOM   386  N NH2 . ARG   A 1 72  ? 42.287 1.258   -20.719 1.00 99.91  ? 617  ARG   A NH2 1 
ATOM   387  N N   . SER   A 1 73  ? 37.681 -3.517  -21.567 1.00 68.97  ? 618  SER   A N   1 
ATOM   388  C CA  . SER   A 1 73  ? 37.860 -4.881  -21.103 1.00 68.89  ? 618  SER   A CA  1 
ATOM   389  C C   . SER   A 1 73  ? 36.648 -5.711  -21.443 1.00 73.12  ? 618  SER   A C   1 
ATOM   390  O O   . SER   A 1 73  ? 36.768 -6.886  -21.773 1.00 79.81  ? 618  SER   A O   1 
ATOM   391  C CB  . SER   A 1 73  ? 38.091 -4.896  -19.598 1.00 73.66  ? 618  SER   A CB  1 
ATOM   392  O OG  . SER   A 1 73  ? 36.982 -4.351  -18.909 1.00 81.87  ? 618  SER   A OG  1 
ATOM   393  N N   . GLN   A 1 74  ? 35.475 -5.109  -21.347 1.00 70.37  ? 619  GLN   A N   1 
ATOM   394  C CA  . GLN   A 1 74  ? 34.252 -5.822  -21.655 1.00 70.95  ? 619  GLN   A CA  1 
ATOM   395  C C   . GLN   A 1 74  ? 33.493 -5.080  -22.724 1.00 66.90  ? 619  GLN   A C   1 
ATOM   396  O O   . GLN   A 1 74  ? 32.772 -4.134  -22.433 1.00 68.58  ? 619  GLN   A O   1 
ATOM   397  C CB  . GLN   A 1 74  ? 33.391 -5.968  -20.406 1.00 65.60  ? 619  GLN   A CB  1 
ATOM   398  C CG  . GLN   A 1 74  ? 34.140 -6.515  -19.206 1.00 73.28  ? 619  GLN   A CG  1 
ATOM   399  C CD  . GLN   A 1 74  ? 33.239 -6.721  -18.008 1.00 75.14  ? 619  GLN   A CD  1 
ATOM   400  O OE1 . GLN   A 1 74  ? 32.017 -6.743  -18.133 1.00 83.17  ? 619  GLN   A OE1 1 
ATOM   401  N NE2 . GLN   A 1 74  ? 33.841 -6.879  -16.837 1.00 72.68  ? 619  GLN   A NE2 1 
ATOM   402  N N   . PRO   A 1 75  ? 33.658 -5.504  -23.974 1.00 67.05  ? 620  PRO   A N   1 
ATOM   403  C CA  . PRO   A 1 75  ? 32.967 -4.851  -25.086 1.00 63.89  ? 620  PRO   A CA  1 
ATOM   404  C C   . PRO   A 1 75  ? 31.473 -4.999  -24.947 1.00 57.81  ? 620  PRO   A C   1 
ATOM   405  O O   . PRO   A 1 75  ? 30.752 -4.080  -25.307 1.00 57.01  ? 620  PRO   A O   1 
ATOM   406  C CB  . PRO   A 1 75  ? 33.475 -5.616  -26.306 1.00 59.21  ? 620  PRO   A CB  1 
ATOM   407  C CG  . PRO   A 1 75  ? 33.971 -6.919  -25.777 1.00 65.86  ? 620  PRO   A CG  1 
ATOM   408  C CD  . PRO   A 1 75  ? 34.517 -6.610  -24.420 1.00 68.89  ? 620  PRO   A CD  1 
ATOM   409  N N   . VAL   A 1 76  ? 31.008 -6.138  -24.456 1.00 55.46  ? 621  VAL   A N   1 
ATOM   410  C CA  . VAL   A 1 76  ? 29.585 -6.312  -24.203 1.00 56.32  ? 621  VAL   A CA  1 
ATOM   411  C C   . VAL   A 1 76  ? 29.416 -6.522  -22.714 1.00 56.27  ? 621  VAL   A C   1 
ATOM   412  O O   . VAL   A 1 76  ? 29.694 -7.600  -22.205 1.00 60.88  ? 621  VAL   A O   1 
ATOM   413  C CB  . VAL   A 1 76  ? 28.988 -7.482  -24.991 1.00 54.36  ? 621  VAL   A CB  1 
ATOM   414  C CG1 . VAL   A 1 76  ? 27.483 -7.531  -24.792 1.00 56.07  ? 621  VAL   A CG1 1 
ATOM   415  C CG2 . VAL   A 1 76  ? 29.324 -7.345  -26.465 1.00 54.13  ? 621  VAL   A CG2 1 
ATOM   416  N N   . MET   A 1 77  ? 28.956 -5.496  -22.010 1.00 54.58  ? 622  MET   A N   1 
ATOM   417  C CA  . MET   A 1 77  ? 28.856 -5.578  -20.560 1.00 53.58  ? 622  MET   A CA  1 
ATOM   418  C C   . MET   A 1 77  ? 27.452 -5.404  -20.012 1.00 53.37  ? 622  MET   A C   1 
ATOM   419  O O   . MET   A 1 77  ? 26.708 -4.544  -20.461 1.00 54.47  ? 622  MET   A O   1 
ATOM   420  C CB  . MET   A 1 77  ? 29.774 -4.522  -19.948 1.00 57.70  ? 622  MET   A CB  1 
ATOM   421  C CG  . MET   A 1 77  ? 29.456 -4.149  -18.517 1.00 57.74  ? 622  MET   A CG  1 
ATOM   422  S SD  . MET   A 1 77  ? 30.456 -2.745  -18.006 1.00 70.82  ? 622  MET   A SD  1 
ATOM   423  C CE  . MET   A 1 77  ? 32.082 -3.485  -18.002 1.00 74.24  ? 622  MET   A CE  1 
ATOM   424  N N   . LYS   A 1 78  ? 27.095 -6.224  -19.033 1.00 56.76  ? 623  LYS   A N   1 
ATOM   425  C CA  . LYS   A 1 78  ? 25.788 -6.114  -18.410 1.00 55.58  ? 623  LYS   A CA  1 
ATOM   426  C C   . LYS   A 1 78  ? 25.768 -4.933  -17.490 1.00 53.10  ? 623  LYS   A C   1 
ATOM   427  O O   . LYS   A 1 78  ? 26.705 -4.711  -16.739 1.00 54.07  ? 623  LYS   A O   1 
ATOM   428  C CB  . LYS   A 1 78  ? 25.445 -7.374  -17.630 1.00 51.99  ? 623  LYS   A CB  1 
ATOM   429  C CG  . LYS   A 1 78  ? 24.444 -8.269  -18.335 1.00 72.29  ? 623  LYS   A CG  1 
ATOM   430  C CD  . LYS   A 1 78  ? 23.975 -9.382  -17.417 1.00 74.91  ? 623  LYS   A CD  1 
ATOM   431  C CE  . LYS   A 1 78  ? 23.565 -8.823  -16.067 1.00 69.39  ? 623  LYS   A CE  1 
ATOM   432  N NZ  . LYS   A 1 78  ? 22.614 -7.688  -16.198 1.00 63.57  ? 623  LYS   A NZ  1 
ATOM   433  N N   . VAL   A 1 79  ? 24.688 -4.176  -17.537 1.00 54.43  ? 624  VAL   A N   1 
ATOM   434  C CA  . VAL   A 1 79  ? 24.622 -2.975  -16.745 1.00 52.87  ? 624  VAL   A CA  1 
ATOM   435  C C   . VAL   A 1 79  ? 23.237 -2.723  -16.203 1.00 50.55  ? 624  VAL   A C   1 
ATOM   436  O O   . VAL   A 1 79  ? 22.289 -3.411  -16.559 1.00 48.42  ? 624  VAL   A O   1 
ATOM   437  C CB  . VAL   A 1 79  ? 25.038 -1.754  -17.589 1.00 56.31  ? 624  VAL   A CB  1 
ATOM   438  C CG1 . VAL   A 1 79  ? 26.496 -1.853  -18.004 1.00 50.01  ? 624  VAL   A CG1 1 
ATOM   439  C CG2 . VAL   A 1 79  ? 24.141 -1.621  -18.808 1.00 49.02  ? 624  VAL   A CG2 1 
ATOM   440  N N   . ALA   A 1 80  ? 23.125 -1.741  -15.327 1.00 50.07  ? 625  ALA   A N   1 
ATOM   441  C CA  . ALA   A 1 80  ? 21.832 -1.368  -14.802 1.00 50.44  ? 625  ALA   A CA  1 
ATOM   442  C C   . ALA   A 1 80  ? 21.544 0.033   -15.273 1.00 46.27  ? 625  ALA   A C   1 
ATOM   443  O O   . ALA   A 1 80  ? 22.441 0.861   -15.344 1.00 45.95  ? 625  ALA   A O   1 
ATOM   444  C CB  . ALA   A 1 80  ? 21.837 -1.430  -13.294 1.00 50.62  ? 625  ALA   A CB  1 
ATOM   445  N N   . VAL   A 1 81  ? 20.297 0.304   -15.616 1.00 44.69  ? 626  VAL   A N   1 
ATOM   446  C CA  . VAL   A 1 81  ? 19.951 1.613   -16.133 1.00 46.00  ? 626  VAL   A CA  1 
ATOM   447  C C   . VAL   A 1 81  ? 18.832 2.262   -15.342 1.00 44.25  ? 626  VAL   A C   1 
ATOM   448  O O   . VAL   A 1 81  ? 17.758 1.694   -15.202 1.00 40.62  ? 626  VAL   A O   1 
ATOM   449  C CB  . VAL   A 1 81  ? 19.552 1.538   -17.620 1.00 49.80  ? 626  VAL   A CB  1 
ATOM   450  C CG1 . VAL   A 1 81  ? 19.352 2.934   -18.186 1.00 46.54  ? 626  VAL   A CG1 1 
ATOM   451  C CG2 . VAL   A 1 81  ? 20.606 0.785   -18.414 1.00 45.22  ? 626  VAL   A CG2 1 
ATOM   452  N N   . LYS   A 1 82  ? 19.091 3.457   -14.824 1.00 48.91  ? 627  LYS   A N   1 
ATOM   453  C CA  . LYS   A 1 82  ? 18.074 4.190   -14.093 1.00 47.77  ? 627  LYS   A CA  1 
ATOM   454  C C   . LYS   A 1 82  ? 17.358 5.106   -15.049 1.00 50.87  ? 627  LYS   A C   1 
ATOM   455  O O   . LYS   A 1 82  ? 17.985 5.859   -15.785 1.00 49.44  ? 627  LYS   A O   1 
ATOM   456  C CB  . LYS   A 1 82  ? 18.695 4.985   -12.949 1.00 48.43  ? 627  LYS   A CB  1 
ATOM   457  C CG  . LYS   A 1 82  ? 17.740 5.913   -12.223 1.00 50.89  ? 627  LYS   A CG  1 
ATOM   458  C CD  . LYS   A 1 82  ? 16.687 5.144   -11.447 1.00 54.46  ? 627  LYS   A CD  1 
ATOM   459  C CE  . LYS   A 1 82  ? 15.785 6.094   -10.679 1.00 61.99  ? 627  LYS   A CE  1 
ATOM   460  N NZ  . LYS   A 1 82  ? 16.551 6.933   -9.717  1.00 65.00  ? 627  LYS   A NZ  1 
ATOM   461  N N   . MET   A 1 83  ? 16.038 5.037   -15.044 1.00 53.79  ? 628  MET   A N   1 
ATOM   462  C CA  . MET   A 1 83  ? 15.259 5.835   -15.963 1.00 56.16  ? 628  MET   A CA  1 
ATOM   463  C C   . MET   A 1 83  ? 13.931 6.199   -15.357 1.00 58.34  ? 628  MET   A C   1 
ATOM   464  O O   . MET   A 1 83  ? 13.465 5.545   -14.430 1.00 63.05  ? 628  MET   A O   1 
ATOM   465  C CB  . MET   A 1 83  ? 15.033 5.054   -17.253 1.00 55.42  ? 628  MET   A CB  1 
ATOM   466  C CG  . MET   A 1 83  ? 14.492 3.653   -17.041 1.00 58.48  ? 628  MET   A CG  1 
ATOM   467  S SD  . MET   A 1 83  ? 14.425 2.713   -18.575 1.00 61.59  ? 628  MET   A SD  1 
ATOM   468  C CE  . MET   A 1 83  ? 13.352 3.754   -19.554 1.00 61.91  ? 628  MET   A CE  1 
ATOM   469  N N   . LEU   A 1 84  ? 13.317 7.249   -15.872 1.00 59.75  ? 629  LEU   A N   1 
ATOM   470  C CA  . LEU   A 1 84  ? 12.007 7.640   -15.399 1.00 60.21  ? 629  LEU   A CA  1 
ATOM   471  C C   . LEU   A 1 84  ? 10.968 6.753   -16.033 1.00 67.45  ? 629  LEU   A C   1 
ATOM   472  O O   . LEU   A 1 84  ? 11.135 6.298   -17.160 1.00 69.13  ? 629  LEU   A O   1 
ATOM   473  C CB  . LEU   A 1 84  ? 11.725 9.093   -15.755 1.00 59.59  ? 629  LEU   A CB  1 
ATOM   474  C CG  . LEU   A 1 84  ? 11.980 10.152  -14.686 1.00 67.70  ? 629  LEU   A CG  1 
ATOM   475  C CD1 . LEU   A 1 84  ? 13.269 9.891   -13.929 1.00 64.39  ? 629  LEU   A CD1 1 
ATOM   476  C CD2 . LEU   A 1 84  ? 11.984 11.530  -15.321 1.00 67.73  ? 629  LEU   A CD2 1 
ATOM   477  N N   . LYS   A 1 85  ? 9.889  6.502   -15.311 1.00 73.85  ? 630  LYS   A N   1 
ATOM   478  C CA  . LYS   A 1 85  ? 8.820  5.684   -15.846 1.00 75.65  ? 630  LYS   A CA  1 
ATOM   479  C C   . LYS   A 1 85  ? 7.990  6.507   -16.801 1.00 79.57  ? 630  LYS   A C   1 
ATOM   480  O O   . LYS   A 1 85  ? 8.086  7.729   -16.821 1.00 82.66  ? 630  LYS   A O   1 
ATOM   481  C CB  . LYS   A 1 85  ? 7.947  5.152   -14.717 1.00 75.19  ? 630  LYS   A CB  1 
ATOM   482  C CG  . LYS   A 1 85  ? 7.771  3.644   -14.729 1.00 78.29  ? 630  LYS   A CG  1 
ATOM   483  C CD  . LYS   A 1 85  ? 6.849  3.186   -13.614 1.00 78.13  ? 630  LYS   A CD  1 
ATOM   484  C CE  . LYS   A 1 85  ? 6.539  1.704   -13.738 1.00 82.32  ? 630  LYS   A CE  1 
ATOM   485  N NZ  . LYS   A 1 85  ? 7.777  0.877   -13.752 1.00 76.86  ? 630  LYS   A NZ  1 
ATOM   486  N N   . PRO   A 1 86  ? 7.164  5.840   -17.606 1.00 85.09  ? 631  PRO   A N   1 
ATOM   487  C CA  . PRO   A 1 86  ? 6.283  6.581   -18.503 1.00 89.27  ? 631  PRO   A CA  1 
ATOM   488  C C   . PRO   A 1 86  ? 5.495  7.632   -17.745 1.00 93.40  ? 631  PRO   A C   1 
ATOM   489  O O   . PRO   A 1 86  ? 5.279  8.723   -18.267 1.00 93.20  ? 631  PRO   A O   1 
ATOM   490  C CB  . PRO   A 1 86  ? 5.343  5.501   -19.011 1.00 93.43  ? 631  PRO   A CB  1 
ATOM   491  C CG  . PRO   A 1 86  ? 6.173  4.265   -19.017 1.00 92.69  ? 631  PRO   A CG  1 
ATOM   492  C CD  . PRO   A 1 86  ? 7.129  4.391   -17.865 1.00 81.71  ? 631  PRO   A CD  1 
ATOM   493  N N   . THR   A 1 87  ? 5.072  7.314   -16.529 1.00 90.99  ? 632  THR   A N   1 
ATOM   494  C CA  . THR   A 1 87  ? 4.343  8.278   -15.715 1.00 96.03  ? 632  THR   A CA  1 
ATOM   495  C C   . THR   A 1 87  ? 5.173  9.528   -15.427 1.00 93.77  ? 632  THR   A C   1 
ATOM   496  O O   . THR   A 1 87  ? 6.262  9.452   -14.862 1.00 90.72  ? 632  THR   A O   1 
ATOM   497  C CB  . THR   A 1 87  ? 3.893  7.656   -14.384 1.00 88.36  ? 632  THR   A CB  1 
ATOM   498  O OG1 . THR   A 1 87  ? 3.435  8.691   -13.507 1.00 84.24  ? 632  THR   A OG1 1 
ATOM   499  C CG2 . THR   A 1 87  ? 5.044  6.916   -13.724 1.00 86.91  ? 632  THR   A CG2 1 
ATOM   500  N N   . SER   A 1 91  ? 8.628  17.050  -12.985 1.00 81.73  ? 636  SER   A N   1 
ATOM   501  C CA  . SER   A 1 91  ? 9.349  17.311  -11.745 1.00 88.44  ? 636  SER   A CA  1 
ATOM   502  C C   . SER   A 1 91  ? 10.385 16.243  -11.461 1.00 89.61  ? 636  SER   A C   1 
ATOM   503  O O   . SER   A 1 91  ? 11.187 16.385  -10.542 1.00 87.79  ? 636  SER   A O   1 
ATOM   504  C CB  . SER   A 1 91  ? 8.376  17.383  -10.569 1.00 86.89  ? 636  SER   A CB  1 
ATOM   505  O OG  . SER   A 1 91  ? 7.723  16.143  -10.372 1.00 88.02  ? 636  SER   A OG  1 
ATOM   506  N N   . SER   A 1 92  ? 10.373 15.169  -12.239 1.00 86.96  ? 637  SER   A N   1 
ATOM   507  C CA  . SER   A 1 92  ? 11.287 14.069  -11.981 1.00 81.71  ? 637  SER   A CA  1 
ATOM   508  C C   . SER   A 1 92  ? 12.478 14.076  -12.918 1.00 74.75  ? 637  SER   A C   1 
ATOM   509  O O   . SER   A 1 92  ? 13.538 13.561  -12.577 1.00 72.16  ? 637  SER   A O   1 
ATOM   510  C CB  . SER   A 1 92  ? 10.537 12.744  -12.100 1.00 78.61  ? 637  SER   A CB  1 
ATOM   511  O OG  . SER   A 1 92  ? 9.451  12.688  -11.194 1.00 77.21  ? 637  SER   A OG  1 
ATOM   512  N N   . LYS   A 1 93  ? 12.316 14.662  -14.092 1.00 72.47  ? 638  LYS   A N   1 
ATOM   513  C CA  . LYS   A 1 93  ? 13.389 14.637  -15.073 1.00 76.09  ? 638  LYS   A CA  1 
ATOM   514  C C   . LYS   A 1 93  ? 14.628 15.325  -14.559 1.00 77.11  ? 638  LYS   A C   1 
ATOM   515  O O   . LYS   A 1 93  ? 15.736 14.815  -14.706 1.00 77.41  ? 638  LYS   A O   1 
ATOM   516  C CB  . LYS   A 1 93  ? 12.935 15.303  -16.365 1.00 80.76  ? 638  LYS   A CB  1 
ATOM   517  C CG  . LYS   A 1 93  ? 14.021 15.401  -17.422 1.00 80.58  ? 638  LYS   A CG  1 
ATOM   518  C CD  . LYS   A 1 93  ? 14.491 14.024  -17.858 1.00 82.83  ? 638  LYS   A CD  1 
ATOM   519  C CE  . LYS   A 1 93  ? 13.352 13.226  -18.468 1.00 82.30  ? 638  LYS   A CE  1 
ATOM   520  N NZ  . LYS   A 1 93  ? 13.802 11.897  -18.960 1.00 64.88  ? 638  LYS   A NZ  1 
ATOM   521  N N   . GLN   A 1 94  ? 14.446 16.491  -13.960 1.00 78.81  ? 639  GLN   A N   1 
ATOM   522  C CA  . GLN   A 1 94  ? 15.580 17.239  -13.445 1.00 78.57  ? 639  GLN   A CA  1 
ATOM   523  C C   . GLN   A 1 94  ? 16.099 16.605  -12.180 1.00 72.03  ? 639  GLN   A C   1 
ATOM   524  O O   . GLN   A 1 94  ? 17.269 16.744  -11.849 1.00 73.65  ? 639  GLN   A O   1 
ATOM   525  C CB  . GLN   A 1 94  ? 15.193 18.694  -13.217 1.00 81.88  ? 639  GLN   A CB  1 
ATOM   526  C CG  . GLN   A 1 94  ? 14.758 19.389  -14.493 1.00 82.43  ? 639  GLN   A CG  1 
ATOM   527  C CD  . GLN   A 1 94  ? 15.742 19.182  -15.629 1.00 90.96  ? 639  GLN   A CD  1 
ATOM   528  O OE1 . GLN   A 1 94  ? 16.954 19.120  -15.416 1.00 89.38  ? 639  GLN   A OE1 1 
ATOM   529  N NE2 . GLN   A 1 94  ? 15.225 19.080  -16.847 1.00 93.34  ? 639  GLN   A NE2 1 
ATOM   530  N N   . ALA   A 1 95  ? 15.233 15.910  -11.465 1.00 69.72  ? 640  ALA   A N   1 
ATOM   531  C CA  . ALA   A 1 95  ? 15.679 15.202  -10.286 1.00 67.07  ? 640  ALA   A CA  1 
ATOM   532  C C   . ALA   A 1 95  ? 16.619 14.104  -10.718 1.00 69.61  ? 640  ALA   A C   1 
ATOM   533  O O   . ALA   A 1 95  ? 17.607 13.825  -10.047 1.00 68.12  ? 640  ALA   A O   1 
ATOM   534  C CB  . ALA   A 1 95  ? 14.498 14.626  -9.544  1.00 70.38  ? 640  ALA   A CB  1 
ATOM   535  N N   . LEU   A 1 96  ? 16.313 13.474  -11.841 1.00 67.16  ? 641  LEU   A N   1 
ATOM   536  C CA  . LEU   A 1 96  ? 17.175 12.429  -12.353 1.00 66.09  ? 641  LEU   A CA  1 
ATOM   537  C C   . LEU   A 1 96  ? 18.486 13.047  -12.753 1.00 62.48  ? 641  LEU   A C   1 
ATOM   538  O O   . LEU   A 1 96  ? 19.545 12.478  -12.523 1.00 62.79  ? 641  LEU   A O   1 
ATOM   539  C CB  . LEU   A 1 96  ? 16.530 11.735  -13.548 1.00 63.22  ? 641  LEU   A CB  1 
ATOM   540  C CG  . LEU   A 1 96  ? 17.122 10.387  -13.952 1.00 58.66  ? 641  LEU   A CG  1 
ATOM   541  C CD1 . LEU   A 1 96  ? 16.962 9.387   -12.820 1.00 59.13  ? 641  LEU   A CD1 1 
ATOM   542  C CD2 . LEU   A 1 96  ? 16.460 9.870   -15.216 1.00 58.61  ? 641  LEU   A CD2 1 
ATOM   543  N N   . MET   A 1 97  ? 18.418 14.225  -13.351 1.00 64.72  ? 642  MET   A N   1 
ATOM   544  C CA  . MET   A 1 97  ? 19.629 14.895  -13.780 1.00 64.33  ? 642  MET   A CA  1 
ATOM   545  C C   . MET   A 1 97  ? 20.455 15.245  -12.570 1.00 64.47  ? 642  MET   A C   1 
ATOM   546  O O   . MET   A 1 97  ? 21.671 15.121  -12.589 1.00 64.06  ? 642  MET   A O   1 
ATOM   547  C CB  . MET   A 1 97  ? 19.304 16.150  -14.576 1.00 59.85  ? 642  MET   A CB  1 
ATOM   548  C CG  . MET   A 1 97  ? 20.492 16.693  -15.352 1.00 67.50  ? 642  MET   A CG  1 
ATOM   549  S SD  . MET   A 1 97  ? 21.077 15.533  -16.602 1.00 79.19  ? 642  MET   A SD  1 
ATOM   550  C CE  . MET   A 1 97  ? 22.578 16.337  -17.151 1.00 60.28  ? 642  MET   A CE  1 
ATOM   551  N N   . SER   A 1 98  ? 19.795 15.677  -11.510 1.00 62.53  ? 643  SER   A N   1 
ATOM   552  C CA  . SER   A 1 98  ? 20.495 16.014  -10.291 1.00 59.54  ? 643  SER   A CA  1 
ATOM   553  C C   . SER   A 1 98  ? 21.145 14.777  -9.718  1.00 59.35  ? 643  SER   A C   1 
ATOM   554  O O   . SER   A 1 98  ? 22.257 14.841  -9.206  1.00 64.59  ? 643  SER   A O   1 
ATOM   555  C CB  . SER   A 1 98  ? 19.523 16.620  -9.294  1.00 62.34  ? 643  SER   A CB  1 
ATOM   556  O OG  . SER   A 1 98  ? 18.838 17.723  -9.857  1.00 72.99  ? 643  SER   A OG  1 
ATOM   557  N N   . GLU   A 1 99  ? 20.460 13.646  -9.802  1.00 57.30  ? 644  GLU   A N   1 
ATOM   558  C CA  . GLU   A 1 99  ? 21.022 12.396  -9.328  1.00 50.29  ? 644  GLU   A CA  1 
ATOM   559  C C   . GLU   A 1 99  ? 22.276 12.113  -10.104 1.00 61.84  ? 644  GLU   A C   1 
ATOM   560  O O   . GLU   A 1 99  ? 23.284 11.705  -9.543  1.00 63.90  ? 644  GLU   A O   1 
ATOM   561  C CB  . GLU   A 1 99  ? 20.020 11.270  -9.519  1.00 46.16  ? 644  GLU   A CB  1 
ATOM   562  C CG  . GLU   A 1 99  ? 20.477 9.902   -9.048  1.00 53.31  ? 644  GLU   A CG  1 
ATOM   563  C CD  . GLU   A 1 99  ? 19.392 8.852   -9.199  1.00 60.16  ? 644  GLU   A CD  1 
ATOM   564  O OE1 . GLU   A 1 99  ? 18.255 9.220   -9.557  1.00 63.44  ? 644  GLU   A OE1 1 
ATOM   565  O OE2 . GLU   A 1 99  ? 19.670 7.660   -8.962  1.00 51.01  ? 644  GLU   A OE2 1 
ATOM   566  N N   . LEU   A 1 100 ? 22.226 12.344  -11.405 1.00 59.62  ? 645  LEU   A N   1 
ATOM   567  C CA  . LEU   A 1 100 ? 23.392 12.130  -12.236 1.00 56.56  ? 645  LEU   A CA  1 
ATOM   568  C C   . LEU   A 1 100 ? 24.506 13.046  -11.801 1.00 54.70  ? 645  LEU   A C   1 
ATOM   569  O O   . LEU   A 1 100 ? 25.655 12.634  -11.707 1.00 56.54  ? 645  LEU   A O   1 
ATOM   570  C CB  . LEU   A 1 100 ? 23.046 12.387  -13.700 1.00 56.73  ? 645  LEU   A CB  1 
ATOM   571  C CG  . LEU   A 1 100 ? 24.150 12.175  -14.731 1.00 53.61  ? 645  LEU   A CG  1 
ATOM   572  C CD1 . LEU   A 1 100 ? 24.611 10.728  -14.720 1.00 53.72  ? 645  LEU   A CD1 1 
ATOM   573  C CD2 . LEU   A 1 100 ? 23.648 12.566  -16.109 1.00 55.73  ? 645  LEU   A CD2 1 
ATOM   574  N N   . LYS   A 1 101 ? 24.168 14.291  -11.518 1.00 54.80  ? 646  LYS   A N   1 
ATOM   575  C CA  . LYS   A 1 101 ? 25.185 15.261  -11.150 1.00 60.54  ? 646  LYS   A CA  1 
ATOM   576  C C   . LYS   A 1 101 ? 25.900 14.897  -9.859  1.00 62.71  ? 646  LYS   A C   1 
ATOM   577  O O   . LYS   A 1 101 ? 27.123 14.934  -9.793  1.00 67.86  ? 646  LYS   A O   1 
ATOM   578  C CB  . LYS   A 1 101 ? 24.566 16.650  -11.037 1.00 63.16  ? 646  LYS   A CB  1 
ATOM   579  C CG  . LYS   A 1 101 ? 23.851 17.107  -12.295 1.00 58.53  ? 646  LYS   A CG  1 
ATOM   580  C CD  . LYS   A 1 101 ? 23.313 18.518  -12.149 1.00 55.05  ? 646  LYS   A CD  1 
ATOM   581  C CE  . LYS   A 1 101 ? 24.425 19.539  -12.293 1.00 63.58  ? 646  LYS   A CE  1 
ATOM   582  N NZ  . LYS   A 1 101 ? 25.027 19.494  -13.653 1.00 68.49  ? 646  LYS   A NZ  1 
ATOM   583  N N   . ILE   A 1 102 ? 25.144 14.530  -8.838  1.00 57.87  ? 647  ILE   A N   1 
ATOM   584  C CA  . ILE   A 1 102 ? 25.762 14.163  -7.581  1.00 59.58  ? 647  ILE   A CA  1 
ATOM   585  C C   . ILE   A 1 102 ? 26.647 12.946  -7.784  1.00 60.75  ? 647  ILE   A C   1 
ATOM   586  O O   . ILE   A 1 102 ? 27.746 12.875  -7.246  1.00 58.95  ? 647  ILE   A O   1 
ATOM   587  C CB  . ILE   A 1 102 ? 24.721 13.899  -6.473  1.00 61.10  ? 647  ILE   A CB  1 
ATOM   588  C CG1 . ILE   A 1 102 ? 23.669 12.903  -6.944  1.00 64.48  ? 647  ILE   A CG1 1 
ATOM   589  C CG2 . ILE   A 1 102 ? 24.054 15.194  -6.047  1.00 64.17  ? 647  ILE   A CG2 1 
ATOM   590  C CD1 . ILE   A 1 102 ? 22.535 12.709  -5.964  1.00 63.48  ? 647  ILE   A CD1 1 
ATOM   591  N N   . MET   A 1 103 ? 26.180 11.997  -8.577  1.00 57.66  ? 648  MET   A N   1 
ATOM   592  C CA  . MET   A 1 103 ? 26.947 10.785  -8.816  1.00 63.42  ? 648  MET   A CA  1 
ATOM   593  C C   . MET   A 1 103 ? 28.231 11.083  -9.557  1.00 61.56  ? 648  MET   A C   1 
ATOM   594  O O   . MET   A 1 103 ? 29.251 10.448  -9.319  1.00 63.62  ? 648  MET   A O   1 
ATOM   595  C CB  . MET   A 1 103 ? 26.111 9.772   -9.594  1.00 59.74  ? 648  MET   A CB  1 
ATOM   596  C CG  . MET   A 1 103 ? 25.110 9.012   -8.744  1.00 61.60  ? 648  MET   A CG  1 
ATOM   597  S SD  . MET   A 1 103 ? 24.302 7.698   -9.672  1.00 58.51  ? 648  MET   A SD  1 
ATOM   598  C CE  . MET   A 1 103 ? 23.373 8.664   -10.853 1.00 53.19  ? 648  MET   A CE  1 
ATOM   599  N N   . THR   A 1 104 ? 28.184 12.049  -10.459 1.00 60.42  ? 649  THR   A N   1 
ATOM   600  C CA  . THR   A 1 104 ? 29.365 12.419  -11.217 1.00 60.22  ? 649  THR   A CA  1 
ATOM   601  C C   . THR   A 1 104 ? 30.444 12.975  -10.322 1.00 63.17  ? 649  THR   A C   1 
ATOM   602  O O   . THR   A 1 104 ? 31.618 12.672  -10.501 1.00 63.43  ? 649  THR   A O   1 
ATOM   603  C CB  . THR   A 1 104 ? 29.019 13.481  -12.272 1.00 58.73  ? 649  THR   A CB  1 
ATOM   604  O OG1 . THR   A 1 104 ? 28.108 12.926  -13.228 1.00 65.34  ? 649  THR   A OG1 1 
ATOM   605  C CG2 . THR   A 1 104 ? 30.271 13.947  -12.987 1.00 69.54  ? 649  THR   A CG2 1 
ATOM   606  N N   . HIS   A 1 105 ? 30.060 13.779  -9.345  1.00 60.87  ? 650  HIS   A N   1 
ATOM   607  C CA  . HIS   A 1 105 ? 31.051 14.432  -8.498  1.00 58.53  ? 650  HIS   A CA  1 
ATOM   608  C C   . HIS   A 1 105 ? 31.420 13.673  -7.230  1.00 62.61  ? 650  HIS   A C   1 
ATOM   609  O O   . HIS   A 1 105 ? 32.351 14.053  -6.532  1.00 71.21  ? 650  HIS   A O   1 
ATOM   610  C CB  . HIS   A 1 105 ? 30.550 15.824  -8.134  1.00 61.38  ? 650  HIS   A CB  1 
ATOM   611  C CG  . HIS   A 1 105 ? 30.252 16.682  -9.321  1.00 64.61  ? 650  HIS   A CG  1 
ATOM   612  N ND1 . HIS   A 1 105 ? 31.211 17.025  -10.248 1.00 62.92  ? 650  HIS   A ND1 1 
ATOM   613  C CD2 . HIS   A 1 105 ? 29.103 17.267  -9.733  1.00 69.13  ? 650  HIS   A CD2 1 
ATOM   614  C CE1 . HIS   A 1 105 ? 30.666 17.782  -11.182 1.00 69.49  ? 650  HIS   A CE1 1 
ATOM   615  N NE2 . HIS   A 1 105 ? 29.388 17.946  -10.892 1.00 70.37  ? 650  HIS   A NE2 1 
ATOM   616  N N   . LEU   A 1 106 ? 30.701 12.604  -6.933  1.00 64.35  ? 651  LEU   A N   1 
ATOM   617  C CA  . LEU   A 1 106 ? 30.990 11.829  -5.739  1.00 69.02  ? 651  LEU   A CA  1 
ATOM   618  C C   . LEU   A 1 106 ? 32.350 11.176  -5.835  1.00 71.52  ? 651  LEU   A C   1 
ATOM   619  O O   . LEU   A 1 106 ? 33.073 11.085  -4.852  1.00 72.26  ? 651  LEU   A O   1 
ATOM   620  C CB  . LEU   A 1 106 ? 29.916 10.769  -5.499  1.00 69.51  ? 651  LEU   A CB  1 
ATOM   621  C CG  . LEU   A 1 106 ? 28.630 11.252  -4.837  1.00 67.47  ? 651  LEU   A CG  1 
ATOM   622  C CD1 . LEU   A 1 106 ? 27.633 10.111  -4.735  1.00 71.62  ? 651  LEU   A CD1 1 
ATOM   623  C CD2 . LEU   A 1 106 ? 28.929 11.832  -3.466  1.00 64.27  ? 651  LEU   A CD2 1 
ATOM   624  N N   . GLY   A 1 107 ? 32.703 10.714  -7.018  1.00 66.11  ? 652  GLY   A N   1 
ATOM   625  C CA  . GLY   A 1 107 ? 33.963 10.033  -7.179  1.00 67.98  ? 652  GLY   A CA  1 
ATOM   626  C C   . GLY   A 1 107 ? 33.808 8.561   -6.923  1.00 71.76  ? 652  GLY   A C   1 
ATOM   627  O O   . GLY   A 1 107 ? 32.731 8.099   -6.569  1.00 75.53  ? 652  GLY   A O   1 
ATOM   628  N N   . PRO   A 1 108 ? 34.889 7.808   -7.095  1.00 70.10  ? 653  PRO   A N   1 
ATOM   629  C CA  . PRO   A 1 108 ? 34.812 6.359   -6.931  1.00 68.79  ? 653  PRO   A CA  1 
ATOM   630  C C   . PRO   A 1 108 ? 34.950 5.869   -5.499  1.00 72.33  ? 653  PRO   A C   1 
ATOM   631  O O   . PRO   A 1 108 ? 35.616 6.519   -4.699  1.00 66.16  ? 653  PRO   A O   1 
ATOM   632  C CB  . PRO   A 1 108 ? 36.015 5.876   -7.731  1.00 62.09  ? 653  PRO   A CB  1 
ATOM   633  C CG  . PRO   A 1 108 ? 37.008 6.974   -7.595  1.00 66.03  ? 653  PRO   A CG  1 
ATOM   634  C CD  . PRO   A 1 108 ? 36.218 8.251   -7.544  1.00 72.01  ? 653  PRO   A CD  1 
ATOM   635  N N   . HIS   A 1 109 ? 34.318 4.745   -5.178  1.00 71.43  ? 654  HIS   A N   1 
ATOM   636  C CA  . HIS   A 1 109 ? 34.463 4.141   -3.858  1.00 63.02  ? 654  HIS   A CA  1 
ATOM   637  C C   . HIS   A 1 109 ? 34.049 2.695   -3.978  1.00 65.48  ? 654  HIS   A C   1 
ATOM   638  O O   . HIS   A 1 109 ? 33.144 2.371   -4.737  1.00 66.35  ? 654  HIS   A O   1 
ATOM   639  C CB  . HIS   A 1 109 ? 33.631 4.849   -2.803  1.00 69.33  ? 654  HIS   A CB  1 
ATOM   640  C CG  . HIS   A 1 109 ? 33.927 4.401   -1.406  1.00 69.56  ? 654  HIS   A CG  1 
ATOM   641  N ND1 . HIS   A 1 109 ? 33.395 3.251   -0.865  1.00 70.35  ? 654  HIS   A ND1 1 
ATOM   642  C CD2 . HIS   A 1 109 ? 34.704 4.946   -0.441  1.00 68.98  ? 654  HIS   A CD2 1 
