data_8Z14
# 
_entry.id   8Z14 
# 
_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   8Z14         pdb_00008z14 10.2210/pdb8z14/pdb 
WWPDB D_1300046771 ?            ?                   
# 
_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       2025-02-19 
# 
_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                        8Z14 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 pengm@sdu.edu.cn          Ming     Peng ? 'principal investigator/group leader' 0000-0003-2819-046X 
3 202221063@mail.sdu.edu.cn Qiaoling Wu   ? 'principal investigator/group leader' 0009-0006-9182-6183 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Peng, M.' 1 0000-0003-2819-046X 
'Wu, Q.L.' 2 0009-0006-9182-6183 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Catalysis' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2155-5435 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            14 
_citation.language                  ? 
_citation.page_first                17780 
_citation.page_last                 17793 
_citation.title                     
'Bacterial Biosynthesis of Nitrile-Containing Natural Products: Basis for Recognition of Diversified Substrates' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acscatal.4c06581 
_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 'Peng, M.'   1 ? 
primary 'Wu, Q.'     2 ? 
primary 'Ma, L.'     3 ? 
primary 'Teng, Z.J.' 4 ? 
primary 'Hou, X.'    5 ? 
primary 'Zhu, H.'    6 ? 
primary 'Ju, J.'     7 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Flavin-dependent monooxygenase'                                             46858.883 1  ? ? ? 
;Sequence reference for Streptomyces ardesiacus (285564) is not available in UniProt at the time of biocuration. Current sequence reference is from UniProt ID A0A7T1BYC5. GenBank Accession Number: PP691700 protein_id="WZN32524.1.
;
2 non-polymer syn '(2~{S})-2-azanyl-3-[6-(3-methylbut-2-enyl)-1~{H}-indol-3-yl]propanoic acid' 272.342   1  ? ? ? ? 
3 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE'                                                785.550   1  ? ? ? ? 
4 water       nat water                                                                        18.015    38 ? ? ? ? 
# 
_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       
;MRVCVIGAGLSGLAVGHALKERGISFVCLEKAPDVGGIWRQPGAGERGPGYRTLHLNTAKQLTGYADFPMPDAYPLYPRH
SQVAAYLRSFAEWAGLLDHVELRTEVVSVRQDADGPWTVVSRGADGAQVSRRFEQVVVASGHHNEPALPDPLPAGADSFA
GTILHSLDYRDGGDFAGRRVVVVGLGASAVDIAADLSRHAERTLLSVRRGLHIVPKQLFGMSVDEIAEAPWWNEMSFDER
RRWVEQALLVARGRLSDYGLPEPDHPVFSSATTLSDEILSRIRHGAVTPKPAIASFDGDRVVFTDGTSEPADAVVYCTGF
HMTFPFLPAGCPMSADGSVELYRRVVPADRPGLYFVGLVRPVGAITRLVEAQAEWVARLVDGAAVLPAADQMREEIGTYL
TGIVQRYGRTEGASIQVDVGPYLAEFRESLPV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MRVCVIGAGLSGLAVGHALKERGISFVCLEKAPDVGGIWRQPGAGERGPGYRTLHLNTAKQLTGYADFPMPDAYPLYPRH
SQVAAYLRSFAEWAGLLDHVELRTEVVSVRQDADGPWTVVSRGADGAQVSRRFEQVVVASGHHNEPALPDPLPAGADSFA
GTILHSLDYRDGGDFAGRRVVVVGLGASAVDIAADLSRHAERTLLSVRRGLHIVPKQLFGMSVDEIAEAPWWNEMSFDER
RRWVEQALLVARGRLSDYGLPEPDHPVFSSATTLSDEILSRIRHGAVTPKPAIASFDGDRVVFTDGTSEPADAVVYCTGF
HMTFPFLPAGCPMSADGSVELYRRVVPADRPGLYFVGLVRPVGAITRLVEAQAEWVARLVDGAAVLPAADQMREEIGTYL
TGIVQRYGRTEGASIQVDVGPYLAEFRESLPV
;
_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 '(2~{S})-2-azanyl-3-[6-(3-methylbut-2-enyl)-1~{H}-indol-3-yl]propanoic acid' A1D7R 
3 'FLAVIN-ADENINE DINUCLEOTIDE'                                                FAD   
4 water                                                                        HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ARG n 
1 3   VAL n 
1 4   CYS n 
1 5   VAL n 
1 6   ILE n 
1 7   GLY n 
1 8   ALA n 
1 9   GLY n 
1 10  LEU n 
1 11  SER n 
1 12  GLY n 
1 13  LEU n 
1 14  ALA n 
1 15  VAL n 
1 16  GLY n 
1 17  HIS n 
1 18  ALA n 
1 19  LEU n 
1 20  LYS n 
1 21  GLU n 
1 22  ARG n 
1 23  GLY n 
1 24  ILE n 
1 25  SER n 
1 26  PHE n 
1 27  VAL n 
1 28  CYS n 
1 29  LEU n 
1 30  GLU n 
1 31  LYS n 
1 32  ALA n 
1 33  PRO n 
1 34  ASP n 
1 35  VAL n 
1 36  GLY n 
1 37  GLY n 
1 38  ILE n 
1 39  TRP n 
1 40  ARG n 
1 41  GLN n 
1 42  PRO n 
1 43  GLY n 
1 44  ALA n 
1 45  GLY n 
1 46  GLU n 
1 47  ARG n 
1 48  GLY n 
1 49  PRO n 
1 50  GLY n 
1 51  TYR n 
1 52  ARG n 
1 53  THR n 
1 54  LEU n 
1 55  HIS n 
1 56  LEU n 
1 57  ASN n 
1 58  THR n 
1 59  ALA n 
1 60  LYS n 
1 61  GLN n 
1 62  LEU n 
1 63  THR n 
1 64  GLY n 
1 65  TYR n 
1 66  ALA n 
1 67  ASP n 
1 68  PHE n 
1 69  PRO n 
1 70  MET n 
1 71  PRO n 
1 72  ASP n 
1 73  ALA n 
1 74  TYR n 
1 75  PRO n 
1 76  LEU n 
1 77  TYR n 
1 78  PRO n 
1 79  ARG n 
1 80  HIS n 
1 81  SER n 
1 82  GLN n 
1 83  VAL n 
1 84  ALA n 
1 85  ALA n 
1 86  TYR n 
1 87  LEU n 
1 88  ARG n 
1 89  SER n 
1 90  PHE n 
1 91  ALA n 
1 92  GLU n 
1 93  TRP n 
1 94  ALA n 
1 95  GLY n 
1 96  LEU n 
1 97  LEU n 
1 98  ASP n 
1 99  HIS n 
1 100 VAL n 
1 101 GLU n 
1 102 LEU n 
1 103 ARG n 
1 104 THR n 
1 105 GLU n 
1 106 VAL n 
1 107 VAL n 
1 108 SER n 
1 109 VAL n 
1 110 ARG n 
1 111 GLN n 
1 112 ASP n 
1 113 ALA n 
1 114 ASP n 
1 115 GLY n 
1 116 PRO n 
1 117 TRP n 
1 118 THR n 
1 119 VAL n 
1 120 VAL n 
1 121 SER n 
1 122 ARG n 
1 123 GLY n 
1 124 ALA n 
1 125 ASP n 
1 126 GLY n 
1 127 ALA n 
1 128 GLN n 
1 129 VAL n 
1 130 SER n 
1 131 ARG n 
1 132 ARG n 
1 133 PHE n 
1 134 GLU n 
1 135 GLN n 
1 136 VAL n 
1 137 VAL n 
1 138 VAL n 
1 139 ALA n 
1 140 SER n 
1 141 GLY n 
1 142 HIS n 
1 143 HIS n 
1 144 ASN n 
1 145 GLU n 
1 146 PRO n 
1 147 ALA n 
1 148 LEU n 
1 149 PRO n 
1 150 ASP n 
1 151 PRO n 
1 152 LEU n 
1 153 PRO n 
1 154 ALA n 
1 155 GLY n 
1 156 ALA n 
1 157 ASP n 
1 158 SER n 
1 159 PHE n 
1 160 ALA n 
1 161 GLY n 
1 162 THR n 
1 163 ILE n 
1 164 LEU n 
1 165 HIS n 
1 166 SER n 
1 167 LEU n 
1 168 ASP n 
1 169 TYR n 
1 170 ARG n 
1 171 ASP n 
1 172 GLY n 
1 173 GLY n 
1 174 ASP n 
1 175 PHE n 
1 176 ALA n 
1 177 GLY n 
1 178 ARG n 
1 179 ARG n 
1 180 VAL n 
1 181 VAL n 
1 182 VAL n 
1 183 VAL n 
1 184 GLY n 
1 185 LEU n 
1 186 GLY n 
1 187 ALA n 
1 188 SER n 
1 189 ALA n 
1 190 VAL n 
1 191 ASP n 
1 192 ILE n 
1 193 ALA n 
1 194 ALA n 
1 195 ASP n 
1 196 LEU n 
1 197 SER n 
1 198 ARG n 
1 199 HIS n 
1 200 ALA n 
1 201 GLU n 
1 202 ARG n 
1 203 THR n 
1 204 LEU n 
1 205 LEU n 
1 206 SER n 
1 207 VAL n 
1 208 ARG n 
1 209 ARG n 
1 210 GLY n 
1 211 LEU n 
1 212 HIS n 
1 213 ILE n 
1 214 VAL n 
1 215 PRO n 
1 216 LYS n 
1 217 GLN n 
1 218 LEU n 
1 219 PHE n 
1 220 GLY n 
1 221 MET n 
1 222 SER n 
1 223 VAL n 
1 224 ASP n 
1 225 GLU n 
1 226 ILE n 
1 227 ALA n 
1 228 GLU n 
1 229 ALA n 
1 230 PRO n 
1 231 TRP n 
1 232 TRP n 
1 233 ASN n 
1 234 GLU n 
1 235 MET n 
1 236 SER n 
1 237 PHE n 
1 238 ASP n 
1 239 GLU n 
1 240 ARG n 
1 241 ARG n 
1 242 ARG n 
1 243 TRP n 
1 244 VAL n 
1 245 GLU n 
1 246 GLN n 
1 247 ALA n 
1 248 LEU n 
1 249 LEU n 
1 250 VAL n 
1 251 ALA n 
1 252 ARG n 
1 253 GLY n 
1 254 ARG n 
1 255 LEU n 
1 256 SER n 
1 257 ASP n 
1 258 TYR n 
1 259 GLY n 
1 260 LEU n 
1 261 PRO n 
1 262 GLU n 
1 263 PRO n 
1 264 ASP n 
1 265 HIS n 
1 266 PRO n 
1 267 VAL n 
1 268 PHE n 
1 269 SER n 
1 270 SER n 
1 271 ALA n 
1 272 THR n 
1 273 THR n 
1 274 LEU n 
1 275 SER n 
1 276 ASP n 
1 277 GLU n 
1 278 ILE n 
1 279 LEU n 
1 280 SER n 
1 281 ARG n 
1 282 ILE n 
1 283 ARG n 
1 284 HIS n 
1 285 GLY n 
1 286 ALA n 
1 287 VAL n 
1 288 THR n 
1 289 PRO n 
1 290 LYS n 
1 291 PRO n 
1 292 ALA n 
1 293 ILE n 
1 294 ALA n 
1 295 SER n 
1 296 PHE n 
1 297 ASP n 
1 298 GLY n 
1 299 ASP n 
1 300 ARG n 
1 301 VAL n 
1 302 VAL n 
1 303 PHE n 
1 304 THR n 
1 305 ASP n 
1 306 GLY n 
1 307 THR n 
1 308 SER n 
1 309 GLU n 
1 310 PRO n 
1 311 ALA n 
1 312 ASP n 
1 313 ALA n 
1 314 VAL n 
1 315 VAL n 
1 316 TYR n 
1 317 CYS n 
1 318 THR n 
1 319 GLY n 
1 320 PHE n 
1 321 HIS n 
1 322 MET n 
1 323 THR n 
1 324 PHE n 
1 325 PRO n 
1 326 PHE n 
1 327 LEU n 
1 328 PRO n 
1 329 ALA n 
1 330 GLY n 
1 331 CYS n 
1 332 PRO n 
1 333 MET n 
1 334 SER n 
1 335 ALA n 
1 336 ASP n 
1 337 GLY n 
1 338 SER n 
1 339 VAL n 
1 340 GLU n 
1 341 LEU n 
1 342 TYR n 
1 343 ARG n 
1 344 ARG n 
1 345 VAL n 
1 346 VAL n 
1 347 PRO n 
1 348 ALA n 
1 349 ASP n 
1 350 ARG n 
1 351 PRO n 
1 352 GLY n 
1 353 LEU n 
1 354 TYR n 
1 355 PHE n 
1 356 VAL n 
1 357 GLY n 
1 358 LEU n 
1 359 VAL n 
1 360 ARG n 
1 361 PRO n 
1 362 VAL n 
1 363 GLY n 
1 364 ALA n 
1 365 ILE n 
1 366 THR n 
1 367 ARG n 
1 368 LEU n 
1 369 VAL n 
1 370 GLU n 
1 371 ALA n 
1 372 GLN n 
1 373 ALA n 
1 374 GLU n 
1 375 TRP n 
1 376 VAL n 
1 377 ALA n 
1 378 ARG n 
1 379 LEU n 
1 380 VAL n 
1 381 ASP n 
1 382 GLY n 
1 383 ALA n 
1 384 ALA n 
1 385 VAL n 
1 386 LEU n 
1 387 PRO n 
1 388 ALA n 
1 389 ALA n 
1 390 ASP n 
1 391 GLN n 
1 392 MET n 
1 393 ARG n 
1 394 GLU n 
1 395 GLU n 
1 396 ILE n 
1 397 GLY n 
1 398 THR n 
1 399 TYR n 
1 400 LEU n 
1 401 THR n 
1 402 GLY n 
1 403 ILE n 
1 404 VAL n 
1 405 GLN n 
1 406 ARG n 
1 407 TYR n 
1 408 GLY n 
1 409 ARG n 
1 410 THR n 
1 411 GLU n 
1 412 GLY n 
1 413 ALA n 
1 414 SER n 
1 415 ILE n 
1 416 GLN n 
1 417 VAL n 
1 418 ASP n 
1 419 VAL n 
1 420 GLY n 
1 421 PRO n 
1 422 TYR n 
1 423 LEU n 
1 424 ALA n 
1 425 GLU n 
1 426 PHE n 
1 427 ARG n 
1 428 GLU n 
1 429 SER n 
1 430 LEU n 
1 431 PRO n 
1 432 VAL 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                   432 
_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      'Streptomyces ardesiacus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     285564 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1D7R 'L-peptide linking' n '(2~{S})-2-azanyl-3-[6-(3-methylbut-2-enyl)-1~{H}-indol-3-yl]propanoic acid' 
6-dimethylallyl-L-tryptophan 'C16 H20 N2 O2'     272.342 
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 
FAD   non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE'                                                ? 'C27 H33 N9 O15 P2' 
785.550 
GLN   'L-peptide linking' y GLUTAMINE                                                                    ? 'C5 H10 N2 O3'      
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                              ? 'C5 H9 N O4'        
147.129 
GLY   'peptide linking'   y GLYCINE                                                                      ? 'C2 H5 N O2'        
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                    ? 'C6 H10 N3 O2 1'    
156.162 
HOH   non-polymer         . WATER                                                                        ? 'H2 O'              
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                   ? 'C6 H13 N O2'       
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                      ? 'C6 H13 N O2'       
131.173 
LYS   'L-peptide linking' y LYSINE                                                                       ? 'C6 H15 N2 O2 1'    
147.195 
MET   'L-peptide linking' y METHIONINE                                                                   ? 'C5 H11 N O2 S'     
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                ? 'C9 H11 N O2'       
165.189 
PRO   'L-peptide linking' y PROLINE                                                                      ? 'C5 H9 N O2'        
115.130 
SER   'L-peptide linking' y SERINE                                                                       ? 'C3 H7 N O3'        
105.093 
THR   'L-peptide linking' y THREONINE                                                                    ? 'C4 H9 N O3'        
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                   ? 'C11 H12 N2 O2'     
204.225 
TYR   'L-peptide linking' y TYROSINE                                                                     ? 'C9 H11 N O3'       
181.189 
VAL   'L-peptide linking' y VALINE                                                                       ? 'C5 H11 N O2'       
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   ARG 2   2   2   ARG ARG A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   CYS 4   4   4   CYS CYS A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   GLY 7   7   7   GLY GLY A . n 
A 1 8   ALA 8   8   8   ALA ALA A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  SER 11  11  11  SER SER A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  ALA 14  14  14  ALA ALA A . n 
A 1 15  VAL 15  15  15  VAL VAL A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  LYS 20  20  20  LYS LYS A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  ARG 22  22  22  ARG ARG A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  VAL 27  27  27  VAL VAL A . n 
A 1 28  CYS 28  28  28  CYS CYS A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  PRO 33  33  33  PRO PRO A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  ILE 38  38  38  ILE ILE A . n 
A 1 39  TRP 39  39  39  TRP TRP A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  GLN 41  41  41  GLN GLN A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  GLU 46  46  46  GLU GLU A . n 
A 1 47  ARG 47  47  47  ARG ARG A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  PRO 49  49  49  PRO PRO A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ARG 52  52  52  ARG ARG A . n 
A 1 53  THR 53  53  53  THR THR A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  HIS 55  55  55  HIS HIS A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  ASN 57  57  57  ASN ASN A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  LYS 60  60  60  LYS LYS A . n 
A 1 61  GLN 61  61  61  GLN GLN A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  TYR 65  65  65  TYR TYR A . n 
A 1 66  ALA 66  66  66  ALA ALA A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  PHE 68  68  68  PHE PHE A . n 
A 1 69  PRO 69  69  69  PRO PRO A . n 
A 1 70  MET 70  70  70  MET MET A . n 
A 1 71  PRO 71  71  71  PRO PRO A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  TYR 74  74  74  TYR TYR A . n 
A 1 75  PRO 75  75  75  PRO PRO A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  TYR 77  77  77  TYR TYR A . n 
A 1 78  PRO 78  78  78  PRO PRO A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  GLN 82  82  82  GLN GLN A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  ALA 85  85  85  ALA ALA A . n 
A 1 86  TYR 86  86  86  TYR TYR A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  ARG 88  88  88  ARG ARG A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  PHE 90  90  90  PHE PHE A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  GLU 92  92  92  GLU GLU A . n 
A 1 93  TRP 93  93  93  TRP TRP A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  LEU 96  96  96  LEU LEU A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  HIS 99  99  99  HIS HIS A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 GLU 101 101 101 GLU GLU A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 ARG 103 103 103 ARG ARG A . n 
A 1 104 THR 104 104 104 THR THR A . n 
A 1 105 GLU 105 105 105 GLU GLU A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ARG 110 110 110 ARG ARG A . n 
A 1 111 GLN 111 111 111 GLN GLN A . n 
A 1 112 ASP 112 112 112 ASP ASP A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 ASP 114 114 114 ASP ASP A . n 
A 1 115 GLY 115 115 115 GLY GLY A . n 
A 1 116 PRO 116 116 116 PRO PRO A . n 
A 1 117 TRP 117 117 117 TRP TRP A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 ARG 122 122 122 ARG ARG A . n 
A 1 123 GLY 123 123 123 GLY GLY A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 GLY 126 126 126 GLY GLY A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 SER 130 130 130 SER SER A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 ARG 132 132 132 ARG ARG A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 GLU 134 134 134 GLU GLU A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 VAL 136 136 136 VAL VAL A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 ALA 139 139 139 ALA ALA A . n 
A 1 140 SER 140 140 140 SER SER A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 HIS 142 142 142 HIS HIS A . n 
A 1 143 HIS 143 143 143 HIS HIS A . n 
A 1 144 ASN 144 144 144 ASN ASN A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 PRO 146 146 146 PRO PRO A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 PRO 149 149 149 PRO PRO A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 PRO 151 151 151 PRO PRO A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 ALA 156 156 156 ALA ALA A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 ALA 160 160 160 ALA ALA A . n 
A 1 161 GLY 161 161 161 GLY GLY A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 ILE 163 163 163 ILE ILE A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 HIS 165 165 165 HIS HIS A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 ASP 168 168 168 ASP ASP A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 ARG 170 170 170 ARG ARG A . n 
A 1 171 ASP 171 171 171 ASP ASP A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 ASP 174 174 174 ASP ASP A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 ALA 176 176 176 ALA ALA A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 ARG 178 178 178 ARG ARG A . n 
A 1 179 ARG 179 179 179 ARG ARG A . n 
A 1 180 VAL 180 180 180 VAL VAL A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 VAL 183 183 183 VAL VAL A . n 
A 1 184 GLY 184 184 184 GLY GLY A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 GLY 186 186 186 GLY GLY A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 SER 188 188 188 SER SER A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 ASP 191 191 191 ASP ASP A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 LEU 196 196 196 LEU LEU A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 ARG 198 198 198 ARG ARG A . n 
A 1 199 HIS 199 199 199 HIS HIS A . n 
A 1 200 ALA 200 200 200 ALA ALA A . n 
A 1 201 GLU 201 201 201 GLU GLU A . n 
A 1 202 ARG 202 202 202 ARG ARG A . n 
A 1 203 THR 203 203 203 THR THR A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 ARG 208 208 208 ARG ARG A . n 
A 1 209 ARG 209 209 209 ARG ARG A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 HIS 212 212 212 HIS HIS A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 VAL 214 214 214 VAL VAL A . n 
A 1 215 PRO 215 215 215 PRO PRO A . n 
A 1 216 LYS 216 216 216 LYS LYS A . n 
A 1 217 GLN 217 217 217 GLN GLN A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 GLY 220 220 220 GLY GLY A . n 
A 1 221 MET 221 221 221 MET MET A . n 
A 1 222 SER 222 222 222 SER SER A . n 
A 1 223 VAL 223 223 223 VAL VAL A . n 
A 1 224 ASP 224 224 224 ASP ASP A . n 
A 1 225 GLU 225 225 225 GLU GLU A . n 
A 1 226 ILE 226 226 226 ILE ILE A . n 
A 1 227 ALA 227 227 227 ALA ALA A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 ALA 229 229 229 ALA ALA A . n 
A 1 230 PRO 230 230 230 PRO PRO A . n 
A 1 231 TRP 231 231 231 TRP TRP A . n 
A 1 232 TRP 232 232 232 TRP TRP A . n 
A 1 233 ASN 233 233 233 ASN ASN A . n 
A 1 234 GLU 234 234 234 GLU GLU A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 SER 236 236 236 SER SER A . n 
A 1 237 PHE 237 237 237 PHE PHE A . n 
A 1 238 ASP 238 238 238 ASP ASP A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 ARG 240 240 240 ARG ARG A . n 
A 1 241 ARG 241 241 241 ARG ARG A . n 
A 1 242 ARG 242 242 242 ARG ARG A . n 
A 1 243 TRP 243 243 243 TRP TRP A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 GLU 245 245 245 GLU GLU A . n 
A 1 246 GLN 246 246 246 GLN GLN A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 LEU 249 249 249 LEU LEU A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 ALA 251 251 251 ALA ALA A . n 
A 1 252 ARG 252 252 252 ARG ARG A . n 
A 1 253 GLY 253 253 253 GLY GLY A . n 
A 1 254 ARG 254 254 254 ARG ARG A . n 
A 1 255 LEU 255 255 255 LEU LEU A . n 
A 1 256 SER 256 256 256 SER SER A . n 
A 1 257 ASP 257 257 257 ASP ASP A . n 
A 1 258 TYR 258 258 258 TYR TYR A . n 
A 1 259 GLY 259 259 259 GLY GLY A . n 
A 1 260 LEU 260 260 260 LEU LEU A . n 
A 1 261 PRO 261 261 261 PRO PRO A . n 
A 1 262 GLU 262 262 262 GLU GLU A . n 
A 1 263 PRO 263 263 263 PRO PRO A . n 
A 1 264 ASP 264 264 264 ASP ASP A . n 
A 1 265 HIS 265 265 265 HIS HIS A . n 
A 1 266 PRO 266 266 266 PRO PRO A . n 
A 1 267 VAL 267 267 267 VAL VAL A . n 
A 1 268 PHE 268 268 268 PHE PHE A . n 
A 1 269 SER 269 269 269 SER SER A . n 
A 1 270 SER 270 270 270 SER SER A . n 
A 1 271 ALA 271 271 271 ALA ALA A . n 
A 1 272 THR 272 272 272 THR THR A . n 
A 1 273 THR 273 273 273 THR THR A . n 
A 1 274 LEU 274 274 274 LEU LEU A . n 
A 1 275 SER 275 275 275 SER SER A . n 
A 1 276 ASP 276 276 276 ASP ASP A . n 
A 1 277 GLU 277 277 277 GLU GLU A . n 
A 1 278 ILE 278 278 278 ILE ILE A . n 
A 1 279 LEU 279 279 279 LEU LEU A . n 
A 1 280 SER 280 280 280 SER SER A . n 
A 1 281 ARG 281 281 281 ARG ARG A . n 
A 1 282 ILE 282 282 282 ILE ILE A . n 
A 1 283 ARG 283 283 283 ARG ARG A . n 
A 1 284 HIS 284 284 284 HIS HIS A . n 
A 1 285 GLY 285 285 285 GLY GLY A . n 
A 1 286 ALA 286 286 286 ALA ALA A . n 
A 1 287 VAL 287 287 287 VAL VAL A . n 
A 1 288 THR 288 288 288 THR THR A . n 
A 1 289 PRO 289 289 289 PRO PRO A . n 
A 1 290 LYS 290 290 290 LYS LYS A . n 
A 1 291 PRO 291 291 291 PRO PRO A . n 
A 1 292 ALA 292 292 292 ALA ALA A . n 
A 1 293 ILE 293 293 293 ILE ILE A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 SER 295 295 295 SER SER A . n 
A 1 296 PHE 296 296 296 PHE PHE A . n 
A 1 297 ASP 297 297 297 ASP ASP A . n 
A 1 298 GLY 298 298 298 GLY GLY A . n 
A 1 299 ASP 299 299 299 ASP ASP A . n 
A 1 300 ARG 300 300 300 ARG ARG A . n 
A 1 301 VAL 301 301 301 VAL VAL A . n 
A 1 302 VAL 302 302 302 VAL VAL A . n 
A 1 303 PHE 303 303 303 PHE PHE A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 ASP 305 305 305 ASP ASP A . n 
A 1 306 GLY 306 306 306 GLY GLY A . n 
A 1 307 THR 307 307 307 THR THR A . n 
A 1 308 SER 308 308 308 SER SER A . n 
A 1 309 GLU 309 309 309 GLU GLU A . n 
A 1 310 PRO 310 310 310 PRO PRO A . n 
A 1 311 ALA 311 311 311 ALA ALA A . n 
A 1 312 ASP 312 312 312 ASP ASP A . n 
A 1 313 ALA 313 313 313 ALA ALA A . n 
A 1 314 VAL 314 314 314 VAL VAL A . n 
A 1 315 VAL 315 315 315 VAL VAL A . n 
A 1 316 TYR 316 316 316 TYR TYR A . n 
A 1 317 CYS 317 317 317 CYS CYS A . n 
A 1 318 THR 318 318 318 THR THR A . n 
A 1 319 GLY 319 319 319 GLY GLY A . n 
A 1 320 PHE 320 320 320 PHE PHE A . n 
A 1 321 HIS 321 321 321 HIS HIS A . n 
A 1 322 MET 322 322 322 MET MET A . n 
A 1 323 THR 323 323 323 THR THR A . n 
A 1 324 PHE 324 324 324 PHE PHE A . n 
A 1 325 PRO 325 325 325 PRO PRO A . n 
A 1 326 PHE 326 326 326 PHE PHE A . n 
A 1 327 LEU 327 327 327 LEU LEU A . n 
A 1 328 PRO 328 328 328 PRO PRO A . n 
A 1 329 ALA 329 329 329 ALA ALA A . n 
A 1 330 GLY 330 330 330 GLY GLY A . n 
A 1 331 CYS 331 331 331 CYS CYS A . n 
A 1 332 PRO 332 332 332 PRO PRO A . n 
A 1 333 MET 333 333 333 MET MET A . n 
A 1 334 SER 334 334 334 SER SER A . n 
A 1 335 ALA 335 335 335 ALA ALA A . n 
A 1 336 ASP 336 336 336 ASP ASP A . n 
A 1 337 GLY 337 337 337 GLY GLY A . n 
A 1 338 SER 338 338 338 SER SER A . n 
A 1 339 VAL 339 339 339 VAL VAL A . n 
A 1 340 GLU 340 340 340 GLU GLU A . n 
A 1 341 LEU 341 341 341 LEU LEU A . n 
A 1 342 TYR 342 342 342 TYR TYR A . n 
A 1 343 ARG 343 343 343 ARG ARG A . n 
A 1 344 ARG 344 344 344 ARG ARG A . n 
A 1 345 VAL 345 345 345 VAL VAL A . n 
A 1 346 VAL 346 346 346 VAL VAL A . n 
A 1 347 PRO 347 347 347 PRO PRO A . n 
A 1 348 ALA 348 348 348 ALA ALA A . n 
A 1 349 ASP 349 349 349 ASP ASP A . n 
A 1 350 ARG 350 350 350 ARG ARG A . n 
A 1 351 PRO 351 351 351 PRO PRO A . n 
A 1 352 GLY 352 352 352 GLY GLY A . n 
A 1 353 LEU 353 353 353 LEU LEU A . n 
A 1 354 TYR 354 354 354 TYR TYR A . n 
A 1 355 PHE 355 355 355 PHE PHE A . n 
A 1 356 VAL 356 356 356 VAL VAL A . n 
A 1 357 GLY 357 357 357 GLY GLY A . n 
A 1 358 LEU 358 358 358 LEU LEU A . n 
A 1 359 VAL 359 359 359 VAL VAL A . n 
A 1 360 ARG 360 360 360 ARG ARG A . n 
A 1 361 PRO 361 361 361 PRO PRO A . n 
A 1 362 VAL 362 362 362 VAL VAL A . n 
A 1 363 GLY 363 363 363 GLY GLY A . n 
A 1 364 ALA 364 364 364 ALA ALA A . n 
A 1 365 ILE 365 365 365 ILE ILE A . n 
A 1 366 THR 366 366 366 THR THR A . n 
A 1 367 ARG 367 367 367 ARG ARG A . n 
A 1 368 LEU 368 368 368 LEU LEU A . n 
A 1 369 VAL 369 369 369 VAL VAL A . n 
A 1 370 GLU 370 370 370 GLU GLU A . n 
A 1 371 ALA 371 371 371 ALA ALA A . n 
A 1 372 GLN 372 372 372 GLN GLN A . n 
A 1 373 ALA 373 373 373 ALA ALA A . n 
A 1 374 GLU 374 374 374 GLU GLU A . n 
A 1 375 TRP 375 375 375 TRP TRP A . n 
A 1 376 VAL 376 376 376 VAL VAL A . n 
A 1 377 ALA 377 377 377 ALA ALA A . n 
A 1 378 ARG 378 378 378 ARG ARG A . n 
A 1 379 LEU 379 379 379 LEU LEU A . n 
A 1 380 VAL 380 380 380 VAL VAL A . n 
A 1 381 ASP 381 381 381 ASP ASP A . n 
A 1 382 GLY 382 382 382 GLY GLY A . n 
A 1 383 ALA 383 383 383 ALA ALA A . n 
A 1 384 ALA 384 384 384 ALA ALA A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 LEU 386 386 386 LEU LEU A . n 
A 1 387 PRO 387 387 387 PRO PRO A . n 
A 1 388 ALA 388 388 388 ALA ALA A . n 
A 1 389 ALA 389 389 389 ALA ALA A . n 
A 1 390 ASP 390 390 390 ASP ASP A . n 
A 1 391 GLN 391 391 391 GLN GLN A . n 
A 1 392 MET 392 392 392 MET MET A . n 
A 1 393 ARG 393 393 393 ARG ARG A . n 
A 1 394 GLU 394 394 394 GLU GLU A . n 
A 1 395 GLU 395 395 395 GLU GLU A . n 
A 1 396 ILE 396 396 396 ILE ILE A . n 
A 1 397 GLY 397 397 397 GLY GLY A . n 
A 1 398 THR 398 398 398 THR THR A . n 
A 1 399 TYR 399 399 399 TYR TYR A . n 
A 1 400 LEU 400 400 400 LEU LEU A . n 
A 1 401 THR 401 401 401 THR THR A . n 
A 1 402 GLY 402 402 402 GLY GLY A . n 
A 1 403 ILE 403 403 403 ILE ILE A . n 
A 1 404 VAL 404 404 404 VAL VAL A . n 
A 1 405 GLN 405 405 405 GLN GLN A . n 
A 1 406 ARG 406 406 406 ARG ARG A . n 
A 1 407 TYR 407 407 407 TYR TYR A . n 
A 1 408 GLY 408 408 408 GLY GLY A . n 
A 1 409 ARG 409 409 409 ARG ARG A . n 
A 1 410 THR 410 410 410 THR THR A . n 
A 1 411 GLU 411 411 411 GLU GLU A . n 
A 1 412 GLY 412 412 412 GLY GLY A . n 
A 1 413 ALA 413 413 413 ALA ALA A . n 
A 1 414 SER 414 414 414 SER SER A . n 
A 1 415 ILE 415 415 415 ILE ILE A . n 
A 1 416 GLN 416 416 416 GLN GLN A . n 
A 1 417 VAL 417 417 417 VAL VAL A . n 
A 1 418 ASP 418 418 418 ASP ASP A . n 
A 1 419 VAL 419 419 419 VAL VAL A . n 
A 1 420 GLY 420 420 420 GLY GLY A . n 
A 1 421 PRO 421 421 421 PRO PRO A . n 
A 1 422 TYR 422 422 422 TYR TYR A . n 
A 1 423 LEU 423 423 423 LEU LEU A . n 
A 1 424 ALA 424 424 424 ALA ALA A . n 
A 1 425 GLU 425 425 425 GLU GLU A . n 
A 1 426 PHE 426 426 426 PHE PHE A . n 
A 1 427 ARG 427 427 ?   ?   ?   A . n 
A 1 428 GLU 428 428 ?   ?   ?   A . n 
A 1 429 SER 429 429 ?   ?   ?   A . n 
A 1 430 LEU 430 430 ?   ?   ?   A . n 
A 1 431 PRO 431 431 ?   ?   ?   A . n 
A 1 432 VAL 432 432 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1D7R ? ? A1D7R ? ? 'SUBJECT OF INVESTIGATION' ? 
2 FAD   ? ? FAD   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1D7R 1  501 501  A1D7R 6DM A . 
C 3 FAD   1  502 1449 FAD   FAD A . 
D 4 HOH   1  601 39   HOH   HOH A . 
D 4 HOH   2  602 34   HOH   HOH A . 
D 4 HOH   3  603 18   HOH   HOH A . 
D 4 HOH   4  604 35   HOH   HOH A . 
D 4 HOH   5  605 12   HOH   HOH A . 
D 4 HOH   6  606 2    HOH   HOH A . 
D 4 HOH   7  607 27   HOH   HOH A . 
D 4 HOH   8  608 5    HOH   HOH A . 
D 4 HOH   9  609 7    HOH   HOH A . 
D 4 HOH   10 610 46   HOH   HOH A . 
D 4 HOH   11 611 19   HOH   HOH A . 
D 4 HOH   12 612 45   HOH   HOH A . 
D 4 HOH   13 613 11   HOH   HOH A . 
D 4 HOH   14 614 33   HOH   HOH A . 
D 4 HOH   15 615 37   HOH   HOH A . 
D 4 HOH   16 616 21   HOH   HOH A . 
D 4 HOH   17 617 4    HOH   HOH A . 
D 4 HOH   18 618 41   HOH   HOH A . 
D 4 HOH   19 619 14   HOH   HOH A . 
D 4 HOH   20 620 13   HOH   HOH A . 
D 4 HOH   21 621 10   HOH   HOH A . 
D 4 HOH   22 622 26   HOH   HOH A . 
D 4 HOH   23 623 28   HOH   HOH A . 
D 4 HOH   24 624 8    HOH   HOH A . 
D 4 HOH   25 625 36   HOH   HOH A . 
D 4 HOH   26 626 42   HOH   HOH A . 
D 4 HOH   27 627 6    HOH   HOH A . 
D 4 HOH   28 628 3    HOH   HOH A . 
D 4 HOH   29 629 24   HOH   HOH A . 
D 4 HOH   30 630 9    HOH   HOH A . 
D 4 HOH   31 631 1    HOH   HOH A . 
D 4 HOH   32 632 44   HOH   HOH A . 
D 4 HOH   33 633 32   HOH   HOH A . 
D 4 HOH   34 634 47   HOH   HOH A . 
D 4 HOH   35 635 15   HOH   HOH A . 
D 4 HOH   36 636 38   HOH   HOH A . 
D 4 HOH   37 637 25   HOH   HOH A . 
D 4 HOH   38 638 40   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   ? ? ? '(1.16_3549: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                  2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Z14 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     66.816 
_cell.length_a_esd                 ? 
_cell.length_b                     66.816 
_cell.length_b_esd                 ? 
_cell.length_c                     375.520 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         8Z14 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                178 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 61 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8Z14 
_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             2.62 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.09 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    '1.6 M Potassium/Sodium phosphate pH 6.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     291 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-05-20 
_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   0.97853 
_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 BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97853 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8Z14 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.638 
_reflns.d_resolution_low                               57.19 
_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                                     15861 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                31.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.209 
_reflns.pdbx_Rpim_I_all                                0.036 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.2 
_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                                    2.64 
_reflns_shell.d_res_low                                     2.78 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2239 
_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                               1.864 
_reflns_shell.pdbx_Rpim_I_all                               0.372 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.812 
_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                                  1.8 
_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                                 8Z14 
_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                            2.638 
_refine.ls_d_res_low                             55.3 
_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                     15752 
_refine.ls_number_reflns_R_free                  779 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.92 
_refine.ls_percent_reflns_R_free                 10.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2269 
_refine.ls_R_factor_R_free                       0.2794 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2213 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       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             1.11 
_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                 27.54 
_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                       2.638 
_refine_hist.d_res_low                        55.3 
_refine_hist.number_atoms_solvent             38 
_refine_hist.number_atoms_total               3366 
_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        3255 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         73 
_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' ? 0.015  ? 3416 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.405  ? 4665 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 23.541 ? 1211 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.069  ? 504  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.017  ? 611  ? 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' 2.638  2.7229 . . 137 1230 100.00 . . . . 0.2843 . . . . . . . . . . . 0.3621 
'X-RAY DIFFRACTION' 2.7229 2.8203 . . 139 1251 100.00 . . . . 0.2859 . . . . . . . . . . . 0.3416 
'X-RAY DIFFRACTION' 2.8203 2.9332 . . 138 1244 100.00 . . . . 0.2733 . . . . . . . . . . . 0.3702 
'X-RAY DIFFRACTION' 2.9332 3.0667 . . 141 1262 100.00 . . . . 0.2759 . . . . . . . . . . . 0.3632 
'X-RAY DIFFRACTION' 3.0667 3.2283 . . 137 1247 100.00 . . . . 0.2481 . . . . . . . . . . . 0.3072 
'X-RAY DIFFRACTION' 3.2283 3.4306 . . 141 1269 100.00 . . . . 0.2375 . . . . . . . . . . . 0.2972 
'X-RAY DIFFRACTION' 3.4306 3.6954 . . 143 1284 100.00 . . . . 0.2310 . . . . . . . . . . . 0.2744 
'X-RAY DIFFRACTION' 3.6954 4.0672 . . 141 1271 100.00 . . . . 0.2018 . . . . . . . . . . . 0.2596 
'X-RAY DIFFRACTION' 4.0672 4.6554 . . 146 1312 100.00 . . . . 0.1845 . . . . . . . . . . . 0.2147 
'X-RAY DIFFRACTION' 4.6554 5.8643 . . 149 1339 100.00 . . . . 0.1972 . . . . . . . . . . . 0.2864 
'X-RAY DIFFRACTION' 5.8643 55.298 . . 164 1467 100.00 . . . . 0.2145 . . . . . . . . . . . 0.2598 
# 
_struct.entry_id                     8Z14 
_struct.title                        'The crystal structure of DiatB-6-DMAT complex' 
_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        8Z14 
_struct_keywords.text            'FAD-dependent oxidoreductase, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A7T1BYC5_STRSQ 
_struct_ref.pdbx_db_accession          A0A7T1BYC5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MRVCVIGAGLSGLAVGHALKERGISFVCLEKAPDVGGIWRQPGAGERGPGYRTLHLNTAKQLTGYADFPMPDAYPLYPRH
SQVAAYLRSFAEWAGLLDHVELRTEVVSVRQDADGPWTVVSRGADGAQVSRRFEQVVVASGHHNEPALPDPLPAGADSFA
GTILHSLDYRDGGDFAGRRVVVVGLGASAVDIAADLSRHAERTLLSVRRGLHIVPKQLFGMSVDEIAEAPWWNEMSFDER
RRWVEQALLVARGRLSDYGLPEPDHPVFSSATTLSDEILSRIRHGAVTPKPAIASFDGDRVVFTDGTSEPADAVVYCTGF
HMTFPFLPAGCPVSADGSVELYRRVVPADRPGLYFVGLVRPVGAITRLVEAQAEWVARLVDGAAVLPAADQMREEIGTYL
TGIVQRYGRTEGASIQVDVGPYLAEFRESLPV
;
_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              8Z14 
_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                 432 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A7T1BYC5 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  432 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       432 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             8Z14 
_struct_ref_seq_dif.mon_id                       MET 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      333 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   A0A7T1BYC5 
_struct_ref_seq_dif.db_mon_id                    VAL 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          333 
_struct_ref_seq_dif.details                      conflict 
_struct_ref_seq_dif.pdbx_auth_seq_num            333 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1480  ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  18390 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_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 GLY A 9   ? ARG A 22  ? GLY A 9   ARG A 22  1 ? 14 
HELX_P HELX_P2  AA2 GLY A 36  ? GLY A 45  ? GLY A 36  GLY A 45  5 ? 10 
HELX_P HELX_P3  AA3 ALA A 59  ? GLY A 64  ? ALA A 59  GLY A 64  1 ? 6  
HELX_P HELX_P4  AA4 ARG A 79  ? ALA A 94  ? ARG A 79  ALA A 94  1 ? 16 
HELX_P HELX_P5  AA5 LEU A 96  ? ASP A 98  ? LEU A 96  ASP A 98  5 ? 3  
HELX_P HELX_P6  AA6 GLY A 155 ? PHE A 159 ? GLY A 155 PHE A 159 5 ? 5  
HELX_P HELX_P7  AA7 LEU A 167 ? TYR A 169 ? LEU A 167 TYR A 169 5 ? 3  
HELX_P HELX_P8  AA8 ASP A 171 ? ALA A 176 ? ASP A 171 ALA A 176 5 ? 6  
HELX_P HELX_P9  AA9 GLY A 186 ? SER A 197 ? GLY A 186 SER A 197 1 ? 12 
HELX_P HELX_P10 AB1 VAL A 223 ? ALA A 227 ? VAL A 223 ALA A 227 1 ? 5  
HELX_P HELX_P11 AB2 ALA A 229 ? GLU A 234 ? ALA A 229 GLU A 234 1 ? 6  
HELX_P HELX_P12 AB3 SER A 236 ? GLY A 253 ? SER A 236 GLY A 253 1 ? 18 
HELX_P HELX_P13 AB4 ARG A 254 ? TYR A 258 ? ARG A 254 TYR A 258 5 ? 5  
HELX_P HELX_P14 AB5 GLU A 277 ? HIS A 284 ? GLU A 277 HIS A 284 1 ? 8  
HELX_P HELX_P15 AB6 LEU A 341 ? VAL A 345 ? LEU A 341 VAL A 345 5 ? 5  
HELX_P HELX_P16 AB7 ILE A 365 ? ASP A 381 ? ILE A 365 ASP A 381 1 ? 17 
HELX_P HELX_P17 AB8 ALA A 388 ? TYR A 407 ? ALA A 388 TYR A 407 1 ? 20 
HELX_P HELX_P18 AB9 GLY A 412 ? SER A 414 ? GLY A 412 SER A 414 5 ? 3  
HELX_P HELX_P19 AC1 ASP A 418 ? ALA A 424 ? ASP A 418 ALA A 424 1 ? 7  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ASP 
_struct_mon_prot_cis.label_seq_id           150 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           ASP 
_struct_mon_prot_cis.auth_seq_id            150 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    151 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     151 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       7.03 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 5 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 3 ? 
AA8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA5 1 2 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA8 1 2 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 100 ? GLU A 101 ? VAL A 100 GLU A 101 
AA1 2 PHE A 26  ? LEU A 29  ? PHE A 26  LEU A 29  
AA1 3 VAL A 3   ? ILE A 6   ? VAL A 3   ILE A 6   
AA1 4 GLN A 135 ? VAL A 138 ? GLN A 135 VAL A 138 
AA1 5 LEU A 353 ? PHE A 355 ? LEU A 353 PHE A 355 
AA2 1 GLU A 105 ? GLN A 111 ? GLU A 105 GLN A 111 
AA2 2 TRP A 117 ? ARG A 122 ? TRP A 117 ARG A 122 
AA2 3 GLN A 128 ? PHE A 133 ? GLN A 128 PHE A 133 
AA3 1 GLU A 145 ? PRO A 146 ? GLU A 145 PRO A 146 
AA3 2 PHE A 320 ? HIS A 321 ? PHE A 320 HIS A 321 
AA4 1 THR A 162 ? HIS A 165 ? THR A 162 HIS A 165 
AA4 2 ALA A 313 ? TYR A 316 ? ALA A 313 TYR A 316 
AA4 3 ARG A 179 ? VAL A 183 ? ARG A 179 VAL A 183 
AA4 4 ARG A 202 ? SER A 206 ? ARG A 202 SER A 206 
AA4 5 THR A 288 ? LYS A 290 ? THR A 288 LYS A 290 
AA5 1 HIS A 212 ? VAL A 214 ? HIS A 212 VAL A 214 
AA5 2 THR A 272 ? LEU A 274 ? THR A 272 LEU A 274 
AA6 1 GLN A 217 ? LEU A 218 ? GLN A 217 LEU A 218 
AA6 2 MET A 221 ? SER A 222 ? MET A 221 SER A 222 
AA7 1 ILE A 293 ? PHE A 296 ? ILE A 293 PHE A 296 
AA7 2 ARG A 300 ? PHE A 303 ? ARG A 300 PHE A 303 
AA7 3 SER A 308 ? PRO A 310 ? SER A 308 PRO A 310 
AA8 1 ARG A 360 ? PRO A 361 ? ARG A 360 PRO A 361 
AA8 2 GLN A 416 ? VAL A 417 ? GLN A 416 VAL A 417 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 101 ? O GLU A 101 N CYS A 28  ? N CYS A 28  
AA1 2 3 O LEU A 29  ? O LEU A 29  N VAL A 5   ? N VAL A 5   
AA1 3 4 N ILE A 6   ? N ILE A 6   O VAL A 137 ? O VAL A 137 
AA1 4 5 N VAL A 138 ? N VAL A 138 O TYR A 354 ? O TYR A 354 
AA2 1 2 N VAL A 107 ? N VAL A 107 O VAL A 120 ? O VAL A 120 
AA2 2 3 N VAL A 119 ? N VAL A 119 O ARG A 131 ? O ARG A 131 
AA3 1 2 N GLU A 145 ? N GLU A 145 O HIS A 321 ? O HIS A 321 
AA4 1 2 N LEU A 164 ? N LEU A 164 O TYR A 316 ? O TYR A 316 
AA4 2 3 O ALA A 313 ? O ALA A 313 N VAL A 181 ? N VAL A 181 
AA4 3 4 N VAL A 182 ? N VAL A 182 O LEU A 204 ? O LEU A 204 
AA4 4 5 N LEU A 205 ? N LEU A 205 O THR A 288 ? O THR A 288 
AA5 1 2 N HIS A 212 ? N HIS A 212 O THR A 273 ? O THR A 273 
AA6 1 2 N LEU A 218 ? N LEU A 218 O MET A 221 ? O MET A 221 
AA7 1 2 N ALA A 294 ? N ALA A 294 O VAL A 302 ? O VAL A 302 
AA7 2 3 N VAL A 301 ? N VAL A 301 O GLU A 309 ? O GLU A 309 
AA8 1 2 N ARG A 360 ? N ARG A 360 O VAL A 417 ? O VAL A 417 
# 
_pdbx_entry_details.entry_id                   8Z14 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   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 PHE A 68  ? ? -160.65 78.35   
2  1 PRO A 116 ? ? -58.27  170.36  
3  1 ALA A 127 ? ? -57.42  106.98  
4  1 ALA A 139 ? ? -143.87 53.76   
5  1 ARG A 170 ? ? -138.49 -56.65  
6  1 ASP A 174 ? ? -69.91  1.50    
7  1 HIS A 199 ? ? -132.93 -55.30  
8  1 ASP A 264 ? ? -89.54  48.01   
9  1 PHE A 268 ? ? 71.42   -4.38   
10 1 PRO A 291 ? ? -73.50  -163.15 
11 1 CYS A 317 ? ? -94.60  55.86   
12 1 VAL A 345 ? ? -132.68 -41.18  
13 1 ARG A 409 ? ? -85.37  45.36   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 2   ? ? 0.122 'SIDE CHAIN' 
2 1 ARG A 40  ? ? 0.080 'SIDE CHAIN' 
3 1 ARG A 47  ? ? 0.191 'SIDE CHAIN' 
4 1 ARG A 122 ? ? 0.155 'SIDE CHAIN' 
5 1 ARG A 409 ? ? 0.132 'SIDE CHAIN' 
# 
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 ARG 427 ? A ARG 427 
2 1 Y 1 A GLU 428 ? A GLU 428 
3 1 Y 1 A SER 429 ? A SER 429 
4 1 Y 1 A LEU 430 ? A LEU 430 
5 1 Y 1 A PRO 431 ? A PRO 431 
6 1 Y 1 A VAL 432 ? A VAL 432 
# 
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 
A1D7R CZ3    C Y N 1   
A1D7R CH2    C Y N 2   
A1D7R CZ2    C Y N 3   
A1D7R CE2    C Y N 4   
A1D7R CD2    C Y N 5   
A1D7R CE3    C Y N 6   
A1D7R CD1    C Y N 7   
A1D7R CG     C Y N 8   
A1D7R CB     C N N 9   
A1D7R CA     C N S 10  
A1D7R C      C N N 11  
A1D7R C12    C N N 12  
A1D7R C13    C N N 13  
A1D7R C14    C N N 14  
A1D7R C15    C N N 15  
A1D7R C16    C N N 16  
A1D7R NE1    N Y N 17  
A1D7R N      N N N 18  
A1D7R O      O N N 19  
A1D7R OXT    O N N 20  
A1D7R HZ3    H N N 21  
A1D7R HZ2    H N N 22  
A1D7R HE3    H N N 23  
A1D7R HD1    H N N 24  
A1D7R HB2    H N N 25  
A1D7R HB3    H N N 26  
A1D7R HA     H N N 27  
A1D7R H8     H N N 28  
A1D7R H9     H N N 29  
A1D7R H10    H N N 30  
A1D7R H13    H N N 31  
A1D7R H14    H N N 32  
A1D7R H15    H N N 33  
A1D7R H16    H N N 34  
A1D7R H17    H N N 35  
A1D7R H18    H N N 36  
A1D7R HE1    H N N 37  
A1D7R H      H N N 38  
A1D7R H2     H N N 39  
A1D7R HXT    H N N 40  
ALA   N      N N N 41  
ALA   CA     C N S 42  
ALA   C      C N N 43  
ALA   O      O N N 44  
ALA   CB     C N N 45  
ALA   OXT    O N N 46  
ALA   H      H N N 47  
ALA   H2     H N N 48  
ALA   HA     H N N 49  
ALA   HB1    H N N 50  
ALA   HB2    H N N 51  
ALA   HB3    H N N 52  
ALA   HXT    H N N 53  
ARG   N      N N N 54  
ARG   CA     C N S 55  
ARG   C      C N N 56  
ARG   O      O N N 57  
ARG   CB     C N N 58  
ARG   CG     C N N 59  
ARG   CD     C N N 60  
ARG   NE     N N N 61  
ARG   CZ     C N N 62  
ARG   NH1    N N N 63  
ARG   NH2    N N N 64  
ARG   OXT    O N N 65  
ARG   H      H N N 66  
ARG   H2     H N N 67  
ARG   HA     H N N 68  
ARG   HB2    H N N 69  
ARG   HB3    H N N 70  
ARG   HG2    H N N 71  
ARG   HG3    H N N 72  
ARG   HD2    H N N 73  
ARG   HD3    H N N 74  
ARG   HE     H N N 75  
ARG   HH11   H N N 76  
ARG   HH12   H N N 77  
ARG   HH21   H N N 78  
ARG   HH22   H N N 79  
ARG   HXT    H N N 80  
ASN   N      N N N 81  
ASN   CA     C N S 82  
ASN   C      C N N 83  
ASN   O      O N N 84  
ASN   CB     C N N 85  
ASN   CG     C N N 86  
ASN   OD1    O N N 87  
ASN   ND2    N N N 88  
ASN   OXT    O N N 89  
ASN   H      H N N 90  
ASN   H2     H N N 91  
ASN   HA     H N N 92  
ASN   HB2    H N N 93  
ASN   HB3    H N N 94  
ASN   HD21   H N N 95  
ASN   HD22   H N N 96  
ASN   HXT    H N N 97  
ASP   N      N N N 98  
ASP   CA     C N S 99  
ASP   C      C N N 100 
ASP   O      O N N 101 
ASP   CB     C N N 102 
ASP   CG     C N N 103 
ASP   OD1    O N N 104 
ASP   OD2    O N N 105 
ASP   OXT    O N N 106 
ASP   H      H N N 107 
ASP   H2     H N N 108 
ASP   HA     H N N 109 
ASP   HB2    H N N 110 
ASP   HB3    H N N 111 
ASP   HD2    H N N 112 
ASP   HXT    H N N 113 
CYS   N      N N N 114 
CYS   CA     C N R 115 
CYS   C      C N N 116 
CYS   O      O N N 117 
CYS   CB     C N N 118 
CYS   SG     S N N 119 
CYS   OXT    O N N 120 
CYS   H      H N N 121 
CYS   H2     H N N 122 
CYS   HA     H N N 123 
CYS   HB2    H N N 124 
CYS   HB3    H N N 125 
CYS   HG     H N N 126 
CYS   HXT    H N N 127 
FAD   PA     P N R 128 
FAD   O1A    O N N 129 
FAD   O2A    O N N 130 
FAD   O5B    O N N 131 
FAD   C5B    C N N 132 
FAD   C4B    C N R 133 
FAD   O4B    O N N 134 
FAD   C3B    C N S 135 
FAD   O3B    O N N 136 
FAD   C2B    C N R 137 
FAD   O2B    O N N 138 
FAD   C1B    C N R 139 
FAD   N9A    N Y N 140 
FAD   C8A    C Y N 141 
FAD   N7A    N Y N 142 
FAD   C5A    C Y N 143 
FAD   C6A    C Y N 144 
FAD   N6A    N N N 145 
FAD   N1A    N Y N 146 
FAD   C2A    C Y N 147 
FAD   N3A    N Y N 148 
FAD   C4A    C Y N 149 
FAD   N1     N N N 150 
FAD   C2     C N N 151 
FAD   O2     O N N 152 
FAD   N3     N N N 153 
FAD   C4     C N N 154 
FAD   O4     O N N 155 
FAD   C4X    C N N 156 
FAD   N5     N N N 157 
FAD   C5X    C Y N 158 
FAD   C6     C Y N 159 
FAD   C7     C Y N 160 
FAD   C7M    C N N 161 
FAD   C8     C Y N 162 
FAD   C8M    C N N 163 
FAD   C9     C Y N 164 
FAD   C9A    C Y N 165 
FAD   N10    N N N 166 
FAD   C10    C N N 167 
FAD   "C1'"  C N N 168 
FAD   "C2'"  C N S 169 
FAD   "O2'"  O N N 170 
FAD   "C3'"  C N S 171 
FAD   "O3'"  O N N 172 
FAD   "C4'"  C N R 173 
FAD   "O4'"  O N N 174 
FAD   "C5'"  C N N 175 
FAD   "O5'"  O N N 176 
FAD   P      P N R 177 
FAD   O1P    O N N 178 
FAD   O2P    O N N 179 
FAD   O3P    O N N 180 
FAD   HOA2   H N N 181 
FAD   H51A   H N N 182 
FAD   H52A   H N N 183 
FAD   H4B    H N N 184 
FAD   H3B    H N N 185 
FAD   HO3A   H N N 186 
FAD   H2B    H N N 187 
FAD   HO2A   H N N 188 
FAD   H1B    H N N 189 
FAD   H8A    H N N 190 
FAD   H61A   H N N 191 
FAD   H62A   H N N 192 
FAD   H2A    H N N 193 
FAD   HN3    H N N 194 
FAD   H6     H N N 195 
FAD   HM71   H N N 196 
FAD   HM72   H N N 197 
FAD   HM73   H N N 198 
FAD   HM81   H N N 199 
FAD   HM82   H N N 200 
FAD   HM83   H N N 201 
FAD   H9     H N N 202 
FAD   "H1'1" H N N 203 
FAD   "H1'2" H N N 204 
FAD   "H2'"  H N N 205 
FAD   "HO2'" H N N 206 
FAD   "H3'"  H N N 207 
FAD   "HO3'" H N N 208 
FAD   "H4'"  H N N 209 
FAD   "HO4'" H N N 210 
FAD   "H5'1" H N N 211 
FAD   "H5'2" H N N 212 
FAD   HOP2   H N N 213 
GLN   N      N N N 214 
GLN   CA     C N S 215 
GLN   C      C N N 216 
GLN   O      O N N 217 
GLN   CB     C N N 218 
GLN   CG     C N N 219 
GLN   CD     C N N 220 
GLN   OE1    O N N 221 
GLN   NE2    N N N 222 
GLN   OXT    O N N 223 
GLN   H      H N N 224 
GLN   H2     H N N 225 
GLN   HA     H N N 226 
GLN   HB2    H N N 227 
GLN   HB3    H N N 228 
GLN   HG2    H N N 229 
GLN   HG3    H N N 230 
GLN   HE21   H N N 231 
GLN   HE22   H N N 232 
GLN   HXT    H N N 233 
GLU   N      N N N 234 
GLU   CA     C N S 235 
GLU   C      C N N 236 
GLU   O      O N N 237 
GLU   CB     C N N 238 
GLU   CG     C N N 239 
GLU   CD     C N N 240 
GLU   OE1    O N N 241 
GLU   OE2    O N N 242 
GLU   OXT    O N N 243 
GLU   H      H N N 244 
GLU   H2     H N N 245 
GLU   HA     H N N 246 
GLU   HB2    H N N 247 
GLU   HB3    H N N 248 
GLU   HG2    H N N 249 
GLU   HG3    H N N 250 
GLU   HE2    H N N 251 
GLU   HXT    H N N 252 
GLY   N      N N N 253 
GLY   CA     C N N 254 
GLY   C      C N N 255 
GLY   O      O N N 256 
GLY   OXT    O N N 257 
GLY   H      H N N 258 
GLY   H2     H N N 259 
GLY   HA2    H N N 260 
GLY   HA3    H N N 261 
GLY   HXT    H N N 262 
HIS   N      N N N 263 
HIS   CA     C N S 264 
HIS   C      C N N 265 
HIS   O      O N N 266 
HIS   CB     C N N 267 
HIS   CG     C Y N 268 
HIS   ND1    N Y N 269 
HIS   CD2    C Y N 270 
HIS   CE1    C Y N 271 
HIS   NE2    N Y N 272 
HIS   OXT    O N N 273 
HIS   H      H N N 274 
HIS   H2     H N N 275 
HIS   HA     H N N 276 
HIS   HB2    H N N 277 
HIS   HB3    H N N 278 
HIS   HD1    H N N 279 
HIS   HD2    H N N 280 
HIS   HE1    H N N 281 
HIS   HE2    H N N 282 
HIS   HXT    H N N 283 
HOH   O      O N N 284 
HOH   H1     H N N 285 
HOH   H2     H N N 286 
ILE   N      N N N 287 
ILE   CA     C N S 288 
ILE   C      C N N 289 
ILE   O      O N N 290 
ILE   CB     C N S 291 
ILE   CG1    C N N 292 
ILE   CG2    C N N 293 
ILE   CD1    C N N 294 
ILE   OXT    O N N 295 
ILE   H      H N N 296 
ILE   H2     H N N 297 
ILE   HA     H N N 298 
ILE   HB     H N N 299 
ILE   HG12   H N N 300 
ILE   HG13   H N N 301 
ILE   HG21   H N N 302 
ILE   HG22   H N N 303 
ILE   HG23   H N N 304 
ILE   HD11   H N N 305 
ILE   HD12   H N N 306 
ILE   HD13   H N N 307 
ILE   HXT    H N N 308 
LEU   N      N N N 309 
LEU   CA     C N S 310 
LEU   C      C N N 311 
LEU   O      O N N 312 
LEU   CB     C N N 313 
LEU   CG     C N N 314 
LEU   CD1    C N N 315 
LEU   CD2    C N N 316 
LEU   OXT    O N N 317 
LEU   H      H N N 318 
LEU   H2     H N N 319 
LEU   HA     H N N 320 
LEU   HB2    H N N 321 
LEU   HB3    H N N 322 
LEU   HG     H N N 323 
LEU   HD11   H N N 324 
LEU   HD12   H N N 325 
LEU   HD13   H N N 326 
LEU   HD21   H N N 327 
LEU   HD22   H N N 328 
LEU   HD23   H N N 329 
LEU   HXT    H N N 330 
LYS   N      N N N 331 
LYS   CA     C N S 332 
LYS   C      C N N 333 
LYS   O      O N N 334 
LYS   CB     C N N 335 
LYS   CG     C N N 336 
LYS   CD     C N N 337 
LYS   CE     C N N 338 
LYS   NZ     N N N 339 
LYS   OXT    O N N 340 
LYS   H      H N N 341 
LYS   H2     H N N 342 
LYS   HA     H N N 343 
LYS   HB2    H N N 344 
LYS   HB3    H N N 345 
LYS   HG2    H N N 346 
LYS   HG3    H N N 347 
LYS   HD2    H N N 348 
LYS   HD3    H N N 349 
LYS   HE2    H N N 350 
LYS   HE3    H N N 351 
LYS   HZ1    H N N 352 
LYS   HZ2    H N N 353 
LYS   HZ3    H N N 354 
LYS   HXT    H N N 355 
MET   N      N N N 356 
MET   CA     C N S 357 
MET   C      C N N 358 
MET   O      O N N 359 
MET   CB     C N N 360 
MET   CG     C N N 361 
MET   SD     S N N 362 
MET   CE     C N N 363 
MET   OXT    O N N 364 
MET   H      H N N 365 
MET   H2     H N N 366 
MET   HA     H N N 367 
MET   HB2    H N N 368 
MET   HB3    H N N 369 
MET   HG2    H N N 370 
MET   HG3    H N N 371 
MET   HE1    H N N 372 
MET   HE2    H N N 373 
MET   HE3    H N N 374 
MET   HXT    H N N 375 
PHE   N      N N N 376 
PHE   CA     C N S 377 
PHE   C      C N N 378 
PHE   O      O N N 379 
PHE   CB     C N N 380 
PHE   CG     C Y N 381 
PHE   CD1    C Y N 382 
PHE   CD2    C Y N 383 
PHE   CE1    C Y N 384 
PHE   CE2    C Y N 385 
PHE   CZ     C Y N 386 
PHE   OXT    O N N 387 
PHE   H      H N N 388 
PHE   H2     H N N 389 
PHE   HA     H N N 390 
PHE   HB2    H N N 391 
PHE   HB3    H N N 392 
PHE   HD1    H N N 393 
PHE   HD2    H N N 394 
PHE   HE1    H N N 395 
PHE   HE2    H N N 396 
PHE   HZ     H N N 397 
PHE   HXT    H N N 398 
PRO   N      N N N 399 
PRO   CA     C N S 400 
PRO   C      C N N 401 
PRO   O      O N N 402 
PRO   CB     C N N 403 
PRO   CG     C N N 404 
PRO   CD     C N N 405 
PRO   OXT    O N N 406 
PRO   H      H N N 407 
PRO   HA     H N N 408 
PRO   HB2    H N N 409 
PRO   HB3    H N N 410 
PRO   HG2    H N N 411 
PRO   HG3    H N N 412 
PRO   HD2    H N N 413 
PRO   HD3    H N N 414 
PRO   HXT    H N N 415 
SER   N      N N N 416 
SER   CA     C N S 417 
SER   C      C N N 418 
SER   O      O N N 419 
SER   CB     C N N 420 
SER   OG     O N N 421 
SER   OXT    O N N 422 
SER   H      H N N 423 
SER   H2     H N N 424 
SER   HA     H N N 425 
SER   HB2    H N N 426 
SER   HB3    H N N 427 
SER   HG     H N N 428 
SER   HXT    H N N 429 
THR   N      N N N 430 
THR   CA     C N S 431 
THR   C      C N N 432 
THR   O      O N N 433 
THR   CB     C N R 434 
THR   OG1    O N N 435 
THR   CG2    C N N 436 
THR   OXT    O N N 437 
THR   H      H N N 438 
THR   H2     H N N 439 
THR   HA     H N N 440 
THR   HB     H N N 441 
THR   HG1    H N N 442 
THR   HG21   H N N 443 
THR   HG22   H N N 444 
THR   HG23   H N N 445 
THR   HXT    H N N 446 
TRP   N      N N N 447 
TRP   CA     C N S 448 
TRP   C      C N N 449 
TRP   O      O N N 450 
TRP   CB     C N N 451 
TRP   CG     C Y N 452 
TRP   CD1    C Y N 453 
TRP   CD2    C Y N 454 
TRP   NE1    N Y N 455 
TRP   CE2    C Y N 456 
TRP   CE3    C Y N 457 
TRP   CZ2    C Y N 458 
TRP   CZ3    C Y N 459 
TRP   CH2    C Y N 460 
TRP   OXT    O N N 461 
TRP   H      H N N 462 
TRP   H2     H N N 463 
TRP   HA     H N N 464 
TRP   HB2    H N N 465 
TRP   HB3    H N N 466 
TRP   HD1    H N N 467 
TRP   HE1    H N N 468 
TRP   HE3    H N N 469 
TRP   HZ2    H N N 470 
TRP   HZ3    H N N 471 
TRP   HH2    H N N 472 
TRP   HXT    H N N 473 
TYR   N      N N N 474 
TYR   CA     C N S 475 
TYR   C      C N N 476 
TYR   O      O N N 477 
TYR   CB     C N N 478 
TYR   CG     C Y N 479 
TYR   CD1    C Y N 480 
TYR   CD2    C Y N 481 
TYR   CE1    C Y N 482 
TYR   CE2    C Y N 483 
TYR   CZ     C Y N 484 
TYR   OH     O N N 485 
TYR   OXT    O N N 486 
TYR   H      H N N 487 
TYR   H2     H N N 488 
TYR   HA     H N N 489 
TYR   HB2    H N N 490 
TYR   HB3    H N N 491 
TYR   HD1    H N N 492 
TYR   HD2    H N N 493 
TYR   HE1    H N N 494 
TYR   HE2    H N N 495 
TYR   HH     H N N 496 
TYR   HXT    H N N 497 
VAL   N      N N N 498 
VAL   CA     C N S 499 
VAL   C      C N N 500 
VAL   O      O N N 501 
VAL   CB     C N N 502 
VAL   CG1    C N N 503 
VAL   CG2    C N N 504 
VAL   OXT    O N N 505 
VAL   H      H N N 506 
VAL   H2     H N N 507 
VAL   HA     H N N 508 
VAL   HB     H N N 509 
VAL   HG11   H N N 510 
VAL   HG12   H N N 511 
VAL   HG13   H N N 512 
VAL   HG21   H N N 513 
VAL   HG22   H N N 514 
VAL   HG23   H N N 515 
VAL   HXT    H N N 516 
# 
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 
A1D7R C15   C14    sing N N 1   
A1D7R C14   C13    doub N N 2   
A1D7R C14   C16    sing N N 3   
A1D7R C12   C13    sing N N 4   
A1D7R C12   CH2    sing N N 5   
A1D7R CZ3   CH2    sing Y N 6   
A1D7R CZ3   CE3    doub Y N 7   
A1D7R CH2   CZ2    doub Y N 8   
A1D7R O     C      doub N N 9   
A1D7R CE3   CD2    sing Y N 10  
A1D7R CZ2   CE2    sing Y N 11  
A1D7R CD2   CE2    doub Y N 12  
A1D7R CD2   CG     sing Y N 13  
A1D7R CE2   NE1    sing Y N 14  
A1D7R C     OXT    sing N N 15  
A1D7R C     CA     sing N N 16  
A1D7R CG    CB     sing N N 17  
A1D7R CG    CD1    doub Y N 18  
A1D7R CB    CA     sing N N 19  
A1D7R NE1   CD1    sing Y N 20  
A1D7R CA    N      sing N N 21  
A1D7R CZ3   HZ3    sing N N 22  
A1D7R CZ2   HZ2    sing N N 23  
A1D7R CE3   HE3    sing N N 24  
A1D7R CD1   HD1    sing N N 25  
A1D7R CB    HB2    sing N N 26  
A1D7R CB    HB3    sing N N 27  
A1D7R CA    HA     sing N N 28  
A1D7R C12   H8     sing N N 29  
A1D7R C12   H9     sing N N 30  
A1D7R C13   H10    sing N N 31  
A1D7R C15   H13    sing N N 32  
A1D7R C15   H14    sing N N 33  
A1D7R C15   H15    sing N N 34  
A1D7R C16   H16    sing N N 35  
A1D7R C16   H17    sing N N 36  
A1D7R C16   H18    sing N N 37  
A1D7R NE1   HE1    sing N N 38  
A1D7R N     H      sing N N 39  
A1D7R N     H2     sing N N 40  
A1D7R OXT   HXT    sing N N 41  
ALA   N     CA     sing N N 42  
ALA   N     H      sing N N 43  
ALA   N     H2     sing N N 44  
ALA   CA    C      sing N N 45  
ALA   CA    CB     sing N N 46  
ALA   CA    HA     sing N N 47  
ALA   C     O      doub N N 48  
ALA   C     OXT    sing N N 49  
ALA   CB    HB1    sing N N 50  
ALA   CB    HB2    sing N N 51  
ALA   CB    HB3    sing N N 52  
ALA   OXT   HXT    sing N N 53  
ARG   N     CA     sing N N 54  
ARG   N     H      sing N N 55  
ARG   N     H2     sing N N 56  
ARG   CA    C      sing N N 57  
ARG   CA    CB     sing N N 58  
ARG   CA    HA     sing N N 59  
ARG   C     O      doub N N 60  
ARG   C     OXT    sing N N 61  
ARG   CB    CG     sing N N 62  
ARG   CB    HB2    sing N N 63  
ARG   CB    HB3    sing N N 64  
ARG   CG    CD     sing N N 65  
ARG   CG    HG2    sing N N 66  
ARG   CG    HG3    sing N N 67  
ARG   CD    NE     sing N N 68  
ARG   CD    HD2    sing N N 69  
ARG   CD    HD3    sing N N 70  
ARG   NE    CZ     sing N N 71  
ARG   NE    HE     sing N N 72  
ARG   CZ    NH1    sing N N 73  
ARG   CZ    NH2    doub N N 74  
ARG   NH1   HH11   sing N N 75  
ARG   NH1   HH12   sing N N 76  
ARG   NH2   HH21   sing N N 77  
ARG   NH2   HH22   sing N N 78  
ARG   OXT   HXT    sing N N 79  
ASN   N     CA     sing N N 80  
ASN   N     H      sing N N 81  
ASN   N     H2     sing N N 82  
ASN   CA    C      sing N N 83  
ASN   CA    CB     sing N N 84  
ASN   CA    HA     sing N N 85  
ASN   C     O      doub N N 86  
ASN   C     OXT    sing N N 87  
ASN   CB    CG     sing N N 88  
ASN   CB    HB2    sing N N 89  
ASN   CB    HB3    sing N N 90  
ASN   CG    OD1    doub N N 91  
ASN   CG    ND2    sing N N 92  
ASN   ND2   HD21   sing N N 93  
ASN   ND2   HD22   sing N N 94  
ASN   OXT   HXT    sing N N 95  
ASP   N     CA     sing N N 96  
ASP   N     H      sing N N 97  
ASP   N     H2     sing N N 98  
ASP   CA    C      sing N N 99  
ASP   CA    CB     sing N N 100 
ASP   CA    HA     sing N N 101 
ASP   C     O      doub N N 102 
ASP   C     OXT    sing N N 103 
ASP   CB    CG     sing N N 104 
ASP   CB    HB2    sing N N 105 
ASP   CB    HB3    sing N N 106 
ASP   CG    OD1    doub N N 107 
ASP   CG    OD2    sing N N 108 
ASP   OD2   HD2    sing N N 109 
ASP   OXT   HXT    sing N N 110 
CYS   N     CA     sing N N 111 
CYS   N     H      sing N N 112 
CYS   N     H2     sing N N 113 
CYS   CA    C      sing N N 114 
CYS   CA    CB     sing N N 115 
CYS   CA    HA     sing N N 116 
CYS   C     O      doub N N 117 
CYS   C     OXT    sing N N 118 
CYS   CB    SG     sing N N 119 
CYS   CB    HB2    sing N N 120 
CYS   CB    HB3    sing N N 121 
CYS   SG    HG     sing N N 122 
CYS   OXT   HXT    sing N N 123 
FAD   PA    O1A    doub N N 124 
FAD   PA    O2A    sing N N 125 
FAD   PA    O5B    sing N N 126 
FAD   PA    O3P    sing N N 127 
FAD   O2A   HOA2   sing N N 128 
FAD   O5B   C5B    sing N N 129 
FAD   C5B   C4B    sing N N 130 
FAD   C5B   H51A   sing N N 131 
FAD   C5B   H52A   sing N N 132 
FAD   C4B   O4B    sing N N 133 
FAD   C4B   C3B    sing N N 134 
FAD   C4B   H4B    sing N N 135 
FAD   O4B   C1B    sing N N 136 
FAD   C3B   O3B    sing N N 137 
FAD   C3B   C2B    sing N N 138 
FAD   C3B   H3B    sing N N 139 
FAD   O3B   HO3A   sing N N 140 
FAD   C2B   O2B    sing N N 141 
FAD   C2B   C1B    sing N N 142 
FAD   C2B   H2B    sing N N 143 
FAD   O2B   HO2A   sing N N 144 
FAD   C1B   N9A    sing N N 145 
FAD   C1B   H1B    sing N N 146 
FAD   N9A   C8A    sing Y N 147 
FAD   N9A   C4A    sing Y N 148 
FAD   C8A   N7A    doub Y N 149 
FAD   C8A   H8A    sing N N 150 
FAD   N7A   C5A    sing Y N 151 
FAD   C5A   C6A    sing Y N 152 
FAD   C5A   C4A    doub Y N 153 
FAD   C6A   N6A    sing N N 154 
FAD   C6A   N1A    doub Y N 155 
FAD   N6A   H61A   sing N N 156 
FAD   N6A   H62A   sing N N 157 
FAD   N1A   C2A    sing Y N 158 
FAD   C2A   N3A    doub Y N 159 
FAD   C2A   H2A    sing N N 160 
FAD   N3A   C4A    sing Y N 161 
FAD   N1    C2     sing N N 162 
FAD   N1    C10    doub N N 163 
FAD   C2    O2     doub N N 164 
FAD   C2    N3     sing N N 165 
FAD   N3    C4     sing N N 166 
FAD   N3    HN3    sing N N 167 
FAD   C4    O4     doub N N 168 
FAD   C4    C4X    sing N N 169 
FAD   C4X   N5     doub N N 170 
FAD   C4X   C10    sing N N 171 
FAD   N5    C5X    sing N N 172 
FAD   C5X   C6     doub Y N 173 
FAD   C5X   C9A    sing Y N 174 
FAD   C6    C7     sing Y N 175 
FAD   C6    H6     sing N N 176 
FAD   C7    C7M    sing N N 177 
FAD   C7    C8     doub Y N 178 
FAD   C7M   HM71   sing N N 179 
FAD   C7M   HM72   sing N N 180 
FAD   C7M   HM73   sing N N 181 
FAD   C8    C8M    sing N N 182 
FAD   C8    C9     sing Y N 183 
FAD   C8M   HM81   sing N N 184 
FAD   C8M   HM82   sing N N 185 
FAD   C8M   HM83   sing N N 186 
FAD   C9    C9A    doub Y N 187 
FAD   C9    H9     sing N N 188 
FAD   C9A   N10    sing N N 189 
FAD   N10   C10    sing N N 190 
FAD   N10   "C1'"  sing N N 191 
FAD   "C1'" "C2'"  sing N N 192 
FAD   "C1'" "H1'1" sing N N 193 
FAD   "C1'" "H1'2" sing N N 194 
FAD   "C2'" "O2'"  sing N N 195 
FAD   "C2'" "C3'"  sing N N 196 
FAD   "C2'" "H2'"  sing N N 197 
FAD   "O2'" "HO2'" sing N N 198 
FAD   "C3'" "O3'"  sing N N 199 
FAD   "C3'" "C4'"  sing N N 200 
FAD   "C3'" "H3'"  sing N N 201 
FAD   "O3'" "HO3'" sing N N 202 
FAD   "C4'" "O4'"  sing N N 203 
FAD   "C4'" "C5'"  sing N N 204 
FAD   "C4'" "H4'"  sing N N 205 
FAD   "O4'" "HO4'" sing N N 206 
FAD   "C5'" "O5'"  sing N N 207 
FAD   "C5'" "H5'1" sing N N 208 
FAD   "C5'" "H5'2" sing N N 209 
FAD   "O5'" P      sing N N 210 
FAD   P     O1P    doub N N 211 
FAD   P     O2P    sing N N 212 
FAD   P     O3P    sing N N 213 
FAD   O2P   HOP2   sing N N 214 
GLN   N     CA     sing N N 215 
GLN   N     H      sing N N 216 
GLN   N     H2     sing N N 217 
GLN   CA    C      sing N N 218 
GLN   CA    CB     sing N N 219 
GLN   CA    HA     sing N N 220 
GLN   C     O      doub N N 221 
GLN   C     OXT    sing N N 222 
GLN   CB    CG     sing N N 223 
GLN   CB    HB2    sing N N 224 
GLN   CB    HB3    sing N N 225 
GLN   CG    CD     sing N N 226 
GLN   CG    HG2    sing N N 227 
GLN   CG    HG3    sing N N 228 
GLN   CD    OE1    doub N N 229 
GLN   CD    NE2    sing N N 230 
GLN   NE2   HE21   sing N N 231 
GLN   NE2   HE22   sing N N 232 
GLN   OXT   HXT    sing N N 233 
GLU   N     CA     sing N N 234 
GLU   N     H      sing N N 235 
GLU   N     H2     sing N N 236 
GLU   CA    C      sing N N 237 
GLU   CA    CB     sing N N 238 
GLU   CA    HA     sing N N 239 
GLU   C     O      doub N N 240 
GLU   C     OXT    sing N N 241 
GLU   CB    CG     sing N N 242 
GLU   CB    HB2    sing N N 243 
GLU   CB    HB3    sing N N 244 
GLU   CG    CD     sing N N 245 
GLU   CG    HG2    sing N N 246 
GLU   CG    HG3    sing N N 247 
GLU   CD    OE1    doub N N 248 
GLU   CD    OE2    sing N N 249 
GLU   OE2   HE2    sing N N 250 
GLU   OXT   HXT    sing N N 251 
GLY   N     CA     sing N N 252 
GLY   N     H      sing N N 253 
GLY   N     H2     sing N N 254 
GLY   CA    C      sing N N 255 
GLY   CA    HA2    sing N N 256 
GLY   CA    HA3    sing N N 257 
GLY   C     O      doub N N 258 
GLY   C     OXT    sing N N 259 
GLY   OXT   HXT    sing N N 260 
HIS   N     CA     sing N N 261 
HIS   N     H      sing N N 262 
HIS   N     H2     sing N N 263 
HIS   CA    C      sing N N 264 
HIS   CA    CB     sing N N 265 
HIS   CA    HA     sing N N 266 
HIS   C     O      doub N N 267 
HIS   C     OXT    sing N N 268 
HIS   CB    CG     sing N N 269 
HIS   CB    HB2    sing N N 270 
HIS   CB    HB3    sing N N 271 
HIS   CG    ND1    sing Y N 272 
HIS   CG    CD2    doub Y N 273 
HIS   ND1   CE1    doub Y N 274 
HIS   ND1   HD1    sing N N 275 
HIS   CD2   NE2    sing Y N 276 
HIS   CD2   HD2    sing N N 277 
HIS   CE1   NE2    sing Y N 278 
HIS   CE1   HE1    sing N N 279 
HIS   NE2   HE2    sing N N 280 
HIS   OXT   HXT    sing N N 281 
HOH   O     H1     sing N N 282 
HOH   O     H2     sing N N 283 
ILE   N     CA     sing N N 284 
ILE   N     H      sing N N 285 
ILE   N     H2     sing N N 286 
ILE   CA    C      sing N N 287 
ILE   CA    CB     sing N N 288 
ILE   CA    HA     sing N N 289 
ILE   C     O      doub N N 290 
ILE   C     OXT    sing N N 291 
ILE   CB    CG1    sing N N 292 
ILE   CB    CG2    sing N N 293 
ILE   CB    HB     sing N N 294 
ILE   CG1   CD1    sing N N 295 
ILE   CG1   HG12   sing N N 296 
ILE   CG1   HG13   sing N N 297 
ILE   CG2   HG21   sing N N 298 
ILE   CG2   HG22   sing N N 299 
ILE   CG2   HG23   sing N N 300 
ILE   CD1   HD11   sing N N 301 
ILE   CD1   HD12   sing N N 302 
ILE   CD1   HD13   sing N N 303 
ILE   OXT   HXT    sing N N 304 
LEU   N     CA     sing N N 305 
LEU   N     H      sing N N 306 
LEU   N     H2     sing N N 307 
LEU   CA    C      sing N N 308 
LEU   CA    CB     sing N N 309 
LEU   CA    HA     sing N N 310 
LEU   C     O      doub N N 311 
LEU   C     OXT    sing N N 312 
LEU   CB    CG     sing N N 313 
LEU   CB    HB2    sing N N 314 
LEU   CB    HB3    sing N N 315 
LEU   CG    CD1    sing N N 316 
LEU   CG    CD2    sing N N 317 
LEU   CG    HG     sing N N 318 
LEU   CD1   HD11   sing N N 319 
LEU   CD1   HD12   sing N N 320 
LEU   CD1   HD13   sing N N 321 
LEU   CD2   HD21   sing N N 322 
LEU   CD2   HD22   sing N N 323 
LEU   CD2   HD23   sing N N 324 
LEU   OXT   HXT    sing N N 325 
LYS   N     CA     sing N N 326 
LYS   N     H      sing N N 327 
LYS   N     H2     sing N N 328 
LYS   CA    C      sing N N 329 
LYS   CA    CB     sing N N 330 
LYS   CA    HA     sing N N 331 
LYS   C     O      doub N N 332 
LYS   C     OXT    sing N N 333 
LYS   CB    CG     sing N N 334 
LYS   CB    HB2    sing N N 335 
LYS   CB    HB3    sing N N 336 
LYS   CG    CD     sing N N 337 
LYS   CG    HG2    sing N N 338 
LYS   CG    HG3    sing N N 339 
LYS   CD    CE     sing N N 340 
LYS   CD    HD2    sing N N 341 
LYS   CD    HD3    sing N N 342 
LYS   CE    NZ     sing N N 343 
LYS   CE    HE2    sing N N 344 
LYS   CE    HE3    sing N N 345 
LYS   NZ    HZ1    sing N N 346 
LYS   NZ    HZ2    sing N N 347 
LYS   NZ    HZ3    sing N N 348 
LYS   OXT   HXT    sing N N 349 
MET   N     CA     sing N N 350 
MET   N     H      sing N N 351 
MET   N     H2     sing N N 352 
MET   CA    C      sing N N 353 
MET   CA    CB     sing N N 354 
MET   CA    HA     sing N N 355 
MET   C     O      doub N N 356 
MET   C     OXT    sing N N 357 
MET   CB    CG     sing N N 358 
MET   CB    HB2    sing N N 359 
MET   CB    HB3    sing N N 360 
MET   CG    SD     sing N N 361 
MET   CG    HG2    sing N N 362 
MET   CG    HG3    sing N N 363 
MET   SD    CE     sing N N 364 
MET   CE    HE1    sing N N 365 
MET   CE    HE2    sing N N 366 
MET   CE    HE3    sing N N 367 
MET   OXT   HXT    sing N N 368 
PHE   N     CA     sing N N 369 
PHE   N     H      sing N N 370 
PHE   N     H2     sing N N 371 
PHE   CA    C      sing N N 372 
PHE   CA    CB     sing N N 373 
PHE   CA    HA     sing N N 374 
PHE   C     O      doub N N 375 
PHE   C     OXT    sing N N 376 
PHE   CB    CG     sing N N 377 
PHE   CB    HB2    sing N N 378 
PHE   CB    HB3    sing N N 379 
PHE   CG    CD1    doub Y N 380 
PHE   CG    CD2    sing Y N 381 
PHE   CD1   CE1    sing Y N 382 
PHE   CD1   HD1    sing N N 383 
PHE   CD2   CE2    doub Y N 384 
PHE   CD2   HD2    sing N N 385 
PHE   CE1   CZ     doub Y N 386 
PHE   CE1   HE1    sing N N 387 
PHE   CE2   CZ     sing Y N 388 
PHE   CE2   HE2    sing N N 389 
PHE   CZ    HZ     sing N N 390 
PHE   OXT   HXT    sing N N 391 
PRO   N     CA     sing N N 392 
PRO   N     CD     sing N N 393 
PRO   N     H      sing N N 394 
PRO   CA    C      sing N N 395 
PRO   CA    CB     sing N N 396 
PRO   CA    HA     sing N N 397 
PRO   C     O      doub N N 398 
PRO   C     OXT    sing N N 399 
PRO   CB    CG     sing N N 400 
PRO   CB    HB2    sing N N 401 
PRO   CB    HB3    sing N N 402 
PRO   CG    CD     sing N N 403 
PRO   CG    HG2    sing N N 404 
PRO   CG    HG3    sing N N 405 
PRO   CD    HD2    sing N N 406 
PRO   CD    HD3    sing N N 407 
PRO   OXT   HXT    sing N N 408 
SER   N     CA     sing N N 409 
SER   N     H      sing N N 410 
SER   N     H2     sing N N 411 
SER   CA    C      sing N N 412 
SER   CA    CB     sing N N 413 
SER   CA    HA     sing N N 414 
SER   C     O      doub N N 415 
SER   C     OXT    sing N N 416 
SER   CB    OG     sing N N 417 
SER   CB    HB2    sing N N 418 
SER   CB    HB3    sing N N 419 
SER   OG    HG     sing N N 420 
SER   OXT   HXT    sing N N 421 
THR   N     CA     sing N N 422 
THR   N     H      sing N N 423 
THR   N     H2     sing N N 424 
THR   CA    C      sing N N 425 
THR   CA    CB     sing N N 426 
THR   CA    HA     sing N N 427 
THR   C     O      doub N N 428 
THR   C     OXT    sing N N 429 
THR   CB    OG1    sing N N 430 
THR   CB    CG2    sing N N 431 
THR   CB    HB     sing N N 432 
THR   OG1   HG1    sing N N 433 
THR   CG2   HG21   sing N N 434 
THR   CG2   HG22   sing N N 435 
THR   CG2   HG23   sing N N 436 
THR   OXT   HXT    sing N N 437 
TRP   N     CA     sing N N 438 
TRP   N     H      sing N N 439 
TRP   N     H2     sing N N 440 
TRP   CA    C      sing N N 441 
TRP   CA    CB     sing N N 442 
TRP   CA    HA     sing N N 443 
TRP   C     O      doub N N 444 
TRP   C     OXT    sing N N 445 
TRP   CB    CG     sing N N 446 
TRP   CB    HB2    sing N N 447 
TRP   CB    HB3    sing N N 448 
TRP   CG    CD1    doub Y N 449 
TRP   CG    CD2    sing Y N 450 
TRP   CD1   NE1    sing Y N 451 
TRP   CD1   HD1    sing N N 452 
TRP   CD2   CE2    doub Y N 453 
TRP   CD2   CE3    sing Y N 454 
TRP   NE1   CE2    sing Y N 455 
TRP   NE1   HE1    sing N N 456 
TRP   CE2   CZ2    sing Y N 457 
TRP   CE3   CZ3    doub Y N 458 
TRP   CE3   HE3    sing N N 459 
TRP   CZ2   CH2    doub Y N 460 
TRP   CZ2   HZ2    sing N N 461 
TRP   CZ3   CH2    sing Y N 462 
TRP   CZ3   HZ3    sing N N 463 
TRP   CH2   HH2    sing N N 464 
TRP   OXT   HXT    sing N N 465 
TYR   N     CA     sing N N 466 
TYR   N     H      sing N N 467 
TYR   N     H2     sing N N 468 
TYR   CA    C      sing N N 469 
TYR   CA    CB     sing N N 470 
TYR   CA    HA     sing N N 471 
TYR   C     O      doub N N 472 
TYR   C     OXT    sing N N 473 
TYR   CB    CG     sing N N 474 
TYR   CB    HB2    sing N N 475 
TYR   CB    HB3    sing N N 476 
TYR   CG    CD1    doub Y N 477 
TYR   CG    CD2    sing Y N 478 
TYR   CD1   CE1    sing Y N 479 
TYR   CD1   HD1    sing N N 480 
TYR   CD2   CE2    doub Y N 481 
TYR   CD2   HD2    sing N N 482 
TYR   CE1   CZ     doub Y N 483 
TYR   CE1   HE1    sing N N 484 
TYR   CE2   CZ     sing Y N 485 
TYR   CE2   HE2    sing N N 486 
TYR   CZ    OH     sing N N 487 
TYR   OH    HH     sing N N 488 
TYR   OXT   HXT    sing N N 489 
VAL   N     CA     sing N N 490 
VAL   N     H      sing N N 491 
VAL   N     H2     sing N N 492 
VAL   CA    C      sing N N 493 
VAL   CA    CB     sing N N 494 
VAL   CA    HA     sing N N 495 
VAL   C     O      doub N N 496 
VAL   C     OXT    sing N N 497 
VAL   CB    CG1    sing N N 498 
VAL   CB    CG2    sing N N 499 
VAL   CB    HB     sing N N 500 
VAL   CG1   HG11   sing N N 501 
VAL   CG1   HG12   sing N N 502 
VAL   CG1   HG13   sing N N 503 
VAL   CG2   HG21   sing N N 504 
VAL   CG2   HG22   sing N N 505 
VAL   CG2   HG23   sing N N 506 
VAL   OXT   HXT    sing N N 507 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8Z14 
_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]   0.014966 
_atom_sites.fract_transf_matrix[1][2]   0.008641 
_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]   0.017282 
_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]   0.002663 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . MET   A 1 1   ? -11.463 13.742 7.883   1.00 43.99  ?  1   MET   A N     1 
ATOM   2    C CA    . MET   A 1 1   ? -12.511 12.997 8.617   1.00 47.99  ?  1   MET   A CA    1 
ATOM   3    C C     . MET   A 1 1   ? -13.896 13.339 8.064   1.00 49.08  ?  1   MET   A C     1 
ATOM   4    O O     . MET   A 1 1   ? -14.489 12.461 7.454   1.00 57.20  ?  1   MET   A O     1 
ATOM   5    C CB    . MET   A 1 1   ? -12.479 13.289 10.114  1.00 53.56  ?  1   MET   A CB    1 
ATOM   6    C CG    . MET   A 1 1   ? -13.450 12.446 10.921  1.00 63.85  ?  1   MET   A CG    1 
ATOM   7    S SD    . MET   A 1 1   ? -13.131 10.670 10.877  1.00 84.41  ?  1   MET   A SD    1 
ATOM   8    C CE    . MET   A 1 1   ? -11.727 10.608 11.997  1.00 65.04  ?  1   MET   A CE    1 
ATOM   9    N N     . ARG   A 1 2   ? -14.422 14.524 8.300   1.00 42.01  ?  2   ARG   A N     1 
ATOM   10   C CA    . ARG   A 1 2   ? -15.868 14.671 8.006   1.00 52.55  ?  2   ARG   A CA    1 
ATOM   11   C C     . ARG   A 1 2   ? -16.097 14.739 6.492   1.00 45.73  ?  2   ARG   A C     1 
ATOM   12   O O     . ARG   A 1 2   ? -16.949 14.001 6.001   1.00 46.42  ?  2   ARG   A O     1 
ATOM   13   C CB    . ARG   A 1 2   ? -16.539 15.874 8.674   1.00 47.63  ?  2   ARG   A CB    1 
ATOM   14   C CG    . ARG   A 1 2   ? -16.444 15.931 10.188  1.00 56.30  ?  2   ARG   A CG    1 
ATOM   15   C CD    . ARG   A 1 2   ? -17.678 16.609 10.738  1.00 52.14  ?  2   ARG   A CD    1 
ATOM   16   N NE    . ARG   A 1 2   ? -18.826 16.305 9.882   1.00 55.64  ?  2   ARG   A NE    1 
ATOM   17   C CZ    . ARG   A 1 2   ? -20.020 16.849 10.021  1.00 60.66  ?  2   ARG   A CZ    1 
ATOM   18   N NH1   . ARG   A 1 2   ? -20.140 18.029 10.596  1.00 51.28  ?  2   ARG   A NH1   1 
ATOM   19   N NH2   . ARG   A 1 2   ? -21.085 16.207 9.584   1.00 54.60  ?  2   ARG   A NH2   1 
ATOM   20   N N     . VAL   A 1 3   ? -15.362 15.593 5.794   1.00 42.53  ?  3   VAL   A N     1 
ATOM   21   C CA    . VAL   A 1 3   ? -15.647 15.778 4.349   1.00 42.55  ?  3   VAL   A CA    1 
ATOM   22   C C     . VAL   A 1 3   ? -14.416 15.532 3.484   1.00 46.23  ?  3   VAL   A C     1 
ATOM   23   O O     . VAL   A 1 3   ? -13.341 15.969 3.862   1.00 44.90  ?  3   VAL   A O     1 
ATOM   24   C CB    . VAL   A 1 3   ? -16.249 17.154 4.018   1.00 39.48  ?  3   VAL   A CB    1 
ATOM   25   C CG1   . VAL   A 1 3   ? -16.688 17.245 2.566   1.00 36.87  ?  3   VAL   A CG1   1 
ATOM   26   C CG2   . VAL   A 1 3   ? -17.391 17.526 4.947   1.00 34.05  ?  3   VAL   A CG2   1 
ATOM   27   N N     . CYS   A 1 4   ? -14.584 14.759 2.419   1.00 45.60  ?  4   CYS   A N     1 
ATOM   28   C CA    . CYS   A 1 4   ? -13.553 14.620 1.400   1.00 42.99  ?  4   CYS   A CA    1 
ATOM   29   C C     . CYS   A 1 4   ? -13.967 15.480 0.215   1.00 43.63  ?  4   CYS   A C     1 
ATOM   30   O O     . CYS   A 1 4   ? -15.073 15.315 -0.318  1.00 42.56  ?  4   CYS   A O     1 
ATOM   31   C CB    . CYS   A 1 4   ? -13.382 13.159 0.989   1.00 39.72  ?  4   CYS   A CB    1 
ATOM   32   S SG    . CYS   A 1 4   ? -12.293 12.848 -0.417  1.00 54.19  ?  4   CYS   A SG    1 
ATOM   33   N N     . VAL   A 1 5   ? -13.097 16.420 -0.158  1.00 42.00  ?  5   VAL   A N     1 
ATOM   34   C CA    . VAL   A 1 5   ? -13.294 17.324 -1.288  1.00 41.64  ?  5   VAL   A CA    1 
ATOM   35   C C     . VAL   A 1 5   ? -12.420 16.822 -2.419  1.00 43.68  ?  5   VAL   A C     1 
ATOM   36   O O     . VAL   A 1 5   ? -11.197 16.709 -2.267  1.00 47.13  ?  5   VAL   A O     1 
ATOM   37   C CB    . VAL   A 1 5   ? -12.930 18.777 -0.933  1.00 39.93  ?  5   VAL   A CB    1 
ATOM   38   C CG1   . VAL   A 1 5   ? -13.053 19.694 -2.147  1.00 37.45  ?  5   VAL   A CG1   1 
ATOM   39   C CG2   . VAL   A 1 5   ? -13.784 19.272 0.208   1.00 38.34  ?  5   VAL   A CG2   1 
ATOM   40   N N     . ILE   A 1 6   ? -13.027 16.530 -3.556  1.00 40.85  ?  6   ILE   A N     1 
ATOM   41   C CA    . ILE   A 1 6   ? -12.295 16.000 -4.695  1.00 44.71  ?  6   ILE   A CA    1 
ATOM   42   C C     . ILE   A 1 6   ? -12.018 17.192 -5.594  1.00 42.96  ?  6   ILE   A C     1 
ATOM   43   O O     . ILE   A 1 6   ? -12.927 17.722 -6.222  1.00 43.68  ?  6   ILE   A O     1 
ATOM   44   C CB    . ILE   A 1 6   ? -13.076 14.889 -5.401  1.00 40.95  ?  6   ILE   A CB    1 
ATOM   45   C CG1   . ILE   A 1 6   ? -13.396 13.784 -4.384  1.00 42.35  ?  6   ILE   A CG1   1 
ATOM   46   C CG2   . ILE   A 1 6   ? -12.281 14.319 -6.528  1.00 42.11  ?  6   ILE   A CG2   1 
ATOM   47   C CD1   . ILE   A 1 6   ? -14.039 12.555 -5.002  1.00 46.05  ?  6   ILE   A CD1   1 
ATOM   48   N N     . GLY   A 1 7   ? -10.765 17.645 -5.614  1.00 44.56  ?  7   GLY   A N     1 
ATOM   49   C CA    . GLY   A 1 7   ? -10.380 18.783 -6.425  1.00 44.85  ?  7   GLY   A CA    1 
ATOM   50   C C     . GLY   A 1 7   ? -9.886  19.968 -5.616  1.00 47.66  ?  7   GLY   A C     1 
ATOM   51   O O     . GLY   A 1 7   ? -10.516 20.355 -4.627  1.00 46.99  ?  7   GLY   A O     1 
ATOM   52   N N     . ALA   A 1 8   ? -8.764  20.565 -6.013  1.00 46.27  ?  8   ALA   A N     1 
ATOM   53   C CA    . ALA   A 1 8   ? -8.290  21.789 -5.373  1.00 41.88  ?  8   ALA   A CA    1 
ATOM   54   C C     . ALA   A 1 8   ? -8.063  22.876 -6.420  1.00 40.30  ?  8   ALA   A C     1 
ATOM   55   O O     . ALA   A 1 8   ? -7.099  23.652 -6.371  1.00 41.38  ?  8   ALA   A O     1 
ATOM   56   C CB    . ALA   A 1 8   ? -7.037  21.534 -4.535  1.00 42.52  ?  8   ALA   A CB    1 
ATOM   57   N N     . GLY   A 1 9   ? -8.933  22.930 -7.400  1.00 43.67  ?  9   GLY   A N     1 
ATOM   58   C CA    . GLY   A 1 9   ? -9.040  24.108 -8.227  1.00 43.82  ?  9   GLY   A CA    1 
ATOM   59   C C     . GLY   A 1 9   ? -9.917  25.130 -7.531  1.00 40.82  ?  9   GLY   A C     1 
ATOM   60   O O     . GLY   A 1 9   ? -10.151 25.078 -6.320  1.00 35.74  ?  9   GLY   A O     1 
ATOM   61   N N     . LEU   A 1 10  ? -10.440 26.057 -8.333  1.00 41.70  ?  10  LEU   A N     1 
ATOM   62   C CA    . LEU   A 1 10  ? -11.189 27.179 -7.791  1.00 40.19  ?  10  LEU   A CA    1 
ATOM   63   C C     . LEU   A 1 10  ? -12.432 26.722 -7.035  1.00 39.13  ?  10  LEU   A C     1 
ATOM   64   O O     . LEU   A 1 10  ? -12.846 27.374 -6.070  1.00 38.04  ?  10  LEU   A O     1 
ATOM   65   C CB    . LEU   A 1 10  ? -11.551 28.140 -8.927  1.00 41.43  ?  10  LEU   A CB    1 
ATOM   66   C CG    . LEU   A 1 10  ? -12.531 29.256 -8.558  1.00 46.41  ?  10  LEU   A CG    1 
ATOM   67   C CD1   . LEU   A 1 10  ? -12.056 30.581 -9.085  1.00 47.60  ?  10  LEU   A CD1   1 
ATOM   68   C CD2   . LEU   A 1 10  ? -13.932 28.959 -9.084  1.00 45.94  ?  10  LEU   A CD2   1 
ATOM   69   N N     . SER   A 1 11  ? -13.039 25.611 -7.444  1.00 42.41  ?  11  SER   A N     1 
ATOM   70   C CA    . SER   A 1 11  ? -14.242 25.169 -6.744  1.00 43.67  ?  11  SER   A CA    1 
ATOM   71   C C     . SER   A 1 11  ? -13.907 24.455 -5.443  1.00 38.30  ?  11  SER   A C     1 
ATOM   72   O O     . SER   A 1 11  ? -14.506 24.750 -4.404  1.00 34.94  ?  11  SER   A O     1 
ATOM   73   C CB    . SER   A 1 11  ? -15.086 24.276 -7.648  1.00 41.41  ?  11  SER   A CB    1 
ATOM   74   O OG    . SER   A 1 11  ? -15.708 25.080 -8.638  1.00 41.29  ?  11  SER   A OG    1 
ATOM   75   N N     . GLY   A 1 12  ? -12.953 23.526 -5.479  1.00 40.05  ?  12  GLY   A N     1 
ATOM   76   C CA    . GLY   A 1 12  ? -12.556 22.836 -4.262  1.00 40.80  ?  12  GLY   A CA    1 
ATOM   77   C C     . GLY   A 1 12  ? -11.941 23.745 -3.215  1.00 38.51  ?  12  GLY   A C     1 
ATOM   78   O O     . GLY   A 1 12  ? -12.037 23.467 -2.018  1.00 38.68  ?  12  GLY   A O     1 
ATOM   79   N N     . LEU   A 1 13  ? -11.308 24.840 -3.639  1.00 41.66  ?  13  LEU   A N     1 
ATOM   80   C CA    . LEU   A 1 13  ? -10.797 25.806 -2.669  1.00 42.09  ?  13  LEU   A CA    1 
ATOM   81   C C     . LEU   A 1 13  ? -11.941 26.584 -2.011  1.00 43.49  ?  13  LEU   A C     1 
ATOM   82   O O     . LEU   A 1 13  ? -11.982 26.718 -0.775  1.00 41.52  ?  13  LEU   A O     1 
ATOM   83   C CB    . LEU   A 1 13  ? -9.785  26.744 -3.333  1.00 36.80  ?  13  LEU   A CB    1 
ATOM   84   C CG    . LEU   A 1 13  ? -8.467  26.126 -3.839  1.00 41.01  ?  13  LEU   A CG    1 
ATOM   85   C CD1   . LEU   A 1 13  ? -7.664  27.134 -4.705  1.00 33.51  ?  13  LEU   A CD1   1 
ATOM   86   C CD2   . LEU   A 1 13  ? -7.592  25.500 -2.701  1.00 33.28  ?  13  LEU   A CD2   1 
ATOM   87   N N     . ALA   A 1 14  ? -12.902 27.077 -2.808  1.00 36.50  ?  14  ALA   A N     1 
ATOM   88   C CA    . ALA   A 1 14  ? -14.066 27.717 -2.199  1.00 37.94  ?  14  ALA   A CA    1 
ATOM   89   C C     . ALA   A 1 14  ? -14.739 26.782 -1.196  1.00 41.26  ?  14  ALA   A C     1 
ATOM   90   O O     . ALA   A 1 14  ? -15.223 27.229 -0.148  1.00 41.54  ?  14  ALA   A O     1 
ATOM   91   C CB    . ALA   A 1 14  ? -15.060 28.172 -3.264  1.00 32.04  ?  14  ALA   A CB    1 
ATOM   92   N N     . VAL   A 1 15  ? -14.732 25.477 -1.478  1.00 35.76  ?  15  VAL   A N     1 
ATOM   93   C CA    . VAL   A 1 15  ? -15.362 24.508 -0.590  1.00 39.47  ?  15  VAL   A CA    1 