ATOM   643  C CE1 . HIS   A 1 109 ? 33.830 3.107   0.373   1.00 66.56  ? 654  HIS   A CE1 1 
ATOM   644  N NE2 . HIS   A 1 109 ? 34.625 4.123   0.655   1.00 64.36  ? 654  HIS   A NE2 1 
ATOM   645  N N   . LEU   A 1 110 ? 34.702 1.820   -3.234  1.00 64.64  ? 655  LEU   A N   1 
ATOM   646  C CA  . LEU   A 1 110 ? 34.424 0.394   -3.341  1.00 64.62  ? 655  LEU   A CA  1 
ATOM   647  C C   . LEU   A 1 110 ? 33.020 0.028   -2.910  1.00 62.70  ? 655  LEU   A C   1 
ATOM   648  O O   . LEU   A 1 110 ? 32.401 -0.853  -3.492  1.00 61.29  ? 655  LEU   A O   1 
ATOM   649  C CB  . LEU   A 1 110 ? 35.438 -0.386  -2.503  1.00 68.09  ? 655  LEU   A CB  1 
ATOM   650  C CG  . LEU   A 1 110 ? 35.278 -1.899  -2.397  1.00 68.86  ? 655  LEU   A CG  1 
ATOM   651  C CD1 . LEU   A 1 110 ? 35.606 -2.550  -3.730  1.00 72.37  ? 655  LEU   A CD1 1 
ATOM   652  C CD2 . LEU   A 1 110 ? 36.190 -2.431  -1.305  1.00 74.71  ? 655  LEU   A CD2 1 
ATOM   653  N N   . ASN   A 1 111 ? 32.512 0.698   -1.891  1.00 62.14  ? 656  ASN   A N   1 
ATOM   654  C CA  . ASN   A 1 111 ? 31.201 0.348   -1.368  1.00 63.81  ? 656  ASN   A CA  1 
ATOM   655  C C   . ASN   A 1 111 ? 30.113 1.241   -1.930  1.00 61.34  ? 656  ASN   A C   1 
ATOM   656  O O   . ASN   A 1 111 ? 28.997 1.258   -1.423  1.00 56.71  ? 656  ASN   A O   1 
ATOM   657  C CB  . ASN   A 1 111 ? 31.239 0.392   0.153   1.00 60.40  ? 656  ASN   A CB  1 
ATOM   658  C CG  . ASN   A 1 111 ? 32.264 -0.562  0.729   1.00 64.64  ? 656  ASN   A CG  1 
ATOM   659  O OD1 . ASN   A 1 111 ? 32.942 -0.249  1.704   1.00 70.96  ? 656  ASN   A OD1 1 
ATOM   660  N ND2 . ASN   A 1 111 ? 32.393 -1.729  0.113   1.00 58.11  ? 656  ASN   A ND2 1 
ATOM   661  N N   . ILE   A 1 112 ? 30.433 1.989   -2.975  1.00 62.85  ? 657  ILE   A N   1 
ATOM   662  C CA  . ILE   A 1 112 ? 29.430 2.805   -3.634  1.00 59.44  ? 657  ILE   A CA  1 
ATOM   663  C C   . ILE   A 1 112 ? 29.314 2.305   -5.055  1.00 60.51  ? 657  ILE   A C   1 
ATOM   664  O O   . ILE   A 1 112 ? 30.318 2.135   -5.735  1.00 65.99  ? 657  ILE   A O   1 
ATOM   665  C CB  . ILE   A 1 112 ? 29.804 4.289   -3.645  1.00 60.71  ? 657  ILE   A CB  1 
ATOM   666  C CG1 . ILE   A 1 112 ? 29.955 4.811   -2.217  1.00 57.70  ? 657  ILE   A CG1 1 
ATOM   667  C CG2 . ILE   A 1 112 ? 28.759 5.094   -4.399  1.00 57.39  ? 657  ILE   A CG2 1 
ATOM   668  C CD1 . ILE   A 1 112 ? 28.688 4.714   -1.399  1.00 52.98  ? 657  ILE   A CD1 1 
ATOM   669  N N   . VAL   A 1 113 ? 28.095 2.057   -5.507  1.00 57.68  ? 658  VAL   A N   1 
ATOM   670  C CA  . VAL   A 1 113 ? 27.894 1.544   -6.850  1.00 56.49  ? 658  VAL   A CA  1 
ATOM   671  C C   . VAL   A 1 113 ? 28.498 2.518   -7.842  1.00 57.68  ? 658  VAL   A C   1 
ATOM   672  O O   . VAL   A 1 113 ? 28.511 3.721   -7.600  1.00 58.83  ? 658  VAL   A O   1 
ATOM   673  C CB  . VAL   A 1 113 ? 26.407 1.308   -7.147  1.00 55.34  ? 658  VAL   A CB  1 
ATOM   674  C CG1 . VAL   A 1 113 ? 25.699 2.627   -7.411  1.00 51.85  ? 658  VAL   A CG1 1 
ATOM   675  C CG2 . VAL   A 1 113 ? 26.243 0.355   -8.318  1.00 55.75  ? 658  VAL   A CG2 1 
ATOM   676  N N   . ASN   A 1 114 ? 29.003 2.014   -8.960  1.00 56.55  ? 659  ASN   A N   1 
ATOM   677  C CA  . ASN   A 1 114 ? 29.698 2.884   -9.908  1.00 57.11  ? 659  ASN   A CA  1 
ATOM   678  C C   . ASN   A 1 114 ? 28.887 3.395   -11.089 1.00 55.28  ? 659  ASN   A C   1 
ATOM   679  O O   . ASN   A 1 114 ? 28.126 2.649   -11.693 1.00 52.84  ? 659  ASN   A O   1 
ATOM   680  C CB  . ASN   A 1 114 ? 30.937 2.158   -10.442 1.00 57.02  ? 659  ASN   A CB  1 
ATOM   681  C CG  . ASN   A 1 114 ? 32.170 2.413   -9.607  1.00 65.84  ? 659  ASN   A CG  1 
ATOM   682  O OD1 . ASN   A 1 114 ? 32.355 3.502   -9.074  1.00 72.22  ? 659  ASN   A OD1 1 
ATOM   683  N ND2 . ASN   A 1 114 ? 33.034 1.413   -9.509  1.00 66.33  ? 659  ASN   A ND2 1 
ATOM   684  N N   . LEU   A 1 115 ? 29.055 4.670   -11.419 1.00 57.48  ? 660  LEU   A N   1 
ATOM   685  C CA  . LEU   A 1 115 ? 28.404 5.228   -12.591 1.00 56.88  ? 660  LEU   A CA  1 
ATOM   686  C C   . LEU   A 1 115 ? 29.278 4.914   -13.772 1.00 53.30  ? 660  LEU   A C   1 
ATOM   687  O O   . LEU   A 1 115 ? 30.481 5.136   -13.728 1.00 52.56  ? 660  LEU   A O   1 
ATOM   688  C CB  . LEU   A 1 115 ? 28.241 6.736   -12.466 1.00 55.18  ? 660  LEU   A CB  1 
ATOM   689  C CG  . LEU   A 1 115 ? 27.812 7.497   -13.719 1.00 54.18  ? 660  LEU   A CG  1 
ATOM   690  C CD1 . LEU   A 1 115 ? 26.369 7.175   -14.061 1.00 59.39  ? 660  LEU   A CD1 1 
ATOM   691  C CD2 . LEU   A 1 115 ? 27.988 8.991   -13.509 1.00 54.61  ? 660  LEU   A CD2 1 
ATOM   692  N N   . LEU   A 1 116 ? 28.688 4.390   -14.830 1.00 51.96  ? 661  LEU   A N   1 
ATOM   693  C CA  . LEU   A 1 116 ? 29.464 3.995   -15.982 1.00 52.14  ? 661  LEU   A CA  1 
ATOM   694  C C   . LEU   A 1 116 ? 29.273 4.984   -17.109 1.00 53.41  ? 661  LEU   A C   1 
ATOM   695  O O   . LEU   A 1 116 ? 30.128 5.121   -17.974 1.00 56.90  ? 661  LEU   A O   1 
ATOM   696  C CB  . LEU   A 1 116 ? 29.038 2.600   -16.413 1.00 52.31  ? 661  LEU   A CB  1 
ATOM   697  C CG  . LEU   A 1 116 ? 28.903 1.549   -15.313 1.00 52.26  ? 661  LEU   A CG  1 
ATOM   698  C CD1 . LEU   A 1 116 ? 28.407 0.239   -15.897 1.00 46.17  ? 661  LEU   A CD1 1 
ATOM   699  C CD2 . LEU   A 1 116 ? 30.224 1.349   -14.591 1.00 51.72  ? 661  LEU   A CD2 1 
ATOM   700  N N   . GLY   A 1 117 ? 28.150 5.683   -17.096 1.00 51.40  ? 662  GLY   A N   1 
ATOM   701  C CA  . GLY   A 1 117 ? 27.867 6.645   -18.138 1.00 52.81  ? 662  GLY   A CA  1 
ATOM   702  C C   . GLY   A 1 117 ? 26.425 7.089   -18.153 1.00 51.27  ? 662  GLY   A C   1 
ATOM   703  O O   . GLY   A 1 117 ? 25.647 6.731   -17.278 1.00 54.90  ? 662  GLY   A O   1 
ATOM   704  N N   . ALA   A 1 118 ? 26.062 7.870   -19.157 1.00 43.94  ? 663  ALA   A N   1 
ATOM   705  C CA  . ALA   A 1 118 ? 24.705 8.362   -19.235 1.00 45.98  ? 663  ALA   A CA  1 
ATOM   706  C C   . ALA   A 1 118 ? 24.265 8.742   -20.633 1.00 53.37  ? 663  ALA   A C   1 
ATOM   707  O O   . ALA   A 1 118 ? 25.086 9.098   -21.472 1.00 52.66  ? 663  ALA   A O   1 
ATOM   708  C CB  . ALA   A 1 118 ? 24.549 9.555   -18.315 1.00 53.66  ? 663  ALA   A CB  1 
ATOM   709  N N   . CYS   A 1 119 ? 22.967 8.663   -20.883 1.00 53.03  ? 664  CYS   A N   1 
ATOM   710  C CA  . CYS   A 1 119 ? 22.424 9.061   -22.164 1.00 46.50  ? 664  CYS   A CA  1 
ATOM   711  C C   . CYS   A 1 119 ? 21.567 10.252  -21.847 1.00 48.90  ? 664  CYS   A C   1 
ATOM   712  O O   . CYS   A 1 119 ? 20.471 10.103  -21.322 1.00 53.90  ? 664  CYS   A O   1 
ATOM   713  C CB  . CYS   A 1 119 ? 21.608 7.932   -22.782 1.00 46.36  ? 664  CYS   A CB  1 
ATOM   714  S SG  . CYS   A 1 119 ? 22.532 6.420   -23.124 1.00 48.45  ? 664  CYS   A SG  1 
ATOM   715  N N   . THR   A 1 120 ? 22.052 11.445  -22.151 1.00 51.96  ? 665  THR   A N   1 
ATOM   716  C CA  . THR   A 1 120 ? 21.333 12.650  -21.767 1.00 53.04  ? 665  THR   A CA  1 
ATOM   717  C C   . THR   A 1 120 ? 20.875 13.493  -22.931 1.00 58.97  ? 665  THR   A C   1 
ATOM   718  O O   . THR   A 1 120 ? 20.114 14.435  -22.749 1.00 61.57  ? 665  THR   A O   1 
ATOM   719  C CB  . THR   A 1 120 ? 22.240 13.537  -20.896 1.00 51.08  ? 665  THR   A CB  1 
ATOM   720  O OG1 . THR   A 1 120 ? 23.327 14.032  -21.685 1.00 57.00  ? 665  THR   A OG1 1 
ATOM   721  C CG2 . THR   A 1 120 ? 22.795 12.745  -19.729 1.00 52.18  ? 665  THR   A CG2 1 
ATOM   722  N N   . LYS   A 1 121 ? 21.320 13.162  -24.132 1.00 60.88  ? 666  LYS   A N   1 
ATOM   723  C CA  . LYS   A 1 121 ? 21.002 13.997  -25.285 1.00 61.51  ? 666  LYS   A CA  1 
ATOM   724  C C   . LYS   A 1 121 ? 19.858 13.491  -26.134 1.00 60.64  ? 666  LYS   A C   1 
ATOM   725  O O   . LYS   A 1 121 ? 19.692 12.289  -26.306 1.00 68.04  ? 666  LYS   A O   1 
ATOM   726  C CB  . LYS   A 1 121 ? 22.244 14.156  -26.164 1.00 55.13  ? 666  LYS   A CB  1 
ATOM   727  C CG  . LYS   A 1 121 ? 23.459 14.678  -25.421 1.00 65.18  ? 666  LYS   A CG  1 
ATOM   728  C CD  . LYS   A 1 121 ? 24.606 14.975  -26.373 1.00 67.38  ? 666  LYS   A CD  1 
ATOM   729  C CE  . LYS   A 1 121 ? 24.974 13.755  -27.199 1.00 72.06  ? 666  LYS   A CE  1 
ATOM   730  N NZ  . LYS   A 1 121 ? 26.150 14.014  -28.075 1.00 58.71  ? 666  LYS   A NZ  1 
ATOM   731  N N   . SER   A 1 122 ? 19.057 14.410  -26.651 1.00 66.07  ? 667  SER   A N   1 
ATOM   732  C CA  . SER   A 1 122 ? 17.972 14.038  -27.556 1.00 67.54  ? 667  SER   A CA  1 
ATOM   733  C C   . SER   A 1 122 ? 17.151 12.860  -27.081 1.00 64.50  ? 667  SER   A C   1 
ATOM   734  O O   . SER   A 1 122 ? 17.036 11.860  -27.781 1.00 70.88  ? 667  SER   A O   1 
ATOM   735  C CB  . SER   A 1 122 ? 18.541 13.746  -28.946 1.00 65.92  ? 667  SER   A CB  1 
ATOM   736  O OG  . SER   A 1 122 ? 19.301 14.841  -29.424 1.00 71.32  ? 667  SER   A OG  1 
ATOM   737  N N   . GLY   A 1 123 ? 16.569 12.974  -25.901 1.00 56.24  ? 668  GLY   A N   1 
ATOM   738  C CA  . GLY   A 1 123 ? 15.722 11.914  -25.410 1.00 58.75  ? 668  GLY   A CA  1 
ATOM   739  C C   . GLY   A 1 123 ? 15.732 11.774  -23.916 1.00 57.08  ? 668  GLY   A C   1 
ATOM   740  O O   . GLY   A 1 123 ? 16.416 12.516  -23.224 1.00 62.33  ? 668  GLY   A O   1 
ATOM   741  N N   . PRO   A 1 124 ? 14.981 10.803  -23.408 1.00 58.57  ? 669  PRO   A N   1 
ATOM   742  C CA  . PRO   A 1 124 ? 14.896 10.610  -21.964 1.00 61.28  ? 669  PRO   A CA  1 
ATOM   743  C C   . PRO   A 1 124 ? 16.261 10.363  -21.356 1.00 58.63  ? 669  PRO   A C   1 
ATOM   744  O O   . PRO   A 1 124 ? 17.128 9.795   -22.005 1.00 53.94  ? 669  PRO   A O   1 
ATOM   745  C CB  . PRO   A 1 124 ? 14.025 9.361   -21.835 1.00 58.47  ? 669  PRO   A CB  1 
ATOM   746  C CG  . PRO   A 1 124 ? 14.119 8.673   -23.153 1.00 59.42  ? 669  PRO   A CG  1 
ATOM   747  C CD  . PRO   A 1 124 ? 14.231 9.781   -24.151 1.00 53.07  ? 669  PRO   A CD  1 
ATOM   748  N N   . ILE   A 1 125 ? 16.453 10.797  -20.120 1.00 55.44  ? 670  ILE   A N   1 
ATOM   749  C CA  . ILE   A 1 125 ? 17.731 10.600  -19.453 1.00 58.97  ? 670  ILE   A CA  1 
ATOM   750  C C   . ILE   A 1 125 ? 17.912 9.172   -18.987 1.00 55.17  ? 670  ILE   A C   1 
ATOM   751  O O   . ILE   A 1 125 ? 17.054 8.621   -18.312 1.00 54.94  ? 670  ILE   A O   1 
ATOM   752  C CB  . ILE   A 1 125 ? 17.889 11.522  -18.230 1.00 60.15  ? 670  ILE   A CB  1 
ATOM   753  C CG1 . ILE   A 1 125 ? 17.758 12.987  -18.633 1.00 60.32  ? 670  ILE   A CG1 1 
ATOM   754  C CG2 . ILE   A 1 125 ? 19.230 11.283  -17.553 1.00 53.68  ? 670  ILE   A CG2 1 
ATOM   755  C CD1 . ILE   A 1 125 ? 18.933 13.504  -19.426 1.00 62.40  ? 670  ILE   A CD1 1 
ATOM   756  N N   . TYR   A 1 126 ? 19.030 8.569   -19.352 1.00 54.34  ? 671  TYR   A N   1 
ATOM   757  C CA  . TYR   A 1 126 ? 19.323 7.228   -18.899 1.00 52.98  ? 671  TYR   A CA  1 
ATOM   758  C C   . TYR   A 1 126 ? 20.623 7.267   -18.134 1.00 50.39  ? 671  TYR   A C   1 
ATOM   759  O O   . TYR   A 1 126 ? 21.633 7.723   -18.654 1.00 55.26  ? 671  TYR   A O   1 
ATOM   760  C CB  . TYR   A 1 126 ? 19.454 6.270   -20.075 1.00 51.46  ? 671  TYR   A CB  1 
ATOM   761  C CG  . TYR   A 1 126 ? 18.181 6.004   -20.837 1.00 48.58  ? 671  TYR   A CG  1 
ATOM   762  C CD1 . TYR   A 1 126 ? 16.943 6.278   -20.283 1.00 53.91  ? 671  TYR   A CD1 1 
ATOM   763  C CD2 . TYR   A 1 126 ? 18.222 5.456   -22.109 1.00 48.80  ? 671  TYR   A CD2 1 
ATOM   764  C CE1 . TYR   A 1 126 ? 15.780 6.030   -20.983 1.00 55.37  ? 671  TYR   A CE1 1 
ATOM   765  C CE2 . TYR   A 1 126 ? 17.066 5.203   -22.816 1.00 48.25  ? 671  TYR   A CE2 1 
ATOM   766  C CZ  . TYR   A 1 126 ? 15.847 5.491   -22.248 1.00 52.52  ? 671  TYR   A CZ  1 
ATOM   767  O OH  . TYR   A 1 126 ? 14.692 5.238   -22.947 1.00 53.05  ? 671  TYR   A OH  1 
ATOM   768  N N   . ILE   A 1 127 ? 20.608 6.792   -16.898 1.00 51.73  ? 672  ILE   A N   1 
ATOM   769  C CA  . ILE   A 1 127 ? 21.825 6.744   -16.102 1.00 50.83  ? 672  ILE   A CA  1 
ATOM   770  C C   . ILE   A 1 127 ? 22.359 5.325   -16.047 1.00 46.97  ? 672  ILE   A C   1 
ATOM   771  O O   . ILE   A 1 127 ? 21.696 4.434   -15.533 1.00 44.23  ? 672  ILE   A O   1 
ATOM   772  C CB  . ILE   A 1 127 ? 21.584 7.262   -14.677 1.00 56.04  ? 672  ILE   A CB  1 
ATOM   773  C CG1 . ILE   A 1 127 ? 20.970 8.662   -14.716 1.00 54.54  ? 672  ILE   A CG1 1 
ATOM   774  C CG2 . ILE   A 1 127 ? 22.882 7.261   -13.887 1.00 55.07  ? 672  ILE   A CG2 1 
ATOM   775  C CD1 . ILE   A 1 127 ? 20.720 9.252   -13.346 1.00 55.39  ? 672  ILE   A CD1 1 
ATOM   776  N N   . ILE   A 1 128 ? 23.557 5.112   -16.575 1.00 46.74  ? 673  ILE   A N   1 
ATOM   777  C CA  . ILE   A 1 128 ? 24.127 3.768   -16.633 1.00 46.75  ? 673  ILE   A CA  1 
ATOM   778  C C   . ILE   A 1 128 ? 24.974 3.453   -15.422 1.00 47.07  ? 673  ILE   A C   1 
ATOM   779  O O   . ILE   A 1 128 ? 25.920 4.166   -15.121 1.00 54.25  ? 673  ILE   A O   1 
ATOM   780  C CB  . ILE   A 1 128 ? 24.961 3.577   -17.905 1.00 49.43  ? 673  ILE   A CB  1 
ATOM   781  C CG1 . ILE   A 1 128 ? 24.163 4.040   -19.123 1.00 49.30  ? 673  ILE   A CG1 1 
ATOM   782  C CG2 . ILE   A 1 128 ? 25.384 2.124   -18.048 1.00 44.52  ? 673  ILE   A CG2 1 
ATOM   783  C CD1 . ILE   A 1 128 ? 24.930 3.974   -20.423 1.00 48.62  ? 673  ILE   A CD1 1 
ATOM   784  N N   . ILE   A 1 129 ? 24.649 2.367   -14.739 1.00 45.82  ? 674  ILE   A N   1 
ATOM   785  C CA  . ILE   A 1 129 ? 25.338 2.032   -13.515 1.00 47.69  ? 674  ILE   A CA  1 
ATOM   786  C C   . ILE   A 1 129 ? 25.783 0.584   -13.499 1.00 47.55  ? 674  ILE   A C   1 
ATOM   787  O O   . ILE   A 1 129 ? 25.272 -0.231  -14.256 1.00 53.09  ? 674  ILE   A O   1 
ATOM   788  C CB  . ILE   A 1 129 ? 24.407 2.305   -12.322 1.00 47.23  ? 674  ILE   A CB  1 
ATOM   789  C CG1 . ILE   A 1 129 ? 23.729 3.666   -12.500 1.00 45.12  ? 674  ILE   A CG1 1 
ATOM   790  C CG2 . ILE   A 1 129 ? 25.168 2.245   -11.010 1.00 49.78  ? 674  ILE   A CG2 1 
ATOM   791  C CD1 . ILE   A 1 129 ? 22.653 3.963   -11.484 1.00 47.39  ? 674  ILE   A CD1 1 
ATOM   792  N N   . GLU   A 1 130 ? 26.746 0.264   -12.649 1.00 51.05  ? 675  GLU   A N   1 
ATOM   793  C CA  . GLU   A 1 130 ? 27.245 -1.099  -12.530 1.00 52.51  ? 675  GLU   A CA  1 
ATOM   794  C C   . GLU   A 1 130 ? 26.185 -2.088  -12.092 1.00 54.38  ? 675  GLU   A C   1 
ATOM   795  O O   . GLU   A 1 130 ? 25.361 -1.781  -11.240 1.00 52.01  ? 675  GLU   A O   1 
ATOM   796  C CB  . GLU   A 1 130 ? 28.394 -1.109  -11.529 1.00 51.86  ? 675  GLU   A CB  1 
ATOM   797  C CG  . GLU   A 1 130 ? 28.652 -2.441  -10.853 1.00 62.53  ? 675  GLU   A CG  1 
ATOM   798  C CD  . GLU   A 1 130 ? 29.666 -2.328  -9.731  1.00 66.08  ? 675  GLU   A CD  1 
ATOM   799  O OE1 . GLU   A 1 130 ? 30.116 -1.200  -9.449  1.00 62.07  ? 675  GLU   A OE1 1 
ATOM   800  O OE2 . GLU   A 1 130 ? 30.012 -3.364  -9.131  1.00 71.89  ? 675  GLU   A OE2 1 
ATOM   801  N N   . TYR   A 1 131 ? 26.202 -3.279  -12.676 1.00 52.32  ? 676  TYR   A N   1 
ATOM   802  C CA  . TYR   A 1 131 ? 25.255 -4.308  -12.289 1.00 53.33  ? 676  TYR   A CA  1 
ATOM   803  C C   . TYR   A 1 131 ? 25.907 -5.206  -11.267 1.00 54.91  ? 676  TYR   A C   1 
ATOM   804  O O   . TYR   A 1 131 ? 27.041 -5.632  -11.450 1.00 56.39  ? 676  TYR   A O   1 
ATOM   805  C CB  . TYR   A 1 131 ? 24.817 -5.119  -13.501 1.00 57.09  ? 676  TYR   A CB  1 
ATOM   806  C CG  . TYR   A 1 131 ? 23.848 -6.232  -13.187 1.00 59.54  ? 676  TYR   A CG  1 
ATOM   807  C CD1 . TYR   A 1 131 ? 24.302 -7.502  -12.868 1.00 62.00  ? 676  TYR   A CD1 1 
ATOM   808  C CD2 . TYR   A 1 131 ? 22.480 -6.014  -13.211 1.00 58.45  ? 676  TYR   A CD2 1 
ATOM   809  C CE1 . TYR   A 1 131 ? 23.421 -8.522  -12.578 1.00 60.20  ? 676  TYR   A CE1 1 
ATOM   810  C CE2 . TYR   A 1 131 ? 21.591 -7.030  -12.925 1.00 60.46  ? 676  TYR   A CE2 1 
ATOM   811  C CZ  . TYR   A 1 131 ? 22.069 -8.281  -12.609 1.00 60.29  ? 676  TYR   A CZ  1 
ATOM   812  O OH  . TYR   A 1 131 ? 21.192 -9.297  -12.322 1.00 67.56  ? 676  TYR   A OH  1 
ATOM   813  N N   . CYS   A 1 132 ? 25.203 -5.487  -10.179 1.00 61.66  ? 677  CYS   A N   1 
ATOM   814  C CA  . CYS   A 1 132 ? 25.762 -6.315  -9.116  1.00 56.14  ? 677  CYS   A CA  1 
ATOM   815  C C   . CYS   A 1 132 ? 25.157 -7.707  -9.166  1.00 60.75  ? 677  CYS   A C   1 
ATOM   816  O O   . CYS   A 1 132 ? 23.940 -7.858  -9.126  1.00 58.60  ? 677  CYS   A O   1 
ATOM   817  C CB  . CYS   A 1 132 ? 25.574 -5.640  -7.761  1.00 57.10  ? 677  CYS   A CB  1 
ATOM   818  S SG  . CYS   A 1 132 ? 26.403 -4.044  -7.636  1.00 56.60  ? 677  CYS   A SG  1 
ATOM   819  N N   . PHE   A 1 133 ? 26.002 -8.726  -9.239  1.00 65.89  ? 678  PHE   A N   1 
ATOM   820  C CA  . PHE   A 1 133 ? 25.526 -10.103 -9.412  1.00 66.99  ? 678  PHE   A CA  1 
ATOM   821  C C   . PHE   A 1 133 ? 24.604 -10.670 -8.355  1.00 68.64  ? 678  PHE   A C   1 
ATOM   822  O O   . PHE   A 1 133 ? 23.593 -11.279 -8.687  1.00 74.08  ? 678  PHE   A O   1 
ATOM   823  C CB  . PHE   A 1 133 ? 26.753 -11.012 -9.511  1.00 71.59  ? 678  PHE   A CB  1 
ATOM   824  C CG  . PHE   A 1 133 ? 26.428 -12.455 -9.738  1.00 76.66  ? 678  PHE   A CG  1 
ATOM   825  C CD1 . PHE   A 1 133 ? 25.966 -12.888 -10.966 1.00 74.42  ? 678  PHE   A CD1 1 
ATOM   826  C CD2 . PHE   A 1 133 ? 26.602 -13.381 -8.727  1.00 81.59  ? 678  PHE   A CD2 1 
ATOM   827  C CE1 . PHE   A 1 133 ? 25.669 -14.217 -11.179 1.00 78.50  ? 678  PHE   A CE1 1 
ATOM   828  C CE2 . PHE   A 1 133 ? 26.308 -14.713 -8.932  1.00 79.34  ? 678  PHE   A CE2 1 
ATOM   829  C CZ  . PHE   A 1 133 ? 25.841 -15.132 -10.161 1.00 79.01  ? 678  PHE   A CZ  1 
ATOM   830  N N   . TYR   A 1 134 ? 24.942 -10.494 -7.089  1.00 64.00  ? 679  TYR   A N   1 
ATOM   831  C CA  . TYR   A 1 134 ? 24.146 -11.102 -6.029  1.00 69.15  ? 679  TYR   A CA  1 
ATOM   832  C C   . TYR   A 1 134 ? 22.885 -10.317 -5.687  1.00 67.36  ? 679  TYR   A C   1 
ATOM   833  O O   . TYR   A 1 134 ? 22.052 -10.794 -4.926  1.00 67.36  ? 679  TYR   A O   1 
ATOM   834  C CB  . TYR   A 1 134 ? 25.005 -11.287 -4.783  1.00 68.73  ? 679  TYR   A CB  1 
ATOM   835  C CG  . TYR   A 1 134 ? 26.268 -12.070 -5.030  1.00 72.08  ? 679  TYR   A CG  1 
ATOM   836  C CD1 . TYR   A 1 134 ? 26.221 -13.425 -5.312  1.00 70.33  ? 679  TYR   A CD1 1 
ATOM   837  C CD2 . TYR   A 1 134 ? 27.507 -11.455 -4.973  1.00 72.99  ? 679  TYR   A CD2 1 
ATOM   838  C CE1 . TYR   A 1 134 ? 27.376 -14.147 -5.536  1.00 70.33  ? 679  TYR   A CE1 1 
ATOM   839  C CE2 . TYR   A 1 134 ? 28.667 -12.168 -5.196  1.00 78.96  ? 679  TYR   A CE2 1 
ATOM   840  C CZ  . TYR   A 1 134 ? 28.595 -13.513 -5.478  1.00 80.36  ? 679  TYR   A CZ  1 
ATOM   841  O OH  . TYR   A 1 134 ? 29.748 -14.227 -5.700  1.00 85.88  ? 679  TYR   A OH  1 
ATOM   842  N N   . GLY   A 1 135 ? 22.739 -9.123  -6.241  1.00 64.38  ? 680  GLY   A N   1 
ATOM   843  C CA  . GLY   A 1 135 ? 21.543 -8.338  -6.006  1.00 59.48  ? 680  GLY   A CA  1 
ATOM   844  C C   . GLY   A 1 135 ? 21.494 -7.577  -4.703  1.00 62.50  ? 680  GLY   A C   1 
ATOM   845  O O   . GLY   A 1 135 ? 22.528 -7.236  -4.141  1.00 63.03  ? 680  GLY   A O   1 
ATOM   846  N N   . ASP   A 1 136 ? 20.288 -7.300  -4.224  1.00 63.23  ? 681  ASP   A N   1 
ATOM   847  C CA  . ASP   A 1 136 ? 20.121 -6.572  -2.971  1.00 59.74  ? 681  ASP   A CA  1 
ATOM   848  C C   . ASP   A 1 136 ? 20.284 -7.471  -1.755  1.00 62.35  ? 681  ASP   A C   1 
ATOM   849  O O   . ASP   A 1 136 ? 20.069 -8.675  -1.835  1.00 61.02  ? 681  ASP   A O   1 
ATOM   850  C CB  . ASP   A 1 136 ? 18.752 -5.896  -2.933  1.00 54.51  ? 681  ASP   A CB  1 
ATOM   851  C CG  . ASP   A 1 136 ? 17.618 -6.878  -2.996  1.00 64.68  ? 681  ASP   A CG  1 
ATOM   852  O OD1 . ASP   A 1 136 ? 17.832 -8.006  -3.478  1.00 80.05  ? 681  ASP   A OD1 1 
ATOM   853  O OD2 . ASP   A 1 136 ? 16.504 -6.519  -2.573  1.00 66.74  ? 681  ASP   A OD2 1 
ATOM   854  N N   . LEU   A 1 137 ? 20.663 -6.886  -0.628  1.00 59.21  ? 682  LEU   A N   1 
ATOM   855  C CA  . LEU   A 1 137 ? 20.861 -7.661  0.585   1.00 58.18  ? 682  LEU   A CA  1 
ATOM   856  C C   . LEU   A 1 137 ? 19.578 -8.307  1.063   1.00 60.00  ? 682  LEU   A C   1 
ATOM   857  O O   . LEU   A 1 137 ? 19.602 -9.412  1.580   1.00 62.64  ? 682  LEU   A O   1 
ATOM   858  C CB  . LEU   A 1 137 ? 21.437 -6.786  1.692   1.00 60.38  ? 682  LEU   A CB  1 
ATOM   859  C CG  . LEU   A 1 137 ? 22.954 -6.812  1.858   1.00 72.11  ? 682  LEU   A CG  1 
ATOM   860  C CD1 . LEU   A 1 137 ? 23.362 -5.941  3.035   1.00 63.96  ? 682  LEU   A CD1 1 
ATOM   861  C CD2 . LEU   A 1 137 ? 23.423 -8.243  2.067   1.00 69.38  ? 682  LEU   A CD2 1 
ATOM   862  N N   . VAL   A 1 138 ? 18.455 -7.628  0.893   1.00 58.97  ? 683  VAL   A N   1 
ATOM   863  C CA  . VAL   A 1 138 ? 17.207 -8.167  1.393   1.00 63.65  ? 683  VAL   A CA  1 
ATOM   864  C C   . VAL   A 1 138 ? 16.985 -9.551  0.825   1.00 62.77  ? 683  VAL   A C   1 
ATOM   865  O O   . VAL   A 1 138 ? 16.769 -10.506 1.566   1.00 67.79  ? 683  VAL   A O   1 
ATOM   866  C CB  . VAL   A 1 138 ? 16.013 -7.282  1.011   1.00 62.00  ? 683  VAL   A CB  1 
ATOM   867  C CG1 . VAL   A 1 138 ? 14.716 -7.901  1.503   1.00 63.25  ? 683  VAL   A CG1 1 
ATOM   868  C CG2 . VAL   A 1 138 ? 16.185 -5.881  1.562   1.00 55.47  ? 683  VAL   A CG2 1 
ATOM   869  N N   . ASN   A 1 139 ? 17.065 -9.671  -0.489  1.00 65.16  ? 684  ASN   A N   1 
ATOM   870  C CA  . ASN   A 1 139 ? 16.834 -10.954 -1.131  1.00 65.30  ? 684  ASN   A CA  1 
ATOM   871  C C   . ASN   A 1 139 ? 17.934 -11.942 -0.802  1.00 64.91  ? 684  ASN   A C   1 
ATOM   872  O O   . ASN   A 1 139 ? 17.675 -13.123 -0.611  1.00 68.96  ? 684  ASN   A O   1 
ATOM   873  C CB  . ASN   A 1 139 ? 16.717 -10.769 -2.640  1.00 67.73  ? 684  ASN   A CB  1 
ATOM   874  C CG  . ASN   A 1 139 ? 15.525 -9.923  -3.027  1.00 67.68  ? 684  ASN   A CG  1 
ATOM   875  O OD1 . ASN   A 1 139 ? 14.619 -9.706  -2.225  1.00 68.23  ? 684  ASN   A OD1 1 
ATOM   876  N ND2 . ASN   A 1 139 ? 15.516 -9.443  -4.264  1.00 69.92  ? 684  ASN   A ND2 1 
ATOM   877  N N   . TYR   A 1 140 ? 19.163 -11.460 -0.731  1.00 54.21  ? 685  TYR   A N   1 
ATOM   878  C CA  . TYR   A 1 140 ? 20.270 -12.335 -0.417  1.00 57.98  ? 685  TYR   A CA  1 
ATOM   879  C C   . TYR   A 1 140 ? 20.087 -12.919 0.959   1.00 67.13  ? 685  TYR   A C   1 
ATOM   880  O O   . TYR   A 1 140 ? 20.201 -14.126 1.151   1.00 71.66  ? 685  TYR   A O   1 
ATOM   881  C CB  . TYR   A 1 140 ? 21.581 -11.574 -0.468  1.00 58.57  ? 685  TYR   A CB  1 
ATOM   882  C CG  . TYR   A 1 140 ? 22.783 -12.431 -0.172  1.00 67.85  ? 685  TYR   A CG  1 
ATOM   883  C CD1 . TYR   A 1 140 ? 23.366 -13.204 -1.163  1.00 70.43  ? 685  TYR   A CD1 1 
ATOM   884  C CD2 . TYR   A 1 140 ? 23.334 -12.469 1.099   1.00 67.41  ? 685  TYR   A CD2 1 
ATOM   885  C CE1 . TYR   A 1 140 ? 24.466 -13.991 -0.898  1.00 71.51  ? 685  TYR   A CE1 1 
ATOM   886  C CE2 . TYR   A 1 140 ? 24.434 -13.253 1.374   1.00 72.21  ? 685  TYR   A CE2 1 
ATOM   887  C CZ  . TYR   A 1 140 ? 24.996 -14.010 0.372   1.00 73.48  ? 685  TYR   A CZ  1 
ATOM   888  O OH  . TYR   A 1 140 ? 26.092 -14.794 0.643   1.00 78.67  ? 685  TYR   A OH  1 
ATOM   889  N N   . LEU   A 1 141 ? 19.785 -12.067 1.923   1.00 64.94  ? 686  LEU   A N   1 
ATOM   890  C CA  . LEU   A 1 141 ? 19.636 -12.528 3.288   1.00 66.12  ? 686  LEU   A CA  1 
ATOM   891  C C   . LEU   A 1 141 ? 18.504 -13.521 3.359   1.00 67.52  ? 686  LEU   A C   1 
ATOM   892  O O   . LEU   A 1 141 ? 18.581 -14.502 4.087   1.00 68.07  ? 686  LEU   A O   1 
ATOM   893  C CB  . LEU   A 1 141 ? 19.384 -11.351 4.225   1.00 62.15  ? 686  LEU   A CB  1 
ATOM   894  C CG  . LEU   A 1 141 ? 20.510 -10.333 4.372   1.00 58.73  ? 686  LEU   A CG  1 
ATOM   895  C CD1 . LEU   A 1 141 ? 20.069 -9.194  5.275   1.00 58.32  ? 686  LEU   A CD1 1 
ATOM   896  C CD2 . LEU   A 1 141 ? 21.764 -10.997 4.913   1.00 57.62  ? 686  LEU   A CD2 1 
ATOM   897  N N   . HIS   A 1 142 ? 17.451 -13.272 2.598   1.00 64.95  ? 687  HIS   A N   1 
ATOM   898  C CA  . HIS   A 1 142 ? 16.317 -14.180 2.588   1.00 72.76  ? 687  HIS   A CA  1 
ATOM   899  C C   . HIS   A 1 142 ? 16.659 -15.551 2.025   1.00 74.90  ? 687  HIS   A C   1 
ATOM   900  O O   . HIS   A 1 142 ? 16.373 -16.568 2.651   1.00 71.78  ? 687  HIS   A O   1 
ATOM   901  C CB  . HIS   A 1 142 ? 15.179 -13.579 1.770   1.00 67.93  ? 687  HIS   A CB  1 
ATOM   902  C CG  . HIS   A 1 142 ? 14.409 -12.518 2.489   1.00 73.72  ? 687  HIS   A CG  1 
ATOM   903  N ND1 . HIS   A 1 142 ? 13.531 -11.672 1.847   1.00 68.93  ? 687  HIS   A ND1 1 
ATOM   904  C CD2 . HIS   A 1 142 ? 14.380 -12.169 3.796   1.00 68.70  ? 687  HIS   A CD2 1 
ATOM   905  C CE1 . HIS   A 1 142 ? 12.995 -10.846 2.727   1.00 66.78  ? 687  HIS   A CE1 1 
ATOM   906  N NE2 . HIS   A 1 142 ? 13.493 -11.127 3.917   1.00 65.99  ? 687  HIS   A NE2 1 
ATOM   907  N N   . LYS   A 1 143 ? 17.275 -15.586 0.852   1.00 69.05  ? 688  LYS   A N   1 
ATOM   908  C CA  . LYS   A 1 143 ? 17.576 -16.858 0.209   1.00 68.43  ? 688  LYS   A CA  1 
ATOM   909  C C   . LYS   A 1 143 ? 18.630 -17.647 0.962   1.00 69.78  ? 688  LYS   A C   1 
ATOM   910  O O   . LYS   A 1 143 ? 18.710 -18.862 0.829   1.00 77.43  ? 688  LYS   A O   1 
ATOM   911  C CB  . LYS   A 1 143 ? 18.046 -16.631 -1.225  1.00 70.27  ? 688  LYS   A CB  1 
ATOM   912  C CG  . LYS   A 1 143 ? 19.442 -16.046 -1.328  1.00 73.01  ? 688  LYS   A CG  1 
ATOM   913  C CD  . LYS   A 1 143 ? 20.201 -16.652 -2.495  1.00 69.22  ? 688  LYS   A CD  1 
ATOM   914  C CE  . LYS   A 1 143 ? 21.653 -16.208 -2.500  1.00 74.57  ? 688  LYS   A CE  1 
ATOM   915  N NZ  . LYS   A 1 143 ? 22.442 -16.908 -3.551  1.00 62.64  ? 688  LYS   A NZ  1 
ATOM   916  N N   . ASN   A 1 144 ? 19.445 -16.959 1.741   1.00 69.97  ? 689  ASN   A N   1 
ATOM   917  C CA  . ASN   A 1 144 ? 20.481 -17.634 2.498   1.00 72.07  ? 689  ASN   A CA  1 
ATOM   918  C C   . ASN   A 1 144 ? 20.139 -17.667 3.974   1.00 75.86  ? 689  ASN   A C   1 
ATOM   919  O O   . ASN   A 1 144 ? 21.025 -17.719 4.820   1.00 80.38  ? 689  ASN   A O   1 
ATOM   920  C CB  . ASN   A 1 144 ? 21.823 -16.954 2.270   1.00 73.93  ? 689  ASN   A CB  1 
ATOM   921  C CG  . ASN   A 1 144 ? 22.394 -17.255 0.903   1.00 76.13  ? 689  ASN   A CG  1 
ATOM   922  O OD1 . ASN   A 1 144 ? 21.863 -18.086 0.168   1.00 72.29  ? 689  ASN   A OD1 1 
ATOM   923  N ND2 . ASN   A 1 144 ? 23.483 -16.588 0.556   1.00 78.75  ? 689  ASN   A ND2 1 
ATOM   924  N N   . ARG   A 1 145 ? 18.850 -17.636 4.282   1.00 74.21  ? 690  ARG   A N   1 
ATOM   925  C CA  . ARG   A 1 145 ? 18.421 -17.660 5.670   1.00 74.29  ? 690  ARG   A CA  1 
ATOM   926  C C   . ARG   A 1 145 ? 18.704 -18.993 6.306   1.00 80.73  ? 690  ARG   A C   1 
ATOM   927  O O   . ARG   A 1 145 ? 19.373 -19.068 7.330   1.00 84.62  ? 690  ARG   A O   1 
ATOM   928  C CB  . ARG   A 1 145 ? 16.924 -17.381 5.766   1.00 77.54  ? 690  ARG   A CB  1 
ATOM   929  C CG  . ARG   A 1 145 ? 16.569 -15.914 5.919   1.00 79.65  ? 690  ARG   A CG  1 
ATOM   930  C CD  . ARG   A 1 145 ? 15.064 -15.728 6.002   1.00 82.23  ? 690  ARG   A CD  1 
ATOM   931  N NE  . ARG   A 1 145 ? 14.700 -14.365 6.371   1.00 85.07  ? 690  ARG   A NE  1 
ATOM   932  C CZ  . ARG   A 1 145 ? 13.448 -13.937 6.493   1.00 86.04  ? 690  ARG   A CZ  1 
ATOM   933  N NH1 . ARG   A 1 145 ? 12.439 -14.766 6.269   1.00 86.53  ? 690  ARG   A NH1 1 
ATOM   934  N NH2 . ARG   A 1 145 ? 13.205 -12.680 6.834   1.00 75.31  ? 690  ARG   A NH2 1 
ATOM   935  N N   . ASP   A 1 146 ? 18.212 -20.056 5.694   1.00 80.60  ? 691  ASP   A N   1 
ATOM   936  C CA  . ASP   A 1 146 ? 18.382 -21.379 6.272   1.00 82.83  ? 691  ASP   A CA  1 
ATOM   937  C C   . ASP   A 1 146 ? 19.853 -21.712 6.425   1.00 79.45  ? 691  ASP   A C   1 
ATOM   938  O O   . ASP   A 1 146 ? 20.244 -22.374 7.375   1.00 78.51  ? 691  ASP   A O   1 
ATOM   939  C CB  . ASP   A 1 146 ? 17.671 -22.417 5.416   1.00 80.47  ? 691  ASP   A CB  1 
ATOM   940  C CG  . ASP   A 1 146 ? 16.179 -22.164 5.317   1.00 82.33  ? 691  ASP   A CG  1 
ATOM   941  O OD1 . ASP   A 1 146 ? 15.718 -21.124 5.830   1.00 82.03  ? 691  ASP   A OD1 1 
ATOM   942  O OD2 . ASP   A 1 146 ? 15.466 -23.001 4.726   1.00 83.83  ? 691  ASP   A OD2 1 
ATOM   943  N N   . SER   A 1 147 ? 20.673 -21.237 5.504   1.00 78.51  ? 692  SER   A N   1 
ATOM   944  C CA  . SER   A 1 147 ? 22.103 -21.456 5.611   1.00 82.36  ? 692  SER   A CA  1 
ATOM   945  C C   . SER   A 1 147 ? 22.631 -20.913 6.921   1.00 81.38  ? 692  SER   A C   1 
ATOM   946  O O   . SER   A 1 147 ? 23.648 -21.378 7.422   1.00 84.56  ? 692  SER   A O   1 
ATOM   947  C CB  . SER   A 1 147 ? 22.830 -20.778 4.457   1.00 84.30  ? 692  SER   A CB  1 
ATOM   948  O OG  . SER   A 1 147 ? 24.193 -20.578 4.772   1.00 84.97  ? 692  SER   A OG  1 
ATOM   949  N N   . PHE   A 1 148 ? 21.948 -19.923 7.478   1.00 78.97  ? 693  PHE   A N   1 
ATOM   950  C CA  . PHE   A 1 148 ? 22.415 -19.313 8.707   1.00 82.56  ? 693  PHE   A CA  1 
ATOM   951  C C   . PHE   A 1 148 ? 22.182 -20.293 9.841   1.00 82.60  ? 693  PHE   A C   1 
ATOM   952  O O   . PHE   A 1 148 ? 21.175 -20.215 10.541  1.00 77.46  ? 693  PHE   A O   1 
ATOM   953  C CB  . PHE   A 1 148 ? 21.702 -17.983 8.948   1.00 76.70  ? 693  PHE   A CB  1 
ATOM   954  C CG  . PHE   A 1 148 ? 22.459 -17.036 9.826   1.00 71.79  ? 693  PHE   A CG  1 
ATOM   955  C CD1 . PHE   A 1 148 ? 23.599 -16.405 9.361   1.00 74.19  ? 693  PHE   A CD1 1 
ATOM   956  C CD2 . PHE   A 1 148 ? 22.024 -16.763 11.110  1.00 70.96  ? 693  PHE   A CD2 1 
ATOM   957  C CE1 . PHE   A 1 148 ? 24.298 -15.527 10.165  1.00 76.49  ? 693  PHE   A CE1 1 
ATOM   958  C CE2 . PHE   A 1 148 ? 22.717 -15.885 11.919  1.00 67.46  ? 693  PHE   A CE2 1 
ATOM   959  C CZ  . PHE   A 1 148 ? 23.857 -15.267 11.446  1.00 66.25  ? 693  PHE   A CZ  1 
ATOM   960  N N   . LEU   A 1 149 ? 23.106 -21.234 10.008  1.00 84.17  ? 694  LEU   A N   1 
ATOM   961  C CA  . LEU   A 1 149 ? 22.986 -22.242 11.058  1.00 81.15  ? 694  LEU   A CA  1 
ATOM   962  C C   . LEU   A 1 149 ? 24.338 -22.894 11.326  1.00 80.70  ? 694  LEU   A C   1 
ATOM   963  O O   . LEU   A 1 149 ? 25.270 -22.758 10.536  1.00 80.85  ? 694  LEU   A O   1 
ATOM   964  C CB  . LEU   A 1 149 ? 21.952 -23.306 10.683  1.00 78.19  ? 694  LEU   A CB  1 
ATOM   965  C CG  . LEU   A 1 149 ? 21.970 -23.911 9.276   1.00 79.73  ? 694  LEU   A CG  1 
ATOM   966  C CD1 . LEU   A 1 149 ? 23.287 -24.589 8.937   1.00 80.96  ? 694  LEU   A CD1 1 
ATOM   967  C CD2 . LEU   A 1 149 ? 20.815 -24.885 9.114   1.00 76.10  ? 694  LEU   A CD2 1 
ATOM   968  N N   . GLY   A 1 172 ? 26.522 -21.241 4.126   1.00 99.92  ? 717  GLY   A N   1 
ATOM   969  C CA  . GLY   A 1 172 ? 26.926 -20.087 3.345   1.00 101.57 ? 717  GLY   A CA  1 
ATOM   970  C C   . GLY   A 1 172 ? 26.914 -18.803 4.144   1.00 95.20  ? 717  GLY   A C   1 
ATOM   971  O O   . GLY   A 1 172 ? 27.964 -18.319 4.563   1.00 91.75  ? 717  GLY   A O   1 
ATOM   972  N N   . LEU   A 1 173 ? 25.730 -18.248 4.362   1.00 90.75  ? 718  LEU   A N   1 
ATOM   973  C CA  . LEU   A 1 173 ? 25.626 -17.003 5.097   1.00 82.46  ? 718  LEU   A CA  1 
ATOM   974  C C   . LEU   A 1 173 ? 26.093 -17.206 6.523   1.00 84.67  ? 718  LEU   A C   1 
ATOM   975  O O   . LEU   A 1 173 ? 25.650 -18.130 7.197   1.00 84.95  ? 718  LEU   A O   1 
ATOM   976  C CB  . LEU   A 1 173 ? 24.190 -16.496 5.069   1.00 82.92  ? 718  LEU   A CB  1 
ATOM   977  C CG  . LEU   A 1 173 ? 23.954 -15.123 5.689   1.00 81.28  ? 718  LEU   A CG  1 
ATOM   978  C CD1 . LEU   A 1 173 ? 24.857 -14.092 5.030   1.00 78.00  ? 718  LEU   A CD1 1 
ATOM   979  C CD2 . LEU   A 1 173 ? 22.491 -14.735 5.550   1.00 76.07  ? 718  LEU   A CD2 1 
ATOM   980  N N   . THR   A 1 174 ? 26.986 -16.344 6.986   1.00 81.78  ? 719  THR   A N   1 
ATOM   981  C CA  . THR   A 1 174 ? 27.527 -16.486 8.326   1.00 78.89  ? 719  THR   A CA  1 
ATOM   982  C C   . THR   A 1 174 ? 27.526 -15.167 9.074   1.00 76.96  ? 719  THR   A C   1 
ATOM   983  O O   . THR   A 1 174 ? 27.481 -14.104 8.468   1.00 77.69  ? 719  THR   A O   1 
ATOM   984  C CB  . THR   A 1 174 ? 28.964 -17.032 8.284   1.00 80.10  ? 719  THR   A CB  1 
ATOM   985  O OG1 . THR   A 1 174 ? 29.804 -16.125 7.564   1.00 79.83  ? 719  THR   A OG1 1 
ATOM   986  C CG2 . THR   A 1 174 ? 28.998 -18.389 7.603   1.00 80.78  ? 719  THR   A CG2 1 
ATOM   987  N N   . LEU   A 1 175 ? 27.599 -15.231 10.393  1.00 73.73  ? 720  LEU   A N   1 
ATOM   988  C CA  . LEU   A 1 175 ? 27.562 -14.023 11.201  1.00 75.62  ? 720  LEU   A CA  1 
ATOM   989  C C   . LEU   A 1 175 ? 28.653 -13.050 10.810  1.00 72.45  ? 720  LEU   A C   1 
ATOM   990  O O   . LEU   A 1 175 ? 28.450 -11.841 10.833  1.00 75.92  ? 720  LEU   A O   1 
ATOM   991  C CB  . LEU   A 1 175 ? 27.690 -14.389 12.678  1.00 74.35  ? 720  LEU   A CB  1 
ATOM   992  C CG  . LEU   A 1 175 ? 27.623 -13.279 13.725  1.00 80.87  ? 720  LEU   A CG  1 
ATOM   993  C CD1 . LEU   A 1 175 ? 27.022 -13.808 15.017  1.00 74.83  ? 720  LEU   A CD1 1 
ATOM   994  C CD2 . LEU   A 1 175 ? 28.997 -12.680 13.973  1.00 86.41  ? 720  LEU   A CD2 1 
ATOM   995  N N   . LEU   A 1 176 ? 29.815 -13.570 10.457  1.00 73.68  ? 721  LEU   A N   1 
ATOM   996  C CA  . LEU   A 1 176 ? 30.917 -12.708 10.079  1.00 77.50  ? 721  LEU   A CA  1 
ATOM   997  C C   . LEU   A 1 176 ? 30.532 -11.954 8.828   1.00 73.59  ? 721  LEU   A C   1 
ATOM   998  O O   . LEU   A 1 176 ? 30.874 -10.786 8.671   1.00 70.76  ? 721  LEU   A O   1 
ATOM   999  C CB  . LEU   A 1 176 ? 32.183 -13.524 9.856   1.00 77.09  ? 721  LEU   A CB  1 
ATOM   1000 C CG  . LEU   A 1 176 ? 33.509 -12.764 9.863   1.00 78.94  ? 721  LEU   A CG  1 
ATOM   1001 C CD1 . LEU   A 1 176 ? 33.760 -12.025 8.557   1.00 80.32  ? 721  LEU   A CD1 1 
ATOM   1002 C CD2 . LEU   A 1 176 ? 33.576 -11.823 11.055  1.00 79.23  ? 721  LEU   A CD2 1 
ATOM   1003 N N   . ASP   A 1 177 ? 29.808 -12.617 7.939   1.00 71.93  ? 722  ASP   A N   1 
ATOM   1004 C CA  . ASP   A 1 177 ? 29.373 -11.974 6.713   1.00 73.43  ? 722  ASP   A CA  1 
ATOM   1005 C C   . ASP   A 1 177 ? 28.533 -10.767 7.048   1.00 71.78  ? 722  ASP   A C   1 
ATOM   1006 O O   . ASP   A 1 177 ? 28.743 -9.685  6.508   1.00 67.90  ? 722  ASP   A O   1 
ATOM   1007 C CB  . ASP   A 1 177 ? 28.556 -12.945 5.871   1.00 76.83  ? 722  ASP   A CB  1 
ATOM   1008 C CG  . ASP   A 1 177 ? 29.321 -14.194 5.513   1.00 86.25  ? 722  ASP   A CG  1 
ATOM   1009 O OD1 . ASP   A 1 177 ? 30.539 -14.242 5.774   1.00 94.69  ? 722  ASP   A OD1 1 
ATOM   1010 O OD2 . ASP   A 1 177 ? 28.704 -15.133 4.969   1.00 87.18  ? 722  ASP   A OD2 1 
ATOM   1011 N N   . LEU   A 1 178 ? 27.591 -10.942 7.961   1.00 68.99  ? 723  LEU   A N   1 
ATOM   1012 C CA  . LEU   A 1 178 ? 26.714 -9.852  8.340   1.00 62.10  ? 723  LEU   A CA  1 
ATOM   1013 C C   . LEU   A 1 178 ? 27.515 -8.678  8.854   1.00 64.72  ? 723  LEU   A C   1 
ATOM   1014 O O   . LEU   A 1 178 ? 27.266 -7.537  8.478   1.00 63.98  ? 723  LEU   A O   1 
ATOM   1015 C CB  . LEU   A 1 178 ? 25.730 -10.324 9.404   1.00 63.37  ? 723  LEU   A CB  1 
ATOM   1016 C CG  . LEU   A 1 178 ? 24.499 -11.118 8.965   1.00 62.64  ? 723  LEU   A CG  1 
ATOM   1017 C CD1 . LEU   A 1 178 ? 24.882 -12.373 8.202   1.00 64.52  ? 723  LEU   A CD1 1 
ATOM   1018 C CD2 . LEU   A 1 178 ? 23.637 -11.466 10.166  1.00 63.22  ? 723  LEU   A CD2 1 
ATOM   1019 N N   . LEU   A 1 179 ? 28.486 -8.952  9.705   1.00 65.72  ? 724  LEU   A N   1 
ATOM   1020 C CA  . LEU   A 1 179 ? 29.309 -7.890  10.249  1.00 68.49  ? 724  LEU   A CA  1 
ATOM   1021 C C   . LEU   A 1 179 ? 30.107 -7.198  9.157   1.00 65.64  ? 724  LEU   A C   1 
ATOM   1022 O O   . LEU   A 1 179 ? 30.328 -5.994  9.216   1.00 60.26  ? 724  LEU   A O   1 
ATOM   1023 C CB  . LEU   A 1 179 ? 30.248 -8.446  11.313  1.00 72.85  ? 724  LEU   A CB  1 
ATOM   1024 C CG  . LEU   A 1 179 ? 29.611 -9.082  12.544  1.00 75.84  ? 724  LEU   A CG  1 
ATOM   1025 C CD1 . LEU   A 1 179 ? 30.691 -9.653  13.446  1.00 71.45  ? 724  LEU   A CD1 1 
ATOM   1026 C CD2 . LEU   A 1 179 ? 28.776 -8.056  13.291  1.00 75.10  ? 724  LEU   A CD2 1 
ATOM   1027 N N   . SER   A 1 180 ? 30.549 -7.958  8.167   1.00 64.67  ? 725  SER   A N   1 
ATOM   1028 C CA  . SER   A 1 180 ? 31.310 -7.380  7.075   1.00 67.43  ? 725  SER   A CA  1 
ATOM   1029 C C   . SER   A 1 180 ? 30.452 -6.402  6.313   1.00 65.20  ? 725  SER   A C   1 
ATOM   1030 O O   . SER   A 1 180 ? 30.886 -5.299  6.000   1.00 63.74  ? 725  SER   A O   1 
ATOM   1031 C CB  . SER   A 1 180 ? 31.808 -8.468  6.135   1.00 70.57  ? 725  SER   A CB  1 
ATOM   1032 O OG  . SER   A 1 180 ? 32.461 -7.912  5.009   1.00 68.11  ? 725  SER   A OG  1 
ATOM   1033 N N   . PHE   A 1 181 ? 29.224 -6.801  6.022   1.00 62.12  ? 726  PHE   A N   1 
ATOM   1034 C CA  . PHE   A 1 181 ? 28.322 -5.922  5.312   1.00 59.42  ? 726  PHE   A CA  1 
ATOM   1035 C C   . PHE   A 1 181 ? 28.145 -4.663  6.120   1.00 62.75  ? 726  PHE   A C   1 
ATOM   1036 O O   . PHE   A 1 181 ? 28.189 -3.561  5.583   1.00 63.75  ? 726  PHE   A O   1 
ATOM   1037 C CB  . PHE   A 1 181 ? 26.972 -6.597  5.115   1.00 61.19  ? 726  PHE   A CB  1 
ATOM   1038 C CG  . PHE   A 1 181 ? 27.047 -7.925  4.423   1.00 61.01  ? 726  PHE   A CG  1 
ATOM   1039 C CD1 . PHE   A 1 181 ? 27.958 -8.145  3.408   1.00 61.37  ? 726  PHE   A CD1 1 
ATOM   1040 C CD2 . PHE   A 1 181 ? 26.186 -8.948  4.776   1.00 63.06  ? 726  PHE   A CD2 1 
ATOM   1041 C CE1 . PHE   A 1 181 ? 28.021 -9.366  2.767   1.00 61.55  ? 726  PHE   A CE1 1 
ATOM   1042 C CE2 . PHE   A 1 181 ? 26.242 -10.171 4.140   1.00 66.43  ? 726  PHE   A CE2 1 
ATOM   1043 C CZ  . PHE   A 1 181 ? 27.161 -10.381 3.133   1.00 64.04  ? 726  PHE   A CZ  1 
ATOM   1044 N N   . THR   A 1 182 ? 27.971 -4.822  7.420   1.00 59.53  ? 727  THR   A N   1 
ATOM   1045 C CA  . THR   A 1 182 ? 27.770 -3.683  8.292   1.00 59.81  ? 727  THR   A CA  1 
ATOM   1046 C C   . THR   A 1 182 ? 28.950 -2.736  8.217   1.00 58.77  ? 727  THR   A C   1 
ATOM   1047 O O   . THR   A 1 182 ? 28.780 -1.526  8.103   1.00 62.35  ? 727  THR   A O   1 
ATOM   1048 C CB  . THR   A 1 182 ? 27.552 -4.170  9.737   1.00 59.32  ? 727  THR   A CB  1 
ATOM   1049 O OG1 . THR   A 1 182 ? 26.342 -4.935  9.802   1.00 56.13  ? 727  THR   A OG1 1 
ATOM   1050 C CG2 . THR   A 1 182 ? 27.456 -3.006  10.697  1.00 53.78  ? 727  THR   A CG2 1 
ATOM   1051 N N   . TYR   A 1 183 ? 30.151 -3.284  8.246   1.00 57.08  ? 728  TYR   A N   1 
ATOM   1052 C CA  . TYR   A 1 183 ? 31.341 -2.454  8.192   1.00 60.74  ? 728  TYR   A CA  1 
ATOM   1053 C C   . TYR   A 1 183 ? 31.468 -1.702  6.890   1.00 59.18  ? 728  TYR   A C   1 
ATOM   1054 O O   . TYR   A 1 183 ? 31.781 -0.516  6.879   1.00 57.31  ? 728  TYR   A O   1 
ATOM   1055 C CB  . TYR   A 1 183 ? 32.588 -3.309  8.379   1.00 62.25  ? 728  TYR   A CB  1 
ATOM   1056 C CG  . TYR   A 1 183 ? 33.869 -2.530  8.225   1.00 67.40  ? 728  TYR   A CG  1 
ATOM   1057 C CD1 . TYR   A 1 183 ? 34.349 -1.738  9.256   1.00 66.44  ? 728  TYR   A CD1 1 
ATOM   1058 C CD2 . TYR   A 1 183 ? 34.594 -2.580  7.044   1.00 69.78  ? 728  TYR   A CD2 1 
ATOM   1059 C CE1 . TYR   A 1 183 ? 35.518 -1.020  9.117   1.00 67.98  ? 728  TYR   A CE1 1 
ATOM   1060 C CE2 . TYR   A 1 183 ? 35.765 -1.866  6.896   1.00 73.09  ? 728  TYR   A CE2 1 
ATOM   1061 C CZ  . TYR   A 1 183 ? 36.221 -1.088  7.935   1.00 73.14  ? 728  TYR   A CZ  1 
ATOM   1062 O OH  . TYR   A 1 183 ? 37.386 -0.376  7.791   1.00 77.27  ? 728  TYR   A OH  1 
ATOM   1063 N N   . GLN   A 1 184 ? 31.228 -2.386  5.785   1.00 62.06  ? 729  GLN   A N   1 
ATOM   1064 C CA  . GLN   A 1 184 ? 31.409 -1.758  4.488   1.00 62.76  ? 729  GLN   A CA  1 
ATOM   1065 C C   . GLN   A 1 184 ? 30.411 -0.637  4.252   1.00 61.93  ? 729  GLN   A C   1 
ATOM   1066 O O   . GLN   A 1 184 ? 30.762 0.409   3.722   1.00 59.43  ? 729  GLN   A O   1 
ATOM   1067 C CB  . GLN   A 1 184 ? 31.308 -2.803  3.383   1.00 61.10  ? 729  GLN   A CB  1 
ATOM   1068 C CG  . GLN   A 1 184 ? 32.253 -3.981  3.526   1.00 63.66  ? 729  GLN   A CG  1 
ATOM   1069 C CD  . GLN   A 1 184 ? 32.119 -4.964  2.381   1.00 67.95  ? 729  GLN   A CD  1 
ATOM   1070 O OE1 . GLN   A 1 184 ? 32.080 -4.574  1.216   1.00 76.81  ? 729  GLN   A OE1 1 
ATOM   1071 N NE2 . GLN   A 1 184 ? 32.054 -6.247  2.707   1.00 69.70  ? 729  GLN   A NE2 1 
ATOM   1072 N N   . VAL   A 1 185 ? 29.170 -0.851  4.656   1.00 60.50  ? 730  VAL   A N   1 
ATOM   1073 C CA  . VAL   A 1 185 ? 28.163 0.169   4.466   1.00 58.39  ? 730  VAL   A CA  1 
ATOM   1074 C C   . VAL   A 1 185 ? 28.577 1.396   5.240   1.00 57.04  ? 730  VAL   A C   1 
ATOM   1075 O O   . VAL   A 1 185 ? 28.416 2.516   4.769   1.00 62.13  ? 730  VAL   A O   1 
ATOM   1076 C CB  . VAL   A 1 185 ? 26.775 -0.298  4.919   1.00 54.49  ? 730  VAL   A CB  1 
ATOM   1077 C CG1 . VAL   A 1 185 ? 25.775 0.844   4.839   1.00 45.86  ? 730  VAL   A CG1 1 
ATOM   1078 C CG2 . VAL   A 1 185 ? 26.315 -1.473  4.075   1.00 50.37  ? 730  VAL   A CG2 1 
ATOM   1079 N N   . ALA   A 1 186 ? 29.133 1.189   6.422   1.00 61.71  ? 731  ALA   A N   1 
ATOM   1080 C CA  . ALA   A 1 186 ? 29.572 2.306   7.237   1.00 57.04  ? 731  ALA   A CA  1 
ATOM   1081 C C   . ALA   A 1 186 ? 30.650 3.088   6.528   1.00 53.91  ? 731  ALA   A C   1 
ATOM   1082 O O   . ALA   A 1 186 ? 30.662 4.314   6.556   1.00 56.04  ? 731  ALA   A O   1 
ATOM   1083 C CB  . ALA   A 1 186 ? 30.080 1.809   8.569   1.00 58.20  ? 731  ALA   A CB  1 
ATOM   1084 N N   . ARG   A 1 187 ? 31.560 2.377   5.888   1.00 58.60  ? 732  ARG   A N   1 
ATOM   1085 C CA  . ARG   A 1 187 ? 32.636 3.035   5.173   1.00 66.55  ? 732  ARG   A CA  1 
ATOM   1086 C C   . ARG   A 1 187 ? 32.118 3.854   4.004   1.00 59.85  ? 732  ARG   A C   1 
ATOM   1087 O O   . ARG   A 1 187 ? 32.522 4.996   3.816   1.00 58.01  ? 732  ARG   A O   1 
ATOM   1088 C CB  . ARG   A 1 187 ? 33.635 1.996   4.680   1.00 65.85  ? 732  ARG   A CB  1 
ATOM   1089 C CG  . ARG   A 1 187 ? 34.330 1.218   5.782   1.00 64.92  ? 732  ARG   A CG  1 
ATOM   1090 C CD  . ARG   A 1 187 ? 35.075 2.151   6.718   1.00 67.68  ? 732  ARG   A CD  1 
ATOM   1091 N NE  . ARG   A 1 187 ? 35.789 3.192   5.987   1.00 72.28  ? 732  ARG   A NE  1 
ATOM   1092 C CZ  . ARG   A 1 187 ? 37.018 3.059   5.502   1.00 77.66  ? 732  ARG   A CZ  1 
ATOM   1093 N NH1 . ARG   A 1 187 ? 37.680 1.924   5.668   1.00 82.46  ? 732  ARG   A NH1 1 
ATOM   1094 N NH2 . ARG   A 1 187 ? 37.584 4.062   4.849   1.00 75.07  ? 732  ARG   A NH2 1 
ATOM   1095 N N   . GLY   A 1 188 ? 31.218 3.277   3.221   1.00 59.79  ? 733  GLY   A N   1 
ATOM   1096 C CA  . GLY   A 1 188 ? 30.651 3.987   2.092   1.00 61.48  ? 733  GLY   A CA  1 
ATOM   1097 C C   . GLY   A 1 188 ? 29.877 5.204   2.528   1.00 61.40  ? 733  GLY   A C   1 
ATOM   1098 O O   . GLY   A 1 188 ? 29.915 6.237   1.870   1.00 56.79  ? 733  GLY   A O   1 
ATOM   1099 N N   . MET   A 1 189 ? 29.169 5.086   3.639   1.00 57.24  ? 734  MET   A N   1 
ATOM   1100 C CA  . MET   A 1 189 ? 28.422 6.216   4.156   1.00 55.72  ? 734  MET   A CA  1 
ATOM   1101 C C   . MET   A 1 189 ? 29.384 7.286   4.609   1.00 54.50  ? 734  MET   A C   1 
ATOM   1102 O O   . MET   A 1 189 ? 29.104 8.470   4.482   1.00 56.33  ? 734  MET   A O   1 
ATOM   1103 C CB  . MET   A 1 189 ? 27.513 5.779   5.295   1.00 51.59  ? 734  MET   A CB  1 
ATOM   1104 C CG  . MET   A 1 189 ? 26.392 4.848   4.871   1.00 59.11  ? 734  MET   A CG  1 
ATOM   1105 S SD  . MET   A 1 189 ? 25.358 5.549   3.573   1.00 50.78  ? 734  MET   A SD  1 
ATOM   1106 C CE  . MET   A 1 189 ? 24.762 7.030   4.376   1.00 47.84  ? 734  MET   A CE  1 
ATOM   1107 N N   . GLU   A 1 190 ? 30.526 6.872   5.134   1.00 59.49  ? 735  GLU   A N   1 
ATOM   1108 C CA  . GLU   A 1 190 ? 31.535 7.828   5.546   1.00 67.09  ? 735  GLU   A CA  1 
ATOM   1109 C C   . GLU   A 1 190 ? 32.008 8.589   4.333   1.00 64.02  ? 735  GLU   A C   1 
ATOM   1110 O O   . GLU   A 1 190 ? 32.185 9.802   4.381   1.00 64.80  ? 735  GLU   A O   1 
ATOM   1111 C CB  . GLU   A 1 190 ? 32.697 7.103   6.207   1.00 63.76  ? 735  GLU   A CB  1 
ATOM   1112 C CG  . GLU   A 1 190 ? 33.835 7.999   6.654   1.00 67.51  ? 735  GLU   A CG  1 
ATOM   1113 C CD  . GLU   A 1 190 ? 34.973 7.211   7.268   1.00 77.49  ? 735  GLU   A CD  1 
ATOM   1114 O OE1 . GLU   A 1 190 ? 34.792 6.001   7.516   1.00 75.39  ? 735  GLU   A OE1 1 
ATOM   1115 O OE2 . GLU   A 1 190 ? 36.046 7.801   7.504   1.00 83.28  ? 735  GLU   A OE2 1 
ATOM   1116 N N   . PHE   A 1 191 ? 32.196 7.881   3.232   1.00 64.96  ? 736  PHE   A N   1 
ATOM   1117 C CA  . PHE   A 1 191 ? 32.624 8.512   2.000   1.00 61.08  ? 736  PHE   A CA  1 
ATOM   1118 C C   . PHE   A 1 191 ? 31.614 9.545   1.544   1.00 61.32  ? 736  PHE   A C   1 
ATOM   1119 O O   . PHE   A 1 191 ? 31.977 10.638  1.130   1.00 66.29  ? 736  PHE   A O   1 
ATOM   1120 C CB  . PHE   A 1 191 ? 32.807 7.432   0.942   1.00 57.60  ? 736  PHE   A CB  1 
ATOM   1121 C CG  . PHE   A 1 191 ? 33.036 7.954   -0.440  1.00 69.17  ? 736  PHE   A CG  1 
ATOM   1122 C CD1 . PHE   A 1 191 ? 34.263 8.472   -0.803  1.00 73.86  ? 736  PHE   A CD1 1 
ATOM   1123 C CD2 . PHE   A 1 191 ? 32.030 7.896   -1.386  1.00 69.95  ? 736  PHE   A CD2 1 
ATOM   1124 C CE1 . PHE   A 1 191 ? 34.479 8.943   -2.082  1.00 71.42  ? 736  PHE   A CE1 1 
ATOM   1125 C CE2 . PHE   A 1 191 ? 32.238 8.364   -2.666  1.00 76.33  ? 736  PHE   A CE2 1 
ATOM   1126 C CZ  . PHE   A 1 191 ? 33.465 8.887   -3.014  1.00 75.94  ? 736  PHE   A CZ  1 
ATOM   1127 N N   . LEU   A 1 192 ? 30.339 9.209   1.623   1.00 58.28  ? 737  LEU   A N   1 
ATOM   1128 C CA  . LEU   A 1 192 ? 29.313 10.121  1.148   1.00 58.63  ? 737  LEU   A CA  1 
ATOM   1129 C C   . LEU   A 1 192 ? 29.232 11.351  2.025   1.00 58.69  ? 737  LEU   A C   1 
ATOM   1130 O O   . LEU   A 1 192 ? 29.043 12.456  1.535   1.00 59.15  ? 737  LEU   A O   1 
ATOM   1131 C CB  . LEU   A 1 192 ? 27.964 9.410   1.081   1.00 56.28  ? 737  LEU   A CB  1 
ATOM   1132 C CG  . LEU   A 1 192 ? 27.908 8.163   0.202   1.00 54.70  ? 737  LEU   A CG  1 
ATOM   1133 C CD1 . LEU   A 1 192 ? 26.492 7.614   0.160   1.00 47.80  ? 737  LEU   A CD1 1 
ATOM   1134 C CD2 . LEU   A 1 192 ? 28.401 8.482   -1.199  1.00 61.46  ? 737  LEU   A CD2 1 
ATOM   1135 N N   . ALA   A 1 193 ? 29.374 11.162  3.324   1.00 61.83  ? 738  ALA   A N   1 
ATOM   1136 C CA  . ALA   A 1 193 ? 29.344 12.284  4.236   1.00 56.11  ? 738  ALA   A CA  1 
ATOM   1137 C C   . ALA   A 1 193 ? 30.549 13.159  3.983   1.00 59.98  ? 738  ALA   A C   1 
ATOM   1138 O O   . ALA   A 1 193 ? 30.470 14.376  4.101   1.00 57.89  ? 738  ALA   A O   1 
ATOM   1139 C CB  . ALA   A 1 193 ? 29.328 11.792  5.663   1.00 58.47  ? 738  ALA   A CB  1 
ATOM   1140 N N   . SER   A 1 194 ? 31.669 12.544  3.634   1.00 60.64  ? 739  SER   A N   1 
ATOM   1141 C CA  . SER   A 1 194 ? 32.858 13.310  3.319   1.00 63.96  ? 739  SER   A CA  1 
ATOM   1142 C C   . SER   A 1 194 ? 32.564 14.181  2.125   1.00 70.02  ? 739  SER   A C   1 
ATOM   1143 O O   . SER   A 1 194 ? 33.031 15.312  2.045   1.00 73.89  ? 739  SER   A O   1 
ATOM   1144 C CB  . SER   A 1 194 ? 34.029 12.391  3.005   1.00 59.35  ? 739  SER   A CB  1 
ATOM   1145 O OG  . SER   A 1 194 ? 33.964 11.917  1.676   1.00 66.55  ? 739  SER   A OG  1 
ATOM   1146 N N   . LYS   A 1 195 ? 31.781 13.661  1.192   1.00 64.34  ? 740  LYS   A N   1 
ATOM   1147 C CA  . LYS   A 1 195 ? 31.448 14.409  -0.005  1.00 65.32  ? 740  LYS   A CA  1 
ATOM   1148 C C   . LYS   A 1 195 ? 30.221 15.256  0.240   1.00 66.78  ? 740  LYS   A C   1 
ATOM   1149 O O   . LYS   A 1 195 ? 29.608 15.748  -0.701  1.00 67.29  ? 740  LYS   A O   1 
ATOM   1150 C CB  . LYS   A 1 195 ? 31.207 13.446  -1.157  1.00 59.33  ? 740  LYS   A CB  1 
ATOM   1151 C CG  . LYS   A 1 195 ? 32.382 12.538  -1.466  1.00 60.37  ? 740  LYS   A CG  1 
ATOM   1152 C CD  . LYS   A 1 195 ? 33.506 13.314  -2.128  1.00 69.32  ? 740  LYS   A CD  1 
ATOM   1153 C CE  . LYS   A 1 195 ? 34.664 12.402  -2.490  1.00 78.54  ? 740  LYS   A CE  1 
ATOM   1154 N NZ  . LYS   A 1 195 ? 35.672 13.096  -3.336  1.00 82.94  ? 740  LYS   A NZ  1 
ATOM   1155 N N   . ASN   A 1 196 ? 29.854 15.421  1.503   1.00 63.79  ? 741  ASN   A N   1 