ATOM   94   C C     . VAL   A 1 15  ? -14.566 24.382 0.714   1.00 44.13  ?  15  VAL   A C     1 
ATOM   95   O O     . VAL   A 1 15  ? -15.135 24.422 1.821   1.00 35.52  ?  15  VAL   A O     1 
ATOM   96   C CB    . VAL   A 1 15  ? -15.514 23.157 -1.319  1.00 39.67  ?  15  VAL   A CB    1 
ATOM   97   C CG1   . VAL   A 1 15  ? -15.969 22.040 -0.385  1.00 32.52  ?  15  VAL   A CG1   1 
ATOM   98   C CG2   . VAL   A 1 15  ? -16.486 23.302 -2.481  1.00 39.68  ?  15  VAL   A CG2   1 
ATOM   99   N N     . GLY   A 1 16  ? -13.237 24.260 0.608   1.00 37.56  ?  16  GLY   A N     1 
ATOM   100  C CA    . GLY   A 1 16  ? -12.419 24.195 1.814   1.00 40.37  ?  16  GLY   A CA    1 
ATOM   101  C C     . GLY   A 1 16  ? -12.507 25.462 2.645   1.00 44.90  ?  16  GLY   A C     1 
ATOM   102  O O     . GLY   A 1 16  ? -12.559 25.412 3.875   1.00 44.20  ?  16  GLY   A O     1 
ATOM   103  N N     . HIS   A 1 17  ? -12.529 26.615 1.983   1.00 43.73  ?  17  HIS   A N     1 
ATOM   104  C CA    . HIS   A 1 17  ? -12.764 27.873 2.678   1.00 42.79  ?  17  HIS   A CA    1 
ATOM   105  C C     . HIS   A 1 17  ? -14.091 27.847 3.427   1.00 44.01  ?  17  HIS   A C     1 
ATOM   106  O O     . HIS   A 1 17  ? -14.172 28.270 4.585   1.00 41.69  ?  17  HIS   A O     1 
ATOM   107  C CB    . HIS   A 1 17  ? -12.743 29.024 1.668   1.00 43.69  ?  17  HIS   A CB    1 
ATOM   108  C CG    . HIS   A 1 17  ? -12.667 30.384 2.291   1.00 44.43  ?  17  HIS   A CG    1 
ATOM   109  N ND1   . HIS   A 1 17  ? -11.967 30.640 3.455   1.00 39.63  ?  17  HIS   A ND1   1 
ATOM   110  C CD2   . HIS   A 1 17  ? -13.179 31.573 1.891   1.00 44.42  ?  17  HIS   A CD2   1 
ATOM   111  C CE1   . HIS   A 1 17  ? -12.052 31.926 3.743   1.00 37.59  ?  17  HIS   A CE1   1 
ATOM   112  N NE2   . HIS   A 1 17  ? -12.789 32.514 2.818   1.00 42.84  ?  17  HIS   A NE2   1 
ATOM   113  N N     . ALA   A 1 18  ? -15.152 27.354 2.774   1.00 41.11  ?  18  ALA   A N     1 
ATOM   114  C CA    . ALA   A 1 18  ? -16.464 27.362 3.409   1.00 38.76  ?  18  ALA   A CA    1 
ATOM   115  C C     . ALA   A 1 18  ? -16.525 26.344 4.533   1.00 41.97  ?  18  ALA   A C     1 
ATOM   116  O O     . ALA   A 1 18  ? -17.138 26.597 5.574   1.00 43.71  ?  18  ALA   A O     1 
ATOM   117  C CB    . ALA   A 1 18  ? -17.558 27.086 2.384   1.00 37.30  ?  18  ALA   A CB    1 
ATOM   118  N N     . LEU   A 1 19  ? -15.884 25.196 4.341   1.00 37.60  ?  19  LEU   A N     1 
ATOM   119  C CA    . LEU   A 1 19  ? -15.810 24.215 5.408   1.00 39.54  ?  19  LEU   A CA    1 
ATOM   120  C C     . LEU   A 1 19  ? -14.959 24.720 6.569   1.00 45.40  ?  19  LEU   A C     1 
ATOM   121  O O     . LEU   A 1 19  ? -15.311 24.522 7.742   1.00 46.57  ?  19  LEU   A O     1 
ATOM   122  C CB    . LEU   A 1 19  ? -15.265 22.913 4.852   1.00 41.78  ?  19  LEU   A CB    1 
ATOM   123  C CG    . LEU   A 1 19  ? -16.241 22.329 3.835   1.00 37.51  ?  19  LEU   A CG    1 
ATOM   124  C CD1   . LEU   A 1 19  ? -15.635 21.112 3.188   1.00 33.06  ?  19  LEU   A CD1   1 
ATOM   125  C CD2   . LEU   A 1 19  ? -17.558 22.004 4.530   1.00 33.77  ?  19  LEU   A CD2   1 
ATOM   126  N N     . LYS   A 1 20  ? -13.850 25.402 6.268   1.00 41.20  ?  20  LYS   A N     1 
ATOM   127  C CA    . LYS   A 1 20  ? -12.996 25.890 7.343   1.00 42.42  ?  20  LYS   A CA    1 
ATOM   128  C C     . LYS   A 1 20  ? -13.704 26.942 8.189   1.00 47.02  ?  20  LYS   A C     1 
ATOM   129  O O     . LYS   A 1 20  ? -13.534 26.975 9.414   1.00 46.73  ?  20  LYS   A O     1 
ATOM   130  C CB    . LYS   A 1 20  ? -11.696 26.447 6.774   1.00 45.89  ?  20  LYS   A CB    1 
ATOM   131  C CG    . LYS   A 1 20  ? -10.668 26.828 7.821   1.00 46.24  ?  20  LYS   A CG    1 
ATOM   132  C CD    . LYS   A 1 20  ? -9.426  25.962 7.734   1.00 44.55  ?  20  LYS   A CD    1 
ATOM   133  C CE    . LYS   A 1 20  ? -8.247  26.692 8.318   1.00 41.58  ?  20  LYS   A CE    1 
ATOM   134  N NZ    . LYS   A 1 20  ? -7.180  25.717 8.671   1.00 57.51  ?  20  LYS   A NZ    1 
ATOM   135  N N     . GLU   A 1 21  ? -14.538 27.776 7.568   1.00 48.40  ?  21  GLU   A N     1 
ATOM   136  C CA    . GLU   A 1 21  ? -15.258 28.794 8.329   1.00 44.54  ?  21  GLU   A CA    1 
ATOM   137  C C     . GLU   A 1 21  ? -16.238 28.179 9.320   1.00 44.33  ?  21  GLU   A C     1 
ATOM   138  O O     . GLU   A 1 21  ? -16.416 28.701 10.422  1.00 49.48  ?  21  GLU   A O     1 
ATOM   139  C CB    . GLU   A 1 21  ? -15.993 29.744 7.389   1.00 40.95  ?  21  GLU   A CB    1 
ATOM   140  C CG    . GLU   A 1 21  ? -15.062 30.628 6.556   1.00 55.72  ?  21  GLU   A CG    1 
ATOM   141  C CD    . GLU   A 1 21  ? -14.115 31.466 7.403   1.00 64.88  ?  21  GLU   A CD    1 
ATOM   142  O OE1   . GLU   A 1 21  ? -12.932 31.044 7.579   1.00 65.86  ?  21  GLU   A OE1   1 
ATOM   143  O OE2   . GLU   A 1 21  ? -14.571 32.531 7.902   1.00 68.11  ?  21  GLU   A OE2   1 
ATOM   144  N N     . ARG   A 1 22  ? -16.909 27.095 8.957   1.00 44.24  ?  22  ARG   A N     1 
ATOM   145  C CA    . ARG   A 1 22  ? -17.834 26.490 9.901   1.00 44.57  ?  22  ARG   A CA    1 
ATOM   146  C C     . ARG   A 1 22  ? -17.138 25.529 10.845  1.00 48.29  ?  22  ARG   A C     1 
ATOM   147  O O     . ARG   A 1 22  ? -17.806 24.868 11.650  1.00 51.67  ?  22  ARG   A O     1 
ATOM   148  C CB    . ARG   A 1 22  ? -18.974 25.796 9.162   1.00 43.28  ?  22  ARG   A CB    1 
ATOM   149  C CG    . ARG   A 1 22  ? -19.823 26.776 8.403   1.00 44.89  ?  22  ARG   A CG    1 
ATOM   150  C CD    . ARG   A 1 22  ? -21.223 26.243 8.185   1.00 48.84  ?  22  ARG   A CD    1 
ATOM   151  N NE    . ARG   A 1 22  ? -22.155 26.520 9.281   1.00 48.84  ?  22  ARG   A NE    1 
ATOM   152  C CZ    . ARG   A 1 22  ? -22.837 27.658 9.442   1.00 51.25  ?  22  ARG   A CZ    1 
ATOM   153  N NH1   . ARG   A 1 22  ? -22.689 28.683 8.608   1.00 42.94  ?  22  ARG   A NH1   1 
ATOM   154  N NH2   . ARG   A 1 22  ? -23.683 27.773 10.456  1.00 61.82  ?  22  ARG   A NH2   1 
ATOM   155  N N     . GLY   A 1 23  ? -15.813 25.457 10.776  1.00 47.79  ?  23  GLY   A N     1 
ATOM   156  C CA    . GLY   A 1 23  ? -15.078 24.558 11.630  1.00 42.65  ?  23  GLY   A CA    1 
ATOM   157  C C     . GLY   A 1 23  ? -15.270 23.113 11.280  1.00 44.42  ?  23  GLY   A C     1 
ATOM   158  O O     . GLY   A 1 23  ? -15.111 22.242 12.144  1.00 48.93  ?  23  GLY   A O     1 
ATOM   159  N N     . ILE   A 1 24  ? -15.606 22.824 10.036  1.00 44.70  ?  24  ILE   A N     1 
ATOM   160  C CA    . ILE   A 1 24  ? -15.860 21.453 9.625   1.00 46.03  ?  24  ILE   A CA    1 
ATOM   161  C C     . ILE   A 1 24  ? -14.555 20.822 9.179   1.00 41.77  ?  24  ILE   A C     1 
ATOM   162  O O     . ILE   A 1 24  ? -13.784 21.410 8.418   1.00 47.84  ?  24  ILE   A O     1 
ATOM   163  C CB    . ILE   A 1 24  ? -16.921 21.397 8.523   1.00 44.00  ?  24  ILE   A CB    1 
ATOM   164  C CG1   . ILE   A 1 24  ? -18.020 22.395 8.870   1.00 39.13  ?  24  ILE   A CG1   1 
ATOM   165  C CG2   . ILE   A 1 24  ? -17.426 19.965 8.370   1.00 38.92  ?  24  ILE   A CG2   1 
ATOM   166  C CD1   . ILE   A 1 24  ? -19.230 22.271 8.034   1.00 46.82  ?  24  ILE   A CD1   1 
ATOM   167  N N     . SER   A 1 25  ? -14.287 19.647 9.706   1.00 45.10  ?  25  SER   A N     1 
ATOM   168  C CA    . SER   A 1 25  ? -13.104 18.893 9.343   1.00 43.06  ?  25  SER   A CA    1 
ATOM   169  C C     . SER   A 1 25  ? -13.220 18.394 7.907   1.00 47.31  ?  25  SER   A C     1 
ATOM   170  O O     . SER   A 1 25  ? -14.264 17.877 7.492   1.00 42.98  ?  25  SER   A O     1 
ATOM   171  C CB    . SER   A 1 25  ? -12.951 17.731 10.336  1.00 44.32  ?  25  SER   A CB    1 
ATOM   172  O OG    . SER   A 1 25  ? -12.360 16.583 9.756   1.00 53.90  ?  25  SER   A OG    1 
ATOM   173  N N     . PHE   A 1 26  ? -12.140 18.537 7.147   1.00 41.76  ?  26  PHE   A N     1 
ATOM   174  C CA    . PHE   A 1 26  ? -12.179 18.147 5.751   1.00 46.09  ?  26  PHE   A CA    1 
ATOM   175  C C     . PHE   A 1 26  ? -10.766 17.915 5.253   1.00 49.91  ?  26  PHE   A C     1 
ATOM   176  O O     . PHE   A 1 26  ? -9.817  18.527 5.734   1.00 57.56  ?  26  PHE   A O     1 
ATOM   177  C CB    . PHE   A 1 26  ? -12.838 19.230 4.900   1.00 43.04  ?  26  PHE   A CB    1 
ATOM   178  C CG    . PHE   A 1 26  ? -11.953 20.385 4.686   1.00 46.71  ?  26  PHE   A CG    1 
ATOM   179  C CD1   . PHE   A 1 26  ? -11.760 21.312 5.701   1.00 45.43  ?  26  PHE   A CD1   1 
ATOM   180  C CD2   . PHE   A 1 26  ? -11.232 20.506 3.512   1.00 45.12  ?  26  PHE   A CD2   1 
ATOM   181  C CE1   . PHE   A 1 26  ? -10.893 22.373 5.536   1.00 48.90  ?  26  PHE   A CE1   1 
ATOM   182  C CE2   . PHE   A 1 26  ? -10.365 21.574 3.334   1.00 51.40  ?  26  PHE   A CE2   1 
ATOM   183  C CZ    . PHE   A 1 26  ? -10.191 22.507 4.351   1.00 49.72  ?  26  PHE   A CZ    1 
ATOM   184  N N     . VAL   A 1 27  ? -10.644 17.054 4.265   1.00 46.85  ?  27  VAL   A N     1 
ATOM   185  C CA    . VAL   A 1 27  ? -9.416  16.915 3.500   1.00 43.34  ?  27  VAL   A CA    1 
ATOM   186  C C     . VAL   A 1 27  ? -9.760  17.171 2.040   1.00 48.47  ?  27  VAL   A C     1 
ATOM   187  O O     . VAL   A 1 27  ? -10.890 16.947 1.591   1.00 48.08  ?  27  VAL   A O     1 
ATOM   188  C CB    . VAL   A 1 27  ? -8.762  15.525 3.690   1.00 43.49  ?  27  VAL   A CB    1 
ATOM   189  C CG1   . VAL   A 1 27  ? -9.663  14.424 3.137   1.00 45.77  ?  27  VAL   A CG1   1 
ATOM   190  C CG2   . VAL   A 1 27  ? -7.353  15.483 3.044   1.00 49.55  ?  27  VAL   A CG2   1 
ATOM   191  N N     . CYS   A 1 28  ? -8.783  17.667 1.301   1.00 46.58  ?  28  CYS   A N     1 
ATOM   192  C CA    . CYS   A 1 28  ? -8.968  18.041 -0.088  1.00 41.53  ?  28  CYS   A CA    1 
ATOM   193  C C     . CYS   A 1 28  ? -7.956  17.269 -0.916  1.00 46.26  ?  28  CYS   A C     1 
ATOM   194  O O     . CYS   A 1 28  ? -6.747  17.452 -0.743  1.00 51.89  ?  28  CYS   A O     1 
ATOM   195  C CB    . CYS   A 1 28  ? -8.776  19.543 -0.252  1.00 47.42  ?  28  CYS   A CB    1 
ATOM   196  S SG    . CYS   A 1 28  ? -9.170  20.075 -1.865  1.00 58.73  ?  28  CYS   A SG    1 
ATOM   197  N N     . LEU   A 1 29  ? -8.441  16.401 -1.797  1.00 43.79  ?  29  LEU   A N     1 
ATOM   198  C CA    . LEU   A 1 29  ? -7.580  15.532 -2.584  1.00 45.97  ?  29  LEU   A CA    1 
ATOM   199  C C     . LEU   A 1 29  ? -7.478  16.098 -3.993  1.00 45.53  ?  29  LEU   A C     1 
ATOM   200  O O     . LEU   A 1 29  ? -8.495  16.462 -4.590  1.00 49.02  ?  29  LEU   A O     1 
ATOM   201  C CB    . LEU   A 1 29  ? -8.128  14.101 -2.605  1.00 49.04  ?  29  LEU   A CB    1 
ATOM   202  C CG    . LEU   A 1 29  ? -8.594  13.556 -1.239  1.00 50.30  ?  29  LEU   A CG    1 
ATOM   203  C CD1   . LEU   A 1 29  ? -8.918  12.052 -1.277  1.00 49.89  ?  29  LEU   A CD1   1 
ATOM   204  C CD2   . LEU   A 1 29  ? -7.548  13.834 -0.153  1.00 52.27  ?  29  LEU   A CD2   1 
ATOM   205  N N     . GLU   A 1 30  ? -6.254  16.171 -4.514  1.00 46.06  ?  30  GLU   A N     1 
ATOM   206  C CA    . GLU   A 1 30  ? -5.974  16.825 -5.785  1.00 48.78  ?  30  GLU   A CA    1 
ATOM   207  C C     . GLU   A 1 30  ? -4.809  16.129 -6.491  1.00 56.99  ?  30  GLU   A C     1 
ATOM   208  O O     . GLU   A 1 30  ? -3.750  15.960 -5.876  1.00 56.76  ?  30  GLU   A O     1 
ATOM   209  C CB    . GLU   A 1 30  ? -5.669  18.304 -5.545  1.00 44.95  ?  30  GLU   A CB    1 
ATOM   210  C CG    . GLU   A 1 30  ? -5.004  18.962 -6.686  1.00 42.72  ?  30  GLU   A CG    1 
ATOM   211  C CD    . GLU   A 1 30  ? -5.958  19.231 -7.800  1.00 48.14  ?  30  GLU   A CD    1 
ATOM   212  O OE1   . GLU   A 1 30  ? -6.988  19.898 -7.572  1.00 45.32  ?  30  GLU   A OE1   1 
ATOM   213  O OE2   . GLU   A 1 30  ? -5.696  18.732 -8.912  1.00 54.82  ?  30  GLU   A OE2   1 
ATOM   214  N N     . LYS   A 1 31  ? -5.001  15.740 -7.775  1.00 53.28  ?  31  LYS   A N     1 
ATOM   215  C CA    . LYS   A 1 31  ? -3.987  14.965 -8.506  1.00 52.08  ?  31  LYS   A CA    1 
ATOM   216  C C     . LYS   A 1 31  ? -2.755  15.802 -8.812  1.00 55.24  ?  31  LYS   A C     1 
ATOM   217  O O     . LYS   A 1 31  ? -1.623  15.330 -8.666  1.00 60.04  ?  31  LYS   A O     1 
ATOM   218  C CB    . LYS   A 1 31  ? -4.515  14.445 -9.844  1.00 57.84  ?  31  LYS   A CB    1 
ATOM   219  C CG    . LYS   A 1 31  ? -5.961  14.163 -9.932  1.00 60.44  ?  31  LYS   A CG    1 
ATOM   220  C CD    . LYS   A 1 31  ? -6.511  14.470 -11.310 1.00 55.09  ?  31  LYS   A CD    1 
ATOM   221  C CE    . LYS   A 1 31  ? -6.428  13.273 -12.241 1.00 67.94  ?  31  LYS   A CE    1 
ATOM   222  N NZ    . LYS   A 1 31  ? -6.694  13.711 -13.637 1.00 64.70  ?  31  LYS   A NZ    1 
ATOM   223  N N     . ALA   A 1 32  ? -2.963  17.022 -9.313  1.00 52.17  ?  32  ALA   A N     1 
ATOM   224  C CA    . ALA   A 1 32  ? -1.868  17.899 -9.694  1.00 51.28  ?  32  ALA   A CA    1 
ATOM   225  C C     . ALA   A 1 32  ? -0.906  18.123 -8.527  1.00 56.32  ?  32  ALA   A C     1 
ATOM   226  O O     . ALA   A 1 32  ? -1.246  17.901 -7.354  1.00 52.95  ?  32  ALA   A O     1 
ATOM   227  C CB    . ALA   A 1 32  ? -2.404  19.243 -10.190 1.00 52.28  ?  32  ALA   A CB    1 
ATOM   228  N N     . PRO   A 1 33  ? 0.329   18.524 -8.826  1.00 56.97  ?  33  PRO   A N     1 
ATOM   229  C CA    . PRO   A 1 33  ? 1.283   18.802 -7.748  1.00 57.99  ?  33  PRO   A CA    1 
ATOM   230  C C     . PRO   A 1 33  ? 1.019   20.104 -7.000  1.00 61.89  ?  33  PRO   A C     1 
ATOM   231  O O     . PRO   A 1 33  ? 1.786   20.428 -6.081  1.00 59.00  ?  33  PRO   A O     1 
ATOM   232  C CB    . PRO   A 1 33  ? 2.638   18.830 -8.478  1.00 50.80  ?  33  PRO   A CB    1 
ATOM   233  C CG    . PRO   A 1 33  ? 2.317   18.973 -9.905  1.00 56.23  ?  33  PRO   A CG    1 
ATOM   234  C CD    . PRO   A 1 33  ? 0.988   18.386 -10.137 1.00 51.46  ?  33  PRO   A CD    1 
ATOM   235  N N     . ASP   A 1 34  ? -0.048  20.835 -7.342  1.00 61.03  ?  34  ASP   A N     1 
ATOM   236  C CA    . ASP   A 1 34  ? -0.349  22.110 -6.702  1.00 56.27  ?  34  ASP   A CA    1 
ATOM   237  C C     . ASP   A 1 34  ? -1.807  22.480 -6.958  1.00 55.62  ?  34  ASP   A C     1 
ATOM   238  O O     . ASP   A 1 34  ? -2.444  21.986 -7.898  1.00 53.51  ?  34  ASP   A O     1 
ATOM   239  C CB    . ASP   A 1 34  ? 0.586   23.213 -7.208  1.00 54.03  ?  34  ASP   A CB    1 
ATOM   240  C CG    . ASP   A 1 34  ? 0.813   24.329 -6.185  1.00 53.85  ?  34  ASP   A CG    1 
ATOM   241  O OD1   . ASP   A 1 34  ? 0.196   24.334 -5.099  1.00 50.23  ?  34  ASP   A OD1   1 
ATOM   242  O OD2   . ASP   A 1 34  ? 1.623   25.224 -6.490  1.00 56.52  ?  34  ASP   A OD2   1 
ATOM   243  N N     . VAL   A 1 35  ? -2.325  23.367 -6.104  1.00 48.92  ?  35  VAL   A N     1 
ATOM   244  C CA    . VAL   A 1 35  ? -3.693  23.859 -6.206  1.00 46.51  ?  35  VAL   A CA    1 
ATOM   245  C C     . VAL   A 1 35  ? -3.784  24.788 -7.404  1.00 44.47  ?  35  VAL   A C     1 
ATOM   246  O O     . VAL   A 1 35  ? -2.759  25.197 -7.958  1.00 43.83  ?  35  VAL   A O     1 
ATOM   247  C CB    . VAL   A 1 35  ? -4.126  24.575 -4.913  1.00 48.57  ?  35  VAL   A CB    1 
ATOM   248  C CG1   . VAL   A 1 35  ? -3.752  23.742 -3.673  1.00 40.41  ?  35  VAL   A CG1   1 
ATOM   249  C CG2   . VAL   A 1 35  ? -3.537  25.976 -4.859  1.00 44.22  ?  35  VAL   A CG2   1 
ATOM   250  N N     . GLY   A 1 36  ? -4.998  25.131 -7.820  1.00 42.94  ?  36  GLY   A N     1 
ATOM   251  C CA    . GLY   A 1 36  ? -5.130  26.032 -8.956  1.00 41.74  ?  36  GLY   A CA    1 
ATOM   252  C C     . GLY   A 1 36  ? -6.030  25.535 -10.072 1.00 45.24  ?  36  GLY   A C     1 
ATOM   253  O O     . GLY   A 1 36  ? -6.579  26.338 -10.840 1.00 44.48  ?  36  GLY   A O     1 
ATOM   254  N N     . GLY   A 1 37  ? -6.205  24.213 -10.169 1.00 41.93  ?  37  GLY   A N     1 
ATOM   255  C CA    . GLY   A 1 37  ? -7.064  23.687 -11.211 1.00 46.27  ?  37  GLY   A CA    1 
ATOM   256  C C     . GLY   A 1 37  ? -6.453  23.889 -12.586 1.00 50.26  ?  37  GLY   A C     1 
ATOM   257  O O     . GLY   A 1 37  ? -5.231  23.802 -12.774 1.00 52.84  ?  37  GLY   A O     1 
ATOM   258  N N     . ILE   A 1 38  ? -7.319  24.181 -13.563 1.00 47.27  ?  38  ILE   A N     1 
ATOM   259  C CA    . ILE   A 1 38  ? -6.856  24.299 -14.947 1.00 47.43  ?  38  ILE   A CA    1 
ATOM   260  C C     . ILE   A 1 38  ? -5.834  25.421 -15.090 1.00 52.35  ?  38  ILE   A C     1 
ATOM   261  O O     . ILE   A 1 38  ? -4.913  25.326 -15.909 1.00 52.04  ?  38  ILE   A O     1 
ATOM   262  C CB    . ILE   A 1 38  ? -8.040  24.500 -15.924 1.00 47.72  ?  38  ILE   A CB    1 
ATOM   263  C CG1   . ILE   A 1 38  ? -8.938  25.651 -15.479 1.00 48.33  ?  38  ILE   A CG1   1 
ATOM   264  C CG2   . ILE   A 1 38  ? -8.847  23.227 -16.080 1.00 39.54  ?  38  ILE   A CG2   1 
ATOM   265  C CD1   . ILE   A 1 38  ? -9.619  26.346 -16.631 1.00 52.84  ?  38  ILE   A CD1   1 
ATOM   266  N N     . TRP   A 1 39  ? -5.958  26.484 -14.288 1.00 51.38  ?  39  TRP   A N     1 
ATOM   267  C CA    . TRP   A 1 39  ? -5.110  27.654 -14.468 1.00 48.97  ?  39  TRP   A CA    1 
ATOM   268  C C     . TRP   A 1 39  ? -3.661  27.370 -14.133 1.00 49.61  ?  39  TRP   A C     1 
ATOM   269  O O     . TRP   A 1 39  ? -2.767  28.078 -14.610 1.00 52.47  ?  39  TRP   A O     1 
ATOM   270  C CB    . TRP   A 1 39  ? -5.634  28.786 -13.607 1.00 51.43  ?  39  TRP   A CB    1 
ATOM   271  C CG    . TRP   A 1 39  ? -7.026  29.066 -13.919 1.00 47.83  ?  39  TRP   A CG    1 
ATOM   272  C CD1   . TRP   A 1 39  ? -8.118  28.611 -13.262 1.00 48.45  ?  39  TRP   A CD1   1 
ATOM   273  C CD2   . TRP   A 1 39  ? -7.502  29.850 -15.004 1.00 50.55  ?  39  TRP   A CD2   1 
ATOM   274  N NE1   . TRP   A 1 39  ? -9.256  29.079 -13.860 1.00 45.17  ?  39  TRP   A NE1   1 
ATOM   275  C CE2   . TRP   A 1 39  ? -8.901  29.849 -14.933 1.00 43.22  ?  39  TRP   A CE2   1 
ATOM   276  C CE3   . TRP   A 1 39  ? -6.876  30.568 -16.025 1.00 52.27  ?  39  TRP   A CE3   1 
ATOM   277  C CZ2   . TRP   A 1 39  ? -9.687  30.529 -15.839 1.00 48.95  ?  39  TRP   A CZ2   1 
ATOM   278  C CZ3   . TRP   A 1 39  ? -7.652  31.243 -16.916 1.00 48.31  ?  39  TRP   A CZ3   1 
ATOM   279  C CH2   . TRP   A 1 39  ? -9.046  31.217 -16.825 1.00 53.04  ?  39  TRP   A CH2   1 
ATOM   280  N N     . ARG   A 1 40  ? -3.389  26.309 -13.408 1.00 50.44  ?  40  ARG   A N     1 
ATOM   281  C CA    . ARG   A 1 40  ? -1.992  26.038 -13.014 1.00 50.69  ?  40  ARG   A CA    1 
ATOM   282  C C     . ARG   A 1 40  ? -1.299  25.244 -14.114 1.00 53.53  ?  40  ARG   A C     1 
ATOM   283  O O     . ARG   A 1 40  ? -0.068  25.197 -14.119 1.00 54.15  ?  40  ARG   A O     1 
ATOM   284  C CB    . ARG   A 1 40  ? -2.002  25.193 -11.745 1.00 46.57  ?  40  ARG   A CB    1 
ATOM   285  C CG    . ARG   A 1 40  ? -0.708  25.220 -10.954 1.00 56.79  ?  40  ARG   A CG    1 
ATOM   286  C CD    . ARG   A 1 40  ? -0.576  23.892 -10.267 1.00 51.94  ?  40  ARG   A CD    1 
ATOM   287  N NE    . ARG   A 1 40  ? -1.236  22.835 -11.033 1.00 58.18  ?  40  ARG   A NE    1 
ATOM   288  C CZ    . ARG   A 1 40  ? -0.570  21.961 -11.761 1.00 63.22  ?  40  ARG   A CZ    1 
ATOM   289  N NH1   . ARG   A 1 40  ? 0.727   21.813 -11.589 1.00 60.24  ?  40  ARG   A NH1   1 
ATOM   290  N NH2   . ARG   A 1 40  ? -1.202  21.243 -12.661 1.00 67.22  ?  40  ARG   A NH2   1 
ATOM   291  N N     . GLN   A 1 41  ? -2.065  24.700 -15.045 1.00 55.31  ?  41  GLN   A N     1 
ATOM   292  C CA    . GLN   A 1 41  ? -1.512  23.769 -16.058 1.00 61.16  ?  41  GLN   A CA    1 
ATOM   293  C C     . GLN   A 1 41  ? -0.763  24.469 -17.198 1.00 59.13  ?  41  GLN   A C     1 
ATOM   294  O O     . GLN   A 1 41  ? 0.382   24.086 -17.442 1.00 62.72  ?  41  GLN   A O     1 
ATOM   295  C CB    . GLN   A 1 41  ? -2.654  22.861 -16.507 1.00 61.81  ?  41  GLN   A CB    1 
ATOM   296  C CG    . GLN   A 1 41  ? -3.374  22.177 -15.355 1.00 62.86  ?  41  GLN   A CG    1 
ATOM   297  C CD    . GLN   A 1 41  ? -4.233  21.025 -15.812 1.00 64.39  ?  41  GLN   A CD    1 
ATOM   298  O OE1   . GLN   A 1 41  ? -5.304  21.214 -16.395 1.00 64.19  ?  41  GLN   A OE1   1 
ATOM   299  N NE2   . GLN   A 1 41  ? -3.759  19.816 -15.557 1.00 63.51  ?  41  GLN   A NE2   1 
ATOM   300  N N     . PRO   A 1 42  ? -1.303  25.462 -17.917 1.00 50.54  ?  42  PRO   A N     1 
ATOM   301  C CA    . PRO   A 1 42  ? -0.542  26.027 -19.006 1.00 50.67  ?  42  PRO   A CA    1 
ATOM   302  C C     . PRO   A 1 42  ? 0.866   26.396 -18.594 1.00 56.63  ?  42  PRO   A C     1 
ATOM   303  O O     . PRO   A 1 42  ? 1.776   26.286 -19.413 1.00 67.79  ?  42  PRO   A O     1 
ATOM   304  C CB    . PRO   A 1 42  ? -1.388  27.203 -19.403 1.00 51.46  ?  42  PRO   A CB    1 
ATOM   305  C CG    . PRO   A 1 42  ? -2.786  26.773 -19.075 1.00 56.74  ?  42  PRO   A CG    1 
ATOM   306  C CD    . PRO   A 1 42  ? -2.607  26.053 -17.760 1.00 57.47  ?  42  PRO   A CD    1 
ATOM   307  N N     . GLY   A 1 43  ? 1.071   26.768 -17.346 1.00 55.80  ?  43  GLY   A N     1 
ATOM   308  C CA    . GLY   A 1 43  ? 2.398   27.232 -16.919 1.00 54.41  ?  43  GLY   A CA    1 
ATOM   309  C C     . GLY   A 1 43  ? 3.320   26.117 -16.502 1.00 59.44  ?  43  GLY   A C     1 
ATOM   310  O O     . GLY   A 1 43  ? 4.452   26.412 -16.100 1.00 57.59  ?  43  GLY   A O     1 
ATOM   311  N N     . ALA   A 1 44  ? 2.855   24.882 -16.587 1.00 63.26  ?  44  ALA   A N     1 
ATOM   312  C CA    . ALA   A 1 44  ? 3.668   23.732 -16.151 1.00 65.29  ?  44  ALA   A CA    1 
ATOM   313  C C     . ALA   A 1 44  ? 3.754   22.734 -17.292 1.00 62.20  ?  44  ALA   A C     1 
ATOM   314  O O     . ALA   A 1 44  ? 4.323   21.660 -17.109 1.00 67.48  ?  44  ALA   A O     1 
ATOM   315  C CB    . ALA   A 1 44  ? 3.052   23.119 -14.933 1.00 68.96  ?  44  ALA   A CB    1 
ATOM   316  N N     . GLY   A 1 45  ? 3.187   23.094 -18.432 1.00 69.24  ?  45  GLY   A N     1 
ATOM   317  C CA    . GLY   A 1 45  ? 3.279   22.242 -19.627 1.00 72.68  ?  45  GLY   A CA    1 
ATOM   318  C C     . GLY   A 1 45  ? 2.472   20.985 -19.480 1.00 74.90  ?  45  GLY   A C     1 
ATOM   319  O O     . GLY   A 1 45  ? 2.958   19.935 -19.930 1.00 82.48  ?  45  GLY   A O     1 
ATOM   320  N N     . GLU   A 1 46  ? 1.273   21.088 -18.922 1.00 69.40  ?  46  GLU   A N     1 
ATOM   321  C CA    . GLU   A 1 46  ? 0.498   19.862 -18.641 1.00 68.72  ?  46  GLU   A CA    1 
ATOM   322  C C     . GLU   A 1 46  ? -0.689  19.797 -19.590 1.00 68.16  ?  46  GLU   A C     1 
ATOM   323  O O     . GLU   A 1 46  ? -1.267  20.844 -19.890 1.00 70.59  ?  46  GLU   A O     1 
ATOM   324  C CB    . GLU   A 1 46  ? 0.036   19.800 -17.186 1.00 61.43  ?  46  GLU   A CB    1 
ATOM   325  C CG    . GLU   A 1 46  ? 1.148   19.971 -16.160 1.00 64.88  ?  46  GLU   A CG    1 
ATOM   326  C CD    . GLU   A 1 46  ? 0.565   19.754 -14.780 1.00 70.99  ?  46  GLU   A CD    1 
ATOM   327  O OE1   . GLU   A 1 46  ? 1.311   19.473 -13.824 1.00 68.77  ?  46  GLU   A OE1   1 
ATOM   328  O OE2   . GLU   A 1 46  ? -0.669  19.859 -14.677 1.00 66.94  ?  46  GLU   A OE2   1 
ATOM   329  N N     . ARG   A 1 47  ? -0.987  18.604 -20.083 1.00 67.40  ?  47  ARG   A N     1 
ATOM   330  C CA    . ARG   A 1 47  ? -2.197  18.451 -20.907 1.00 70.11  ?  47  ARG   A CA    1 
ATOM   331  C C     . ARG   A 1 47  ? -3.347  18.981 -20.068 1.00 70.25  ?  47  ARG   A C     1 
ATOM   332  O O     . ARG   A 1 47  ? -3.596  18.453 -18.984 1.00 69.90  ?  47  ARG   A O     1 
ATOM   333  C CB    . ARG   A 1 47  ? -2.503  17.003 -21.303 1.00 72.17  ?  47  ARG   A CB    1 
ATOM   334  C CG    . ARG   A 1 47  ? -1.710  16.463 -22.481 1.00 80.16  ?  47  ARG   A CG    1 
ATOM   335  C CD    . ARG   A 1 47  ? -2.176  15.064 -22.836 1.00 81.98  ?  47  ARG   A CD    1 
ATOM   336  N NE    . ARG   A 1 47  ? -3.555  15.047 -23.331 1.00 80.00  ?  47  ARG   A NE    1 
ATOM   337  C CZ    . ARG   A 1 47  ? -4.230  13.940 -23.597 1.00 86.18  ?  47  ARG   A CZ    1 
ATOM   338  N NH1   . ARG   A 1 47  ? -4.997  13.873 -24.669 1.00 86.19  ?  47  ARG   A NH1   1 
ATOM   339  N NH2   . ARG   A 1 47  ? -4.133  12.901 -22.791 1.00 90.11  ?  47  ARG   A NH2   1 
ATOM   340  N N     . GLY   A 1 48  ? -3.982  20.019 -20.554 1.00 60.36  ?  48  GLY   A N     1 
ATOM   341  C CA    . GLY   A 1 48  ? -5.153  20.566 -19.879 1.00 60.44  ?  48  GLY   A CA    1 
ATOM   342  C C     . GLY   A 1 48  ? -5.866  21.359 -20.922 1.00 62.48  ?  48  GLY   A C     1 
ATOM   343  O O     . GLY   A 1 48  ? -5.274  21.547 -21.995 1.00 67.18  ?  48  GLY   A O     1 
ATOM   344  N N     . PRO   A 1 49  ? -7.093  21.849 -20.730 1.00 60.33  ?  49  PRO   A N     1 
ATOM   345  C CA    . PRO   A 1 49  ? -7.703  22.661 -21.751 1.00 55.88  ?  49  PRO   A CA    1 
ATOM   346  C C     . PRO   A 1 49  ? -7.144  24.026 -21.933 1.00 52.65  ?  49  PRO   A C     1 
ATOM   347  O O     . PRO   A 1 49  ? -7.652  24.660 -22.767 1.00 63.09  ?  49  PRO   A O     1 
ATOM   348  C CB    . PRO   A 1 49  ? -9.120  22.785 -21.276 1.00 56.13  ?  49  PRO   A CB    1 
ATOM   349  C CG    . PRO   A 1 49  ? -9.040  22.713 -19.864 1.00 56.63  ?  49  PRO   A CG    1 
ATOM   350  C CD    . PRO   A 1 49  ? -8.164  21.574 -19.690 1.00 57.64  ?  49  PRO   A CD    1 
ATOM   351  N N     . GLY   A 1 50  ? -6.154  24.474 -21.221 1.00 50.24  ?  50  GLY   A N     1 
ATOM   352  C CA    . GLY   A 1 50  ? -5.635  25.796 -21.412 1.00 54.89  ?  50  GLY   A CA    1 
ATOM   353  C C     . GLY   A 1 50  ? -4.501  25.791 -22.356 1.00 60.42  ?  50  GLY   A C     1 
ATOM   354  O O     . GLY   A 1 50  ? -4.088  24.737 -22.755 1.00 60.23  ?  50  GLY   A O     1 
ATOM   355  N N     . TYR   A 1 51  ? -4.000  26.973 -22.669 1.00 59.82  ?  51  TYR   A N     1 
ATOM   356  C CA    . TYR   A 1 51  ? -2.920  27.144 -23.626 1.00 54.17  ?  51  TYR   A CA    1 
ATOM   357  C C     . TYR   A 1 51  ? -2.097  28.357 -23.211 1.00 57.13  ?  51  TYR   A C     1 
ATOM   358  O O     . TYR   A 1 51  ? -2.559  29.214 -22.455 1.00 59.41  ?  51  TYR   A O     1 
ATOM   359  C CB    . TYR   A 1 51  ? -3.470  27.317 -25.032 1.00 48.52  ?  51  TYR   A CB    1 
ATOM   360  C CG    . TYR   A 1 51  ? -4.792  28.029 -25.045 1.00 52.06  ?  51  TYR   A CG    1 
ATOM   361  C CD1   . TYR   A 1 51  ? -5.973  27.343 -24.792 1.00 51.95  ?  51  TYR   A CD1   1 
ATOM   362  C CD2   . TYR   A 1 51  ? -4.866  29.392 -25.308 1.00 54.96  ?  51  TYR   A CD2   1 
ATOM   363  C CE1   . TYR   A 1 51  ? -7.196  27.996 -24.790 1.00 51.40  ?  51  TYR   A CE1   1 
ATOM   364  C CE2   . TYR   A 1 51  ? -6.085  30.052 -25.318 1.00 50.21  ?  51  TYR   A CE2   1 
ATOM   365  C CZ    . TYR   A 1 51  ? -7.245  29.346 -25.052 1.00 49.61  ?  51  TYR   A CZ    1 
ATOM   366  O OH    . TYR   A 1 51  ? -8.462  29.975 -25.042 1.00 53.67  ?  51  TYR   A OH    1 
ATOM   367  N N     . ARG   A 1 52  ? -0.872  28.428 -23.731 1.00 55.25  ?  52  ARG   A N     1 
ATOM   368  C CA    . ARG   A 1 52  ? 0.092   29.422 -23.277 1.00 57.48  ?  52  ARG   A CA    1 
ATOM   369  C C     . ARG   A 1 52  ? -0.441  30.858 -23.337 1.00 54.88  ?  52  ARG   A C     1 
ATOM   370  O O     . ARG   A 1 52  ? 0.065   31.709 -22.604 1.00 58.05  ?  52  ARG   A O     1 
ATOM   371  C CB    . ARG   A 1 52  ? 1.388   29.290 -24.106 1.00 60.42  ?  52  ARG   A CB    1 
ATOM   372  C CG    . ARG   A 1 52  ? 2.696   29.827 -23.461 1.00 60.33  ?  52  ARG   A CG    1 
ATOM   373  C CD    . ARG   A 1 52  ? 3.267   28.930 -22.348 1.00 66.73  ?  52  ARG   A CD    1 
ATOM   374  N NE    . ARG   A 1 52  ? 4.139   29.684 -21.430 1.00 79.32  ?  52  ARG   A NE    1 
ATOM   375  C CZ    . ARG   A 1 52  ? 3.852   29.955 -20.149 1.00 73.86  ?  52  ARG   A CZ    1 
ATOM   376  N NH1   . ARG   A 1 52  ? 2.721   29.519 -19.610 1.00 67.51  ?  52  ARG   A NH1   1 
ATOM   377  N NH2   . ARG   A 1 52  ? 4.699   30.653 -19.396 1.00 64.83  ?  52  ARG   A NH2   1 
ATOM   378  N N     . THR   A 1 53  ? -1.444  31.160 -24.171 1.00 51.57  ?  53  THR   A N     1 
ATOM   379  C CA    . THR   A 1 53  ? -1.903  32.540 -24.334 1.00 51.82  ?  53  THR   A CA    1 
ATOM   380  C C     . THR   A 1 53  ? -3.306  32.771 -23.777 1.00 52.58  ?  53  THR   A C     1 
ATOM   381  O O     . THR   A 1 53  ? -4.041  33.629 -24.272 1.00 52.73  ?  53  THR   A O     1 
ATOM   382  C CB    . THR   A 1 53  ? -1.850  32.975 -25.805 1.00 54.27  ?  53  THR   A CB    1 
ATOM   383  O OG1   . THR   A 1 53  ? -3.008  32.502 -26.511 1.00 49.59  ?  53  THR   A OG1   1 
ATOM   384  C CG2   . THR   A 1 53  ? -0.571  32.489 -26.493 1.00 47.40  ?  53  THR   A CG2   1 
ATOM   385  N N     . LEU   A 1 54  ? -3.681  32.040 -22.731 1.00 57.10  ?  54  LEU   A N     1 
ATOM   386  C CA    . LEU   A 1 54  ? -5.019  32.132 -22.154 1.00 53.18  ?  54  LEU   A CA    1 
ATOM   387  C C     . LEU   A 1 54  ? -5.081  33.212 -21.077 1.00 54.05  ?  54  LEU   A C     1 
ATOM   388  O O     . LEU   A 1 54  ? -4.267  33.214 -20.148 1.00 53.76  ?  54  LEU   A O     1 
ATOM   389  C CB    . LEU   A 1 54  ? -5.434  30.790 -21.553 1.00 53.84  ?  54  LEU   A CB    1 
ATOM   390  C CG    . LEU   A 1 54  ? -6.695  30.828 -20.691 1.00 54.16  ?  54  LEU   A CG    1 
ATOM   391  C CD1   . LEU   A 1 54  ? -7.951  30.941 -21.536 1.00 46.17  ?  54  LEU   A CD1   1 
ATOM   392  C CD2   . LEU   A 1 54  ? -6.744  29.601 -19.816 1.00 54.43  ?  54  LEU   A CD2   1 
ATOM   393  N N     . HIS   A 1 55  ? -6.057  34.116 -21.203 1.00 51.40  ?  55  HIS   A N     1 
ATOM   394  C CA    . HIS   A 1 55  ? -6.375  35.122 -20.200 1.00 49.50  ?  55  HIS   A CA    1 
ATOM   395  C C     . HIS   A 1 55  ? -7.814  34.919 -19.743 1.00 56.41  ?  55  HIS   A C     1 
ATOM   396  O O     . HIS   A 1 55  ? -8.586  34.196 -20.381 1.00 58.34  ?  55  HIS   A O     1 
ATOM   397  C CB    . HIS   A 1 55  ? -6.198  36.558 -20.738 1.00 44.46  ?  55  HIS   A CB    1 
ATOM   398  C CG    . HIS   A 1 55  ? -4.765  36.978 -20.888 1.00 53.12  ?  55  HIS   A CG    1 
ATOM   399  N ND1   . HIS   A 1 55  ? -4.209  38.013 -20.164 1.00 49.21  ?  55  HIS   A ND1   1 
ATOM   400  C CD2   . HIS   A 1 55  ? -3.778  36.516 -21.697 1.00 52.99  ?  55  HIS   A CD2   1 
ATOM   401  C CE1   . HIS   A 1 55  ? -2.941  38.160 -20.505 1.00 48.98  ?  55  HIS   A CE1   1 
ATOM   402  N NE2   . HIS   A 1 55  ? -2.654  37.264 -21.433 1.00 53.20  ?  55  HIS   A NE2   1 
ATOM   403  N N     . LEU   A 1 56  ? -8.175  35.540 -18.617 1.00 52.80  ?  56  LEU   A N     1 
ATOM   404  C CA    . LEU   A 1 56  ? -9.588  35.659 -18.300 1.00 50.95  ?  56  LEU   A CA    1 
ATOM   405  C C     . LEU   A 1 56  ? -10.307 36.376 -19.435 1.00 55.96  ?  56  LEU   A C     1 
ATOM   406  O O     . LEU   A 1 56  ? -9.726  37.200 -20.146 1.00 50.57  ?  56  LEU   A O     1 
ATOM   407  C CB    . LEU   A 1 56  ? -9.805  36.428 -16.995 1.00 51.17  ?  56  LEU   A CB    1 
ATOM   408  C CG    . LEU   A 1 56  ? -9.198  35.908 -15.685 1.00 55.88  ?  56  LEU   A CG    1 
ATOM   409  C CD1   . LEU   A 1 56  ? -9.772  36.654 -14.488 1.00 50.10  ?  56  LEU   A CD1   1 
ATOM   410  C CD2   . LEU   A 1 56  ? -9.437  34.417 -15.525 1.00 54.31  ?  56  LEU   A CD2   1 
ATOM   411  N N     . ASN   A 1 57  ? -11.577 36.025 -19.623 1.00 56.69  ?  57  ASN   A N     1 
ATOM   412  C CA    . ASN   A 1 57  ? -12.527 36.839 -20.370 1.00 54.51  ?  57  ASN   A CA    1 
ATOM   413  C C     . ASN   A 1 57  ? -13.625 37.368 -19.464 1.00 59.73  ?  57  ASN   A C     1 
ATOM   414  O O     . ASN   A 1 57  ? -14.631 37.881 -19.959 1.00 70.55  ?  57  ASN   A O     1 
ATOM   415  C CB    . ASN   A 1 57  ? -13.150 36.048 -21.520 1.00 56.66  ?  57  ASN   A CB    1 
ATOM   416  C CG    . ASN   A 1 57  ? -13.911 34.810 -21.046 1.00 62.84  ?  57  ASN   A CG    1 
ATOM   417  O OD1   . ASN   A 1 57  ? -13.646 34.265 -19.979 1.00 70.28  ?  57  ASN   A OD1   1 
ATOM   418  N ND2   . ASN   A 1 57  ? -14.857 34.367 -21.842 1.00 63.80  ?  57  ASN   A ND2   1 
ATOM   419  N N     . THR   A 1 58  ? -13.483 37.205 -18.153 1.00 57.26  ?  58  THR   A N     1 
ATOM   420  C CA    . THR   A 1 58  ? -14.347 37.853 -17.178 1.00 58.32  ?  58  THR   A CA    1 
ATOM   421  C C     . THR   A 1 58  ? -13.550 38.909 -16.423 1.00 54.05  ?  58  THR   A C     1 
ATOM   422  O O     . THR   A 1 58  ? -12.331 38.787 -16.255 1.00 55.14  ?  58  THR   A O     1 
ATOM   423  C CB    . THR   A 1 58  ? -14.948 36.835 -16.196 1.00 56.08  ?  58  THR   A CB    1 
ATOM   424  O OG1   . THR   A 1 58  ? -13.964 35.868 -15.820 1.00 46.17  ?  58  THR   A OG1   1 
ATOM   425  C CG2   . THR   A 1 58  ? -16.099 36.112 -16.847 1.00 59.49  ?  58  THR   A CG2   1 
ATOM   426  N N     . ALA   A 1 59  ? -14.238 39.959 -15.986 1.00 56.61  ?  59  ALA   A N     1 
ATOM   427  C CA    . ALA   A 1 59  ? -13.582 40.989 -15.182 1.00 54.83  ?  59  ALA   A CA    1 
ATOM   428  C C     . ALA   A 1 59  ? -12.994 40.378 -13.911 1.00 52.27  ?  59  ALA   A C     1 
ATOM   429  O O     . ALA   A 1 59  ? -13.625 39.543 -13.255 1.00 50.95  ?  59  ALA   A O     1 
ATOM   430  C CB    . ALA   A 1 59  ? -14.575 42.102 -14.836 1.00 50.71  ?  59  ALA   A CB    1 
ATOM   431  N N     . LYS   A 1 60  ? -11.761 40.776 -13.573 1.00 53.50  ?  60  LYS   A N     1 
ATOM   432  C CA    . LYS   A 1 60  ? -11.099 40.176 -12.413 1.00 50.61  ?  60  LYS   A CA    1 
ATOM   433  C C     . LYS   A 1 60  ? -11.886 40.410 -11.135 1.00 50.20  ?  60  LYS   A C     1 
ATOM   434  O O     . LYS   A 1 60  ? -11.890 39.549 -10.247 1.00 52.93  ?  60  LYS   A O     1 
ATOM   435  C CB    . LYS   A 1 60  ? -9.683  40.726 -12.243 1.00 49.57  ?  60  LYS   A CB    1 
ATOM   436  C CG    . LYS   A 1 60  ? -9.638  42.213 -11.991 1.00 48.60  ?  60  LYS   A CG    1 
ATOM   437  C CD    . LYS   A 1 60  ? -8.433  42.585 -11.167 1.00 46.95  ?  60  LYS   A CD    1 
ATOM   438  C CE    . LYS   A 1 60  ? -8.141  44.081 -11.302 1.00 45.29  ?  60  LYS   A CE    1 
ATOM   439  N NZ    . LYS   A 1 60  ? -6.790  44.436 -10.775 1.00 47.76  ?  60  LYS   A NZ    1 
ATOM   440  N N     . GLN   A 1 61  ? -12.557 41.559 -11.024 1.00 49.43  ?  61  GLN   A N     1 
ATOM   441  C CA    . GLN   A 1 61  ? -13.292 41.871 -9.805  1.00 50.21  ?  61  GLN   A CA    1 
ATOM   442  C C     . GLN   A 1 61  ? -14.479 40.933 -9.618  1.00 51.76  ?  61  GLN   A C     1 
ATOM   443  O O     . GLN   A 1 61  ? -14.786 40.534 -8.490  1.00 54.03  ?  61  GLN   A O     1 
ATOM   444  C CB    . GLN   A 1 61  ? -13.740 43.329 -9.831  1.00 49.43  ?  61  GLN   A CB    1 
ATOM   445  C CG    . GLN   A 1 61  ? -14.758 43.637 -10.925 1.00 56.12  ?  61  GLN   A CG    1 
ATOM   446  C CD    . GLN   A 1 61  ? -14.121 44.237 -12.154 1.00 57.74  ?  61  GLN   A CD    1 
ATOM   447  O OE1   . GLN   A 1 61  ? -12.895 44.160 -12.339 1.00 56.29  ?  61  GLN   A OE1   1 
ATOM   448  N NE2   . GLN   A 1 61  ? -14.943 44.866 -12.996 1.00 59.60  ?  61  GLN   A NE2   1 
ATOM   449  N N     . LEU   A 1 62  ? -15.147 40.554 -10.710 1.00 53.31  ?  62  LEU   A N     1 
ATOM   450  C CA    . LEU   A 1 62  ? -16.185 39.528 -10.669 1.00 50.30  ?  62  LEU   A CA    1 
ATOM   451  C C     . LEU   A 1 62  ? -15.624 38.113 -10.671 1.00 48.25  ?  62  LEU   A C     1 
ATOM   452  O O     . LEU   A 1 62  ? -16.397 37.157 -10.545 1.00 51.86  ?  62  LEU   A O     1 
ATOM   453  C CB    . LEU   A 1 62  ? -17.141 39.699 -11.850 1.00 51.10  ?  62  LEU   A CB    1 
ATOM   454  C CG    . LEU   A 1 62  ? -17.627 41.144 -11.965 1.00 56.86  ?  62  LEU   A CG    1 
ATOM   455  C CD1   . LEU   A 1 62  ? -18.203 41.445 -13.346 1.00 54.53  ?  62  LEU   A CD1   1 
ATOM   456  C CD2   . LEU   A 1 62  ? -18.633 41.426 -10.843 1.00 46.19  ?  62  LEU   A CD2   1 
ATOM   457  N N     . THR   A 1 63  ? -14.317 37.942 -10.804 1.00 42.79  ?  63  THR   A N     1 
ATOM   458  C CA    . THR   A 1 63  ? -13.748 36.611 -10.941 1.00 46.53  ?  63  THR   A CA    1 
ATOM   459  C C     . THR   A 1 63  ? -13.030 36.143 -9.696  1.00 42.09  ?  63  THR   A C     1 
ATOM   460  O O     . THR   A 1 63  ? -13.095 34.963 -9.367  1.00 43.45  ?  63  THR   A O     1 
ATOM   461  C CB    . THR   A 1 63  ? -12.772 36.568 -12.128 1.00 51.34  ?  63  THR   A CB    1 
ATOM   462  O OG1   . THR   A 1 63  ? -13.408 37.126 -13.288 1.00 54.54  ?  63  THR   A OG1   1 
ATOM   463  C CG2   . THR   A 1 63  ? -12.303 35.133 -12.409 1.00 33.66  ?  63  THR   A CG2   1 
ATOM   464  N N     . GLY   A 1 64  ? -12.323 37.039 -9.011  1.00 48.51  ?  64  GLY   A N     1 
ATOM   465  C CA    . GLY   A 1 64  ? -11.719 36.685 -7.744  1.00 46.05  ?  64  GLY   A CA    1 
ATOM   466  C C     . GLY   A 1 64  ? -12.762 36.442 -6.669  1.00 46.28  ?  64  GLY   A C     1 
ATOM   467  O O     . GLY   A 1 64  ? -13.939 36.796 -6.808  1.00 40.37  ?  64  GLY   A O     1 
ATOM   468  N N     . TYR   A 1 65  ? -12.324 35.791 -5.587  1.00 43.43  ?  65  TYR   A N     1 
ATOM   469  C CA    . TYR   A 1 65  ? -13.207 35.581 -4.457  1.00 40.39  ?  65  TYR   A CA    1 
ATOM   470  C C     . TYR   A 1 65  ? -13.550 36.925 -3.839  1.00 44.29  ?  65  TYR   A C     1 
ATOM   471  O O     . TYR   A 1 65  ? -12.739 37.858 -3.846  1.00 43.76  ?  65  TYR   A O     1 
ATOM   472  C CB    . TYR   A 1 65  ? -12.561 34.665 -3.427  1.00 40.91  ?  65  TYR   A CB    1 
ATOM   473  C CG    . TYR   A 1 65  ? -12.223 33.270 -3.940  1.00 41.74  ?  65  TYR   A CG    1 
ATOM   474  C CD1   . TYR   A 1 65  ? -13.222 32.381 -4.361  1.00 37.13  ?  65  TYR   A CD1   1 
ATOM   475  C CD2   . TYR   A 1 65  ? -10.897 32.840 -4.004  1.00 39.65  ?  65  TYR   A CD2   1 
ATOM   476  C CE1   . TYR   A 1 65  ? -12.899 31.101 -4.822  1.00 35.16  ?  65  TYR   A CE1   1 
ATOM   477  C CE2   . TYR   A 1 65  ? -10.568 31.590 -4.465  1.00 36.25  ?  65  TYR   A CE2   1 
ATOM   478  C CZ    . TYR   A 1 65  ? -11.562 30.713 -4.863  1.00 39.83  ?  65  TYR   A CZ    1 
ATOM   479  O OH    . TYR   A 1 65  ? -11.189 29.456 -5.307  1.00 39.72  ?  65  TYR   A OH    1 
ATOM   480  N N     . ALA   A 1 66  ? -14.779 37.031 -3.328  1.00 40.47  ?  66  ALA   A N     1 
ATOM   481  C CA    . ALA   A 1 66  ? -15.271 38.323 -2.851  1.00 45.44  ?  66  ALA   A CA    1 
ATOM   482  C C     . ALA   A 1 66  ? -14.494 38.827 -1.623  1.00 48.65  ?  66  ALA   A C     1 
ATOM   483  O O     . ALA   A 1 66  ? -14.259 40.032 -1.490  1.00 43.14  ?  66  ALA   A O     1 
ATOM   484  C CB    . ALA   A 1 66  ? -16.764 38.225 -2.548  1.00 43.03  ?  66  ALA   A CB    1 
ATOM   485  N N     . ASP   A 1 67  ? -14.086 37.929 -0.717  1.00 45.36  ?  67  ASP   A N     1 
ATOM   486  C CA    . ASP   A 1 67  ? -13.306 38.299 0.460   1.00 43.14  ?  67  ASP   A CA    1 
ATOM   487  C C     . ASP   A 1 67  ? -11.792 38.287 0.217   1.00 45.91  ?  67  ASP   A C     1 
ATOM   488  O O     . ASP   A 1 67  ? -11.017 38.216 1.178   1.00 50.42  ?  67  ASP   A O     1 
ATOM   489  C CB    . ASP   A 1 67  ? -13.640 37.363 1.626   1.00 39.10  ?  67  ASP   A CB    1 
ATOM   490  C CG    . ASP   A 1 67  ? -13.293 35.917 1.333   1.00 44.74  ?  67  ASP   A CG    1 
ATOM   491  O OD1   . ASP   A 1 67  ? -13.191 35.563 0.139   1.00 52.00  ?  67  ASP   A OD1   1 
ATOM   492  O OD2   . ASP   A 1 67  ? -13.147 35.122 2.283   1.00 43.32  ?  67  ASP   A OD2   1 
ATOM   493  N N     . PHE   A 1 68  ? -11.353 38.330 -1.023  1.00 43.48  ?  68  PHE   A N     1 
ATOM   494  C CA    . PHE   A 1 68  ? -9.923  38.162 -1.255  1.00 46.56  ?  68  PHE   A CA    1 
ATOM   495  C C     . PHE   A 1 68  ? -9.589  38.713 -2.632  1.00 49.43  ?  68  PHE   A C     1 
ATOM   496  O O     . PHE   A 1 68  ? -9.442  37.961 -3.605  1.00 44.31  ?  68  PHE   A O     1 
ATOM   497  C CB    . PHE   A 1 68  ? -9.541  36.691 -1.130  1.00 44.04  ?  68  PHE   A CB    1 
ATOM   498  C CG    . PHE   A 1 68  ? -8.081  36.436 -1.162  1.00 44.81  ?  68  PHE   A CG    1 
ATOM   499  C CD1   . PHE   A 1 68  ? -7.296  36.671 -0.052  1.00 49.98  ?  68  PHE   A CD1   1 
ATOM   500  C CD2   . PHE   A 1 68  ? -7.484  35.924 -2.299  1.00 44.42  ?  68  PHE   A CD2   1 
ATOM   501  C CE1   . PHE   A 1 68  ? -5.929  36.400 -0.082  1.00 46.24  ?  68  PHE   A CE1   1 
ATOM   502  C CE2   . PHE   A 1 68  ? -6.127  35.656 -2.336  1.00 40.66  ?  68  PHE   A CE2   1 
ATOM   503  C CZ    . PHE   A 1 68  ? -5.351  35.887 -1.230  1.00 43.29  ?  68  PHE   A CZ    1 
ATOM   504  N N     . PRO   A 1 69  ? -9.486  40.027 -2.756  1.00 54.70  ?  69  PRO   A N     1 
ATOM   505  C CA    . PRO   A 1 69  ? -9.310  40.620 -4.080  1.00 45.03  ?  69  PRO   A CA    1 
ATOM   506  C C     . PRO   A 1 69  ? -7.967  40.239 -4.684  1.00 43.81  ?  69  PRO   A C     1 
ATOM   507  O O     . PRO   A 1 69  ? -6.997  39.945 -3.984  1.00 47.85  ?  69  PRO   A O     1 
ATOM   508  C CB    . PRO   A 1 69  ? -9.409  42.125 -3.809  1.00 48.82  ?  69  PRO   A CB    1 
ATOM   509  C CG    . PRO   A 1 69  ? -9.066  42.274 -2.353  1.00 53.53  ?  69  PRO   A CG    1 
ATOM   510  C CD    . PRO   A 1 69  ? -9.503  41.028 -1.670  1.00 46.28  ?  69  PRO   A CD    1 
ATOM   511  N N     . MET   A 1 70  ? -7.938  40.214 -6.013  1.00 50.08  ?  70  MET   A N     1 
ATOM   512  C CA    . MET   A 1 70  ? -6.701  40.007 -6.738  1.00 46.76  ?  70  MET   A CA    1 
ATOM   513  C C     . MET   A 1 70  ? -5.813  41.237 -6.582  1.00 46.68  ?  70  MET   A C     1 
ATOM   514  O O     . MET   A 1 70  ? -6.319  42.341 -6.381  1.00 46.79  ?  70  MET   A O     1 
ATOM   515  C CB    . MET   A 1 70  ? -6.989  39.763 -8.216  1.00 48.16  ?  70  MET   A CB    1 
ATOM   516  C CG    . MET   A 1 70  ? -7.764  38.501 -8.503  1.00 45.39  ?  70  MET   A CG    1 
ATOM   517  S SD    . MET   A 1 70  ? -7.728  38.080 -10.256 1.00 55.73  ?  70  MET   A SD    1 
ATOM   518  C CE    . MET   A 1 70  ? -8.876  36.701 -10.291 1.00 52.02  ?  70  MET   A CE    1 
ATOM   519  N N     . PRO   A 1 71  ? -4.493  41.073 -6.676  1.00 43.32  ?  71  PRO   A N     1 
ATOM   520  C CA    . PRO   A 1 71  ? -3.592  42.227 -6.609  1.00 37.29  ?  71  PRO   A CA    1 
ATOM   521  C C     . PRO   A 1 71  ? -4.067  43.353 -7.505  1.00 43.83  ?  71  PRO   A C     1 
ATOM   522  O O     . PRO   A 1 71  ? -4.535  43.125 -8.621  1.00 54.66  ?  71  PRO   A O     1 
ATOM   523  C CB    . PRO   A 1 71  ? -2.260  41.657 -7.098  1.00 39.80  ?  71  PRO   A CB    1 
ATOM   524  C CG    . PRO   A 1 71  ? -2.347  40.232 -6.759  1.00 45.03  ?  71  PRO   A CG    1 
ATOM   525  C CD    . PRO   A 1 71  ? -3.767  39.838 -6.992  1.00 43.46  ?  71  PRO   A CD    1 
ATOM   526  N N     . ASP   A 1 72  ? -3.966  44.580 -7.008  1.00 47.89  ?  72  ASP   A N     1 
ATOM   527  C CA    . ASP   A 1 72  ? -4.481  45.690 -7.794  1.00 47.26  ?  72  ASP   A CA    1 
ATOM   528  C C     . ASP   A 1 72  ? -3.596  45.984 -9.003  1.00 45.44  ?  72  ASP   A C     1 