ATOM   1156 C CA  . ASN   A 1 196 ? 28.682 16.215  1.858   1.00 61.91  ? 741  ASN   A CA  1 
ATOM   1157 C C   . ASN   A 1 196 ? 27.420 15.716  1.175   1.00 64.76  ? 741  ASN   A C   1 
ATOM   1158 O O   . ASN   A 1 196 ? 26.651 16.503  0.633   1.00 65.33  ? 741  ASN   A O   1 
ATOM   1159 C CB  . ASN   A 1 196 ? 28.916 17.684  1.534   1.00 66.84  ? 741  ASN   A CB  1 
ATOM   1160 C CG  . ASN   A 1 196 ? 29.891 18.341  2.485   1.00 79.30  ? 741  ASN   A CG  1 
ATOM   1161 O OD1 . ASN   A 1 196 ? 29.964 19.565  2.565   1.00 89.10  ? 741  ASN   A OD1 1 
ATOM   1162 N ND2 . ASN   A 1 196 ? 30.639 17.530  3.221   1.00 77.60  ? 741  ASN   A ND2 1 
ATOM   1163 N N   . CYS   A 1 197 ? 27.198 14.408  1.217   1.00 60.54  ? 742  CYS   A N   1 
ATOM   1164 C CA  . CYS   A 1 197 ? 26.022 13.834  0.587   1.00 57.59  ? 742  CYS   A CA  1 
ATOM   1165 C C   . CYS   A 1 197 ? 25.120 13.126  1.565   1.00 57.05  ? 742  CYS   A C   1 
ATOM   1166 O O   . CYS   A 1 197 ? 25.570 12.263  2.309   1.00 58.91  ? 742  CYS   A O   1 
ATOM   1167 C CB  . CYS   A 1 197 ? 26.436 12.842  -0.500  1.00 61.65  ? 742  CYS   A CB  1 
ATOM   1168 S SG  . CYS   A 1 197 ? 25.073 11.961  -1.292  1.00 63.73  ? 742  CYS   A SG  1 
ATOM   1169 N N   . VAL   A 1 198 ? 23.843 13.480  1.566   1.00 57.05  ? 743  VAL   A N   1 
ATOM   1170 C CA  . VAL   A 1 198 ? 22.885 12.780  2.404   1.00 54.00  ? 743  VAL   A CA  1 
ATOM   1171 C C   . VAL   A 1 198 ? 22.055 11.895  1.492   1.00 52.68  ? 743  VAL   A C   1 
ATOM   1172 O O   . VAL   A 1 198 ? 21.292 12.398  0.679   1.00 55.99  ? 743  VAL   A O   1 
ATOM   1173 C CB  . VAL   A 1 198 ? 21.997 13.751  3.195   1.00 54.39  ? 743  VAL   A CB  1 
ATOM   1174 C CG1 . VAL   A 1 198 ? 21.089 12.988  4.143   1.00 55.37  ? 743  VAL   A CG1 1 
ATOM   1175 C CG2 . VAL   A 1 198 ? 22.855 14.741  3.964   1.00 49.69  ? 743  VAL   A CG2 1 
ATOM   1176 N N   . HIS   A 1 199 ? 22.210 10.583  1.611   1.00 52.63  ? 744  HIS   A N   1 
ATOM   1177 C CA  . HIS   A 1 199 ? 21.508 9.641   0.745   1.00 48.37  ? 744  HIS   A CA  1 
ATOM   1178 C C   . HIS   A 1 199 ? 20.007 9.708   0.904   1.00 50.36  ? 744  HIS   A C   1 
ATOM   1179 O O   . HIS   A 1 199 ? 19.279 9.674   -0.080  1.00 50.81  ? 744  HIS   A O   1 
ATOM   1180 C CB  . HIS   A 1 199 ? 22.003 8.233   1.061   1.00 45.56  ? 744  HIS   A CB  1 
ATOM   1181 C CG  . HIS   A 1 199 ? 21.615 7.206   0.047   1.00 49.29  ? 744  HIS   A CG  1 
ATOM   1182 N ND1 . HIS   A 1 199 ? 20.444 6.487   0.127   1.00 47.78  ? 744  HIS   A ND1 1 
ATOM   1183 C CD2 . HIS   A 1 199 ? 22.253 6.763   -1.061  1.00 54.38  ? 744  HIS   A CD2 1 
ATOM   1184 C CE1 . HIS   A 1 199 ? 20.372 5.652   -0.892  1.00 52.85  ? 744  HIS   A CE1 1 
ATOM   1185 N NE2 . HIS   A 1 199 ? 21.457 5.800   -1.629  1.00 55.23  ? 744  HIS   A NE2 1 
ATOM   1186 N N   . ARG   A 1 200 ? 19.540 9.773   2.138   1.00 49.68  ? 745  ARG   A N   1 
ATOM   1187 C CA  . ARG   A 1 200 ? 18.110 9.880   2.412   1.00 41.82  ? 745  ARG   A CA  1 
ATOM   1188 C C   . ARG   A 1 200 ? 17.314 8.615   2.080   1.00 45.71  ? 745  ARG   A C   1 
ATOM   1189 O O   . ARG   A 1 200 ? 16.096 8.613   2.203   1.00 44.88  ? 745  ARG   A O   1 
ATOM   1190 C CB  . ARG   A 1 200 ? 17.523 11.116  1.717   1.00 48.18  ? 745  ARG   A CB  1 
ATOM   1191 C CG  . ARG   A 1 200 ? 18.086 12.427  2.237   1.00 44.40  ? 745  ARG   A CG  1 
ATOM   1192 C CD  . ARG   A 1 200 ? 17.360 13.637  1.677   1.00 45.81  ? 745  ARG   A CD  1 
ATOM   1193 N NE  . ARG   A 1 200 ? 15.927 13.597  1.950   1.00 52.93  ? 745  ARG   A NE  1 
ATOM   1194 C CZ  . ARG   A 1 200 ? 14.985 13.601  1.014   1.00 58.90  ? 745  ARG   A CZ  1 
ATOM   1195 N NH1 . ARG   A 1 200 ? 15.316 13.660  -0.267  1.00 57.28  ? 745  ARG   A NH1 1 
ATOM   1196 N NH2 . ARG   A 1 200 ? 13.707 13.561  1.359   1.00 58.37  ? 745  ARG   A NH2 1 
ATOM   1197 N N   . ASP   A 1 201 ? 17.987 7.540   1.685   1.00 46.48  ? 746  ASP   A N   1 
ATOM   1198 C CA  . ASP   A 1 201 ? 17.288 6.275   1.438   1.00 45.72  ? 746  ASP   A CA  1 
ATOM   1199 C C   . ASP   A 1 201 ? 18.161 5.065   1.722   1.00 42.00  ? 746  ASP   A C   1 
ATOM   1200 O O   . ASP   A 1 201 ? 18.180 4.119   0.949   1.00 45.24  ? 746  ASP   A O   1 
ATOM   1201 C CB  . ASP   A 1 201 ? 16.758 6.201   0.007   1.00 47.96  ? 746  ASP   A CB  1 
ATOM   1202 C CG  . ASP   A 1 201 ? 15.660 5.175   -0.153  1.00 53.45  ? 746  ASP   A CG  1 
ATOM   1203 O OD1 . ASP   A 1 201 ? 15.192 4.643   0.873   1.00 54.31  ? 746  ASP   A OD1 1 
ATOM   1204 O OD2 . ASP   A 1 201 ? 15.263 4.901   -1.302  1.00 57.27  ? 746  ASP   A OD2 1 
ATOM   1205 N N   . LEU   A 1 202 ? 18.873 5.088   2.837   1.00 44.21  ? 747  LEU   A N   1 
ATOM   1206 C CA  . LEU   A 1 202 ? 19.698 3.951   3.203   1.00 43.70  ? 747  LEU   A CA  1 
ATOM   1207 C C   . LEU   A 1 202 ? 18.830 2.825   3.705   1.00 47.58  ? 747  LEU   A C   1 
ATOM   1208 O O   . LEU   A 1 202 ? 18.117 2.980   4.687   1.00 48.30  ? 747  LEU   A O   1 
ATOM   1209 C CB  . LEU   A 1 202 ? 20.727 4.331   4.262   1.00 45.04  ? 747  LEU   A CB  1 
ATOM   1210 C CG  . LEU   A 1 202 ? 21.678 3.228   4.714   1.00 41.74  ? 747  LEU   A CG  1 
ATOM   1211 C CD1 . LEU   A 1 202 ? 22.471 2.701   3.531   1.00 46.36  ? 747  LEU   A CD1 1 
ATOM   1212 C CD2 . LEU   A 1 202 ? 22.607 3.756   5.791   1.00 46.28  ? 747  LEU   A CD2 1 
ATOM   1213 N N   . ALA   A 1 203 ? 18.886 1.691   3.024   1.00 43.58  ? 748  ALA   A N   1 
ATOM   1214 C CA  . ALA   A 1 203 ? 18.092 0.549   3.406   1.00 39.63  ? 748  ALA   A CA  1 
ATOM   1215 C C   . ALA   A 1 203 ? 18.685 -0.665  2.735   1.00 44.63  ? 748  ALA   A C   1 
ATOM   1216 O O   . ALA   A 1 203 ? 19.522 -0.535  1.853   1.00 43.14  ? 748  ALA   A O   1 
ATOM   1217 C CB  . ALA   A 1 203 ? 16.659 0.747   2.988   1.00 36.18  ? 748  ALA   A CB  1 
ATOM   1218 N N   . ALA   A 1 204 ? 18.261 -1.848  3.146   1.00 47.64  ? 749  ALA   A N   1 
ATOM   1219 C CA  . ALA   A 1 204 ? 18.822 -3.075  2.595   1.00 50.14  ? 749  ALA   A CA  1 
ATOM   1220 C C   . ALA   A 1 204 ? 18.460 -3.254  1.132   1.00 53.69  ? 749  ALA   A C   1 
ATOM   1221 O O   . ALA   A 1 204 ? 19.162 -3.935  0.396   1.00 54.88  ? 749  ALA   A O   1 
ATOM   1222 C CB  . ALA   A 1 204 ? 18.371 -4.270  3.411   1.00 48.08  ? 749  ALA   A CB  1 
ATOM   1223 N N   . ARG   A 1 205 ? 17.362 -2.650  0.711   1.00 49.49  ? 750  ARG   A N   1 
ATOM   1224 C CA  . ARG   A 1 205 ? 16.977 -2.718  -0.683  1.00 46.15  ? 750  ARG   A CA  1 
ATOM   1225 C C   . ARG   A 1 205 ? 17.973 -1.967  -1.529  1.00 48.25  ? 750  ARG   A C   1 
ATOM   1226 O O   . ARG   A 1 205 ? 18.133 -2.258  -2.704  1.00 50.74  ? 750  ARG   A O   1 
ATOM   1227 C CB  . ARG   A 1 205 ? 15.592 -2.118  -0.866  1.00 42.90  ? 750  ARG   A CB  1 
ATOM   1228 C CG  . ARG   A 1 205 ? 15.442 -0.702  -0.351  1.00 42.71  ? 750  ARG   A CG  1 
ATOM   1229 C CD  . ARG   A 1 205 ? 13.999 -0.250  -0.474  1.00 38.68  ? 750  ARG   A CD  1 
ATOM   1230 N NE  . ARG   A 1 205 ? 13.795 1.076   0.093   1.00 44.63  ? 750  ARG   A NE  1 
ATOM   1231 C CZ  . ARG   A 1 205 ? 13.504 1.302   1.367   1.00 46.48  ? 750  ARG   A CZ  1 
ATOM   1232 N NH1 . ARG   A 1 205 ? 13.386 0.289   2.210   1.00 46.86  ? 750  ARG   A NH1 1 
ATOM   1233 N NH2 . ARG   A 1 205 ? 13.335 2.540   1.800   1.00 48.83  ? 750  ARG   A NH2 1 
ATOM   1234 N N   . ASN   A 1 206 ? 18.650 -0.999  -0.933  1.00 45.43  ? 751  ASN   A N   1 
ATOM   1235 C CA  . ASN   A 1 206 ? 19.581 -0.173  -1.685  1.00 50.66  ? 751  ASN   A CA  1 
ATOM   1236 C C   . ASN   A 1 206 ? 21.023 -0.514  -1.379  1.00 48.26  ? 751  ASN   A C   1 
ATOM   1237 O O   . ASN   A 1 206 ? 21.923 0.234   -1.736  1.00 52.87  ? 751  ASN   A O   1 
ATOM   1238 C CB  . ASN   A 1 206 ? 19.300 1.307   -1.424  1.00 51.67  ? 751  ASN   A CB  1 
ATOM   1239 C CG  . ASN   A 1 206 ? 17.940 1.738   -1.928  1.00 50.54  ? 751  ASN   A CG  1 
ATOM   1240 O OD1 . ASN   A 1 206 ? 17.393 1.148   -2.856  1.00 50.73  ? 751  ASN   A OD1 1 
ATOM   1241 N ND2 . ASN   A 1 206 ? 17.390 2.779   -1.323  1.00 54.74  ? 751  ASN   A ND2 1 
ATOM   1242 N N   . VAL   A 1 207 ? 21.254 -1.629  -0.706  1.00 44.10  ? 752  VAL   A N   1 
ATOM   1243 C CA  . VAL   A 1 207 ? 22.620 -2.076  -0.485  1.00 50.83  ? 752  VAL   A CA  1 
ATOM   1244 C C   . VAL   A 1 207 ? 22.789 -3.312  -1.343  1.00 53.23  ? 752  VAL   A C   1 
ATOM   1245 O O   . VAL   A 1 207 ? 22.097 -4.303  -1.144  1.00 53.64  ? 752  VAL   A O   1 
ATOM   1246 C CB  . VAL   A 1 207 ? 22.922 -2.386  0.985   1.00 49.36  ? 752  VAL   A CB  1 
ATOM   1247 C CG1 . VAL   A 1 207 ? 24.344 -2.897  1.130   1.00 50.79  ? 752  VAL   A CG1 1 
ATOM   1248 C CG2 . VAL   A 1 207 ? 22.708 -1.149  1.840   1.00 44.88  ? 752  VAL   A CG2 1 
ATOM   1249 N N   . LEU   A 1 208 ? 23.692 -3.258  -2.309  1.00 52.16  ? 753  LEU   A N   1 
ATOM   1250 C CA  . LEU   A 1 208 ? 23.845 -4.370  -3.233  1.00 53.20  ? 753  LEU   A CA  1 
ATOM   1251 C C   . LEU   A 1 208 ? 25.080 -5.204  -2.964  1.00 57.27  ? 753  LEU   A C   1 
ATOM   1252 O O   . LEU   A 1 208 ? 26.031 -4.733  -2.354  1.00 59.04  ? 753  LEU   A O   1 
ATOM   1253 C CB  . LEU   A 1 208 ? 23.890 -3.841  -4.665  1.00 55.40  ? 753  LEU   A CB  1 
ATOM   1254 C CG  . LEU   A 1 208 ? 22.664 -3.084  -5.172  1.00 54.32  ? 753  LEU   A CG  1 
ATOM   1255 C CD1 . LEU   A 1 208 ? 22.999 -2.317  -6.439  1.00 54.30  ? 753  LEU   A CD1 1 
ATOM   1256 C CD2 . LEU   A 1 208 ? 21.496 -4.027  -5.403  1.00 55.82  ? 753  LEU   A CD2 1 
ATOM   1257 N N   . LEU   A 1 209 ? 25.061 -6.448  -3.419  1.00 59.05  ? 754  LEU   A N   1 
ATOM   1258 C CA  . LEU   A 1 209 ? 26.205 -7.325  -3.234  1.00 63.59  ? 754  LEU   A CA  1 
ATOM   1259 C C   . LEU   A 1 209 ? 26.851 -7.675  -4.556  1.00 68.82  ? 754  LEU   A C   1 
ATOM   1260 O O   . LEU   A 1 209 ? 26.232 -8.294  -5.412  1.00 64.43  ? 754  LEU   A O   1 
ATOM   1261 C CB  . LEU   A 1 209 ? 25.786 -8.603  -2.517  1.00 64.98  ? 754  LEU   A CB  1 
ATOM   1262 C CG  . LEU   A 1 209 ? 26.158 -8.704  -1.039  1.00 73.46  ? 754  LEU   A CG  1 
ATOM   1263 C CD1 . LEU   A 1 209 ? 25.706 -10.040 -0.471  1.00 71.06  ? 754  LEU   A CD1 1 
ATOM   1264 C CD2 . LEU   A 1 209 ? 27.658 -8.531  -0.867  1.00 70.55  ? 754  LEU   A CD2 1 
ATOM   1265 N N   . ALA   A 1 210 ? 28.106 -7.290  -4.717  1.00 70.87  ? 755  ALA   A N   1 
ATOM   1266 C CA  . ALA   A 1 210 ? 28.820 -7.584  -5.943  1.00 66.68  ? 755  ALA   A CA  1 
ATOM   1267 C C   . ALA   A 1 210 ? 29.687 -8.812  -5.784  1.00 76.69  ? 755  ALA   A C   1 
ATOM   1268 O O   . ALA   A 1 210 ? 29.754 -9.396  -4.707  1.00 75.64  ? 755  ALA   A O   1 
ATOM   1269 C CB  . ALA   A 1 210 ? 29.674 -6.399  -6.340  1.00 65.88  ? 755  ALA   A CB  1 
ATOM   1270 N N   . GLN   A 1 211 ? 30.364 -9.200  -6.856  1.00 73.69  ? 756  GLN   A N   1 
ATOM   1271 C CA  . GLN   A 1 211 ? 31.228 -10.362 -6.799  1.00 77.60  ? 756  GLN   A CA  1 
ATOM   1272 C C   . GLN   A 1 211 ? 32.299 -10.137 -5.760  1.00 78.49  ? 756  GLN   A C   1 
ATOM   1273 O O   . GLN   A 1 211 ? 32.825 -9.035  -5.637  1.00 79.31  ? 756  GLN   A O   1 
ATOM   1274 C CB  . GLN   A 1 211 ? 31.847 -10.643 -8.165  1.00 82.40  ? 756  GLN   A CB  1 
ATOM   1275 C CG  . GLN   A 1 211 ? 32.640 -9.487  -8.746  1.00 85.20  ? 756  GLN   A CG  1 
ATOM   1276 C CD  . GLN   A 1 211 ? 33.249 -9.826  -10.091 1.00 100.67 ? 756  GLN   A CD  1 
ATOM   1277 O OE1 . GLN   A 1 211 ? 34.022 -9.049  -10.649 1.00 106.99 ? 756  GLN   A OE1 1 
ATOM   1278 N NE2 . GLN   A 1 211 ? 32.905 -10.994 -10.618 1.00 97.41  ? 756  GLN   A NE2 1 
ATOM   1279 N N   . GLY   A 1 212 ? 32.625 -11.177 -5.005  1.00 78.70  ? 757  GLY   A N   1 
ATOM   1280 C CA  . GLY   A 1 212 ? 33.592 -11.028 -3.936  1.00 81.98  ? 757  GLY   A CA  1 
ATOM   1281 C C   . GLY   A 1 212 ? 32.880 -10.599 -2.680  1.00 79.53  ? 757  GLY   A C   1 
ATOM   1282 O O   . GLY   A 1 212 ? 33.518 -10.201 -1.709  1.00 82.20  ? 757  GLY   A O   1 
ATOM   1283 N N   . LYS   A 1 213 ? 31.556 -10.669 -2.698  1.00 76.94  ? 758  LYS   A N   1 
ATOM   1284 C CA  . LYS   A 1 213 ? 30.768 -10.255 -1.548  1.00 76.28  ? 758  LYS   A CA  1 
ATOM   1285 C C   . LYS   A 1 213 ? 31.135 -8.857  -1.105  1.00 76.40  ? 758  LYS   A C   1 
ATOM   1286 O O   . LYS   A 1 213 ? 31.226 -8.586  0.088   1.00 78.37  ? 758  LYS   A O   1 
ATOM   1287 C CB  . LYS   A 1 213 ? 30.934 -11.232 -0.388  1.00 81.40  ? 758  LYS   A CB  1 
ATOM   1288 C CG  . LYS   A 1 213 ? 30.052 -12.464 -0.474  1.00 79.22  ? 758  LYS   A CG  1 
ATOM   1289 C CD  . LYS   A 1 213 ? 29.988 -13.169 0.871   1.00 76.85  ? 758  LYS   A CD  1 
ATOM   1290 C CE  . LYS   A 1 213 ? 29.086 -14.388 0.818   1.00 78.17  ? 758  LYS   A CE  1 
ATOM   1291 N NZ  . LYS   A 1 213 ? 28.874 -14.983 2.166   1.00 89.51  ? 758  LYS   A NZ  1 
ATOM   1292 N N   . ILE   A 1 214 ? 31.350 -7.966  -2.060  1.00 76.17  ? 759  ILE   A N   1 
ATOM   1293 C CA  . ILE   A 1 214 ? 31.631 -6.581  -1.717  1.00 77.63  ? 759  ILE   A CA  1 
ATOM   1294 C C   . ILE   A 1 214 ? 30.339 -5.795  -1.836  1.00 75.29  ? 759  ILE   A C   1 
ATOM   1295 O O   . ILE   A 1 214 ? 29.657 -5.874  -2.853  1.00 71.32  ? 759  ILE   A O   1 
ATOM   1296 C CB  . ILE   A 1 214 ? 32.718 -5.976  -2.612  1.00 70.72  ? 759  ILE   A CB  1 
ATOM   1297 C CG1 . ILE   A 1 214 ? 34.030 -6.731  -2.424  1.00 74.38  ? 759  ILE   A CG1 1 
ATOM   1298 C CG2 . ILE   A 1 214 ? 32.901 -4.503  -2.293  1.00 71.76  ? 759  ILE   A CG2 1 
ATOM   1299 C CD1 . ILE   A 1 214 ? 34.512 -6.742  -0.992  1.00 76.00  ? 759  ILE   A CD1 1 
ATOM   1300 N N   . VAL   A 1 215 ? 29.987 -5.053  -0.796  1.00 67.38  ? 760  VAL   A N   1 
ATOM   1301 C CA  . VAL   A 1 215 ? 28.718 -4.339  -0.801  1.00 67.11  ? 760  VAL   A CA  1 
ATOM   1302 C C   . VAL   A 1 215 ? 28.795 -3.028  -1.557  1.00 65.55  ? 760  VAL   A C   1 
ATOM   1303 O O   . VAL   A 1 215 ? 29.848 -2.405  -1.624  1.00 69.33  ? 760  VAL   A O   1 
ATOM   1304 C CB  . VAL   A 1 215 ? 28.213 -4.069  0.630   1.00 68.76  ? 760  VAL   A CB  1 
ATOM   1305 C CG1 . VAL   A 1 215 ? 28.413 -5.294  1.504   1.00 68.01  ? 760  VAL   A CG1 1 
ATOM   1306 C CG2 . VAL   A 1 215 ? 28.904 -2.856  1.224   1.00 66.70  ? 760  VAL   A CG2 1 
ATOM   1307 N N   . LYS   A 1 216 ? 27.675 -2.618  -2.138  1.00 60.89  ? 761  LYS   A N   1 
ATOM   1308 C CA  . LYS   A 1 216 ? 27.634 -1.378  -2.887  1.00 56.87  ? 761  LYS   A CA  1 
ATOM   1309 C C   . LYS   A 1 216 ? 26.359 -0.641  -2.559  1.00 54.90  ? 761  LYS   A C   1 
ATOM   1310 O O   . LYS   A 1 216 ? 25.277 -1.206  -2.660  1.00 54.96  ? 761  LYS   A O   1 
ATOM   1311 C CB  . LYS   A 1 216 ? 27.669 -1.660  -4.382  1.00 58.71  ? 761  LYS   A CB  1 
ATOM   1312 C CG  . LYS   A 1 216 ? 28.749 -2.624  -4.838  1.00 58.52  ? 761  LYS   A CG  1 
ATOM   1313 C CD  . LYS   A 1 216 ? 30.081 -1.924  -5.022  1.00 64.06  ? 761  LYS   A CD  1 
ATOM   1314 C CE  . LYS   A 1 216 ? 31.128 -2.890  -5.548  1.00 62.75  ? 761  LYS   A CE  1 
ATOM   1315 N NZ  . LYS   A 1 216 ? 32.465 -2.252  -5.689  1.00 63.53  ? 761  LYS   A NZ  1 
ATOM   1316 N N   . ILE   A 1 217 ? 26.472 0.622   -2.174  1.00 50.65  ? 762  ILE   A N   1 
ATOM   1317 C CA  . ILE   A 1 217 ? 25.285 1.419   -1.900  1.00 54.22  ? 762  ILE   A CA  1 
ATOM   1318 C C   . ILE   A 1 217 ? 24.756 2.032   -3.189  1.00 52.44  ? 762  ILE   A C   1 
ATOM   1319 O O   . ILE   A 1 217 ? 25.526 2.502   -4.017  1.00 47.95  ? 762  ILE   A O   1 
ATOM   1320 C CB  . ILE   A 1 217 ? 25.562 2.507   -0.845  1.00 46.62  ? 762  ILE   A CB  1 
ATOM   1321 C CG1 . ILE   A 1 217 ? 26.047 1.862   0.454   1.00 47.72  ? 762  ILE   A CG1 1 
ATOM   1322 C CG2 . ILE   A 1 217 ? 24.321 3.350   -0.602  1.00 42.46  ? 762  ILE   A CG2 1 
ATOM   1323 C CD1 . ILE   A 1 217 ? 26.550 2.847   1.483   1.00 50.93  ? 762  ILE   A CD1 1 
ATOM   1324 N N   . CYS   A 1 218 ? 23.443 2.027   -3.358  1.00 49.52  ? 763  CYS   A N   1 
ATOM   1325 C CA  . CYS   A 1 218 ? 22.858 2.552   -4.576  1.00 47.71  ? 763  CYS   A CA  1 
ATOM   1326 C C   . CYS   A 1 218 ? 21.635 3.414   -4.353  1.00 55.69  ? 763  CYS   A C   1 
ATOM   1327 O O   . CYS   A 1 218 ? 21.321 3.770   -3.224  1.00 49.39  ? 763  CYS   A O   1 
ATOM   1328 C CB  . CYS   A 1 218 ? 22.456 1.399   -5.498  1.00 46.52  ? 763  CYS   A CB  1 
ATOM   1329 S SG  . CYS   A 1 218 ? 20.979 0.503   -4.986  1.00 58.20  ? 763  CYS   A SG  1 
ATOM   1330 N N   . ASP   A 1 219 ? 20.948 3.750   -5.437  1.00 56.51  ? 764  ASP   A N   1 
ATOM   1331 C CA  . ASP   A 1 219 ? 19.720 4.550   -5.371  1.00 50.09  ? 764  ASP   A CA  1 
ATOM   1332 C C   . ASP   A 1 219 ? 19.858 5.928   -4.782  1.00 53.16  ? 764  ASP   A C   1 
ATOM   1333 O O   . ASP   A 1 219 ? 19.499 6.159   -3.637  1.00 55.11  ? 764  ASP   A O   1 
ATOM   1334 C CB  . ASP   A 1 219 ? 18.602 3.794   -4.649  1.00 47.43  ? 764  ASP   A CB  1 
ATOM   1335 C CG  . ASP   A 1 219 ? 17.230 4.335   -4.978  1.00 51.41  ? 764  ASP   A CG  1 
ATOM   1336 O OD1 . ASP   A 1 219 ? 17.146 5.414   -5.597  1.00 50.24  ? 764  ASP   A OD1 1 
ATOM   1337 O OD2 . ASP   A 1 219 ? 16.232 3.679   -4.623  1.00 61.10  ? 764  ASP   A OD2 1 
ATOM   1338 N N   . PHE   A 1 220 ? 20.386 6.853   -5.558  1.00 57.40  ? 765  PHE   A N   1 
ATOM   1339 C CA  . PHE   A 1 220 ? 20.399 8.222   -5.112  1.00 54.74  ? 765  PHE   A CA  1 
ATOM   1340 C C   . PHE   A 1 220 ? 19.087 8.735   -5.685  1.00 51.56  ? 765  PHE   A C   1 
ATOM   1341 O O   . PHE   A 1 220 ? 18.227 7.940   -6.048  1.00 59.39  ? 765  PHE   A O   1 
ATOM   1342 C CB  . PHE   A 1 220 ? 21.618 8.957   -5.631  1.00 48.82  ? 765  PHE   A CB  1 
ATOM   1343 C CG  . PHE   A 1 220 ? 22.907 8.436   -5.071  1.00 56.41  ? 765  PHE   A CG  1 
ATOM   1344 C CD1 . PHE   A 1 220 ? 23.520 7.329   -5.627  1.00 59.54  ? 765  PHE   A CD1 1 
ATOM   1345 C CD2 . PHE   A 1 220 ? 23.493 9.038   -3.973  1.00 62.99  ? 765  PHE   A CD2 1 
ATOM   1346 C CE1 . PHE   A 1 220 ? 24.700 6.839   -5.107  1.00 60.72  ? 765  PHE   A CE1 1 
ATOM   1347 C CE2 . PHE   A 1 220 ? 24.673 8.554   -3.448  1.00 61.25  ? 765  PHE   A CE2 1 
ATOM   1348 C CZ  . PHE   A 1 220 ? 25.278 7.452   -4.015  1.00 57.20  ? 765  PHE   A CZ  1 
ATOM   1349 N N   . GLY   A 1 221 ? 18.895 10.033  -5.776  1.00 51.30  ? 766  GLY   A N   1 
ATOM   1350 C CA  . GLY   A 1 221 ? 17.613 10.522  -6.247  1.00 58.45  ? 766  GLY   A CA  1 
ATOM   1351 C C   . GLY   A 1 221 ? 16.884 11.219  -5.139  1.00 59.55  ? 766  GLY   A C   1 
ATOM   1352 O O   . GLY   A 1 221 ? 16.188 12.202  -5.377  1.00 57.07  ? 766  GLY   A O   1 
ATOM   1353 N N   . LEU   A 1 222 ? 17.012 10.708  -3.928  1.00 56.98  ? 767  LEU   A N   1 
ATOM   1354 C CA  . LEU   A 1 222 ? 16.452 11.401  -2.795  1.00 54.39  ? 767  LEU   A CA  1 
ATOM   1355 C C   . LEU   A 1 222 ? 17.655 12.059  -2.185  1.00 60.70  ? 767  LEU   A C   1 
ATOM   1356 O O   . LEU   A 1 222 ? 17.541 12.812  -1.230  1.00 63.28  ? 767  LEU   A O   1 
ATOM   1357 C CB  . LEU   A 1 222 ? 15.800 10.441  -1.814  1.00 52.80  ? 767  LEU   A CB  1 
ATOM   1358 C CG  . LEU   A 1 222 ? 14.501 9.767   -2.238  1.00 59.24  ? 767  LEU   A CG  1 
ATOM   1359 C CD1 . LEU   A 1 222 ? 13.963 8.930   -1.089  1.00 50.94  ? 767  LEU   A CD1 1 
ATOM   1360 C CD2 . LEU   A 1 222 ? 13.487 10.818  -2.657  1.00 59.37  ? 767  LEU   A CD2 1 
ATOM   1361 N N   . ALA   A 1 223 ? 18.822 11.793  -2.754  1.00 52.55  ? 768  ALA   A N   1 
ATOM   1362 C CA  . ALA   A 1 223 ? 20.055 12.321  -2.197  1.00 52.72  ? 768  ALA   A CA  1 
ATOM   1363 C C   . ALA   A 1 223 ? 20.218 13.804  -2.425  1.00 58.91  ? 768  ALA   A C   1 
ATOM   1364 O O   . ALA   A 1 223 ? 19.917 14.312  -3.500  1.00 54.81  ? 768  ALA   A O   1 
ATOM   1365 C CB  . ALA   A 1 223 ? 21.242 11.570  -2.768  1.00 44.68  ? 768  ALA   A CB  1 
ATOM   1366 N N   . ARG   A 1 224 ? 20.704 14.501  -1.407  1.00 62.91  ? 769  ARG   A N   1 
ATOM   1367 C CA  . ARG   A 1 224 ? 20.889 15.936  -1.509  1.00 59.27  ? 769  ARG   A CA  1 
ATOM   1368 C C   . ARG   A 1 224 ? 22.262 16.335  -1.038  1.00 58.46  ? 769  ARG   A C   1 
ATOM   1369 O O   . ARG   A 1 224 ? 22.925 15.582  -0.334  1.00 60.33  ? 769  ARG   A O   1 
ATOM   1370 C CB  . ARG   A 1 224 ? 19.848 16.671  -0.675  1.00 54.30  ? 769  ARG   A CB  1 
ATOM   1371 C CG  . ARG   A 1 224 ? 18.616 17.101  -1.443  1.00 63.60  ? 769  ARG   A CG  1 
ATOM   1372 C CD  . ARG   A 1 224 ? 17.581 15.997  -1.504  1.00 66.27  ? 769  ARG   A CD  1 
ATOM   1373 N NE  . ARG   A 1 224 ? 16.466 16.377  -2.360  1.00 70.08  ? 769  ARG   A NE  1 
ATOM   1374 C CZ  . ARG   A 1 224 ? 16.391 16.082  -3.651  1.00 66.64  ? 769  ARG   A CZ  1 
ATOM   1375 N NH1 . ARG   A 1 224 ? 17.362 15.393  -4.230  1.00 63.87  ? 769  ARG   A NH1 1 
ATOM   1376 N NH2 . ARG   A 1 224 ? 15.342 16.470  -4.360  1.00 79.45  ? 769  ARG   A NH2 1 
ATOM   1377 N N   . ASP   A 1 225 ? 22.704 17.516  -1.440  1.00 64.04  ? 770  ASP   A N   1 
ATOM   1378 C CA  . ASP   A 1 225 ? 23.978 18.016  -0.975  1.00 66.07  ? 770  ASP   A CA  1 
ATOM   1379 C C   . ASP   A 1 225 ? 23.681 19.014  0.106   1.00 71.34  ? 770  ASP   A C   1 
ATOM   1380 O O   . ASP   A 1 225 ? 23.025 20.018  -0.148  1.00 76.21  ? 770  ASP   A O   1 
ATOM   1381 C CB  . ASP   A 1 225 ? 24.751 18.674  -2.110  1.00 70.46  ? 770  ASP   A CB  1 
ATOM   1382 C CG  . ASP   A 1 225 ? 26.116 19.157  -1.683  1.00 72.42  ? 770  ASP   A CG  1 
ATOM   1383 O OD1 . ASP   A 1 225 ? 26.193 19.999  -0.768  1.00 79.03  ? 770  ASP   A OD1 1 
ATOM   1384 O OD2 . ASP   A 1 225 ? 27.115 18.704  -2.274  1.00 76.00  ? 770  ASP   A OD2 1 
ATOM   1385 N N   . ILE   A 1 226 ? 24.143 18.738  1.316   1.00 70.42  ? 771  ILE   A N   1 
ATOM   1386 C CA  . ILE   A 1 226 ? 23.913 19.639  2.434   1.00 68.21  ? 771  ILE   A CA  1 
ATOM   1387 C C   . ILE   A 1 226 ? 23.586 21.055  1.969   1.00 70.30  ? 771  ILE   A C   1 
ATOM   1388 O O   . ILE   A 1 226 ? 23.646 22.007  2.742   1.00 83.79  ? 771  ILE   A O   1 
ATOM   1389 C CB  . ILE   A 1 226 ? 25.135 19.667  3.363   1.00 70.33  ? 771  ILE   A CB  1 
ATOM   1390 C CG1 . ILE   A 1 226 ? 26.423 19.879  2.564   1.00 73.62  ? 771  ILE   A CG1 1 
ATOM   1391 C CG2 . ILE   A 1 226 ? 25.229 18.369  4.145   1.00 58.70  ? 771  ILE   A CG2 1 
ATOM   1392 C CD1 . ILE   A 1 226 ? 26.673 21.306  2.127   1.00 71.66  ? 771  ILE   A CD1 1 
ATOM   1393 N N   . THR   A 1 238 ? 6.092  13.493  -3.380  1.00 81.76  ? 783  THR   A N   1 
ATOM   1394 C CA  . THR   A 1 238 ? 7.122  12.480  -3.222  1.00 72.87  ? 783  THR   A CA  1 
ATOM   1395 C C   . THR   A 1 238 ? 6.786  11.515  -2.104  1.00 70.92  ? 783  THR   A C   1 
ATOM   1396 O O   . THR   A 1 238 ? 6.350  11.921  -1.033  1.00 65.97  ? 783  THR   A O   1 
ATOM   1397 C CB  . THR   A 1 238 ? 8.494  13.113  -2.937  1.00 70.17  ? 783  THR   A CB  1 
ATOM   1398 O OG1 . THR   A 1 238 ? 9.469  12.078  -2.762  1.00 67.26  ? 783  THR   A OG1 1 
ATOM   1399 C CG2 . THR   A 1 238 ? 8.439  13.971  -1.683  1.00 61.67  ? 783  THR   A CG2 1 
ATOM   1400 N N   . PHE   A 1 239 ? 6.976  10.230  -2.357  1.00 69.76  ? 784  PHE   A N   1 
ATOM   1401 C CA  . PHE   A 1 239 ? 6.720  9.231   -1.339  1.00 58.38  ? 784  PHE   A CA  1 
ATOM   1402 C C   . PHE   A 1 239 ? 8.027  8.958   -0.645  1.00 56.93  ? 784  PHE   A C   1 
ATOM   1403 O O   . PHE   A 1 239 ? 9.060  8.864   -1.292  1.00 59.57  ? 784  PHE   A O   1 
ATOM   1404 C CB  . PHE   A 1 239 ? 6.144  7.971   -1.965  1.00 60.82  ? 784  PHE   A CB  1 
ATOM   1405 C CG  . PHE   A 1 239 ? 4.860  8.197   -2.700  1.00 68.57  ? 784  PHE   A CG  1 
ATOM   1406 C CD1 . PHE   A 1 239 ? 4.866  8.662   -4.002  1.00 70.85  ? 784  PHE   A CD1 1 
ATOM   1407 C CD2 . PHE   A 1 239 ? 3.646  7.944   -2.089  1.00 63.29  ? 784  PHE   A CD2 1 
ATOM   1408 C CE1 . PHE   A 1 239 ? 3.683  8.873   -4.683  1.00 64.25  ? 784  PHE   A CE1 1 
ATOM   1409 C CE2 . PHE   A 1 239 ? 2.460  8.151   -2.763  1.00 70.46  ? 784  PHE   A CE2 1 
ATOM   1410 C CZ  . PHE   A 1 239 ? 2.478  8.616   -4.062  1.00 65.00  ? 784  PHE   A CZ  1 
ATOM   1411 N N   . LEU   A 1 240 ? 7.997  8.836   0.672   1.00 58.95  ? 785  LEU   A N   1 