ATOM   529  O O     . ASP   A 1 72  ? -4.044  46.629 -9.955  1.00 45.20  ?  72  ASP   A O     1 
ATOM   530  C CB    . ASP   A 1 72  ? -4.633  46.927 -6.907  1.00 52.28  ?  72  ASP   A CB    1 
ATOM   531  C CG    . ASP   A 1 72  ? -5.338  48.072 -7.619  1.00 67.74  ?  72  ASP   A CG    1 
ATOM   532  O OD1   . ASP   A 1 72  ? -6.054  47.827 -8.625  1.00 74.14  ?  72  ASP   A OD1   1 
ATOM   533  O OD2   . ASP   A 1 72  ? -5.168  49.225 -7.179  1.00 75.95  ?  72  ASP   A OD2   1 
ATOM   534  N N     . ALA   A 1 73  ? -2.350  45.516 -8.990  1.00 47.79  ?  73  ALA   A N     1 
ATOM   535  C CA    . ALA   A 1 73  ? -1.521  45.577 -10.183 1.00 44.22  ?  73  ALA   A CA    1 
ATOM   536  C C     . ALA   A 1 73  ? -2.118  44.771 -11.334 1.00 51.58  ?  73  ALA   A C     1 
ATOM   537  O O     . ALA   A 1 73  ? -1.832  45.080 -12.501 1.00 48.59  ?  73  ALA   A O     1 
ATOM   538  C CB    . ALA   A 1 73  ? -0.112  45.077 -9.857  1.00 41.65  ?  73  ALA   A CB    1 
ATOM   539  N N     . TYR   A 1 74  ? -2.950  43.763 -11.039 1.00 43.57  ?  74  TYR   A N     1 
ATOM   540  C CA    . TYR   A 1 74  ? -3.462  42.913 -12.095 1.00 45.52  ?  74  TYR   A CA    1 
ATOM   541  C C     . TYR   A 1 74  ? -4.289  43.734 -13.069 1.00 44.87  ?  74  TYR   A C     1 
ATOM   542  O O     . TYR   A 1 74  ? -4.927  44.713 -12.674 1.00 44.98  ?  74  TYR   A O     1 
ATOM   543  C CB    . TYR   A 1 74  ? -4.334  41.792 -11.549 1.00 51.76  ?  74  TYR   A CB    1 
ATOM   544  C CG    . TYR   A 1 74  ? -3.596  40.551 -11.100 1.00 47.00  ?  74  TYR   A CG    1 
ATOM   545  C CD1   . TYR   A 1 74  ? -2.259  40.596 -10.722 1.00 37.94  ?  74  TYR   A CD1   1 
ATOM   546  C CD2   . TYR   A 1 74  ? -4.264  39.335 -11.023 1.00 44.56  ?  74  TYR   A CD2   1 
ATOM   547  C CE1   . TYR   A 1 74  ? -1.616  39.469 -10.279 1.00 37.96  ?  74  TYR   A CE1   1 
ATOM   548  C CE2   . TYR   A 1 74  ? -3.622  38.196 -10.586 1.00 45.69  ?  74  TYR   A CE2   1 
ATOM   549  C CZ    . TYR   A 1 74  ? -2.306  38.263 -10.207 1.00 42.07  ?  74  TYR   A CZ    1 
ATOM   550  O OH    . TYR   A 1 74  ? -1.692  37.108 -9.758  1.00 41.54  ?  74  TYR   A OH    1 
ATOM   551  N N     . PRO   A 1 75  ? -4.299  43.350 -14.340 1.00 46.73  ?  75  PRO   A N     1 
ATOM   552  C CA    . PRO   A 1 75  ? -5.178  43.988 -15.321 1.00 42.35  ?  75  PRO   A CA    1 
ATOM   553  C C     . PRO   A 1 75  ? -6.596  43.455 -15.163 1.00 41.92  ?  75  PRO   A C     1 
ATOM   554  O O     . PRO   A 1 75  ? -6.861  42.569 -14.365 1.00 43.58  ?  75  PRO   A O     1 
ATOM   555  C CB    . PRO   A 1 75  ? -4.569  43.559 -16.659 1.00 46.75  ?  75  PRO   A CB    1 
ATOM   556  C CG    . PRO   A 1 75  ? -4.014  42.159 -16.365 1.00 44.04  ?  75  PRO   A CG    1 
ATOM   557  C CD    . PRO   A 1 75  ? -3.527  42.228 -14.922 1.00 45.52  ?  75  PRO   A CD    1 
ATOM   558  N N     . LEU   A 1 76  ? -7.504  43.997 -15.971 1.00 43.22  ?  76  LEU   A N     1 
ATOM   559  C CA    . LEU   A 1 76  ? -8.869  43.492 -15.990 1.00 44.52  ?  76  LEU   A CA    1 
ATOM   560  C C     . LEU   A 1 76  ? -8.911  42.003 -16.329 1.00 49.21  ?  76  LEU   A C     1 
ATOM   561  O O     . LEU   A 1 76  ? -9.569  41.221 -15.632 1.00 50.11  ?  76  LEU   A O     1 
ATOM   562  C CB    . LEU   A 1 76  ? -9.704  44.296 -16.979 1.00 49.45  ?  76  LEU   A CB    1 
ATOM   563  C CG    . LEU   A 1 76  ? -11.214 44.100 -16.791 1.00 56.48  ?  76  LEU   A CG    1 
ATOM   564  C CD1   . LEU   A 1 76  ? -11.730 44.848 -15.548 1.00 47.15  ?  76  LEU   A CD1   1 
ATOM   565  C CD2   . LEU   A 1 76  ? -11.981 44.512 -18.047 1.00 49.87  ?  76  LEU   A CD2   1 
ATOM   566  N N     . TYR   A 1 77  ? -8.198  41.587 -17.388 1.00 46.33  ?  77  TYR   A N     1 
ATOM   567  C CA    . TYR   A 1 77  ? -8.126  40.181 -17.790 1.00 45.36  ?  77  TYR   A CA    1 
ATOM   568  C C     . TYR   A 1 77  ? -6.735  39.593 -17.589 1.00 46.80  ?  77  TYR   A C     1 
ATOM   569  O O     . TYR   A 1 77  ? -5.961  39.499 -18.549 1.00 45.60  ?  77  TYR   A O     1 
ATOM   570  C CB    . TYR   A 1 77  ? -8.543  40.022 -19.246 1.00 44.11  ?  77  TYR   A CB    1 
ATOM   571  C CG    . TYR   A 1 77  ? -9.853  40.631 -19.601 1.00 45.56  ?  77  TYR   A CG    1 
ATOM   572  C CD1   . TYR   A 1 77  ? -11.022 40.173 -19.023 1.00 45.69  ?  77  TYR   A CD1   1 
ATOM   573  C CD2   . TYR   A 1 77  ? -9.933  41.641 -20.578 1.00 49.24  ?  77  TYR   A CD2   1 
ATOM   574  C CE1   . TYR   A 1 77  ? -12.248 40.720 -19.369 1.00 51.47  ?  77  TYR   A CE1   1 
ATOM   575  C CE2   . TYR   A 1 77  ? -11.156 42.208 -20.923 1.00 46.38  ?  77  TYR   A CE2   1 
ATOM   576  C CZ    . TYR   A 1 77  ? -12.307 41.738 -20.316 1.00 51.85  ?  77  TYR   A CZ    1 
ATOM   577  O OH    . TYR   A 1 77  ? -13.525 42.267 -20.659 1.00 57.47  ?  77  TYR   A OH    1 
ATOM   578  N N     . PRO   A 1 78  ? -6.390  39.116 -16.391 1.00 49.83  ?  78  PRO   A N     1 
ATOM   579  C CA    . PRO   A 1 78  ? -5.030  38.593 -16.157 1.00 47.57  ?  78  PRO   A CA    1 
ATOM   580  C C     . PRO   A 1 78  ? -4.713  37.353 -16.987 1.00 45.82  ?  78  PRO   A C     1 
ATOM   581  O O     . PRO   A 1 78  ? -5.602  36.615 -17.428 1.00 44.41  ?  78  PRO   A O     1 
ATOM   582  C CB    . PRO   A 1 78  ? -5.026  38.248 -14.656 1.00 45.44  ?  78  PRO   A CB    1 
ATOM   583  C CG    . PRO   A 1 78  ? -6.292  38.841 -14.103 1.00 44.87  ?  78  PRO   A CG    1 
ATOM   584  C CD    . PRO   A 1 78  ? -7.257  38.964 -15.214 1.00 41.42  ?  78  PRO   A CD    1 
ATOM   585  N N     . ARG   A 1 79  ? -3.411  37.111 -17.168 1.00 49.04  ?  79  ARG   A N     1 
ATOM   586  C CA    . ARG   A 1 79  ? -2.952  35.891 -17.825 1.00 49.80  ?  79  ARG   A CA    1 
ATOM   587  C C     . ARG   A 1 79  ? -3.115  34.702 -16.877 1.00 48.98  ?  79  ARG   A C     1 
ATOM   588  O O     . ARG   A 1 79  ? -3.313  34.856 -15.669 1.00 48.52  ?  79  ARG   A O     1 
ATOM   589  C CB    . ARG   A 1 79  ? -1.492  36.021 -18.291 1.00 45.48  ?  79  ARG   A CB    1 
ATOM   590  C CG    . ARG   A 1 79  ? -1.162  35.190 -19.569 1.00 54.17  ?  79  ARG   A CG    1 
ATOM   591  C CD    . ARG   A 1 79  ? 0.301   35.316 -20.103 1.00 58.44  ?  79  ARG   A CD    1 
ATOM   592  N NE    . ARG   A 1 79  ? 1.254   34.623 -19.224 1.00 65.65  ?  79  ARG   A NE    1 
ATOM   593  C CZ    . ARG   A 1 79  ? 2.042   33.610 -19.586 1.00 58.79  ?  79  ARG   A CZ    1 
ATOM   594  N NH1   . ARG   A 1 79  ? 2.014   33.161 -20.827 1.00 53.11  ?  79  ARG   A NH1   1 
ATOM   595  N NH2   . ARG   A 1 79  ? 2.852   33.034 -18.695 1.00 56.36  ?  79  ARG   A NH2   1 
ATOM   596  N N     . HIS   A 1 80  ? -3.015  33.495 -17.443 1.00 48.00  ?  80  HIS   A N     1 
ATOM   597  C CA    . HIS   A 1 80  ? -3.265  32.282 -16.674 1.00 48.78  ?  80  HIS   A CA    1 
ATOM   598  C C     . HIS   A 1 80  ? -2.260  32.102 -15.542 1.00 47.76  ?  80  HIS   A C     1 
ATOM   599  O O     . HIS   A 1 80  ? -2.597  31.516 -14.509 1.00 46.68  ?  80  HIS   A O     1 
ATOM   600  C CB    . HIS   A 1 80  ? -3.240  31.069 -17.596 1.00 51.19  ?  80  HIS   A CB    1 
ATOM   601  C CG    . HIS   A 1 80  ? -1.897  30.816 -18.195 1.00 52.17  ?  80  HIS   A CG    1 
ATOM   602  N ND1   . HIS   A 1 80  ? -1.523  31.314 -19.426 1.00 49.80  ?  80  HIS   A ND1   1 
ATOM   603  C CD2   . HIS   A 1 80  ? -0.826  30.143 -17.716 1.00 50.46  ?  80  HIS   A CD2   1 
ATOM   604  C CE1   . HIS   A 1 80  ? -0.280  30.949 -19.679 1.00 52.17  ?  80  HIS   A CE1   1 
ATOM   605  N NE2   . HIS   A 1 80  ? 0.165   30.238 -18.657 1.00 47.94  ?  80  HIS   A NE2   1 
ATOM   606  N N     . SER   A 1 81  ? -1.025  32.575 -15.713 1.00 46.40  ?  81  SER   A N     1 
ATOM   607  C CA    . SER   A 1 81  ? -0.067  32.514 -14.609 1.00 47.43  ?  81  SER   A CA    1 
ATOM   608  C C     . SER   A 1 81  ? -0.499  33.411 -13.450 1.00 45.43  ?  81  SER   A C     1 
ATOM   609  O O     . SER   A 1 81  ? -0.467  32.988 -12.286 1.00 44.79  ?  81  SER   A O     1 
ATOM   610  C CB    . SER   A 1 81  ? 1.332   32.876 -15.113 1.00 44.35  ?  81  SER   A CB    1 
ATOM   611  O OG    . SER   A 1 81  ? 1.270   33.939 -16.060 1.00 52.05  ?  81  SER   A OG    1 
ATOM   612  N N     . GLN   A 1 82  ? -0.925  34.642 -13.749 1.00 43.48  ?  82  GLN   A N     1 
ATOM   613  C CA    . GLN   A 1 82  ? -1.447  35.524 -12.710 1.00 46.27  ?  82  GLN   A CA    1 
ATOM   614  C C     . GLN   A 1 82  ? -2.606  34.867 -11.973 1.00 45.78  ?  82  GLN   A C     1 
ATOM   615  O O     . GLN   A 1 82  ? -2.645  34.865 -10.736 1.00 44.82  ?  82  GLN   A O     1 
ATOM   616  C CB    . GLN   A 1 82  ? -1.869  36.873 -13.319 1.00 45.02  ?  82  GLN   A CB    1 
ATOM   617  C CG    . GLN   A 1 82  ? -0.676  37.718 -13.799 1.00 44.47  ?  82  GLN   A CG    1 
ATOM   618  C CD    . GLN   A 1 82  ? -1.067  38.971 -14.569 1.00 48.87  ?  82  GLN   A CD    1 
ATOM   619  O OE1   . GLN   A 1 82  ? -1.800  38.915 -15.553 1.00 53.84  ?  82  GLN   A OE1   1 
ATOM   620  N NE2   . GLN   A 1 82  ? -0.546  40.113 -14.133 1.00 55.84  ?  82  GLN   A NE2   1 
ATOM   621  N N     . VAL   A 1 83  ? -3.541  34.271 -12.714 1.00 45.38  ?  83  VAL   A N     1 
ATOM   622  C CA    . VAL   A 1 83  ? -4.679  33.611 -12.084 1.00 41.23  ?  83  VAL   A CA    1 
ATOM   623  C C     . VAL   A 1 83  ? -4.217  32.434 -11.236 1.00 42.62  ?  83  VAL   A C     1 
ATOM   624  O O     . VAL   A 1 83  ? -4.724  32.207 -10.131 1.00 44.01  ?  83  VAL   A O     1 
ATOM   625  C CB    . VAL   A 1 83  ? -5.677  33.171 -13.161 1.00 47.92  ?  83  VAL   A CB    1 
ATOM   626  C CG1   . VAL   A 1 83  ? -6.905  32.577 -12.513 1.00 43.00  ?  83  VAL   A CG1   1 
ATOM   627  C CG2   . VAL   A 1 83  ? -6.030  34.357 -14.060 1.00 45.38  ?  83  VAL   A CG2   1 
ATOM   628  N N     . ALA   A 1 84  ? -3.247  31.665 -11.735 1.00 47.37  ?  84  ALA   A N     1 
ATOM   629  C CA    . ALA   A 1 84  ? -2.753  30.520 -10.978 1.00 43.69  ?  84  ALA   A CA    1 
ATOM   630  C C     . ALA   A 1 84  ? -2.001  30.968 -9.728  1.00 45.57  ?  84  ALA   A C     1 
ATOM   631  O O     . ALA   A 1 84  ? -2.131  30.347 -8.665  1.00 41.53  ?  84  ALA   A O     1 
ATOM   632  C CB    . ALA   A 1 84  ? -1.875  29.649 -11.861 1.00 42.87  ?  84  ALA   A CB    1 
ATOM   633  N N     . ALA   A 1 85  ? -1.230  32.060 -9.828  1.00 44.92  ?  85  ALA   A N     1 
ATOM   634  C CA    . ALA   A 1 85  ? -0.564  32.611 -8.651  1.00 39.65  ?  85  ALA   A CA    1 
ATOM   635  C C     . ALA   A 1 85  ? -1.581  33.074 -7.610  1.00 42.28  ?  85  ALA   A C     1 
ATOM   636  O O     . ALA   A 1 85  ? -1.455  32.754 -6.419  1.00 39.21  ?  85  ALA   A O     1 
ATOM   637  C CB    . ALA   A 1 85  ? 0.354   33.763 -9.056  1.00 37.46  ?  85  ALA   A CB    1 
ATOM   638  N N     . TYR   A 1 86  ? -2.602  33.817 -8.050  1.00 40.86  ?  86  TYR   A N     1 
ATOM   639  C CA    . TYR   A 1 86  ? -3.657  34.279 -7.151  1.00 41.61  ?  86  TYR   A CA    1 
ATOM   640  C C     . TYR   A 1 86  ? -4.284  33.123 -6.369  1.00 44.48  ?  86  TYR   A C     1 
ATOM   641  O O     . TYR   A 1 86  ? -4.486  33.214 -5.147  1.00 39.27  ?  86  TYR   A O     1 
ATOM   642  C CB    . TYR   A 1 86  ? -4.732  35.013 -7.955  1.00 45.94  ?  86  TYR   A CB    1 
ATOM   643  C CG    . TYR   A 1 86  ? -6.027  35.165 -7.203  1.00 50.94  ?  86  TYR   A CG    1 
ATOM   644  C CD1   . TYR   A 1 86  ? -6.138  36.097 -6.175  1.00 44.76  ?  86  TYR   A CD1   1 
ATOM   645  C CD2   . TYR   A 1 86  ? -7.138  34.369 -7.501  1.00 44.74  ?  86  TYR   A CD2   1 
ATOM   646  C CE1   . TYR   A 1 86  ? -7.310  36.251 -5.466  1.00 45.99  ?  86  TYR   A CE1   1 
ATOM   647  C CE2   . TYR   A 1 86  ? -8.332  34.516 -6.787  1.00 48.09  ?  86  TYR   A CE2   1 
ATOM   648  C CZ    . TYR   A 1 86  ? -8.414  35.463 -5.758  1.00 51.32  ?  86  TYR   A CZ    1 
ATOM   649  O OH    . TYR   A 1 86  ? -9.593  35.635 -5.017  1.00 46.73  ?  86  TYR   A OH    1 
ATOM   650  N N     . LEU   A 1 87  ? -4.617  32.029 -7.062  1.00 40.96  ?  87  LEU   A N     1 
ATOM   651  C CA    . LEU   A 1 87  ? -5.260  30.906 -6.384  1.00 40.93  ?  87  LEU   A CA    1 
ATOM   652  C C     . LEU   A 1 87  ? -4.316  30.203 -5.410  1.00 39.25  ?  87  LEU   A C     1 
ATOM   653  O O     . LEU   A 1 87  ? -4.770  29.660 -4.399  1.00 37.13  ?  87  LEU   A O     1 
ATOM   654  C CB    . LEU   A 1 87  ? -5.805  29.913 -7.409  1.00 39.94  ?  87  LEU   A CB    1 
ATOM   655  C CG    . LEU   A 1 87  ? -6.940  30.446 -8.279  1.00 40.66  ?  87  LEU   A CG    1 
ATOM   656  C CD1   . LEU   A 1 87  ? -7.238  29.470 -9.400  1.00 38.16  ?  87  LEU   A CD1   1 
ATOM   657  C CD2   . LEU   A 1 87  ? -8.181  30.719 -7.445  1.00 31.88  ?  87  LEU   A CD2   1 
ATOM   658  N N     . ARG   A 1 88  ? -3.010  30.178 -5.697  1.00 41.47  ?  88  ARG   A N     1 
ATOM   659  C CA    . ARG   A 1 88  ? -2.078  29.641 -4.710  1.00 43.06  ?  88  ARG   A CA    1 
ATOM   660  C C     . ARG   A 1 88  ? -2.065  30.517 -3.458  1.00 44.18  ?  88  ARG   A C     1 
ATOM   661  O O     . ARG   A 1 88  ? -2.037  30.006 -2.329  1.00 36.99  ?  88  ARG   A O     1 
ATOM   662  C CB    . ARG   A 1 88  ? -0.676  29.516 -5.320  1.00 39.77  ?  88  ARG   A CB    1 
ATOM   663  C CG    . ARG   A 1 88  ? 0.442   29.156 -4.325  1.00 39.58  ?  88  ARG   A CG    1 
ATOM   664  C CD    . ARG   A 1 88  ? 0.271   27.771 -3.690  1.00 40.50  ?  88  ARG   A CD    1 
ATOM   665  N NE    . ARG   A 1 88  ? 1.154   27.594 -2.537  1.00 43.68  ?  88  ARG   A NE    1 
ATOM   666  C CZ    . ARG   A 1 88  ? 1.567   26.418 -2.069  1.00 46.86  ?  88  ARG   A CZ    1 
ATOM   667  N NH1   . ARG   A 1 88  ? 1.184   25.289 -2.648  1.00 46.61  ?  88  ARG   A NH1   1 
ATOM   668  N NH2   . ARG   A 1 88  ? 2.374   26.367 -1.020  1.00 50.65  ?  88  ARG   A NH2   1 
ATOM   669  N N     . SER   A 1 89  ? -2.130  31.840 -3.648  1.00 40.98  ?  89  SER   A N     1 
ATOM   670  C CA    . SER   A 1 89  ? -2.095  32.754 -2.524  1.00 41.26  ?  89  SER   A CA    1 
ATOM   671  C C     . SER   A 1 89  ? -3.358  32.629 -1.672  1.00 46.65  ?  89  SER   A C     1 
ATOM   672  O O     . SER   A 1 89  ? -3.282  32.661 -0.435  1.00 46.11  ?  89  SER   A O     1 
ATOM   673  C CB    . SER   A 1 89  ? -1.886  34.183 -3.028  1.00 45.13  ?  89  SER   A CB    1 
ATOM   674  O OG    . SER   A 1 89  ? -1.267  34.993 -2.033  1.00 50.73  ?  89  SER   A OG    1 
ATOM   675  N N     . PHE   A 1 90  ? -4.518  32.434 -2.309  1.00 45.93  ?  90  PHE   A N     1 
ATOM   676  C CA    . PHE   A 1 90  ? -5.755  32.236 -1.559  1.00 43.34  ?  90  PHE   A CA    1 
ATOM   677  C C     . PHE   A 1 90  ? -5.647  31.022 -0.635  1.00 43.14  ?  90  PHE   A C     1 
ATOM   678  O O     . PHE   A 1 90  ? -5.948  31.103 0.565   1.00 44.24  ?  90  PHE   A O     1 
ATOM   679  C CB    . PHE   A 1 90  ? -6.919  32.084 -2.540  1.00 40.22  ?  90  PHE   A CB    1 
ATOM   680  C CG    . PHE   A 1 90  ? -8.229  31.777 -1.888  1.00 41.25  ?  90  PHE   A CG    1 
ATOM   681  C CD1   . PHE   A 1 90  ? -8.932  32.768 -1.210  1.00 42.62  ?  90  PHE   A CD1   1 
ATOM   682  C CD2   . PHE   A 1 90  ? -8.764  30.494 -1.952  1.00 40.74  ?  90  PHE   A CD2   1 
ATOM   683  C CE1   . PHE   A 1 90  ? -10.153 32.487 -0.594  1.00 44.02  ?  90  PHE   A CE1   1 
ATOM   684  C CE2   . PHE   A 1 90  ? -9.984  30.198 -1.355  1.00 42.12  ?  90  PHE   A CE2   1 
ATOM   685  C CZ    . PHE   A 1 90  ? -10.682 31.202 -0.665  1.00 44.62  ?  90  PHE   A CZ    1 
ATOM   686  N N     . ALA   A 1 91  ? -5.196  29.888 -1.174  1.00 40.14  ?  91  ALA   A N     1 
ATOM   687  C CA    . ALA   A 1 91  ? -5.098  28.686 -0.356  1.00 43.12  ?  91  ALA   A CA    1 
ATOM   688  C C     . ALA   A 1 91  ? -4.152  28.908 0.816   1.00 43.21  ?  91  ALA   A C     1 
ATOM   689  O O     . ALA   A 1 91  ? -4.405  28.423 1.925   1.00 44.81  ?  91  ALA   A O     1 
ATOM   690  C CB    . ALA   A 1 91  ? -4.649  27.498 -1.210  1.00 37.93  ?  91  ALA   A CB    1 
ATOM   691  N N     . GLU   A 1 92  ? -3.067  29.656 0.588   1.00 40.49  ?  92  GLU   A N     1 
ATOM   692  C CA    . GLU   A 1 92  ? -2.171  30.049 1.674   1.00 46.16  ?  92  GLU   A CA    1 
ATOM   693  C C     . GLU   A 1 92  ? -2.907  30.913 2.700   1.00 47.18  ?  92  GLU   A C     1 
ATOM   694  O O     . GLU   A 1 92  ? -3.016  30.559 3.879   1.00 41.61  ?  92  GLU   A O     1 
ATOM   695  C CB    . GLU   A 1 92  ? -0.951  30.781 1.091   1.00 44.08  ?  92  GLU   A CB    1 
ATOM   696  C CG    . GLU   A 1 92  ? 0.078   29.819 0.443   1.00 47.50  ?  92  GLU   A CG    1 
ATOM   697  C CD    . GLU   A 1 92  ? 1.069   30.486 -0.530  1.00 48.99  ?  92  GLU   A CD    1 
ATOM   698  O OE1   . GLU   A 1 92  ? 0.978   31.710 -0.784  1.00 42.95  ?  92  GLU   A OE1   1 
ATOM   699  O OE2   . GLU   A 1 92  ? 1.937   29.760 -1.071  1.00 54.78  ?  92  GLU   A OE2   1 
ATOM   700  N N     . TRP   A 1 93  ? -3.478  32.024 2.240   1.00 47.70  ?  93  TRP   A N     1 
ATOM   701  C CA    . TRP   A 1 93  ? -4.130  32.971 3.130   1.00 46.01  ?  93  TRP   A CA    1 
ATOM   702  C C     . TRP   A 1 93  ? -5.266  32.338 3.913   1.00 46.93  ?  93  TRP   A C     1 
ATOM   703  O O     . TRP   A 1 93  ? -5.552  32.767 5.029   1.00 50.88  ?  93  TRP   A O     1 
ATOM   704  C CB    . TRP   A 1 93  ? -4.642  34.146 2.308   1.00 43.01  ?  93  TRP   A CB    1 
ATOM   705  C CG    . TRP   A 1 93  ? -5.537  35.108 3.050   1.00 48.72  ?  93  TRP   A CG    1 
ATOM   706  C CD1   . TRP   A 1 93  ? -5.147  36.189 3.789   1.00 47.81  ?  93  TRP   A CD1   1 
ATOM   707  C CD2   . TRP   A 1 93  ? -6.966  35.109 3.067   1.00 47.04  ?  93  TRP   A CD2   1 
ATOM   708  N NE1   . TRP   A 1 93  ? -6.239  36.856 4.259   1.00 45.77  ?  93  TRP   A NE1   1 
ATOM   709  C CE2   . TRP   A 1 93  ? -7.371  36.212 3.839   1.00 51.66  ?  93  TRP   A CE2   1 
ATOM   710  C CE3   . TRP   A 1 93  ? -7.944  34.289 2.502   1.00 44.69  ?  93  TRP   A CE3   1 
ATOM   711  C CZ2   . TRP   A 1 93  ? -8.711  36.505 4.073   1.00 50.33  ?  93  TRP   A CZ2   1 
ATOM   712  C CZ3   . TRP   A 1 93  ? -9.268  34.589 2.731   1.00 43.34  ?  93  TRP   A CZ3   1 
ATOM   713  C CH2   . TRP   A 1 93  ? -9.639  35.683 3.511   1.00 41.51  ?  93  TRP   A CH2   1 
ATOM   714  N N     . ALA   A 1 94  ? -5.926  31.334 3.349   1.00 46.73  ?  94  ALA   A N     1 
ATOM   715  C CA    . ALA   A 1 94  ? -7.085  30.721 3.976   1.00 45.41  ?  94  ALA   A CA    1 
ATOM   716  C C     . ALA   A 1 94  ? -6.728  29.508 4.833   1.00 46.77  ?  94  ALA   A C     1 
ATOM   717  O O     . ALA   A 1 94  ? -7.634  28.853 5.370   1.00 39.70  ?  94  ALA   A O     1 
ATOM   718  C CB    . ALA   A 1 94  ? -8.104  30.328 2.896   1.00 47.04  ?  94  ALA   A CB    1 
ATOM   719  N N     . GLY   A 1 95  ? -5.441  29.196 4.969   1.00 45.54  ?  95  GLY   A N     1 
ATOM   720  C CA    . GLY   A 1 95  ? -5.021  28.068 5.780   1.00 44.34  ?  95  GLY   A CA    1 
ATOM   721  C C     . GLY   A 1 95  ? -5.544  26.735 5.292   1.00 50.61  ?  95  GLY   A C     1 
ATOM   722  O O     . GLY   A 1 95  ? -5.919  25.883 6.105   1.00 52.82  ?  95  GLY   A O     1 
ATOM   723  N N     . LEU   A 1 96  ? -5.563  26.530 3.977   1.00 52.07  ?  96  LEU   A N     1 
ATOM   724  C CA    . LEU   A 1 96  ? -6.142  25.336 3.376   1.00 47.26  ?  96  LEU   A CA    1 
ATOM   725  C C     . LEU   A 1 96  ? -5.123  24.251 3.064   1.00 48.84  ?  96  LEU   A C     1 
ATOM   726  O O     . LEU   A 1 96  ? -5.480  23.071 3.096   1.00 47.90  ?  96  LEU   A O     1 
ATOM   727  C CB    . LEU   A 1 96  ? -6.870  25.703 2.083   1.00 44.85  ?  96  LEU   A CB    1 
ATOM   728  C CG    . LEU   A 1 96  ? -7.933  26.780 2.264   1.00 48.39  ?  96  LEU   A CG    1 
ATOM   729  C CD1   . LEU   A 1 96  ? -8.506  27.154 0.914   1.00 41.71  ?  96  LEU   A CD1   1 
ATOM   730  C CD2   . LEU   A 1 96  ? -9.021  26.295 3.199   1.00 45.51  ?  96  LEU   A CD2   1 
ATOM   731  N N     . LEU   A 1 97  ? -3.865  24.618 2.780   1.00 48.57  ?  97  LEU   A N     1 
ATOM   732  C CA    . LEU   A 1 97  ? -2.884  23.661 2.265   1.00 54.77  ?  97  LEU   A CA    1 
ATOM   733  C C     . LEU   A 1 97  ? -2.511  22.591 3.288   1.00 54.33  ?  97  LEU   A C     1 
ATOM   734  O O     . LEU   A 1 97  ? -2.047  21.503 2.907   1.00 46.60  ?  97  LEU   A O     1 
ATOM   735  C CB    . LEU   A 1 97  ? -1.637  24.411 1.792   1.00 52.10  ?  97  LEU   A CB    1 
ATOM   736  C CG    . LEU   A 1 97  ? -1.918  25.449 0.711   1.00 47.78  ?  97  LEU   A CG    1 
ATOM   737  C CD1   . LEU   A 1 97  ? -0.683  26.265 0.444   1.00 44.85  ?  97  LEU   A CD1   1 
ATOM   738  C CD2   . LEU   A 1 97  ? -2.387  24.745 -0.560  1.00 45.84  ?  97  LEU   A CD2   1 
ATOM   739  N N     . ASP   A 1 98  ? -2.715  22.881 4.573   1.00 54.45  ?  98  ASP   A N     1 
ATOM   740  C CA    . ASP   A 1 98  ? -2.624  21.864 5.610   1.00 56.99  ?  98  ASP   A CA    1 
ATOM   741  C C     . ASP   A 1 98  ? -3.664  20.761 5.413   1.00 54.35  ?  98  ASP   A C     1 
ATOM   742  O O     . ASP   A 1 98  ? -3.483  19.643 5.913   1.00 49.27  ?  98  ASP   A O     1 
ATOM   743  C CB    . ASP   A 1 98  ? -2.790  22.542 6.973   1.00 60.64  ?  98  ASP   A CB    1 
ATOM   744  C CG    . ASP   A 1 98  ? -2.334  21.671 8.120   1.00 73.21  ?  98  ASP   A CG    1 
ATOM   745  O OD1   . ASP   A 1 98  ? -1.532  20.752 7.850   1.00 77.59  ?  98  ASP   A OD1   1 
ATOM   746  O OD2   . ASP   A 1 98  ? -2.767  21.902 9.286   1.00 74.11  ?  98  ASP   A OD2   1 
ATOM   747  N N     . HIS   A 1 99  ? -4.742  21.053 4.687   1.00 52.56  ?  99  HIS   A N     1 
ATOM   748  C CA    . HIS   A 1 99  ? -5.816  20.110 4.426   1.00 49.18  ?  99  HIS   A CA    1 
ATOM   749  C C     . HIS   A 1 99  ? -5.783  19.542 3.007   1.00 50.89  ?  99  HIS   A C     1 
ATOM   750  O O     . HIS   A 1 99  ? -6.651  18.729 2.662   1.00 47.74  ?  99  HIS   A O     1 
ATOM   751  C CB    . HIS   A 1 99  ? -7.171  20.789 4.678   1.00 50.22  ?  99  HIS   A CB    1 
ATOM   752  C CG    . HIS   A 1 99  ? -7.326  21.361 6.053   1.00 52.25  ?  99  HIS   A CG    1 
ATOM   753  N ND1   . HIS   A 1 99  ? -8.364  21.007 6.894   1.00 61.23  ?  99  HIS   A ND1   1 
ATOM   754  C CD2   . HIS   A 1 99  ? -6.584  22.266 6.734   1.00 47.36  ?  99  HIS   A CD2   1 
ATOM   755  C CE1   . HIS   A 1 99  ? -8.249  21.665 8.035   1.00 59.13  ?  99  HIS   A CE1   1 
ATOM   756  N NE2   . HIS   A 1 99  ? -7.180  22.440 7.961   1.00 59.47  ?  99  HIS   A NE2   1 
ATOM   757  N N     . VAL   A 1 100 ? -4.817  19.947 2.176   1.00 48.77  ?  100 VAL   A N     1 
ATOM   758  C CA    . VAL   A 1 100 ? -4.760  19.546 0.772   1.00 49.28  ?  100 VAL   A CA    1 
ATOM   759  C C     . VAL   A 1 100 ? -3.713  18.452 0.608   1.00 56.07  ?  100 VAL   A C     1 
ATOM   760  O O     . VAL   A 1 100 ? -2.532  18.653 0.927   1.00 55.33  ?  100 VAL   A O     1 
ATOM   761  C CB    . VAL   A 1 100 ? -4.432  20.735 -0.140  1.00 49.92  ?  100 VAL   A CB    1 
ATOM   762  C CG1   . VAL   A 1 100 ? -4.249  20.255 -1.560  1.00 46.73  ?  100 VAL   A CG1   1 
ATOM   763  C CG2   . VAL   A 1 100 ? -5.520  21.791 -0.055  1.00 48.92  ?  100 VAL   A CG2   1 
ATOM   764  N N     . GLU   A 1 101 ? -4.147  17.291 0.110   1.00 52.67  ?  101 GLU   A N     1 
ATOM   765  C CA    . GLU   A 1 101 ? -3.250  16.208 -0.292  1.00 51.35  ?  101 GLU   A CA    1 
ATOM   766  C C     . GLU   A 1 101 ? -3.006  16.354 -1.791  1.00 50.76  ?  101 GLU   A C     1 
ATOM   767  O O     . GLU   A 1 101 ? -3.838  15.958 -2.615  1.00 51.94  ?  101 GLU   A O     1 
ATOM   768  C CB    . GLU   A 1 101 ? -3.834  14.840 0.051   1.00 49.04  ?  101 GLU   A CB    1 
ATOM   769  C CG    . GLU   A 1 101 ? -3.663  14.415 1.506   1.00 47.43  ?  101 GLU   A CG    1 
ATOM   770  C CD    . GLU   A 1 101 ? -4.193  12.995 1.762   1.00 53.42  ?  101 GLU   A CD    1 
ATOM   771  O OE1   . GLU   A 1 101 ? -4.767  12.757 2.844   1.00 44.34  ?  101 GLU   A OE1   1 
ATOM   772  O OE2   . GLU   A 1 101 ? -4.032  12.111 0.880   1.00 53.30  ?  101 GLU   A OE2   1 
ATOM   773  N N     . LEU   A 1 102 ? -1.867  16.936 -2.139  1.00 52.11  ?  102 LEU   A N     1 
ATOM   774  C CA    . LEU   A 1 102 ? -1.451  17.029 -3.523  1.00 53.36  ?  102 LEU   A CA    1 
ATOM   775  C C     . LEU   A 1 102 ? -0.960  15.677 -4.014  1.00 51.21  ?  102 LEU   A C     1 
ATOM   776  O O     . LEU   A 1 102 ? -0.687  14.774 -3.225  1.00 49.43  ?  102 LEU   A O     1 
ATOM   777  C CB    . LEU   A 1 102 ? -0.360  18.076 -3.678  1.00 54.14  ?  102 LEU   A CB    1 
ATOM   778  C CG    . LEU   A 1 102 ? -0.885  19.465 -3.351  1.00 57.07  ?  102 LEU   A CG    1 
ATOM   779  C CD1   . LEU   A 1 102 ? 0.293   20.420 -3.237  1.00 53.25  ?  102 LEU   A CD1   1 
ATOM   780  C CD2   . LEU   A 1 102 ? -1.916  19.920 -4.402  1.00 49.97  ?  102 LEU   A CD2   1 
ATOM   781  N N     . ARG   A 1 103 ? -0.846  15.543 -5.344  1.00 54.04  ?  103 ARG   A N     1 
ATOM   782  C CA    . ARG   A 1 103 ? -0.440  14.278 -5.975  1.00 55.82  ?  103 ARG   A CA    1 
ATOM   783  C C     . ARG   A 1 103 ? -1.287  13.099 -5.482  1.00 62.39  ?  103 ARG   A C     1 
ATOM   784  O O     . ARG   A 1 103 ? -0.824  11.954 -5.432  1.00 57.98  ?  103 ARG   A O     1 
ATOM   785  C CB    . ARG   A 1 103 ? 1.047   13.989 -5.747  1.00 56.93  ?  103 ARG   A CB    1 
ATOM   786  C CG    . ARG   A 1 103 ? 1.975   14.950 -6.431  1.00 55.94  ?  103 ARG   A CG    1 
ATOM   787  C CD    . ARG   A 1 103 ? 3.412   14.469 -6.315  1.00 66.09  ?  103 ARG   A CD    1 
ATOM   788  N NE    . ARG   A 1 103 ? 4.315   15.330 -7.072  1.00 72.27  ?  103 ARG   A NE    1 
ATOM   789  C CZ    . ARG   A 1 103 ? 4.437   15.303 -8.396  1.00 77.89  ?  103 ARG   A CZ    1 
ATOM   790  N NH1   . ARG   A 1 103 ? 3.724   14.445 -9.121  1.00 76.29  ?  103 ARG   A NH1   1 
ATOM   791  N NH2   . ARG   A 1 103 ? 5.274   16.133 -9.003  1.00 75.45  ?  103 ARG   A NH2   1 
ATOM   792  N N     . THR   A 1 104 ? -2.532  13.376 -5.094  1.00 61.74  ?  104 THR   A N     1 
ATOM   793  C CA    . THR   A 1 104 ? -3.469  12.357 -4.640  1.00 60.38  ?  104 THR   A CA    1 
ATOM   794  C C     . THR   A 1 104 ? -4.687  12.355 -5.559  1.00 60.04  ?  104 THR   A C     1 
ATOM   795  O O     . THR   A 1 104 ? -5.409  13.354 -5.662  1.00 57.61  ?  104 THR   A O     1 
ATOM   796  C CB    . THR   A 1 104 ? -3.857  12.597 -3.183  1.00 53.71  ?  104 THR   A CB    1 
ATOM   797  O OG1   . THR   A 1 104 ? -2.750  12.245 -2.349  1.00 53.81  ?  104 THR   A OG1   1 
ATOM   798  C CG2   . THR   A 1 104 ? -5.058  11.743 -2.794  1.00 55.66  ?  104 THR   A CG2   1 
ATOM   799  N N     . GLU   A 1 105 ? -4.916  11.236 -6.222  1.00 56.21  ?  105 GLU   A N     1 
ATOM   800  C CA    . GLU   A 1 105 ? -5.947  11.140 -7.240  1.00 60.68  ?  105 GLU   A CA    1 
ATOM   801  C C     . GLU   A 1 105 ? -7.047  10.207 -6.757  1.00 56.06  ?  105 GLU   A C     1 
ATOM   802  O O     . GLU   A 1 105 ? -6.760  9.092  -6.308  1.00 56.04  ?  105 GLU   A O     1 
ATOM   803  C CB    . GLU   A 1 105 ? -5.338  10.636 -8.543  1.00 58.24  ?  105 GLU   A CB    1 
ATOM   804  C CG    . GLU   A 1 105 ? -6.334  10.257 -9.591  1.00 58.84  ?  105 GLU   A CG    1 
ATOM   805  C CD    . GLU   A 1 105 ? -5.678  9.490  -10.705 1.00 66.48  ?  105 GLU   A CD    1 
ATOM   806  O OE1   . GLU   A 1 105 ? -6.218  9.514  -11.831 1.00 63.68  ?  105 GLU   A OE1   1 
ATOM   807  O OE2   . GLU   A 1 105 ? -4.612  8.877  -10.449 1.00 68.29  ?  105 GLU   A OE2   1 
ATOM   808  N N     . VAL   A 1 106 ? -8.305  10.651 -6.832  1.00 49.79  ?  106 VAL   A N     1 
ATOM   809  C CA    . VAL   A 1 106 ? -9.368  9.784  -6.325  1.00 43.89  ?  106 VAL   A CA    1 
ATOM   810  C C     . VAL   A 1 106 ? -9.704  8.777  -7.414  1.00 42.84  ?  106 VAL   A C     1 
ATOM   811  O O     . VAL   A 1 106 ? -9.798  9.141  -8.588  1.00 45.86  ?  106 VAL   A O     1 
ATOM   812  C CB    . VAL   A 1 106 ? -10.596 10.608 -5.897  1.00 45.54  ?  106 VAL   A CB    1 
ATOM   813  C CG1   . VAL   A 1 106 ? -11.701 9.699  -5.387  1.00 44.63  ?  106 VAL   A CG1   1 
ATOM   814  C CG2   . VAL   A 1 106 ? -10.217 11.643 -4.843  1.00 42.41  ?  106 VAL   A CG2   1 
ATOM   815  N N     . VAL   A 1 107 ? -9.831  7.499  -7.051  1.00 44.30  ?  107 VAL   A N     1 
ATOM   816  C CA    . VAL   A 1 107 ? -10.056 6.438  -8.032  1.00 46.60  ?  107 VAL   A CA    1 
ATOM   817  C C     . VAL   A 1 107 ? -11.440 5.811  -7.884  1.00 47.14  ?  107 VAL   A C     1 
ATOM   818  O O     . VAL   A 1 107 ? -12.073 5.478  -8.887  1.00 48.46  ?  107 VAL   A O     1 
ATOM   819  C CB    . VAL   A 1 107 ? -8.950  5.354  -8.005  1.00 48.08  ?  107 VAL   A CB    1 
ATOM   820  C CG1   . VAL   A 1 107 ? -7.590  5.961  -8.381  1.00 52.65  ?  107 VAL   A CG1   1 
ATOM   821  C CG2   . VAL   A 1 107 ? -8.867  4.689  -6.678  1.00 53.42  ?  107 VAL   A CG2   1 
ATOM   822  N N     . SER   A 1 108 ? -11.959 5.693  -6.666  1.00 50.56  ?  108 SER   A N     1 
ATOM   823  C CA    . SER   A 1 108 ? -13.353 5.309  -6.517  1.00 44.71  ?  108 SER   A CA    1 
ATOM   824  C C     . SER   A 1 108 ? -13.962 6.025  -5.331  1.00 44.05  ?  108 SER   A C     1 
ATOM   825  O O     . SER   A 1 108 ? -13.286 6.322  -4.343  1.00 49.07  ?  108 SER   A O     1 
ATOM   826  C CB    . SER   A 1 108 ? -13.529 3.796  -6.343  1.00 45.55  ?  108 SER   A CB    1 
ATOM   827  O OG    . SER   A 1 108 ? -12.595 3.276  -5.419  1.00 45.92  ?  108 SER   A OG    1 
ATOM   828  N N     . VAL   A 1 109 ? -15.259 6.283  -5.440  1.00 43.12  ?  109 VAL   A N     1 
ATOM   829  C CA    . VAL   A 1 109 ? -16.081 6.799  -4.357  1.00 41.69  ?  109 VAL   A CA    1 
ATOM   830  C C     . VAL   A 1 109 ? -17.342 5.945  -4.351  1.00 44.21  ?  109 VAL   A C     1 
ATOM   831  O O     . VAL   A 1 109 ? -18.032 5.863  -5.371  1.00 43.26  ?  109 VAL   A O     1 
ATOM   832  C CB    . VAL   A 1 109 ? -16.409 8.296  -4.540  1.00 41.20  ?  109 VAL   A CB    1 
ATOM   833  C CG1   . VAL   A 1 109 ? -17.375 8.793  -3.457  1.00 44.12  ?  109 VAL   A CG1   1 
ATOM   834  C CG2   . VAL   A 1 109 ? -15.138 9.136  -4.506  1.00 40.64  ?  109 VAL   A CG2   1 
ATOM   835  N N     . ARG   A 1 110 ? -17.617 5.266  -3.230  1.00 46.43  ?  110 ARG   A N     1 
ATOM   836  C CA    . ARG   A 1 110 ? -18.771 4.364  -3.149  1.00 50.40  ?  110 ARG   A CA    1 
ATOM   837  C C     . ARG   A 1 110 ? -19.514 4.573  -1.835  1.00 47.67  ?  110 ARG   A C     1 
ATOM   838  O O     . ARG   A 1 110 ? -18.895 4.662  -0.771  1.00 50.09  ?  110 ARG   A O     1 
ATOM   839  C CB    . ARG   A 1 110 ? -18.371 2.880  -3.285  1.00 44.75  ?  110 ARG   A CB    1 
ATOM   840  C CG    . ARG   A 1 110 ? -17.179 2.582  -4.180  1.00 50.93  ?  110 ARG   A CG    1 
ATOM   841  C CD    . ARG   A 1 110 ? -16.992 1.072  -4.360  1.00 47.60  ?  110 ARG   A CD    1 
ATOM   842  N NE    . ARG   A 1 110 ? -17.929 0.536  -5.341  1.00 56.57  ?  110 ARG   A NE    1 
ATOM   843  C CZ    . ARG   A 1 110 ? -17.594 0.115  -6.558  1.00 55.60  ?  110 ARG   A CZ    1 
ATOM   844  N NH1   . ARG   A 1 110 ? -16.326 0.140  -6.968  1.00 57.55  ?  110 ARG   A NH1   1 
ATOM   845  N NH2   . ARG   A 1 110 ? -18.537 -0.338 -7.367  1.00 65.21  ?  110 ARG   A NH2   1 
ATOM   846  N N     . GLN   A 1 111 ? -20.839 4.626  -1.905  1.00 45.23  ?  111 GLN   A N     1 
ATOM   847  C CA    . GLN   A 1 111 ? -21.647 4.871  -0.718  1.00 49.49  ?  111 GLN   A CA    1 
ATOM   848  C C     . GLN   A 1 111 ? -21.865 3.565  0.049   1.00 54.14  ?  111 GLN   A C     1 
ATOM   849  O O     . GLN   A 1 111 ? -22.533 2.644  -0.441  1.00 45.36  ?  111 GLN   A O     1 
ATOM   850  C CB    . GLN   A 1 111 ? -22.972 5.504  -1.103  1.00 48.16  ?  111 GLN   A CB    1 
ATOM   851  C CG    . GLN   A 1 111 ? -23.852 5.776  0.091   1.00 52.21  ?  111 GLN   A CG    1 
ATOM   852  C CD    . GLN   A 1 111 ? -25.105 6.543  -0.293  1.00 57.97  ?  111 GLN   A CD    1 
ATOM   853  O OE1   . GLN   A 1 111 ? -25.396 7.592  0.294   1.00 57.42  ?  111 GLN   A OE1   1 
ATOM   854  N NE2   . GLN   A 1 111 ? -25.853 6.028  -1.287  1.00 54.51  ?  111 GLN   A NE2   1 
ATOM   855  N N     . ASP   A 1 112 ? -21.292 3.495  1.255   1.00 52.33  ?  112 ASP   A N     1 
ATOM   856  C CA    . ASP   A 1 112 ? -21.419 2.328  2.108   1.00 49.00  ?  112 ASP   A CA    1 
ATOM   857  C C     . ASP   A 1 112 ? -22.848 2.197  2.592   1.00 52.92  ?  112 ASP   A C     1 
ATOM   858  O O     . ASP   A 1 112 ? -23.584 3.179  2.697   1.00 55.00  ?  112 ASP   A O     1 
ATOM   859  C CB    . ASP   A 1 112 ? -20.482 2.430  3.304   1.00 51.83  ?  112 ASP   A CB    1 
ATOM   860  C CG    . ASP   A 1 112 ? -19.019 2.459  2.903   1.00 51.16  ?  112 ASP   A CG    1 
ATOM   861  O OD1   . ASP   A 1 112 ? -18.606 1.624  2.071   1.00 52.59  ?  112 ASP   A OD1   1 
ATOM   862  O OD2   . ASP   A 1 112 ? -18.279 3.316  3.432   1.00 52.96  ?  112 ASP   A OD2   1 
ATOM   863  N N     . ALA   A 1 113 ? -23.238 0.963  2.890   1.00 53.01  ?  113 ALA   A N     1 
ATOM   864  C CA    . ALA   A 1 113 ? -24.631 0.686  3.208   1.00 55.28  ?  113 ALA   A CA    1 
ATOM   865  C C     . ALA   A 1 113 ? -25.106 1.383  4.477   1.00 53.97  ?  113 ALA   A C     1 
ATOM   866  O O     . ALA   A 1 113 ? -26.317 1.426  4.706   1.00 54.86  ?  113 ALA   A O     1 
ATOM   867  C CB    . ALA   A 1 113 ? -24.842 -0.826 3.320   1.00 53.27  ?  113 ALA   A CB    1 
ATOM   868  N N     . ASP   A 1 114 ? -24.161 1.942  5.238   1.00 52.90  ?  114 ASP   A N     1 
ATOM   869  C CA    . ASP   A 1 114 ? -24.456 2.563  6.554   1.00 56.70  ?  114 ASP   A CA    1 
ATOM   870  C C     . ASP   A 1 114 ? -24.447 4.090  6.510   1.00 57.01  ?  114 ASP   A C     1 
ATOM   871  O O     . ASP   A 1 114 ? -24.675 4.710  7.556   1.00 59.35  ?  114 ASP   A O     1 
ATOM   872  C CB    . ASP   A 1 114 ? -23.448 2.102  7.594   1.00 55.43  ?  114 ASP   A CB    1 
ATOM   873  C CG    . ASP   A 1 114 ? -22.001 2.497  7.374   1.00 59.38  ?  114 ASP   A CG    1 
ATOM   874  O OD1   . ASP   A 1 114 ? -21.569 2.489  6.215   1.00 67.81  ?  114 ASP   A OD1   1 
ATOM   875  O OD2   . ASP   A 1 114 ? -21.321 2.795  8.370   1.00 55.97  ?  114 ASP   A OD2   1 
ATOM   876  N N     . GLY   A 1 115 ? -24.162 4.673  5.361   1.00 53.44  ?  115 GLY   A N     1 
ATOM   877  C CA    . GLY   A 1 115 ? -24.213 6.133  5.246   1.00 50.04  ?  115 GLY   A CA    1 
ATOM   878  C C     . GLY   A 1 115 ? -22.931 6.715  4.715   1.00 51.47  ?  115 GLY   A C     1 
ATOM   879  O O     . GLY   A 1 115 ? -22.982 7.394  3.687   1.00 52.35  ?  115 GLY   A O     1 
ATOM   880  N N     . PRO   A 1 116 ? -21.788 6.519  5.385   1.00 53.55  ?  116 PRO   A N     1 
ATOM   881  C CA    . PRO   A 1 116 ? -20.528 6.999  4.857   1.00 50.32  ?  116 PRO   A CA    1 
ATOM   882  C C     . PRO   A 1 116 ? -20.042 6.535  3.488   1.00 49.08  ?  116 PRO   A C     1 
ATOM   883  O O     . PRO   A 1 116 ? -20.610 5.619  2.902   1.00 50.03  ?  116 PRO   A O     1 
ATOM   884  C CB    . PRO   A 1 116 ? -19.622 6.532  5.997   1.00 52.95  ?  116 PRO   A CB    1 
ATOM   885  C CG    . PRO   A 1 116 ? -20.470 6.672  7.211   1.00 54.62  ?  116 PRO   A CG    1 
ATOM   886  C CD    . PRO   A 1 116 ? -21.681 5.949  6.704   1.00 51.91  ?  116 PRO   A CD    1 
ATOM   887  N N     . TRP   A 1 117 ? -18.985 7.167  2.992   1.00 49.62  ?  117 TRP   A N     1 
ATOM   888  C CA    . TRP   A 1 117 ? -18.449 6.900  1.671   1.00 45.48  ?  117 TRP   A CA    1 
ATOM   889  C C     . TRP   A 1 117 ? -17.026 6.388  1.803   1.00 46.14  ?  117 TRP   A C     1 
ATOM   890  O O     . TRP   A 1 117 ? -16.213 6.991  2.510   1.00 46.97  ?  117 TRP   A O     1 
ATOM   891  C CB    . TRP   A 1 117 ? -18.477 8.175  0.820   1.00 49.50  ?  117 TRP   A CB    1 
ATOM   892  C CG    . TRP   A 1 117 ? -19.865 8.750  0.644   1.00 50.81  ?  117 TRP   A CG    1 
ATOM   893  C CD1   . TRP   A 1 117 ? -20.594 9.425  1.576   1.00 43.30  ?  117 TRP   A CD1   1 
ATOM   894  C CD2   . TRP   A 1 117 ? -20.679 8.696  -0.538  1.00 44.62  ?  117 TRP   A CD2   1 
ATOM   895  N NE1   . TRP   A 1 117 ? -21.811 9.792  1.053   1.00 45.88  ?  117 TRP   A NE1   1 
ATOM   896  C CE2   . TRP   A 1 117 ? -21.888 9.359  -0.243  1.00 46.31  ?  117 TRP   A CE2   1 
ATOM   897  C CE3   . TRP   A 1 117 ? -20.500 8.156  -1.819  1.00 49.46  ?  117 TRP   A CE3   1 
ATOM   898  C CZ2   . TRP   A 1 117 ? -22.917 9.497  -1.181  1.00 45.49  ?  117 TRP   A CZ2   1 
ATOM   899  C CZ3   . TRP   A 1 117 ? -21.526 8.286  -2.745  1.00 48.36  ?  117 TRP   A CZ3   1 
ATOM   900  C CH2   . TRP   A 1 117 ? -22.722 8.946  -2.418  1.00 44.74  ?  117 TRP   A CH2   1 
ATOM   901  N N     . THR   A 1 118 ? -16.717 5.287  1.129   1.00 40.99  ?  118 THR   A N     1 
ATOM   902  C CA    . THR   A 1 118 ? -15.341 4.826  1.059   1.00 41.19  ?  118 THR   A CA    1 
ATOM   903  C C     . THR   A 1 118 ? -14.686 5.420  -0.186  1.00 39.05  ?  118 THR   A C     1 
ATOM   904  O O     . THR   A 1 118 ? -15.177 5.239  -1.304  1.00 42.74  ?  118 THR   A O     1 
ATOM   905  C CB    . THR   A 1 118 ? -15.274 3.301  1.056   1.00 42.16  ?  118 THR   A CB    1 
ATOM   906  O OG1   . THR   A 1 118 ? -15.728 2.806  2.315   1.00 47.53  ?  118 THR   A OG1   1 
ATOM   907  C CG2   . THR   A 1 118 ? -13.850 2.815  0.785   1.00 36.50  ?  118 THR   A CG2   1 
ATOM   908  N N     . VAL   A 1 119 ? -13.599 6.150  0.022   1.00 41.83  ?  119 VAL   A N     1 
ATOM   909  C CA    . VAL   A 1 119 ? -12.858 6.840  -1.025  1.00 45.41  ?  119 VAL   A CA    1 
ATOM   910  C C     . VAL   A 1 119 ? -11.499 6.160  -1.142  1.00 47.96  ?  119 VAL   A C     1 
ATOM   911  O O     . VAL   A 1 119 ? -10.753 6.057  -0.158  1.00 48.03  ?  119 VAL   A O     1 
ATOM   912  C CB    . VAL   A 1 119 ? -12.708 8.340  -0.707  1.00 46.48  ?  119 VAL   A CB    1 
ATOM   913  C CG1   . VAL   A 1 119 ? -11.795 9.032  -1.710  1.00 40.55  ?  119 VAL   A CG1   1 
ATOM   914  C CG2   . VAL   A 1 119 ? -14.096 9.017  -0.609  1.00 40.61  ?  119 VAL   A CG2   1 
ATOM   915  N N     . VAL   A 1 120 ? -11.188 5.660  -2.323  1.00 48.47  ?  120 VAL   A N     1 
ATOM   916  C CA    . VAL   A 1 120 ? -9.887  5.063  -2.578  1.00 52.31  ?  120 VAL   A CA    1 
ATOM   917  C C     . VAL   A 1 120 ? -9.065  6.074  -3.349  1.00 49.67  ?  120 VAL   A C     1 
ATOM   918  O O     . VAL   A 1 120 ? -9.520  6.599  -4.371  1.00 47.56  ?  120 VAL   A O     1 
ATOM   919  C CB    . VAL   A 1 120 ? -10.011 3.744  -3.353  1.00 47.48  ?  120 VAL   A CB    1 
ATOM   920  C CG1   . VAL   A 1 120 ? -8.639  3.160  -3.576  1.00 44.49  ?  120 VAL   A CG1   1 
ATOM   921  C CG2   . VAL   A 1 120 ? -10.916 2.776  -2.591  1.00 45.22  ?  120 VAL   A CG2   1 
ATOM   922  N N     . SER   A 1 121 ? -7.869  6.331  -2.849  1.00 48.05  ?  121 SER   A N     1 
ATOM   923  C CA    . SER   A 1 121 ? -7.020  7.370  -3.457  1.00 52.24  ?  121 SER   A CA    1 
ATOM   924  C C     . SER   A 1 121 ? -5.656  6.798  -3.830  1.00 58.81  ?  121 SER   A C     1 
ATOM   925  O O     . SER   A 1 121 ? -5.126  5.971  -3.091  1.00 56.99  ?  121 SER   A O     1 
ATOM   926  C CB    . SER   A 1 121 ? -6.867  8.499  -2.509  1.00 52.98  ?  121 SER   A CB    1 
ATOM   927  O OG    . SER   A 1 121 ? -7.089  8.091  -1.170  1.00 57.58  ?  121 SER   A OG    1 
ATOM   928  N N     . ARG   A 1 122 ? -5.126  7.258  -4.946  1.00 59.83  ?  122 ARG   A N     1 
ATOM   929  C CA    . ARG   A 1 122 ? -3.794  6.813  -5.388  1.00 66.39  ?  122 ARG   A CA    1 
ATOM   930  C C     . ARG   A 1 122 ? -2.810  7.911  -5.021  1.00 72.72  ?  122 ARG   A C     1 
ATOM   931  O O     . ARG   A 1 122 ? -2.950  9.025  -5.536  1.00 71.80  ?  122 ARG   A O     1 
ATOM   932  C CB    . ARG   A 1 122 ? -3.763  6.633  -6.903  1.00 66.76  ?  122 ARG   A CB    1 
ATOM   933  C CG    . ARG   A 1 122 ? -3.060  5.362  -7.343  1.00 75.73  ?  122 ARG   A CG    1 
ATOM   934  C CD    . ARG   A 1 122 ? -3.447  4.987  -8.753  1.00 80.92  ?  122 ARG   A CD    1 
ATOM   935  N NE    . ARG   A 1 122 ? -3.313  6.117  -9.676  1.00 79.71  ?  122 ARG   A NE    1 
ATOM   936  C CZ    . ARG   A 1 122 ? -3.601  6.037  -10.965 1.00 87.54  ?  122 ARG   A CZ    1 
ATOM   937  N NH1   . ARG   A 1 122 ? -4.559  5.227  -11.372 1.00 86.83  ?  122 ARG   A NH1   1 
ATOM   938  N NH2   . ARG   A 1 122 ? -2.936  6.768  -11.841 1.00 90.10  ?  122 ARG   A NH2   1 
ATOM   939  N N     . GLY   A 1 123 ? -1.853  7.588  -4.169  1.00 75.87  ?  123 GLY   A N     1 
ATOM   940  C CA    . GLY   A 1 123 ? -0.859  8.572  -3.736  1.00 72.77  ?  123 GLY   A CA    1 
ATOM   941  C C     . GLY   A 1 123 ? 0.189   8.809  -4.785  1.00 80.09  ?  123 GLY   A C     1 
ATOM   942  O O     . GLY   A 1 123 ? 0.014   8.355  -5.920  1.00 82.28  ?  123 GLY   A O     1 
ATOM   943  N N     . ALA   A 1 124 ? 1.263   9.486  -4.410  1.00 82.48  ?  124 ALA   A N     1 
ATOM   944  C CA    . ALA   A 1 124 ? 2.286   9.845  -5.410  1.00 83.68  ?  124 ALA   A CA    1 
ATOM   945  C C     . ALA   A 1 124 ? 2.971   8.594  -5.932  1.00 89.68  ?  124 ALA   A C     1 
ATOM   946  O O     . ALA   A 1 124 ? 3.310   8.565  -7.124  1.00 88.96  ?  124 ALA   A O     1 
ATOM   947  C CB    . ALA   A 1 124 ? 3.278   10.754 -4.772  1.00 81.79  ?  124 ALA   A CB    1 
ATOM   948  N N     . ASP   A 1 125 ? 3.144   7.591  -5.074  1.00 89.37  ?  125 ASP   A N     1 
ATOM   949  C CA    . ASP   A 1 125 ? 3.743   6.360  -5.582  1.00 89.16  ?  125 ASP   A CA    1 
ATOM   950  C C     . ASP   A 1 125 ? 2.811   5.560  -6.472  1.00 89.03  ?  125 ASP   A C     1 
ATOM   951  O O     . ASP   A 1 125 ? 3.277   4.679  -7.204  1.00 86.40  ?  125 ASP   A O     1 
ATOM   952  C CB    . ASP   A 1 125 ? 4.135   5.492  -4.409  1.00 86.56  ?  125 ASP   A CB    1 
ATOM   953  C CG    . ASP   A 1 125 ? 4.705   6.301  -3.305  1.00 91.10  ?  125 ASP   A CG    1 
ATOM   954  O OD1   . ASP   A 1 125 ? 5.306   7.351  -3.622  1.00 97.07  ?  125 ASP   A OD1   1 
ATOM   955  O OD2   . ASP   A 1 125 ? 4.514   5.922  -2.134  1.00 96.60  ?  125 ASP   A OD2   1 
ATOM   956  N N     . GLY   A 1 126 ? 1.517   5.850  -6.428  1.00 88.38  ?  126 GLY   A N     1 
ATOM   957  C CA    . GLY   A 1 126 ? 0.514   4.910  -6.858  1.00 83.77  ?  126 GLY   A CA    1 
ATOM   958  C C     . GLY   A 1 126 ? 0.000   4.040  -5.737  1.00 82.67  ?  126 GLY   A C     1 
ATOM   959  O O     . GLY   A 1 126 ? -0.927  3.252  -5.966  1.00 84.48  ?  126 GLY   A O     1 
ATOM   960  N N     . ALA   A 1 127 ? 0.571   4.160  -4.530  1.00 76.56  ?  127 ALA   A N     1 
ATOM   961  C CA    . ALA   A 1 127 ? 0.077   3.442  -3.356  1.00 76.02  ?  127 ALA   A CA    1 
ATOM   962  C C     . ALA   A 1 127 ? -1.392  3.746  -3.055  1.00 74.91  ?  127 ALA   A C     1 