ATOM   1412 C CA  . LEU   A 1 240 ? 9.239  8.688   1.413   1.00 50.06  ? 785  LEU   A CA  1 
ATOM   1413 C C   . LEU   A 1 240 ? 9.328  7.425   2.253   1.00 47.07  ? 785  LEU   A C   1 
ATOM   1414 O O   . LEU   A 1 240 ? 8.314  6.909   2.708   1.00 48.04  ? 785  LEU   A O   1 
ATOM   1415 C CB  . LEU   A 1 240 ? 9.427  9.918   2.297   1.00 52.39  ? 785  LEU   A CB  1 
ATOM   1416 C CG  . LEU   A 1 240 ? 9.460  11.255  1.561   1.00 59.30  ? 785  LEU   A CG  1 
ATOM   1417 C CD1 . LEU   A 1 240 ? 9.558  12.402  2.551   1.00 58.90  ? 785  LEU   A CD1 1 
ATOM   1418 C CD2 . LEU   A 1 240 ? 10.617 11.290  0.577   1.00 53.78  ? 785  LEU   A CD2 1 
ATOM   1419 N N   . PRO   A 1 241 ? 10.551 6.928   2.470   1.00 44.04  ? 786  PRO   A N   1 
ATOM   1420 C CA  . PRO   A 1 241 ? 10.756 5.700   3.247   1.00 42.64  ? 786  PRO   A CA  1 
ATOM   1421 C C   . PRO   A 1 241 ? 10.639 5.938   4.742   1.00 44.55  ? 786  PRO   A C   1 
ATOM   1422 O O   . PRO   A 1 241 ? 11.646 5.880   5.434   1.00 41.62  ? 786  PRO   A O   1 
ATOM   1423 C CB  . PRO   A 1 241 ? 12.189 5.334   2.898   1.00 40.23  ? 786  PRO   A CB  1 
ATOM   1424 C CG  . PRO   A 1 241 ? 12.854 6.636   2.624   1.00 40.89  ? 786  PRO   A CG  1 
ATOM   1425 C CD  . PRO   A 1 241 ? 11.815 7.483   1.958   1.00 41.24  ? 786  PRO   A CD  1 
ATOM   1426 N N   . VAL   A 1 242 ? 9.431  6.137   5.247   1.00 42.11  ? 787  VAL   A N   1 
ATOM   1427 C CA  . VAL   A 1 242 ? 9.244  6.494   6.656   1.00 47.76  ? 787  VAL   A CA  1 
ATOM   1428 C C   . VAL   A 1 242 ? 9.872  5.566   7.695   1.00 45.73  ? 787  VAL   A C   1 
ATOM   1429 O O   . VAL   A 1 242 ? 10.523 6.040   8.618   1.00 47.35  ? 787  VAL   A O   1 
ATOM   1430 C CB  . VAL   A 1 242 ? 7.740  6.632   6.970   1.00 44.43  ? 787  VAL   A CB  1 
ATOM   1431 C CG1 . VAL   A 1 242 ? 7.532  7.092   8.402   1.00 50.02  ? 787  VAL   A CG1 1 
ATOM   1432 C CG2 . VAL   A 1 242 ? 7.081  7.592   5.995   1.00 42.10  ? 787  VAL   A CG2 1 
ATOM   1433 N N   . LYS   A 1 243 ? 9.677  4.264   7.571   1.00 42.45  ? 788  LYS   A N   1 
ATOM   1434 C CA  . LYS   A 1 243 ? 10.181 3.353   8.594   1.00 45.23  ? 788  LYS   A CA  1 
ATOM   1435 C C   . LYS   A 1 243 ? 11.693 3.373   8.701   1.00 41.60  ? 788  LYS   A C   1 
ATOM   1436 O O   . LYS   A 1 243 ? 12.259 2.740   9.580   1.00 47.06  ? 788  LYS   A O   1 
ATOM   1437 C CB  . LYS   A 1 243 ? 9.673  1.935   8.340   1.00 41.68  ? 788  LYS   A CB  1 
ATOM   1438 C CG  . LYS   A 1 243 ? 8.219  1.736   8.721   1.00 46.53  ? 788  LYS   A CG  1 
ATOM   1439 C CD  . LYS   A 1 243 ? 7.836  0.268   8.703   1.00 46.94  ? 788  LYS   A CD  1 
ATOM   1440 C CE  . LYS   A 1 243 ? 6.394  0.078   9.135   1.00 44.74  ? 788  LYS   A CE  1 
ATOM   1441 N NZ  . LYS   A 1 243 ? 6.017  -1.360  9.173   1.00 50.19  ? 788  LYS   A NZ  1 
ATOM   1442 N N   . TRP   A 1 244 ? 12.347 4.108   7.817   1.00 46.17  ? 789  TRP   A N   1 
ATOM   1443 C CA  . TRP   A 1 244 ? 13.795 4.214   7.847   1.00 42.80  ? 789  TRP   A CA  1 
ATOM   1444 C C   . TRP   A 1 244 ? 14.196 5.633   8.145   1.00 43.79  ? 789  TRP   A C   1 
ATOM   1445 O O   . TRP   A 1 244 ? 15.375 5.939   8.239   1.00 46.62  ? 789  TRP   A O   1 
ATOM   1446 C CB  . TRP   A 1 244 ? 14.376 3.803   6.503   1.00 40.28  ? 789  TRP   A CB  1 
ATOM   1447 C CG  . TRP   A 1 244 ? 14.378 2.341   6.233   1.00 41.02  ? 789  TRP   A CG  1 
ATOM   1448 C CD1 . TRP   A 1 244 ? 15.423 1.484   6.390   1.00 38.98  ? 789  TRP   A CD1 1 
ATOM   1449 C CD2 . TRP   A 1 244 ? 13.290 1.561   5.736   1.00 39.83  ? 789  TRP   A CD2 1 
ATOM   1450 N NE1 . TRP   A 1 244 ? 15.052 0.215   6.032   1.00 40.30  ? 789  TRP   A NE1 1 
ATOM   1451 C CE2 . TRP   A 1 244 ? 13.745 0.235   5.626   1.00 41.98  ? 789  TRP   A CE2 1 
ATOM   1452 C CE3 . TRP   A 1 244 ? 11.972 1.853   5.379   1.00 38.70  ? 789  TRP   A CE3 1 
ATOM   1453 C CZ2 . TRP   A 1 244 ? 12.931 -0.796  5.174   1.00 40.18  ? 789  TRP   A CZ2 1 
ATOM   1454 C CZ3 . TRP   A 1 244 ? 11.167 0.830   4.932   1.00 40.12  ? 789  TRP   A CZ3 1 
ATOM   1455 C CH2 . TRP   A 1 244 ? 11.648 -0.479  4.833   1.00 43.91  ? 789  TRP   A CH2 1 
ATOM   1456 N N   . MET   A 1 245 ? 13.217 6.509   8.301   1.00 41.68  ? 790  MET   A N   1 
ATOM   1457 C CA  . MET   A 1 245 ? 13.518 7.918   8.497   1.00 45.37  ? 790  MET   A CA  1 
ATOM   1458 C C   . MET   A 1 245 ? 13.551 8.353   9.951   1.00 51.74  ? 790  MET   A C   1 
ATOM   1459 O O   . MET   A 1 245 ? 12.822 7.831   10.786  1.00 43.31  ? 790  MET   A O   1 
ATOM   1460 C CB  . MET   A 1 245 ? 12.516 8.780   7.722   1.00 43.87  ? 790  MET   A CB  1 
ATOM   1461 C CG  . MET   A 1 245 ? 12.529 8.551   6.221   1.00 49.58  ? 790  MET   A CG  1 
ATOM   1462 S SD  . MET   A 1 245 ? 11.566 9.751   5.282   1.00 47.88  ? 790  MET   A SD  1 
ATOM   1463 C CE  . MET   A 1 245 ? 10.025 9.758   6.184   1.00 51.32  ? 790  MET   A CE  1 
ATOM   1464 N N   . ALA   A 1 246 ? 14.398 9.325   10.244  1.00 45.62  ? 791  ALA   A N   1 
ATOM   1465 C CA  . ALA   A 1 246 ? 14.518 9.818   11.600  1.00 47.94  ? 791  ALA   A CA  1 
ATOM   1466 C C   . ALA   A 1 246 ? 13.405 10.782  11.935  1.00 48.32  ? 791  ALA   A C   1 
ATOM   1467 O O   . ALA   A 1 246 ? 12.833 11.412  11.052  1.00 54.65  ? 791  ALA   A O   1 
ATOM   1468 C CB  . ALA   A 1 246 ? 15.867 10.483  11.787  1.00 48.04  ? 791  ALA   A CB  1 
ATOM   1469 N N   . PRO   A 1 247 ? 13.101 10.915  13.225  1.00 52.62  ? 792  PRO   A N   1 
ATOM   1470 C CA  . PRO   A 1 247 ? 11.988 11.774  13.637  1.00 52.80  ? 792  PRO   A CA  1 
ATOM   1471 C C   . PRO   A 1 247 ? 12.111 13.219  13.140  1.00 51.80  ? 792  PRO   A C   1 
ATOM   1472 O O   . PRO   A 1 247 ? 11.114 13.799  12.725  1.00 49.82  ? 792  PRO   A O   1 
ATOM   1473 C CB  . PRO   A 1 247 ? 12.053 11.705  15.170  1.00 49.40  ? 792  PRO   A CB  1 
ATOM   1474 C CG  . PRO   A 1 247 ? 13.366 11.083  15.508  1.00 50.14  ? 792  PRO   A CG  1 
ATOM   1475 C CD  . PRO   A 1 247 ? 13.699 10.196  14.357  1.00 45.94  ? 792  PRO   A CD  1 
ATOM   1476 N N   . GLU   A 1 248 ? 13.308 13.782  13.169  1.00 48.13  ? 793  GLU   A N   1 
ATOM   1477 C CA  . GLU   A 1 248 ? 13.507 15.141  12.703  1.00 51.47  ? 793  GLU   A CA  1 
ATOM   1478 C C   . GLU   A 1 248 ? 13.169 15.262  11.235  1.00 52.80  ? 793  GLU   A C   1 
ATOM   1479 O O   . GLU   A 1 248 ? 12.626 16.270  10.802  1.00 54.56  ? 793  GLU   A O   1 
ATOM   1480 C CB  . GLU   A 1 248 ? 14.948 15.589  12.935  1.00 50.08  ? 793  GLU   A CB  1 
ATOM   1481 C CG  . GLU   A 1 248 ? 16.007 14.806  12.181  1.00 48.33  ? 793  GLU   A CG  1 
ATOM   1482 C CD  . GLU   A 1 248 ? 16.575 13.663  12.991  1.00 53.20  ? 793  GLU   A CD  1 
ATOM   1483 O OE1 . GLU   A 1 248 ? 15.907 13.213  13.943  1.00 53.33  ? 793  GLU   A OE1 1 
ATOM   1484 O OE2 . GLU   A 1 248 ? 17.693 13.214  12.671  1.00 56.26  ? 793  GLU   A OE2 1 
ATOM   1485 N N   . SER   A 1 249 ? 13.499 14.238  10.464  1.00 50.66  ? 794  SER   A N   1 
ATOM   1486 C CA  . SER   A 1 249 ? 13.247 14.275  9.036   1.00 50.43  ? 794  SER   A CA  1 
ATOM   1487 C C   . SER   A 1 249 ? 11.764 14.193  8.738   1.00 48.01  ? 794  SER   A C   1 
ATOM   1488 O O   . SER   A 1 249 ? 11.267 14.881  7.857   1.00 50.64  ? 794  SER   A O   1 
ATOM   1489 C CB  . SER   A 1 249 ? 14.002 13.139  8.360   1.00 52.06  ? 794  SER   A CB  1 
ATOM   1490 O OG  . SER   A 1 249 ? 15.381 13.199  8.668   1.00 51.67  ? 794  SER   A OG  1 
ATOM   1491 N N   . ILE   A 1 250 ? 11.055 13.353  9.472   1.00 43.43  ? 795  ILE   A N   1 
ATOM   1492 C CA  . ILE   A 1 250 ? 9.626  13.185  9.254   1.00 48.56  ? 795  ILE   A CA  1 
ATOM   1493 C C   . ILE   A 1 250 ? 8.818  14.346  9.766   1.00 56.12  ? 795  ILE   A C   1 
ATOM   1494 O O   . ILE   A 1 250 ? 7.949  14.856  9.068   1.00 55.93  ? 795  ILE   A O   1 
ATOM   1495 C CB  . ILE   A 1 250 ? 9.113  11.933  9.979   1.00 50.78  ? 795  ILE   A CB  1 
ATOM   1496 C CG1 . ILE   A 1 250 ? 9.983  10.724  9.630   1.00 50.04  ? 795  ILE   A CG1 1 
ATOM   1497 C CG2 . ILE   A 1 250 ? 7.656  11.675  9.633   1.00 53.56  ? 795  ILE   A CG2 1 
ATOM   1498 C CD1 . ILE   A 1 250 ? 9.589  9.462   10.361  1.00 53.67  ? 795  ILE   A CD1 1 
ATOM   1499 N N   . PHE   A 1 251 ? 9.101  14.774  10.985  1.00 55.71  ? 796  PHE   A N   1 
ATOM   1500 C CA  . PHE   A 1 251 ? 8.315  15.833  11.593  1.00 55.97  ? 796  PHE   A CA  1 
ATOM   1501 C C   . PHE   A 1 251 ? 8.800  17.244  11.285  1.00 55.50  ? 796  PHE   A C   1 
ATOM   1502 O O   . PHE   A 1 251 ? 8.017  18.183  11.325  1.00 57.31  ? 796  PHE   A O   1 
ATOM   1503 C CB  . PHE   A 1 251 ? 8.296  15.637  13.111  1.00 56.66  ? 796  PHE   A CB  1 
ATOM   1504 C CG  . PHE   A 1 251 ? 7.847  14.274  13.550  1.00 59.27  ? 796  PHE   A CG  1 
ATOM   1505 C CD1 . PHE   A 1 251 ? 6.702  13.704  13.029  1.00 61.99  ? 796  PHE   A CD1 1 
ATOM   1506 C CD2 . PHE   A 1 251 ? 8.559  13.576  14.508  1.00 55.50  ? 796  PHE   A CD2 1 
ATOM   1507 C CE1 . PHE   A 1 251 ? 6.286  12.454  13.441  1.00 59.05  ? 796  PHE   A CE1 1 
ATOM   1508 C CE2 . PHE   A 1 251 ? 8.149  12.327  14.926  1.00 52.08  ? 796  PHE   A CE2 1 
ATOM   1509 C CZ  . PHE   A 1 251 ? 7.010  11.765  14.392  1.00 52.48  ? 796  PHE   A CZ  1 
ATOM   1510 N N   . ASP   A 1 252 ? 10.079 17.409  10.990  1.00 54.38  ? 797  ASP   A N   1 
ATOM   1511 C CA  . ASP   A 1 252 ? 10.607 18.754  10.794  1.00 58.20  ? 797  ASP   A CA  1 
ATOM   1512 C C   . ASP   A 1 252 ? 11.352 18.925  9.485   1.00 56.45  ? 797  ASP   A C   1 
ATOM   1513 O O   . ASP   A 1 252 ? 12.010 19.937  9.278   1.00 57.50  ? 797  ASP   A O   1 
ATOM   1514 C CB  . ASP   A 1 252 ? 11.513 19.121  11.968  1.00 52.14  ? 797  ASP   A CB  1 
ATOM   1515 C CG  . ASP   A 1 252 ? 10.771 19.157  13.282  1.00 58.10  ? 797  ASP   A CG  1 
ATOM   1516 O OD1 . ASP   A 1 252 ? 9.590  19.557  13.286  1.00 59.42  ? 797  ASP   A OD1 1 
ATOM   1517 O OD2 . ASP   A 1 252 ? 11.372 18.795  14.312  1.00 62.10  ? 797  ASP   A OD2 1 
ATOM   1518 N N   . ASN   A 1 253 ? 11.250 17.947  8.601   1.00 55.77  ? 798  ASN   A N   1 
ATOM   1519 C CA  . ASN   A 1 253 ? 11.883 18.042  7.291   1.00 58.22  ? 798  ASN   A CA  1 
ATOM   1520 C C   . ASN   A 1 253 ? 13.351 18.391  7.380   1.00 57.51  ? 798  ASN   A C   1 
ATOM   1521 O O   . ASN   A 1 253 ? 13.863 19.128  6.548   1.00 58.40  ? 798  ASN   A O   1 
ATOM   1522 C CB  . ASN   A 1 253 ? 11.157 19.070  6.427   1.00 54.57  ? 798  ASN   A CB  1 
ATOM   1523 C CG  . ASN   A 1 253 ? 9.668  18.815  6.347   1.00 68.83  ? 798  ASN   A CG  1 
ATOM   1524 O OD1 . ASN   A 1 253 ? 9.138  17.939  7.027   1.00 76.88  ? 798  ASN   A OD1 1 
ATOM   1525 N ND2 . ASN   A 1 253 ? 8.983  19.585  5.514   1.00 72.60  ? 798  ASN   A ND2 1 
ATOM   1526 N N   . LEU   A 1 254 ? 14.035 17.854  8.376   1.00 48.96  ? 799  LEU   A N   1 
ATOM   1527 C CA  . LEU   A 1 254 ? 15.459 18.107  8.515   1.00 51.08  ? 799  LEU   A CA  1 
ATOM   1528 C C   . LEU   A 1 254 ? 16.247 16.866  8.182   1.00 50.65  ? 799  LEU   A C   1 
ATOM   1529 O O   . LEU   A 1 254 ? 16.028 15.814  8.766   1.00 55.66  ? 799  LEU   A O   1 
ATOM   1530 C CB  . LEU   A 1 254 ? 15.785 18.567  9.931   1.00 56.57  ? 799  LEU   A CB  1 
ATOM   1531 C CG  . LEU   A 1 254 ? 14.950 19.727  10.464  1.00 58.11  ? 799  LEU   A CG  1 
ATOM   1532 C CD1 . LEU   A 1 254 ? 15.290 20.000  11.919  1.00 53.44  ? 799  LEU   A CD1 1 
ATOM   1533 C CD2 . LEU   A 1 254 ? 15.161 20.968  9.613   1.00 61.36  ? 799  LEU   A CD2 1 
ATOM   1534 N N   . TYR   A 1 255 ? 17.169 16.984  7.239   1.00 51.88  ? 800  TYR   A N   1 
ATOM   1535 C CA  . TYR   A 1 255 ? 17.943 15.833  6.816   1.00 46.83  ? 800  TYR   A CA  1 
ATOM   1536 C C   . TYR   A 1 255 ? 19.419 16.110  6.914   1.00 47.10  ? 800  TYR   A C   1 
ATOM   1537 O O   . TYR   A 1 255 ? 19.908 17.082  6.357   1.00 47.91  ? 800  TYR   A O   1 
ATOM   1538 C CB  . TYR   A 1 255 ? 17.589 15.451  5.382   1.00 43.91  ? 800  TYR   A CB  1 
ATOM   1539 C CG  . TYR   A 1 255 ? 16.164 15.010  5.171   1.00 45.79  ? 800  TYR   A CG  1 
ATOM   1540 C CD1 . TYR   A 1 255 ? 15.154 15.937  4.974   1.00 46.18  ? 800  TYR   A CD1 1 
ATOM   1541 C CD2 . TYR   A 1 255 ? 15.832 13.666  5.147   1.00 45.63  ? 800  TYR   A CD2 1 
ATOM   1542 C CE1 . TYR   A 1 255 ? 13.850 15.538  4.773   1.00 49.15  ? 800  TYR   A CE1 1 
ATOM   1543 C CE2 . TYR   A 1 255 ? 14.531 13.257  4.944   1.00 52.10  ? 800  TYR   A CE2 1 
ATOM   1544 C CZ  . TYR   A 1 255 ? 13.545 14.199  4.759   1.00 53.33  ? 800  TYR   A CZ  1 
ATOM   1545 O OH  . TYR   A 1 255 ? 12.248 13.797  4.557   1.00 58.05  ? 800  TYR   A OH  1 
ATOM   1546 N N   . THR   A 1 256 ? 20.136 15.247  7.616   1.00 49.33  ? 801  THR   A N   1 
ATOM   1547 C CA  . THR   A 1 256 ? 21.570 15.405  7.765   1.00 48.52  ? 801  THR   A CA  1 
ATOM   1548 C C   . THR   A 1 256 ? 22.236 14.058  7.676   1.00 47.32  ? 801  THR   A C   1 
ATOM   1549 O O   . THR   A 1 256 ? 21.582 13.057  7.433   1.00 48.93  ? 801  THR   A O   1 
ATOM   1550 C CB  . THR   A 1 256 ? 21.936 16.019  9.127   1.00 51.60  ? 801  THR   A CB  1 
ATOM   1551 O OG1 . THR   A 1 256 ? 21.747 15.044  10.160  1.00 50.58  ? 801  THR   A OG1 1 
ATOM   1552 C CG2 . THR   A 1 256 ? 21.077 17.239  9.420   1.00 42.55  ? 801  THR   A CG2 1 
ATOM   1553 N N   . THR   A 1 257 ? 23.543 14.023  7.868   1.00 48.34  ? 802  THR   A N   1 
ATOM   1554 C CA  . THR   A 1 257 ? 24.240 12.754  7.886   1.00 50.89  ? 802  THR   A CA  1 
ATOM   1555 C C   . THR   A 1 257 ? 23.734 11.967  9.063   1.00 54.35  ? 802  THR   A C   1 
ATOM   1556 O O   . THR   A 1 257 ? 23.643 10.747  9.009   1.00 56.87  ? 802  THR   A O   1 
ATOM   1557 C CB  . THR   A 1 257 ? 25.751 12.947  8.014   1.00 52.22  ? 802  THR   A CB  1 
ATOM   1558 O OG1 . THR   A 1 257 ? 26.245 13.596  6.839   1.00 68.58  ? 802  THR   A OG1 1 
ATOM   1559 C CG2 . THR   A 1 257 ? 26.447 11.611  8.164   1.00 52.08  ? 802  THR   A CG2 1 
ATOM   1560 N N   . LEU   A 1 258 ? 23.392 12.665  10.132  1.00 44.42  ? 803  LEU   A N   1 
ATOM   1561 C CA  . LEU   A 1 258 ? 22.910 12.001  11.331  1.00 54.34  ? 803  LEU   A CA  1 
ATOM   1562 C C   . LEU   A 1 258 ? 21.568 11.346  11.101  1.00 54.28  ? 803  LEU   A C   1 
ATOM   1563 O O   . LEU   A 1 258 ? 21.254 10.336  11.725  1.00 52.10  ? 803  LEU   A O   1 
ATOM   1564 C CB  . LEU   A 1 258 ? 22.842 12.997  12.480  1.00 60.88  ? 803  LEU   A CB  1 
ATOM   1565 C CG  . LEU   A 1 258 ? 24.211 13.556  12.863  1.00 55.84  ? 803  LEU   A CG  1 
ATOM   1566 C CD1 . LEU   A 1 258 ? 24.088 14.727  13.821  1.00 64.88  ? 803  LEU   A CD1 1 
ATOM   1567 C CD2 . LEU   A 1 258 ? 25.085 12.457  13.445  1.00 56.75  ? 803  LEU   A CD2 1 
ATOM   1568 N N   . SER   A 1 259 ? 20.772 11.896  10.201  1.00 52.43  ? 804  SER   A N   1 
ATOM   1569 C CA  . SER   A 1 259 ? 19.508 11.263  9.876   1.00 47.36  ? 804  SER   A CA  1 
ATOM   1570 C C   . SER   A 1 259 ? 19.794 9.951   9.173   1.00 48.39  ? 804  SER   A C   1 
ATOM   1571 O O   . SER   A 1 259 ? 19.081 8.971   9.363   1.00 53.99  ? 804  SER   A O   1 
ATOM   1572 C CB  . SER   A 1 259 ? 18.645 12.183  9.017   1.00 48.19  ? 804  SER   A CB  1 
ATOM   1573 O OG  . SER   A 1 259 ? 19.258 12.465  7.776   1.00 62.38  ? 804  SER   A OG  1 
ATOM   1574 N N   . ASP   A 1 260 ? 20.848 9.921   8.373   1.00 49.76  ? 805  ASP   A N   1 
ATOM   1575 C CA  . ASP   A 1 260 ? 21.227 8.697   7.684   1.00 53.71  ? 805  ASP   A CA  1 
ATOM   1576 C C   . ASP   A 1 260 ? 21.743 7.675   8.672   1.00 50.11  ? 805  ASP   A C   1 
ATOM   1577 O O   . ASP   A 1 260 ? 21.643 6.478   8.438   1.00 53.15  ? 805  ASP   A O   1 
ATOM   1578 C CB  . ASP   A 1 260 ? 22.278 8.989   6.614   1.00 56.53  ? 805  ASP   A CB  1 
ATOM   1579 C CG  . ASP   A 1 260 ? 21.701 9.685   5.403   1.00 57.04  ? 805  ASP   A CG  1 
ATOM   1580 O OD1 . ASP   A 1 260 ? 20.467 9.858   5.343   1.00 57.92  ? 805  ASP   A OD1 1 
ATOM   1581 O OD2 . ASP   A 1 260 ? 22.484 10.052  4.505   1.00 59.80  ? 805  ASP   A OD2 1 
ATOM   1582 N N   . VAL   A 1 261 ? 22.304 8.146   9.774   1.00 51.74  ? 806  VAL   A N   1 
ATOM   1583 C CA  . VAL   A 1 261 ? 22.789 7.248   10.804  1.00 53.14  ? 806  VAL   A CA  1 
ATOM   1584 C C   . VAL   A 1 261 ? 21.621 6.482   11.398  1.00 51.18  ? 806  VAL   A C   1 
ATOM   1585 O O   . VAL   A 1 261 ? 21.744 5.302   11.714  1.00 47.93  ? 806  VAL   A O   1 
ATOM   1586 C CB  . VAL   A 1 261 ? 23.539 8.025   11.892  1.00 50.33  ? 806  VAL   A CB  1 
ATOM   1587 C CG1 . VAL   A 1 261 ? 23.953 7.099   13.023  1.00 57.68  ? 806  VAL   A CG1 1 
ATOM   1588 C CG2 . VAL   A 1 261 ? 24.749 8.727   11.301  1.00 46.21  ? 806  VAL   A CG2 1 
ATOM   1589 N N   . TRP   A 1 262 ? 20.481 7.136   11.539  1.00 47.58  ? 807  TRP   A N   1 
ATOM   1590 C CA  . TRP   A 1 262 ? 19.298 6.455   12.020  1.00 47.21  ? 807  TRP   A CA  1 
ATOM   1591 C C   . TRP   A 1 262 ? 18.924 5.357   11.055  1.00 48.52  ? 807  TRP   A C   1 
ATOM   1592 O O   . TRP   A 1 262 ? 18.584 4.254   11.465  1.00 45.22  ? 807  TRP   A O   1 
ATOM   1593 C CB  . TRP   A 1 262 ? 18.160 7.456   12.143  1.00 49.61  ? 807  TRP   A CB  1 
ATOM   1594 C CG  . TRP   A 1 262 ? 16.826 6.881   12.473  1.00 49.79  ? 807  TRP   A CG  1 
ATOM   1595 C CD1 . TRP   A 1 262 ? 16.003 6.189   11.640  1.00 46.08  ? 807  TRP   A CD1 1 
ATOM   1596 C CD2 . TRP   A 1 262 ? 16.138 6.984   13.721  1.00 50.35  ? 807  TRP   A CD2 1 
ATOM   1597 N NE1 . TRP   A 1 262 ? 14.852 5.838   12.296  1.00 49.05  ? 807  TRP   A NE1 1 
ATOM   1598 C CE2 . TRP   A 1 262 ? 14.911 6.316   13.577  1.00 46.22  ? 807  TRP   A CE2 1 
ATOM   1599 C CE3 . TRP   A 1 262 ? 16.446 7.571   14.950  1.00 47.94  ? 807  TRP   A CE3 1 
ATOM   1600 C CZ2 . TRP   A 1 262 ? 13.992 6.216   14.615  1.00 50.71  ? 807  TRP   A CZ2 1 
ATOM   1601 C CZ3 . TRP   A 1 262 ? 15.534 7.470   15.977  1.00 52.55  ? 807  TRP   A CZ3 1 
ATOM   1602 C CH2 . TRP   A 1 262 ? 14.322 6.798   15.804  1.00 47.79  ? 807  TRP   A CH2 1 
ATOM   1603 N N   . SER   A 1 263 ? 18.994 5.655   9.767   1.00 45.64  ? 808  SER   A N   1 
ATOM   1604 C CA  . SER   A 1 263 ? 18.650 4.675   8.749   1.00 43.37  ? 808  SER   A CA  1 
ATOM   1605 C C   . SER   A 1 263 ? 19.601 3.506   8.797   1.00 42.17  ? 808  SER   A C   1 
ATOM   1606 O O   . SER   A 1 263 ? 19.205 2.377   8.544   1.00 42.75  ? 808  SER   A O   1 
ATOM   1607 C CB  . SER   A 1 263 ? 18.673 5.333   7.378   1.00 46.27  ? 808  SER   A CB  1 
ATOM   1608 O OG  . SER   A 1 263 ? 17.750 6.402   7.314   1.00 50.05  ? 808  SER   A OG  1 
ATOM   1609 N N   . TYR   A 1 264 ? 20.858 3.769   9.114   1.00 44.00  ? 809  TYR   A N   1 
ATOM   1610 C CA  . TYR   A 1 264 ? 21.838 2.706   9.254   1.00 52.40  ? 809  TYR   A CA  1 
ATOM   1611 C C   . TYR   A 1 264 ? 21.418 1.754   10.348  1.00 48.20  ? 809  TYR   A C   1 
ATOM   1612 O O   . TYR   A 1 264 ? 21.559 0.546   10.209  1.00 49.48  ? 809  TYR   A O   1 
ATOM   1613 C CB  . TYR   A 1 264 ? 23.179 3.326   9.593   1.00 54.26  ? 809  TYR   A CB  1 
ATOM   1614 C CG  . TYR   A 1 264 ? 24.337 2.371   9.673   1.00 57.38  ? 809  TYR   A CG  1 
ATOM   1615 C CD1 . TYR   A 1 264 ? 24.924 1.869   8.524   1.00 49.98  ? 809  TYR   A CD1 1 
ATOM   1616 C CD2 . TYR   A 1 264 ? 24.868 2.001   10.897  1.00 49.19  ? 809  TYR   A CD2 1 
ATOM   1617 C CE1 . TYR   A 1 264 ? 25.996 1.006   8.592   1.00 54.25  ? 809  TYR   A CE1 1 
ATOM   1618 C CE2 . TYR   A 1 264 ? 25.939 1.140   10.976  1.00 48.50  ? 809  TYR   A CE2 1 
ATOM   1619 C CZ  . TYR   A 1 264 ? 26.497 0.646   9.820   1.00 61.06  ? 809  TYR   A CZ  1 
ATOM   1620 O OH  . TYR   A 1 264 ? 27.565 -0.209  9.894   1.00 64.07  ? 809  TYR   A OH  1 
ATOM   1621 N N   . GLY   A 1 265 ? 20.887 2.289   11.437  1.00 43.03  ? 810  GLY   A N   1 
ATOM   1622 C CA  . GLY   A 1 265 ? 20.415 1.452   12.519  1.00 48.40  ? 810  GLY   A CA  1 
ATOM   1623 C C   . GLY   A 1 265 ? 19.269 0.594   12.068  1.00 48.61  ? 810  GLY   A C   1 
ATOM   1624 O O   . GLY   A 1 265 ? 19.211 -0.586  12.393  1.00 48.16  ? 810  GLY   A O   1 
ATOM   1625 N N   . ILE   A 1 266 ? 18.350 1.178   11.318  1.00 44.44  ? 811  ILE   A N   1 
ATOM   1626 C CA  . ILE   A 1 266 ? 17.240 0.416   10.791  1.00 45.58  ? 811  ILE   A CA  1 
ATOM   1627 C C   . ILE   A 1 266 ? 17.780 -0.634  9.844   1.00 44.19  ? 811  ILE   A C   1 
ATOM   1628 O O   . ILE   A 1 266 ? 17.266 -1.744  9.781   1.00 47.30  ? 811  ILE   A O   1 
ATOM   1629 C CB  . ILE   A 1 266 ? 16.233 1.324   10.070  1.00 41.42  ? 811  ILE   A CB  1 
ATOM   1630 C CG1 . ILE   A 1 266 ? 15.780 2.456   10.990  1.00 46.57  ? 811  ILE   A CG1 1 
ATOM   1631 C CG2 . ILE   A 1 266 ? 15.036 0.519   9.593   1.00 43.56  ? 811  ILE   A CG2 1 
ATOM   1632 C CD1 . ILE   A 1 266 ? 14.995 1.986   12.193  1.00 45.19  ? 811  ILE   A CD1 1 
ATOM   1633 N N   . LEU   A 1 267 ? 18.836 -0.295  9.121   1.00 43.74  ? 812  LEU   A N   1 
ATOM   1634 C CA  . LEU   A 1 267 ? 19.446 -1.246  8.211   1.00 51.93  ? 812  LEU   A CA  1 
ATOM   1635 C C   . LEU   A 1 267 ? 20.046 -2.407  8.966   1.00 49.86  ? 812  LEU   A C   1 
ATOM   1636 O O   . LEU   A 1 267 ? 19.919 -3.551  8.552   1.00 51.21  ? 812  LEU   A O   1 
ATOM   1637 C CB  . LEU   A 1 267 ? 20.528 -0.568  7.380   1.00 50.56  ? 812  LEU   A CB  1 
ATOM   1638 C CG  . LEU   A 1 267 ? 21.485 -1.477  6.615   1.00 46.70  ? 812  LEU   A CG  1 
ATOM   1639 C CD1 . LEU   A 1 267 ? 20.747 -2.222  5.517   1.00 54.88  ? 812  LEU   A CD1 1 
ATOM   1640 C CD2 . LEU   A 1 267 ? 22.628 -0.660  6.038   1.00 47.36  ? 812  LEU   A CD2 1 
ATOM   1641 N N   . LEU   A 1 268 ? 20.708 -2.114  10.073  1.00 43.63  ? 813  LEU   A N   1 
ATOM   1642 C CA  . LEU   A 1 268 ? 21.321 -3.164  10.859  1.00 50.31  ? 813  LEU   A CA  1 
ATOM   1643 C C   . LEU   A 1 268 ? 20.265 -4.121  11.372  1.00 50.00  ? 813  LEU   A C   1 
ATOM   1644 O O   . LEU   A 1 268 ? 20.476 -5.325  11.405  1.00 52.52  ? 813  LEU   A O   1 
ATOM   1645 C CB  . LEU   A 1 268 ? 22.115 -2.571  12.012  1.00 49.75  ? 813  LEU   A CB  1 
ATOM   1646 C CG  . LEU   A 1 268 ? 23.291 -1.687  11.620  1.00 54.72  ? 813  LEU   A CG  1 
ATOM   1647 C CD1 . LEU   A 1 268 ? 24.194 -1.488  12.824  1.00 53.01  ? 813  LEU   A CD1 1 
ATOM   1648 C CD2 . LEU   A 1 268 ? 24.056 -2.338  10.481  1.00 57.29  ? 813  LEU   A CD2 1 
ATOM   1649 N N   . TRP   A 1 269 ? 19.122 -3.592  11.765  1.00 46.88  ? 814  TRP   A N   1 
ATOM   1650 C CA  . TRP   A 1 269 ? 18.042 -4.440  12.222  1.00 49.71  ? 814  TRP   A CA  1 
ATOM   1651 C C   . TRP   A 1 269 ? 17.587 -5.320  11.084  1.00 47.61  ? 814  TRP   A C   1 
ATOM   1652 O O   . TRP   A 1 269 ? 17.244 -6.473  11.291  1.00 48.05  ? 814  TRP   A O   1 
ATOM   1653 C CB  . TRP   A 1 269 ? 16.885 -3.594  12.746  1.00 43.91  ? 814  TRP   A CB  1 
ATOM   1654 C CG  . TRP   A 1 269 ? 15.766 -4.389  13.311  1.00 41.69  ? 814  TRP   A CG  1 
ATOM   1655 C CD1 . TRP   A 1 269 ? 15.585 -4.733  14.614  1.00 50.77  ? 814  TRP   A CD1 1 
ATOM   1656 C CD2 . TRP   A 1 269 ? 14.661 -4.940  12.593  1.00 44.34  ? 814  TRP   A CD2 1 
ATOM   1657 N NE1 . TRP   A 1 269 ? 14.436 -5.467  14.754  1.00 51.37  ? 814  TRP   A NE1 1 
ATOM   1658 C CE2 . TRP   A 1 269 ? 13.850 -5.609  13.525  1.00 40.89  ? 814  TRP   A CE2 1 
ATOM   1659 C CE3 . TRP   A 1 269 ? 14.280 -4.933  11.250  1.00 47.82  ? 814  TRP   A CE3 1 
ATOM   1660 C CZ2 . TRP   A 1 269 ? 12.682 -6.263  13.158  1.00 41.10  ? 814  TRP   A CZ2 1 
ATOM   1661 C CZ3 . TRP   A 1 269 ? 13.124 -5.583  10.890  1.00 46.88  ? 814  TRP   A CZ3 1 
ATOM   1662 C CH2 . TRP   A 1 269 ? 12.337 -6.239  11.838  1.00 47.16  ? 814  TRP   A CH2 1 
ATOM   1663 N N   . GLU   A 1 270 ? 17.574 -4.776  9.880   1.00 47.59  ? 815  GLU   A N   1 
ATOM   1664 C CA  . GLU   A 1 270 ? 17.207 -5.566  8.721   1.00 50.90  ? 815  GLU   A CA  1 
ATOM   1665 C C   . GLU   A 1 270 ? 18.208 -6.679  8.498   1.00 50.72  ? 815  GLU   A C   1 
ATOM   1666 O O   . GLU   A 1 270 ? 17.833 -7.815  8.229   1.00 53.60  ? 815  GLU   A O   1 
ATOM   1667 C CB  . GLU   A 1 270 ? 17.151 -4.688  7.479   1.00 51.53  ? 815  GLU   A CB  1 
ATOM   1668 C CG  . GLU   A 1 270 ? 16.015 -3.687  7.435   1.00 49.34  ? 815  GLU   A CG  1 
ATOM   1669 C CD  . GLU   A 1 270 ? 16.076 -2.823  6.193   1.00 54.60  ? 815  GLU   A CD  1 
ATOM   1670 O OE1 . GLU   A 1 270 ? 17.006 -1.999  6.085   1.00 55.34  ? 815  GLU   A OE1 1 
ATOM   1671 O OE2 . GLU   A 1 270 ? 15.198 -2.969  5.321   1.00 51.62  ? 815  GLU   A OE2 1 
ATOM   1672 N N   . ILE   A 1 271 ? 19.486 -6.357  8.609   1.00 42.32  ? 816  ILE   A N   1 
ATOM   1673 C CA  . ILE   A 1 271 ? 20.516 -7.346  8.378   1.00 48.88  ? 816  ILE   A CA  1 
ATOM   1674 C C   . ILE   A 1 271 ? 20.492 -8.436  9.423   1.00 57.40  ? 816  ILE   A C   1 
ATOM   1675 O O   . ILE   A 1 271 ? 20.547 -9.615  9.090   1.00 58.00  ? 816  ILE   A O   1 
ATOM   1676 C CB  . ILE   A 1 271 ? 21.904 -6.700  8.385   1.00 50.36  ? 816  ILE   A CB  1 
ATOM   1677 C CG1 . ILE   A 1 271 ? 22.055 -5.757  7.192   1.00 52.32  ? 816  ILE   A CG1 1 
ATOM   1678 C CG2 . ILE   A 1 271 ? 22.987 -7.764  8.358   1.00 58.06  ? 816  ILE   A CG2 1 
ATOM   1679 C CD1 . ILE   A 1 271 ? 23.392 -5.053  7.139   1.00 47.96  ? 816  ILE   A CD1 1 
ATOM   1680 N N   . PHE   A 1 272 ? 20.387 -8.060  10.688  1.00 53.47  ? 817  PHE   A N   1 
ATOM   1681 C CA  . PHE   A 1 272 ? 20.450 -9.055  11.749  1.00 52.86  ? 817  PHE   A CA  1 
ATOM   1682 C C   . PHE   A 1 272 ? 19.096 -9.680  12.010  1.00 52.54  ? 817  PHE   A C   1 
ATOM   1683 O O   . PHE   A 1 272 ? 18.940 -10.456 12.944  1.00 57.70  ? 817  PHE   A O   1 
ATOM   1684 C CB  . PHE   A 1 272 ? 21.074 -8.448  12.998  1.00 55.51  ? 817  PHE   A CB  1 
ATOM   1685 C CG  . PHE   A 1 272 ? 22.531 -8.143  12.838  1.00 56.91  ? 817  PHE   A CG  1 
ATOM   1686 C CD1 . PHE   A 1 272 ? 23.482 -9.113  13.086  1.00 59.36  ? 817  PHE   A CD1 1 
ATOM   1687 C CD2 . PHE   A 1 272 ? 22.949 -6.898  12.409  1.00 56.44  ? 817  PHE   A CD2 1 
ATOM   1688 C CE1 . PHE   A 1 272 ? 24.826 -8.843  12.927  1.00 62.26  ? 817  PHE   A CE1 1 
ATOM   1689 C CE2 . PHE   A 1 272 ? 24.290 -6.620  12.248  1.00 58.10  ? 817  PHE   A CE2 1 
ATOM   1690 C CZ  . PHE   A 1 272 ? 25.231 -7.594  12.508  1.00 59.09  ? 817  PHE   A CZ  1 
ATOM   1691 N N   . SER   A 1 273 ? 18.113 -9.339  11.195  1.00 48.34  ? 818  SER   A N   1 
ATOM   1692 C CA  . SER   A 1 273 ? 16.825 -9.980  11.294  1.00 45.66  ? 818  SER   A CA  1 
ATOM   1693 C C   . SER   A 1 273 ? 16.791 -10.845 10.071  1.00 57.17  ? 818  SER   A C   1 
ATOM   1694 O O   . SER   A 1 273 ? 15.791 -11.494 9.789   1.00 56.98  ? 818  SER   A O   1 
ATOM   1695 C CB  . SER   A 1 273 ? 15.707 -8.964  11.253  1.00 45.55  ? 818  SER   A CB  1 
ATOM   1696 O OG  . SER   A 1 273 ? 15.748 -8.212  10.057  1.00 60.71  ? 818  SER   A OG  1 
ATOM   1697 N N   . LEU   A 1 274 ? 17.889 -10.844 9.323   1.00 57.08  ? 819  LEU   A N   1 
ATOM   1698 C CA  . LEU   A 1 274 ? 17.980 -11.632 8.099   1.00 59.07  ? 819  LEU   A CA  1 
ATOM   1699 C C   . LEU   A 1 274 ? 16.860 -11.306 7.131   1.00 58.54  ? 819  LEU   A C   1 
ATOM   1700 O O   . LEU   A 1 274 ? 16.135 -12.192 6.697   1.00 55.43  ? 819  LEU   A O   1 
ATOM   1701 C CB  . LEU   A 1 274 ? 18.011 -13.123 8.422   1.00 67.97  ? 819  LEU   A CB  1 
ATOM   1702 C CG  . LEU   A 1 274 ? 19.098 -13.551 9.406   1.00 67.60  ? 819  LEU   A CG  1 
ATOM   1703 C CD1 . LEU   A 1 274 ? 18.984 -15.034 9.716   1.00 71.09  ? 819  LEU   A CD1 1 
ATOM   1704 C CD2 . LEU   A 1 274 ? 20.477 -13.221 8.859   1.00 68.28  ? 819  LEU   A CD2 1 
ATOM   1705 N N   . GLY   A 1 275 ? 16.719 -10.031 6.791   1.00 58.09  ? 820  GLY   A N   1 
ATOM   1706 C CA  . GLY   A 1 275 ? 15.722 -9.635  5.814   1.00 57.29  ? 820  GLY   A CA  1 
ATOM   1707 C C   . GLY   A 1 275 ? 14.370 -9.254  6.356   1.00 55.47  ? 820  GLY   A C   1 
ATOM   1708 O O   . GLY   A 1 275 ? 13.389 -9.242  5.624   1.00 55.90  ? 820  GLY   A O   1 
ATOM   1709 N N   . GLY   A 1 276 ? 14.309 -8.932  7.635   1.00 53.87  ? 821  GLY   A N   1 
ATOM   1710 C CA  . GLY   A 1 276 ? 13.048 -8.584  8.245   1.00 43.06  ? 821  GLY   A CA  1 
ATOM   1711 C C   . GLY   A 1 276 ? 12.549 -7.211  7.889   1.00 51.59  ? 821  GLY   A C   1 
ATOM   1712 O O   . GLY   A 1 276 ? 13.339 -6.307  7.646   1.00 51.90  ? 821  GLY   A O   1 
ATOM   1713 N N   . THR   A 1 277 ? 11.236 -7.049  7.855   1.00 52.12  ? 822  THR   A N   1 
ATOM   1714 C CA  . THR   A 1 277 ? 10.656 -5.751  7.584   1.00 49.08  ? 822  THR   A CA  1 
ATOM   1715 C C   . THR   A 1 277 ? 10.602 -4.942  8.860   1.00 51.75  ? 822  THR   A C   1 
ATOM   1716 O O   . THR   A 1 277 ? 10.089 -5.406  9.868   1.00 51.92  ? 822  THR   A O   1 
ATOM   1717 C CB  . THR   A 1 277 ? 9.235  -5.884  7.023   1.00 51.02  ? 822  THR   A CB  1 
ATOM   1718 O OG1 . THR   A 1 277 ? 9.279  -6.564  5.764   1.00 59.36  ? 822  THR   A OG1 1 
ATOM   1719 C CG2 . THR   A 1 277 ? 8.611  -4.513  6.830   1.00 56.04  ? 822  THR   A CG2 1 
ATOM   1720 N N   . PRO   A 1 278 ? 11.134 -3.720  8.822   1.00 51.63  ? 823  PRO   A N   1 
ATOM   1721 C CA  . PRO   A 1 278 ? 11.153 -2.878  10.016  1.00 47.43  ? 823  PRO   A CA  1 
ATOM   1722 C C   . PRO   A 1 278 ? 9.760  -2.672  10.590  1.00 47.26  ? 823  PRO   A C   1 
ATOM   1723 O O   . PRO   A 1 278 ? 8.796  -2.594  9.840   1.00 49.52  ? 823  PRO   A O   1 
ATOM   1724 C CB  . PRO   A 1 278 ? 11.723 -1.567  9.493   1.00 44.82  ? 823  PRO   A CB  1 
ATOM   1725 C CG  . PRO   A 1 278 ? 12.591 -1.972  8.356   1.00 49.46  ? 823  PRO   A CG  1 
ATOM   1726 C CD  . PRO   A 1 278 ? 11.864 -3.106  7.701   1.00 50.78  ? 823  PRO   A CD  1 
ATOM   1727 N N   . TYR   A 1 279 ? 9.657  -2.600  11.910  1.00 48.10  ? 824  TYR   A N   1 
ATOM   1728 C CA  . TYR   A 1 279 ? 8.368  -2.422  12.564  1.00 47.65  ? 824  TYR   A CA  1 
ATOM   1729 C C   . TYR   A 1 279 ? 7.392  -3.443  12.037  1.00 49.40  ? 824  TYR   A C   1 
ATOM   1730 O O   . TYR   A 1 279 ? 6.384  -3.093  11.441  1.00 55.07  ? 824  TYR   A O   1 
ATOM   1731 C CB  . TYR   A 1 279 ? 7.874  -0.994  12.365  1.00 46.28  ? 824  TYR   A CB  1 
ATOM   1732 C CG  . TYR   A 1 279 ? 8.883  0.032   12.810  1.00 53.52  ? 824  TYR   A CG  1 
ATOM   1733 C CD1 . TYR   A 1 279 ? 8.936  0.453   14.129  1.00 44.53  ? 824  TYR   A CD1 1 
ATOM   1734 C CD2 . TYR   A 1 279 ? 9.798  0.565   11.916  1.00 49.22  ? 824  TYR   A CD2 1 
ATOM   1735 C CE1 . TYR   A 1 279 ? 9.865  1.384   14.542  1.00 47.99  ? 824  TYR   A CE1 1 
ATOM   1736 C CE2 . TYR   A 1 279 ? 10.731 1.495   12.321  1.00 40.57  ? 824  TYR   A CE2 1 
ATOM   1737 C CZ  . TYR   A 1 279 ? 10.759 1.900   13.635  1.00 45.34  ? 824  TYR   A CZ  1 
ATOM   1738 O OH  . TYR   A 1 279 ? 11.683 2.827   14.044  1.00 51.40  ? 824  TYR   A OH  1 
ATOM   1739 N N   . PRO   A 1 280 ? 7.673  -4.723  12.285  1.00 52.60  ? 825  PRO   A N   1 
ATOM   1740 C CA  . PRO   A 1 280 ? 6.834  -5.786  11.721  1.00 48.14  ? 825  PRO   A CA  1 
ATOM   1741 C C   . PRO   A 1 280 ? 5.401  -5.773  12.202  1.00 52.20  ? 825  PRO   A C   1 
ATOM   1742 O O   . PRO   A 1 280 ? 5.157  -5.922  13.389  1.00 56.19  ? 825  PRO   A O   1 
ATOM   1743 C CB  . PRO   A 1 280 ? 7.520  -7.058  12.213  1.00 46.99  ? 825  PRO   A CB  1 
ATOM   1744 C CG  . PRO   A 1 280 ? 8.331  -6.646  13.391  1.00 51.58  ? 825  PRO   A CG  1 
ATOM   1745 C CD  . PRO   A 1 280 ? 8.778  -5.253  13.097  1.00 50.50  ? 825  PRO   A CD  1 
ATOM   1746 N N   . GLY   A 1 281 ? 4.461  -5.627  11.281  1.00 45.70  ? 826  GLY   A N   1 
ATOM   1747 C CA  . GLY   A 1 281 ? 3.060  -5.633  11.638  1.00 46.40  ? 826  GLY   A CA  1 
ATOM   1748 C C   . GLY   A 1 281 ? 2.490  -4.256  11.847  1.00 55.78  ? 826  GLY   A C   1 
ATOM   1749 O O   . GLY   A 1 281 ? 1.279  -4.070  11.819  1.00 56.62  ? 826  GLY   A O   1 
ATOM   1750 N N   . MET   A 1 282 ? 3.360  -3.281  12.050  1.00 59.49  ? 827  MET   A N   1 
ATOM   1751 C CA  . MET   A 1 282 ? 2.902  -1.930  12.304  1.00 57.20  ? 827  MET   A CA  1 
ATOM   1752 C C   . MET   A 1 282 ? 2.639  -1.185  11.016  1.00 58.99  ? 827  MET   A C   1 
ATOM   1753 O O   . MET   A 1 282 ? 3.467  -1.188  10.114  1.00 58.74  ? 827  MET   A O   1 
ATOM   1754 C CB  . MET   A 1 282 ? 3.928  -1.173  13.143  1.00 54.59  ? 827  MET   A CB  1 
ATOM   1755 C CG  . MET   A 1 282 ? 3.506  -0.942  14.579  1.00 55.84  ? 827  MET   A CG  1 
ATOM   1756 S SD  . MET   A 1 282 ? 4.816  -0.168  15.536  1.00 68.19  ? 827  MET   A SD  1 
ATOM   1757 C CE  . MET   A 1 282 ? 6.086  -1.418  15.411  1.00 53.41  ? 827  MET   A CE  1 
ATOM   1758 N N   . MET   A 1 283 ? 1.484  -0.546  10.926  1.00 60.88  ? 828  MET   A N   1 
ATOM   1759 C CA  . MET   A 1 283 ? 1.160  0.238   9.754   1.00 52.64  ? 828  MET   A CA  1 
ATOM   1760 C C   . MET   A 1 283 ? 1.443  1.688   10.065  1.00 58.95  ? 828  MET   A C   1 
ATOM   1761 O O   . MET   A 1 283 ? 1.162  2.152   11.163  1.00 59.28  ? 828  MET   A O   1 
ATOM   1762 C CB  . MET   A 1 283 ? -0.306 0.056   9.391   1.00 57.53  ? 828  MET   A CB  1 
ATOM   1763 C CG  . MET   A 1 283 ? -0.746 -1.396  9.329   1.00 70.34  ? 828  MET   A CG  1 
ATOM   1764 S SD  . MET   A 1 283 ? 0.155  -2.353  8.096   1.00 96.06  ? 828  MET   A SD  1 
ATOM   1765 C CE  . MET   A 1 283 ? -0.301 -4.020  8.563   1.00 67.53  ? 828  MET   A CE  1 
ATOM   1766 N N   . VAL   A 1 284 ? 2.004  2.412   9.108   1.00 56.21  ? 829  VAL   A N   1 
ATOM   1767 C CA  . VAL   A 1 284 ? 2.360  3.797   9.356   1.00 50.90  ? 829  VAL   A CA  1 
ATOM   1768 C C   . VAL   A 1 284 ? 1.105  4.630   9.454   1.00 51.12  ? 829  VAL   A C   1 
ATOM   1769 O O   . VAL   A 1 284 ? 0.385  4.795   8.478   1.00 58.81  ? 829  VAL   A O   1 
ATOM   1770 C CB  . VAL   A 1 284 ? 3.289  4.355   8.270   1.00 53.53  ? 829  VAL   A CB  1 
ATOM   1771 C CG1 . VAL   A 1 284 ? 3.597  5.816   8.547   1.00 55.05  ? 829  VAL   A CG1 1 
ATOM   1772 C CG2 . VAL   A 1 284 ? 4.572  3.544   8.210   1.00 50.74  ? 829  VAL   A CG2 1 
ATOM   1773 N N   . ASP   A 1 285 ? 0.843  5.156   10.638  1.00 55.68  ? 830  ASP   A N   1 
ATOM   1774 C CA  . ASP   A 1 285 ? -0.345 5.946   10.853  1.00 52.78  ? 830  ASP   A CA  1 
ATOM   1775 C C   . ASP   A 1 285 ? -0.107 6.894   11.997  1.00 53.78  ? 830  ASP   A C   1 
ATOM   1776 O O   . ASP   A 1 285 ? 1.007  7.011   12.490  1.00 53.51  ? 830  ASP   A O   1 
ATOM   1777 C CB  . ASP   A 1 285 ? -1.520 5.037   11.173  1.00 55.58  ? 830  ASP   A CB  1 
ATOM   1778 C CG  . ASP   A 1 285 ? -1.264 4.146   12.373  1.00 62.95  ? 830  ASP   A CG  1 
ATOM   1779 O OD1 . ASP   A 1 285 ? -0.178 4.240   12.979  1.00 62.54  ? 830  ASP   A OD1 1 
ATOM   1780 O OD2 . ASP   A 1 285 ? -2.157 3.346   12.711  1.00 67.01  ? 830  ASP   A OD2 1 
ATOM   1781 N N   . SER   A 1 286 ? -1.160 7.555   12.444  1.00 53.67  ? 831  SER   A N   1 
ATOM   1782 C CA  . SER   A 1 286 ? -1.041 8.502   13.536  1.00 57.94  ? 831  SER   A CA  1 
ATOM   1783 C C   . SER   A 1 286 ? -0.374 7.881   14.745  1.00 58.34  ? 831  SER   A C   1 
ATOM   1784 O O   . SER   A 1 286 ? 0.470  8.505   15.381  1.00 57.58  ? 831  SER   A O   1 
ATOM   1785 C CB  . SER   A 1 286 ? -2.427 8.995   13.925  1.00 53.70  ? 831  SER   A CB  1 
ATOM   1786 O OG  . SER   A 1 286 ? -3.114 9.516   12.806  1.00 72.29  ? 831  SER   A OG  1 
ATOM   1787 N N   . THR   A 1 287 ? -0.743 6.650   15.063  1.00 57.38  ? 832  THR   A N   1 
ATOM   1788 C CA  . THR   A 1 287 ? -0.196 5.987   16.234  1.00 59.67  ? 832  THR   A CA  1 
ATOM   1789 C C   . THR   A 1 287 ? 1.287  5.711   16.073  1.00 54.46  ? 832  THR   A C   1 
ATOM   1790 O O   . THR   A 1 287 ? 2.057  5.873   17.011  1.00 53.03  ? 832  THR   A O   1 
ATOM   1791 C CB  . THR   A 1 287 ? -0.950 4.676   16.511  1.00 57.69  ? 832  THR   A CB  1 
ATOM   1792 O OG1 . THR   A 1 287 ? -2.340 4.958   16.699  1.00 51.58  ? 832  THR   A OG1 1 
ATOM   1793 C CG2 . THR   A 1 287 ? -0.406 3.999   17.752  1.00 61.28  ? 832  THR   A CG2 1 
ATOM   1794 N N   . PHE   A 1 288 ? 1.692  5.311   14.881  1.00 52.14  ? 833  PHE   A N   1 
ATOM   1795 C CA  . PHE   A 1 288 ? 3.091  5.027   14.630  1.00 48.87  ? 833  PHE   A CA  1 
ATOM   1796 C C   . PHE   A 1 288 ? 3.929  6.243   14.931  1.00 44.74  ? 833  PHE   A C   1 
ATOM   1797 O O   . PHE   A 1 288 ? 4.950  6.151   15.603  1.00 44.48  ? 833  PHE   A O   1 
ATOM   1798 C CB  . PHE   A 1 288 ? 3.269  4.615   13.172  1.00 49.35  ? 833  PHE   A CB  1 
ATOM   1799 C CG  . PHE   A 1 288 ? 4.695  4.443   12.748  1.00 49.92  ? 833  PHE   A CG  1 
ATOM   1800 C CD1 . PHE   A 1 288 ? 5.402  3.309   13.096  1.00 45.15  ? 833  PHE   A CD1 1 
ATOM   1801 C CD2 . PHE   A 1 288 ? 5.318  5.403   11.974  1.00 46.93  ? 833  PHE   A CD2 1 
ATOM   1802 C CE1 . PHE   A 1 288 ? 6.712  3.143   12.697  1.00 45.54  ? 833  PHE   A CE1 1 
ATOM   1803 C CE2 . PHE   A 1 288 ? 6.627  5.245   11.570  1.00 50.38  ? 833  PHE   A CE2 1 
ATOM   1804 C CZ  . PHE   A 1 288 ? 7.325  4.112   11.930  1.00 50.37  ? 833  PHE   A CZ  1 
ATOM   1805 N N   . TYR   A 1 289 ? 3.491  7.388   14.441  1.00 45.53  ? 834  TYR   A N   1 
ATOM   1806 C CA  . TYR   A 1 289 ? 4.246  8.608   14.641  1.00 50.49  ? 834  TYR   A CA  1 
ATOM   1807 C C   . TYR   A 1 289 ? 4.273  9.013   16.101  1.00 46.72  ? 834  TYR   A C   1 
ATOM   1808 O O   . TYR   A 1 289 ? 5.304  9.435   16.611  1.00 48.12  ? 834  TYR   A O   1 
ATOM   1809 C CB  . TYR   A 1 289 ? 3.651  9.730   13.799  1.00 49.69  ? 834  TYR   A CB  1 
ATOM   1810 C CG  . TYR   A 1 289 ? 3.729  9.515   12.310  1.00 52.32  ? 834  TYR   A CG  1 
ATOM   1811 C CD1 . TYR   A 1 289 ? 4.951  9.438   11.665  1.00 50.67  ? 834  TYR   A CD1 1 
ATOM   1812 C CD2 . TYR   A 1 289 ? 2.578  9.418   11.544  1.00 48.17  ? 834  TYR   A CD2 1 
ATOM   1813 C CE1 . TYR   A 1 289 ? 5.026  9.251   10.301  1.00 46.81  ? 834  TYR   A CE1 1 
ATOM   1814 C CE2 . TYR   A 1 289 ? 2.643  9.231   10.181  1.00 40.17  ? 834  TYR   A CE2 1 
ATOM   1815 C CZ  . TYR   A 1 289 ? 3.870  9.149   9.566   1.00 47.40  ? 834  TYR   A CZ  1 
ATOM   1816 O OH  . TYR   A 1 289 ? 3.941  8.965   8.207   1.00 61.52  ? 834  TYR   A OH  1 
ATOM   1817 N N   . ASN   A 1 290 ? 3.144  8.879   16.778  1.00 48.72  ? 835  ASN   A N   1 
ATOM   1818 C CA  . ASN   A 1 290 ? 3.074  9.238   18.182  1.00 52.50  ? 835  ASN   A CA  1 
ATOM   1819 C C   . ASN   A 1 290 ? 4.017  8.387   18.991  1.00 47.87  ? 835  ASN   A C   1 
ATOM   1820 O O   . ASN   A 1 290 ? 4.684  8.873   19.894  1.00 51.14  ? 835  ASN   A O   1 
ATOM   1821 C CB  . ASN   A 1 290 ? 1.652  9.068   18.695  1.00 50.26  ? 835  ASN   A CB  1 
ATOM   1822 C CG  . ASN   A 1 290 ? 0.785  10.276  18.419  1.00 64.84  ? 835  ASN   A CG  1 
ATOM   1823 O OD1 . ASN   A 1 290 ? 1.281  11.395  18.311  1.00 66.76  ? 835  ASN   A OD1 1 
ATOM   1824 N ND2 . ASN   A 1 290 ? -0.520 10.058  18.317  1.00 64.66  ? 835  ASN   A ND2 1 
ATOM   1825 N N   . LYS   A 1 291 ? 4.081  7.112   18.659  1.00 48.90  ? 836  LYS   A N   1 
ATOM   1826 C CA  . LYS   A 1 291 ? 4.948  6.209   19.381  1.00 47.96  ? 836  LYS   A CA  1 
ATOM   1827 C C   . LYS   A 1 291 ? 6.407  6.565   19.181  1.00 49.75  ? 836  LYS   A C   1 
ATOM   1828 O O   . LYS   A 1 291 ? 7.165  6.643   20.137  1.00 50.49  ? 836  LYS   A O   1 
ATOM   1829 C CB  . LYS   A 1 291 ? 4.696  4.774   18.930  1.00 49.94  ? 836  LYS   A CB  1 
ATOM   1830 C CG  . LYS   A 1 291 ? 3.352  4.202   19.333  1.00 49.43  ? 836  LYS   A CG  1 
ATOM   1831 C CD  . LYS   A 1 291 ? 3.243  2.759   18.874  1.00 50.34  ? 836  LYS   A CD  1 
ATOM   1832 C CE  . LYS   A 1 291 ? 1.971  2.105   19.379  1.00 55.42  ? 836  LYS   A CE  1 
ATOM   1833 N NZ  . LYS   A 1 291 ? 1.869  0.692   18.926  1.00 56.95  ? 836  LYS   A NZ  1 
ATOM   1834 N N   . ILE   A 1 292 ? 6.805  6.778   17.938  1.00 47.15  ? 837  ILE   A N   1 
ATOM   1835 C CA  . ILE   A 1 292 ? 8.195  7.081   17.662  1.00 49.50  ? 837  ILE   A CA  1 
ATOM   1836 C C   . ILE   A 1 292 ? 8.539  8.405   18.302  1.00 53.62  ? 837  ILE   A C   1 
ATOM   1837 O O   . ILE   A 1 292 ? 9.641  8.588   18.805  1.00 56.67  ? 837  ILE   A O   1 
ATOM   1838 C CB  . ILE   A 1 292 ? 8.492  7.105   16.154  1.00 54.24  ? 837  ILE   A CB  1 
ATOM   1839 C CG1 . ILE   A 1 292 ? 8.309  5.708   15.567  1.00 50.45  ? 837  ILE   A CG1 1 
ATOM   1840 C CG2 . ILE   A 1 292 ? 9.903  7.600   15.892  1.00 52.81  ? 837  ILE   A CG2 1 
ATOM   1841 C CD1 . ILE   A 1 292 ? 9.155  5.451   14.344  1.00 57.99  ? 837  ILE   A CD1 1 
ATOM   1842 N N   . LYS   A 1 293 ? 7.597  9.332   18.295  1.00 51.79  ? 838  LYS   A N   1 
ATOM   1843 C CA  . LYS   A 1 293 ? 7.823  10.601  18.953  1.00 53.72  ? 838  LYS   A CA  1 
ATOM   1844 C C   . LYS   A 1 293 ? 8.010  10.370  20.434  1.00 51.04  ? 838  LYS   A C   1 
ATOM   1845 O O   . LYS   A 1 293 ? 8.896  10.947  21.048  1.00 53.17  ? 838  LYS   A O   1 
ATOM   1846 C CB  . LYS   A 1 293 ? 6.641  11.528  18.713  1.00 50.72  ? 838  LYS   A CB  1 
ATOM   1847 C CG  . LYS   A 1 293 ? 6.790  12.903  19.335  1.00 58.24  ? 838  LYS   A CG  1 
ATOM   1848 C CD  . LYS   A 1 293 ? 5.512  13.710  19.188  1.00 68.29  ? 838  LYS   A CD  1 
ATOM   1849 C CE  . LYS   A 1 293 ? 5.640  15.071  19.849  1.00 72.83  ? 838  LYS   A CE  1 
ATOM   1850 N NZ  . LYS   A 1 293 ? 4.369  15.840  19.778  1.00 71.09  ? 838  LYS   A NZ  1 
ATOM   1851 N N   . SER   A 1 294 ? 7.180  9.512   21.004  1.00 48.87  ? 839  SER   A N   1 
ATOM   1852 C CA  . SER   A 1 294 ? 7.274  9.214   22.419  1.00 44.35  ? 839  SER   A CA  1 
ATOM   1853 C C   . SER   A 1 294 ? 8.530  8.422   22.729  1.00 50.13  ? 839  SER   A C   1 
ATOM   1854 O O   . SER   A 1 294 ? 8.915  8.311   23.886  1.00 60.68  ? 839  SER   A O   1 
ATOM   1855 C CB  . SER   A 1 294 ? 6.041  8.445   22.873  1.00 47.46  ? 839  SER   A CB  1 
ATOM   1856 O OG  . SER   A 1 294 ? 4.858  9.161   22.578  1.00 54.11  ? 839  SER   A OG  1 
ATOM   1857 N N   . GLY   A 1 295 ? 9.173  7.868   21.710  1.00 50.24  ? 840  GLY   A N   1 
ATOM   1858 C CA  . GLY   A 1 295 ? 10.425 7.169   21.930  1.00 49.02  ? 840  GLY   A CA  1 
ATOM   1859 C C   . GLY   A 1 295 ? 10.472 5.687   21.645  1.00 47.33  ? 840  GLY   A C   1 
ATOM   1860 O O   . GLY   A 1 295 ? 11.431 5.020   22.014  1.00 46.30  ? 840  GLY   A O   1 
ATOM   1861 N N   . TYR   A 1 296 ? 9.445  5.169   20.990  1.00 43.08  ? 841  TYR   A N   1 
ATOM   1862 C CA  . TYR   A 1 296 ? 9.406  3.755   20.675  1.00 42.77  ? 841  TYR   A CA  1 
ATOM   1863 C C   . TYR   A 1 296 ? 10.525 3.345   19.754  1.00 49.05  ? 841  TYR   A C   1 
ATOM   1864 O O   . TYR   A 1 296 ? 10.777 3.996   18.749  1.00 52.03  ? 841  TYR   A O   1 
ATOM   1865 C CB  . TYR   A 1 296 ? 8.082  3.366   20.032  1.00 48.78  ? 841  TYR   A CB  1 
ATOM   1866 C CG  . TYR   A 1 296 ? 8.057  1.924   19.595  1.00 54.56  ? 841  TYR   A CG  1 
ATOM   1867 C CD1 . TYR   A 1 296 ? 7.895  0.905   20.520  1.00 55.59  ? 841  TYR   A CD1 1 
ATOM   1868 C CD2 . TYR   A 1 296 ? 8.216  1.578   18.262  1.00 48.34  ? 841  TYR   A CD2 1 
ATOM   1869 C CE1 . TYR   A 1 296 ? 7.881  -0.417  20.130  1.00 51.10  ? 841  TYR   A CE1 1 
ATOM   1870 C CE2 . TYR   A 1 296 ? 8.203  0.258   17.864  1.00 47.12  ? 841  TYR   A CE2 1 
ATOM   1871 C CZ  . TYR   A 1 296 ? 8.035  -0.734  18.803  1.00 50.64  ? 841  TYR   A CZ  1 
ATOM   1872 O OH  . TYR   A 1 296 ? 8.020  -2.051  18.418  1.00 52.14  ? 841  TYR   A OH  1 
ATOM   1873 N N   . ARG   A 1 297 ? 11.191 2.255   20.090  1.00 42.27  ? 842  ARG   A N   1 
ATOM   1874 C CA  . ARG   A 1 297 ? 12.251 1.748   19.257  1.00 48.85  ? 842  ARG   A CA  1 
ATOM   1875 C C   . ARG   A 1 297 ? 12.047 0.258   19.116  1.00 53.43  ? 842  ARG   A C   1 
ATOM   1876 O O   . ARG   A 1 297 ? 11.474 -0.375  19.995  1.00 53.70  ? 842  ARG   A O   1 
ATOM   1877 C CB  . ARG   A 1 297 ? 13.609 2.027   19.884  1.00 46.18  ? 842  ARG   A CB  1 
ATOM   1878 C CG  . ARG   A 1 297 ? 13.933 3.486   20.143  1.00 46.20  ? 842  ARG   A CG  1 
ATOM   1879 C CD  . ARG   A 1 297 ? 14.146 4.248   18.851  1.00 53.29  ? 842  ARG   A CD  1 
ATOM   1880 N NE  . ARG   A 1 297 ? 13.088 5.224   18.644  1.00 56.84  ? 842  ARG   A NE  1 
ATOM   1881 C CZ  . ARG   A 1 297 ? 13.149 6.485   19.048  1.00 51.72  ? 842  ARG   A CZ  1 
ATOM   1882 N NH1 . ARG   A 1 297 ? 14.228 6.935   19.669  1.00 46.70  ? 842  ARG   A NH1 1 
ATOM   1883 N NH2 . ARG   A 1 297 ? 12.132 7.299   18.820  1.00 55.50  ? 842  ARG   A NH2 1 
ATOM   1884 N N   . MET   A 1 298 ? 12.507 -0.311  18.012  1.00 50.95  ? 843  MET   A N   1 
ATOM   1885 C CA  . MET   A 1 298 ? 12.380 -1.742  17.796  1.00 50.47  ? 843  MET   A CA  1 
ATOM   1886 C C   . MET   A 1 298 ? 13.241 -2.519  18.767  1.00 52.43  ? 843  MET   A C   1 
ATOM   1887 O O   . MET   A 1 298 ? 14.255 -2.021  19.243  1.00 51.17  ? 843  MET   A O   1 
ATOM   1888 C CB  . MET   A 1 298 ? 12.768 -2.110  16.364  1.00 48.24  ? 843  MET   A CB  1 
ATOM   1889 C CG  . MET   A 1 298 ? 11.717 -1.802  15.317  1.00 48.42  ? 843  MET   A CG  1 
ATOM   1890 S SD  . MET   A 1 298 ? 12.212 -2.398  13.691  1.00 54.25  ? 843  MET   A SD  1 
ATOM   1891 C CE  . MET   A 1 298 ? 13.675 -1.413  13.399  1.00 42.13  ? 843  MET   A CE  1 
ATOM   1892 N N   . ALA   A 1 299 ? 12.842 -3.748  19.055  1.00 54.86  ? 844  ALA   A N   1 
ATOM   1893 C CA  . ALA   A 1 299 ? 13.601 -4.582  19.973  1.00 54.43  ? 844  ALA   A CA  1 
ATOM   1894 C C   . ALA   A 1 299 ? 14.727 -5.305  19.270  1.00 57.10  ? 844  ALA   A C   1 
ATOM   1895 O O   . ALA   A 1 299 ? 14.813 -5.291  18.048  1.00 59.51  ? 844  ALA   A O   1 
ATOM   1896 C CB  . ALA   A 1 299 ? 12.685 -5.580  20.644  1.00 40.54  ? 844  ALA   A CB  1 
ATOM   1897 N N   . LYS   A 1 300 ? 15.588 -5.949  20.043  1.00 59.86  ? 845  LYS   A N   1 
ATOM   1898 C CA  . LYS   A 1 300 ? 16.724 -6.638  19.460  1.00 59.99  ? 845  LYS   A CA  1 
ATOM   1899 C C   . LYS   A 1 300 ? 16.285 -7.683  18.469  1.00 61.86  ? 845  LYS   A C   1 
ATOM   1900 O O   . LYS   A 1 300 ? 15.371 -8.450  18.735  1.00 63.12  ? 845  LYS   A O   1 
ATOM   1901 C CB  . LYS   A 1 300 ? 17.587 -7.294  20.536  1.00 65.04  ? 845  LYS   A CB  1 
ATOM   1902 C CG  . LYS   A 1 300 ? 18.741 -8.099  19.964  1.00 66.71  ? 845  LYS   A CG  1 
ATOM   1903 C CD  . LYS   A 1 300 ? 19.523 -8.829  21.040  1.00 68.54  ? 845  LYS   A CD  1 
ATOM   1904 C CE  . LYS   A 1 300 ? 20.289 -7.859  21.921  1.00 82.68  ? 845  LYS   A CE  1 
ATOM   1905 N NZ  . LYS   A 1 300 ? 21.137 -8.576  22.913  1.00 91.94  ? 845  LYS   A NZ  1 
ATOM   1906 N N   . PRO   A 1 301 ? 16.935 -7.707  17.308  1.00 62.86  ? 846  PRO   A N   1 
ATOM   1907 C CA  . PRO   A 1 301 ? 16.620 -8.755  16.341  1.00 60.49  ? 846  PRO   A CA  1 
ATOM   1908 C C   . PRO   A 1 301 ? 17.113 -10.105 16.830  1.00 65.55  ? 846  PRO   A C   1 
ATOM   1909 O O   . PRO   A 1 301 ? 18.025 -10.153 17.646  1.00 61.11  ? 846  PRO   A O   1 
ATOM   1910 C CB  . PRO   A 1 301 ? 17.361 -8.312  15.079  1.00 62.58  ? 846  PRO   A CB  1 
ATOM   1911 C CG  . PRO   A 1 301 ? 18.352 -7.296  15.517  1.00 63.94  ? 846  PRO   A CG  1 
ATOM   1912 C CD  . PRO   A 1 301 ? 17.802 -6.659  16.751  1.00 61.77  ? 846  PRO   A CD  1 
ATOM   1913 N N   . ASP   A 1 302 ? 16.534 -11.186 16.331  1.00 70.03  ? 847  ASP   A N   1 
ATOM   1914 C CA  . ASP   A 1 302 ? 16.872 -12.527 16.817  1.00 70.80  ? 847  ASP   A CA  1 
ATOM   1915 C C   . ASP   A 1 302 ? 18.323 -12.953 16.643  1.00 66.99  ? 847  ASP   A C   1 
ATOM   1916 O O   . ASP   A 1 302 ? 18.867 -13.638 17.500  1.00 69.53  ? 847  ASP   A O   1 
ATOM   1917 C CB  . ASP   A 1 302 ? 15.956 -13.549 16.142  1.00 64.87  ? 847  ASP   A CB  1 
ATOM   1918 C CG  . ASP   A 1 302 ? 14.492 -13.242 16.357  1.00 71.29  ? 847  ASP   A CG  1 
ATOM   1919 O OD1 . ASP   A 1 302 ? 14.189 -12.302 17.119  1.00 70.82  ? 847  ASP   A OD1 1 
ATOM   1920 O OD2 . ASP   A 1 302 ? 13.642 -13.939 15.767  1.00 73.85  ? 847  ASP   A OD2 1 
ATOM   1921 N N   . HIS   A 1 303 ? 18.952 -12.561 15.548  1.00 63.75  ? 848  HIS   A N   1 
ATOM   1922 C CA  . HIS   A 1 303 ? 20.316 -12.998 15.288  1.00 59.93  ? 848  HIS   A CA  1 
ATOM   1923 C C   . HIS   A 1 303 ? 21.310 -11.878 15.504  1.00 58.46  ? 848  HIS   A C   1 
ATOM   1924 O O   . HIS   A 1 303 ? 22.315 -11.791 14.812  1.00 65.72  ? 848  HIS   A O   1 