ATOM   963  O O     . ALA   A 1 127 ? -1.737  4.834  -2.571  1.00 70.53  ?  127 ALA   A O     1 
ATOM   964  C CB    . ALA   A 1 127 ? 0.933   3.767  -2.131  1.00 72.81  ?  127 ALA   A CB    1 
ATOM   965  N N     . GLN   A 1 128 ? -2.265  2.781  -3.329  1.00 72.99  ?  128 GLN   A N     1 
ATOM   966  C CA    . GLN   A 1 128 ? -3.687  2.981  -3.090  1.00 71.18  ?  128 GLN   A CA    1 
ATOM   967  C C     . GLN   A 1 128 ? -3.968  2.901  -1.598  1.00 60.32  ?  128 GLN   A C     1 
ATOM   968  O O     . GLN   A 1 128 ? -3.581  1.934  -0.941  1.00 64.76  ?  128 GLN   A O     1 
ATOM   969  C CB    . GLN   A 1 128 ? -4.519  1.947  -3.852  1.00 72.83  ?  128 GLN   A CB    1 
ATOM   970  C CG    . GLN   A 1 128 ? -4.810  2.315  -5.313  1.00 74.04  ?  128 GLN   A CG    1 
ATOM   971  C CD    . GLN   A 1 128 ? -4.091  1.397  -6.309  1.00 85.73  ?  128 GLN   A CD    1 
ATOM   972  O OE1   . GLN   A 1 128 ? -3.129  0.702  -5.956  1.00 86.05  ?  128 GLN   A OE1   1 
ATOM   973  N NE2   . GLN   A 1 128 ? -4.550  1.402  -7.557  1.00 75.72  ?  128 GLN   A NE2   1 
ATOM   974  N N     . VAL   A 1 129 ? -4.622  3.927  -1.071  1.00 59.48  ?  129 VAL   A N     1 
ATOM   975  C CA    . VAL   A 1 129 ? -5.170  3.940  0.279   1.00 61.18  ?  129 VAL   A CA    1 
ATOM   976  C C     . VAL   A 1 129 ? -6.681  4.051  0.159   1.00 58.08  ?  129 VAL   A C     1 
ATOM   977  O O     . VAL   A 1 129 ? -7.212  4.658  -0.783  1.00 60.24  ?  129 VAL   A O     1 
ATOM   978  C CB    . VAL   A 1 129 ? -4.613  5.099  1.130   1.00 55.87  ?  129 VAL   A CB    1 
ATOM   979  C CG1   . VAL   A 1 129 ? -5.086  4.964  2.583   1.00 55.59  ?  129 VAL   A CG1   1 
ATOM   980  C CG2   . VAL   A 1 129 ? -3.072  5.132  1.040   1.00 57.77  ?  129 VAL   A CG2   1 
ATOM   981  N N     . SER   A 1 130 ? -7.380  3.462  1.121   1.00 48.04  ?  130 SER   A N     1 
ATOM   982  C CA    . SER   A 1 130 ? -8.833  3.436  1.116   1.00 46.62  ?  130 SER   A CA    1 
ATOM   983  C C     . SER   A 1 130 ? -9.293  4.066  2.422   1.00 53.55  ?  130 SER   A C     1 
ATOM   984  O O     . SER   A 1 130 ? -8.886  3.623  3.496   1.00 55.11  ?  130 SER   A O     1 
ATOM   985  C CB    . SER   A 1 130 ? -9.342  1.999  0.942   1.00 46.83  ?  130 SER   A CB    1 
ATOM   986  O OG    . SER   A 1 130 ? -10.656 1.820  1.426   1.00 48.56  ?  130 SER   A OG    1 
ATOM   987  N N     . ARG   A 1 131 ? -10.101 5.124  2.337   1.00 50.12  ?  131 ARG   A N     1 
ATOM   988  C CA    . ARG   A 1 131 ? -10.513 5.864  3.519   1.00 45.67  ?  131 ARG   A CA    1 
ATOM   989  C C     . ARG   A 1 131 ? -12.028 6.030  3.532   1.00 48.78  ?  131 ARG   A C     1 
ATOM   990  O O     . ARG   A 1 131 ? -12.710 5.818  2.525   1.00 46.38  ?  131 ARG   A O     1 
ATOM   991  C CB    . ARG   A 1 131 ? -9.831  7.228  3.583   1.00 48.52  ?  131 ARG   A CB    1 
ATOM   992  C CG    . ARG   A 1 131 ? -8.384  7.139  3.956   1.00 50.92  ?  131 ARG   A CG    1 
ATOM   993  C CD    . ARG   A 1 131 ? -7.731  8.498  3.879   1.00 49.59  ?  131 ARG   A CD    1 
ATOM   994  N NE    . ARG   A 1 131 ? -7.308  8.765  2.514   1.00 55.39  ?  131 ARG   A NE    1 
ATOM   995  C CZ    . ARG   A 1 131 ? -6.729  9.889  2.124   1.00 53.49  ?  131 ARG   A CZ    1 
ATOM   996  N NH1   . ARG   A 1 131 ? -6.503  10.851 3.015   1.00 54.00  ?  131 ARG   A NH1   1 
ATOM   997  N NH2   . ARG   A 1 131 ? -6.378  10.047 0.852   1.00 45.47  ?  131 ARG   A NH2   1 
ATOM   998  N N     . ARG   A 1 132 ? -12.563 6.419  4.687   1.00 42.34  ?  132 ARG   A N     1 
ATOM   999  C CA    . ARG   A 1 132 ? -13.999 6.619  4.845   1.00 46.67  ?  132 ARG   A CA    1 
ATOM   1000 C C     . ARG   A 1 132 ? -14.312 8.038  5.293   1.00 49.13  ?  132 ARG   A C     1 
ATOM   1001 O O     . ARG   A 1 132 ? -13.632 8.594  6.160   1.00 57.13  ?  132 ARG   A O     1 
ATOM   1002 C CB    . ARG   A 1 132 ? -14.592 5.647  5.843   1.00 43.42  ?  132 ARG   A CB    1 
ATOM   1003 C CG    . ARG   A 1 132 ? -14.512 4.215  5.403   1.00 47.54  ?  132 ARG   A CG    1 
ATOM   1004 C CD    . ARG   A 1 132 ? -15.290 3.335  6.347   1.00 56.25  ?  132 ARG   A CD    1 
ATOM   1005 N NE    . ARG   A 1 132 ? -16.712 3.307  6.022   1.00 54.10  ?  132 ARG   A NE    1 
ATOM   1006 C CZ    . ARG   A 1 132 ? -17.675 3.336  6.937   1.00 58.76  ?  132 ARG   A CZ    1 
ATOM   1007 N NH1   . ARG   A 1 132 ? -17.351 3.414  8.229   1.00 59.19  ?  132 ARG   A NH1   1 
ATOM   1008 N NH2   . ARG   A 1 132 ? -18.954 3.295  6.561   1.00 52.08  ?  132 ARG   A NH2   1 
ATOM   1009 N N     . PHE   A 1 133 ? -15.355 8.619  4.710   1.00 48.05  ?  133 PHE   A N     1 
ATOM   1010 C CA    . PHE   A 1 133 ? -15.726 9.988  5.012   1.00 43.41  ?  133 PHE   A CA    1 
ATOM   1011 C C     . PHE   A 1 133 ? -17.226 10.061 5.166   1.00 46.16  ?  133 PHE   A C     1 
ATOM   1012 O O     . PHE   A 1 133 ? -17.963 9.299  4.541   1.00 49.57  ?  133 PHE   A O     1 
ATOM   1013 C CB    . PHE   A 1 133 ? -15.261 10.934 3.931   1.00 46.15  ?  133 PHE   A CB    1 
ATOM   1014 C CG    . PHE   A 1 133 ? -13.778 10.974 3.785   1.00 45.95  ?  133 PHE   A CG    1 
ATOM   1015 C CD1   . PHE   A 1 133 ? -13.007 11.796 4.600   1.00 45.27  ?  133 PHE   A CD1   1 
ATOM   1016 C CD2   . PHE   A 1 133 ? -13.147 10.182 2.844   1.00 43.78  ?  133 PHE   A CD2   1 
ATOM   1017 C CE1   . PHE   A 1 133 ? -11.626 11.824 4.468   1.00 43.56  ?  133 PHE   A CE1   1 
ATOM   1018 C CE2   . PHE   A 1 133 ? -11.766 10.210 2.709   1.00 47.68  ?  133 PHE   A CE2   1 
ATOM   1019 C CZ    . PHE   A 1 133 ? -11.009 11.036 3.529   1.00 49.12  ?  133 PHE   A CZ    1 
ATOM   1020 N N     . GLU   A 1 134 ? -17.671 10.956 6.040   1.00 49.02  ?  134 GLU   A N     1 
ATOM   1021 C CA    . GLU   A 1 134 ? -19.105 11.100 6.226   1.00 47.56  ?  134 GLU   A CA    1 
ATOM   1022 C C     . GLU   A 1 134 ? -19.741 11.637 4.964   1.00 46.23  ?  134 GLU   A C     1 
ATOM   1023 O O     . GLU   A 1 134 ? -20.830 11.199 4.577   1.00 51.92  ?  134 GLU   A O     1 
ATOM   1024 C CB    . GLU   A 1 134 ? -19.395 12.022 7.410   1.00 52.06  ?  134 GLU   A CB    1 
ATOM   1025 C CG    . GLU   A 1 134 ? -19.434 11.321 8.752   1.00 56.37  ?  134 GLU   A CG    1 
ATOM   1026 C CD    . GLU   A 1 134 ? -19.376 12.309 9.898   1.00 72.12  ?  134 GLU   A CD    1 
ATOM   1027 O OE1   . GLU   A 1 134 ? -18.633 12.051 10.888  1.00 73.76  ?  134 GLU   A OE1   1 
ATOM   1028 O OE2   . GLU   A 1 134 ? -20.074 13.355 9.789   1.00 72.75  ?  134 GLU   A OE2   1 
ATOM   1029 N N     . GLN   A 1 135 ? -19.061 12.587 4.310   1.00 46.93  ?  135 GLN   A N     1 
ATOM   1030 C CA    . GLN   A 1 135 ? -19.568 13.311 3.156   1.00 44.51  ?  135 GLN   A CA    1 
ATOM   1031 C C     . GLN   A 1 135 ? -18.430 13.540 2.177   1.00 46.57  ?  135 GLN   A C     1 
ATOM   1032 O O     . GLN   A 1 135 ? -17.260 13.613 2.571   1.00 42.45  ?  135 GLN   A O     1 
ATOM   1033 C CB    . GLN   A 1 135 ? -20.177 14.653 3.559   1.00 47.22  ?  135 GLN   A CB    1 
ATOM   1034 C CG    . GLN   A 1 135 ? -21.191 14.540 4.679   1.00 41.92  ?  135 GLN   A CG    1 
ATOM   1035 C CD    . GLN   A 1 135 ? -22.368 15.433 4.470   1.00 51.29  ?  135 GLN   A CD    1 
ATOM   1036 O OE1   . GLN   A 1 135 ? -22.803 15.646 3.334   1.00 54.54  ?  135 GLN   A OE1   1 
ATOM   1037 N NE2   . GLN   A 1 135 ? -22.917 15.960 5.566   1.00 56.78  ?  135 GLN   A NE2   1 
ATOM   1038 N N     . VAL   A 1 136 ? -18.799 13.626 0.892   1.00 44.21  ?  136 VAL   A N     1 
ATOM   1039 C CA    . VAL   A 1 136 ? -17.897 13.858 -0.233  1.00 36.39  ?  136 VAL   A CA    1 
ATOM   1040 C C     . VAL   A 1 136 ? -18.434 15.034 -1.037  1.00 40.38  ?  136 VAL   A C     1 
ATOM   1041 O O     . VAL   A 1 136 ? -19.577 14.990 -1.510  1.00 40.59  ?  136 VAL   A O     1 
ATOM   1042 C CB    . VAL   A 1 136 ? -17.785 12.634 -1.151  1.00 41.07  ?  136 VAL   A CB    1 
ATOM   1043 C CG1   . VAL   A 1 136 ? -16.689 12.843 -2.182  1.00 38.94  ?  136 VAL   A CG1   1 
ATOM   1044 C CG2   . VAL   A 1 136 ? -17.543 11.382 -0.356  1.00 45.23  ?  136 VAL   A CG2   1 
ATOM   1045 N N     . VAL   A 1 137 ? -17.616 16.070 -1.211  1.00 37.32  ?  137 VAL   A N     1 
ATOM   1046 C CA    . VAL   A 1 137 ? -17.924 17.158 -2.128  1.00 36.63  ?  137 VAL   A CA    1 
ATOM   1047 C C     . VAL   A 1 137 ? -17.105 16.946 -3.401  1.00 38.47  ?  137 VAL   A C     1 
ATOM   1048 O O     . VAL   A 1 137 ? -15.879 16.778 -3.348  1.00 40.21  ?  137 VAL   A O     1 
ATOM   1049 C CB    . VAL   A 1 137 ? -17.648 18.526 -1.485  1.00 37.74  ?  137 VAL   A CB    1 
ATOM   1050 C CG1   . VAL   A 1 137 ? -17.889 19.622 -2.487  1.00 38.16  ?  137 VAL   A CG1   1 
ATOM   1051 C CG2   . VAL   A 1 137 ? -18.561 18.732 -0.243  1.00 37.80  ?  137 VAL   A CG2   1 
ATOM   1052 N N     . VAL   A 1 138 ? -17.780 16.903 -4.546  1.00 43.38  ?  138 VAL   A N     1 
ATOM   1053 C CA    . VAL   A 1 138 ? -17.128 16.721 -5.838  1.00 41.51  ?  138 VAL   A CA    1 
ATOM   1054 C C     . VAL   A 1 138 ? -16.913 18.089 -6.450  1.00 35.61  ?  138 VAL   A C     1 
ATOM   1055 O O     . VAL   A 1 138 ? -17.868 18.856 -6.608  1.00 36.10  ?  138 VAL   A O     1 
ATOM   1056 C CB    . VAL   A 1 138 ? -17.956 15.833 -6.771  1.00 39.74  ?  138 VAL   A CB    1 
ATOM   1057 C CG1   . VAL   A 1 138 ? -17.315 15.805 -8.163  1.00 35.96  ?  138 VAL   A CG1   1 
ATOM   1058 C CG2   . VAL   A 1 138 ? -18.021 14.472 -6.192  1.00 40.99  ?  138 VAL   A CG2   1 
ATOM   1059 N N     . ALA   A 1 139 ? -15.659 18.392 -6.764  1.00 33.73  ?  139 ALA   A N     1 
ATOM   1060 C CA    . ALA   A 1 139 ? -15.269 19.643 -7.405  1.00 37.25  ?  139 ALA   A CA    1 
ATOM   1061 C C     . ALA   A 1 139 ? -14.129 19.349 -8.373  1.00 41.09  ?  139 ALA   A C     1 
ATOM   1062 O O     . ALA   A 1 139 ? -13.053 19.947 -8.308  1.00 38.78  ?  139 ALA   A O     1 
ATOM   1063 C CB    . ALA   A 1 139 ? -14.859 20.706 -6.387  1.00 31.52  ?  139 ALA   A CB    1 
ATOM   1064 N N     . SER   A 1 140 ? -14.351 18.395 -9.268  1.00 40.13  ?  140 SER   A N     1 
ATOM   1065 C CA    . SER   A 1 140 ? -13.304 17.917 -10.152 1.00 42.08  ?  140 SER   A CA    1 
ATOM   1066 C C     . SER   A 1 140 ? -13.373 18.553 -11.527 1.00 44.19  ?  140 SER   A C     1 
ATOM   1067 O O     . SER   A 1 140 ? -12.546 18.231 -12.381 1.00 44.58  ?  140 SER   A O     1 
ATOM   1068 C CB    . SER   A 1 140 ? -13.372 16.398 -10.255 1.00 35.32  ?  140 SER   A CB    1 
ATOM   1069 O OG    . SER   A 1 140 ? -14.725 16.014 -10.318 1.00 43.21  ?  140 SER   A OG    1 
ATOM   1070 N N     . GLY   A 1 141 ? -14.295 19.489 -11.734 1.00 44.43  ?  141 GLY   A N     1 
ATOM   1071 C CA    . GLY   A 1 141 ? -14.410 20.190 -12.992 1.00 47.33  ?  141 GLY   A CA    1 
ATOM   1072 C C     . GLY   A 1 141 ? -15.144 19.348 -14.017 1.00 55.67  ?  141 GLY   A C     1 
ATOM   1073 O O     . GLY   A 1 141 ? -15.392 18.157 -13.828 1.00 58.82  ?  141 GLY   A O     1 
ATOM   1074 N N     . HIS   A 1 142 ? -15.518 19.982 -15.124 1.00 46.14  ?  142 HIS   A N     1 
ATOM   1075 C CA    . HIS   A 1 142 ? -16.183 19.231 -16.179 1.00 54.88  ?  142 HIS   A CA    1 
ATOM   1076 C C     . HIS   A 1 142 ? -15.543 19.473 -17.549 1.00 55.25  ?  142 HIS   A C     1 
ATOM   1077 O O     . HIS   A 1 142 ? -16.223 19.414 -18.570 1.00 58.27  ?  142 HIS   A O     1 
ATOM   1078 C CB    . HIS   A 1 142 ? -17.671 19.559 -16.211 1.00 50.70  ?  142 HIS   A CB    1 
ATOM   1079 C CG    . HIS   A 1 142 ? -17.953 21.024 -16.267 1.00 55.93  ?  142 HIS   A CG    1 
ATOM   1080 N ND1   . HIS   A 1 142 ? -17.884 21.838 -15.158 1.00 54.84  ?  142 HIS   A ND1   1 
ATOM   1081 C CD2   . HIS   A 1 142 ? -18.294 21.827 -17.303 1.00 60.05  ?  142 HIS   A CD2   1 
ATOM   1082 C CE1   . HIS   A 1 142 ? -18.182 23.076 -15.505 1.00 50.07  ?  142 HIS   A CE1   1 
ATOM   1083 N NE2   . HIS   A 1 142 ? -18.430 23.098 -16.802 1.00 60.24  ?  142 HIS   A NE2   1 
ATOM   1084 N N     . HIS   A 1 143 ? -14.240 19.739 -17.592 1.00 54.06  ?  143 HIS   A N     1 
ATOM   1085 C CA    . HIS   A 1 143 ? -13.486 19.901 -18.835 1.00 52.07  ?  143 HIS   A CA    1 
ATOM   1086 C C     . HIS   A 1 143 ? -12.299 18.956 -18.865 1.00 50.69  ?  143 HIS   A C     1 
ATOM   1087 O O     . HIS   A 1 143 ? -11.166 19.377 -19.126 1.00 52.79  ?  143 HIS   A O     1 
ATOM   1088 C CB    . HIS   A 1 143 ? -12.923 21.313 -19.037 1.00 54.28  ?  143 HIS   A CB    1 
ATOM   1089 C CG    . HIS   A 1 143 ? -13.942 22.401 -18.987 1.00 56.31  ?  143 HIS   A CG    1 
ATOM   1090 N ND1   . HIS   A 1 143 ? -13.935 23.373 -18.011 1.00 58.13  ?  143 HIS   A ND1   1 
ATOM   1091 C CD2   . HIS   A 1 143 ? -14.974 22.700 -19.809 1.00 63.72  ?  143 HIS   A CD2   1 
ATOM   1092 C CE1   . HIS   A 1 143 ? -14.933 24.212 -18.218 1.00 57.87  ?  143 HIS   A CE1   1 
ATOM   1093 N NE2   . HIS   A 1 143 ? -15.580 23.827 -19.304 1.00 67.68  ?  143 HIS   A NE2   1 
ATOM   1094 N N     . ASN   A 1 144 ? -12.521 17.662 -18.592 1.00 52.34  ?  144 ASN   A N     1 
ATOM   1095 C CA    . ASN   A 1 144 ? -11.392 16.742 -18.462 1.00 62.26  ?  144 ASN   A CA    1 
ATOM   1096 C C     . ASN   A 1 144 ? -11.504 15.492 -19.340 1.00 66.61  ?  144 ASN   A C     1 
ATOM   1097 O O     . ASN   A 1 144 ? -10.679 14.577 -19.195 1.00 70.50  ?  144 ASN   A O     1 
ATOM   1098 C CB    . ASN   A 1 144 ? -11.139 16.339 -16.981 1.00 59.88  ?  144 ASN   A CB    1 
ATOM   1099 C CG    . ASN   A 1 144 ? -12.427 16.225 -16.130 1.00 66.36  ?  144 ASN   A CG    1 
ATOM   1100 O OD1   . ASN   A 1 144 ? -13.369 15.460 -16.446 1.00 66.83  ?  144 ASN   A OD1   1 
ATOM   1101 N ND2   . ASN   A 1 144 ? -12.465 16.997 -15.042 1.00 53.02  ?  144 ASN   A ND2   1 
ATOM   1102 N N     . GLU   A 1 145 ? -12.473 15.429 -20.251 1.00 62.96  ?  145 GLU   A N     1 
ATOM   1103 C CA    . GLU   A 1 145 ? -12.513 14.383 -21.274 1.00 59.73  ?  145 GLU   A CA    1 
ATOM   1104 C C     . GLU   A 1 145 ? -12.693 15.076 -22.612 1.00 58.42  ?  145 GLU   A C     1 
ATOM   1105 O O     . GLU   A 1 145 ? -13.723 15.749 -22.825 1.00 53.05  ?  145 GLU   A O     1 
ATOM   1106 C CB    . GLU   A 1 145 ? -13.635 13.368 -21.047 1.00 60.74  ?  145 GLU   A CB    1 
ATOM   1107 C CG    . GLU   A 1 145 ? -13.244 11.955 -21.410 1.00 64.29  ?  145 GLU   A CG    1 
ATOM   1108 C CD    . GLU   A 1 145 ? -11.880 11.566 -20.840 1.00 77.05  ?  145 GLU   A CD    1 
ATOM   1109 O OE1   . GLU   A 1 145 ? -11.635 11.812 -19.631 1.00 74.86  ?  145 GLU   A OE1   1 
ATOM   1110 O OE2   . GLU   A 1 145 ? -11.051 11.011 -21.601 1.00 76.45  ?  145 GLU   A OE2   1 
ATOM   1111 N N     . PRO   A 1 146 ? -11.740 14.963 -23.531 1.00 63.63  ?  146 PRO   A N     1 
ATOM   1112 C CA    . PRO   A 1 146 ? -11.895 15.640 -24.820 1.00 61.12  ?  146 PRO   A CA    1 
ATOM   1113 C C     . PRO   A 1 146 ? -13.106 15.095 -25.560 1.00 63.81  ?  146 PRO   A C     1 
ATOM   1114 O O     . PRO   A 1 146 ? -13.517 13.947 -25.373 1.00 64.53  ?  146 PRO   A O     1 
ATOM   1115 C CB    . PRO   A 1 146 ? -10.586 15.326 -25.551 1.00 53.99  ?  146 PRO   A CB    1 
ATOM   1116 C CG    . PRO   A 1 146 ? -10.126 14.066 -24.941 1.00 60.53  ?  146 PRO   A CG    1 
ATOM   1117 C CD    . PRO   A 1 146 ? -10.509 14.160 -23.485 1.00 62.95  ?  146 PRO   A CD    1 
ATOM   1118 N N     . ALA   A 1 147 ? -13.700 15.955 -26.373 1.00 60.14  ?  147 ALA   A N     1 
ATOM   1119 C CA    . ALA   A 1 147 ? -14.864 15.615 -27.168 1.00 60.47  ?  147 ALA   A CA    1 
ATOM   1120 C C     . ALA   A 1 147 ? -14.455 15.802 -28.626 1.00 66.29  ?  147 ALA   A C     1 
ATOM   1121 O O     . ALA   A 1 147 ? -14.530 16.915 -29.157 1.00 64.56  ?  147 ALA   A O     1 
ATOM   1122 C CB    . ALA   A 1 147 ? -16.061 16.485 -26.775 1.00 57.24  ?  147 ALA   A CB    1 
ATOM   1123 N N     . LEU   A 1 148 ? -13.989 14.712 -29.262 1.00 70.41  ?  148 LEU   A N     1 
ATOM   1124 C CA    . LEU   A 1 148 ? -13.650 14.749 -30.688 1.00 69.07  ?  148 LEU   A CA    1 
ATOM   1125 C C     . LEU   A 1 148 ? -14.900 14.485 -31.533 1.00 69.50  ?  148 LEU   A C     1 
ATOM   1126 O O     . LEU   A 1 148 ? -15.738 13.661 -31.158 1.00 66.37  ?  148 LEU   A O     1 
ATOM   1127 C CB    . LEU   A 1 148 ? -12.563 13.722 -31.023 1.00 69.14  ?  148 LEU   A CB    1 
ATOM   1128 C CG    . LEU   A 1 148 ? -11.097 14.145 -30.820 1.00 67.48  ?  148 LEU   A CG    1 
ATOM   1129 C CD1   . LEU   A 1 148 ? -10.169 12.943 -30.630 1.00 69.89  ?  148 LEU   A CD1   1 
ATOM   1130 C CD2   . LEU   A 1 148 ? -10.593 15.039 -31.975 1.00 61.39  ?  148 LEU   A CD2   1 
ATOM   1131 N N     . PRO   A 1 149 ? -15.058 15.132 -32.717 1.00 75.60  ?  149 PRO   A N     1 
ATOM   1132 C CA    . PRO   A 1 149 ? -16.271 14.967 -33.503 1.00 80.01  ?  149 PRO   A CA    1 
ATOM   1133 C C     . PRO   A 1 149 ? -16.430 13.579 -34.091 1.00 80.08  ?  149 PRO   A C     1 
ATOM   1134 O O     . PRO   A 1 149 ? -15.436 12.896 -34.379 1.00 78.03  ?  149 PRO   A O     1 
ATOM   1135 C CB    . PRO   A 1 149 ? -16.069 15.998 -34.590 1.00 72.53  ?  149 PRO   A CB    1 
ATOM   1136 C CG    . PRO   A 1 149 ? -14.598 15.971 -34.835 1.00 67.04  ?  149 PRO   A CG    1 
ATOM   1137 C CD    . PRO   A 1 149 ? -14.101 16.014 -33.416 1.00 69.11  ?  149 PRO   A CD    1 
ATOM   1138 N N     . ASP   A 1 150 ? -17.676 13.157 -34.265 1.00 80.75  ?  150 ASP   A N     1 
ATOM   1139 C CA    . ASP   A 1 150 ? -17.942 11.818 -34.856 1.00 83.34  ?  150 ASP   A CA    1 
ATOM   1140 C C     . ASP   A 1 150 ? -18.970 11.977 -35.979 1.00 83.71  ?  150 ASP   A C     1 
ATOM   1141 O O     . ASP   A 1 150 ? -20.088 12.437 -35.706 1.00 88.20  ?  150 ASP   A O     1 
ATOM   1142 C CB    . ASP   A 1 150 ? -18.325 10.800 -33.792 1.00 80.23  ?  150 ASP   A CB    1 
ATOM   1143 C CG    . ASP   A 1 150 ? -17.989 9.353  -34.116 1.00 84.29  ?  150 ASP   A CG    1 
ATOM   1144 O OD1   . ASP   A 1 150 ? -16.943 9.122  -34.752 1.00 84.97  ?  150 ASP   A OD1   1 
ATOM   1145 O OD2   . ASP   A 1 150 ? -18.775 8.472  -33.726 1.00 82.45  ?  150 ASP   A OD2   1 
ATOM   1146 N N     . PRO   A 1 151 ? -18.616 11.630 -37.233 1.00 79.66  ?  151 PRO   A N     1 
ATOM   1147 C CA    . PRO   A 1 151 ? -17.347 10.980 -37.470 1.00 78.60  ?  151 PRO   A CA    1 
ATOM   1148 C C     . PRO   A 1 151 ? -16.215 11.923 -37.781 1.00 77.90  ?  151 PRO   A C     1 
ATOM   1149 O O     . PRO   A 1 151 ? -16.427 13.047 -38.252 1.00 72.68  ?  151 PRO   A O     1 
ATOM   1150 C CB    . PRO   A 1 151 ? -17.706 10.106 -38.670 1.00 75.76  ?  151 PRO   A CB    1 
ATOM   1151 C CG    . PRO   A 1 151 ? -18.680 10.940 -39.462 1.00 76.21  ?  151 PRO   A CG    1 
ATOM   1152 C CD    . PRO   A 1 151 ? -19.403 11.808 -38.451 1.00 76.20  ?  151 PRO   A CD    1 
ATOM   1153 N N     . LEU   A 1 152 ? -15.007 11.484 -37.471 1.00 73.75  ?  152 LEU   A N     1 
ATOM   1154 C CA    . LEU   A 1 152 ? -13.860 12.289 -37.908 1.00 73.23  ?  152 LEU   A CA    1 
ATOM   1155 C C     . LEU   A 1 152 ? -13.934 12.203 -39.428 1.00 79.97  ?  152 LEU   A C     1 
ATOM   1156 O O     . LEU   A 1 152 ? -13.998 11.072 -39.932 1.00 78.62  ?  152 LEU   A O     1 
ATOM   1157 C CB    . LEU   A 1 152 ? -12.562 11.704 -37.378 1.00 70.56  ?  152 LEU   A CB    1 
ATOM   1158 C CG    . LEU   A 1 152 ? -11.523 12.713 -36.881 1.00 80.98  ?  152 LEU   A CG    1 
ATOM   1159 C CD1   . LEU   A 1 152 ? -12.179 13.723 -35.968 1.00 78.73  ?  152 LEU   A CD1   1 
ATOM   1160 C CD2   . LEU   A 1 152 ? -10.382 12.028 -36.158 1.00 79.83  ?  152 LEU   A CD2   1 
ATOM   1161 N N     . PRO   A 1 153 ? -13.995 13.324 -40.171 1.00 76.41  ?  153 PRO   A N     1 
ATOM   1162 C CA    . PRO   A 1 153 ? -13.991 13.268 -41.622 1.00 68.15  ?  153 PRO   A CA    1 
ATOM   1163 C C     . PRO   A 1 153 ? -13.047 12.339 -42.380 1.00 65.23  ?  153 PRO   A C     1 
ATOM   1164 O O     . PRO   A 1 153 ? -11.879 12.153 -42.013 1.00 65.76  ?  153 PRO   A O     1 
ATOM   1165 C CB    . PRO   A 1 153 ? -13.524 14.671 -41.983 1.00 70.05  ?  153 PRO   A CB    1 
ATOM   1166 C CG    . PRO   A 1 153 ? -13.216 15.343 -40.670 1.00 72.79  ?  153 PRO   A CG    1 
ATOM   1167 C CD    . PRO   A 1 153 ? -14.084 14.657 -39.651 1.00 73.03  ?  153 PRO   A CD    1 
ATOM   1168 N N     . ALA   A 1 154 ? -13.539 11.801 -43.489 1.00 67.15  ?  154 ALA   A N     1 
ATOM   1169 C CA    . ALA   A 1 154 ? -12.889 10.666 -44.181 1.00 62.54  ?  154 ALA   A CA    1 
ATOM   1170 C C     . ALA   A 1 154 ? -11.465 10.968 -44.598 1.00 61.22  ?  154 ALA   A C     1 
ATOM   1171 O O     . ALA   A 1 154 ? -11.156 12.098 -44.966 1.00 58.97  ?  154 ALA   A O     1 
ATOM   1172 C CB    . ALA   A 1 154 ? -13.708 10.293 -45.371 1.00 58.75  ?  154 ALA   A CB    1 
ATOM   1173 N N     . GLY   A 1 155 ? -10.650 9.926  -44.617 1.00 60.50  ?  155 GLY   A N     1 
ATOM   1174 C CA    . GLY   A 1 155 ? -9.254  10.158 -44.899 1.00 60.75  ?  155 GLY   A CA    1 
ATOM   1175 C C     . GLY   A 1 155 ? -8.418  10.432 -43.677 1.00 66.05  ?  155 GLY   A C     1 
ATOM   1176 O O     . GLY   A 1 155 ? -7.204  10.642 -43.817 1.00 67.55  ?  155 GLY   A O     1 
ATOM   1177 N N     . ALA   A 1 156 ? -9.035  10.432 -42.487 1.00 62.96  ?  156 ALA   A N     1 
ATOM   1178 C CA    . ALA   A 1 156 ? -8.316  10.715 -41.248 1.00 67.99  ?  156 ALA   A CA    1 
ATOM   1179 C C     . ALA   A 1 156 ? -7.031  9.899  -41.140 1.00 69.07  ?  156 ALA   A C     1 
ATOM   1180 O O     . ALA   A 1 156 ? -5.986  10.417 -40.717 1.00 65.34  ?  156 ALA   A O     1 
ATOM   1181 C CB    . ALA   A 1 156 ? -9.227  10.446 -40.051 1.00 68.55  ?  156 ALA   A CB    1 
ATOM   1182 N N     . ASP   A 1 157 ? -7.083  8.627  -41.544 1.00 67.92  ?  157 ASP   A N     1 
ATOM   1183 C CA    . ASP   A 1 157 ? -5.906  7.775  -41.447 1.00 72.39  ?  157 ASP   A CA    1 
ATOM   1184 C C     . ASP   A 1 157 ? -4.923  8.040  -42.575 1.00 72.36  ?  157 ASP   A C     1 
ATOM   1185 O O     . ASP   A 1 157 ? -3.723  7.772  -42.427 1.00 74.02  ?  157 ASP   A O     1 
ATOM   1186 C CB    . ASP   A 1 157 ? -6.338  6.315  -41.440 1.00 75.46  ?  157 ASP   A CB    1 
ATOM   1187 C CG    . ASP   A 1 157 ? -7.429  6.047  -40.423 1.00 80.92  ?  157 ASP   A CG    1 
ATOM   1188 O OD1   . ASP   A 1 157 ? -7.118  5.908  -39.213 1.00 80.10  ?  157 ASP   A OD1   1 
ATOM   1189 O OD2   . ASP   A 1 157 ? -8.607  5.999  -40.842 1.00 87.34  ?  157 ASP   A OD2   1 
ATOM   1190 N N     . SER   A 1 158 ? -5.404  8.575  -43.696 1.00 72.81  ?  158 SER   A N     1 
ATOM   1191 C CA    . SER   A 1 158 ? -4.493  8.973  -44.757 1.00 70.16  ?  158 SER   A CA    1 
ATOM   1192 C C     . SER   A 1 158 ? -3.596  10.111 -44.319 1.00 73.15  ?  158 SER   A C     1 
ATOM   1193 O O     . SER   A 1 158 ? -2.540  10.316 -44.928 1.00 73.58  ?  158 SER   A O     1 
ATOM   1194 C CB    . SER   A 1 158 ? -5.279  9.417  -45.994 1.00 70.03  ?  158 SER   A CB    1 
ATOM   1195 O OG    . SER   A 1 158 ? -6.409  8.585  -46.157 1.00 72.58  ?  158 SER   A OG    1 
ATOM   1196 N N     . PHE   A 1 159 ? -4.003  10.862 -43.290 1.00 68.93  ?  159 PHE   A N     1 
ATOM   1197 C CA    . PHE   A 1 159 ? -3.481  12.207 -43.092 1.00 68.17  ?  159 PHE   A CA    1 
ATOM   1198 C C     . PHE   A 1 159 ? -1.998  12.195 -42.736 1.00 70.68  ?  159 PHE   A C     1 
ATOM   1199 O O     . PHE   A 1 159 ? -1.568  11.507 -41.801 1.00 73.27  ?  159 PHE   A O     1 
ATOM   1200 C CB    . PHE   A 1 159 ? -4.268  12.953 -42.019 1.00 69.07  ?  159 PHE   A CB    1 
ATOM   1201 C CG    . PHE   A 1 159 ? -4.068  14.436 -42.075 1.00 71.01  ?  159 PHE   A CG    1 
ATOM   1202 C CD1   . PHE   A 1 159 ? -4.424  15.140 -43.216 1.00 64.73  ?  159 PHE   A CD1   1 
ATOM   1203 C CD2   . PHE   A 1 159 ? -3.471  15.120 -41.014 1.00 70.16  ?  159 PHE   A CD2   1 
ATOM   1204 C CE1   . PHE   A 1 159 ? -4.225  16.504 -43.299 1.00 64.46  ?  159 PHE   A CE1   1 
ATOM   1205 C CE2   . PHE   A 1 159 ? -3.267  16.493 -41.086 1.00 65.16  ?  159 PHE   A CE2   1 
ATOM   1206 C CZ    . PHE   A 1 159 ? -3.649  17.186 -42.233 1.00 69.87  ?  159 PHE   A CZ    1 
ATOM   1207 N N     . ALA   A 1 160 ? -1.226  12.980 -43.497 1.00 61.90  ?  160 ALA   A N     1 
ATOM   1208 C CA    . ALA   A 1 160 ? 0.218   13.030 -43.325 1.00 69.98  ?  160 ALA   A CA    1 
ATOM   1209 C C     . ALA   A 1 160 ? 0.600   13.746 -42.040 1.00 73.52  ?  160 ALA   A C     1 
ATOM   1210 O O     . ALA   A 1 160 ? 1.562   13.355 -41.367 1.00 76.81  ?  160 ALA   A O     1 
ATOM   1211 C CB    . ALA   A 1 160 ? 0.861   13.721 -44.523 1.00 72.12  ?  160 ALA   A CB    1 
ATOM   1212 N N     . GLY   A 1 161 ? -0.131  14.795 -41.689 1.00 68.62  ?  161 GLY   A N     1 
ATOM   1213 C CA    . GLY   A 1 161 ? 0.127   15.547 -40.481 1.00 67.46  ?  161 GLY   A CA    1 
ATOM   1214 C C     . GLY   A 1 161 ? -0.518  14.946 -39.249 1.00 69.02  ?  161 GLY   A C     1 
ATOM   1215 O O     . GLY   A 1 161 ? -0.933  13.785 -39.228 1.00 71.67  ?  161 GLY   A O     1 
ATOM   1216 N N     . THR   A 1 162 ? -0.604  15.774 -38.210 1.00 64.61  ?  162 THR   A N     1 
ATOM   1217 C CA    . THR   A 1 162 ? -1.126  15.407 -36.902 1.00 59.79  ?  162 THR   A CA    1 
ATOM   1218 C C     . THR   A 1 162 ? -2.526  15.970 -36.716 1.00 59.81  ?  162 THR   A C     1 
ATOM   1219 O O     . THR   A 1 162 ? -2.786  17.129 -37.047 1.00 56.88  ?  162 THR   A O     1 
ATOM   1220 C CB    . THR   A 1 162 ? -0.229  15.946 -35.795 1.00 54.91  ?  162 THR   A CB    1 
ATOM   1221 O OG1   . THR   A 1 162 ? 0.278   17.218 -36.205 1.00 65.70  ?  162 THR   A OG1   1 
ATOM   1222 C CG2   . THR   A 1 162 ? 0.922   15.008 -35.521 1.00 61.66  ?  162 THR   A CG2   1 
ATOM   1223 N N     . ILE   A 1 163 ? -3.417  15.141 -36.180 1.00 59.84  ?  163 ILE   A N     1 
ATOM   1224 C CA    . ILE   A 1 163 ? -4.753  15.546 -35.762 1.00 53.48  ?  163 ILE   A CA    1 
ATOM   1225 C C     . ILE   A 1 163 ? -4.771  15.555 -34.245 1.00 53.62  ?  163 ILE   A C     1 
ATOM   1226 O O     . ILE   A 1 163 ? -4.347  14.585 -33.609 1.00 58.14  ?  163 ILE   A O     1 
ATOM   1227 C CB    . ILE   A 1 163 ? -5.821  14.600 -36.327 1.00 59.92  ?  163 ILE   A CB    1 
ATOM   1228 C CG1   . ILE   A 1 163 ? -5.746  14.619 -37.857 1.00 59.48  ?  163 ILE   A CG1   1 
ATOM   1229 C CG2   . ILE   A 1 163 ? -7.207  14.982 -35.819 1.00 56.55  ?  163 ILE   A CG2   1 
ATOM   1230 C CD1   . ILE   A 1 163 ? -7.004  14.140 -38.542 1.00 65.27  ?  163 ILE   A CD1   1 
ATOM   1231 N N     . LEU   A 1 164 ? -5.225  16.655 -33.658 1.00 50.55  ?  164 LEU   A N     1 
ATOM   1232 C CA    . LEU   A 1 164 ? -5.151  16.757 -32.209 1.00 52.53  ?  164 LEU   A CA    1 
ATOM   1233 C C     . LEU   A 1 164 ? -6.325  17.566 -31.699 1.00 50.81  ?  164 LEU   A C     1 
ATOM   1234 O O     . LEU   A 1 164 ? -6.941  18.340 -32.435 1.00 48.80  ?  164 LEU   A O     1 
ATOM   1235 C CB    . LEU   A 1 164 ? -3.839  17.386 -31.741 1.00 48.81  ?  164 LEU   A CB    1 
ATOM   1236 C CG    . LEU   A 1 164 ? -3.501  18.793 -32.232 1.00 51.93  ?  164 LEU   A CG    1 
ATOM   1237 C CD1   . LEU   A 1 164 ? -2.637  19.546 -31.214 1.00 46.02  ?  164 LEU   A CD1   1 
ATOM   1238 C CD2   . LEU   A 1 164 ? -2.800  18.738 -33.584 1.00 52.22  ?  164 LEU   A CD2   1 
ATOM   1239 N N     . HIS   A 1 165 ? -6.645  17.342 -30.430 1.00 54.63  ?  165 HIS   A N     1 
ATOM   1240 C CA    . HIS   A 1 165 ? -7.638  18.133 -29.727 1.00 53.10  ?  165 HIS   A CA    1 
ATOM   1241 C C     . HIS   A 1 165 ? -6.944  19.304 -29.046 1.00 53.23  ?  165 HIS   A C     1 
ATOM   1242 O O     . HIS   A 1 165 ? -5.736  19.257 -28.775 1.00 52.09  ?  165 HIS   A O     1 
ATOM   1243 C CB    . HIS   A 1 165 ? -8.381  17.272 -28.706 1.00 53.52  ?  165 HIS   A CB    1 
ATOM   1244 C CG    . HIS   A 1 165 ? -9.654  17.884 -28.220 1.00 54.61  ?  165 HIS   A CG    1 
ATOM   1245 N ND1   . HIS   A 1 165 ? -9.734  18.593 -27.040 1.00 54.90  ?  165 HIS   A ND1   1 
ATOM   1246 C CD2   . HIS   A 1 165 ? -10.896 17.900 -28.759 1.00 56.45  ?  165 HIS   A CD2   1 
ATOM   1247 C CE1   . HIS   A 1 165 ? -10.973 19.022 -26.877 1.00 59.09  ?  165 HIS   A CE1   1 
ATOM   1248 N NE2   . HIS   A 1 165 ? -11.698 18.617 -27.907 1.00 54.90  ?  165 HIS   A NE2   1 
ATOM   1249 N N     . SER   A 1 166 ? -7.723  20.368 -28.785 1.00 45.57  ?  166 SER   A N     1 
ATOM   1250 C CA    . SER   A 1 166 ? -7.195  21.517 -28.042 1.00 52.54  ?  166 SER   A CA    1 
ATOM   1251 C C     . SER   A 1 166 ? -6.578  21.099 -26.709 1.00 56.91  ?  166 SER   A C     1 
ATOM   1252 O O     . SER   A 1 166 ? -5.664  21.770 -26.196 1.00 56.62  ?  166 SER   A O     1 
ATOM   1253 C CB    . SER   A 1 166 ? -8.295  22.543 -27.801 1.00 48.35  ?  166 SER   A CB    1 
ATOM   1254 O OG    . SER   A 1 166 ? -9.354  21.959 -27.074 1.00 54.68  ?  166 SER   A OG    1 
ATOM   1255 N N     . LEU   A 1 167 ? -7.051  19.986 -26.144 1.00 56.38  ?  167 LEU   A N     1 
ATOM   1256 C CA    . LEU   A 1 167 ? -6.434  19.457 -24.937 1.00 61.96  ?  167 LEU   A CA    1 
ATOM   1257 C C     . LEU   A 1 167 ? -4.935  19.314 -25.112 1.00 60.41  ?  167 LEU   A C     1 
ATOM   1258 O O     . LEU   A 1 167 ? -4.160  19.619 -24.201 1.00 63.30  ?  167 LEU   A O     1 
ATOM   1259 C CB    . LEU   A 1 167 ? -7.058  18.113 -24.589 1.00 64.99  ?  167 LEU   A CB    1 
ATOM   1260 C CG    . LEU   A 1 167 ? -6.426  17.438 -23.387 1.00 67.15  ?  167 LEU   A CG    1 
ATOM   1261 C CD1   . LEU   A 1 167 ? -6.707  18.272 -22.155 1.00 65.94  ?  167 LEU   A CD1   1 
ATOM   1262 C CD2   . LEU   A 1 167 ? -7.027  16.054 -23.252 1.00 68.56  ?  167 LEU   A CD2   1 
ATOM   1263 N N     . ASP   A 1 168 ? -4.512  18.877 -26.292 1.00 60.83  ?  168 ASP   A N     1 
ATOM   1264 C CA    . ASP   A 1 168 ? -3.100  18.719 -26.595 1.00 60.04  ?  168 ASP   A CA    1 
ATOM   1265 C C     . ASP   A 1 168 ? -2.462  20.000 -27.109 1.00 58.90  ?  168 ASP   A C     1 
ATOM   1266 O O     . ASP   A 1 168 ? -1.235  20.056 -27.219 1.00 54.17  ?  168 ASP   A O     1 
ATOM   1267 C CB    . ASP   A 1 168 ? -2.917  17.596 -27.620 1.00 59.75  ?  168 ASP   A CB    1 
ATOM   1268 C CG    . ASP   A 1 168 ? -3.557  16.290 -27.172 1.00 66.70  ?  168 ASP   A CG    1 
ATOM   1269 O OD1   . ASP   A 1 168 ? -3.042  15.687 -26.206 1.00 65.72  ?  168 ASP   A OD1   1 
ATOM   1270 O OD2   . ASP   A 1 168 ? -4.582  15.882 -27.773 1.00 66.64  ?  168 ASP   A OD2   1 
ATOM   1271 N N     . TYR   A 1 169 ? -3.250  21.021 -27.437 1.00 58.83  ?  169 TYR   A N     1 
ATOM   1272 C CA    . TYR   A 1 169 ? -2.657  22.280 -27.855 1.00 52.16  ?  169 TYR   A CA    1 
ATOM   1273 C C     . TYR   A 1 169 ? -2.067  22.987 -26.647 1.00 55.06  ?  169 TYR   A C     1 
ATOM   1274 O O     . TYR   A 1 169 ? -2.634  22.968 -25.548 1.00 64.83  ?  169 TYR   A O     1 
ATOM   1275 C CB    . TYR   A 1 169 ? -3.685  23.165 -28.555 1.00 51.28  ?  169 TYR   A CB    1 
ATOM   1276 C CG    . TYR   A 1 169 ? -3.107  24.449 -29.126 1.00 53.74  ?  169 TYR   A CG    1 
ATOM   1277 C CD1   . TYR   A 1 169 ? -2.964  25.583 -28.333 1.00 51.51  ?  169 TYR   A CD1   1 
ATOM   1278 C CD2   . TYR   A 1 169 ? -2.710  24.532 -30.466 1.00 55.54  ?  169 TYR   A CD2   1 
ATOM   1279 C CE1   . TYR   A 1 169 ? -2.439  26.754 -28.839 1.00 48.70  ?  169 TYR   A CE1   1 
ATOM   1280 C CE2   . TYR   A 1 169 ? -2.178  25.712 -30.993 1.00 48.29  ?  169 TYR   A CE2   1 
ATOM   1281 C CZ    . TYR   A 1 169 ? -2.056  26.817 -30.172 1.00 50.20  ?  169 TYR   A CZ    1 
ATOM   1282 O OH    . TYR   A 1 169 ? -1.565  27.993 -30.672 1.00 43.05  ?  169 TYR   A OH    1 
ATOM   1283 N N     . ARG   A 1 170 ? -0.933  23.633 -26.872 1.00 57.83  ?  170 ARG   A N     1 
ATOM   1284 C CA    . ARG   A 1 170 ? -0.031  24.056 -25.813 1.00 55.47  ?  170 ARG   A CA    1 
ATOM   1285 C C     . ARG   A 1 170 ? 0.500   25.463 -26.100 1.00 56.65  ?  170 ARG   A C     1 
ATOM   1286 O O     . ARG   A 1 170 ? 0.321   26.368 -25.281 1.00 58.64  ?  170 ARG   A O     1 
ATOM   1287 C CB    . ARG   A 1 170 ? 1.090   23.019 -25.692 1.00 50.95  ?  170 ARG   A CB    1 
ATOM   1288 C CG    . ARG   A 1 170 ? 2.099   23.219 -24.598 1.00 59.12  ?  170 ARG   A CG    1 
ATOM   1289 C CD    . ARG   A 1 170 ? 3.438   22.580 -24.994 1.00 64.91  ?  170 ARG   A CD    1 
ATOM   1290 N NE    . ARG   A 1 170 ? 4.427   23.606 -25.326 1.00 74.60  ?  170 ARG   A NE    1 
ATOM   1291 C CZ    . ARG   A 1 170 ? 5.551   23.400 -26.013 1.00 77.85  ?  170 ARG   A CZ    1 
ATOM   1292 N NH1   . ARG   A 1 170 ? 6.375   24.418 -26.248 1.00 77.43  ?  170 ARG   A NH1   1 
ATOM   1293 N NH2   . ARG   A 1 170 ? 5.844   22.192 -26.486 1.00 74.38  ?  170 ARG   A NH2   1 
ATOM   1294 N N     . ASP   A 1 171 ? 1.132   25.672 -27.258 1.00 55.55  ?  171 ASP   A N     1 
ATOM   1295 C CA    . ASP   A 1 171 ? 1.605   26.995 -27.645 1.00 51.88  ?  171 ASP   A CA    1 
ATOM   1296 C C     . ASP   A 1 171 ? 1.633   27.112 -29.166 1.00 53.06  ?  171 ASP   A C     1 
ATOM   1297 O O     . ASP   A 1 171 ? 1.919   26.147 -29.877 1.00 49.93  ?  171 ASP   A O     1 
ATOM   1298 C CB    . ASP   A 1 171 ? 2.998   27.297 -27.063 1.00 55.61  ?  171 ASP   A CB    1 
ATOM   1299 C CG    . ASP   A 1 171 ? 3.448   28.753 -27.298 1.00 57.90  ?  171 ASP   A CG    1 
ATOM   1300 O OD1   . ASP   A 1 171 ? 3.560   29.195 -28.459 1.00 55.66  ?  171 ASP   A OD1   1 
ATOM   1301 O OD2   . ASP   A 1 171 ? 3.699   29.472 -26.311 1.00 69.18  ?  171 ASP   A OD2   1 
ATOM   1302 N N     . GLY   A 1 172 ? 1.355   28.324 -29.653 1.00 49.28  ?  172 GLY   A N     1 
ATOM   1303 C CA    . GLY   A 1 172 ? 1.417   28.577 -31.078 1.00 49.63  ?  172 GLY   A CA    1 
ATOM   1304 C C     . GLY   A 1 172 ? 2.786   28.333 -31.670 1.00 52.54  ?  172 GLY   A C     1 
ATOM   1305 O O     . GLY   A 1 172 ? 2.905   27.953 -32.837 1.00 52.56  ?  172 GLY   A O     1 
ATOM   1306 N N     . GLY   A 1 173 ? 3.836   28.540 -30.883 1.00 48.88  ?  173 GLY   A N     1 
ATOM   1307 C CA    . GLY   A 1 173 ? 5.166   28.314 -31.405 1.00 48.58  ?  173 GLY   A CA    1 
ATOM   1308 C C     . GLY   A 1 173 ? 5.466   26.869 -31.735 1.00 50.03  ?  173 GLY   A C     1 
ATOM   1309 O O     . GLY   A 1 173 ? 6.431   26.601 -32.453 1.00 57.95  ?  173 GLY   A O     1 
ATOM   1310 N N     . ASP   A 1 174 ? 4.662   25.928 -31.229 1.00 54.56  ?  174 ASP   A N     1 
ATOM   1311 C CA    . ASP   A 1 174 ? 4.819   24.518 -31.575 1.00 49.18  ?  174 ASP   A CA    1 
ATOM   1312 C C     . ASP   A 1 174 ? 4.432   24.229 -33.005 1.00 52.36  ?  174 ASP   A C     1 
ATOM   1313 O O     . ASP   A 1 174 ? 4.459   23.064 -33.412 1.00 51.54  ?  174 ASP   A O     1 
ATOM   1314 C CB    . ASP   A 1 174 ? 3.976   23.643 -30.653 1.00 53.77  ?  174 ASP   A CB    1 
ATOM   1315 C CG    . ASP   A 1 174 ? 4.466   23.657 -29.227 1.00 61.84  ?  174 ASP   A CG    1 
ATOM   1316 O OD1   . ASP   A 1 174 ? 5.618   24.092 -29.000 1.00 60.98  ?  174 ASP   A OD1   1 
ATOM   1317 O OD2   . ASP   A 1 174 ? 3.686   23.250 -28.336 1.00 62.19  ?  174 ASP   A OD2   1 
ATOM   1318 N N     . PHE   A 1 175 ? 4.040   25.260 -33.758 1.00 53.23  ?  175 PHE   A N     1 
ATOM   1319 C CA    . PHE   A 1 175 ? 3.605   25.111 -35.139 1.00 51.84  ?  175 PHE   A CA    1 
ATOM   1320 C C     . PHE   A 1 175 ? 4.189   26.202 -36.011 1.00 51.96  ?  175 PHE   A C     1 
ATOM   1321 O O     . PHE   A 1 175 ? 3.640   26.477 -37.082 1.00 51.61  ?  175 PHE   A O     1 
ATOM   1322 C CB    . PHE   A 1 175 ? 2.081   25.159 -35.266 1.00 53.73  ?  175 PHE   A CB    1 
ATOM   1323 C CG    . PHE   A 1 175 ? 1.376   24.133 -34.440 1.00 55.84  ?  175 PHE   A CG    1 
ATOM   1324 C CD1   . PHE   A 1 175 ? 1.244   24.303 -33.063 1.00 50.30  ?  175 PHE   A CD1   1 
ATOM   1325 C CD2   . PHE   A 1 175 ? 0.848   22.996 -35.034 1.00 46.95  ?  175 PHE   A CD2   1 
ATOM   1326 C CE1   . PHE   A 1 175 ? 0.604   23.364 -32.306 1.00 49.72  ?  175 PHE   A CE1   1 
ATOM   1327 C CE2   . PHE   A 1 175 ? 0.209   22.045 -34.280 1.00 45.57  ?  175 PHE   A CE2   1 
ATOM   1328 C CZ    . PHE   A 1 175 ? 0.081   22.225 -32.914 1.00 54.64  ?  175 PHE   A CZ    1 
ATOM   1329 N N     . ALA   A 1 176 ? 5.252   26.861 -35.556 1.00 54.69  ?  176 ALA   A N     1 
ATOM   1330 C CA    . ALA   A 1 176 ? 5.907   27.872 -36.375 1.00 53.34  ?  176 ALA   A CA    1 
ATOM   1331 C C     . ALA   A 1 176 ? 6.185   27.313 -37.765 1.00 63.80  ?  176 ALA   A C     1 
ATOM   1332 O O     . ALA   A 1 176 ? 6.644   26.173 -37.913 1.00 66.84  ?  176 ALA   A O     1 
ATOM   1333 C CB    . ALA   A 1 176 ? 7.203   28.320 -35.711 1.00 43.75  ?  176 ALA   A CB    1 
ATOM   1334 N N     . GLY   A 1 177 ? 5.848   28.095 -38.792 1.00 56.39  ?  177 GLY   A N     1 
ATOM   1335 C CA    . GLY   A 1 177 ? 6.098   27.684 -40.159 1.00 60.08  ?  177 GLY   A CA    1 
ATOM   1336 C C     . GLY   A 1 177 ? 5.164   26.632 -40.733 1.00 59.96  ?  177 GLY   A C     1 
ATOM   1337 O O     . GLY   A 1 177 ? 5.171   26.430 -41.958 1.00 69.21  ?  177 GLY   A O     1 
ATOM   1338 N N     . ARG   A 1 178 ? 4.350   25.967 -39.915 1.00 57.66  ?  178 ARG   A N     1 
ATOM   1339 C CA    . ARG   A 1 178 ? 3.441   24.962 -40.449 1.00 58.54  ?  178 ARG   A CA    1 
ATOM   1340 C C     . ARG   A 1 178 ? 2.145   25.598 -40.942 1.00 54.81  ?  178 ARG   A C     1 
ATOM   1341 O O     . ARG   A 1 178 ? 1.916   26.810 -40.849 1.00 57.25  ?  178 ARG   A O     1 
ATOM   1342 C CB    . ARG   A 1 178 ? 3.117   23.885 -39.415 1.00 58.48  ?  178 ARG   A CB    1 
ATOM   1343 C CG    . ARG   A 1 178 ? 4.132   23.688 -38.317 1.00 63.26  ?  178 ARG   A CG    1 
ATOM   1344 C CD    . ARG   A 1 178 ? 5.505   23.303 -38.833 1.00 71.43  ?  178 ARG   A CD    1 
ATOM   1345 N NE    . ARG   A 1 178 ? 5.621   21.894 -39.198 1.00 76.02  ?  178 ARG   A NE    1 
ATOM   1346 C CZ    . ARG   A 1 178 ? 6.760   21.329 -39.584 1.00 80.61  ?  178 ARG   A CZ    1 
ATOM   1347 N NH1   . ARG   A 1 178 ? 7.871   22.058 -39.641 1.00 74.51  ?  178 ARG   A NH1   1 
ATOM   1348 N NH2   . ARG   A 1 178 ? 6.793   20.040 -39.911 1.00 88.76  ?  178 ARG   A NH2   1 
ATOM   1349 N N     . ARG   A 1 179 ? 1.279   24.751 -41.477 1.00 53.81  ?  179 ARG   A N     1 
ATOM   1350 C CA    . ARG   A 1 179 ? -0.030  25.154 -41.963 1.00 54.49  ?  179 ARG   A CA    1 
ATOM   1351 C C     . ARG   A 1 179 ? -1.049  24.389 -41.133 1.00 55.63  ?  179 ARG   A C     1 
ATOM   1352 O O     . ARG   A 1 179 ? -0.999  23.157 -41.081 1.00 54.43  ?  179 ARG   A O     1 
ATOM   1353 C CB    . ARG   A 1 179 ? -0.151  24.859 -43.460 1.00 56.93  ?  179 ARG   A CB    1 
ATOM   1354 C CG    . ARG   A 1 179 ? 0.822   25.692 -44.316 1.00 51.72  ?  179 ARG   A CG    1 
ATOM   1355 C CD    . ARG   A 1 179 ? 1.041   25.080 -45.700 1.00 64.93  ?  179 ARG   A CD    1 
ATOM   1356 N NE    . ARG   A 1 179 ? 0.925   26.112 -46.734 1.00 71.44  ?  179 ARG   A NE    1 
ATOM   1357 C CZ    . ARG   A 1 179 ? -0.227  26.656 -47.133 1.00 70.54  ?  179 ARG   A CZ    1 
ATOM   1358 N NH1   . ARG   A 1 179 ? -1.397  26.261 -46.609 1.00 71.86  ?  179 ARG   A NH1   1 
ATOM   1359 N NH2   . ARG   A 1 179 ? -0.212  27.604 -48.059 1.00 69.29  ?  179 ARG   A NH2   1 
ATOM   1360 N N     . VAL   A 1 180 ? -1.926  25.112 -40.426 1.00 52.29  ?  180 VAL   A N     1 
ATOM   1361 C CA    . VAL   A 1 180 ? -2.790  24.504 -39.415 1.00 48.45  ?  180 VAL   A CA    1 
ATOM   1362 C C     . VAL   A 1 180 ? -4.244  24.904 -39.635 1.00 45.44  ?  180 VAL   A C     1 
ATOM   1363 O O     . VAL   A 1 180 ? -4.551  26.078 -39.868 1.00 47.41  ?  180 VAL   A O     1 
ATOM   1364 C CB    . VAL   A 1 180 ? -2.349  24.882 -37.981 1.00 50.07  ?  180 VAL   A CB    1 
ATOM   1365 C CG1   . VAL   A 1 180 ? -3.041  23.984 -36.963 1.00 46.08  ?  180 VAL   A CG1   1 
ATOM   1366 C CG2   . VAL   A 1 180 ? -0.834  24.770 -37.840 1.00 45.45  ?  180 VAL   A CG2   1 
ATOM   1367 N N     . VAL   A 1 181 ? -5.146  23.931 -39.514 1.00 47.72  ?  181 VAL   A N     1 
ATOM   1368 C CA    . VAL   A 1 181 ? -6.585  24.183 -39.471 1.00 47.93  ?  181 VAL   A CA    1 
ATOM   1369 C C     . VAL   A 1 181 ? -7.057  24.055 -38.029 1.00 54.01  ?  181 VAL   A C     1 
ATOM   1370 O O     . VAL   A 1 181 ? -6.701  23.090 -37.330 1.00 52.91  ?  181 VAL   A O     1 
ATOM   1371 C CB    . VAL   A 1 181 ? -7.355  23.203 -40.371 1.00 45.79  ?  181 VAL   A CB    1 
ATOM   1372 C CG1   . VAL   A 1 181 ? -8.859  23.541 -40.376 1.00 43.98  ?  181 VAL   A CG1   1 
ATOM   1373 C CG2   . VAL   A 1 181 ? -6.756  23.187 -41.763 1.00 44.68  ?  181 VAL   A CG2   1 
ATOM   1374 N N     . VAL   A 1 182 ? -7.860  25.027 -37.584 1.00 44.79  ?  182 VAL   A N     1 
ATOM   1375 C CA    . VAL   A 1 182 ? -8.545  24.983 -36.296 1.00 46.45  ?  182 VAL   A CA    1 
ATOM   1376 C C     . VAL   A 1 182 ? -10.024 24.746 -36.555 1.00 51.77  ?  182 VAL   A C     1 
ATOM   1377 O O     . VAL   A 1 182 ? -10.650 25.471 -37.344 1.00 51.58  ?  182 VAL   A O     1 
ATOM   1378 C CB    . VAL   A 1 182 ? -8.346  26.280 -35.495 1.00 49.69  ?  182 VAL   A CB    1 
ATOM   1379 C CG1   . VAL   A 1 182 ? -9.049  26.181 -34.152 1.00 43.45  ?  182 VAL   A CG1   1 
ATOM   1380 C CG2   . VAL   A 1 182 ? -6.857  26.599 -35.345 1.00 45.77  ?  182 VAL   A CG2   1 
ATOM   1381 N N     . VAL   A 1 183 ? -10.588 23.746 -35.889 1.00 53.96  ?  183 VAL   A N     1 
ATOM   1382 C CA    . VAL   A 1 183 ? -11.982 23.374 -36.089 1.00 53.58  ?  183 VAL   A CA    1 
ATOM   1383 C C     . VAL   A 1 183 ? -12.762 23.784 -34.851 1.00 54.22  ?  183 VAL   A C     1 
ATOM   1384 O O     . VAL   A 1 183 ? -12.459 23.341 -33.735 1.00 50.87  ?  183 VAL   A O     1 
ATOM   1385 C CB    . VAL   A 1 183 ? -12.143 21.874 -36.368 1.00 52.02  ?  183 VAL   A CB    1 
ATOM   1386 C CG1   . VAL   A 1 183 ? -13.608 21.506 -36.355 1.00 44.97  ?  183 VAL   A CG1   1 
ATOM   1387 C CG2   . VAL   A 1 183 ? -11.506 21.516 -37.696 1.00 51.58  ?  183 VAL   A CG2   1 
ATOM   1388 N N     . GLY   A 1 184 ? -13.768 24.625 -35.060 1.00 58.75  ?  184 GLY   A N     1 
ATOM   1389 C CA    . GLY   A 1 184 ? -14.652 25.070 -34.009 1.00 52.00  ?  184 GLY   A CA    1 
ATOM   1390 C C     . GLY   A 1 184 ? -14.780 26.573 -34.020 1.00 55.60  ?  184 GLY   A C     1 
ATOM   1391 O O     . GLY   A 1 184 ? -13.948 27.267 -34.617 1.00 54.95  ?  184 GLY   A O     1 
ATOM   1392 N N     . LEU   A 1 185 ? -15.810 27.088 -33.359 1.00 56.42  ?  185 LEU   A N     1 
ATOM   1393 C CA    . LEU   A 1 185 ? -15.955 28.519 -33.131 1.00 59.46  ?  185 LEU   A CA    1 
ATOM   1394 C C     . LEU   A 1 185 ? -16.196 28.797 -31.656 1.00 56.90  ?  185 LEU   A C     1 
ATOM   1395 O O     . LEU   A 1 185 ? -16.934 29.714 -31.288 1.00 56.01  ?  185 LEU   A O     1 
ATOM   1396 C CB    . LEU   A 1 185 ? -17.074 29.104 -33.984 1.00 56.15  ?  185 LEU   A CB    1 
ATOM   1397 C CG    . LEU   A 1 185 ? -16.854 30.581 -34.300 1.00 58.04  ?  185 LEU   A CG    1 
ATOM   1398 C CD1   . LEU   A 1 185 ? -15.438 30.768 -34.843 1.00 53.19  ?  185 LEU   A CD1   1 
ATOM   1399 C CD2   . LEU   A 1 185 ? -17.922 31.118 -35.266 1.00 63.14  ?  185 LEU   A CD2   1 
ATOM   1400 N N     . GLY   A 1 186 ? -15.593 27.980 -30.789 1.00 56.13  ?  186 GLY   A N     1 
ATOM   1401 C CA    . GLY   A 1 186 ? -15.708 28.157 -29.360 1.00 47.41  ?  186 GLY   A CA    1 
ATOM   1402 C C     . GLY   A 1 186 ? -14.657 29.109 -28.831 1.00 53.00  ?  186 GLY   A C     1 
ATOM   1403 O O     . GLY   A 1 186 ? -13.887 29.720 -29.573 1.00 48.12  ?  186 GLY   A O     1 
ATOM   1404 N N     . ALA   A 1 187 ? -14.646 29.256 -27.505 1.00 56.43  ?  187 ALA   A N     1 
ATOM   1405 C CA    . ALA   A 1 187 ? -13.661 30.138 -26.890 1.00 46.86  ?  187 ALA   A CA    1 
ATOM   1406 C C     . ALA   A 1 187 ? -12.253 29.591 -27.091 1.00 50.55  ?  187 ALA   A C     1 
ATOM   1407 O O     . ALA   A 1 187 ? -11.305 30.356 -27.305 1.00 46.05  ?  187 ALA   A O     1 
ATOM   1408 C CB    . ALA   A 1 187 ? -13.970 30.325 -25.409 1.00 45.15  ?  187 ALA   A CB    1 
ATOM   1409 N N     . SER   A 1 188 ? -12.104 28.265 -27.041 1.00 50.38  ?  188 SER   A N     1 
ATOM   1410 C CA    . SER   A 1 188 ? -10.814 27.655 -27.340 1.00 50.92  ?  188 SER   A CA    1 
ATOM   1411 C C     . SER   A 1 188 ? -10.409 27.892 -28.793 1.00 55.22  ?  188 SER   A C     1 
ATOM   1412 O O     . SER   A 1 188 ? -9.226  28.120 -29.083 1.00 55.89  ?  188 SER   A O     1 
ATOM   1413 C CB    . SER   A 1 188 ? -10.871 26.161 -27.056 1.00 49.97  ?  188 SER   A CB    1 
ATOM   1414 O OG    . SER   A 1 188 ? -10.995 25.915 -25.671 1.00 65.16  ?  188 SER   A OG    1 
ATOM   1415 N N     . ALA   A 1 189 ? -11.382 27.887 -29.718 1.00 49.85  ?  189 ALA   A N     1 
ATOM   1416 C CA    . ALA   A 1 189 ? -11.068 27.965 -31.143 1.00 50.18  ?  189 ALA   A CA    1 
ATOM   1417 C C     . ALA   A 1 189 ? -10.624 29.366 -31.561 1.00 48.69  ?  189 ALA   A C     1 
ATOM   1418 O O     . ALA   A 1 189 ? -9.635  29.516 -32.286 1.00 46.59  ?  189 ALA   A O     1 
ATOM   1419 C CB    . ALA   A 1 189 ? -12.266 27.515 -31.981 1.00 48.29  ?  189 ALA   A CB    1 
ATOM   1420 N N     . VAL   A 1 190 ? -11.333 30.409 -31.138 1.00 47.10  ?  190 VAL   A N     1 
ATOM   1421 C CA    . VAL   A 1 190 ? -10.886 31.731 -31.554 1.00 47.60  ?  190 VAL   A CA    1 
ATOM   1422 C C     . VAL   A 1 190 ? -9.549  32.065 -30.898 1.00 45.94  ?  190 VAL   A C     1 
ATOM   1423 O O     . VAL   A 1 190 ? -8.658  32.618 -31.547 1.00 46.83  ?  190 VAL   A O     1 
ATOM   1424 C CB    . VAL   A 1 190 ? -11.962 32.804 -31.289 1.00 46.62  ?  190 VAL   A CB    1 
ATOM   1425 C CG1   . VAL   A 1 190 ? -13.188 32.505 -32.117 1.00 44.07  ?  190 VAL   A CG1   1 
ATOM   1426 C CG2   . VAL   A 1 190 ? -12.318 32.926 -29.788 1.00 42.60  ?  190 VAL   A CG2   1 
ATOM   1427 N N     . ASP   A 1 191 ? -9.359  31.685 -29.629 1.00 43.38  ?  191 ASP   A N     1 
ATOM   1428 C CA    . ASP   A 1 191 ? -8.087  31.946 -28.951 1.00 41.53  ?  191 ASP   A CA    1 
ATOM   1429 C C     . ASP   A 1 191 ? -6.928  31.214 -29.638 1.00 48.90  ?  191 ASP   A C     1 
ATOM   1430 O O     . ASP   A 1 191 ? -5.859  31.796 -29.897 1.00 43.81  ?  191 ASP   A O     1 
ATOM   1431 C CB    . ASP   A 1 191 ? -8.170  31.510 -27.492 1.00 49.63  ?  191 ASP   A CB    1 
ATOM   1432 C CG    . ASP   A 1 191 ? -8.851  32.533 -26.574 1.00 52.74  ?  191 ASP   A CG    1 
ATOM   1433 O OD1   . ASP   A 1 191 ? -9.386  33.581 -27.057 1.00 46.77  ?  191 ASP   A OD1   1 
ATOM   1434 O OD2   . ASP   A 1 191 ? -8.833  32.251 -25.338 1.00 52.94  ?  191 ASP   A OD2   1 
ATOM   1435 N N     . ILE   A 1 192 ? -7.129  29.928 -29.945 1.00 50.39  ?  192 ILE   A N     1 
ATOM   1436 C CA    . ILE   A 1 192 ? -6.072  29.138 -30.568 1.00 48.61  ?  192 ILE   A CA    1 
ATOM   1437 C C     . ILE   A 1 192 ? -5.792  29.631 -31.988 1.00 44.96  ?  192 ILE   A C     1 
ATOM   1438 O O     . ILE   A 1 192 ? -4.629  29.765 -32.386 1.00 46.38  ?  192 ILE   A O     1 
ATOM   1439 C CB    . ILE   A 1 192 ? -6.438  27.643 -30.522 1.00 48.77  ?  192 ILE   A CB    1 
ATOM   1440 C CG1   . ILE   A 1 192 ? -6.005  27.037 -29.186 1.00 47.69  ?  192 ILE   A CG1   1 
ATOM   1441 C CG2   . ILE   A 1 192 ? -5.802  26.888 -31.661 1.00 49.75  ?  192 ILE   A CG2   1 
ATOM   1442 C CD1   . ILE   A 1 192 ? -6.955  25.930 -28.687 1.00 49.88  ?  192 ILE   A CD1   1 
ATOM   1443 N N     . ALA   A 1 193 ? -6.842  29.931 -32.765 1.00 43.56  ?  193 ALA   A N     1 
ATOM   1444 C CA    . ALA   A 1 193 ? -6.645  30.477 -34.112 1.00 40.90  ?  193 ALA   A CA    1 
ATOM   1445 C C     . ALA   A 1 193 ? -5.861  31.786 -34.067 1.00 41.86  ?  193 ALA   A C     1 
ATOM   1446 O O     . ALA   A 1 193 ? -4.885  31.964 -34.804 1.00 36.72  ?  193 ALA   A O     1 
ATOM   1447 C CB    . ALA   A 1 193 ? -7.991  30.685 -34.804 1.00 37.99  ?  193 ALA   A CB    1 
ATOM   1448 N N     . ALA   A 1 194 ? -6.261  32.712 -33.189 1.00 43.71  ?  194 ALA   A N     1 
ATOM   1449 C CA    . ALA   A 1 194 ? -5.516  33.962 -33.060 1.00 42.38  ?  194 ALA   A CA    1 
ATOM   1450 C C     . ALA   A 1 194 ? -4.075  33.700 -32.664 1.00 41.74  ?  194 ALA   A C     1 
ATOM   1451 O O     . ALA   A 1 194 ? -3.161  34.331 -33.205 1.00 43.56  ?  194 ALA   A O     1 
ATOM   1452 C CB    . ALA   A 1 194 ? -6.180  34.900 -32.055 1.00 36.65  ?  194 ALA   A CB    1 
ATOM   1453 N N     . ASP   A 1 195 ? -3.839  32.759 -31.743 1.00 38.40  ?  195 ASP   A N     1 
ATOM   1454 C CA    . ASP   A 1 195 ? -2.457  32.452 -31.395 1.00 35.75  ?  195 ASP   A CA    1 
ATOM   1455 C C     . ASP   A 1 195 ? -1.692  31.904 -32.605 1.00 42.55  ?  195 ASP   A C     1 
ATOM   1456 O O     . ASP   A 1 195 ? -0.625  32.421 -32.962 1.00 43.62  ?  195 ASP   A O     1 
ATOM   1457 C CB    . ASP   A 1 195 ? -2.397  31.474 -30.227 1.00 37.76  ?  195 ASP   A CB    1 
ATOM   1458 C CG    . ASP   A 1 195 ? -0.971  31.266 -29.720 1.00 43.73  ?  195 ASP   A CG    1 
ATOM   1459 O OD1   . ASP   A 1 195 ? -0.171  32.235 -29.763 1.00 44.39  ?  195 ASP   A OD1   1 
ATOM   1460 O OD2   . ASP   A 1 195 ? -0.642  30.136 -29.293 1.00 41.17  ?  195 ASP   A OD2   1 
ATOM   1461 N N     . LEU   A 1 196 ? -2.225  30.855 -33.253 1.00 41.47  ?  196 LEU   A N     1 
ATOM   1462 C CA    . LEU   A 1 196 ? -1.554  30.276 -34.419 1.00 42.57  ?  196 LEU   A CA    1 
ATOM   1463 C C     . LEU   A 1 196 ? -1.273  31.334 -35.480 1.00 43.47  ?  196 LEU   A C     1 
ATOM   1464 O O     . LEU   A 1 196 ? -0.173  31.383 -36.045 1.00 40.31  ?  196 LEU   A O     1 
ATOM   1465 C CB    . LEU   A 1 196 ? -2.384  29.135 -35.000 1.00 36.91  ?  196 LEU   A CB    1 
ATOM   1466 C CG    . LEU   A 1 196 ? -2.175  27.833 -34.216 1.00 41.12  ?  196 LEU   A CG    1 
ATOM   1467 C CD1   . LEU   A 1 196 ? -3.194  26.801 -34.611 1.00 39.45  ?  196 LEU   A CD1   1 
ATOM   1468 C CD2   . LEU   A 1 196 ? -0.760  27.279 -34.345 1.00 42.90  ?  196 LEU   A CD2   1 
ATOM   1469 N N     . SER   A 1 197 ? -2.228  32.238 -35.690 1.00 41.02  ?  197 SER   A N     1 
ATOM   1470 C CA    . SER   A 1 197 ? -2.093  33.297 -36.676 1.00 43.67  ?  197 SER   A CA    1 
ATOM   1471 C C     . SER   A 1 197 ? -0.826  34.138 -36.515 1.00 48.53  ?  197 SER   A C     1 
ATOM   1472 O O     . SER   A 1 197 ? -0.459  34.870 -37.445 1.00 51.73  ?  197 SER   A O     1 
ATOM   1473 C CB    . SER   A 1 197 ? -3.308  34.218 -36.595 1.00 47.60  ?  197 SER   A CB    1 
ATOM   1474 O OG    . SER   A 1 197 ? -3.045  35.303 -35.730 1.00 48.54  ?  197 SER   A OG    1 
ATOM   1475 N N     . ARG   A 1 198 ? -0.139  34.068 -35.378 1.00 45.52  ?  198 ARG   A N     1 
ATOM   1476 C CA    . ARG   A 1 198 ? 1.132   34.773 -35.243 1.00 48.94  ?  198 ARG   A CA    1 
ATOM   1477 C C     . ARG   A 1 198 ? 2.332   33.832 -35.220 1.00 49.14  ?  198 ARG   A C     1 
ATOM   1478 O O     . ARG   A 1 198 ? 3.456   34.278 -34.948 1.00 43.93  ?  198 ARG   A O     1 
ATOM   1479 C CB    . ARG   A 1 198 ? 1.116   35.670 -33.999 1.00 43.11  ?  198 ARG   A CB    1 
ATOM   1480 C CG    . ARG   A 1 198 ? 0.341   36.954 -34.240 1.00 50.63  ?  198 ARG   A CG    1 
ATOM   1481 C CD    . ARG   A 1 198 ? 0.007   37.717 -32.975 1.00 56.43  ?  198 ARG   A CD    1 
ATOM   1482 N NE    . ARG   A 1 198 ? -0.663  38.985 -33.293 1.00 62.44  ?  198 ARG   A NE    1 
ATOM   1483 C CZ    . ARG   A 1 198 ? -1.935  39.261 -33.010 1.00 59.32  ?  198 ARG   A CZ    1 
ATOM   1484 N NH1   . ARG   A 1 198 ? -2.696  38.365 -32.386 1.00 56.75  ?  198 ARG   A NH1   1 
ATOM   1485 N NH2   . ARG   A 1 198 ? -2.444  40.440 -33.342 1.00 57.95  ?  198 ARG   A NH2   1 
ATOM   1486 N N     . HIS   A 1 199 ? 2.128   32.548 -35.518 1.00 49.05  ?  199 HIS   A N     1 
ATOM   1487 C CA    . HIS   A 1 199 ? 3.237   31.605 -35.554 1.00 51.12  ?  199 HIS   A CA    1 
ATOM   1488 C C     . HIS   A 1 199 ? 3.198   30.743 -36.812 1.00 52.85  ?  199 HIS   A C     1 
ATOM   1489 O O     . HIS   A 1 199 ? 4.182   30.682 -37.553 1.00 53.27  ?  199 HIS   A O     1 
ATOM   1490 C CB    . HIS   A 1 199 ? 3.226   30.742 -34.298 1.00 46.50  ?  199 HIS   A CB    1 
ATOM   1491 C CG    . HIS   A 1 199 ? 3.585   31.503 -33.070 1.00 54.06  ?  199 HIS   A CG    1 
ATOM   1492 N ND1   . HIS   A 1 199 ? 2.637   32.056 -32.235 1.00 52.73  ?  199 HIS   A ND1   1 
ATOM   1493 C CD2   . HIS   A 1 199 ? 4.789   31.842 -32.555 1.00 55.90  ?  199 HIS   A CD2   1 
ATOM   1494 C CE1   . HIS   A 1 199 ? 3.244   32.690 -31.250 1.00 53.78  ?  199 HIS   A CE1   1 
ATOM   1495 N NE2   . HIS   A 1 199 ? 4.549   32.575 -31.420 1.00 55.40  ?  199 HIS   A NE2   1 
ATOM   1496 N N     . ALA   A 1 200 ? 2.086   30.057 -37.057 1.00 53.15  ?  200 ALA   A N     1 
ATOM   1497 C CA    . ALA   A 1 200 ? 1.996   29.263 -38.271 1.00 54.55  ?  200 ALA   A CA    1 
ATOM   1498 C C     . ALA   A 1 200 ? 2.189   30.156 -39.478 1.00 56.88  ?  200 ALA   A C     1 
ATOM   1499 O O     . ALA   A 1 200 ? 1.881   31.353 -39.451 1.00 53.67  ?  200 ALA   A O     1 
ATOM   1500 C CB    . ALA   A 1 200 ? 0.646   28.557 -38.383 1.00 51.21  ?  200 ALA   A CB    1 
ATOM   1501 N N     . GLU   A 1 201 ? 2.727   29.562 -40.541 1.00 55.74  ?  201 GLU   A N     1 
ATOM   1502 C CA    . GLU   A 1 201 ? 2.697   30.238 -41.825 1.00 57.11  ?  201 GLU   A CA    1 
ATOM   1503 C C     . GLU   A 1 201 ? 1.263   30.577 -42.205 1.00 52.98  ?  201 GLU   A C     1 
ATOM   1504 O O     . GLU   A 1 201 ? 0.966   31.713 -42.589 1.00 56.73  ?  201 GLU   A O     1 
ATOM   1505 C CB    . GLU   A 1 201 ? 3.366   29.367 -42.882 1.00 62.28  ?  201 GLU   A CB    1 
ATOM   1506 C CG    . GLU   A 1 201 ? 3.250   29.882 -44.306 1.00 56.44  ?  201 GLU   A CG    1 
ATOM   1507 C CD    . GLU   A 1 201 ? 3.769   28.856 -45.286 1.00 73.57  ?  201 GLU   A CD    1 
ATOM   1508 O OE1   . GLU   A 1 201 ? 4.766   28.174 -44.942 1.00 72.22  ?  201 GLU   A OE1   1 
ATOM   1509 O OE2   . GLU   A 1 201 ? 3.161   28.700 -46.373 1.00 82.62  ?  201 GLU   A OE2   1 
ATOM   1510 N N     . ARG   A 1 202 ? 0.346   29.626 -42.038 1.00 48.70  ?  202 ARG   A N     1 
ATOM   1511 C CA    . ARG   A 1 202 ? -1.038  29.837 -42.429 1.00 49.28  ?  202 ARG   A CA    1 
ATOM   1512 C C     . ARG   A 1 202 ? -1.990  29.198 -41.423 1.00 53.22  ?  202 ARG   A C     1 
ATOM   1513 O O     . ARG   A 1 202 ? -1.746  28.078 -40.954 1.00 49.84  ?  202 ARG   A O     1 
ATOM   1514 C CB    . ARG   A 1 202 ? -1.273  29.268 -43.821 1.00 52.91  ?  202 ARG   A CB    1 
ATOM   1515 C CG    . ARG   A 1 202 ? -2.549  29.710 -44.446 1.00 54.10  ?  202 ARG   A CG    1 
ATOM   1516 C CD    . ARG   A 1 202 ? -2.284  30.750 -45.508 1.00 62.18  ?  202 ARG   A CD    1 
ATOM   1517 N NE    . ARG   A 1 202 ? -3.534  31.359 -45.955 1.00 62.06  ?  202 ARG   A NE    1 
ATOM   1518 C CZ    . ARG   A 1 202 ? -4.442  30.711 -46.668 1.00 53.45  ?  202 ARG   A CZ    1 
ATOM   1519 N NH1   . ARG   A 1 202 ? -4.223  29.449 -47.010 1.00 59.44  ?  202 ARG   A NH1   1 
ATOM   1520 N NH2   . ARG   A 1 202 ? -5.553  31.320 -47.033 1.00 52.09  ?  202 ARG   A NH2   1 
ATOM   1521 N N     . THR   A 1 203 ? -3.083  29.914 -41.106 1.00 49.75  ?  203 THR   A N     1 
ATOM   1522 C CA    . THR   A 1 203 ? -4.059  29.502 -40.094 1.00 42.12  ?  203 THR   A CA    1 
ATOM   1523 C C     . THR   A 1 203 ? -5.476  29.572 -40.663 1.00 49.33  ?  203 THR   A C     1 
ATOM   1524 O O     . THR   A 1 203 ? -5.967  30.660 -41.009 1.00 45.20  ?  203 THR   A O     1 
ATOM   1525 C CB    . THR   A 1 203 ? -3.954  30.381 -38.848 1.00 41.53  ?  203 THR   A CB    1 
ATOM   1526 O OG1   . THR   A 1 203 ? -2.586  30.483 -38.457 1.00 49.83  ?  203 THR   A OG1   1 
ATOM   1527 C CG2   . THR   A 1 203 ? -4.736  29.803 -37.698 1.00 40.64  ?  203 THR   A CG2   1 
ATOM   1528 N N     . LEU   A 1 204 ? -6.143  28.416 -40.725 1.00 47.23  ?  204 LEU   A N     1 
ATOM   1529 C CA    . LEU   A 1 204 ? -7.497  28.294 -41.251 1.00 48.34  ?  204 LEU   A CA    1 
ATOM   1530 C C     . LEU   A 1 204 ? -8.483  27.982 -40.135 1.00 48.61  ?  204 LEU   A C     1 
ATOM   1531 O O     . LEU   A 1 204 ? -8.219  27.129 -39.280 1.00 50.74  ?  204 LEU   A O     1 
ATOM   1532 C CB    . LEU   A 1 204 ? -7.554  27.207 -42.316 1.00 49.49  ?  204 LEU   A CB    1 
ATOM   1533 C CG    . LEU   A 1 204 ? -6.567  27.635 -43.395 1.00 53.25  ?  204 LEU   A CG    1 
ATOM   1534 C CD1   . LEU   A 1 204 ? -5.452  26.608 -43.609 1.00 46.70  ?  204 LEU   A CD1   1 
ATOM   1535 C CD2   . LEU   A 1 204 ? -7.331  27.948 -44.668 1.00 57.36  ?  204 LEU   A CD2   1 
ATOM   1536 N N     . LEU   A 1 205 ? -9.626  28.661 -40.149 1.00 42.56  ?  205 LEU   A N     1 
ATOM   1537 C CA    . LEU   A 1 205 ? -10.619 28.515 -39.090 1.00 44.87  ?  205 LEU   A CA    1 
ATOM   1538 C C     . LEU   A 1 205 ? -11.860 27.888 -39.714 1.00 48.74  ?  205 LEU   A C     1 
ATOM   1539 O O     . LEU   A 1 205 ? -12.644 28.562 -40.390 1.00 47.62  ?  205 LEU   A O     1 
ATOM   1540 C CB    . LEU   A 1 205 ? -10.919 29.857 -38.412 1.00 44.70  ?  205 LEU   A CB    1 
ATOM   1541 C CG    . LEU   A 1 205 ? -11.888 29.844 -37.201 1.00 47.57  ?  205 LEU   A CG    1 
ATOM   1542 C CD1   . LEU   A 1 205 ? -11.434 28.953 -36.027 1.00 41.68  ?  205 LEU   A CD1   1 
ATOM   1543 C CD2   . LEU   A 1 205 ? -12.155 31.245 -36.715 1.00 39.91  ?  205 LEU   A CD2   1 
ATOM   1544 N N     . SER   A 1 206 ? -12.030 26.591 -39.483 1.00 50.00  ?  206 SER   A N     1 
ATOM   1545 C CA    . SER   A 1 206 ? -13.088 25.804 -40.104 1.00 47.29  ?  206 SER   A CA    1 
ATOM   1546 C C     . SER   A 1 206 ? -14.263 25.737 -39.137 1.00 58.17  ?  206 SER   A C     1 
ATOM   1547 O O     . SER   A 1 206 ? -14.187 25.057 -38.103 1.00 60.10  ?  206 SER   A O     1 
ATOM   1548 C CB    . SER   A 1 206 ? -12.565 24.408 -40.442 1.00 50.16  ?  206 SER   A CB    1 
ATOM   1549 O OG    . SER   A 1 206 ? -13.588 23.430 -40.465 1.00 52.90  ?  206 SER   A OG    1 
ATOM   1550 N N     . VAL   A 1 207 ? -15.348 26.435 -39.464 1.00 56.31  ?  207 VAL   A N     1 
ATOM   1551 C CA    . VAL   A 1 207 ? -16.517 26.477 -38.596 1.00 58.97  ?  207 VAL   A CA    1 
ATOM   1552 C C     . VAL   A 1 207 ? -17.756 26.101 -39.396 1.00 65.56  ?  207 VAL   A C     1 
ATOM   1553 O O     . VAL   A 1 207 ? -17.982 26.625 -40.492 1.00 67.39  ?  207 VAL   A O     1 
ATOM   1554 C CB    . VAL   A 1 207 ? -16.693 27.853 -37.920 1.00 60.46  ?  207 VAL   A CB    1 
ATOM   1555 C CG1   . VAL   A 1 207 ? -16.644 28.961 -38.930 1.00 59.38  ?  207 VAL   A CG1   1 
ATOM   1556 C CG2   . VAL   A 1 207 ? -18.013 27.891 -37.163 1.00 66.77  ?  207 VAL   A CG2   1 
ATOM   1557 N N     . ARG   A 1 208 ? -18.567 25.204 -38.831 1.00 71.72  ?  208 ARG   A N     1 
ATOM   1558 C CA    . ARG   A 1 208 ? -19.732 24.623 -39.488 1.00 72.73  ?  208 ARG   A CA    1 
ATOM   1559 C C     . ARG   A 1 208 ? -21.061 25.088 -38.914 1.00 75.70  ?  208 ARG   A C     1 
ATOM   1560 O O     . ARG   A 1 208 ? -22.050 25.146 -39.649 1.00 78.00  ?  208 ARG   A O     1 
ATOM   1561 C CB    . ARG   A 1 208 ? -19.639 23.094 -39.413 1.00 77.27  ?  208 ARG   A CB    1 
ATOM   1562 C CG    . ARG   A 1 208 ? -20.901 22.325 -39.100 1.00 75.19  ?  208 ARG   A CG    1 
ATOM   1563 C CD    . ARG   A 1 208 ? -20.523 20.952 -38.538 1.00 70.67  ?  208 ARG   A CD    1 
ATOM   1564 N NE    . ARG   A 1 208 ? -21.707 20.219 -38.108 1.00 87.05  ?  208 ARG   A NE    1 
ATOM   1565 C CZ    . ARG   A 1 208 ? -22.055 20.018 -36.839 1.00 98.11  ?  208 ARG   A CZ    1 
ATOM   1566 N NH1   . ARG   A 1 208 ? -23.165 19.343 -36.561 1.00 102.24 ?  208 ARG   A NH1   1 
ATOM   1567 N NH2   . ARG   A 1 208 ? -21.309 20.500 -35.847 1.00 97.68  ?  208 ARG   A NH2   1 
ATOM   1568 N N     . ARG   A 1 209 ? -21.108 25.431 -37.628 1.00 76.71  ?  209 ARG   A N     1 
ATOM   1569 C CA    . ARG   A 1 209 ? -22.250 26.109 -37.025 1.00 77.18  ?  209 ARG   A CA    1 
ATOM   1570 C C     . ARG   A 1 209 ? -21.791 27.481 -36.548 1.00 75.87  ?  209 ARG   A C     1 
ATOM   1571 O O     . ARG   A 1 209 ? -20.901 27.576 -35.693 1.00 72.09  ?  209 ARG   A O     1 
ATOM   1572 C CB    . ARG   A 1 209 ? -22.839 25.301 -35.862 1.00 80.20  ?  209 ARG   A CB    1 
ATOM   1573 C CG    . ARG   A 1 209 ? -23.059 23.808 -36.131 1.00 85.74  ?  209 ARG   A CG    1 
ATOM   1574 C CD    . ARG   A 1 209 ? -24.238 23.255 -35.315 1.00 92.79  ?  209 ARG   A CD    1 
ATOM   1575 N NE    . ARG   A 1 209 ? -24.162 23.652 -33.907 1.00 97.58  ?  209 ARG   A NE    1 
ATOM   1576 C CZ    . ARG   A 1 209 ? -25.102 24.343 -33.264 1.00 96.00  ?  209 ARG   A CZ    1 
ATOM   1577 N NH1   . ARG   A 1 209 ? -26.210 24.712 -33.898 1.00 98.14  ?  209 ARG   A NH1   1 
ATOM   1578 N NH2   . ARG   A 1 209 ? -24.939 24.662 -31.983 1.00 90.00  ?  209 ARG   A NH2   1 
ATOM   1579 N N     . GLY   A 1 210 ? -22.383 28.536 -37.113 1.00 71.51  ?  210 GLY   A N     1 
ATOM   1580 C CA    . GLY   A 1 210 ? -22.111 29.890 -36.668 1.00 68.21  ?  210 GLY   A CA    1 
ATOM   1581 C C     . GLY   A 1 210 ? -22.426 30.143 -35.203 1.00 73.99  ?  210 GLY   A C     1 
ATOM   1582 O O     . GLY   A 1 210 ? -23.488 29.755 -34.698 1.00 68.42  ?  210 GLY   A O     1 
ATOM   1583 N N     . LEU   A 1 211 ? -21.488 30.767 -34.497 1.00 77.68  ?  211 LEU   A N     1 
ATOM   1584 C CA    . LEU   A 1 211 ? -21.732 31.298 -33.165 1.00 74.81  ?  211 LEU   A CA    1 
ATOM   1585 C C     . LEU   A 1 211 ? -21.622 32.807 -33.219 1.00 75.37  ?  211 LEU   A C     1 
ATOM   1586 O O     . LEU   A 1 211 ? -21.072 33.370 -34.168 1.00 77.16  ?  211 LEU   A O     1 
ATOM   1587 C CB    . LEU   A 1 211 ? -20.754 30.748 -32.135 1.00 67.15  ?  211 LEU   A CB    1 
ATOM   1588 C CG    . LEU   A 1 211 ? -21.062 29.323 -31.710 1.00 65.72  ?  211 LEU   A CG    1 
ATOM   1589 C CD1   . LEU   A 1 211 ? -20.460 29.055 -30.351 1.00 65.83  ?  211 LEU   A CD1   1 
ATOM   1590 C CD2   . LEU   A 1 211 ? -22.568 29.110 -31.691 1.00 75.86  ?  211 LEU   A CD2   1 
ATOM   1591 N N     . HIS   A 1 212 ? -22.167 33.465 -32.205 1.00 80.99  ?  212 HIS   A N     1 
ATOM   1592 C CA    . HIS   A 1 212 ? -22.136 34.918 -32.168 1.00 81.29  ?  212 HIS   A CA    1 
ATOM   1593 C C     . HIS   A 1 212 ? -20.818 35.366 -31.557 1.00 73.65  ?  212 HIS   A C     1 
ATOM   1594 O O     . HIS   A 1 212 ? -20.397 34.846 -30.517 1.00 72.00  ?  212 HIS   A O     1 
ATOM   1595 C CB    . HIS   A 1 212 ? -23.325 35.469 -31.388 1.00 81.64  ?  212 HIS   A CB    1 
ATOM   1596 C CG    . HIS   A 1 212 ? -24.628 35.331 -32.111 1.00 84.66  ?  212 HIS   A CG    1 
ATOM   1597 N ND1   . HIS   A 1 212 ? -25.032 36.204 -33.100 1.00 83.61  ?  212 HIS   A ND1   1 
ATOM   1598 C CD2   . HIS   A 1 212 ? -25.610 34.407 -31.999 1.00 80.80  ?  212 HIS   A CD2   1 
ATOM   1599 C CE1   . HIS   A 1 212 ? -26.217 35.834 -33.552 1.00 83.89  ?  212 HIS   A CE1   1 
ATOM   1600 N NE2   . HIS   A 1 212 ? -26.587 34.742 -32.905 1.00 81.31  ?  212 HIS   A NE2   1 
ATOM   1601 N N     . ILE   A 1 213 ? -20.160 36.313 -32.226 1.00 72.55  ?  213 ILE   A N     1 
ATOM   1602 C CA    . ILE   A 1 213 ? -18.811 36.733 -31.867 1.00 75.02  ?  213 ILE   A CA    1 
ATOM   1603 C C     . ILE   A 1 213 ? -18.879 38.089 -31.174 1.00 73.52  ?  213 ILE   A C     1 
ATOM   1604 O O     . ILE   A 1 213 ? -18.892 39.141 -31.827 1.00 70.17  ?  213 ILE   A O     1 
ATOM   1605 C CB    . ILE   A 1 213 ? -17.903 36.769 -33.115 1.00 70.66  ?  213 ILE   A CB    1 
ATOM   1606 C CG1   . ILE   A 1 213 ? -17.777 35.365 -33.710 1.00 67.48  ?  213 ILE   A CG1   1 
ATOM   1607 C CG2   . ILE   A 1 213 ? -16.521 37.314 -32.787 1.00 62.70  ?  213 ILE   A CG2   1 
ATOM   1608 C CD1   . ILE   A 1 213 ? -17.063 34.375 -32.807 1.00 60.98  ?  213 ILE   A CD1   1 
ATOM   1609 N N     . VAL   A 1 214 ? -18.943 38.082 -29.849 1.00 69.67  ?  214 VAL   A N     1 
ATOM   1610 C CA    . VAL   A 1 214 ? -19.087 39.344 -29.134 1.00 67.15  ?  214 VAL   A CA    1 
ATOM   1611 C C     . VAL   A 1 214 ? -17.743 39.756 -28.541 1.00 66.22  ?  214 VAL   A C     1 
ATOM   1612 O O     . VAL   A 1 214 ? -17.016 38.909 -27.989 1.00 64.34  ?  214 VAL   A O     1 
ATOM   1613 C CB    . VAL   A 1 214 ? -20.183 39.250 -28.066 1.00 65.83  ?  214 VAL   A CB    1 
ATOM   1614 C CG1   . VAL   A 1 214 ? -19.778 38.280 -26.955 1.00 69.72  ?  214 VAL   A CG1   1 
ATOM   1615 C CG2   . VAL   A 1 214 ? -20.441 40.627 -27.473 1.00 66.87  ?  214 VAL   A CG2   1 
ATOM   1616 N N     . PRO   A 1 215 ? -17.356 41.029 -28.661 1.00 61.54  ?  215 PRO   A N     1 
ATOM   1617 C CA    . PRO   A 1 215 ? -16.100 41.474 -28.051 1.00 60.55  ?  215 PRO   A CA    1 
ATOM   1618 C C     . PRO   A 1 215 ? -16.150 41.346 -26.535 1.00 62.65  ?  215 PRO   A C     1 
ATOM   1619 O O     . PRO   A 1 215 ? -17.214 41.199 -25.930 1.00 64.92  ?  215 PRO   A O     1 
ATOM   1620 C CB    . PRO   A 1 215 ? -15.977 42.940 -28.501 1.00 60.27  ?  215 PRO   A CB    1 
ATOM   1621 C CG    . PRO   A 1 215 ? -17.306 43.312 -29.098 1.00 55.86  ?  215 PRO   A CG    1 
ATOM   1622 C CD    . PRO   A 1 215 ? -17.914 42.042 -29.575 1.00 65.80  ?  215 PRO   A CD    1 
ATOM   1623 N N     . LYS   A 1 216 ? -14.967 41.371 -25.917 1.00 59.04  ?  216 LYS   A N     1 
ATOM   1624 C CA    . LYS   A 1 216 ? -14.919 41.345 -24.460 1.00 61.06  ?  216 LYS   A CA    1 
ATOM   1625 C C     . LYS   A 1 216 ? -15.497 42.607 -23.834 1.00 60.76  ?  216 LYS   A C     1 
ATOM   1626 O O     . LYS   A 1 216 ? -15.641 42.670 -22.608 1.00 61.70  ?  216 LYS   A O     1 
ATOM   1627 C CB    . LYS   A 1 216 ? -13.477 41.139 -23.980 1.00 57.31  ?  216 LYS   A CB    1 
ATOM   1628 C CG    . LYS   A 1 216 ? -12.954 39.741 -24.251 1.00 55.59  ?  216 LYS   A CG    1 
ATOM   1629 C CD    . LYS   A 1 216 ? -11.588 39.506 -23.645 1.00 53.23  ?  216 LYS   A CD    1 
ATOM   1630 C CE    . LYS   A 1 216 ? -11.218 38.041 -23.766 1.00 55.36  ?  216 LYS   A CE    1 
ATOM   1631 N NZ    . LYS   A 1 216 ? -9.904  37.752 -23.175 1.00 47.30  ?  216 LYS   A NZ    1 
ATOM   1632 N N     . GLN   A 1 217 ? -15.860 43.593 -24.639 1.00 61.46  ?  217 GLN   A N     1 
ATOM   1633 C CA    . GLN   A 1 217 ? -16.099 44.926 -24.121 1.00 61.96  ?  217 GLN   A CA    1 
ATOM   1634 C C     . GLN   A 1 217 ? -17.038 45.676 -25.055 1.00 60.19  ?  217 GLN   A C     1 
ATOM   1635 O O     . GLN   A 1 217 ? -16.784 45.777 -26.262 1.00 59.41  ?  217 GLN   A O     1 
ATOM   1636 C CB    . GLN   A 1 217 ? -14.767 45.674 -23.973 1.00 60.30  ?  217 GLN   A CB    1 
ATOM   1637 C CG    . GLN   A 1 217 ? -14.906 47.156 -23.930 1.00 60.68  ?  217 GLN   A CG    1 
ATOM   1638 C CD    . GLN   A 1 217 ? -14.914 47.757 -25.312 1.00 61.46  ?  217 GLN   A CD    1 
ATOM   1639 O OE1   . GLN   A 1 217 ? -14.099 47.411 -26.158 1.00 64.42  ?  217 GLN   A OE1   1 
ATOM   1640 N NE2   . GLN   A 1 217 ? -15.899 48.598 -25.575 1.00 62.40  ?  217 GLN   A NE2   1 
ATOM   1641 N N     . LEU   A 1 218 ? -18.111 46.210 -24.489 1.00 59.45  ?  218 LEU   A N     1 
ATOM   1642 C CA    . LEU   A 1 218 ? -18.935 47.205 -25.156 1.00 64.56  ?  218 LEU   A CA    1 
ATOM   1643 C C     . LEU   A 1 218 ? -19.075 48.408 -24.232 1.00 67.59  ?  218 LEU   A C     1 
ATOM   1644 O O     . LEU   A 1 218 ? -19.166 48.253 -23.008 1.00 60.88  ?  218 LEU   A O     1 
ATOM   1645 C CB    . LEU   A 1 218 ? -20.300 46.637 -25.526 1.00 65.80  ?  218 LEU   A CB    1 
ATOM   1646 C CG    . LEU   A 1 218 ? -20.259 45.522 -26.574 1.00 62.09  ?  218 LEU   A CG    1 
ATOM   1647 C CD1   . LEU   A 1 218 ? -21.192 44.392 -26.180 1.00 65.25  ?  218 LEU   A CD1   1 
ATOM   1648 C CD2   . LEU   A 1 218 ? -20.591 46.043 -27.953 1.00 57.77  ?  218 LEU   A CD2   1 
ATOM   1649 N N     . PHE   A 1 219 ? -19.065 49.603 -24.825 1.00 69.67  ?  219 PHE   A N     1 
ATOM   1650 C CA    . PHE   A 1 219 ? -19.085 50.852 -24.065 1.00 68.48  ?  219 PHE   A CA    1 
ATOM   1651 C C     . PHE   A 1 219 ? -17.966 50.886 -23.031 1.00 66.40  ?  219 PHE   A C     1 
ATOM   1652 O O     . PHE   A 1 219 ? -18.147 51.334 -21.896 1.00 71.56  ?  219 PHE   A O     1 
ATOM   1653 C CB    . PHE   A 1 219 ? -20.441 51.068 -23.397 1.00 73.42  ?  219 PHE   A CB    1 
ATOM   1654 C CG    . PHE   A 1 219 ? -21.490 51.588 -24.322 1.00 72.26  ?  219 PHE   A CG    1 
ATOM   1655 C CD1   . PHE   A 1 219 ? -21.535 52.938 -24.648 1.00 71.52  ?  219 PHE   A CD1   1 
ATOM   1656 C CD2   . PHE   A 1 219 ? -22.432 50.728 -24.866 1.00 76.87  ?  219 PHE   A CD2   1 
ATOM   1657 C CE1   . PHE   A 1 219 ? -22.502 53.429 -25.514 1.00 81.11  ?  219 PHE   A CE1   1 
ATOM   1658 C CE2   . PHE   A 1 219 ? -23.406 51.205 -25.733 1.00 83.57  ?  219 PHE   A CE2   1 
ATOM   1659 C CZ    . PHE   A 1 219 ? -23.443 52.563 -26.056 1.00 87.68  ?  219 PHE   A CZ    1 
ATOM   1660 N N     . GLY   A 1 220 ? -16.797 50.394 -23.422 1.00 65.71  ?  220 GLY   A N     1 
ATOM   1661 C CA    . GLY   A 1 220 ? -15.694 50.261 -22.501 1.00 65.60  ?  220 GLY   A CA    1 
ATOM   1662 C C     . GLY   A 1 220 ? -15.906 49.290 -21.361 1.00 58.29  ?  220 GLY   A C     1 
ATOM   1663 O O     . GLY   A 1 220 ? -15.001 49.128 -20.541 1.00 61.87  ?  220 GLY   A O     1 
ATOM   1664 N N     . MET   A 1 221 ? -17.052 48.632 -21.278 1.00 63.84  ?  221 MET   A N     1 
ATOM   1665 C CA    . MET   A 1 221 ? -17.368 47.786 -20.135 1.00 69.83  ?  221 MET   A CA    1 
ATOM   1666 C C     . MET   A 1 221 ? -17.241 46.319 -20.515 1.00 65.66  ?  221 MET   A C     1 
ATOM   1667 O O     . MET   A 1 221 ? -17.604 45.918 -21.623 1.00 63.06  ?  221 MET   A O     1 
ATOM   1668 C CB    . MET   A 1 221 ? -18.789 48.042 -19.629 1.00 68.24  ?  221 MET   A CB    1 
ATOM   1669 C CG    . MET   A 1 221 ? -19.010 49.323 -18.869 1.00 74.30  ?  221 MET   A CG    1 
ATOM   1670 S SD    . MET   A 1 221 ? -20.628 49.295 -18.039 1.00 91.96  ?  221 MET   A SD    1 
ATOM   1671 C CE    . MET   A 1 221 ? -20.602 47.678 -17.237 1.00 75.72  ?  221 MET   A CE    1 
ATOM   1672 N N     . SER   A 1 222 ? -16.736 45.523 -19.586 1.00 63.88  ?  222 SER   A N     1 
ATOM   1673 C CA    . SER   A 1 222 ? -16.758 44.085 -19.769 1.00 66.23  ?  222 SER   A CA    1 
ATOM   1674 C C     . SER   A 1 222 ? -18.206 43.626 -19.892 1.00 68.05  ?  222 SER   A C     1 
ATOM   1675 O O     . SER   A 1 222 ? -19.102 44.191 -19.262 1.00 70.59  ?  222 SER   A O     1 
ATOM   1676 C CB    . SER   A 1 222 ? -16.054 43.411 -18.590 1.00 62.98  ?  222 SER   A CB    1 
ATOM   1677 O OG    . SER   A 1 222 ? -15.544 42.143 -18.936 1.00 64.46  ?  222 SER   A OG    1 
ATOM   1678 N N     . VAL   A 1 223 ? -18.445 42.617 -20.736 1.00 70.46  ?  223 VAL   A N     1 
ATOM   1679 C CA    . VAL   A 1 223 ? -19.823 42.176 -20.949 1.00 70.27  ?  223 VAL   A CA    1 
ATOM   1680 C C     . VAL   A 1 223 ? -20.341 41.421 -19.736 1.00 67.41  ?  223 VAL   A C     1 
ATOM   1681 O O     . VAL   A 1 223 ? -21.553 41.385 -19.493 1.00 70.98  ?  223 VAL   A O     1 
ATOM   1682 C CB    . VAL   A 1 223 ? -19.947 41.326 -22.231 1.00 60.75  ?  223 VAL   A CB    1 
ATOM   1683 C CG1   . VAL   A 1 223 ? -19.438 42.110 -23.418 1.00 63.65  ?  223 VAL   A CG1   1 
ATOM   1684 C CG2   . VAL   A 1 223 ? -19.224 40.005 -22.083 1.00 57.13  ?  223 VAL   A CG2   1 
ATOM   1685 N N     . ASP   A 1 224 ? -19.455 40.797 -18.962 1.00 61.60  ?  224 ASP   A N     1 
ATOM   1686 C CA    . ASP   A 1 224 ? -19.922 40.169 -17.738 1.00 68.44  ?  224 ASP   A CA    1 
ATOM   1687 C C     . ASP   A 1 224 ? -20.279 41.200 -16.671 1.00 72.17  ?  224 ASP   A C     1 
ATOM   1688 O O     . ASP   A 1 224 ? -21.099 40.906 -15.796 1.00 73.19  ?  224 ASP   A O     1 
ATOM   1689 C CB    . ASP   A 1 224 ? -18.882 39.177 -17.212 1.00 65.62  ?  224 ASP   A CB    1 
ATOM   1690 C CG    . ASP   A 1 224 ? -17.631 39.850 -16.709 1.00 61.46  ?  224 ASP   A CG    1 
ATOM   1691 O OD1   . ASP   A 1 224 ? -17.203 40.847 -17.316 1.00 62.30  ?  224 ASP   A OD1   1 
ATOM   1692 O OD2   . ASP   A 1 224 ? -17.070 39.371 -15.707 1.00 61.19  ?  224 ASP   A OD2   1 
ATOM   1693 N N     . GLU   A 1 225 ? -19.709 42.402 -16.731 1.00 67.42  ?  225 GLU   A N     1 
ATOM   1694 C CA    . GLU   A 1 225 ? -20.111 43.434 -15.795 1.00 69.51  ?  225 GLU   A CA    1 
ATOM   1695 C C     . GLU   A 1 225 ? -21.256 44.283 -16.330 1.00 76.58  ?  225 GLU   A C     1 
ATOM   1696 O O     . GLU   A 1 225 ? -21.980 44.891 -15.537 1.00 82.49  ?  225 GLU   A O     1 
ATOM   1697 C CB    . GLU   A 1 225 ? -18.898 44.306 -15.383 1.00 74.32  ?  225 GLU   A CB    1 
ATOM   1698 C CG    . GLU   A 1 225 ? -18.211 45.204 -16.456 1.00 78.60  ?  225 GLU   A CG    1 
ATOM   1699 C CD    . GLU   A 1 225 ? -16.818 45.762 -16.017 1.00 76.88  ?  225 GLU   A CD    1 
ATOM   1700 O OE1   . GLU   A 1 225 ? -16.234 46.619 -16.741 1.00 73.22  ?  225 GLU   A OE1   1 
ATOM   1701 O OE2   . GLU   A 1 225 ? -16.306 45.340 -14.949 1.00 73.22  ?  225 GLU   A OE2   1 
ATOM   1702 N N     . ILE   A 1 226 ? -21.462 44.321 -17.647 1.00 77.56  ?  226 ILE   A N     1 
ATOM   1703 C CA    . ILE   A 1 226 ? -22.704 44.895 -18.161 1.00 79.82  ?  226 ILE   A CA    1 
ATOM   1704 C C     . ILE   A 1 226 ? -23.892 44.076 -17.680 1.00 84.49  ?  226 ILE   A C     1 
ATOM   1705 O O     . ILE   A 1 226 ? -24.975 44.620 -17.422 1.00 84.24  ?  226 ILE   A O     1 
ATOM   1706 C CB    . ILE   A 1 226 ? -22.663 44.979 -19.698 1.00 75.82  ?  226 ILE   A CB    1 
ATOM   1707 C CG1   . ILE   A 1 226 ? -21.563 45.944 -20.140 1.00 75.95  ?  226 ILE   A CG1   1 
ATOM   1708 C CG2   . ILE   A 1 226 ? -24.012 45.400 -20.254 1.00 75.04  ?  226 ILE   A CG2   1 
ATOM   1709 C CD1   . ILE   A 1 226 ? -21.731 46.502 -21.522 1.00 70.40  ?  226 ILE   A CD1   1 
ATOM   1710 N N     . ALA   A 1 227 ? -23.694 42.765 -17.512 1.00 83.44  ?  227 ALA   A N     1 
ATOM   1711 C CA    . ALA   A 1 227 ? -24.772 41.865 -17.123 1.00 84.98  ?  227 ALA   A CA    1 
ATOM   1712 C C     . ALA   A 1 227 ? -25.451 42.284 -15.826 1.00 91.98  ?  227 ALA   A C     1 
ATOM   1713 O O     . ALA   A 1 227 ? -26.617 41.928 -15.616 1.00 92.48  ?  227 ALA   A O     1 
ATOM   1714 C CB    . ALA   A 1 227 ? -24.241 40.433 -17.001 1.00 80.90  ?  227 ALA   A CB    1 
ATOM   1715 N N     . GLU   A 1 228 ? -24.766 43.033 -14.953 1.00 92.41  ?  228 GLU   A N     1 
ATOM   1716 C CA    . GLU   A 1 228 ? -25.392 43.531 -13.733 1.00 92.22  ?  228 GLU   A CA    1 
ATOM   1717 C C     . GLU   A 1 228 ? -25.388 45.053 -13.633 1.00 92.30  ?  228 GLU   A C     1 
ATOM   1718 O O     . GLU   A 1 228 ? -25.757 45.596 -12.584 1.00 97.84  ?  228 GLU   A O     1 
ATOM   1719 C CB    . GLU   A 1 228 ? -24.732 42.913 -12.502 1.00 98.28  ?  228 GLU   A CB    1 
ATOM   1720 C CG    . GLU   A 1 228 ? -25.647 42.913 -11.278 1.00 99.25  ?  228 GLU   A CG    1 
ATOM   1721 C CD    . GLU   A 1 228 ? -25.317 41.821 -10.292 1.00 105.75 ?  228 GLU   A CD    1 
ATOM   1722 O OE1   . GLU   A 1 228 ? -26.242 41.085 -9.879  1.00 109.34 ?  228 GLU   A OE1   1 
ATOM   1723 O OE2   . GLU   A 1 228 ? -24.132 41.705 -9.924  1.00 116.78 ?  228 GLU   A OE2   1 
ATOM   1724 N N     . ALA   A 1 229 ? -24.989 45.757 -14.691 1.00 95.35  ?  229 ALA   A N     1 
ATOM   1725 C CA    . ALA   A 1 229 ? -25.269 47.183 -14.805 1.00 96.47  ?  229 ALA   A CA    1 
ATOM   1726 C C     . ALA   A 1 229 ? -26.749 47.393 -14.519 1.00 102.80 ?  229 ALA   A C     1 
ATOM   1727 O O     . ALA   A 1 229 ? -27.595 46.912 -15.286 1.00 105.33 ?  229 ALA   A O     1 
ATOM   1728 C CB    . ALA   A 1 229 ? -24.911 47.715 -16.197 1.00 95.39  ?  229 ALA   A CB    1 
ATOM   1729 N N     . PRO   A 1 230 ? -27.101 48.069 -13.416 1.00 105.37 ?  230 PRO   A N     1 
ATOM   1730 C CA    . PRO   A 1 230 ? -28.527 48.197 -13.062 1.00 104.07 ?  230 PRO   A CA    1 
ATOM   1731 C C     . PRO   A 1 230 ? -29.381 48.734 -14.197 1.00 99.88  ?  230 PRO   A C     1 
ATOM   1732 O O     . PRO   A 1 230 ? -30.517 48.279 -14.375 1.00 98.52  ?  230 PRO   A O     1 
ATOM   1733 C CB    . PRO   A 1 230 ? -28.496 49.149 -11.858 1.00 102.51 ?  230 PRO   A CB    1 
ATOM   1734 C CG    . PRO   A 1 230 ? -27.129 48.952 -11.263 1.00 98.44  ?  230 PRO   A CG    1 
ATOM   1735 C CD    . PRO   A 1 230 ? -26.224 48.737 -12.437 1.00 98.49  ?  230 PRO   A CD    1 
ATOM   1736 N N     . TRP   A 1 231 ? -28.846 49.660 -15.000 1.00 103.06 ?  231 TRP   A N     1 
ATOM   1737 C CA    . TRP   A 1 231 ? -29.591 50.147 -16.157 1.00 107.12 ?  231 TRP   A CA    1 
ATOM   1738 C C     . TRP   A 1 231 ? -29.855 49.024 -17.159 1.00 108.42 ?  231 TRP   A C     1 
ATOM   1739 O O     . TRP   A 1 231 ? -30.865 49.050 -17.875 1.00 109.30 ?  231 TRP   A O     1 
ATOM   1740 C CB    . TRP   A 1 231 ? -28.860 51.350 -16.795 1.00 102.83 ?  231 TRP   A CB    1 
ATOM   1741 C CG    . TRP   A 1 231 ? -27.663 51.099 -17.737 1.00 106.81 ?  231 TRP   A CG    1 
ATOM   1742 C CD1   . TRP   A 1 231 ? -26.958 49.935 -17.912 1.00 105.14 ?  231 TRP   A CD1   1 
ATOM   1743 C CD2   . TRP   A 1 231 ? -27.046 52.068 -18.612 1.00 108.73 ?  231 TRP   A CD2   1 
ATOM   1744 N NE1   . TRP   A 1 231 ? -25.960 50.117 -18.843 1.00 103.83 ?  231 TRP   A NE1   1 
ATOM   1745 C CE2   . TRP   A 1 231 ? -25.991 51.415 -19.287 1.00 107.35 ?  231 TRP   A CE2   1 
ATOM   1746 C CE3   . TRP   A 1 231 ? -27.290 53.424 -18.893 1.00 108.19 ?  231 TRP   A CE3   1 
ATOM   1747 C CZ2   . TRP   A 1 231 ? -25.179 52.071 -20.226 1.00 107.28 ?  231 TRP   A CZ2   1 
ATOM   1748 C CZ3   . TRP   A 1 231 ? -26.481 54.075 -19.826 1.00 106.96 ?  231 TRP   A CZ3   1 
ATOM   1749 C CH2   . TRP   A 1 231 ? -25.440 53.395 -20.480 1.00 106.72 ?  231 TRP   A CH2   1 
ATOM   1750 N N     . TRP   A 1 232 ? -28.995 48.004 -17.181 1.00 106.13 ?  232 TRP   A N     1 
ATOM   1751 C CA    . TRP   A 1 232 ? -29.181 46.890 -18.099 1.00 104.88 ?  232 TRP   A CA    1 
ATOM   1752 C C     . TRP   A 1 232 ? -30.129 45.838 -17.536 1.00 102.60 ?  232 TRP   A C     1 
ATOM   1753 O O     . TRP   A 1 232 ? -30.783 45.129 -18.306 1.00 105.32 ?  232 TRP   A O     1 
ATOM   1754 C CB    . TRP   A 1 232 ? -27.824 46.261 -18.436 1.00 101.13 ?  232 TRP   A CB    1 
ATOM   1755 C CG    . TRP   A 1 232 ? -27.891 45.200 -19.488 1.00 89.49  ?  232 TRP   A CG    1 
ATOM   1756 C CD1   . TRP   A 1 232 ? -27.894 45.387 -20.831 1.00 91.32  ?  232 TRP   A CD1   1 
ATOM   1757 C CD2   . TRP   A 1 232 ? -27.970 43.784 -19.278 1.00 91.46  ?  232 TRP   A CD2   1 
ATOM   1758 N NE1   . TRP   A 1 232 ? -27.966 44.174 -21.483 1.00 97.37  ?  232 TRP   A NE1   1 
ATOM   1759 C CE2   . TRP   A 1 232 ? -28.014 43.174 -20.548 1.00 95.65  ?  232 TRP   A CE2   1 
ATOM   1760 C CE3   . TRP   A 1 232 ? -28.010 42.973 -18.142 1.00 94.13  ?  232 TRP   A CE3   1 
ATOM   1761 C CZ2   . TRP   A 1 232 ? -28.090 41.791 -20.713 1.00 91.25  ?  232 TRP   A CZ2   1 
ATOM   1762 C CZ3   . TRP   A 1 232 ? -28.088 41.598 -18.309 1.00 91.16  ?  232 TRP   A CZ3   1 
ATOM   1763 C CH2   . TRP   A 1 232 ? -28.129 41.023 -19.583 1.00 87.68  ?  232 TRP   A CH2   1 
ATOM   1764 N N     . ASN   A 1 233 ? -30.228 45.727 -16.211 1.00 102.34 ?  233 ASN   A N     1 
ATOM   1765 C CA    . ASN   A 1 233 ? -31.064 44.687 -15.615 1.00 104.93 ?  233 ASN   A CA    1 
ATOM   1766 C C     . ASN   A 1 233 ? -32.549 45.001 -15.746 1.00 105.72 ?  233 ASN   A C     1 
ATOM   1767 O O     . ASN   A 1 233 ? -33.377 44.080 -15.776 1.00 99.47  ?  233 ASN   A O     1 
ATOM   1768 C CB    . ASN   A 1 233 ? -30.689 44.501 -14.148 1.00 105.36 ?  233 ASN   A CB    1 
ATOM   1769 C CG    . ASN   A 1 233 ? -29.239 44.125 -13.972 1.00 105.67 ?  233 ASN   A CG    1 
ATOM   1770 O OD1   . ASN   A 1 233 ? -28.493 44.794 -13.249 1.00 101.91 ?  233 ASN   A OD1   1 
ATOM   1771 N ND2   . ASN   A 1 233 ? -28.822 43.057 -14.649 1.00 101.58 ?  233 ASN   A ND2   1 
ATOM   1772 N N     . GLU   A 1 234 ? -32.903 46.285 -15.811 1.00 105.47 ?  234 GLU   A N     1 
ATOM   1773 C CA    . GLU   A 1 234 ? -34.286 46.709 -15.996 1.00 104.16 ?  234 GLU   A CA    1 
ATOM   1774 C C     . GLU   A 1 234 ? -34.735 46.636 -17.448 1.00 108.02 ?  234 GLU   A C     1 
ATOM   1775 O O     . GLU   A 1 234 ? -35.849 47.077 -17.757 1.00 104.17 ?  234 GLU   A O     1 
ATOM   1776 C CB    . GLU   A 1 234 ? -34.464 48.127 -15.461 1.00 102.11 ?  234 GLU   A CB    1 
ATOM   1777 C CG    . GLU   A 1 234 ? -34.322 48.199 -13.964 1.00 105.36 ?  234 GLU   A CG    1 
ATOM   1778 C CD    . GLU   A 1 234 ? -33.637 49.466 -13.509 1.00 106.64 ?  234 GLU   A CD    1 
ATOM   1779 O OE1   . GLU   A 1 234 ? -32.967 49.421 -12.454 1.00 101.01 ?  234 GLU   A OE1   1 
ATOM   1780 O OE2   . GLU   A 1 234 ? -33.756 50.496 -14.208 1.00 105.22 ?  234 GLU   A OE2   1 
ATOM   1781 N N     . MET   A 1 235 ? -33.875 46.128 -18.330 1.00 109.25 ?  235 MET   A N     1 
ATOM   1782 C CA    . MET   A 1 235 ? -34.243 45.778 -19.695 1.00 104.59 ?  235 MET   A CA    1 
ATOM   1783 C C     . MET   A 1 235 ? -35.189 44.574 -19.689 1.00 108.56 ?  235 MET   A C     1 
ATOM   1784 O O     . MET   A 1 235 ? -35.080 43.684 -18.834 1.00 104.86 ?  235 MET   A O     1 
ATOM   1785 C CB    . MET   A 1 235 ? -32.977 45.422 -20.484 1.00 105.89 ?  235 MET   A CB    1 
ATOM   1786 C CG    . MET   A 1 235 ? -32.177 46.569 -21.112 1.00 107.23 ?  235 MET   A CG    1 
ATOM   1787 S SD    . MET   A 1 235 ? -33.106 47.736 -22.122 1.00 118.29 ?  235 MET   A SD    1 
ATOM   1788 C CE    . MET   A 1 235 ? -31.971 49.122 -22.147 1.00 109.46 ?  235 MET   A CE    1 
ATOM   1789 N N     . SER   A 1 236 ? -36.134 44.543 -20.633 1.00 108.66 ?  236 SER   A N     1 
ATOM   1790 C CA    . SER   A 1 236 ? -36.783 43.266 -20.895 1.00 107.18 ?  236 SER   A CA    1 
ATOM   1791 C C     . SER   A 1 236 ? -35.904 42.449 -21.839 1.00 107.13 ?  236 SER   A C     1 
ATOM   1792 O O     . SER   A 1 236 ? -34.906 42.939 -22.374 1.00 106.44 ?  236 SER   A O     1 
ATOM   1793 C CB    . SER   A 1 236 ? -38.184 43.457 -21.474 1.00 105.56 ?  236 SER   A CB    1 
ATOM   1794 O OG    . SER   A 1 236 ? -38.155 43.577 -22.886 1.00 108.36 ?  236 SER   A OG    1 
ATOM   1795 N N     . PHE   A 1 237 ? -36.269 41.183 -22.035 1.00 108.39 ?  237 PHE   A N     1 
ATOM   1796 C CA    . PHE   A 1 237 ? -35.389 40.281 -22.771 1.00 104.54 ?  237 PHE   A CA    1 
ATOM   1797 C C     . PHE   A 1 237 ? -35.104 40.804 -24.176 1.00 103.37 ?  237 PHE   A C     1 
ATOM   1798 O O     . PHE   A 1 237 ? -33.944 40.977 -24.563 1.00 105.64 ?  237 PHE   A O     1 
ATOM   1799 C CB    . PHE   A 1 237 ? -35.988 38.879 -22.824 1.00 101.22 ?  237 PHE   A CB    1 
ATOM   1800 C CG    . PHE   A 1 237 ? -35.042 37.844 -23.367 1.00 107.01 ?  237 PHE   A CG    1 
ATOM   1801 C CD1   . PHE   A 1 237 ? -33.727 38.174 -23.668 1.00 110.33 ?  237 PHE   A CD1   1 
ATOM   1802 C CD2   . PHE   A 1 237 ? -35.470 36.547 -23.600 1.00 106.62 ?  237 PHE   A CD2   1 
ATOM   1803 C CE1   . PHE   A 1 237 ? -32.856 37.224 -24.175 1.00 111.48 ?  237 PHE   A CE1   1 
ATOM   1804 C CE2   . PHE   A 1 237 ? -34.608 35.602 -24.114 1.00 100.68 ?  237 PHE   A CE2   1 
ATOM   1805 C CZ    . PHE   A 1 237 ? -33.300 35.936 -24.396 1.00 108.86 ?  237 PHE   A CZ    1 
ATOM   1806 N N     . ASP   A 1 238 ? -36.145 41.063 -24.959 1.00 101.92 ?  238 ASP   A N     1 
ATOM   1807 C CA    . ASP   A 1 238 ? -35.940 41.615 -26.294 1.00 110.00 ?  238 ASP   A CA    1 
ATOM   1808 C C     . ASP   A 1 238 ? -35.840 43.142 -26.293 1.00 110.93 ?  238 ASP   A C     1 
ATOM   1809 O O     . ASP   A 1 238 ? -35.801 43.753 -27.372 1.00 103.80 ?  238 ASP   A O     1 
ATOM   1810 C CB    . ASP   A 1 238 ? -37.032 41.106 -27.258 1.00 112.86 ?  238 ASP   A CB    1 
ATOM   1811 C CG    . ASP   A 1 238 ? -38.308 41.935 -27.229 1.00 113.08 ?  238 ASP   A CG    1 
ATOM   1812 O OD1   . ASP   A 1 238 ? -38.356 42.984 -27.909 1.00 110.97 ?  238 ASP   A OD1   1 
ATOM   1813 O OD2   . ASP   A 1 238 ? -39.266 41.525 -26.544 1.00 117.91 ?  238 ASP   A OD2   1 
ATOM   1814 N N     . GLU   A 1 239 ? -35.802 43.759 -25.108 1.00 109.46 ?  239 GLU   A N     1 
ATOM   1815 C CA    . GLU   A 1 239 ? -35.370 45.139 -24.935 1.00 107.26 ?  239 GLU   A CA    1 
ATOM   1816 C C     . GLU   A 1 239 ? -33.856 45.255 -24.888 1.00 104.87 ?  239 GLU   A C     1 
ATOM   1817 O O     . GLU   A 1 239 ? -33.297 46.172 -25.491 1.00 97.24  ?  239 GLU   A O     1 
ATOM   1818 C CB    . GLU   A 1 239 ? -35.958 45.721 -23.638 1.00 108.49 ?  239 GLU   A CB    1 
ATOM   1819 C CG    . GLU   A 1 239 ? -37.188 46.586 -23.765 1.00 107.37 ?  239 GLU   A CG    1 
ATOM   1820 C CD    . GLU   A 1 239 ? -37.304 47.564 -22.605 1.00 110.63 ?  239 GLU   A CD    1 
ATOM   1821 O OE1   . GLU   A 1 239 ? -36.915 48.744 -22.757 1.00 107.98 ?  239 GLU   A OE1   1 
ATOM   1822 O OE2   . GLU   A 1 239 ? -37.761 47.130 -21.520 1.00 110.49 ?  239 GLU   A OE2   1 
ATOM   1823 N N     . ARG   A 1 240 ? -33.190 44.337 -24.178 1.00 101.51 ?  240 ARG   A N     1 
ATOM   1824 C CA    . ARG   A 1 240 ? -31.730 44.322 -24.079 1.00 103.87 ?  240 ARG   A CA    1 
ATOM   1825 C C     . ARG   A 1 240 ? -31.097 43.717 -25.332 1.00 102.19 ?  240 ARG   A C     1 
ATOM   1826 O O     . ARG   A 1 240 ? -30.156 44.288 -25.898 1.00 95.65  ?  240 ARG   A O     1 
ATOM   1827 C CB    . ARG   A 1 240 ? -31.290 43.556 -22.815 1.00 101.36 ?  240 ARG   A CB    1 
ATOM   1828 C CG    . ARG   A 1 240 ? -31.761 42.109 -22.767 1.00 99.42  ?  240 ARG   A CG    1 
ATOM   1829 C CD    . ARG   A 1 240 ? -31.423 41.434 -21.464 1.00 99.71  ?  240 ARG   A CD    1 
ATOM   1830 N NE    . ARG   A 1 240 ? -31.922 42.183 -20.316 1.00 103.65 ?  240 ARG   A NE    1 
ATOM   1831 C CZ    . ARG   A 1 240 ? -32.157 41.650 -19.121 1.00 101.43 ?  240 ARG   A CZ    1 