ATOM   1925 C CB  . HIS   A 1 303 ? 20.412 -13.549 13.873  1.00 62.70  ? 848  HIS   A CB  1 
ATOM   1926 C CG  . HIS   A 1 303 ? 19.390 -14.597 13.574  1.00 62.66  ? 848  HIS   A CG  1 
ATOM   1927 N ND1 . HIS   A 1 303 ? 18.167 -14.303 13.014  1.00 72.47  ? 848  HIS   A ND1 1 
ATOM   1928 C CD2 . HIS   A 1 303 ? 19.401 -15.935 13.775  1.00 65.64  ? 848  HIS   A CD2 1 
ATOM   1929 C CE1 . HIS   A 1 303 ? 17.471 -15.417 12.874  1.00 76.02  ? 848  HIS   A CE1 1 
ATOM   1930 N NE2 . HIS   A 1 303 ? 18.198 -16.421 13.327  1.00 75.85  ? 848  HIS   A NE2 1 
ATOM   1931 N N   . ALA   A 1 304 ? 21.041 -11.032 16.484  1.00 65.46  ? 849  ALA   A N   1 
ATOM   1932 C CA  . ALA   A 1 304 ? 21.915 -9.904  16.756  1.00 65.40  ? 849  ALA   A CA  1 
ATOM   1933 C C   . ALA   A 1 304 ? 22.590 -9.985  18.111  1.00 74.12  ? 849  ALA   A C   1 
ATOM   1934 O O   . ALA   A 1 304 ? 21.967 -10.368 19.096  1.00 73.29  ? 849  ALA   A O   1 
ATOM   1935 C CB  . ALA   A 1 304 ? 21.123 -8.619  16.666  1.00 65.65  ? 849  ALA   A CB  1 
ATOM   1936 N N   . THR   A 1 305 ? 23.859 -9.608  18.164  1.00 74.97  ? 850  THR   A N   1 
ATOM   1937 C CA  . THR   A 1 305 ? 24.584 -9.613  19.415  1.00 72.42  ? 850  THR   A CA  1 
ATOM   1938 C C   . THR   A 1 305 ? 24.221 -8.383  20.206  1.00 75.70  ? 850  THR   A C   1 
ATOM   1939 O O   . THR   A 1 305 ? 23.655 -7.439  19.667  1.00 78.60  ? 850  THR   A O   1 
ATOM   1940 C CB  . THR   A 1 305 ? 26.092 -9.587  19.170  1.00 76.72  ? 850  THR   A CB  1 
ATOM   1941 O OG1 . THR   A 1 305 ? 26.504 -8.248  18.870  1.00 80.84  ? 850  THR   A OG1 1 
ATOM   1942 C CG2 . THR   A 1 305 ? 26.454 -10.498 18.009  1.00 74.72  ? 850  THR   A CG2 1 
ATOM   1943 N N   . SER   A 1 306 ? 24.550 -8.380  21.489  1.00 72.76  ? 851  SER   A N   1 
ATOM   1944 C CA  . SER   A 1 306 ? 24.267 -7.222  22.319  1.00 74.85  ? 851  SER   A CA  1 
ATOM   1945 C C   . SER   A 1 306 ? 25.072 -6.046  21.826  1.00 76.77  ? 851  SER   A C   1 
ATOM   1946 O O   . SER   A 1 306 ? 24.615 -4.907  21.866  1.00 77.83  ? 851  SER   A O   1 
ATOM   1947 C CB  . SER   A 1 306 ? 24.599 -7.509  23.777  1.00 71.84  ? 851  SER   A CB  1 
ATOM   1948 O OG  . SER   A 1 306 ? 24.300 -6.393  24.594  1.00 79.80  ? 851  SER   A OG  1 
ATOM   1949 N N   . GLU   A 1 307 ? 26.279 -6.319  21.357  1.00 75.13  ? 852  GLU   A N   1 
ATOM   1950 C CA  . GLU   A 1 307 ? 27.141 -5.253  20.881  1.00 76.12  ? 852  GLU   A CA  1 
ATOM   1951 C C   . GLU   A 1 307 ? 26.556 -4.546  19.658  1.00 77.63  ? 852  GLU   A C   1 
ATOM   1952 O O   . GLU   A 1 307 ? 26.569 -3.322  19.582  1.00 77.44  ? 852  GLU   A O   1 
ATOM   1953 C CB  . GLU   A 1 307 ? 28.529 -5.809  20.577  1.00 73.54  ? 852  GLU   A CB  1 
ATOM   1954 C CG  . GLU   A 1 307 ? 29.294 -6.252  21.811  1.00 79.75  ? 852  GLU   A CG  1 
ATOM   1955 C CD  . GLU   A 1 307 ? 30.484 -7.130  21.480  1.00 88.30  ? 852  GLU   A CD  1 
ATOM   1956 O OE1 . GLU   A 1 307 ? 30.409 -7.883  20.488  1.00 89.94  ? 852  GLU   A OE1 1 
ATOM   1957 O OE2 . GLU   A 1 307 ? 31.489 -7.077  22.218  1.00 87.38  ? 852  GLU   A OE2 1 
ATOM   1958 N N   . VAL   A 1 308 ? 26.023 -5.310  18.715  1.00 70.43  ? 853  VAL   A N   1 
ATOM   1959 C CA  . VAL   A 1 308 ? 25.451 -4.705  17.524  1.00 70.93  ? 853  VAL   A CA  1 
ATOM   1960 C C   . VAL   A 1 308 ? 24.140 -3.986  17.836  1.00 68.61  ? 853  VAL   A C   1 
ATOM   1961 O O   . VAL   A 1 308 ? 23.862 -2.935  17.273  1.00 69.74  ? 853  VAL   A O   1 
ATOM   1962 C CB  . VAL   A 1 308 ? 25.237 -5.737  16.395  1.00 72.91  ? 853  VAL   A CB  1 
ATOM   1963 C CG1 . VAL   A 1 308 ? 26.539 -6.454  16.084  1.00 72.10  ? 853  VAL   A CG1 1 
ATOM   1964 C CG2 . VAL   A 1 308 ? 24.148 -6.730  16.755  1.00 77.38  ? 853  VAL   A CG2 1 
ATOM   1965 N N   . TYR   A 1 309 ? 23.337 -4.543  18.733  1.00 69.33  ? 854  TYR   A N   1 
ATOM   1966 C CA  . TYR   A 1 309 ? 22.091 -3.899  19.109  1.00 67.27  ? 854  TYR   A CA  1 
ATOM   1967 C C   . TYR   A 1 309 ? 22.393 -2.570  19.753  1.00 64.12  ? 854  TYR   A C   1 
ATOM   1968 O O   . TYR   A 1 309 ? 21.649 -1.612  19.589  1.00 65.96  ? 854  TYR   A O   1 
ATOM   1969 C CB  . TYR   A 1 309 ? 21.285 -4.773  20.057  1.00 60.16  ? 854  TYR   A CB  1 
ATOM   1970 C CG  . TYR   A 1 309 ? 19.956 -4.176  20.434  1.00 63.09  ? 854  TYR   A CG  1 
ATOM   1971 C CD1 . TYR   A 1 309 ? 18.977 -3.967  19.478  1.00 67.15  ? 854  TYR   A CD1 1 
ATOM   1972 C CD2 . TYR   A 1 309 ? 19.679 -3.823  21.744  1.00 61.24  ? 854  TYR   A CD2 1 
ATOM   1973 C CE1 . TYR   A 1 309 ? 17.757 -3.419  19.815  1.00 64.60  ? 854  TYR   A CE1 1 
ATOM   1974 C CE2 . TYR   A 1 309 ? 18.462 -3.276  22.091  1.00 58.95  ? 854  TYR   A CE2 1 
ATOM   1975 C CZ  . TYR   A 1 309 ? 17.505 -3.078  21.123  1.00 61.05  ? 854  TYR   A CZ  1 
ATOM   1976 O OH  . TYR   A 1 309 ? 16.290 -2.533  21.462  1.00 62.89  ? 854  TYR   A OH  1 
ATOM   1977 N N   . GLU   A 1 310 ? 23.490 -2.507  20.486  1.00 60.53  ? 855  GLU   A N   1 
ATOM   1978 C CA  . GLU   A 1 310 ? 23.879 -1.264  21.110  1.00 62.83  ? 855  GLU   A CA  1 
ATOM   1979 C C   . GLU   A 1 310 ? 24.168 -0.242  20.044  1.00 66.47  ? 855  GLU   A C   1 
ATOM   1980 O O   . GLU   A 1 310 ? 23.809 0.923   20.181  1.00 61.70  ? 855  GLU   A O   1 
ATOM   1981 C CB  . GLU   A 1 310 ? 25.104 -1.475  21.983  1.00 70.04  ? 855  GLU   A CB  1 
ATOM   1982 C CG  . GLU   A 1 310 ? 25.678 -0.192  22.560  1.00 75.38  ? 855  GLU   A CG  1 
ATOM   1983 C CD  . GLU   A 1 310 ? 24.690 0.549   23.439  1.00 78.94  ? 855  GLU   A CD  1 
ATOM   1984 O OE1 . GLU   A 1 310 ? 23.743 -0.088  23.945  1.00 76.38  ? 855  GLU   A OE1 1 
ATOM   1985 O OE2 . GLU   A 1 310 ? 24.859 1.771   23.620  1.00 77.08  ? 855  GLU   A OE2 1 
ATOM   1986 N N   . ILE   A 1 311 ? 24.813 -0.675  18.972  1.00 65.72  ? 856  ILE   A N   1 
ATOM   1987 C CA  . ILE   A 1 311 ? 25.075 0.226   17.869  1.00 62.48  ? 856  ILE   A CA  1 
ATOM   1988 C C   . ILE   A 1 311 ? 23.765 0.790   17.364  1.00 58.92  ? 856  ILE   A C   1 
ATOM   1989 O O   . ILE   A 1 311 ? 23.631 1.995   17.186  1.00 59.60  ? 856  ILE   A O   1 
ATOM   1990 C CB  . ILE   A 1 311 ? 25.790 -0.498  16.727  1.00 62.76  ? 856  ILE   A CB  1 
ATOM   1991 C CG1 . ILE   A 1 311 ? 27.163 -0.981  17.193  1.00 58.28  ? 856  ILE   A CG1 1 
ATOM   1992 C CG2 . ILE   A 1 311 ? 25.921 0.413   15.519  1.00 60.35  ? 856  ILE   A CG2 1 
ATOM   1993 C CD1 . ILE   A 1 311 ? 27.883 -1.841  16.181  1.00 65.27  ? 856  ILE   A CD1 1 
ATOM   1994 N N   . MET   A 1 312 ? 22.784 -0.076  17.167  1.00 53.80  ? 857  MET   A N   1 
ATOM   1995 C CA  . MET   A 1 312 ? 21.487 0.374   16.702  1.00 54.82  ? 857  MET   A CA  1 
ATOM   1996 C C   . MET   A 1 312 ? 20.892 1.372   17.667  1.00 59.56  ? 857  MET   A C   1 
ATOM   1997 O O   . MET   A 1 312 ? 20.332 2.381   17.252  1.00 58.58  ? 857  MET   A O   1 
ATOM   1998 C CB  . MET   A 1 312 ? 20.524 -0.801  16.558  1.00 54.53  ? 857  MET   A CB  1 
ATOM   1999 C CG  . MET   A 1 312 ? 21.017 -1.951  15.705  1.00 51.39  ? 857  MET   A CG  1 
ATOM   2000 S SD  . MET   A 1 312 ? 19.753 -3.228  15.584  1.00 54.79  ? 857  MET   A SD  1 
ATOM   2001 C CE  . MET   A 1 312 ? 20.713 -4.590  14.937  1.00 60.56  ? 857  MET   A CE  1 
ATOM   2002 N N   . VAL   A 1 313 ? 20.998 1.094   18.957  1.00 56.98  ? 858  VAL   A N   1 
ATOM   2003 C CA  . VAL   A 1 313 ? 20.395 1.968   19.954  1.00 53.89  ? 858  VAL   A CA  1 
ATOM   2004 C C   . VAL   A 1 313 ? 21.008 3.349   19.897  1.00 54.28  ? 858  VAL   A C   1 
ATOM   2005 O O   . VAL   A 1 313 ? 20.306 4.349   19.972  1.00 56.46  ? 858  VAL   A O   1 
ATOM   2006 C CB  . VAL   A 1 313 ? 20.546 1.391   21.374  1.00 64.06  ? 858  VAL   A CB  1 
ATOM   2007 C CG1 . VAL   A 1 313 ? 20.116 2.408   22.418  1.00 54.45  ? 858  VAL   A CG1 1 
ATOM   2008 C CG2 . VAL   A 1 313 ? 19.745 0.108   21.510  1.00 61.41  ? 858  VAL   A CG2 1 
ATOM   2009 N N   . LYS   A 1 314 ? 22.321 3.407   19.760  1.00 56.46  ? 859  LYS   A N   1 
ATOM   2010 C CA  . LYS   A 1 314 ? 22.985 4.688   19.656  1.00 57.03  ? 859  LYS   A CA  1 
ATOM   2011 C C   . LYS   A 1 314 ? 22.493 5.414   18.431  1.00 51.60  ? 859  LYS   A C   1 
ATOM   2012 O O   . LYS   A 1 314 ? 22.223 6.608   18.474  1.00 54.32  ? 859  LYS   A O   1 
ATOM   2013 C CB  . LYS   A 1 314 ? 24.491 4.491   19.565  1.00 59.55  ? 859  LYS   A CB  1 
ATOM   2014 C CG  . LYS   A 1 314 ? 25.122 3.829   20.773  1.00 63.19  ? 859  LYS   A CG  1 
ATOM   2015 C CD  . LYS   A 1 314 ? 26.585 3.525   20.500  1.00 67.66  ? 859  LYS   A CD  1 
ATOM   2016 C CE  . LYS   A 1 314 ? 27.297 3.054   21.754  1.00 67.42  ? 859  LYS   A CE  1 
ATOM   2017 N NZ  . LYS   A 1 314 ? 27.276 4.103   22.808  1.00 82.16  ? 859  LYS   A NZ  1 
ATOM   2018 N N   . CYS   A 1 315 ? 22.363 4.691   17.334  1.00 52.12  ? 860  CYS   A N   1 
ATOM   2019 C CA  . CYS   A 1 315 ? 21.941 5.303   16.090  1.00 51.56  ? 860  CYS   A CA  1 
ATOM   2020 C C   . CYS   A 1 315 ? 20.536 5.848   16.188  1.00 54.84  ? 860  CYS   A C   1 
ATOM   2021 O O   . CYS   A 1 315 ? 20.148 6.696   15.395  1.00 54.19  ? 860  CYS   A O   1 
ATOM   2022 C CB  . CYS   A 1 315 ? 22.033 4.281   14.961  1.00 47.51  ? 860  CYS   A CB  1 
ATOM   2023 S SG  . CYS   A 1 315 ? 23.710 3.788   14.510  1.00 51.30  ? 860  CYS   A SG  1 
ATOM   2024 N N   . TRP   A 1 316 ? 19.774 5.382   17.169  1.00 46.31  ? 861  TRP   A N   1 
ATOM   2025 C CA  . TRP   A 1 316 ? 18.383 5.805   17.281  1.00 47.88  ? 861  TRP   A CA  1 
ATOM   2026 C C   . TRP   A 1 316 ? 18.149 6.771   18.428  1.00 51.15  ? 861  TRP   A C   1 
ATOM   2027 O O   . TRP   A 1 316 ? 17.073 6.790   19.016  1.00 54.31  ? 861  TRP   A O   1 
ATOM   2028 C CB  . TRP   A 1 316 ? 17.465 4.595   17.432  1.00 43.00  ? 861  TRP   A CB  1 
ATOM   2029 C CG  . TRP   A 1 316 ? 17.462 3.676   16.266  1.00 51.08  ? 861  TRP   A CG  1 
ATOM   2030 C CD1 . TRP   A 1 316 ? 17.677 4.004   14.963  1.00 50.85  ? 861  TRP   A CD1 1 
ATOM   2031 C CD2 . TRP   A 1 316 ? 17.210 2.270   16.291  1.00 52.56  ? 861  TRP   A CD2 1 
ATOM   2032 N NE1 . TRP   A 1 316 ? 17.586 2.886   14.174  1.00 50.11  ? 861  TRP   A NE1 1 
ATOM   2033 C CE2 . TRP   A 1 316 ? 17.298 1.807   14.966  1.00 52.82  ? 861  TRP   A CE2 1 
ATOM   2034 C CE3 . TRP   A 1 316 ? 16.922 1.355   17.306  1.00 47.70  ? 861  TRP   A CE3 1 
ATOM   2035 C CZ2 . TRP   A 1 316 ? 17.109 0.471   14.630  1.00 54.95  ? 861  TRP   A CZ2 1 
ATOM   2036 C CZ3 . TRP   A 1 316 ? 16.734 0.031   16.971  1.00 50.34  ? 861  TRP   A CZ3 1 
ATOM   2037 C CH2 . TRP   A 1 316 ? 16.829 -0.399  15.644  1.00 50.01  ? 861  TRP   A CH2 1 
ATOM   2038 N N   . ASN   A 1 317 ? 19.148 7.580   18.741  1.00 58.28  ? 862  ASN   A N   1 
ATOM   2039 C CA  . ASN   A 1 317 ? 18.984 8.570   19.785  1.00 53.29  ? 862  ASN   A CA  1 
ATOM   2040 C C   . ASN   A 1 317 ? 18.107 9.673   19.261  1.00 60.03  ? 862  ASN   A C   1 
ATOM   2041 O O   . ASN   A 1 317 ? 18.208 10.054  18.102  1.00 62.37  ? 862  ASN   A O   1 
ATOM   2042 C CB  . ASN   A 1 317 ? 20.333 9.129   20.223  1.00 56.50  ? 862  ASN   A CB  1 
ATOM   2043 C CG  . ASN   A 1 317 ? 20.230 10.026  21.440  1.00 64.58  ? 862  ASN   A CG  1 
ATOM   2044 O OD1 . ASN   A 1 317 ? 19.227 10.701  21.654  1.00 65.74  ? 862  ASN   A OD1 1 
ATOM   2045 N ND2 . ASN   A 1 317 ? 21.282 10.041  22.243  1.00 69.40  ? 862  ASN   A ND2 1 
ATOM   2046 N N   . SER   A 1 318 ? 17.239 10.190  20.113  1.00 61.96  ? 863  SER   A N   1 
ATOM   2047 C CA  . SER   A 1 318 ? 16.363 11.264  19.707  1.00 62.03  ? 863  SER   A CA  1 
ATOM   2048 C C   . SER   A 1 318 ? 17.186 12.482  19.351  1.00 65.05  ? 863  SER   A C   1 
ATOM   2049 O O   . SER   A 1 318 ? 16.825 13.235  18.456  1.00 74.65  ? 863  SER   A O   1 
ATOM   2050 C CB  . SER   A 1 318 ? 15.379 11.587  20.823  1.00 62.81  ? 863  SER   A CB  1 
ATOM   2051 O OG  . SER   A 1 318 ? 14.615 10.447  21.164  1.00 67.59  ? 863  SER   A OG  1 
ATOM   2052 N N   . GLU   A 1 319 ? 18.291 12.682  20.051  1.00 62.12  ? 864  GLU   A N   1 
ATOM   2053 C CA  . GLU   A 1 319 ? 19.155 13.812  19.763  1.00 64.55  ? 864  GLU   A CA  1 
ATOM   2054 C C   . GLU   A 1 319 ? 20.093 13.476  18.630  1.00 68.51  ? 864  GLU   A C   1 
ATOM   2055 O O   . GLU   A 1 319 ? 21.017 12.691  18.798  1.00 68.10  ? 864  GLU   A O   1 
ATOM   2056 C CB  . GLU   A 1 319 ? 19.952 14.204  20.997  1.00 67.84  ? 864  GLU   A CB  1 
ATOM   2057 C CG  . GLU   A 1 319 ? 19.092 14.644  22.167  1.00 80.67  ? 864  GLU   A CG  1 
ATOM   2058 C CD  . GLU   A 1 319 ? 19.273 13.766  23.389  1.00 84.91  ? 864  GLU   A CD  1 
ATOM   2059 O OE1 . GLU   A 1 319 ? 20.068 12.807  23.329  1.00 89.17  ? 864  GLU   A OE1 1 
ATOM   2060 O OE2 . GLU   A 1 319 ? 18.616 14.036  24.414  1.00 81.72  ? 864  GLU   A OE2 1 
ATOM   2061 N N   . PRO   A 1 320 ? 19.872 14.089  17.469  1.00 64.78  ? 865  PRO   A N   1 
ATOM   2062 C CA  . PRO   A 1 320 ? 20.684 13.751  16.304  1.00 63.21  ? 865  PRO   A CA  1 
ATOM   2063 C C   . PRO   A 1 320 ? 22.153 13.910  16.591  1.00 64.66  ? 865  PRO   A C   1 
ATOM   2064 O O   . PRO   A 1 320 ? 22.959 13.092  16.164  1.00 63.82  ? 865  PRO   A O   1 
ATOM   2065 C CB  . PRO   A 1 320 ? 20.244 14.792  15.284  1.00 62.37  ? 865  PRO   A CB  1 
ATOM   2066 C CG  . PRO   A 1 320 ? 18.848 15.128  15.668  1.00 58.95  ? 865  PRO   A CG  1 
ATOM   2067 C CD  . PRO   A 1 320 ? 18.857 15.109  17.164  1.00 66.42  ? 865  PRO   A CD  1 
ATOM   2068 N N   . GLU   A 1 321 ? 22.502 14.941  17.332  1.00 68.68  ? 866  GLU   A N   1 
ATOM   2069 C CA  . GLU   A 1 321 ? 23.897 15.220  17.612  1.00 73.75  ? 866  GLU   A CA  1 
ATOM   2070 C C   . GLU   A 1 321 ? 24.547 14.197  18.535  1.00 67.94  ? 866  GLU   A C   1 
ATOM   2071 O O   . GLU   A 1 321 ? 25.762 14.188  18.694  1.00 59.68  ? 866  GLU   A O   1 
ATOM   2072 C CB  . GLU   A 1 321 ? 24.006 16.619  18.216  1.00 74.72  ? 866  GLU   A CB  1 
ATOM   2073 C CG  . GLU   A 1 321 ? 23.304 17.700  17.409  1.00 78.60  ? 866  GLU   A CG  1 
ATOM   2074 C CD  . GLU   A 1 321 ? 21.793 17.653  17.543  1.00 79.16  ? 866  GLU   A CD  1 
ATOM   2075 O OE1 . GLU   A 1 321 ? 21.293 16.950  18.445  1.00 77.18  ? 866  GLU   A OE1 1 
ATOM   2076 O OE2 . GLU   A 1 321 ? 21.104 18.323  16.748  1.00 85.99  ? 866  GLU   A OE2 1 
ATOM   2077 N N   . LYS   A 1 322 ? 23.743 13.341  19.146  1.00 68.06  ? 867  LYS   A N   1 
ATOM   2078 C CA  . LYS   A 1 322 ? 24.281 12.342  20.055  1.00 65.92  ? 867  LYS   A CA  1 
ATOM   2079 C C   . LYS   A 1 322 ? 24.407 10.991  19.382  1.00 64.22  ? 867  LYS   A C   1 
ATOM   2080 O O   . LYS   A 1 322 ? 24.910 10.046  19.979  1.00 60.84  ? 867  LYS   A O   1 
ATOM   2081 C CB  . LYS   A 1 322 ? 23.406 12.232  21.298  1.00 69.88  ? 867  LYS   A CB  1 
ATOM   2082 C CG  . LYS   A 1 322 ? 23.194 13.551  22.013  1.00 73.44  ? 867  LYS   A CG  1 
ATOM   2083 C CD  . LYS   A 1 322 ? 24.522 14.196  22.369  1.00 83.00  ? 867  LYS   A CD  1 
ATOM   2084 C CE  . LYS   A 1 322 ? 24.318 15.585  22.949  1.00 90.19  ? 867  LYS   A CE  1 
ATOM   2085 N NZ  . LYS   A 1 322 ? 25.609 16.231  23.313  1.00 97.27  ? 867  LYS   A NZ  1 
ATOM   2086 N N   . ARG   A 1 323 ? 23.961 10.895  18.137  1.00 63.46  ? 868  ARG   A N   1 
ATOM   2087 C CA  . ARG   A 1 323 ? 24.096 9.648   17.398  1.00 52.13  ? 868  ARG   A CA  1 
ATOM   2088 C C   . ARG   A 1 323 ? 25.523 9.490   16.913  1.00 53.41  ? 868  ARG   A C   1 
ATOM   2089 O O   . ARG   A 1 323 ? 26.216 10.475  16.696  1.00 61.06  ? 868  ARG   A O   1 
ATOM   2090 C CB  . ARG   A 1 323 ? 23.122 9.610   16.226  1.00 55.97  ? 868  ARG   A CB  1 
ATOM   2091 C CG  . ARG   A 1 323 ? 21.669 9.784   16.622  1.00 59.34  ? 868  ARG   A CG  1 
ATOM   2092 C CD  . ARG   A 1 323 ? 20.807 10.036  15.400  1.00 47.68  ? 868  ARG   A CD  1 
ATOM   2093 N NE  . ARG   A 1 323 ? 19.485 10.522  15.769  1.00 55.27  ? 868  ARG   A NE  1 
ATOM   2094 C CZ  . ARG   A 1 323 ? 18.590 10.971  14.899  1.00 53.74  ? 868  ARG   A CZ  1 
ATOM   2095 N NH1 . ARG   A 1 323 ? 18.881 10.999  13.609  1.00 53.48  ? 868  ARG   A NH1 1 
ATOM   2096 N NH2 . ARG   A 1 323 ? 17.409 11.398  15.321  1.00 53.24  ? 868  ARG   A NH2 1 
ATOM   2097 N N   . PRO   A 1 324 ? 25.973 8.248   16.747  1.00 45.47  ? 869  PRO   A N   1 
ATOM   2098 C CA  . PRO   A 1 324 ? 27.354 8.000   16.325  1.00 49.27  ? 869  PRO   A CA  1 
ATOM   2099 C C   . PRO   A 1 324 ? 27.645 8.353   14.864  1.00 63.21  ? 869  PRO   A C   1 
ATOM   2100 O O   . PRO   A 1 324 ? 26.793 8.156   14.007  1.00 55.83  ? 869  PRO   A O   1 
ATOM   2101 C CB  . PRO   A 1 324 ? 27.502 6.494   16.531  1.00 47.93  ? 869  PRO   A CB  1 
ATOM   2102 C CG  . PRO   A 1 324 ? 26.122 5.952   16.429  1.00 53.46  ? 869  PRO   A CG  1 
ATOM   2103 C CD  . PRO   A 1 324 ? 25.242 7.003   17.029  1.00 48.79  ? 869  PRO   A CD  1 
ATOM   2104 N N   . SER   A 1 325 ? 28.839 8.863   14.586  1.00 64.03  ? 870  SER   A N   1 
ATOM   2105 C CA  . SER   A 1 325 ? 29.226 9.202   13.221  1.00 55.66  ? 870  SER   A CA  1 
ATOM   2106 C C   . SER   A 1 325 ? 29.631 7.968   12.461  1.00 63.03  ? 870  SER   A C   1 
ATOM   2107 O O   . SER   A 1 325 ? 29.965 6.954   13.054  1.00 65.17  ? 870  SER   A O   1 
ATOM   2108 C CB  . SER   A 1 325 ? 30.404 10.162  13.223  1.00 59.98  ? 870  SER   A CB  1 
ATOM   2109 O OG  . SER   A 1 325 ? 31.615 9.479   13.489  1.00 63.38  ? 870  SER   A OG  1 
ATOM   2110 N N   . PHE   A 1 326 ? 29.612 8.056   11.140  1.00 58.14  ? 871  PHE   A N   1 
ATOM   2111 C CA  . PHE   A 1 326 ? 29.975 6.911   10.330  1.00 54.69  ? 871  PHE   A CA  1 
ATOM   2112 C C   . PHE   A 1 326 ? 31.432 6.627   10.566  1.00 59.01  ? 871  PHE   A C   1 
ATOM   2113 O O   . PHE   A 1 326 ? 31.829 5.469   10.640  1.00 66.89  ? 871  PHE   A O   1 
ATOM   2114 C CB  . PHE   A 1 326 ? 29.651 7.130   8.851   1.00 66.07  ? 871  PHE   A CB  1 
ATOM   2115 C CG  . PHE   A 1 326 ? 28.181 7.101   8.551   1.00 61.30  ? 871  PHE   A CG  1 
ATOM   2116 C CD1 . PHE   A 1 326 ? 27.438 5.962   8.802   1.00 51.50  ? 871  PHE   A CD1 1 
ATOM   2117 C CD2 . PHE   A 1 326 ? 27.542 8.209   8.026   1.00 55.31  ? 871  PHE   A CD2 1 
ATOM   2118 C CE1 . PHE   A 1 326 ? 26.084 5.927   8.534   1.00 50.83  ? 871  PHE   A CE1 1 
ATOM   2119 C CE2 . PHE   A 1 326 ? 26.189 8.181   7.754   1.00 53.53  ? 871  PHE   A CE2 1 
ATOM   2120 C CZ  . PHE   A 1 326 ? 25.458 7.039   8.009   1.00 54.02  ? 871  PHE   A CZ  1 
ATOM   2121 N N   . TYR   A 1 327 ? 32.247 7.665   10.688  1.00 60.83  ? 872  TYR   A N   1 
ATOM   2122 C CA  . TYR   A 1 327 ? 33.628 7.386   11.060  1.00 68.32  ? 872  TYR   A CA  1 
ATOM   2123 C C   . TYR   A 1 327 ? 33.672 6.597   12.363  1.00 72.12  ? 872  TYR   A C   1 
ATOM   2124 O O   . TYR   A 1 327 ? 34.191 5.475   12.412  1.00 73.97  ? 872  TYR   A O   1 
ATOM   2125 C CB  . TYR   A 1 327 ? 34.448 8.673   11.192  1.00 69.31  ? 872  TYR   A CB  1 
ATOM   2126 C CG  . TYR   A 1 327 ? 35.898 8.340   11.465  1.00 80.30  ? 872  TYR   A CG  1 
ATOM   2127 C CD1 . TYR   A 1 327 ? 36.614 7.510   10.597  1.00 80.65  ? 872  TYR   A CD1 1 
ATOM   2128 C CD2 . TYR   A 1 327 ? 36.541 8.807   12.611  1.00 87.11  ? 872  TYR   A CD2 1 
ATOM   2129 C CE1 . TYR   A 1 327 ? 37.942 7.170   10.851  1.00 90.85  ? 872  TYR   A CE1 1 
ATOM   2130 C CE2 . TYR   A 1 327 ? 37.872 8.470   12.879  1.00 85.13  ? 872  TYR   A CE2 1 
ATOM   2131 C CZ  . TYR   A 1 327 ? 38.568 7.653   11.995  1.00 91.44  ? 872  TYR   A CZ  1 
ATOM   2132 O OH  . TYR   A 1 327 ? 39.886 7.319   12.251  1.00 86.34  ? 872  TYR   A OH  1 
ATOM   2133 N N   . HIS   A 1 328 ? 33.100 7.170   13.428  1.00 66.26  ? 873  HIS   A N   1 
ATOM   2134 C CA  . HIS   A 1 328 ? 33.011 6.471   14.702  1.00 71.83  ? 873  HIS   A CA  1 
ATOM   2135 C C   . HIS   A 1 328 ? 32.380 5.091   14.540  1.00 71.18  ? 873  HIS   A C   1 
ATOM   2136 O O   . HIS   A 1 328 ? 32.851 4.113   15.134  1.00 69.99  ? 873  HIS   A O   1 
ATOM   2137 C CB  . HIS   A 1 328 ? 32.228 7.334   15.697  1.00 68.89  ? 873  HIS   A CB  1 
ATOM   2138 C CG  . HIS   A 1 328 ? 32.366 6.899   17.117  1.00 76.57  ? 873  HIS   A CG  1 
ATOM   2139 N ND1 . HIS   A 1 328 ? 31.500 7.311   18.108  1.00 85.42  ? 873  HIS   A ND1 1 
ATOM   2140 C CD2 . HIS   A 1 328 ? 33.246 6.058   17.712  1.00 80.82  ? 873  HIS   A CD2 1 
ATOM   2141 C CE1 . HIS   A 1 328 ? 31.852 6.760   19.258  1.00 82.07  ? 873  HIS   A CE1 1 
ATOM   2142 N NE2 . HIS   A 1 328 ? 32.904 5.990   19.044  1.00 82.31  ? 873  HIS   A NE2 1 
ATOM   2143 N N   . LEU   A 1 329 ? 31.347 4.968   13.723  1.00 68.59  ? 874  LEU   A N   1 
ATOM   2144 C CA  . LEU   A 1 329 ? 30.680 3.679   13.581  1.00 67.08  ? 874  LEU   A CA  1 
ATOM   2145 C C   . LEU   A 1 329 ? 31.610 2.657   12.967  1.00 66.76  ? 874  LEU   A C   1 
ATOM   2146 O O   . LEU   A 1 329 ? 31.561 1.477   13.306  1.00 71.28  ? 874  LEU   A O   1 
ATOM   2147 C CB  . LEU   A 1 329 ? 29.413 3.804   12.737  1.00 59.90  ? 874  LEU   A CB  1 
ATOM   2148 C CG  . LEU   A 1 329 ? 28.192 4.413   13.420  1.00 64.33  ? 874  LEU   A CG  1 
ATOM   2149 C CD1 . LEU   A 1 329 ? 27.100 4.718   12.409  1.00 58.23  ? 874  LEU   A CD1 1 
ATOM   2150 C CD2 . LEU   A 1 329 ? 27.685 3.473   14.500  1.00 66.80  ? 874  LEU   A CD2 1 
ATOM   2151 N N   . SER   A 1 330 ? 32.472 3.107   12.073  1.00 64.44  ? 875  SER   A N   1 
ATOM   2152 C CA  . SER   A 1 330 ? 33.372 2.190   11.396  1.00 70.41  ? 875  SER   A CA  1 
ATOM   2153 C C   . SER   A 1 330 ? 34.316 1.515   12.371  1.00 69.54  ? 875  SER   A C   1 
ATOM   2154 O O   . SER   A 1 330 ? 34.482 0.299   12.342  1.00 73.41  ? 875  SER   A O   1 
ATOM   2155 C CB  . SER   A 1 330 ? 34.166 2.938   10.328  1.00 70.86  ? 875  SER   A CB  1 
ATOM   2156 O OG  . SER   A 1 330 ? 33.304 3.510   9.362   1.00 69.03  ? 875  SER   A OG  1 
ATOM   2157 N N   . GLU   A 1 331 ? 34.922 2.297   13.249  1.00 74.72  ? 876  GLU   A N   1 
ATOM   2158 C CA  . GLU   A 1 331 ? 35.862 1.744   14.208  1.00 78.05  ? 876  GLU   A CA  1 
ATOM   2159 C C   . GLU   A 1 331 ? 35.204 0.702   15.085  1.00 76.29  ? 876  GLU   A C   1 
ATOM   2160 O O   . GLU   A 1 331 ? 35.773 -0.359  15.328  1.00 76.17  ? 876  GLU   A O   1 
ATOM   2161 C CB  . GLU   A 1 331 ? 36.423 2.860   15.077  1.00 80.19  ? 876  GLU   A CB  1 
ATOM   2162 C CG  . GLU   A 1 331 ? 37.116 3.961   14.296  1.00 83.28  ? 876  GLU   A CG  1 
ATOM   2163 C CD  . GLU   A 1 331 ? 37.521 5.130   15.171  1.00 91.76  ? 876  GLU   A CD  1 
ATOM   2164 O OE1 . GLU   A 1 331 ? 36.990 5.244   16.295  1.00 90.52  ? 876  GLU   A OE1 1 
ATOM   2165 O OE2 . GLU   A 1 331 ? 38.375 5.932   14.738  1.00 96.15  ? 876  GLU   A OE2 1 
ATOM   2166 N N   . ILE   A 1 332 ? 33.999 0.990   15.555  1.00 71.74  ? 877  ILE   A N   1 
ATOM   2167 C CA  . ILE   A 1 332 ? 33.320 0.069   16.449  1.00 69.46  ? 877  ILE   A CA  1 
ATOM   2168 C C   . ILE   A 1 332 ? 33.138 -1.272  15.781  1.00 74.60  ? 877  ILE   A C   1 
ATOM   2169 O O   . ILE   A 1 332 ? 33.459 -2.312  16.354  1.00 79.72  ? 877  ILE   A O   1 
ATOM   2170 C CB  . ILE   A 1 332 ? 31.950 0.617   16.863  1.00 69.59  ? 877  ILE   A CB  1 
ATOM   2171 C CG1 . ILE   A 1 332 ? 32.116 1.968   17.560  1.00 70.90  ? 877  ILE   A CG1 1 
ATOM   2172 C CG2 . ILE   A 1 332 ? 31.230 -0.372  17.764  1.00 67.60  ? 877  ILE   A CG2 1 
ATOM   2173 C CD1 . ILE   A 1 332 ? 30.809 2.623   17.944  1.00 62.49  ? 877  ILE   A CD1 1 
ATOM   2174 N N   . VAL   A 1 333 ? 32.640 -1.255  14.557  1.00 72.98  ? 878  VAL   A N   1 
ATOM   2175 C CA  . VAL   A 1 333 ? 32.391 -2.503  13.867  1.00 71.58  ? 878  VAL   A CA  1 
ATOM   2176 C C   . VAL   A 1 333 ? 33.712 -3.218  13.630  1.00 76.35  ? 878  VAL   A C   1 
ATOM   2177 O O   . VAL   A 1 333 ? 33.792 -4.436  13.738  1.00 76.50  ? 878  VAL   A O   1 
ATOM   2178 C CB  . VAL   A 1 333 ? 31.641 -2.271  12.547  1.00 71.70  ? 878  VAL   A CB  1 
ATOM   2179 C CG1 . VAL   A 1 333 ? 31.303 -3.599  11.891  1.00 64.37  ? 878  VAL   A CG1 1 
ATOM   2180 C CG2 . VAL   A 1 333 ? 30.378 -1.468  12.800  1.00 65.70  ? 878  VAL   A CG2 1 
ATOM   2181 N N   . GLU   A 1 334 ? 34.757 -2.464  13.329  1.00 75.50  ? 879  GLU   A N   1 