ATOM   1832 N NH1   . ARG   A 1 240 ? -31.939 40.354 -18.919 1.00 93.66  ?  240 ARG   A NH1   1 
ATOM   1833 N NH2   . ARG   A 1 240 ? -32.609 42.413 -18.129 1.00 99.21  ?  240 ARG   A NH2   1 
ATOM   1834 N N     . ARG   A 1 241 ? -31.609 42.558 -25.774 1.00 103.56 ?  241 ARG   A N     1 
ATOM   1835 C CA    . ARG   A 1 241 ? -31.207 41.983 -27.050 1.00 96.00  ?  241 ARG   A CA    1 
ATOM   1836 C C     . ARG   A 1 241 ? -31.385 42.994 -28.168 1.00 95.15  ?  241 ARG   A C     1 
ATOM   1837 O O     . ARG   A 1 241 ? -30.615 42.998 -29.133 1.00 93.24  ?  241 ARG   A O     1 
ATOM   1838 C CB    . ARG   A 1 241 ? -32.016 40.711 -27.311 1.00 98.62  ?  241 ARG   A CB    1 
ATOM   1839 C CG    . ARG   A 1 241 ? -31.989 40.192 -28.753 1.00 102.35 ?  241 ARG   A CG    1 
ATOM   1840 C CD    . ARG   A 1 241 ? -32.814 38.902 -28.918 1.00 100.83 ?  241 ARG   A CD    1 
ATOM   1841 N NE    . ARG   A 1 241 ? -32.116 37.719 -28.404 1.00 103.53 ?  241 ARG   A NE    1 
ATOM   1842 C CZ    . ARG   A 1 241 ? -32.655 36.503 -28.305 1.00 103.29 ?  241 ARG   A CZ    1 
ATOM   1843 N NH1   . ARG   A 1 241 ? -33.909 36.295 -28.687 1.00 104.62 ?  241 ARG   A NH1   1 
ATOM   1844 N NH2   . ARG   A 1 241 ? -31.941 35.488 -27.826 1.00 99.30  ?  241 ARG   A NH2   1 
ATOM   1845 N N     . ARG   A 1 242 ? -32.370 43.883 -28.034 1.00 101.41 ?  242 ARG   A N     1 
ATOM   1846 C CA    . ARG   A 1 242 ? -32.479 45.024 -28.939 1.00 103.80 ?  242 ARG   A CA    1 
ATOM   1847 C C     . ARG   A 1 242 ? -31.195 45.847 -28.935 1.00 96.55  ?  242 ARG   A C     1 
ATOM   1848 O O     . ARG   A 1 242 ? -30.593 46.094 -29.987 1.00 92.43  ?  242 ARG   A O     1 
ATOM   1849 C CB    . ARG   A 1 242 ? -33.680 45.890 -28.544 1.00 106.95 ?  242 ARG   A CB    1 
ATOM   1850 C CG    . ARG   A 1 242 ? -33.936 47.087 -29.457 1.00 111.59 ?  242 ARG   A CG    1 
ATOM   1851 C CD    . ARG   A 1 242 ? -34.740 46.689 -30.692 1.00 111.70 ?  242 ARG   A CD    1 
ATOM   1852 N NE    . ARG   A 1 242 ? -35.556 47.790 -31.198 1.00 125.65 ?  242 ARG   A NE    1 
ATOM   1853 C CZ    . ARG   A 1 242 ? -36.158 47.796 -32.388 1.00 131.86 ?  242 ARG   A CZ    1 
ATOM   1854 N NH1   . ARG   A 1 242 ? -36.039 46.756 -33.206 1.00 124.04 ?  242 ARG   A NH1   1 
ATOM   1855 N NH2   . ARG   A 1 242 ? -36.883 48.846 -32.760 1.00 131.91 ?  242 ARG   A NH2   1 
ATOM   1856 N N     . TRP   A 1 243 ? -30.751 46.267 -27.748 1.00 99.77  ?  243 TRP   A N     1 
ATOM   1857 C CA    . TRP   A 1 243 ? -29.572 47.121 -27.657 1.00 96.11  ?  243 TRP   A CA    1 
ATOM   1858 C C     . TRP   A 1 243 ? -28.280 46.323 -27.812 1.00 88.92  ?  243 TRP   A C     1 
ATOM   1859 O O     . TRP   A 1 243 ? -27.336 46.797 -28.452 1.00 85.94  ?  243 TRP   A O     1 
ATOM   1860 C CB    . TRP   A 1 243 ? -29.578 47.886 -26.331 1.00 95.33  ?  243 TRP   A CB    1 
ATOM   1861 C CG    . TRP   A 1 243 ? -28.244 48.481 -26.003 1.00 97.78  ?  243 TRP   A CG    1 
ATOM   1862 C CD1   . TRP   A 1 243 ? -27.706 49.638 -26.507 1.00 96.24  ?  243 TRP   A CD1   1 
ATOM   1863 C CD2   . TRP   A 1 243 ? -27.262 47.932 -25.119 1.00 92.44  ?  243 TRP   A CD2   1 
ATOM   1864 N NE1   . TRP   A 1 243 ? -26.453 49.843 -25.977 1.00 92.86  ?  243 TRP   A NE1   1 
ATOM   1865 C CE2   . TRP   A 1 243 ? -26.156 48.810 -25.125 1.00 88.36  ?  243 TRP   A CE2   1 
ATOM   1866 C CE3   . TRP   A 1 243 ? -27.210 46.783 -24.323 1.00 90.11  ?  243 TRP   A CE3   1 
ATOM   1867 C CZ2   . TRP   A 1 243 ? -25.014 48.574 -24.364 1.00 84.71  ?  243 TRP   A CZ2   1 
ATOM   1868 C CZ3   . TRP   A 1 243 ? -26.076 46.551 -23.567 1.00 85.32  ?  243 TRP   A CZ3   1 
ATOM   1869 C CH2   . TRP   A 1 243 ? -24.994 47.444 -23.590 1.00 87.69  ?  243 TRP   A CH2   1 
ATOM   1870 N N     . VAL   A 1 244 ? -28.222 45.118 -27.236 1.00 90.92  ?  244 VAL   A N     1 
ATOM   1871 C CA    . VAL   A 1 244 ? -27.027 44.277 -27.350 1.00 86.72  ?  244 VAL   A CA    1 
ATOM   1872 C C     . VAL   A 1 244 ? -26.686 44.030 -28.810 1.00 85.74  ?  244 VAL   A C     1 
ATOM   1873 O O     . VAL   A 1 244 ? -25.522 44.122 -29.221 1.00 79.45  ?  244 VAL   A O     1 
ATOM   1874 C CB    . VAL   A 1 244 ? -27.229 42.947 -26.603 1.00 85.18  ?  244 VAL   A CB    1 
ATOM   1875 C CG1   . VAL   A 1 244 ? -26.097 41.994 -26.915 1.00 74.72  ?  244 VAL   A CG1   1 
ATOM   1876 C CG2   . VAL   A 1 244 ? -27.331 43.189 -25.106 1.00 94.28  ?  244 VAL   A CG2   1 
ATOM   1877 N N     . GLU   A 1 245 ? -27.700 43.710 -29.614 1.00 85.89  ?  245 GLU   A N     1 
ATOM   1878 C CA    . GLU   A 1 245 ? -27.448 43.338 -30.996 1.00 84.14  ?  245 GLU   A CA    1 
ATOM   1879 C C     . GLU   A 1 245 ? -27.191 44.547 -31.876 1.00 82.08  ?  245 GLU   A C     1 
ATOM   1880 O O     . GLU   A 1 245 ? -26.486 44.428 -32.882 1.00 80.76  ?  245 GLU   A O     1 
ATOM   1881 C CB    . GLU   A 1 245 ? -28.604 42.499 -31.526 1.00 87.38  ?  245 GLU   A CB    1 
ATOM   1882 C CG    . GLU   A 1 245 ? -28.695 41.168 -30.788 1.00 94.14  ?  245 GLU   A CG    1 
ATOM   1883 C CD    . GLU   A 1 245 ? -29.544 40.144 -31.504 1.00 100.27 ?  245 GLU   A CD    1 
ATOM   1884 O OE1   . GLU   A 1 245 ? -30.713 40.463 -31.832 1.00 96.32  ?  245 GLU   A OE1   1 
ATOM   1885 O OE2   . GLU   A 1 245 ? -29.033 39.019 -31.733 1.00 100.88 ?  245 GLU   A OE2   1 
ATOM   1886 N N     . GLN   A 1 246 ? -27.719 45.713 -31.514 1.00 83.65  ?  246 GLN   A N     1 
ATOM   1887 C CA    . GLN   A 1 246 ? -27.273 46.923 -32.190 1.00 84.64  ?  246 GLN   A CA    1 
ATOM   1888 C C     . GLN   A 1 246 ? -25.912 47.372 -31.682 1.00 80.03  ?  246 GLN   A C     1 
ATOM   1889 O O     . GLN   A 1 246 ? -25.162 48.013 -32.429 1.00 77.68  ?  246 GLN   A O     1 
ATOM   1890 C CB    . GLN   A 1 246 ? -28.290 48.047 -32.016 1.00 87.18  ?  246 GLN   A CB    1 
ATOM   1891 C CG    . GLN   A 1 246 ? -29.686 47.709 -32.488 1.00 91.21  ?  246 GLN   A CG    1 
ATOM   1892 C CD    . GLN   A 1 246 ? -30.680 48.807 -32.148 1.00 103.06 ?  246 GLN   A CD    1 
ATOM   1893 O OE1   . GLN   A 1 246 ? -31.314 48.789 -31.086 1.00 100.27 ?  246 GLN   A OE1   1 
ATOM   1894 N NE2   . GLN   A 1 246 ? -30.814 49.780 -33.049 1.00 104.86 ?  246 GLN   A NE2   1 
ATOM   1895 N N     . ALA   A 1 247 ? -25.586 47.062 -30.419 1.00 77.28  ?  247 ALA   A N     1 
ATOM   1896 C CA    . ALA   A 1 247 ? -24.239 47.323 -29.922 1.00 75.65  ?  247 ALA   A CA    1 
ATOM   1897 C C     . ALA   A 1 247 ? -23.211 46.587 -30.764 1.00 75.09  ?  247 ALA   A C     1 
ATOM   1898 O O     . ALA   A 1 247 ? -22.204 47.170 -31.182 1.00 70.18  ?  247 ALA   A O     1 
ATOM   1899 C CB    . ALA   A 1 247 ? -24.116 46.905 -28.457 1.00 73.41  ?  247 ALA   A CB    1 
ATOM   1900 N N     . LEU   A 1 248 ? -23.468 45.307 -31.041 1.00 74.38  ?  248 LEU   A N     1 
ATOM   1901 C CA    . LEU   A 1 248 ? -22.580 44.526 -31.892 1.00 71.61  ?  248 LEU   A CA    1 
ATOM   1902 C C     . LEU   A 1 248 ? -22.454 45.146 -33.279 1.00 73.77  ?  248 LEU   A C     1 
ATOM   1903 O O     . LEU   A 1 248 ? -21.347 45.288 -33.811 1.00 71.00  ?  248 LEU   A O     1 
ATOM   1904 C CB    . LEU   A 1 248 ? -23.083 43.085 -31.984 1.00 70.54  ?  248 LEU   A CB    1 
ATOM   1905 C CG    . LEU   A 1 248 ? -23.089 42.337 -30.651 1.00 71.62  ?  248 LEU   A CG    1 
ATOM   1906 C CD1   . LEU   A 1 248 ? -23.131 40.837 -30.869 1.00 73.40  ?  248 LEU   A CD1   1 
ATOM   1907 C CD2   . LEU   A 1 248 ? -21.868 42.725 -29.850 1.00 66.14  ?  248 LEU   A CD2   1 
ATOM   1908 N N     . LEU   A 1 249 ? -23.571 45.540 -33.880 1.00 69.68  ?  249 LEU   A N     1 
ATOM   1909 C CA    . LEU   A 1 249 ? -23.480 45.929 -35.279 1.00 69.83  ?  249 LEU   A CA    1 
ATOM   1910 C C     . LEU   A 1 249 ? -22.633 47.184 -35.470 1.00 74.09  ?  249 LEU   A C     1 
ATOM   1911 O O     . LEU   A 1 249 ? -21.890 47.278 -36.457 1.00 74.64  ?  249 LEU   A O     1 
ATOM   1912 C CB    . LEU   A 1 249 ? -24.880 46.088 -35.868 1.00 76.28  ?  249 LEU   A CB    1 
ATOM   1913 C CG    . LEU   A 1 249 ? -25.651 44.758 -35.832 1.00 80.73  ?  249 LEU   A CG    1 
ATOM   1914 C CD1   . LEU   A 1 249 ? -27.183 44.919 -35.933 1.00 79.24  ?  249 LEU   A CD1   1 
ATOM   1915 C CD2   . LEU   A 1 249 ? -25.110 43.832 -36.900 1.00 77.19  ?  249 LEU   A CD2   1 
ATOM   1916 N N     . VAL   A 1 250 ? -22.678 48.132 -34.529 1.00 75.46  ?  250 VAL   A N     1 
ATOM   1917 C CA    . VAL   A 1 250 ? -21.809 49.302 -34.647 1.00 73.64  ?  250 VAL   A CA    1 
ATOM   1918 C C     . VAL   A 1 250 ? -20.368 48.928 -34.322 1.00 65.94  ?  250 VAL   A C     1 
ATOM   1919 O O     . VAL   A 1 250 ? -19.428 49.421 -34.955 1.00 66.66  ?  250 VAL   A O     1 
ATOM   1920 C CB    . VAL   A 1 250 ? -22.328 50.453 -33.755 1.00 76.31  ?  250 VAL   A CB    1 
ATOM   1921 C CG1   . VAL   A 1 250 ? -22.670 49.946 -32.358 1.00 74.04  ?  250 VAL   A CG1   1 
ATOM   1922 C CG2   . VAL   A 1 250 ? -21.309 51.608 -33.676 1.00 70.65  ?  250 VAL   A CG2   1 
ATOM   1923 N N     . ALA   A 1 251 ? -20.177 48.021 -33.365 1.00 61.63  ?  251 ALA   A N     1 
ATOM   1924 C CA    . ALA   A 1 251 ? -18.827 47.657 -32.962 1.00 66.05  ?  251 ALA   A CA    1 
ATOM   1925 C C     . ALA   A 1 251 ? -18.131 46.807 -34.023 1.00 68.39  ?  251 ALA   A C     1 
ATOM   1926 O O     . ALA   A 1 251 ? -16.938 46.995 -34.290 1.00 71.29  ?  251 ALA   A O     1 
ATOM   1927 C CB    . ALA   A 1 251 ? -18.868 46.926 -31.622 1.00 66.10  ?  251 ALA   A CB    1 
ATOM   1928 N N     . ARG   A 1 252 ? -18.856 45.887 -34.661 1.00 66.63  ?  252 ARG   A N     1 
ATOM   1929 C CA    . ARG   A 1 252 ? -18.220 44.907 -35.537 1.00 63.90  ?  252 ARG   A CA    1 
ATOM   1930 C C     . ARG   A 1 252 ? -18.897 44.694 -36.894 1.00 71.24  ?  252 ARG   A C     1 
ATOM   1931 O O     . ARG   A 1 252 ? -18.258 44.111 -37.779 1.00 67.27  ?  252 ARG   A O     1 
ATOM   1932 C CB    . ARG   A 1 252 ? -18.120 43.554 -34.817 1.00 58.43  ?  252 ARG   A CB    1 
ATOM   1933 C CG    . ARG   A 1 252 ? -19.459 43.048 -34.380 1.00 63.48  ?  252 ARG   A CG    1 
ATOM   1934 C CD    . ARG   A 1 252 ? -19.482 41.581 -34.082 1.00 67.10  ?  252 ARG   A CD    1 
ATOM   1935 N NE    . ARG   A 1 252 ? -20.727 40.996 -34.582 1.00 68.07  ?  252 ARG   A NE    1 
ATOM   1936 C CZ    . ARG   A 1 252 ? -21.308 39.913 -34.077 1.00 70.81  ?  252 ARG   A CZ    1 
ATOM   1937 N NH1   . ARG   A 1 252 ? -20.766 39.280 -33.051 1.00 71.54  ?  252 ARG   A NH1   1 
ATOM   1938 N NH2   . ARG   A 1 252 ? -22.423 39.446 -34.617 1.00 79.90  ?  252 ARG   A NH2   1 
ATOM   1939 N N     . GLY   A 1 253 ? -20.131 45.163 -37.125 1.00 70.71  ?  253 GLY   A N     1 
ATOM   1940 C CA    . GLY   A 1 253 ? -20.923 44.645 -38.228 1.00 65.20  ?  253 GLY   A CA    1 
ATOM   1941 C C     . GLY   A 1 253 ? -21.603 43.360 -37.787 1.00 67.66  ?  253 GLY   A C     1 
ATOM   1942 O O     . GLY   A 1 253 ? -21.732 43.093 -36.585 1.00 68.73  ?  253 GLY   A O     1 
ATOM   1943 N N     . ARG   A 1 254 ? -22.048 42.551 -38.753 1.00 74.83  ?  254 ARG   A N     1 
ATOM   1944 C CA    . ARG   A 1 254 ? -22.444 41.183 -38.421 1.00 75.69  ?  254 ARG   A CA    1 
ATOM   1945 C C     . ARG   A 1 254 ? -21.461 40.201 -39.036 1.00 76.65  ?  254 ARG   A C     1 
ATOM   1946 O O     . ARG   A 1 254 ? -20.647 40.544 -39.900 1.00 69.61  ?  254 ARG   A O     1 
ATOM   1947 C CB    . ARG   A 1 254 ? -23.875 40.836 -38.863 1.00 76.92  ?  254 ARG   A CB    1 
ATOM   1948 C CG    . ARG   A 1 254 ? -24.555 39.780 -37.941 1.00 76.30  ?  254 ARG   A CG    1 
ATOM   1949 C CD    . ARG   A 1 254 ? -24.935 40.410 -36.594 1.00 81.34  ?  254 ARG   A CD    1 
ATOM   1950 N NE    . ARG   A 1 254 ? -25.121 39.466 -35.489 1.00 86.14  ?  254 ARG   A NE    1 
ATOM   1951 C CZ    . ARG   A 1 254 ? -25.497 39.826 -34.256 1.00 89.54  ?  254 ARG   A CZ    1 
ATOM   1952 N NH1   . ARG   A 1 254 ? -25.735 41.105 -33.971 1.00 80.47  ?  254 ARG   A NH1   1 
ATOM   1953 N NH2   . ARG   A 1 254 ? -25.643 38.912 -33.301 1.00 86.62  ?  254 ARG   A NH2   1 
ATOM   1954 N N     . LEU   A 1 255 ? -21.554 38.959 -38.559 1.00 76.16  ?  255 LEU   A N     1 
ATOM   1955 C CA    . LEU   A 1 255 ? -20.563 37.944 -38.878 1.00 72.78  ?  255 LEU   A CA    1 
ATOM   1956 C C     . LEU   A 1 255 ? -20.461 37.650 -40.373 1.00 75.28  ?  255 LEU   A C     1 
ATOM   1957 O O     . LEU   A 1 255 ? -19.424 37.151 -40.815 1.00 74.81  ?  255 LEU   A O     1 
ATOM   1958 C CB    . LEU   A 1 255 ? -20.901 36.688 -38.081 1.00 74.04  ?  255 LEU   A CB    1 
ATOM   1959 C CG    . LEU   A 1 255 ? -21.122 37.090 -36.617 1.00 69.70  ?  255 LEU   A CG    1 
ATOM   1960 C CD1   . LEU   A 1 255 ? -21.559 35.925 -35.747 1.00 71.73  ?  255 LEU   A CD1   1 
ATOM   1961 C CD2   . LEU   A 1 255 ? -19.845 37.699 -36.080 1.00 70.68  ?  255 LEU   A CD2   1 
ATOM   1962 N N     . SER   A 1 256 ? -21.485 37.996 -41.165 1.00 82.15  ?  256 SER   A N     1 
ATOM   1963 C CA    . SER   A 1 256 ? -21.586 37.540 -42.552 1.00 77.04  ?  256 SER   A CA    1 
ATOM   1964 C C     . SER   A 1 256 ? -20.589 38.215 -43.492 1.00 78.48  ?  256 SER   A C     1 
ATOM   1965 O O     . SER   A 1 256 ? -20.373 37.707 -44.600 1.00 79.86  ?  256 SER   A O     1 
ATOM   1966 C CB    . SER   A 1 256 ? -23.004 37.766 -43.089 1.00 79.28  ?  256 SER   A CB    1 
ATOM   1967 O OG    . SER   A 1 256 ? -23.085 38.976 -43.835 1.00 82.32  ?  256 SER   A OG    1 
ATOM   1968 N N     . ASP   A 1 257 ? -19.987 39.341 -43.106 1.00 76.26  ?  257 ASP   A N     1 
ATOM   1969 C CA    . ASP   A 1 257 ? -18.920 39.924 -43.914 1.00 73.56  ?  257 ASP   A CA    1 
ATOM   1970 C C     . ASP   A 1 257 ? -17.528 39.625 -43.356 1.00 71.89  ?  257 ASP   A C     1 
ATOM   1971 O O     . ASP   A 1 257 ? -16.576 40.358 -43.647 1.00 70.52  ?  257 ASP   A O     1 
ATOM   1972 C CB    . ASP   A 1 257 ? -19.110 41.437 -44.099 1.00 74.35  ?  257 ASP   A CB    1 
ATOM   1973 C CG    . ASP   A 1 257 ? -19.572 42.146 -42.840 1.00 84.97  ?  257 ASP   A CG    1 
ATOM   1974 O OD1   . ASP   A 1 257 ? -20.273 41.520 -42.024 1.00 85.83  ?  257 ASP   A OD1   1 
ATOM   1975 O OD2   . ASP   A 1 257 ? -19.219 43.337 -42.663 1.00 85.90  ?  257 ASP   A OD2   1 
ATOM   1976 N N     . TYR   A 1 258 ? -17.385 38.559 -42.572 1.00 67.27  ?  258 TYR   A N     1 
ATOM   1977 C CA    . TYR   A 1 258 ? -16.070 38.041 -42.228 1.00 62.13  ?  258 TYR   A CA    1 
ATOM   1978 C C     . TYR   A 1 258 ? -15.862 36.639 -42.774 1.00 63.99  ?  258 TYR   A C     1 
ATOM   1979 O O     . TYR   A 1 258 ? -14.876 35.986 -42.417 1.00 67.79  ?  258 TYR   A O     1 
ATOM   1980 C CB    . TYR   A 1 258 ? -15.858 38.050 -40.712 1.00 62.48  ?  258 TYR   A CB    1 
ATOM   1981 C CG    . TYR   A 1 258 ? -15.919 39.430 -40.113 1.00 66.65  ?  258 TYR   A CG    1 
ATOM   1982 C CD1   . TYR   A 1 258 ? -14.864 40.326 -40.270 1.00 61.47  ?  258 TYR   A CD1   1 
ATOM   1983 C CD2   . TYR   A 1 258 ? -17.034 39.845 -39.397 1.00 66.96  ?  258 TYR   A CD2   1 
ATOM   1984 C CE1   . TYR   A 1 258 ? -14.918 41.596 -39.728 1.00 55.78  ?  258 TYR   A CE1   1 
ATOM   1985 C CE2   . TYR   A 1 258 ? -17.096 41.109 -38.853 1.00 63.68  ?  258 TYR   A CE2   1 
ATOM   1986 C CZ    . TYR   A 1 258 ? -16.037 41.978 -39.017 1.00 59.87  ?  258 TYR   A CZ    1 
ATOM   1987 O OH    . TYR   A 1 258 ? -16.110 43.237 -38.466 1.00 65.15  ?  258 TYR   A OH    1 
ATOM   1988 N N     . GLY   A 1 259 ? -16.759 36.160 -43.631 1.00 63.78  ?  259 GLY   A N     1 
ATOM   1989 C CA    . GLY   A 1 259 ? -16.686 34.786 -44.078 1.00 61.40  ?  259 GLY   A CA    1 
ATOM   1990 C C     . GLY   A 1 259 ? -17.110 33.796 -43.029 1.00 59.91  ?  259 GLY   A C     1 
ATOM   1991 O O     . GLY   A 1 259 ? -16.733 32.627 -43.106 1.00 65.49  ?  259 GLY   A O     1 
ATOM   1992 N N     . LEU   A 1 260 ? -17.887 34.237 -42.043 1.00 58.02  ?  260 LEU   A N     1 
ATOM   1993 C CA    . LEU   A 1 260 ? -18.360 33.436 -40.935 1.00 60.72  ?  260 LEU   A CA    1 
ATOM   1994 C C     . LEU   A 1 260 ? -19.824 33.057 -41.124 1.00 64.57  ?  260 LEU   A C     1 
ATOM   1995 O O     . LEU   A 1 260 ? -20.640 33.902 -41.517 1.00 65.39  ?  260 LEU   A O     1 
ATOM   1996 C CB    . LEU   A 1 260 ? -18.199 34.196 -39.615 1.00 60.72  ?  260 LEU   A CB    1 
ATOM   1997 C CG    . LEU   A 1 260 ? -16.762 34.294 -39.111 1.00 59.32  ?  260 LEU   A CG    1 
ATOM   1998 C CD1   . LEU   A 1 260 ? -16.736 34.605 -37.629 1.00 58.19  ?  260 LEU   A CD1   1 
ATOM   1999 C CD2   . LEU   A 1 260 ? -16.031 32.996 -39.390 1.00 63.53  ?  260 LEU   A CD2   1 
ATOM   2000 N N     . PRO   A 1 261 ? -20.182 31.803 -40.857 1.00 60.84  ?  261 PRO   A N     1 
ATOM   2001 C CA    . PRO   A 1 261 ? -21.599 31.431 -40.855 1.00 63.91  ?  261 PRO   A CA    1 
ATOM   2002 C C     . PRO   A 1 261 ? -22.345 32.246 -39.809 1.00 67.74  ?  261 PRO   A C     1 
ATOM   2003 O O     . PRO   A 1 261 ? -21.937 32.305 -38.644 1.00 73.63  ?  261 PRO   A O     1 
ATOM   2004 C CB    . PRO   A 1 261 ? -21.571 29.941 -40.501 1.00 65.07  ?  261 PRO   A CB    1 
ATOM   2005 C CG    . PRO   A 1 261 ? -20.301 29.773 -39.692 1.00 61.75  ?  261 PRO   A CG    1 
ATOM   2006 C CD    . PRO   A 1 261 ? -19.322 30.735 -40.314 1.00 64.40  ?  261 PRO   A CD    1 
ATOM   2007 N N     . GLU   A 1 262 ? -23.471 32.936 -40.252 1.00 70.28  ?  262 GLU   A N     1 
ATOM   2008 C CA    . GLU   A 1 262 ? -24.069 33.568 -39.085 1.00 75.18  ?  262 GLU   A CA    1 
ATOM   2009 C C     . GLU   A 1 262 ? -25.044 32.619 -38.409 1.00 70.59  ?  262 GLU   A C     1 
ATOM   2010 O O     . GLU   A 1 262 ? -25.642 31.768 -39.061 1.00 73.03  ?  262 GLU   A O     1 
ATOM   2011 C CB    . GLU   A 1 262 ? -24.784 34.848 -39.465 1.00 76.56  ?  262 GLU   A CB    1 
ATOM   2012 C CG    . GLU   A 1 262 ? -25.729 34.691 -40.596 1.00 80.84  ?  262 GLU   A CG    1 
ATOM   2013 C CD    . GLU   A 1 262 ? -25.906 35.997 -41.331 1.00 93.17  ?  262 GLU   A CD    1 
ATOM   2014 O OE1   . GLU   A 1 262 ? -25.319 37.018 -40.873 1.00 88.84  ?  262 GLU   A OE1   1 
ATOM   2015 O OE2   . GLU   A 1 262 ? -26.628 35.996 -42.360 1.00 99.18  ?  262 GLU   A OE2   1 
ATOM   2016 N N     . PRO   A 1 263 ? -25.286 32.728 -37.089 1.00 79.24  ?  263 PRO   A N     1 
ATOM   2017 C CA    . PRO   A 1 263 ? -26.056 31.707 -36.395 1.00 85.55  ?  263 PRO   A CA    1 
ATOM   2018 C C     . PRO   A 1 263 ? -27.559 31.609 -36.597 1.00 87.25  ?  263 PRO   A C     1 
ATOM   2019 O O     . PRO   A 1 263 ? -28.171 32.580 -37.060 1.00 85.89  ?  263 PRO   A O     1 
ATOM   2020 C CB    . PRO   A 1 263 ? -25.688 32.054 -34.947 1.00 84.48  ?  263 PRO   A CB    1 
ATOM   2021 C CG    . PRO   A 1 263 ? -24.493 32.951 -35.044 1.00 78.45  ?  263 PRO   A CG    1 
ATOM   2022 C CD    . PRO   A 1 263 ? -24.918 33.822 -36.178 1.00 76.59  ?  263 PRO   A CD    1 
ATOM   2023 N N     . ASP   A 1 264 ? -28.133 30.461 -36.233 1.00 85.84  ?  264 ASP   A N     1 
ATOM   2024 C CA    . ASP   A 1 264 ? -29.582 30.210 -36.450 1.00 92.75  ?  264 ASP   A CA    1 
ATOM   2025 C C     . ASP   A 1 264 ? -30.390 30.678 -35.256 1.00 94.86  ?  264 ASP   A C     1 
ATOM   2026 O O     . ASP   A 1 264 ? -31.277 29.924 -34.828 1.00 99.56  ?  264 ASP   A O     1 
ATOM   2027 C CB    . ASP   A 1 264 ? -29.856 28.728 -36.589 1.00 91.98  ?  264 ASP   A CB    1 
ATOM   2028 C CG    . ASP   A 1 264 ? -28.630 27.836 -36.519 1.00 100.19 ?  264 ASP   A CG    1 
ATOM   2029 O OD1   . ASP   A 1 264 ? -28.032 27.754 -35.430 1.00 101.55 ?  264 ASP   A OD1   1 
ATOM   2030 O OD2   . ASP   A 1 264 ? -28.295 27.224 -37.553 1.00 96.48  ?  264 ASP   A OD2   1 
ATOM   2031 N N     . HIS   A 1 265 ? -30.138 31.888 -34.783 1.00 97.42  ?  265 HIS   A N     1 
ATOM   2032 C CA    . HIS   A 1 265 ? -30.769 32.337 -33.527 1.00 96.64  ?  265 HIS   A CA    1 
ATOM   2033 C C     . HIS   A 1 265 ? -30.294 33.759 -33.306 1.00 97.57  ?  265 HIS   A C     1 
ATOM   2034 O O     . HIS   A 1 265 ? -29.446 34.217 -34.080 1.00 100.95 ?  265 HIS   A O     1 
ATOM   2035 C CB    . HIS   A 1 265 ? -30.364 31.410 -32.393 1.00 94.32  ?  265 HIS   A CB    1 
ATOM   2036 C CG    . HIS   A 1 265 ? -28.928 31.024 -32.377 1.00 97.13  ?  265 HIS   A CG    1 
ATOM   2037 N ND1   . HIS   A 1 265 ? -28.508 29.792 -32.822 1.00 102.82 ?  265 HIS   A ND1   1 
ATOM   2038 C CD2   . HIS   A 1 265 ? -27.835 31.665 -31.970 1.00 92.86  ?  265 HIS   A CD2   1 
ATOM   2039 C CE1   . HIS   A 1 265 ? -27.196 29.708 -32.694 1.00 97.62  ?  265 HIS   A CE1   1 
ATOM   2040 N NE2   . HIS   A 1 265 ? -26.770 30.837 -32.184 1.00 95.75  ?  265 HIS   A NE2   1 
ATOM   2041 N N     . PRO   A 1 266 ? -30.763 34.488 -32.280 1.00 99.80  ?  266 PRO   A N     1 
ATOM   2042 C CA    . PRO   A 1 266 ? -30.113 35.703 -31.858 1.00 99.54  ?  266 PRO   A CA    1 
ATOM   2043 C C     . PRO   A 1 266 ? -29.263 35.389 -30.670 1.00 96.88  ?  266 PRO   A C     1 
ATOM   2044 O O     . PRO   A 1 266 ? -29.223 34.236 -30.236 1.00 95.27  ?  266 PRO   A O     1 
ATOM   2045 C CB    . PRO   A 1 266 ? -31.283 36.615 -31.533 1.00 100.85 ?  266 PRO   A CB    1 
ATOM   2046 C CG    . PRO   A 1 266 ? -32.515 35.807 -31.872 1.00 99.79  ?  266 PRO   A CG    1 
ATOM   2047 C CD    . PRO   A 1 266 ? -32.096 34.370 -31.678 1.00 100.45 ?  266 PRO   A CD    1 
ATOM   2048 N N     . VAL   A 1 267 ? -28.584 36.403 -30.159 1.00 95.01  ?  267 VAL   A N     1 
ATOM   2049 C CA    . VAL   A 1 267 ? -27.643 36.207 -29.030 1.00 95.28  ?  267 VAL   A CA    1 
ATOM   2050 C C     . VAL   A 1 267 ? -28.352 35.601 -27.823 1.00 98.53  ?  267 VAL   A C     1 
ATOM   2051 O O     . VAL   A 1 267 ? -29.576 35.708 -27.747 1.00 98.12  ?  267 VAL   A O     1 
ATOM   2052 C CB    . VAL   A 1 267 ? -27.047 37.574 -28.661 1.00 96.19  ?  267 VAL   A CB    1 
ATOM   2053 C CG1   . VAL   A 1 267 ? -26.112 38.086 -29.746 1.00 93.57  ?  267 VAL   A CG1   1 
ATOM   2054 C CG2   . VAL   A 1 267 ? -28.132 38.602 -28.384 1.00 95.85  ?  267 VAL   A CG2   1 
ATOM   2055 N N     . PHE   A 1 268 ? -27.575 35.022 -26.912 1.00 98.24  ?  268 PHE   A N     1 
ATOM   2056 C CA    . PHE   A 1 268 ? -28.107 34.444 -25.647 1.00 98.49  ?  268 PHE   A CA    1 
ATOM   2057 C C     . PHE   A 1 268 ? -28.869 33.183 -25.976 1.00 97.07  ?  268 PHE   A C     1 
ATOM   2058 O O     . PHE   A 1 268 ? -29.267 32.457 -25.045 1.00 91.57  ?  268 PHE   A O     1 
ATOM   2059 C CB    . PHE   A 1 268 ? -28.946 35.426 -24.822 1.00 103.56 ?  268 PHE   A CB    1 
ATOM   2060 C CG    . PHE   A 1 268 ? -28.594 36.907 -24.851 1.00 101.65 ?  268 PHE   A CG    1 
ATOM   2061 C CD1   . PHE   A 1 268 ? -27.310 37.350 -24.561 1.00 96.91  ?  268 PHE   A CD1   1 
ATOM   2062 C CD2   . PHE   A 1 268 ? -29.567 37.858 -25.135 1.00 102.89 ?  268 PHE   A CD2   1 
ATOM   2063 C CE1   . PHE   A 1 268 ? -27.011 38.702 -24.577 1.00 96.56  ?  268 PHE   A CE1   1 
ATOM   2064 C CE2   . PHE   A 1 268 ? -29.264 39.209 -25.144 1.00 98.36  ?  268 PHE   A CE2   1 
ATOM   2065 C CZ    . PHE   A 1 268 ? -27.986 39.626 -24.867 1.00 96.67  ?  268 PHE   A CZ    1 
ATOM   2066 N N     . SER   A 1 269 ? -28.998 32.890 -27.266 1.00 98.93  ?  269 SER   A N     1 
ATOM   2067 C CA    . SER   A 1 269 ? -29.782 31.702 -27.690 1.00 102.38 ?  269 SER   A CA    1 
ATOM   2068 C C     . SER   A 1 269 ? -29.112 30.386 -27.286 1.00 98.61  ?  269 SER   A C     1 
ATOM   2069 O O     . SER   A 1 269 ? -29.705 29.648 -26.495 1.00 100.02 ?  269 SER   A O     1 
ATOM   2070 C CB    . SER   A 1 269 ? -30.007 31.725 -29.146 1.00 96.55  ?  269 SER   A CB    1 
ATOM   2071 O OG    . SER   A 1 269 ? -30.979 32.716 -29.430 1.00 97.72  ?  269 SER   A OG    1 
ATOM   2072 N N     . SER   A 1 270 ? -27.975 30.068 -27.879 1.00 94.76  ?  270 SER   A N     1 
ATOM   2073 C CA    . SER   A 1 270 ? -27.278 28.852 -27.415 1.00 95.10  ?  270 SER   A CA    1 
ATOM   2074 C C     . SER   A 1 270 ? -25.996 29.286 -26.711 1.00 97.90  ?  270 SER   A C     1 
ATOM   2075 O O     . SER   A 1 270 ? -25.885 29.050 -25.498 1.00 103.61 ?  270 SER   A O     1 
ATOM   2076 C CB    . SER   A 1 270 ? -27.004 27.920 -28.536 1.00 101.81 ?  270 SER   A CB    1 
ATOM   2077 O OG    . SER   A 1 270 ? -27.514 26.626 -28.243 1.00 103.49 ?  270 SER   A OG    1 
ATOM   2078 N N     . ALA   A 1 271 ? -25.081 29.912 -27.437 1.00 98.69  ?  271 ALA   A N     1 
ATOM   2079 C CA    . ALA   A 1 271 ? -23.886 30.462 -26.754 1.00 98.76  ?  271 ALA   A CA    1 
ATOM   2080 C C     . ALA   A 1 271 ? -23.226 31.511 -27.641 1.00 90.39  ?  271 ALA   A C     1 
ATOM   2081 O O     . ALA   A 1 271 ? -23.511 31.580 -28.856 1.00 80.19  ?  271 ALA   A O     1 
ATOM   2082 C CB    . ALA   A 1 271 ? -22.907 29.376 -26.336 1.00 86.52  ?  271 ALA   A CB    1 
ATOM   2083 N N     . THR   A 1 272 ? -22.401 32.339 -27.015 1.00 93.83  ?  272 THR   A N     1 
ATOM   2084 C CA    . THR   A 1 272 ? -21.682 33.392 -27.743 1.00 86.30  ?  272 THR   A CA    1 
ATOM   2085 C C     . THR   A 1 272 ? -20.220 33.186 -27.457 1.00 79.55  ?  272 THR   A C     1 
ATOM   2086 O O     . THR   A 1 272 ? -19.883 32.758 -26.339 1.00 77.42  ?  272 THR   A O     1 
ATOM   2087 C CB    . THR   A 1 272 ? -22.153 34.744 -27.222 1.00 85.19  ?  272 THR   A CB    1 
ATOM   2088 O OG1   . THR   A 1 272 ? -21.752 34.754 -25.855 1.00 85.78  ?  272 THR   A OG1   1 
ATOM   2089 C CG2   . THR   A 1 272 ? -23.654 34.931 -27.341 1.00 87.67  ?  272 THR   A CG2   1 
ATOM   2090 N N     . THR   A 1 273 ? -19.374 33.473 -28.428 1.00 70.92  ?  273 THR   A N     1 
ATOM   2091 C CA    . THR   A 1 273 ? -17.948 33.359 -28.139 1.00 72.38  ?  273 THR   A CA    1 
ATOM   2092 C C     . THR   A 1 273 ? -17.393 34.741 -27.923 1.00 65.21  ?  273 THR   A C     1 
ATOM   2093 O O     . THR   A 1 273 ? -17.792 35.655 -28.651 1.00 64.01  ?  273 THR   A O     1 
ATOM   2094 C CB    . THR   A 1 273 ? -17.278 32.580 -29.267 1.00 63.81  ?  273 THR   A CB    1 
ATOM   2095 O OG1   . THR   A 1 273 ? -17.957 31.333 -29.307 1.00 65.51  ?  273 THR   A OG1   1 
ATOM   2096 C CG2   . THR   A 1 273 ? -15.800 32.360 -29.019 1.00 54.42  ?  273 THR   A CG2   1 
ATOM   2097 N N     . LEU   A 1 274 ? -16.516 34.877 -26.942 1.00 56.12  ?  274 LEU   A N     1 
ATOM   2098 C CA    . LEU   A 1 274 ? -15.892 36.158 -26.622 1.00 60.69  ?  274 LEU   A CA    1 
ATOM   2099 C C     . LEU   A 1 274 ? -14.500 36.244 -27.240 1.00 52.09  ?  274 LEU   A C     1 
ATOM   2100 O O     . LEU   A 1 274 ? -13.638 35.406 -26.956 1.00 49.32  ?  274 LEU   A O     1 
ATOM   2101 C CB    . LEU   A 1 274 ? -15.797 36.340 -25.106 1.00 64.42  ?  274 LEU   A CB    1 
ATOM   2102 C CG    . LEU   A 1 274 ? -17.090 36.779 -24.425 1.00 63.85  ?  274 LEU   A CG    1 
ATOM   2103 C CD1   . LEU   A 1 274 ? -17.116 36.287 -23.013 1.00 62.11  ?  274 LEU   A CD1   1 
ATOM   2104 C CD2   . LEU   A 1 274 ? -17.219 38.293 -24.494 1.00 68.85  ?  274 LEU   A CD2   1 
ATOM   2105 N N     . SER   A 1 275 ? -14.275 37.270 -28.056 1.00 50.09  ?  275 SER   A N     1 
ATOM   2106 C CA    . SER   A 1 275 ? -12.943 37.545 -28.574 1.00 48.54  ?  275 SER   A CA    1 
ATOM   2107 C C     . SER   A 1 275 ? -12.756 39.032 -28.794 1.00 47.90  ?  275 SER   A C     1 
ATOM   2108 O O     . SER   A 1 275 ? -13.698 39.755 -29.109 1.00 51.66  ?  275 SER   A O     1 
ATOM   2109 C CB    . SER   A 1 275 ? -12.648 36.838 -29.901 1.00 48.31  ?  275 SER   A CB    1 
ATOM   2110 O OG    . SER   A 1 275 ? -11.245 36.848 -30.132 1.00 42.21  ?  275 SER   A OG    1 
ATOM   2111 N N     . ASP   A 1 276 ? -11.512 39.468 -28.662 1.00 51.96  ?  276 ASP   A N     1 
ATOM   2112 C CA    . ASP   A 1 276 ? -11.102 40.792 -29.098 1.00 45.60  ?  276 ASP   A CA    1 
ATOM   2113 C C     . ASP   A 1 276 ? -10.364 40.762 -30.424 1.00 45.37  ?  276 ASP   A C     1 
ATOM   2114 O O     . ASP   A 1 276 ? -10.181 41.815 -31.033 1.00 51.59  ?  276 ASP   A O     1 
ATOM   2115 C CB    . ASP   A 1 276 ? -10.194 41.432 -28.044 1.00 47.12  ?  276 ASP   A CB    1 
ATOM   2116 C CG    . ASP   A 1 276 ? -10.965 42.081 -26.934 1.00 50.52  ?  276 ASP   A CG    1 
ATOM   2117 O OD1   . ASP   A 1 276 ? -12.194 42.243 -27.083 1.00 53.18  ?  276 ASP   A OD1   1 
ATOM   2118 O OD2   . ASP   A 1 276 ? -10.335 42.433 -25.915 1.00 57.53  ?  276 ASP   A OD2   1 
ATOM   2119 N N     . GLU   A 1 277 ? -9.952  39.584 -30.884 1.00 42.68  ?  277 GLU   A N     1 
ATOM   2120 C CA    . GLU   A 1 277 ? -8.950  39.428 -31.928 1.00 42.75  ?  277 GLU   A CA    1 
ATOM   2121 C C     . GLU   A 1 277 ? -9.476  38.860 -33.238 1.00 45.25  ?  277 GLU   A C     1 
ATOM   2122 O O     . GLU   A 1 277 ? -9.139  39.377 -34.306 1.00 43.01  ?  277 GLU   A O     1 
ATOM   2123 C CB    . GLU   A 1 277 ? -7.841  38.510 -31.425 1.00 37.30  ?  277 GLU   A CB    1 
ATOM   2124 C CG    . GLU   A 1 277 ? -7.116  39.037 -30.269 1.00 44.47  ?  277 GLU   A CG    1 
ATOM   2125 C CD    . GLU   A 1 277 ? -5.830  38.298 -30.049 1.00 54.94  ?  277 GLU   A CD    1 
ATOM   2126 O OE1   . GLU   A 1 277 ? -5.708  37.647 -28.988 1.00 56.40  ?  277 GLU   A OE1   1 
ATOM   2127 O OE2   . GLU   A 1 277 ? -4.951  38.359 -30.947 1.00 55.68  ?  277 GLU   A OE2   1 
ATOM   2128 N N     . ILE   A 1 278 ? -10.303 37.814 -33.178 1.00 42.48  ?  278 ILE   A N     1 
ATOM   2129 C CA    . ILE   A 1 278 ? -10.468 36.920 -34.321 1.00 47.24  ?  278 ILE   A CA    1 
ATOM   2130 C C     . ILE   A 1 278 ? -11.007 37.663 -35.548 1.00 46.68  ?  278 ILE   A C     1 
ATOM   2131 O O     . ILE   A 1 278 ? -10.550 37.422 -36.672 1.00 50.08  ?  278 ILE   A O     1 
ATOM   2132 C CB    . ILE   A 1 278 ? -11.334 35.703 -33.930 1.00 44.79  ?  278 ILE   A CB    1 
ATOM   2133 C CG1   . ILE   A 1 278 ? -11.127 34.571 -34.936 1.00 42.03  ?  278 ILE   A CG1   1 
ATOM   2134 C CG2   . ILE   A 1 278 ? -12.804 36.069 -33.742 1.00 45.67  ?  278 ILE   A CG2   1 
ATOM   2135 C CD1   . ILE   A 1 278 ? -9.714  34.044 -34.930 1.00 44.01  ?  278 ILE   A CD1   1 
ATOM   2136 N N     . LEU   A 1 279 ? -11.935 38.609 -35.361 1.00 44.89  ?  279 LEU   A N     1 
ATOM   2137 C CA    . LEU   A 1 279 ? -12.440 39.357 -36.516 1.00 48.51  ?  279 LEU   A CA    1 
ATOM   2138 C C     . LEU   A 1 279 ? -11.332 40.174 -37.179 1.00 48.54  ?  279 LEU   A C     1 
ATOM   2139 O O     . LEU   A 1 279 ? -11.194 40.156 -38.407 1.00 50.47  ?  279 LEU   A O     1 
ATOM   2140 C CB    . LEU   A 1 279 ? -13.608 40.259 -36.112 1.00 52.04  ?  279 LEU   A CB    1 
ATOM   2141 C CG    . LEU   A 1 279 ? -14.855 39.583 -35.519 1.00 57.94  ?  279 LEU   A CG    1 
ATOM   2142 C CD1   . LEU   A 1 279 ? -16.020 40.567 -35.461 1.00 53.23  ?  279 LEU   A CD1   1 
ATOM   2143 C CD2   . LEU   A 1 279 ? -15.247 38.307 -36.272 1.00 53.51  ?  279 LEU   A CD2   1 
ATOM   2144 N N     . SER   A 1 280 ? -10.513 40.870 -36.385 1.00 46.19  ?  280 SER   A N     1 
ATOM   2145 C CA    . SER   A 1 280 ? -9.410  41.635 -36.956 1.00 43.60  ?  280 SER   A CA    1 
ATOM   2146 C C     . SER   A 1 280 ? -8.340  40.726 -37.550 1.00 46.59  ?  280 SER   A C     1 
ATOM   2147 O O     . SER   A 1 280 ? -7.711  41.081 -38.558 1.00 44.20  ?  280 SER   A O     1 
ATOM   2148 C CB    . SER   A 1 280 ? -8.789  42.550 -35.906 1.00 46.93  ?  280 SER   A CB    1 
ATOM   2149 O OG    . SER   A 1 280 ? -7.522  43.019 -36.348 1.00 50.87  ?  280 SER   A OG    1 
ATOM   2150 N N     . ARG   A 1 281 ? -8.098  39.561 -36.942 1.00 44.03  ?  281 ARG   A N     1 
ATOM   2151 C CA    . ARG   A 1 281 ? -7.143  38.637 -37.552 1.00 48.50  ?  281 ARG   A CA    1 
ATOM   2152 C C     . ARG   A 1 281 ? -7.618  38.212 -38.939 1.00 54.41  ?  281 ARG   A C     1 
ATOM   2153 O O     . ARG   A 1 281 ? -6.822  38.176 -39.895 1.00 51.07  ?  281 ARG   A O     1 
ATOM   2154 C CB    . ARG   A 1 281 ? -6.908  37.421 -36.655 1.00 47.17  ?  281 ARG   A CB    1 
ATOM   2155 C CG    . ARG   A 1 281 ? -6.247  37.764 -35.325 1.00 41.62  ?  281 ARG   A CG    1 
ATOM   2156 C CD    . ARG   A 1 281 ? -5.198  38.852 -35.508 1.00 43.16  ?  281 ARG   A CD    1 
ATOM   2157 N NE    . ARG   A 1 281 ? -3.904  38.293 -35.887 1.00 48.76  ?  281 ARG   A NE    1 
ATOM   2158 C CZ    . ARG   A 1 281 ? -2.997  38.931 -36.616 1.00 42.36  ?  281 ARG   A CZ    1 
ATOM   2159 N NH1   . ARG   A 1 281 ? -3.248  40.151 -37.050 1.00 45.93  ?  281 ARG   A NH1   1 
ATOM   2160 N NH2   . ARG   A 1 281 ? -1.850  38.348 -36.920 1.00 38.22  ?  281 ARG   A NH2   1 
ATOM   2161 N N     . ILE   A 1 282 ? -8.923  37.926 -39.081 1.00 48.06  ?  282 ILE   A N     1 
ATOM   2162 C CA    . ILE   A 1 282 ? -9.463  37.645 -40.405 1.00 46.60  ?  282 ILE   A CA    1 
ATOM   2163 C C     . ILE   A 1 282 ? -9.142  38.796 -41.352 1.00 50.64  ?  282 ILE   A C     1 
ATOM   2164 O O     . ILE   A 1 282 ? -8.509  38.600 -42.398 1.00 53.90  ?  282 ILE   A O     1 
ATOM   2165 C CB    . ILE   A 1 282 ? -10.978 37.376 -40.335 1.00 50.30  ?  282 ILE   A CB    1 
ATOM   2166 C CG1   . ILE   A 1 282 ? -11.261 36.022 -39.696 1.00 48.53  ?  282 ILE   A CG1   1 
ATOM   2167 C CG2   . ILE   A 1 282 ? -11.613 37.417 -41.744 1.00 40.56  ?  282 ILE   A CG2   1 
ATOM   2168 C CD1   . ILE   A 1 282 ? -12.712 35.805 -39.396 1.00 46.03  ?  282 ILE   A CD1   1 
ATOM   2169 N N     . ARG   A 1 283 ? -9.527  40.024 -40.973 1.00 45.32  ?  283 ARG   A N     1 
ATOM   2170 C CA    . ARG   A 1 283 ? -9.381  41.181 -41.848 1.00 44.54  ?  283 ARG   A CA    1 
ATOM   2171 C C     . ARG   A 1 283 ? -7.930  41.531 -42.167 1.00 50.17  ?  283 ARG   A C     1 
ATOM   2172 O O     . ARG   A 1 283 ? -7.693  42.302 -43.109 1.00 49.10  ?  283 ARG   A O     1 
ATOM   2173 C CB    . ARG   A 1 283 ? -10.081 42.389 -41.238 1.00 43.83  ?  283 ARG   A CB    1 
ATOM   2174 C CG    . ARG   A 1 283 ? -11.578 42.242 -41.249 1.00 48.65  ?  283 ARG   A CG    1 
ATOM   2175 C CD    . ARG   A 1 283 ? -12.209 43.093 -42.333 1.00 51.68  ?  283 ARG   A CD    1 
ATOM   2176 N NE    . ARG   A 1 283 ? -13.563 42.656 -42.671 1.00 52.47  ?  283 ARG   A NE    1 
ATOM   2177 C CZ    . ARG   A 1 283 ? -14.629 43.443 -42.598 1.00 56.75  ?  283 ARG   A CZ    1 
ATOM   2178 N NH1   . ARG   A 1 283 ? -14.490 44.692 -42.173 1.00 61.08  ?  283 ARG   A NH1   1 
ATOM   2179 N NH2   . ARG   A 1 283 ? -15.829 42.983 -42.924 1.00 62.48  ?  283 ARG   A NH2   1 
ATOM   2180 N N     . HIS   A 1 284 ? -6.959  40.986 -41.437 1.00 49.24  ?  284 HIS   A N     1 
ATOM   2181 C CA    . HIS   A 1 284 ? -5.558  41.154 -41.791 1.00 47.47  ?  284 HIS   A CA    1 
ATOM   2182 C C     . HIS   A 1 284 ? -5.001  39.977 -42.584 1.00 48.01  ?  284 HIS   A C     1 
ATOM   2183 O O     . HIS   A 1 284 ? -3.807  39.965 -42.891 1.00 48.45  ?  284 HIS   A O     1 
ATOM   2184 C CB    . HIS   A 1 284 ? -4.724  41.400 -40.532 1.00 48.82  ?  284 HIS   A CB    1 
ATOM   2185 C CG    . HIS   A 1 284 ? -4.994  42.724 -39.894 1.00 46.47  ?  284 HIS   A CG    1 
ATOM   2186 N ND1   . HIS   A 1 284 ? -6.099  42.960 -39.103 1.00 53.16  ?  284 HIS   A ND1   1 
ATOM   2187 C CD2   . HIS   A 1 284 ? -4.333  43.900 -39.973 1.00 45.87  ?  284 HIS   A CD2   1 
ATOM   2188 C CE1   . HIS   A 1 284 ? -6.090  44.216 -38.697 1.00 48.57  ?  284 HIS   A CE1   1 
ATOM   2189 N NE2   . HIS   A 1 284 ? -5.030  44.809 -39.213 1.00 49.18  ?  284 HIS   A NE2   1 
ATOM   2190 N N     . GLY   A 1 285 ? -5.839  39.006 -42.952 1.00 49.90  ?  285 GLY   A N     1 
ATOM   2191 C CA    . GLY   A 1 285 ? -5.368  37.799 -43.591 1.00 42.35  ?  285 GLY   A CA    1 
ATOM   2192 C C     . GLY   A 1 285 ? -4.689  36.796 -42.679 1.00 49.20  ?  285 GLY   A C     1 
ATOM   2193 O O     . GLY   A 1 285 ? -4.271  35.732 -43.155 1.00 54.62  ?  285 GLY   A O     1 
ATOM   2194 N N     . ALA   A 1 286 ? -4.571  37.069 -41.381 1.00 47.77  ?  286 ALA   A N     1 
ATOM   2195 C CA    . ALA   A 1 286 ? -3.858  36.129 -40.532 1.00 44.77  ?  286 ALA   A CA    1 
ATOM   2196 C C     . ALA   A 1 286 ? -4.649  34.856 -40.262 1.00 44.35  ?  286 ALA   A C     1 
ATOM   2197 O O     . ALA   A 1 286 ? -4.041  33.826 -39.954 1.00 43.74  ?  286 ALA   A O     1 
ATOM   2198 C CB    . ALA   A 1 286 ? -3.472  36.805 -39.219 1.00 48.42  ?  286 ALA   A CB    1 
ATOM   2199 N N     . VAL   A 1 287 ? -5.978  34.902 -40.349 1.00 43.25  ?  287 VAL   A N     1 
ATOM   2200 C CA    . VAL   A 1 287 ? -6.820  33.720 -40.192 1.00 46.73  ?  287 VAL   A CA    1 
ATOM   2201 C C     . VAL   A 1 287 ? -7.815  33.687 -41.339 1.00 49.15  ?  287 VAL   A C     1 
ATOM   2202 O O     . VAL   A 1 287 ? -8.502  34.682 -41.599 1.00 51.32  ?  287 VAL   A O     1 
ATOM   2203 C CB    . VAL   A 1 287 ? -7.563  33.695 -38.839 1.00 46.58  ?  287 VAL   A CB    1 
ATOM   2204 C CG1   . VAL   A 1 287 ? -8.469  32.456 -38.738 1.00 41.92  ?  287 VAL   A CG1   1 
ATOM   2205 C CG2   . VAL   A 1 287 ? -6.583  33.677 -37.697 1.00 44.15  ?  287 VAL   A CG2   1 
ATOM   2206 N N     . THR   A 1 288 ? -7.913  32.542 -42.013 1.00 43.98  ?  288 THR   A N     1 
ATOM   2207 C CA    . THR   A 1 288 ? -8.843  32.436 -43.126 1.00 47.95  ?  288 THR   A CA    1 
ATOM   2208 C C     . THR   A 1 288 ? -10.049 31.602 -42.722 1.00 49.31  ?  288 THR   A C     1 
ATOM   2209 O O     . THR   A 1 288 ? -9.898  30.425 -42.353 1.00 46.64  ?  288 THR   A O     1 
ATOM   2210 C CB    . THR   A 1 288 ? -8.160  31.834 -44.356 1.00 52.77  ?  288 THR   A CB    1 
ATOM   2211 O OG1   . THR   A 1 288 ? -6.839  32.384 -44.490 1.00 48.33  ?  288 THR   A OG1   1 
ATOM   2212 C CG2   . THR   A 1 288 ? -8.962  32.164 -45.587 1.00 50.97  ?  288 THR   A CG2   1 
ATOM   2213 N N     . PRO   A 1 289 ? -11.253 32.166 -42.757 1.00 52.85  ?  289 PRO   A N     1 
ATOM   2214 C CA    . PRO   A 1 289 ? -12.442 31.370 -42.439 1.00 49.38  ?  289 PRO   A CA    1 
ATOM   2215 C C     . PRO   A 1 289 ? -12.712 30.360 -43.538 1.00 50.56  ?  289 PRO   A C     1 
ATOM   2216 O O     . PRO   A 1 289 ? -12.365 30.573 -44.699 1.00 57.48  ?  289 PRO   A O     1 
ATOM   2217 C CB    . PRO   A 1 289 ? -13.561 32.413 -42.334 1.00 49.19  ?  289 PRO   A CB    1 
ATOM   2218 C CG    . PRO   A 1 289 ? -13.067 33.592 -43.123 1.00 49.39  ?  289 PRO   A CG    1 
ATOM   2219 C CD    . PRO   A 1 289 ? -11.568 33.575 -43.056 1.00 50.42  ?  289 PRO   A CD    1 
ATOM   2220 N N     . LYS   A 1 290 ? -13.308 29.238 -43.149 1.00 48.46  ?  290 LYS   A N     1 
ATOM   2221 C CA    . LYS   A 1 290 ? -13.578 28.105 -44.020 1.00 47.55  ?  290 LYS   A CA    1 
ATOM   2222 C C     . LYS   A 1 290 ? -14.811 27.392 -43.502 1.00 58.64  ?  290 LYS   A C     1 
ATOM   2223 O O     . LYS   A 1 290 ? -15.080 27.415 -42.288 1.00 57.03  ?  290 LYS   A O     1 
ATOM   2224 C CB    . LYS   A 1 290 ? -12.399 27.120 -44.062 1.00 52.16  ?  290 LYS   A CB    1 
ATOM   2225 C CG    . LYS   A 1 290 ? -11.241 27.515 -44.967 1.00 55.02  ?  290 LYS   A CG    1 
ATOM   2226 C CD    . LYS   A 1 290 ? -11.583 27.349 -46.437 1.00 54.61  ?  290 LYS   A CD    1 
ATOM   2227 C CE    . LYS   A 1 290 ? -10.432 27.820 -47.314 1.00 51.78  ?  290 LYS   A CE    1 
ATOM   2228 N NZ    . LYS   A 1 290 ? -10.919 28.317 -48.627 1.00 58.96  ?  290 LYS   A NZ    1 
ATOM   2229 N N     . PRO   A 1 291 ? -15.571 26.715 -44.375 1.00 61.18  ?  291 PRO   A N     1 
ATOM   2230 C CA    . PRO   A 1 291 ? -16.702 25.906 -43.902 1.00 62.13  ?  291 PRO   A CA    1 
ATOM   2231 C C     . PRO   A 1 291 ? -16.237 24.626 -43.221 1.00 58.68  ?  291 PRO   A C     1 
ATOM   2232 O O     . PRO   A 1 291 ? -15.067 24.503 -42.850 1.00 55.94  ?  291 PRO   A O     1 
ATOM   2233 C CB    . PRO   A 1 291 ? -17.478 25.609 -45.188 1.00 60.21  ?  291 PRO   A CB    1 
ATOM   2234 C CG    . PRO   A 1 291 ? -16.396 25.531 -46.224 1.00 61.89  ?  291 PRO   A CG    1 
ATOM   2235 C CD    . PRO   A 1 291 ? -15.354 26.560 -45.826 1.00 59.16  ?  291 PRO   A CD    1 
ATOM   2236 N N     . ALA   A 1 292 ? -17.133 23.661 -43.059 1.00 61.54  ?  292 ALA   A N     1 
ATOM   2237 C CA    . ALA   A 1 292 ? -16.745 22.436 -42.377 1.00 61.28  ?  292 ALA   A CA    1 
ATOM   2238 C C     . ALA   A 1 292 ? -15.708 21.666 -43.199 1.00 60.22  ?  292 ALA   A C     1 
ATOM   2239 O O     . ALA   A 1 292 ? -15.656 21.760 -44.429 1.00 56.65  ?  292 ALA   A O     1 
ATOM   2240 C CB    . ALA   A 1 292 ? -17.973 21.572 -42.100 1.00 51.48  ?  292 ALA   A CB    1 
ATOM   2241 N N     . ILE   A 1 293 ? -14.844 20.932 -42.494 1.00 61.40  ?  293 ILE   A N     1 
ATOM   2242 C CA    . ILE   A 1 293 ? -13.915 20.026 -43.159 1.00 59.43  ?  293 ILE   A CA    1 
ATOM   2243 C C     . ILE   A 1 293 ? -14.708 18.898 -43.800 1.00 72.08  ?  293 ILE   A C     1 
ATOM   2244 O O     . ILE   A 1 293 ? -15.579 18.287 -43.160 1.00 66.77  ?  293 ILE   A O     1 
ATOM   2245 C CB    . ILE   A 1 293 ? -12.889 19.459 -42.171 1.00 55.38  ?  293 ILE   A CB    1 
ATOM   2246 C CG1   . ILE   A 1 293 ? -11.877 20.513 -41.748 1.00 49.95  ?  293 ILE   A CG1   1 
ATOM   2247 C CG2   . ILE   A 1 293 ? -12.177 18.278 -42.791 1.00 61.92  ?  293 ILE   A CG2   1 
ATOM   2248 C CD1   . ILE   A 1 293 ? -10.746 19.939 -40.899 1.00 52.11  ?  293 ILE   A CD1   1 
ATOM   2249 N N     . ALA   A 1 294 ? -14.383 18.562 -45.038 1.00 71.67  ?  294 ALA   A N     1 
ATOM   2250 C CA    . ALA   A 1 294 ? -15.090 17.515 -45.757 1.00 67.27  ?  294 ALA   A CA    1 
ATOM   2251 C C     . ALA   A 1 294 ? -14.334 16.242 -45.905 1.00 65.89  ?  294 ALA   A C     1 
ATOM   2252 O O     . ALA   A 1 294 ? -14.907 15.231 -45.981 1.00 70.77  ?  294 ALA   A O     1 
ATOM   2253 C CB    . ALA   A 1 294 ? -15.506 18.024 -47.093 1.00 64.48  ?  294 ALA   A CB    1 
ATOM   2254 N N     . SER   A 1 295 ? -13.025 16.304 -45.942 1.00 62.69  ?  295 SER   A N     1 
ATOM   2255 C CA    . SER   A 1 295 ? -12.205 15.127 -46.053 1.00 59.40  ?  295 SER   A CA    1 
ATOM   2256 C C     . SER   A 1 295 ? -10.749 15.470 -45.975 1.00 59.54  ?  295 SER   A C     1 
ATOM   2257 O O     . SER   A 1 295 ? -10.391 16.583 -46.090 1.00 59.36  ?  295 SER   A O     1 
ATOM   2258 C CB    . SER   A 1 295 ? -12.540 14.376 -47.307 1.00 62.21  ?  295 SER   A CB    1 
ATOM   2259 O OG    . SER   A 1 295 ? -11.656 14.601 -48.355 1.00 57.03  ?  295 SER   A OG    1 
ATOM   2260 N N     . PHE   A 1 296 ? -9.915  14.491 -45.747 1.00 61.13  ?  296 PHE   A N     1 
ATOM   2261 C CA    . PHE   A 1 296 ? -8.510  14.708 -45.661 1.00 65.06  ?  296 PHE   A CA    1 
ATOM   2262 C C     . PHE   A 1 296 ? -8.025  13.995 -46.845 1.00 67.80  ?  296 PHE   A C     1 
ATOM   2263 O O     . PHE   A 1 296 ? -8.233  12.853 -46.969 1.00 70.32  ?  296 PHE   A O     1 
ATOM   2264 C CB    . PHE   A 1 296 ? -7.894  14.066 -44.428 1.00 66.89  ?  296 PHE   A CB    1 
ATOM   2265 C CG    . PHE   A 1 296 ? -8.480  14.519 -43.156 1.00 68.13  ?  296 PHE   A CG    1 
ATOM   2266 C CD1   . PHE   A 1 296 ? -8.170  15.732 -42.636 1.00 74.72  ?  296 PHE   A CD1   1 