ATOM   2182 C CA  . GLU   A 1 334 ? 36.066 -3.062  13.124  1.00 78.21  ? 879  GLU   A CA  1 
ATOM   2183 C C   . GLU   A 1 334 ? 36.420 -3.975  14.269  1.00 81.81  ? 879  GLU   A C   1 
ATOM   2184 O O   . GLU   A 1 334 ? 36.833 -5.112  14.061  1.00 81.68  ? 879  GLU   A O   1 
ATOM   2185 C CB  . GLU   A 1 334 ? 37.126 -1.978  13.012  1.00 80.69  ? 879  GLU   A CB  1 
ATOM   2186 C CG  . GLU   A 1 334 ? 38.546 -2.507  12.938  1.00 89.92  ? 879  GLU   A CG  1 
ATOM   2187 C CD  . GLU   A 1 334 ? 39.578 -1.399  12.964  1.00 95.50  ? 879  GLU   A CD  1 
ATOM   2188 O OE1 . GLU   A 1 334 ? 39.183 -0.221  13.092  1.00 93.54  ? 879  GLU   A OE1 1 
ATOM   2189 O OE2 . GLU   A 1 334 ? 40.782 -1.705  12.856  1.00 98.83  ? 879  GLU   A OE2 1 
ATOM   2190 N N   . ASN   A 1 335 ? 36.260 -3.479  15.486  1.00 80.79  ? 880  ASN   A N   1 
ATOM   2191 C CA  . ASN   A 1 335 ? 36.581 -4.266  16.664  1.00 78.89  ? 880  ASN   A CA  1 
ATOM   2192 C C   . ASN   A 1 335 ? 35.759 -5.535  16.711  1.00 80.76  ? 880  ASN   A C   1 
ATOM   2193 O O   . ASN   A 1 335 ? 36.215 -6.554  17.217  1.00 84.63  ? 880  ASN   A O   1 
ATOM   2194 C CB  . ASN   A 1 335 ? 36.335 -3.425  17.915  1.00 83.65  ? 880  ASN   A CB  1 
ATOM   2195 C CG  . ASN   A 1 335 ? 36.520 -4.207  19.200  1.00 93.42  ? 880  ASN   A CG  1 
ATOM   2196 O OD1 . ASN   A 1 335 ? 35.690 -5.041  19.561  1.00 96.27  ? 880  ASN   A OD1 1 
ATOM   2197 N ND2 . ASN   A 1 335 ? 37.603 -3.921  19.912  1.00 88.40  ? 880  ASN   A ND2 1 
ATOM   2198 N N   . LEU   A 1 336 ? 34.549 -5.484  16.182  1.00 78.34  ? 881  LEU   A N   1 
ATOM   2199 C CA  . LEU   A 1 336 ? 33.672 -6.638  16.239  1.00 75.50  ? 881  LEU   A CA  1 
ATOM   2200 C C   . LEU   A 1 336 ? 34.113 -7.717  15.274  1.00 76.59  ? 881  LEU   A C   1 
ATOM   2201 O O   . LEU   A 1 336 ? 33.547 -8.805  15.253  1.00 78.20  ? 881  LEU   A O   1 
ATOM   2202 C CB  . LEU   A 1 336 ? 32.244 -6.211  15.929  1.00 74.83  ? 881  LEU   A CB  1 
ATOM   2203 C CG  . LEU   A 1 336 ? 31.719 -5.043  16.759  1.00 79.25  ? 881  LEU   A CG  1 
ATOM   2204 C CD1 . LEU   A 1 336 ? 30.346 -4.615  16.269  1.00 78.89  ? 881  LEU   A CD1 1 
ATOM   2205 C CD2 . LEU   A 1 336 ? 31.680 -5.408  18.234  1.00 83.51  ? 881  LEU   A CD2 1 
ATOM   2206 N N   . LEU   A 1 337 ? 35.118 -7.421  14.466  1.00 77.27  ? 882  LEU   A N   1 
ATOM   2207 C CA  . LEU   A 1 337 ? 35.593 -8.387  13.484  1.00 79.70  ? 882  LEU   A CA  1 
ATOM   2208 C C   . LEU   A 1 337 ? 37.080 -8.635  13.636  1.00 81.53  ? 882  LEU   A C   1 
ATOM   2209 O O   . LEU   A 1 337 ? 37.777 -7.868  14.292  1.00 81.95  ? 882  LEU   A O   1 
ATOM   2210 C CB  . LEU   A 1 337 ? 35.292 -7.911  12.059  1.00 76.88  ? 882  LEU   A CB  1 
ATOM   2211 C CG  . LEU   A 1 337 ? 33.854 -7.963  11.545  1.00 68.25  ? 882  LEU   A CG  1 
ATOM   2212 C CD1 . LEU   A 1 337 ? 33.040 -6.820  12.124  1.00 77.47  ? 882  LEU   A CD1 1 
ATOM   2213 C CD2 . LEU   A 1 337 ? 33.844 -7.893  10.027  1.00 72.99  ? 882  LEU   A CD2 1 
ATOM   2214 N N   . PRO   A 1 338 ? 37.586 -9.719  13.022  1.00 81.44  ? 883  PRO   A N   1 
ATOM   2215 C CA  . PRO   A 1 338 ? 39.031 -9.954  13.081  1.00 84.78  ? 883  PRO   A CA  1 
ATOM   2216 C C   . PRO   A 1 338 ? 39.851 -8.784  12.561  1.00 88.84  ? 883  PRO   A C   1 
ATOM   2217 O O   . PRO   A 1 338 ? 39.497 -8.194  11.547  1.00 89.45  ? 883  PRO   A O   1 
ATOM   2218 C CB  . PRO   A 1 338 ? 39.225 -11.166 12.165  1.00 82.86  ? 883  PRO   A CB  1 
ATOM   2219 C CG  . PRO   A 1 338 ? 37.969 -11.286 11.371  1.00 81.91  ? 883  PRO   A CG  1 
ATOM   2220 C CD  . PRO   A 1 338 ? 36.901 -10.800 12.292  1.00 79.70  ? 883  PRO   A CD  1 
ATOM   2221 N N   . GLY   A 1 339 ? 40.945 -8.460  13.240  1.00 94.15  ? 884  GLY   A N   1 
ATOM   2222 C CA  . GLY   A 1 339 ? 41.801 -7.365  12.816  1.00 86.91  ? 884  GLY   A CA  1 
ATOM   2223 C C   . GLY   A 1 339 ? 42.413 -7.637  11.465  1.00 93.58  ? 884  GLY   A C   1 
ATOM   2224 O O   . GLY   A 1 339 ? 42.884 -6.721  10.793  1.00 92.61  ? 884  GLY   A O   1 
ATOM   2225 N N   . GLN   A 1 340 ? 42.423 -8.898  11.060  1.00 93.39  ? 885  GLN   A N   1 
ATOM   2226 C CA  . GLN   A 1 340 ? 42.932 -9.244  9.748   1.00 93.11  ? 885  GLN   A CA  1 
ATOM   2227 C C   . GLN   A 1 340 ? 42.013 -8.686  8.680   1.00 93.25  ? 885  GLN   A C   1 
ATOM   2228 O O   . GLN   A 1 340 ? 42.444 -8.418  7.561   1.00 92.74  ? 885  GLN   A O   1 
ATOM   2229 C CB  . GLN   A 1 340 ? 43.042 -10.758 9.619   1.00 95.75  ? 885  GLN   A CB  1 
ATOM   2230 C CG  . GLN   A 1 340 ? 41.738 -11.500 9.847   1.00 100.86 ? 885  GLN   A CG  1 
ATOM   2231 C CD  . GLN   A 1 340 ? 41.953 -12.976 10.118  1.00 107.95 ? 885  GLN   A CD  1 
ATOM   2232 O OE1 . GLN   A 1 340 ? 43.079 -13.419 10.336  1.00 111.87 ? 885  GLN   A OE1 1 
ATOM   2233 N NE2 . GLN   A 1 340 ? 40.870 -13.743 10.112  1.00 106.72 ? 885  GLN   A NE2 1 
ATOM   2234 N N   . TYR   A 1 341 ? 40.745 -8.499  9.024   1.00 91.11  ? 886  TYR   A N   1 
ATOM   2235 C CA  . TYR   A 1 341 ? 39.779 -7.995  8.062   1.00 89.77  ? 886  TYR   A CA  1 
ATOM   2236 C C   . TYR   A 1 341 ? 40.189 -6.648  7.519   1.00 91.55  ? 886  TYR   A C   1 
ATOM   2237 O O   . TYR   A 1 341 ? 40.206 -6.444  6.309   1.00 88.16  ? 886  TYR   A O   1 
ATOM   2238 C CB  . TYR   A 1 341 ? 38.410 -7.878  8.725   1.00 82.89  ? 886  TYR   A CB  1 
ATOM   2239 C CG  . TYR   A 1 341 ? 37.308 -7.356  7.836   1.00 77.01  ? 886  TYR   A CG  1 
ATOM   2240 C CD1 . TYR   A 1 341 ? 37.078 -5.995  7.708   1.00 76.14  ? 886  TYR   A CD1 1 
ATOM   2241 C CD2 . TYR   A 1 341 ? 36.482 -8.227  7.143   1.00 80.47  ? 886  TYR   A CD2 1 
ATOM   2242 C CE1 . TYR   A 1 341 ? 36.065 -5.515  6.903   1.00 78.20  ? 886  TYR   A CE1 1 
ATOM   2243 C CE2 . TYR   A 1 341 ? 35.466 -7.756  6.336   1.00 78.86  ? 886  TYR   A CE2 1 
ATOM   2244 C CZ  . TYR   A 1 341 ? 35.262 -6.401  6.221   1.00 79.60  ? 886  TYR   A CZ  1 
ATOM   2245 O OH  . TYR   A 1 341 ? 34.251 -5.930  5.419   1.00 71.52  ? 886  TYR   A OH  1 
ATOM   2246 N N   . LYS   A 1 342 ? 40.543 -5.728  8.402   1.00 83.46  ? 887  LYS   A N   1 
ATOM   2247 C CA  . LYS   A 1 342 ? 40.860 -4.386  7.954   1.00 84.39  ? 887  LYS   A CA  1 
ATOM   2248 C C   . LYS   A 1 342 ? 41.894 -4.406  6.848   1.00 93.19  ? 887  LYS   A C   1 
ATOM   2249 O O   . LYS   A 1 342 ? 41.737 -3.732  5.833   1.00 94.02  ? 887  LYS   A O   1 
ATOM   2250 C CB  . LYS   A 1 342 ? 41.370 -3.553  9.122   1.00 86.10  ? 887  LYS   A CB  1 
ATOM   2251 C CG  . LYS   A 1 342 ? 42.043 -2.256  8.709   1.00 89.31  ? 887  LYS   A CG  1 
ATOM   2252 C CD  . LYS   A 1 342 ? 41.041 -1.280  8.123   1.00 88.06  ? 887  LYS   A CD  1 
ATOM   2253 C CE  . LYS   A 1 342 ? 40.032 -0.853  9.173   1.00 87.32  ? 887  LYS   A CE  1 
ATOM   2254 N NZ  . LYS   A 1 342 ? 40.696 -0.183  10.322  1.00 96.56  ? 887  LYS   A NZ  1 
ATOM   2255 N N   . LYS   A 1 343 ? 42.951 -5.182  7.028   1.00 92.62  ? 888  LYS   A N   1 
ATOM   2256 C CA  . LYS   A 1 343 ? 44.014 -5.193  6.042   1.00 95.20  ? 888  LYS   A CA  1 
ATOM   2257 C C   . LYS   A 1 343 ? 43.499 -5.657  4.704   1.00 92.60  ? 888  LYS   A C   1 
ATOM   2258 O O   . LYS   A 1 343 ? 43.719 -5.002  3.691   1.00 92.62  ? 888  LYS   A O   1 
ATOM   2259 C CB  . LYS   A 1 343 ? 45.142 -6.113  6.495   1.00 97.45  ? 888  LYS   A CB  1 
ATOM   2260 C CG  . LYS   A 1 343 ? 46.307 -6.182  5.522   1.00 99.14  ? 888  LYS   A CG  1 
ATOM   2261 C CD  . LYS   A 1 343 ? 47.446 -7.038  6.054   1.00 97.10  ? 888  LYS   A CD  1 
ATOM   2262 C CE  . LYS   A 1 343 ? 48.276 -6.305  7.098   1.00 81.06  ? 888  LYS   A CE  1 
ATOM   2263 N NZ  . LYS   A 1 343 ? 47.555 -6.088  8.382   1.00 89.56  ? 888  LYS   A NZ  1 
ATOM   2264 N N   . SER   A 1 344 ? 42.803 -6.783  4.697   1.00 93.80  ? 889  SER   A N   1 
ATOM   2265 C CA  . SER   A 1 344 ? 42.290 -7.325  3.451   1.00 94.00  ? 889  SER   A CA  1 
ATOM   2266 C C   . SER   A 1 344 ? 41.356 -6.328  2.795   1.00 90.43  ? 889  SER   A C   1 
ATOM   2267 O O   . SER   A 1 344 ? 41.402 -6.129  1.583   1.00 92.32  ? 889  SER   A O   1 
ATOM   2268 C CB  . SER   A 1 344 ? 41.572 -8.645  3.707   1.00 96.32  ? 889  SER   A CB  1 
ATOM   2269 O OG  . SER   A 1 344 ? 40.572 -8.494  4.699   1.00 99.88  ? 889  SER   A OG  1 
ATOM   2270 N N   . TYR   A 1 345 ? 40.519 -5.686  3.593   1.00 88.32  ? 890  TYR   A N   1 
ATOM   2271 C CA  . TYR   A 1 345 ? 39.630 -4.680  3.052   1.00 87.68  ? 890  TYR   A CA  1 
ATOM   2272 C C   . TYR   A 1 345 ? 40.440 -3.598  2.375   1.00 87.41  ? 890  TYR   A C   1 
ATOM   2273 O O   . TYR   A 1 345 ? 40.135 -3.195  1.259   1.00 87.58  ? 890  TYR   A O   1 
ATOM   2274 C CB  . TYR   A 1 345 ? 38.772 -4.074  4.163   1.00 77.98  ? 890  TYR   A CB  1 
ATOM   2275 C CG  . TYR   A 1 345 ? 37.956 -2.879  3.732   1.00 76.42  ? 890  TYR   A CG  1 
ATOM   2276 C CD1 . TYR   A 1 345 ? 36.692 -3.040  3.183   1.00 76.82  ? 890  TYR   A CD1 1 
ATOM   2277 C CD2 . TYR   A 1 345 ? 38.448 -1.591  3.876   1.00 76.24  ? 890  TYR   A CD2 1 
ATOM   2278 C CE1 . TYR   A 1 345 ? 35.943 -1.951  2.787   1.00 75.48  ? 890  TYR   A CE1 1 
ATOM   2279 C CE2 . TYR   A 1 345 ? 37.706 -0.496  3.481   1.00 79.21  ? 890  TYR   A CE2 1 
ATOM   2280 C CZ  . TYR   A 1 345 ? 36.456 -0.683  2.938   1.00 76.50  ? 890  TYR   A CZ  1 
ATOM   2281 O OH  . TYR   A 1 345 ? 35.715 0.405   2.545   1.00 70.04  ? 890  TYR   A OH  1 
ATOM   2282 N N   . GLU   A 1 346 ? 41.486 -3.133  3.038   1.00 84.40  ? 891  GLU   A N   1 
ATOM   2283 C CA  . GLU   A 1 346 ? 42.279 -2.050  2.483   1.00 86.98  ? 891  GLU   A CA  1 
ATOM   2284 C C   . GLU   A 1 346 ? 42.925 -2.459  1.178   1.00 90.70  ? 891  GLU   A C   1 
ATOM   2285 O O   . GLU   A 1 346 ? 43.090 -1.643  0.277   1.00 86.93  ? 891  GLU   A O   1 
ATOM   2286 C CB  . GLU   A 1 346 ? 43.348 -1.607  3.475   1.00 86.51  ? 891  GLU   A CB  1 
ATOM   2287 C CG  . GLU   A 1 346 ? 42.788 -1.036  4.767   1.00 91.08  ? 891  GLU   A CG  1 
ATOM   2288 C CD  . GLU   A 1 346 ? 42.037 0.265   4.561   1.00 86.69  ? 891  GLU   A CD  1 
ATOM   2289 O OE1 . GLU   A 1 346 ? 42.016 0.777   3.424   1.00 94.36  ? 891  GLU   A OE1 1 
ATOM   2290 O OE2 . GLU   A 1 346 ? 41.470 0.783   5.544   1.00 84.73  ? 891  GLU   A OE2 1 
ATOM   2291 N N   . LYS   A 1 347 ? 43.298 -3.724  1.075   1.00 92.98  ? 892  LYS   A N   1 
ATOM   2292 C CA  . LYS   A 1 347 ? 43.944 -4.191  -0.135  1.00 89.66  ? 892  LYS   A CA  1 
ATOM   2293 C C   . LYS   A 1 347 ? 42.963 -4.087  -1.265  1.00 88.75  ? 892  LYS   A C   1 
ATOM   2294 O O   . LYS   A 1 347 ? 43.278 -3.554  -2.325  1.00 95.14  ? 892  LYS   A O   1 
ATOM   2295 C CB  . LYS   A 1 347 ? 44.424 -5.626  0.028   1.00 88.90  ? 892  LYS   A CB  1 
ATOM   2296 C CG  . LYS   A 1 347 ? 45.389 -5.790  1.184   1.00 98.41  ? 892  LYS   A CG  1 
ATOM   2297 C CD  . LYS   A 1 347 ? 46.390 -4.648  1.194   1.00 96.58  ? 892  LYS   A CD  1 
ATOM   2298 C CE  . LYS   A 1 347 ? 47.131 -4.566  2.516   1.00 100.89 ? 892  LYS   A CE  1 
ATOM   2299 N NZ  . LYS   A 1 347 ? 48.016 -3.370  2.573   1.00 103.20 ? 892  LYS   A NZ  1 
ATOM   2300 N N   . ILE   A 1 348 ? 41.759 -4.581  -1.036  1.00 84.45  ? 893  ILE   A N   1 
ATOM   2301 C CA  . ILE   A 1 348 ? 40.734 -4.500  -2.050  1.00 86.35  ? 893  ILE   A CA  1 
ATOM   2302 C C   . ILE   A 1 348 ? 40.437 -3.050  -2.342  1.00 87.94  ? 893  ILE   A C   1 
ATOM   2303 O O   . ILE   A 1 348 ? 40.235 -2.677  -3.493  1.00 88.18  ? 893  ILE   A O   1 
ATOM   2304 C CB  . ILE   A 1 348 ? 39.454 -5.186  -1.572  1.00 83.76  ? 893  ILE   A CB  1 
ATOM   2305 C CG1 . ILE   A 1 348 ? 39.765 -6.608  -1.107  1.00 87.33  ? 893  ILE   A CG1 1 
ATOM   2306 C CG2 . ILE   A 1 348 ? 38.410 -5.192  -2.677  1.00 86.67  ? 893  ILE   A CG2 1 
ATOM   2307 C CD1 . ILE   A 1 348 ? 38.574 -7.328  -0.516  1.00 88.35  ? 893  ILE   A CD1 1 
ATOM   2308 N N   . HIS   A 1 349 ? 40.433 -2.222  -1.310  1.00 83.29  ? 894  HIS   A N   1 
ATOM   2309 C CA  . HIS   A 1 349 ? 40.083 -0.822  -1.487  1.00 84.11  ? 894  HIS   A CA  1 
ATOM   2310 C C   . HIS   A 1 349 ? 41.185 -0.035  -2.159  1.00 90.03  ? 894  HIS   A C   1 
ATOM   2311 O O   . HIS   A 1 349 ? 41.027 1.155   -2.411  1.00 95.98  ? 894  HIS   A O   1 
ATOM   2312 C CB  . HIS   A 1 349 ? 39.747 -0.188  -0.140  1.00 89.42  ? 894  HIS   A CB  1 
ATOM   2313 C CG  . HIS   A 1 349 ? 39.154 1.181   -0.248  1.00 90.00  ? 894  HIS   A CG  1 
ATOM   2314 N ND1 . HIS   A 1 349 ? 37.903 1.408   -0.778  1.00 92.51  ? 894  HIS   A ND1 1 
ATOM   2315 C CD2 . HIS   A 1 349 ? 39.637 2.393   0.112   1.00 89.64  ? 894  HIS   A CD2 1 
ATOM   2316 C CE1 . HIS   A 1 349 ? 37.643 2.703   -0.745  1.00 92.23  ? 894  HIS   A CE1 1 
ATOM   2317 N NE2 . HIS   A 1 349 ? 38.678 3.322   -0.208  1.00 95.36  ? 894  HIS   A NE2 1 
ATOM   2318 N N   . LEU   A 1 350 ? 42.311 -0.674  -2.430  1.00 90.82  ? 895  LEU   A N   1 
ATOM   2319 C CA  . LEU   A 1 350 ? 43.379 0.005   -3.149  1.00 90.27  ? 895  LEU   A CA  1 
ATOM   2320 C C   . LEU   A 1 350 ? 43.409 -0.525  -4.555  1.00 88.85  ? 895  LEU   A C   1 
ATOM   2321 O O   . LEU   A 1 350 ? 43.709 0.204   -5.495  1.00 87.14  ? 895  LEU   A O   1 
ATOM   2322 C CB  . LEU   A 1 350 ? 44.720 -0.212  -2.467  1.00 88.53  ? 895  LEU   A CB  1 
ATOM   2323 C CG  . LEU   A 1 350 ? 45.112 0.785   -1.376  1.00 94.66  ? 895  LEU   A CG  1 
ATOM   2324 C CD1 . LEU   A 1 350 ? 43.940 1.148   -0.477  1.00 94.74  ? 895  LEU   A CD1 1 
ATOM   2325 C CD2 . LEU   A 1 350 ? 46.285 0.257   -0.566  1.00 101.75 ? 895  LEU   A CD2 1 
ATOM   2326 N N   . ASP   A 1 351 ? 43.094 -1.801  -4.705  1.00 88.38  ? 896  ASP   A N   1 
ATOM   2327 C CA  . ASP   A 1 351 ? 43.032 -2.382  -6.028  1.00 90.32  ? 896  ASP   A CA  1 
ATOM   2328 C C   . ASP   A 1 351 ? 41.910 -1.731  -6.803  1.00 91.73  ? 896  ASP   A C   1 
ATOM   2329 O O   . ASP   A 1 351 ? 42.118 -1.245  -7.912  1.00 94.45  ? 896  ASP   A O   1 
ATOM   2330 C CB  . ASP   A 1 351 ? 42.792 -3.883  -5.927  1.00 92.67  ? 896  ASP   A CB  1 
ATOM   2331 C CG  . ASP   A 1 351 ? 43.865 -4.590  -5.130  1.00 99.49  ? 896  ASP   A CG  1 
ATOM   2332 O OD1 . ASP   A 1 351 ? 44.814 -3.917  -4.678  1.00 96.65  ? 896  ASP   A OD1 1 
ATOM   2333 O OD2 . ASP   A 1 351 ? 43.762 -5.821  -4.954  1.00 108.10 ? 896  ASP   A OD2 1 
ATOM   2334 N N   . PHE   A 1 352 ? 40.720 -1.706  -6.217  1.00 89.83  ? 897  PHE   A N   1 
ATOM   2335 C CA  . PHE   A 1 352 ? 39.574 -1.082  -6.864  1.00 86.40  ? 897  PHE   A CA  1 
ATOM   2336 C C   . PHE   A 1 352 ? 40.009 0.182   -7.579  1.00 81.63  ? 897  PHE   A C   1 
ATOM   2337 O O   . PHE   A 1 352 ? 39.626 0.415   -8.720  1.00 83.61  ? 897  PHE   A O   1 
ATOM   2338 C CB  . PHE   A 1 352 ? 38.500 -0.800  -5.808  1.00 82.59  ? 897  PHE   A CB  1 
ATOM   2339 C CG  . PHE   A 1 352 ? 37.390 0.094   -6.274  1.00 75.04  ? 897  PHE   A CG  1 
ATOM   2340 C CD1 . PHE   A 1 352 ? 36.310 -0.424  -6.961  1.00 66.52  ? 897  PHE   A CD1 1 
ATOM   2341 C CD2 . PHE   A 1 352 ? 37.414 1.448   -5.993  1.00 74.92  ? 897  PHE   A CD2 1 
ATOM   2342 C CE1 . PHE   A 1 352 ? 35.283 0.397   -7.379  1.00 69.37  ? 897  PHE   A CE1 1 
ATOM   2343 C CE2 . PHE   A 1 352 ? 36.392 2.274   -6.409  1.00 72.11  ? 897  PHE   A CE2 1 
ATOM   2344 C CZ  . PHE   A 1 352 ? 35.324 1.748   -7.102  1.00 71.80  ? 897  PHE   A CZ  1 
ATOM   2345 N N   . LEU   A 1 353 ? 40.814 0.995   -6.916  1.00 77.70  ? 898  LEU   A N   1 
ATOM   2346 C CA  . LEU   A 1 353 ? 41.332 2.221   -7.527  1.00 83.95  ? 898  LEU   A CA  1 
ATOM   2347 C C   . LEU   A 1 353 ? 42.573 1.937   -8.379  1.00 89.02  ? 898  LEU   A C   1 
ATOM   2348 O O   . LEU   A 1 353 ? 43.342 2.847   -8.706  1.00 83.04  ? 898  LEU   A O   1 
ATOM   2349 C CB  . LEU   A 1 353 ? 41.661 3.273   -6.459  1.00 76.63  ? 898  LEU   A CB  1 
ATOM   2350 C CG  . LEU   A 1 353 ? 40.476 3.880   -5.702  1.00 80.83  ? 898  LEU   A CG  1 
ATOM   2351 C CD1 . LEU   A 1 353 ? 40.836 4.192   -4.247  1.00 84.84  ? 898  LEU   A CD1 1 
ATOM   2352 C CD2 . LEU   A 1 353 ? 39.956 5.126   -6.405  1.00 78.17  ? 898  LEU   A CD2 1 
HETATM 2353 C C14 . A1LV8 B 2 .   ? 21.475 -4.408  -9.572  1.00 47.94  ? 1001 A1LV8 A C14 1 
HETATM 2354 C C10 . A1LV8 B 2 .   ? 19.560 2.872   -8.719  1.00 46.89  ? 1001 A1LV8 A C10 1 
HETATM 2355 C C12 . A1LV8 B 2 .   ? 22.655 -2.616  -9.792  1.00 49.62  ? 1001 A1LV8 A C12 1 
HETATM 2356 C C01 . A1LV8 B 2 .   ? 18.402 3.046   -7.973  1.00 46.24  ? 1001 A1LV8 A C01 1 
HETATM 2357 C C02 . A1LV8 B 2 .   ? 17.748 1.941   -7.425  1.00 45.72  ? 1001 A1LV8 A C02 1 
HETATM 2358 C C03 . A1LV8 B 2 .   ? 18.245 0.668   -7.633  1.00 45.75  ? 1001 A1LV8 A C03 1 
HETATM 2359 C C04 . A1LV8 B 2 .   ? 19.436 0.489   -8.397  1.00 48.99  ? 1001 A1LV8 A C04 1 
HETATM 2360 C C06 . A1LV8 B 2 .   ? 21.016 -0.997  -9.290  1.00 49.61  ? 1001 A1LV8 A C06 1 
HETATM 2361 C C07 . A1LV8 B 2 .   ? 21.719 0.055   -9.865  1.00 50.14  ? 1001 A1LV8 A C07 1 
HETATM 2362 C C08 . A1LV8 B 2 .   ? 21.261 1.354   -9.692  1.00 46.73  ? 1001 A1LV8 A C08 1 
HETATM 2363 C C09 . A1LV8 B 2 .   ? 20.076 1.562   -8.929  1.00 49.25  ? 1001 A1LV8 A C09 1 
HETATM 2364 C C15 . A1LV8 B 2 .   ? 20.950 -5.725  -9.500  1.00 54.79  ? 1001 A1LV8 A C15 1 
HETATM 2365 C C16 . A1LV8 B 2 .   ? 19.616 -5.923  -9.164  1.00 59.51  ? 1001 A1LV8 A C16 1 
HETATM 2366 C C17 . A1LV8 B 2 .   ? 18.794 -4.829  -8.897  1.00 57.69  ? 1001 A1LV8 A C17 1 
HETATM 2367 C C18 . A1LV8 B 2 .   ? 19.308 -3.548  -8.971  1.00 57.07  ? 1001 A1LV8 A C18 1 
HETATM 2368 C C19 . A1LV8 B 2 .   ? 20.665 -3.342  -9.311  1.00 50.87  ? 1001 A1LV8 A C19 1 
HETATM 2369 C C21 . A1LV8 B 2 .   ? 17.187 -6.202  -7.893  1.00 57.58  ? 1001 A1LV8 A C21 1 
HETATM 2370 C C22 . A1LV8 B 2 .   ? 16.499 -5.877  -6.575  1.00 53.45  ? 1001 A1LV8 A C22 1 
HETATM 2371 C C23 . A1LV8 B 2 .   ? 15.572 -4.675  -6.656  1.00 50.22  ? 1001 A1LV8 A C23 1 
HETATM 2372 C C25 . A1LV8 B 2 .   ? 16.161 -2.562  -5.666  1.00 49.17  ? 1001 A1LV8 A C25 1 
HETATM 2373 C C26 . A1LV8 B 2 .   ? 15.573 -1.987  -6.947  1.00 54.67  ? 1001 A1LV8 A C26 1 
HETATM 2374 C C27 . A1LV8 B 2 .   ? 16.126 -0.593  -7.243  1.00 49.90  ? 1001 A1LV8 A C27 1 
HETATM 2375 C C29 . A1LV8 B 2 .   ? 18.221 -1.185  -5.983  1.00 44.76  ? 1001 A1LV8 A C29 1 
HETATM 2376 C C30 . A1LV8 B 2 .   ? 17.676 -2.584  -5.740  1.00 48.26  ? 1001 A1LV8 A C30 1 
HETATM 2377 N N05 . A1LV8 B 2 .   ? 19.918 -0.766  -8.592  1.00 52.33  ? 1001 A1LV8 A N05 1 
HETATM 2378 N N11 . A1LV8 B 2 .   ? 21.434 -2.235  -9.451  1.00 52.08  ? 1001 A1LV8 A N11 1 
HETATM 2379 N N13 . A1LV8 B 2 .   ? 22.713 -3.935  -9.868  1.00 50.71  ? 1001 A1LV8 A N13 1 
HETATM 2380 N N24 . A1LV8 B 2 .   ? 15.666 -3.910  -5.426  1.00 58.01  ? 1001 A1LV8 A N24 1 
HETATM 2381 N N28 . A1LV8 B 2 .   ? 17.559 -0.468  -7.053  1.00 52.04  ? 1001 A1LV8 A N28 1 
HETATM 2382 O O20 . A1LV8 B 2 .   ? 17.453 -5.011  -8.564  1.00 58.36  ? 1001 A1LV8 A O20 1 
HETATM 2383 O O   . HOH   C 3 .   ? 40.649 0.922   -4.696  1.00 81.84  ? 1101 HOH   A O   1 
HETATM 2384 O O   . HOH   C 3 .   ? 6.275  -4.720  15.136  1.00 58.77  ? 1102 HOH   A O   1 
HETATM 2385 O O   . HOH   C 3 .   ? 32.124 4.297   -6.811  1.00 62.00  ? 1103 HOH   A O   1 
HETATM 2386 O O   . HOH   C 3 .   ? 13.898 8.326   -17.956 1.00 62.20  ? 1104 HOH   A O   1 
HETATM 2387 O O   . HOH   C 3 .   ? 12.304 9.636   19.522  1.00 55.81  ? 1105 HOH   A O   1 
HETATM 2388 O O   . HOH   C 3 .   ? 14.221 -5.643  -2.184  1.00 66.80  ? 1106 HOH   A O   1 
HETATM 2389 O O   . HOH   C 3 .   ? 21.526 6.286   -8.048  1.00 48.27  ? 1107 HOH   A O   1 
HETATM 2390 O O   . HOH   C 3 .   ? 28.657 20.352  -0.470  1.00 82.57  ? 1108 HOH   A O   1 
HETATM 2391 O O   . HOH   C 3 .   ? 27.762 18.299  -12.831 1.00 57.57  ? 1109 HOH   A O   1 
HETATM 2392 O O   . HOH   C 3 .   ? 10.482 15.522  5.243   1.00 64.86  ? 1110 HOH   A O   1 
HETATM 2393 O O   . HOH   C 3 .   ? 18.748 8.610   -2.375  1.00 48.23  ? 1111 HOH   A O   1 
HETATM 2394 O O   . HOH   C 3 .   ? 19.261 14.908  10.866  1.00 55.95  ? 1112 HOH   A O   1 
HETATM 2395 O O   . HOH   C 3 .   ? 14.388 13.966  -4.726  1.00 60.36  ? 1113 HOH   A O   1 
HETATM 2396 O O   . HOH   C 3 .   ? 15.619 10.375  8.183   1.00 52.86  ? 1114 HOH   A O   1 
HETATM 2397 O O   . HOH   C 3 .   ? 8.539  -3.285  16.154  1.00 44.43  ? 1115 HOH   A O   1 
HETATM 2398 O O   . HOH   C 3 .   ? 28.180 -3.639  -14.823 1.00 45.64  ? 1116 HOH   A O   1 
HETATM 2399 O O   . HOH   C 3 .   ? 12.494 4.264   11.959  1.00 45.51  ? 1117 HOH   A O   1 
HETATM 2400 O O   . HOH   C 3 .   ? 18.893 3.006   -25.774 1.00 55.57  ? 1118 HOH   A O   1 
HETATM 2401 O O   . HOH   C 3 .   ? 12.410 -9.451  -13.902 1.00 72.66  ? 1119 HOH   A O   1 
HETATM 2402 O O   . HOH   C 3 .   ? 10.655 6.446   11.501  1.00 45.28  ? 1120 HOH   A O   1 
HETATM 2403 O O   . HOH   C 3 .   ? 32.178 -0.075  -7.207  1.00 66.85  ? 1121 HOH   A O   1 
HETATM 2404 O O   . HOH   C 3 .   ? 29.182 -8.327  -9.108  1.00 74.34  ? 1122 HOH   A O   1 
HETATM 2405 O O   . HOH   C 3 .   ? -3.754 7.498   11.101  1.00 65.95  ? 1123 HOH   A O   1 
HETATM 2406 O O   . HOH   C 3 .   ? 0.303  11.930  15.813  1.00 63.04  ? 1124 HOH   A O   1 
HETATM 2407 O O   . HOH   C 3 .   ? 11.045 -4.935  17.358  1.00 56.46  ? 1125 HOH   A O   1 
HETATM 2408 O O   . HOH   C 3 .   ? 28.822 -7.762  -17.524 1.00 65.13  ? 1126 HOH   A O   1 
HETATM 2409 O O   . HOH   C 3 .   ? 15.228 -2.460  2.534   1.00 45.58  ? 1127 HOH   A O   1 
HETATM 2410 O O   . HOH   C 3 .   ? 14.760 6.050   -3.822  1.00 54.26  ? 1128 HOH   A O   1 
HETATM 2411 O O   . HOH   C 3 .   ? 30.816 -2.236  -23.140 1.00 52.76  ? 1129 HOH   A O   1 
HETATM 2412 O O   . HOH   C 3 .   ? 14.202 3.892   -9.020  1.00 56.78  ? 1130 HOH   A O   1 
HETATM 2413 O O   . HOH   C 3 .   ? 17.811 11.204  24.058  1.00 75.56  ? 1131 HOH   A O   1 
HETATM 2414 O O   . HOH   C 3 .   ? -4.384 2.961   10.934  1.00 62.86  ? 1132 HOH   A O   1 
HETATM 2415 O O   . HOH   C 3 .   ? 1.503  9.319   6.703   1.00 50.11  ? 1133 HOH   A O   1 
HETATM 2416 O O   . HOH   C 3 .   ? 20.803 6.121   22.215  1.00 66.07  ? 1134 HOH   A O   1 
HETATM 2417 O O   . HOH   C 3 .   ? 16.393 8.786   22.751  1.00 65.10  ? 1135 HOH   A O   1 
HETATM 2418 O O   . HOH   C 3 .   ? 16.005 7.275   4.820   1.00 54.12  ? 1136 HOH   A O   1 
HETATM 2419 O O   . HOH   C 3 .   ? 33.153 35.324  -5.106  1.00 47.15  ? 1137 HOH   A O   1 
HETATM 2420 O O   . HOH   C 3 .   ? 14.570 0.778   -3.690  1.00 51.89  ? 1138 HOH   A O   1 
HETATM 2421 O O   . HOH   C 3 .   ? 23.460 23.395  0.068   1.00 85.60  ? 1139 HOH   A O   1 
HETATM 2422 O O   . HOH   C 3 .   ? 8.881  4.043   -8.253  1.00 54.37  ? 1140 HOH   A O   1 
HETATM 2423 O O   . HOH   C 3 .   ? 31.805 8.783   -9.895  1.00 60.86  ? 1141 HOH   A O   1 
HETATM 2424 O O   . HOH   C 3 .   ? 39.770 39.838  -1.679  1.00 50.34  ? 1142 HOH   A O   1 
HETATM 2425 O O   . HOH   C 3 .   ? 10.845 -4.326  4.114   1.00 46.71  ? 1143 HOH   A O   1 
HETATM 2426 O O   . HOH   C 3 .   ? 13.975 1.663   15.944  1.00 54.96  ? 1144 HOH   A O   1 
HETATM 2427 O O   . HOH   C 3 .   ? 12.567 7.064   -19.972 1.00 61.13  ? 1145 HOH   A O   1 
HETATM 2428 O O   . HOH   C 3 .   ? 19.213 20.355  5.926   1.00 49.51  ? 1146 HOH   A O   1 
HETATM 2429 O O   . HOH   C 3 .   ? 30.440 6.372   -8.847  1.00 69.66  ? 1147 HOH   A O   1 
HETATM 2430 O O   . HOH   C 3 .   ? 9.654  1.350   -21.536 1.00 68.13  ? 1148 HOH   A O   1 
HETATM 2431 O O   . HOH   C 3 .   ? 16.839 19.872  4.551   1.00 56.50  ? 1149 HOH   A O   1 
HETATM 2432 O O   . HOH   C 3 .   ? 32.717 6.962   -10.780 1.00 59.52  ? 1150 HOH   A O   1 
HETATM 2433 O O   . HOH   C 3 .   ? 8.070  17.082  -2.384  1.00 64.04  ? 1151 HOH   A O   1 
HETATM 2434 O O   . HOH   C 3 .   ? 15.588 18.712  2.355   1.00 60.08  ? 1152 HOH   A O   1 
HETATM 2435 O O   . HOH   C 3 .   ? 9.234  -13.044 14.316  1.00 70.48  ? 1153 HOH   A O   1 
HETATM 2436 O O   . HOH   C 3 .   ? 29.729 -15.182 -10.804 1.00 90.60  ? 1154 HOH   A O   1 
HETATM 2437 O O   . HOH   C 3 .   ? 8.332  -10.743 12.606  1.00 76.56  ? 1155 HOH   A O   1 
# 