ATOM   2267 C CD2   . PHE   A 1 296 ? -9.361  13.753 -42.507 1.00 64.60  ?  296 PHE   A CD2   1 
ATOM   2268 C CE1   . PHE   A 1 296 ? -8.749  16.165 -41.483 1.00 68.91  ?  296 PHE   A CE1   1 
ATOM   2269 C CE2   . PHE   A 1 296 ? -9.938  14.174 -41.368 1.00 62.88  ?  296 PHE   A CE2   1 
ATOM   2270 C CZ    . PHE   A 1 296 ? -9.629  15.365 -40.847 1.00 68.89  ?  296 PHE   A CZ    1 
ATOM   2271 N N     . ASP   A 1 297 ? -7.368  14.695 -47.721 1.00 70.41  ?  297 ASP   A N     1 
ATOM   2272 C CA    . ASP   A 1 297 ? -6.883  14.130 -48.922 1.00 67.15  ?  297 ASP   A CA    1 
ATOM   2273 C C     . ASP   A 1 297 ? -5.449  13.757 -48.872 1.00 70.40  ?  297 ASP   A C     1 
ATOM   2274 O O     . ASP   A 1 297 ? -4.869  13.632 -49.882 1.00 78.74  ?  297 ASP   A O     1 
ATOM   2275 C CB    . ASP   A 1 297 ? -7.098  15.147 -50.008 1.00 70.11  ?  297 ASP   A CB    1 
ATOM   2276 C CG    . ASP   A 1 297 ? -7.327  14.537 -51.349 1.00 77.26  ?  297 ASP   A CG    1 
ATOM   2277 O OD1   . ASP   A 1 297 ? -6.714  13.520 -51.636 1.00 75.23  ?  297 ASP   A OD1   1 
ATOM   2278 O OD2   . ASP   A 1 297 ? -8.071  15.117 -52.140 1.00 66.74  ?  297 ASP   A OD2   1 
ATOM   2279 N N     . GLY   A 1 298 ? -4.891  13.521 -47.717 1.00 70.98  ?  298 GLY   A N     1 
ATOM   2280 C CA    . GLY   A 1 298 ? -3.511  13.107 -47.646 1.00 71.03  ?  298 GLY   A CA    1 
ATOM   2281 C C     . GLY   A 1 298 ? -2.614  14.167 -47.107 1.00 74.02  ?  298 GLY   A C     1 
ATOM   2282 O O     . GLY   A 1 298 ? -2.069  14.077 -46.027 1.00 65.93  ?  298 GLY   A O     1 
ATOM   2283 N N     . ASP   A 1 299 ? -2.481  15.198 -47.894 1.00 72.35  ?  299 ASP   A N     1 
ATOM   2284 C CA    . ASP   A 1 299 ? -1.671  16.294 -47.502 1.00 72.56  ?  299 ASP   A CA    1 
ATOM   2285 C C     . ASP   A 1 299 ? -2.499  17.492 -47.313 1.00 69.01  ?  299 ASP   A C     1 
ATOM   2286 O O     . ASP   A 1 299 ? -2.103  18.392 -46.656 1.00 65.54  ?  299 ASP   A O     1 
ATOM   2287 C CB    . ASP   A 1 299 ? -0.642  16.595 -48.556 1.00 73.37  ?  299 ASP   A CB    1 
ATOM   2288 C CG    . ASP   A 1 299 ? 0.394   17.496 -48.065 1.00 80.45  ?  299 ASP   A CG    1 
ATOM   2289 O OD1   . ASP   A 1 299 ? 0.566   17.642 -46.858 1.00 76.42  ?  299 ASP   A OD1   1 
ATOM   2290 O OD2   . ASP   A 1 299 ? 1.056   18.092 -48.879 1.00 81.15  ?  299 ASP   A OD2   1 
ATOM   2291 N N     . ARG   A 1 300 ? -3.659  17.496 -47.913 1.00 65.84  ?  300 ARG   A N     1 
ATOM   2292 C CA    . ARG   A 1 300 ? -4.519  18.612 -47.834 1.00 65.84  ?  300 ARG   A CA    1 
ATOM   2293 C C     . ARG   A 1 300 ? -5.751  18.331 -47.080 1.00 64.59  ?  300 ARG   A C     1 
ATOM   2294 O O     . ARG   A 1 300 ? -6.062  17.240 -46.832 1.00 61.04  ?  300 ARG   A O     1 
ATOM   2295 C CB    . ARG   A 1 300 ? -4.967  18.955 -49.237 1.00 64.72  ?  300 ARG   A CB    1 
ATOM   2296 C CG    . ARG   A 1 300 ? -3.897  18.886 -50.282 1.00 65.62  ?  300 ARG   A CG    1 
ATOM   2297 C CD    . ARG   A 1 300 ? -4.396  19.313 -51.637 1.00 57.08  ?  300 ARG   A CD    1 
ATOM   2298 N NE    . ARG   A 1 300 ? -4.686  20.718 -51.777 1.00 60.18  ?  300 ARG   A NE    1 
ATOM   2299 C CZ    . ARG   A 1 300 ? -3.784  21.643 -52.043 1.00 61.68  ?  300 ARG   A CZ    1 
ATOM   2300 N NH1   . ARG   A 1 300 ? -2.532  21.332 -52.153 1.00 60.56  ?  300 ARG   A NH1   1 
ATOM   2301 N NH2   . ARG   A 1 300 ? -4.136  22.885 -52.178 1.00 58.77  ?  300 ARG   A NH2   1 
ATOM   2302 N N     . VAL   A 1 301 ? -6.453  19.377 -46.736 1.00 60.14  ?  301 VAL   A N     1 
ATOM   2303 C CA    . VAL   A 1 301 ? -7.784  19.267 -46.163 1.00 62.12  ?  301 VAL   A CA    1 
ATOM   2304 C C     . VAL   A 1 301 ? -8.748  19.794 -47.211 1.00 57.36  ?  301 VAL   A C     1 
ATOM   2305 O O     . VAL   A 1 301 ? -8.476  20.814 -47.856 1.00 55.61  ?  301 VAL   A O     1 
ATOM   2306 C CB    . VAL   A 1 301 ? -7.914  20.042 -44.831 1.00 60.98  ?  301 VAL   A CB    1 
ATOM   2307 C CG1   . VAL   A 1 301 ? -9.378  20.217 -44.442 1.00 54.77  ?  301 VAL   A CG1   1 
ATOM   2308 C CG2   . VAL   A 1 301 ? -7.161  19.330 -43.711 1.00 58.03  ?  301 VAL   A CG2   1 
ATOM   2309 N N     . VAL   A 1 302 ? -9.856  19.090 -47.408 1.00 50.85  ?  302 VAL   A N     1 
ATOM   2310 C CA    . VAL   A 1 302 ? -10.887 19.540 -48.324 1.00 57.01  ?  302 VAL   A CA    1 
ATOM   2311 C C     . VAL   A 1 302 ? -12.063 20.014 -47.504 1.00 59.48  ?  302 VAL   A C     1 
ATOM   2312 O O     . VAL   A 1 302 ? -12.533 19.300 -46.613 1.00 66.51  ?  302 VAL   A O     1 
ATOM   2313 C CB    . VAL   A 1 302 ? -11.323 18.447 -49.309 1.00 58.89  ?  302 VAL   A CB    1 
ATOM   2314 C CG1   . VAL   A 1 302 ? -12.314 19.045 -50.306 1.00 59.04  ?  302 VAL   A CG1   1 
ATOM   2315 C CG2   . VAL   A 1 302 ? -10.113 17.859 -50.016 1.00 54.83  ?  302 VAL   A CG2   1 
ATOM   2316 N N     . PHE   A 1 303 ? -12.532 21.210 -47.801 1.00 58.74  ?  303 PHE   A N     1 
ATOM   2317 C CA    . PHE   A 1 303 ? -13.700 21.753 -47.141 1.00 59.17  ?  303 PHE   A CA    1 
ATOM   2318 C C     . PHE   A 1 303 ? -14.915 21.571 -48.029 1.00 64.28  ?  303 PHE   A C     1 
ATOM   2319 O O     . PHE   A 1 303 ? -14.811 21.385 -49.247 1.00 64.28  ?  303 PHE   A O     1 
ATOM   2320 C CB    . PHE   A 1 303 ? -13.482 23.225 -46.792 1.00 58.18  ?  303 PHE   A CB    1 
ATOM   2321 C CG    . PHE   A 1 303 ? -12.197 23.462 -46.056 1.00 59.92  ?  303 PHE   A CG    1 
ATOM   2322 C CD1   . PHE   A 1 303 ? -12.090 23.147 -44.712 1.00 60.36  ?  303 PHE   A CD1   1 
ATOM   2323 C CD2   . PHE   A 1 303 ? -11.079 23.933 -46.716 1.00 57.80  ?  303 PHE   A CD2   1 
ATOM   2324 C CE1   . PHE   A 1 303 ? -10.909 23.333 -44.031 1.00 54.47  ?  303 PHE   A CE1   1 
ATOM   2325 C CE2   . PHE   A 1 303 ? -9.895  24.119 -46.037 1.00 59.93  ?  303 PHE   A CE2   1 
ATOM   2326 C CZ    . PHE   A 1 303 ? -9.815  23.815 -44.692 1.00 53.53  ?  303 PHE   A CZ    1 
ATOM   2327 N N     . THR   A 1 304 ? -16.081 21.620 -47.387 1.00 67.68  ?  304 THR   A N     1 
ATOM   2328 C CA    . THR   A 1 304 ? -17.335 21.267 -48.030 1.00 61.74  ?  304 THR   A CA    1 
ATOM   2329 C C     . THR   A 1 304 ? -17.737 22.231 -49.133 1.00 60.25  ?  304 THR   A C     1 
ATOM   2330 O O     . THR   A 1 304 ? -18.690 21.931 -49.858 1.00 68.01  ?  304 THR   A O     1 
ATOM   2331 C CB    . THR   A 1 304 ? -18.449 21.193 -46.983 1.00 66.27  ?  304 THR   A CB    1 
ATOM   2332 O OG1   . THR   A 1 304 ? -18.681 22.496 -46.429 1.00 60.68  ?  304 THR   A OG1   1 
ATOM   2333 C CG2   . THR   A 1 304 ? -18.059 20.231 -45.872 1.00 64.13  ?  304 THR   A CG2   1 
ATOM   2334 N N     . ASP   A 1 305 ? -17.076 23.380 -49.265 1.00 57.53  ?  305 ASP   A N     1 
ATOM   2335 C CA    . ASP   A 1 305 ? -17.354 24.271 -50.384 1.00 57.12  ?  305 ASP   A CA    1 
ATOM   2336 C C     . ASP   A 1 305 ? -16.578 23.879 -51.630 1.00 57.50  ?  305 ASP   A C     1 
ATOM   2337 O O     . ASP   A 1 305 ? -16.599 24.613 -52.627 1.00 57.83  ?  305 ASP   A O     1 
ATOM   2338 C CB    . ASP   A 1 305 ? -17.059 25.731 -50.013 1.00 54.74  ?  305 ASP   A CB    1 
ATOM   2339 C CG    . ASP   A 1 305 ? -15.579 25.994 -49.760 1.00 59.56  ?  305 ASP   A CG    1 
ATOM   2340 O OD1   . ASP   A 1 305 ? -14.815 25.013 -49.585 1.00 56.87  ?  305 ASP   A OD1   1 
ATOM   2341 O OD2   . ASP   A 1 305 ? -15.182 27.190 -49.737 1.00 61.79  ?  305 ASP   A OD2   1 
ATOM   2342 N N     . GLY   A 1 306 ? -15.901 22.734 -51.594 1.00 58.61  ?  306 GLY   A N     1 
ATOM   2343 C CA    . GLY   A 1 306 ? -15.043 22.314 -52.669 1.00 59.57  ?  306 GLY   A CA    1 
ATOM   2344 C C     . GLY   A 1 306 ? -13.591 22.730 -52.528 1.00 63.78  ?  306 GLY   A C     1 
ATOM   2345 O O     . GLY   A 1 306 ? -12.726 22.128 -53.183 1.00 60.56  ?  306 GLY   A O     1 
ATOM   2346 N N     . THR   A 1 307 ? -13.286 23.728 -51.695 1.00 59.68  ?  307 THR   A N     1 
ATOM   2347 C CA    . THR   A 1 307 ? -11.910 24.202 -51.673 1.00 56.78  ?  307 THR   A CA    1 
ATOM   2348 C C     . THR   A 1 307 ? -11.024 23.257 -50.880 1.00 52.77  ?  307 THR   A C     1 
ATOM   2349 O O     . THR   A 1 307 ? -11.478 22.469 -50.048 1.00 55.07  ?  307 THR   A O     1 
ATOM   2350 C CB    . THR   A 1 307 ? -11.790 25.620 -51.100 1.00 56.49  ?  307 THR   A CB    1 
ATOM   2351 O OG1   . THR   A 1 307 ? -11.950 25.597 -49.669 1.00 54.61  ?  307 THR   A OG1   1 
ATOM   2352 C CG2   . THR   A 1 307 ? -12.810 26.552 -51.753 1.00 53.04  ?  307 THR   A CG2   1 
ATOM   2353 N N     . SER   A 1 308 ? -9.734  23.357 -51.157 1.00 57.51  ?  308 SER   A N     1 
ATOM   2354 C CA    . SER   A 1 308 ? -8.735  22.454 -50.625 1.00 56.82  ?  308 SER   A CA    1 
ATOM   2355 C C     . SER   A 1 308 ? -7.612  23.277 -50.022 1.00 56.88  ?  308 SER   A C     1 
ATOM   2356 O O     . SER   A 1 308 ? -7.444  24.454 -50.343 1.00 61.67  ?  308 SER   A O     1 
ATOM   2357 C CB    . SER   A 1 308 ? -8.230  21.521 -51.729 1.00 57.35  ?  308 SER   A CB    1 
ATOM   2358 O OG    . SER   A 1 308 ? -6.874  21.164 -51.585 1.00 59.95  ?  308 SER   A OG    1 
ATOM   2359 N N     . GLU   A 1 309 ? -6.848  22.655 -49.135 1.00 57.36  ?  309 GLU   A N     1 
ATOM   2360 C CA    . GLU   A 1 309 ? -5.789  23.408 -48.490 1.00 61.05  ?  309 GLU   A CA    1 
ATOM   2361 C C     . GLU   A 1 309 ? -4.704  22.483 -47.958 1.00 60.72  ?  309 GLU   A C     1 
ATOM   2362 O O     . GLU   A 1 309 ? -5.011  21.556 -47.200 1.00 63.14  ?  309 GLU   A O     1 
ATOM   2363 C CB    . GLU   A 1 309 ? -6.379  24.246 -47.361 1.00 61.21  ?  309 GLU   A CB    1 
ATOM   2364 C CG    . GLU   A 1 309 ? -5.554  25.459 -47.019 1.00 63.48  ?  309 GLU   A CG    1 
ATOM   2365 C CD    . GLU   A 1 309 ? -5.981  26.683 -47.787 1.00 62.54  ?  309 GLU   A CD    1 
ATOM   2366 O OE1   . GLU   A 1 309 ? -7.147  26.744 -48.265 1.00 62.82  ?  309 GLU   A OE1   1 
ATOM   2367 O OE2   . GLU   A 1 309 ? -5.128  27.582 -47.919 1.00 67.08  ?  309 GLU   A OE2   1 
ATOM   2368 N N     . PRO   A 1 310 ? -3.438  22.688 -48.329 1.00 59.24  ?  310 PRO   A N     1 
ATOM   2369 C CA    . PRO   A 1 310 ? -2.357  21.950 -47.661 1.00 62.93  ?  310 PRO   A CA    1 
ATOM   2370 C C     . PRO   A 1 310 ? -2.347  22.277 -46.172 1.00 62.76  ?  310 PRO   A C     1 
ATOM   2371 O O     . PRO   A 1 310 ? -2.573  23.422 -45.773 1.00 56.37  ?  310 PRO   A O     1 
ATOM   2372 C CB    . PRO   A 1 310 ? -1.089  22.447 -48.368 1.00 59.82  ?  310 PRO   A CB    1 
ATOM   2373 C CG    . PRO   A 1 310 ? -1.468  23.747 -48.974 1.00 56.49  ?  310 PRO   A CG    1 
ATOM   2374 C CD    . PRO   A 1 310 ? -2.925  23.646 -49.322 1.00 55.79  ?  310 PRO   A CD    1 
ATOM   2375 N N     . ALA   A 1 311 ? -2.109  21.250 -45.352 1.00 60.21  ?  311 ALA   A N     1 
ATOM   2376 C CA    . ALA   A 1 311 ? -2.250  21.365 -43.907 1.00 57.41  ?  311 ALA   A CA    1 
ATOM   2377 C C     . ALA   A 1 311 ? -1.345  20.363 -43.213 1.00 59.34  ?  311 ALA   A C     1 
ATOM   2378 O O     . ALA   A 1 311 ? -1.427  19.162 -43.473 1.00 63.15  ?  311 ALA   A O     1 
ATOM   2379 C CB    . ALA   A 1 311 ? -3.695  21.124 -43.468 1.00 56.77  ?  311 ALA   A CB    1 
ATOM   2380 N N     . ASP   A 1 312 ? -0.512  20.860 -42.312 1.00 55.59  ?  312 ASP   A N     1 
ATOM   2381 C CA    . ASP   A 1 312 ? 0.360   20.022 -41.506 1.00 59.08  ?  312 ASP   A CA    1 
ATOM   2382 C C     . ASP   A 1 312 ? -0.292  19.543 -40.206 1.00 61.04  ?  312 ASP   A C     1 
ATOM   2383 O O     . ASP   A 1 312 ? 0.197   18.568 -39.616 1.00 55.81  ?  312 ASP   A O     1 
ATOM   2384 C CB    . ASP   A 1 312 ? 1.645   20.785 -41.158 1.00 57.29  ?  312 ASP   A CB    1 
ATOM   2385 C CG    . ASP   A 1 312 ? 2.330   21.385 -42.379 1.00 60.11  ?  312 ASP   A CG    1 
ATOM   2386 O OD1   . ASP   A 1 312 ? 1.782   21.316 -43.502 1.00 71.91  ?  312 ASP   A OD1   1 
ATOM   2387 O OD2   . ASP   A 1 312 ? 3.408   21.971 -42.208 1.00 63.91  ?  312 ASP   A OD2   1 
ATOM   2388 N N     . ALA   A 1 313 ? -1.362  20.201 -39.739 1.00 59.00  ?  313 ALA   A N     1 
ATOM   2389 C CA    . ALA   A 1 313 ? -1.974  19.851 -38.461 1.00 54.07  ?  313 ALA   A CA    1 
ATOM   2390 C C     . ALA   A 1 313 ? -3.416  20.338 -38.400 1.00 53.31  ?  313 ALA   A C     1 
ATOM   2391 O O     . ALA   A 1 313 ? -3.747  21.388 -38.961 1.00 55.87  ?  313 ALA   A O     1 
ATOM   2392 C CB    . ALA   A 1 313 ? -1.182  20.442 -37.293 1.00 48.87  ?  313 ALA   A CB    1 
ATOM   2393 N N     . VAL   A 1 314 ? -4.263  19.582 -37.700 1.00 47.73  ?  314 VAL   A N     1 
ATOM   2394 C CA    . VAL   A 1 314 ? -5.620  20.021 -37.372 1.00 55.31  ?  314 VAL   A CA    1 
ATOM   2395 C C     . VAL   A 1 314 ? -5.811  19.941 -35.859 1.00 53.47  ?  314 VAL   A C     1 
ATOM   2396 O O     . VAL   A 1 314 ? -5.640  18.869 -35.261 1.00 53.91  ?  314 VAL   A O     1 
ATOM   2397 C CB    . VAL   A 1 314 ? -6.691  19.195 -38.100 1.00 53.39  ?  314 VAL   A CB    1 
ATOM   2398 C CG1   . VAL   A 1 314 ? -8.081  19.693 -37.707 1.00 53.74  ?  314 VAL   A CG1   1 
ATOM   2399 C CG2   . VAL   A 1 314 ? -6.493  19.294 -39.598 1.00 50.68  ?  314 VAL   A CG2   1 
ATOM   2400 N N     . VAL   A 1 315 ? -6.160  21.071 -35.242 1.00 48.49  ?  315 VAL   A N     1 
ATOM   2401 C CA    . VAL   A 1 315 ? -6.450  21.124 -33.812 1.00 48.74  ?  315 VAL   A CA    1 
ATOM   2402 C C     . VAL   A 1 315 ? -7.961  21.180 -33.638 1.00 48.37  ?  315 VAL   A C     1 
ATOM   2403 O O     . VAL   A 1 315 ? -8.635  22.092 -34.141 1.00 46.68  ?  315 VAL   A O     1 
ATOM   2404 C CB    . VAL   A 1 315 ? -5.753  22.311 -33.129 1.00 47.75  ?  315 VAL   A CB    1 
ATOM   2405 C CG1   . VAL   A 1 315 ? -4.281  22.079 -33.114 1.00 52.13  ?  315 VAL   A CG1   1 
ATOM   2406 C CG2   . VAL   A 1 315 ? -6.000  23.570 -33.884 1.00 48.22  ?  315 VAL   A CG2   1 
ATOM   2407 N N     . TYR   A 1 316 ? -8.510  20.176 -32.976 1.00 50.30  ?  316 TYR   A N     1 
ATOM   2408 C CA    . TYR   A 1 316 ? -9.953  20.120 -32.785 1.00 58.22  ?  316 TYR   A CA    1 
ATOM   2409 C C     . TYR   A 1 316 ? -10.280 20.878 -31.504 1.00 52.92  ?  316 TYR   A C     1 
ATOM   2410 O O     . TYR   A 1 316 ? -9.904  20.456 -30.404 1.00 48.31  ?  316 TYR   A O     1 
ATOM   2411 C CB    . TYR   A 1 316 ? -10.458 18.672 -32.790 1.00 58.80  ?  316 TYR   A CB    1 
ATOM   2412 C CG    . TYR   A 1 316 ? -10.831 18.237 -34.212 1.00 59.37  ?  316 TYR   A CG    1 
ATOM   2413 C CD1   . TYR   A 1 316 ? -12.039 18.620 -34.785 1.00 56.88  ?  316 TYR   A CD1   1 
ATOM   2414 C CD2   . TYR   A 1 316 ? -9.948  17.505 -35.000 1.00 55.53  ?  316 TYR   A CD2   1 
ATOM   2415 C CE1   . TYR   A 1 316 ? -12.366 18.267 -36.094 1.00 58.79  ?  316 TYR   A CE1   1 
ATOM   2416 C CE2   . TYR   A 1 316 ? -10.274 17.148 -36.298 1.00 58.70  ?  316 TYR   A CE2   1 
ATOM   2417 C CZ    . TYR   A 1 316 ? -11.483 17.535 -36.840 1.00 57.93  ?  316 TYR   A CZ    1 
ATOM   2418 O OH    . TYR   A 1 316 ? -11.820 17.191 -38.129 1.00 57.15  ?  316 TYR   A OH    1 
ATOM   2419 N N     . CYS   A 1 317 ? -10.905 22.041 -31.675 1.00 53.29  ?  317 CYS   A N     1 
ATOM   2420 C CA    . CYS   A 1 317 ? -11.445 22.882 -30.607 1.00 49.30  ?  317 CYS   A CA    1 
ATOM   2421 C C     . CYS   A 1 317 ? -12.909 22.588 -30.386 1.00 46.28  ?  317 CYS   A C     1 
ATOM   2422 O O     . CYS   A 1 317 ? -13.758 23.472 -30.453 1.00 46.99  ?  317 CYS   A O     1 
ATOM   2423 C CB    . CYS   A 1 317 ? -11.227 24.347 -30.932 1.00 41.08  ?  317 CYS   A CB    1 
ATOM   2424 S SG    . CYS   A 1 317 ? -9.491  24.733 -30.868 1.00 51.90  ?  317 CYS   A SG    1 
ATOM   2425 N N     . THR   A 1 318 ? -13.213 21.323 -30.122 1.00 52.69  ?  318 THR   A N     1 
ATOM   2426 C CA    . THR   A 1 318 ? -14.597 20.877 -30.076 1.00 56.94  ?  318 THR   A CA    1 
ATOM   2427 C C     . THR   A 1 318 ? -15.093 20.644 -28.665 1.00 54.96  ?  318 THR   A C     1 
ATOM   2428 O O     . THR   A 1 318 ? -16.218 20.176 -28.486 1.00 59.45  ?  318 THR   A O     1 
ATOM   2429 C CB    . THR   A 1 318 ? -14.781 19.613 -30.914 1.00 56.94  ?  318 THR   A CB    1 
ATOM   2430 O OG1   . THR   A 1 318 ? -13.821 18.625 -30.514 1.00 55.68  ?  318 THR   A OG1   1 
ATOM   2431 C CG2   . THR   A 1 318 ? -14.592 19.953 -32.377 1.00 51.06  ?  318 THR   A CG2   1 
ATOM   2432 N N     . GLY   A 1 319 ? -14.295 20.967 -27.666 1.00 53.81  ?  319 GLY   A N     1 
ATOM   2433 C CA    . GLY   A 1 319 ? -14.788 21.007 -26.316 1.00 52.49  ?  319 GLY   A CA    1 
ATOM   2434 C C     . GLY   A 1 319 ? -14.614 19.692 -25.591 1.00 56.87  ?  319 GLY   A C     1 
ATOM   2435 O O     . GLY   A 1 319 ? -13.901 18.783 -26.024 1.00 52.92  ?  319 GLY   A O     1 
ATOM   2436 N N     . PHE   A 1 320 ? -15.296 19.598 -24.450 1.00 53.26  ?  320 PHE   A N     1 
ATOM   2437 C CA    . PHE   A 1 320 ? -15.023 18.536 -23.506 1.00 52.70  ?  320 PHE   A CA    1 
ATOM   2438 C C     . PHE   A 1 320 ? -16.296 17.814 -23.113 1.00 56.68  ?  320 PHE   A C     1 
ATOM   2439 O O     . PHE   A 1 320 ? -17.396 18.366 -23.191 1.00 53.67  ?  320 PHE   A O     1 
ATOM   2440 C CB    . PHE   A 1 320 ? -14.310 19.083 -22.277 1.00 51.93  ?  320 PHE   A CB    1 
ATOM   2441 C CG    . PHE   A 1 320 ? -12.900 19.454 -22.550 1.00 49.96  ?  320 PHE   A CG    1 
ATOM   2442 C CD1   . PHE   A 1 320 ? -11.901 18.495 -22.471 1.00 52.42  ?  320 PHE   A CD1   1 
ATOM   2443 C CD2   . PHE   A 1 320 ? -12.575 20.744 -22.939 1.00 51.10  ?  320 PHE   A CD2   1 
ATOM   2444 C CE1   . PHE   A 1 320 ? -10.593 18.814 -22.753 1.00 56.73  ?  320 PHE   A CE1   1 
ATOM   2445 C CE2   . PHE   A 1 320 ? -11.269 21.084 -23.216 1.00 54.54  ?  320 PHE   A CE2   1 
ATOM   2446 C CZ    . PHE   A 1 320 ? -10.267 20.117 -23.120 1.00 61.03  ?  320 PHE   A CZ    1 
ATOM   2447 N N     . HIS   A 1 321 ? -16.126 16.548 -22.740 1.00 57.57  ?  321 HIS   A N     1 
ATOM   2448 C CA    . HIS   A 1 321 ? -17.202 15.748 -22.190 1.00 54.77  ?  321 HIS   A CA    1 
ATOM   2449 C C     . HIS   A 1 321 ? -17.145 15.800 -20.675 1.00 57.38  ?  321 HIS   A C     1 
ATOM   2450 O O     . HIS   A 1 321 ? -16.087 15.993 -20.073 1.00 57.03  ?  321 HIS   A O     1 
ATOM   2451 C CB    . HIS   A 1 321 ? -17.118 14.292 -22.651 1.00 60.05  ?  321 HIS   A CB    1 
ATOM   2452 C CG    . HIS   A 1 321 ? -17.496 14.087 -24.086 1.00 64.43  ?  321 HIS   A CG    1 
ATOM   2453 N ND1   . HIS   A 1 321 ? -18.639 14.626 -24.641 1.00 63.86  ?  321 HIS   A ND1   1 
ATOM   2454 C CD2   . HIS   A 1 321 ? -16.886 13.394 -25.077 1.00 66.14  ?  321 HIS   A CD2   1 
ATOM   2455 C CE1   . HIS   A 1 321 ? -18.712 14.279 -25.912 1.00 64.11  ?  321 HIS   A CE1   1 
ATOM   2456 N NE2   . HIS   A 1 321 ? -17.663 13.528 -26.201 1.00 69.07  ?  321 HIS   A NE2   1 
ATOM   2457 N N     . MET   A 1 322 ? -18.294 15.575 -20.076 1.00 56.40  ?  322 MET   A N     1 
ATOM   2458 C CA    . MET   A 1 322 ? -18.522 15.709 -18.648 1.00 48.42  ?  322 MET   A CA    1 
ATOM   2459 C C     . MET   A 1 322 ? -18.590 14.304 -18.051 1.00 50.57  ?  322 MET   A C     1 
ATOM   2460 O O     . MET   A 1 322 ? -19.607 13.618 -18.171 1.00 57.70  ?  322 MET   A O     1 
ATOM   2461 C CB    . MET   A 1 322 ? -19.812 16.494 -18.485 1.00 51.86  ?  322 MET   A CB    1 
ATOM   2462 C CG    . MET   A 1 322 ? -20.408 16.645 -17.131 1.00 62.60  ?  322 MET   A CG    1 
ATOM   2463 S SD    . MET   A 1 322 ? -21.637 17.965 -17.304 1.00 75.76  ?  322 MET   A SD    1 
ATOM   2464 C CE    . MET   A 1 322 ? -20.696 19.234 -18.179 1.00 56.55  ?  322 MET   A CE    1 
ATOM   2465 N N     . THR   A 1 323 ? -17.497 13.854 -17.437 1.00 52.01  ?  323 THR   A N     1 
ATOM   2466 C CA    . THR   A 1 323 ? -17.450 12.523 -16.830 1.00 56.41  ?  323 THR   A CA    1 
ATOM   2467 C C     . THR   A 1 323 ? -16.903 12.568 -15.408 1.00 45.19  ?  323 THR   A C     1 
ATOM   2468 O O     . THR   A 1 323 ? -16.218 13.507 -15.009 1.00 49.47  ?  323 THR   A O     1 
ATOM   2469 C CB    . THR   A 1 323 ? -16.581 11.548 -17.624 1.00 51.01  ?  323 THR   A CB    1 
ATOM   2470 O OG1   . THR   A 1 323 ? -15.270 12.109 -17.774 1.00 48.15  ?  323 THR   A OG1   1 
ATOM   2471 C CG2   . THR   A 1 323 ? -17.219 11.246 -18.973 1.00 54.81  ?  323 THR   A CG2   1 
ATOM   2472 N N     . PHE   A 1 324 ? -17.175 11.500 -14.666 1.00 46.03  ?  324 PHE   A N     1 
ATOM   2473 C CA    . PHE   A 1 324 ? -16.743 11.361 -13.272 1.00 42.67  ?  324 PHE   A CA    1 
ATOM   2474 C C     . PHE   A 1 324 ? -16.236 9.951  -13.054 1.00 41.14  ?  324 PHE   A C     1 
ATOM   2475 O O     . PHE   A 1 324 ? -16.937 9.112  -12.470 1.00 42.90  ?  324 PHE   A O     1 
ATOM   2476 C CB    . PHE   A 1 324 ? -17.894 11.660 -12.317 1.00 39.62  ?  324 PHE   A CB    1 
ATOM   2477 C CG    . PHE   A 1 324 ? -18.471 13.016 -12.504 1.00 43.04  ?  324 PHE   A CG    1 
ATOM   2478 C CD1   . PHE   A 1 324 ? -17.870 14.115 -11.914 1.00 41.51  ?  324 PHE   A CD1   1 
ATOM   2479 C CD2   . PHE   A 1 324 ? -19.592 13.204 -13.294 1.00 44.08  ?  324 PHE   A CD2   1 
ATOM   2480 C CE1   . PHE   A 1 324 ? -18.374 15.373 -12.098 1.00 41.99  ?  324 PHE   A CE1   1 
ATOM   2481 C CE2   . PHE   A 1 324 ? -20.108 14.451 -13.479 1.00 47.61  ?  324 PHE   A CE2   1 
ATOM   2482 C CZ    . PHE   A 1 324 ? -19.500 15.546 -12.877 1.00 51.35  ?  324 PHE   A CZ    1 
ATOM   2483 N N     . PRO   A 1 325 ? -15.021 9.638  -13.523 1.00 43.20  ?  325 PRO   A N     1 
ATOM   2484 C CA    . PRO   A 1 325 ? -14.597 8.220  -13.554 1.00 45.33  ?  325 PRO   A CA    1 
ATOM   2485 C C     . PRO   A 1 325 ? -14.531 7.576  -12.180 1.00 50.94  ?  325 PRO   A C     1 
ATOM   2486 O O     . PRO   A 1 325 ? -14.705 6.353  -12.070 1.00 52.79  ?  325 PRO   A O     1 
ATOM   2487 C CB    . PRO   A 1 325 ? -13.223 8.258  -14.244 1.00 33.88  ?  325 PRO   A CB    1 
ATOM   2488 C CG    . PRO   A 1 325 ? -12.827 9.679  -14.294 1.00 40.81  ?  325 PRO   A CG    1 
ATOM   2489 C CD    . PRO   A 1 325 ? -14.090 10.505 -14.267 1.00 41.45  ?  325 PRO   A CD    1 
ATOM   2490 N N     . PHE   A 1 326 ? -14.466 8.375  -11.124 1.00 51.36  ?  326 PHE   A N     1 
ATOM   2491 C CA    . PHE   A 1 326 ? -14.334 7.853  -9.742  1.00 43.57  ?  326 PHE   A CA    1 
ATOM   2492 C C     . PHE   A 1 326 ? -15.680 7.518  -9.181  1.00 44.65  ?  326 PHE   A C     1 
ATOM   2493 O O     . PHE   A 1 326 ? -15.777 6.972  -8.105  1.00 52.01  ?  326 PHE   A O     1 
ATOM   2494 C CB    . PHE   A 1 326 ? -13.644 8.959  -8.952  1.00 43.50  ?  326 PHE   A CB    1 
ATOM   2495 C CG    . PHE   A 1 326 ? -14.173 10.373 -9.108  1.00 45.73  ?  326 PHE   A CG    1 
ATOM   2496 C CD1   . PHE   A 1 326 ? -15.228 10.823 -8.331  1.00 47.31  ?  326 PHE   A CD1   1 
ATOM   2497 C CD2   . PHE   A 1 326 ? -13.587 11.256 -10.001 1.00 44.74  ?  326 PHE   A CD2   1 
ATOM   2498 C CE1   . PHE   A 1 326 ? -15.700 12.112 -8.466  1.00 49.93  ?  326 PHE   A CE1   1 
ATOM   2499 C CE2   . PHE   A 1 326 ? -14.067 12.542 -10.131 1.00 46.01  ?  326 PHE   A CE2   1 
ATOM   2500 C CZ    . PHE   A 1 326 ? -15.117 12.965 -9.362  1.00 46.41  ?  326 PHE   A CZ    1 
ATOM   2501 N N     . LEU   A 1 327 ? -16.717 7.857  -9.918  1.00 45.78  ?  327 LEU   A N     1 
ATOM   2502 C CA    . LEU   A 1 327 ? -18.090 7.539  -9.479  1.00 54.27  ?  327 LEU   A CA    1 
ATOM   2503 C C     . LEU   A 1 327 ? -18.636 6.377  -10.300 1.00 53.26  ?  327 LEU   A C     1 
ATOM   2504 O O     . LEU   A 1 327 ? -19.084 6.617  -11.414 1.00 57.66  ?  327 LEU   A O     1 
ATOM   2505 C CB    . LEU   A 1 327 ? -18.986 8.766  -9.620  1.00 49.39  ?  327 LEU   A CB    1 
ATOM   2506 C CG    . LEU   A 1 327 ? -18.989 9.768  -8.469  1.00 50.94  ?  327 LEU   A CG    1 
ATOM   2507 C CD1   . LEU   A 1 327 ? -20.147 10.697 -8.745  1.00 53.37  ?  327 LEU   A CD1   1 
ATOM   2508 C CD2   . LEU   A 1 327 ? -19.192 9.034  -7.168  1.00 48.04  ?  327 LEU   A CD2   1 
ATOM   2509 N N     . PRO   A 1 328 ? -18.584 5.116  -9.826  1.00 53.41  ?  328 PRO   A N     1 
ATOM   2510 C CA    . PRO   A 1 328 ? -19.017 4.012  -10.656 1.00 58.04  ?  328 PRO   A CA    1 
ATOM   2511 C C     . PRO   A 1 328 ? -20.365 4.190  -11.311 1.00 59.60  ?  328 PRO   A C     1 
ATOM   2512 O O     . PRO   A 1 328 ? -20.521 3.840  -12.485 1.00 60.37  ?  328 PRO   A O     1 
ATOM   2513 C CB    . PRO   A 1 328 ? -19.050 2.940  -9.605  1.00 56.62  ?  328 PRO   A CB    1 
ATOM   2514 C CG    . PRO   A 1 328 ? -17.810 3.199  -8.814  1.00 60.50  ?  328 PRO   A CG    1 
ATOM   2515 C CD    . PRO   A 1 328 ? -18.075 4.648  -8.525  1.00 55.70  ?  328 PRO   A CD    1 
ATOM   2516 N N     . ALA   A 1 329 ? -21.311 4.746  -10.583 1.00 63.32  ?  329 ALA   A N     1 
ATOM   2517 C CA    . ALA   A 1 329 ? -22.684 4.872  -11.097 1.00 65.29  ?  329 ALA   A CA    1 
ATOM   2518 C C     . ALA   A 1 329 ? -22.852 6.044  -12.055 1.00 66.23  ?  329 ALA   A C     1 
ATOM   2519 O O     . ALA   A 1 329 ? -23.817 6.030  -12.821 1.00 66.93  ?  329 ALA   A O     1 
ATOM   2520 C CB    . ALA   A 1 329 ? -23.556 5.067  -9.905  1.00 72.45  ?  329 ALA   A CB    1 
ATOM   2521 N N     . GLY   A 1 330 ? -22.003 7.061  -11.953 1.00 69.72  ?  330 GLY   A N     1 
ATOM   2522 C CA    . GLY   A 1 330 ? -22.106 8.257  -12.807 1.00 65.77  ?  330 GLY   A CA    1 
ATOM   2523 C C     . GLY   A 1 330 ? -22.712 9.432  -12.075 1.00 71.92  ?  330 GLY   A C     1 
ATOM   2524 O O     . GLY   A 1 330 ? -23.288 9.213  -10.999 1.00 70.22  ?  330 GLY   A O     1 
ATOM   2525 N N     . CYS   A 1 331 ? -22.592 10.639 -12.633 1.00 70.24  ?  331 CYS   A N     1 
ATOM   2526 C CA    . CYS   A 1 331 ? -23.273 11.798 -12.006 1.00 71.65  ?  331 CYS   A CA    1 
ATOM   2527 C C     . CYS   A 1 331 ? -24.757 11.658 -12.280 1.00 77.13  ?  331 CYS   A C     1 
ATOM   2528 O O     . CYS   A 1 331 ? -25.117 11.180 -13.368 1.00 73.68  ?  331 CYS   A O     1 
ATOM   2529 C CB    . CYS   A 1 331 ? -22.903 13.140 -12.599 1.00 65.29  ?  331 CYS   A CB    1 
ATOM   2530 S SG    . CYS   A 1 331 ? -24.304 14.260 -12.821 1.00 87.99  ?  331 CYS   A SG    1 
ATOM   2531 N N     . PRO   A 1 332 ? -25.628 12.033 -11.334 1.00 75.42  ?  332 PRO   A N     1 
ATOM   2532 C CA    . PRO   A 1 332 ? -27.030 11.793 -11.561 1.00 72.92  ?  332 PRO   A CA    1 
ATOM   2533 C C     . PRO   A 1 332 ? -27.405 12.334 -12.912 1.00 70.33  ?  332 PRO   A C     1 
ATOM   2534 O O     . PRO   A 1 332 ? -27.127 13.497 -13.204 1.00 67.22  ?  332 PRO   A O     1 
ATOM   2535 C CB    . PRO   A 1 332 ? -27.648 12.559 -10.417 1.00 75.15  ?  332 PRO   A CB    1 
ATOM   2536 C CG    . PRO   A 1 332 ? -26.603 12.563 -9.341  1.00 70.03  ?  332 PRO   A CG    1 
ATOM   2537 C CD    . PRO   A 1 332 ? -25.296 12.674 -10.080 1.00 65.10  ?  332 PRO   A CD    1 
ATOM   2538 N N     . MET   A 1 333 ? -28.042 11.500 -13.729 1.00 79.07  ?  333 MET   A N     1 
ATOM   2539 C CA    . MET   A 1 333 ? -28.491 11.926 -14.993 1.00 76.26  ?  333 MET   A CA    1 
ATOM   2540 C C     . MET   A 1 333 ? -29.823 11.384 -15.343 1.00 79.58  ?  333 MET   A C     1 
ATOM   2541 O O     . MET   A 1 333 ? -30.202 10.331 -14.933 1.00 78.83  ?  333 MET   A O     1 
ATOM   2542 C CB    . MET   A 1 333 ? -27.554 11.323 -15.990 1.00 77.52  ?  333 MET   A CB    1 
ATOM   2543 C CG    . MET   A 1 333 ? -26.851 12.314 -16.858 1.00 85.08  ?  333 MET   A CG    1 
ATOM   2544 S SD    . MET   A 1 333 ? -25.207 11.752 -17.204 1.00 101.53 ?  333 MET   A SD    1 
ATOM   2545 C CE    . MET   A 1 333 ? -24.206 12.981 -16.371 1.00 76.92  ?  333 MET   A CE    1 
ATOM   2546 N N     . SER   A 1 334 ? -30.539 12.136 -16.125 1.00 79.31  ?  334 SER   A N     1 
ATOM   2547 C CA    . SER   A 1 334 ? -31.775 11.641 -16.713 1.00 85.17  ?  334 SER   A CA    1 
ATOM   2548 C C     . SER   A 1 334 ? -31.453 10.803 -17.951 1.00 87.12  ?  334 SER   A C     1 
ATOM   2549 O O     . SER   A 1 334 ? -30.331 10.827 -18.470 1.00 84.96  ?  334 SER   A O     1 
ATOM   2550 C CB    . SER   A 1 334 ? -32.708 12.799 -17.083 1.00 82.71  ?  334 SER   A CB    1 
ATOM   2551 O OG    . SER   A 1 334 ? -32.260 13.487 -18.240 1.00 76.86  ?  334 SER   A OG    1 
ATOM   2552 N N     . ALA   A 1 335 ? -32.435 10.123 -18.539 1.00 86.82  ?  335 ALA   A N     1 
ATOM   2553 C CA    . ALA   A 1 335 ? -32.060 9.303  -19.713 1.00 85.04  ?  335 ALA   A CA    1 
ATOM   2554 C C     . ALA   A 1 335 ? -31.580 10.202 -20.846 1.00 79.18  ?  335 ALA   A C     1 
ATOM   2555 O O     . ALA   A 1 335 ? -30.594 9.864  -21.502 1.00 77.82  ?  335 ALA   A O     1 
ATOM   2556 C CB    . ALA   A 1 335 ? -33.211 8.441  -20.153 1.00 85.30  ?  335 ALA   A CB    1 
ATOM   2557 N N     . ASP   A 1 336 ? -32.215 11.351 -21.031 1.00 81.41  ?  336 ASP   A N     1 
ATOM   2558 C CA    . ASP   A 1 336 ? -31.724 12.299 -22.061 1.00 82.14  ?  336 ASP   A CA    1 
ATOM   2559 C C     . ASP   A 1 336 ? -30.251 12.557 -21.807 1.00 85.14  ?  336 ASP   A C     1 
ATOM   2560 O O     . ASP   A 1 336 ? -29.584 13.053 -22.719 1.00 91.88  ?  336 ASP   A O     1 
ATOM   2561 C CB    . ASP   A 1 336 ? -32.441 13.637 -22.065 1.00 82.42  ?  336 ASP   A CB    1 
ATOM   2562 C CG    . ASP   A 1 336 ? -33.602 13.797 -21.095 1.00 92.18  ?  336 ASP   A CG    1 
ATOM   2563 O OD1   . ASP   A 1 336 ? -34.233 12.778 -20.754 1.00 97.04  ?  336 ASP   A OD1   1 
ATOM   2564 O OD2   . ASP   A 1 336 ? -33.870 14.946 -20.696 1.00 92.50  ?  336 ASP   A OD2   1 
ATOM   2565 N N     . GLY   A 1 337 ? -29.779 12.251 -20.604 1.00 84.43  ?  337 GLY   A N     1 
ATOM   2566 C CA    . GLY   A 1 337 ? -28.380 12.532 -20.250 1.00 83.05  ?  337 GLY   A CA    1 
ATOM   2567 C C     . GLY   A 1 337 ? -28.307 13.894 -19.626 1.00 82.47  ?  337 GLY   A C     1 
ATOM   2568 O O     . GLY   A 1 337 ? -27.202 14.441 -19.515 1.00 81.77  ?  337 GLY   A O     1 
ATOM   2569 N N     . SER   A 1 338 ? -29.463 14.424 -19.239 1.00 83.08  ?  338 SER   A N     1 
ATOM   2570 C CA    . SER   A 1 338 ? -29.394 15.696 -18.543 1.00 78.70  ?  338 SER   A CA    1 
ATOM   2571 C C     . SER   A 1 338 ? -29.032 15.489 -17.072 1.00 75.03  ?  338 SER   A C     1 
ATOM   2572 O O     . SER   A 1 338 ? -29.434 14.505 -16.440 1.00 69.73  ?  338 SER   A O     1 
ATOM   2573 C CB    . SER   A 1 338 ? -30.736 16.419 -18.660 1.00 75.12  ?  338 SER   A CB    1 
ATOM   2574 O OG    . SER   A 1 338 ? -31.030 16.709 -20.015 1.00 77.80  ?  338 SER   A OG    1 
ATOM   2575 N N     . VAL   A 1 339 ? -28.250 16.431 -16.536 1.00 71.55  ?  339 VAL   A N     1 
ATOM   2576 C CA    . VAL   A 1 339 ? -27.850 16.392 -15.131 1.00 67.58  ?  339 VAL   A CA    1 
ATOM   2577 C C     . VAL   A 1 339 ? -29.074 16.523 -14.235 1.00 63.19  ?  339 VAL   A C     1 
ATOM   2578 O O     . VAL   A 1 339 ? -29.926 17.402 -14.439 1.00 60.47  ?  339 VAL   A O     1 
ATOM   2579 C CB    . VAL   A 1 339 ? -26.839 17.509 -14.830 1.00 65.25  ?  339 VAL   A CB    1 
ATOM   2580 C CG1   . VAL   A 1 339 ? -26.478 17.500 -13.365 1.00 54.63  ?  339 VAL   A CG1   1 
ATOM   2581 C CG2   . VAL   A 1 339 ? -25.604 17.360 -15.692 1.00 65.76  ?  339 VAL   A CG2   1 
ATOM   2582 N N     . GLU   A 1 340 ? -29.148 15.670 -13.215 1.00 56.51  ?  340 GLU   A N     1 
ATOM   2583 C CA    . GLU   A 1 340 ? -30.236 15.701 -12.244 1.00 61.67  ?  340 GLU   A CA    1 
ATOM   2584 C C     . GLU   A 1 340 ? -29.665 16.048 -10.872 1.00 55.67  ?  340 GLU   A C     1 
ATOM   2585 O O     . GLU   A 1 340 ? -29.395 15.172 -10.047 1.00 54.45  ?  340 GLU   A O     1 
ATOM   2586 C CB    . GLU   A 1 340 ? -30.959 14.381 -12.229 1.00 66.22  ?  340 GLU   A CB    1 
ATOM   2587 C CG    . GLU   A 1 340 ? -31.752 14.127 -13.500 1.00 74.56  ?  340 GLU   A CG    1 
ATOM   2588 C CD    . GLU   A 1 340 ? -32.720 12.976 -13.351 1.00 76.96  ?  340 GLU   A CD    1 
ATOM   2589 O OE1   . GLU   A 1 340 ? -32.579 12.190 -12.384 1.00 75.32  ?  340 GLU   A OE1   1 
ATOM   2590 O OE2   . GLU   A 1 340 ? -33.636 12.881 -14.190 1.00 80.37  ?  340 GLU   A OE2   1 
ATOM   2591 N N     . LEU   A 1 341 ? -29.516 17.347 -10.616 1.00 49.97  ?  341 LEU   A N     1 
ATOM   2592 C CA    . LEU   A 1 341 ? -28.990 17.834 -9.342  1.00 47.47  ?  341 LEU   A CA    1 
ATOM   2593 C C     . LEU   A 1 341 ? -29.879 18.947 -8.819  1.00 47.72  ?  341 LEU   A C     1 
ATOM   2594 O O     . LEU   A 1 341 ? -29.960 20.020 -9.427  1.00 46.72  ?  341 LEU   A O     1 
ATOM   2595 C CB    . LEU   A 1 341 ? -27.559 18.335 -9.493  1.00 42.46  ?  341 LEU   A CB    1 
ATOM   2596 C CG    . LEU   A 1 341 ? -26.548 17.224 -9.743  1.00 46.37  ?  341 LEU   A CG    1 
ATOM   2597 C CD1   . LEU   A 1 341 ? -25.187 17.835 -10.024 1.00 43.51  ?  341 LEU   A CD1   1 
ATOM   2598 C CD2   . LEU   A 1 341 ? -26.506 16.252 -8.554  1.00 45.40  ?  341 LEU   A CD2   1 
ATOM   2599 N N     . TYR   A 1 342 ? -30.531 18.696 -7.697  1.00 45.89  ?  342 TYR   A N     1 
ATOM   2600 C CA    . TYR   A 1 342 ? -31.340 19.714 -7.039  1.00 48.27  ?  342 TYR   A CA    1 
ATOM   2601 C C     . TYR   A 1 342 ? -30.552 21.013 -6.854  1.00 45.26  ?  342 TYR   A C     1 
ATOM   2602 O O     . TYR   A 1 342 ? -29.449 21.007 -6.302  1.00 46.52  ?  342 TYR   A O     1 
ATOM   2603 C CB    . TYR   A 1 342 ? -31.818 19.167 -5.691  1.00 50.14  ?  342 TYR   A CB    1 
ATOM   2604 C CG    . TYR   A 1 342 ? -32.574 20.162 -4.858  1.00 51.50  ?  342 TYR   A CG    1 
ATOM   2605 C CD1   . TYR   A 1 342 ? -33.646 20.854 -5.389  1.00 45.59  ?  342 TYR   A CD1   1 
ATOM   2606 C CD2   . TYR   A 1 342 ? -32.215 20.402 -3.536  1.00 48.70  ?  342 TYR   A CD2   1 
ATOM   2607 C CE1   . TYR   A 1 342 ? -34.337 21.758 -4.643  1.00 50.34  ?  342 TYR   A CE1   1 
ATOM   2608 C CE2   . TYR   A 1 342 ? -32.905 21.302 -2.770  1.00 48.87  ?  342 TYR   A CE2   1 
ATOM   2609 C CZ    . TYR   A 1 342 ? -33.966 21.984 -3.331  1.00 54.16  ?  342 TYR   A CZ    1 
ATOM   2610 O OH    . TYR   A 1 342 ? -34.664 22.893 -2.577  1.00 50.50  ?  342 TYR   A OH    1 
ATOM   2611 N N     . ARG   A 1 343 ? -31.114 22.123 -7.342  1.00 44.39  ?  343 ARG   A N     1 
ATOM   2612 C CA    . ARG   A 1 343 ? -30.464 23.430 -7.295  1.00 41.44  ?  343 ARG   A CA    1 
ATOM   2613 C C     . ARG   A 1 343 ? -29.047 23.352 -7.853  1.00 45.28  ?  343 ARG   A C     1 
ATOM   2614 O O     . ARG   A 1 343 ? -28.156 24.099 -7.438  1.00 43.40  ?  343 ARG   A O     1 
ATOM   2615 C CB    . ARG   A 1 343 ? -30.454 24.008 -5.878  1.00 45.87  ?  343 ARG   A CB    1 
ATOM   2616 C CG    . ARG   A 1 343 ? -31.807 24.055 -5.199  1.00 50.07  ?  343 ARG   A CG    1 
ATOM   2617 C CD    . ARG   A 1 343 ? -32.127 25.466 -4.641  1.00 54.40  ?  343 ARG   A CD    1 
ATOM   2618 N NE    . ARG   A 1 343 ? -31.446 25.694 -3.376  1.00 50.59  ?  343 ARG   A NE    1 
ATOM   2619 C CZ    . ARG   A 1 343 ? -30.754 26.789 -3.077  1.00 50.90  ?  343 ARG   A CZ    1 
ATOM   2620 N NH1   . ARG   A 1 343 ? -30.648 27.791 -3.947  1.00 53.09  ?  343 ARG   A NH1   1 
ATOM   2621 N NH2   . ARG   A 1 343 ? -30.166 26.878 -1.893  1.00 51.52  ?  343 ARG   A NH2   1 
ATOM   2622 N N     . ARG   A 1 344 ? -28.854 22.435 -8.807  1.00 46.46  ?  344 ARG   A N     1 
ATOM   2623 C CA    . ARG   A 1 344 ? -27.619 22.211 -9.551  1.00 40.42  ?  344 ARG   A CA    1 
ATOM   2624 C C     . ARG   A 1 344 ? -26.517 21.601 -8.690  1.00 44.14  ?  344 ARG   A C     1 
ATOM   2625 O O     . ARG   A 1 344 ? -25.355 21.580 -9.101  1.00 46.09  ?  344 ARG   A O     1 
ATOM   2626 C CB    . ARG   A 1 344 ? -27.121 23.502 -10.228 1.00 39.06  ?  344 ARG   A CB    1 
ATOM   2627 C CG    . ARG   A 1 344 ? -28.207 24.351 -10.945 1.00 45.62  ?  344 ARG   A CG    1 
ATOM   2628 C CD    . ARG   A 1 344 ? -28.914 23.656 -12.171 1.00 45.34  ?  344 ARG   A CD    1 
ATOM   2629 N NE    . ARG   A 1 344 ? -29.954 22.699 -11.775 1.00 40.96  ?  344 ARG   A NE    1 
ATOM   2630 C CZ    . ARG   A 1 344 ? -31.076 23.026 -11.130 1.00 45.96  ?  344 ARG   A CZ    1 
ATOM   2631 N NH1   . ARG   A 1 344 ? -31.334 24.294 -10.813 1.00 47.03  ?  344 ARG   A NH1   1 
ATOM   2632 N NH2   . ARG   A 1 344 ? -31.949 22.086 -10.800 1.00 47.09  ?  344 ARG   A NH2   1 
ATOM   2633 N N     . VAL   A 1 345 ? -26.838 21.071 -7.507  1.00 45.13  ?  345 VAL   A N     1 
ATOM   2634 C CA    . VAL   A 1 345 ? -25.777 20.671 -6.587  1.00 46.04  ?  345 VAL   A CA    1 
ATOM   2635 C C     . VAL   A 1 345 ? -25.976 19.280 -5.994  1.00 44.34  ?  345 VAL   A C     1 
ATOM   2636 O O     . VAL   A 1 345 ? -25.013 18.508 -5.874  1.00 42.22  ?  345 VAL   A O     1 
ATOM   2637 C CB    . VAL   A 1 345 ? -25.625 21.709 -5.462  1.00 44.51  ?  345 VAL   A CB    1 
ATOM   2638 C CG1   . VAL   A 1 345 ? -24.712 21.165 -4.347  1.00 40.46  ?  345 VAL   A CG1   1 
ATOM   2639 C CG2   . VAL   A 1 345 ? -25.112 23.034 -6.025  1.00 32.44  ?  345 VAL   A CG2   1 
ATOM   2640 N N     . VAL   A 1 346 ? -27.204 18.942 -5.624  1.00 42.96  ?  346 VAL   A N     1 
ATOM   2641 C CA    . VAL   A 1 346 ? -27.437 17.858 -4.674  1.00 47.70  ?  346 VAL   A CA    1 
ATOM   2642 C C     . VAL   A 1 346 ? -28.153 16.712 -5.384  1.00 46.27  ?  346 VAL   A C     1 
ATOM   2643 O O     . VAL   A 1 346 ? -29.250 16.910 -5.919  1.00 45.88  ?  346 VAL   A O     1 
ATOM   2644 C CB    . VAL   A 1 346 ? -28.246 18.337 -3.459  1.00 50.41  ?  346 VAL   A CB    1 
ATOM   2645 C CG1   . VAL   A 1 346 ? -28.352 17.224 -2.394  1.00 43.48  ?  346 VAL   A CG1   1 
ATOM   2646 C CG2   . VAL   A 1 346 ? -27.624 19.631 -2.900  1.00 46.73  ?  346 VAL   A CG2   1 
ATOM   2647 N N     . PRO   A 1 347 ? -27.583 15.510 -5.395  1.00 48.98  ?  347 PRO   A N     1 
ATOM   2648 C CA    . PRO   A 1 347 ? -28.342 14.347 -5.869  1.00 51.33  ?  347 PRO   A CA    1 
ATOM   2649 C C     . PRO   A 1 347 ? -29.559 14.079 -4.987  1.00 50.09  ?  347 PRO   A C     1 
ATOM   2650 O O     . PRO   A 1 347 ? -29.508 14.183 -3.758  1.00 52.23  ?  347 PRO   A O     1 
ATOM   2651 C CB    . PRO   A 1 347 ? -27.318 13.200 -5.807  1.00 53.98  ?  347 PRO   A CB    1 
ATOM   2652 C CG    . PRO   A 1 347 ? -26.188 13.695 -4.933  1.00 49.10  ?  347 PRO   A CG    1 
ATOM   2653 C CD    . PRO   A 1 347 ? -26.177 15.182 -5.087  1.00 50.35  ?  347 PRO   A CD    1 
ATOM   2654 N N     . ALA   A 1 348 ? -30.669 13.734 -5.640  1.00 54.81  ?  348 ALA   A N     1 
ATOM   2655 C CA    . ALA   A 1 348 ? -31.921 13.517 -4.934  1.00 47.13  ?  348 ALA   A CA    1 
ATOM   2656 C C     . ALA   A 1 348 ? -31.894 12.283 -4.056  1.00 52.72  ?  348 ALA   A C     1 
ATOM   2657 O O     . ALA   A 1 348 ? -32.666 12.206 -3.094  1.00 58.41  ?  348 ALA   A O     1 
ATOM   2658 C CB    . ALA   A 1 348 ? -33.063 13.400 -5.936  1.00 50.86  ?  348 ALA   A CB    1 
ATOM   2659 N N     . ASP   A 1 349 ? -31.034 11.316 -4.354  1.00 55.84  ?  349 ASP   A N     1 
ATOM   2660 C CA    . ASP   A 1 349 ? -31.135 10.005 -3.730  1.00 55.43  ?  349 ASP   A CA    1 
ATOM   2661 C C     . ASP   A 1 349 ? -29.841 9.564  -3.074  1.00 57.35  ?  349 ASP   A C     1 
ATOM   2662 O O     . ASP   A 1 349 ? -29.692 8.381  -2.764  1.00 62.26  ?  349 ASP   A O     1 
ATOM   2663 C CB    . ASP   A 1 349 ? -31.556 8.966  -4.767  1.00 61.46  ?  349 ASP   A CB    1 
ATOM   2664 C CG    . ASP   A 1 349 ? -32.905 9.286  -5.387  1.00 71.99  ?  349 ASP   A CG    1 
ATOM   2665 O OD1   . ASP   A 1 349 ? -33.892 9.416  -4.609  1.00 66.92  ?  349 ASP   A OD1   1 
ATOM   2666 O OD2   . ASP   A 1 349 ? -32.972 9.428  -6.640  1.00 68.04  ?  349 ASP   A OD2   1 
ATOM   2667 N N     . ARG   A 1 350 ? -28.905 10.477 -2.861  1.00 58.38  ?  350 ARG   A N     1 
ATOM   2668 C CA    . ARG   A 1 350 ? -27.563 10.137 -2.401  1.00 56.23  ?  350 ARG   A CA    1 
ATOM   2669 C C     . ARG   A 1 350 ? -27.173 11.140 -1.320  1.00 54.74  ?  350 ARG   A C     1 
ATOM   2670 O O     . ARG   A 1 350 ? -26.605 12.201 -1.607  1.00 54.59  ?  350 ARG   A O     1 
ATOM   2671 C CB    . ARG   A 1 350 ? -26.578 10.139 -3.567  1.00 52.73  ?  350 ARG   A CB    1 
ATOM   2672 C CG    . ARG   A 1 350 ? -26.605 8.865  -4.390  1.00 54.10  ?  350 ARG   A CG    1 
ATOM   2673 C CD    . ARG   A 1 350 ? -25.395 8.801  -5.316  1.00 60.73  ?  350 ARG   A CD    1 
ATOM   2674 N NE    . ARG   A 1 350 ? -25.627 9.436  -6.617  1.00 60.07  ?  350 ARG   A NE    1 
ATOM   2675 C CZ    . ARG   A 1 350 ? -24.869 9.225  -7.690  1.00 68.56  ?  350 ARG   A CZ    1 
ATOM   2676 N NH1   . ARG   A 1 350 ? -23.826 8.409  -7.622  1.00 76.95  ?  350 ARG   A NH1   1 
ATOM   2677 N NH2   . ARG   A 1 350 ? -25.148 9.824  -8.831  1.00 70.63  ?  350 ARG   A NH2   1 
ATOM   2678 N N     . PRO   A 1 351 ? -27.509 10.859 -0.072  1.00 50.11  ?  351 PRO   A N     1 
ATOM   2679 C CA    . PRO   A 1 351 ? -27.118 11.781 0.996   1.00 50.41  ?  351 PRO   A CA    1 
ATOM   2680 C C     . PRO   A 1 351 ? -25.617 11.745 1.196   1.00 47.92  ?  351 PRO   A C     1 
ATOM   2681 O O     . PRO   A 1 351 ? -24.977 10.704 1.045   1.00 50.52  ?  351 PRO   A O     1 
ATOM   2682 C CB    . PRO   A 1 351 ? -27.868 11.257 2.220   1.00 49.97  ?  351 PRO   A CB    1 
ATOM   2683 C CG    . PRO   A 1 351 ? -28.353 9.888  1.822   1.00 53.04  ?  351 PRO   A CG    1 
ATOM   2684 C CD    . PRO   A 1 351 ? -28.474 9.846  0.370   1.00 47.07  ?  351 PRO   A CD    1 
ATOM   2685 N N     . GLY   A 1 352 ? -25.056 12.912 1.505   1.00 45.43  ?  352 GLY   A N     1 
ATOM   2686 C CA    . GLY   A 1 352 ? -23.650 13.043 1.774   1.00 40.93  ?  352 GLY   A CA    1 
ATOM   2687 C C     . GLY   A 1 352 ? -22.816 13.349 0.563   1.00 48.50  ?  352 GLY   A C     1 
ATOM   2688 O O     . GLY   A 1 352 ? -21.586 13.478 0.694   1.00 48.19  ?  352 GLY   A O     1 
ATOM   2689 N N     . LEU   A 1 353 ? -23.444 13.472 -0.607  1.00 47.35  ?  353 LEU   A N     1 
ATOM   2690 C CA    . LEU   A 1 353 ? -22.770 13.782 -1.852  1.00 43.19  ?  353 LEU   A CA    1 
ATOM   2691 C C     . LEU   A 1 353 ? -23.187 15.164 -2.354  1.00 43.73  ?  353 LEU   A C     1 
ATOM   2692 O O     . LEU   A 1 353 ? -24.351 15.550 -2.257  1.00 44.40  ?  353 LEU   A O     1 
ATOM   2693 C CB    . LEU   A 1 353 ? -23.077 12.720 -2.899  1.00 44.60  ?  353 LEU   A CB    1 
ATOM   2694 C CG    . LEU   A 1 353 ? -22.224 12.788 -4.162  1.00 43.92  ?  353 LEU   A CG    1 
ATOM   2695 C CD1   . LEU   A 1 353 ? -20.743 12.498 -3.862  1.00 40.80  ?  353 LEU   A CD1   1 
ATOM   2696 C CD2   . LEU   A 1 353 ? -22.791 11.772 -5.102  1.00 46.10  ?  353 LEU   A CD2   1 
ATOM   2697 N N     . TYR   A 1 354 ? -22.227 15.905 -2.892  1.00 42.18  ?  354 TYR   A N     1 
ATOM   2698 C CA    . TYR   A 1 354 ? -22.489 17.240 -3.388  1.00 44.07  ?  354 TYR   A CA    1 
ATOM   2699 C C     . TYR   A 1 354 ? -21.572 17.508 -4.567  1.00 46.04  ?  354 TYR   A C     1 
ATOM   2700 O O     . TYR   A 1 354 ? -20.402 17.111 -4.549  1.00 48.00  ?  354 TYR   A O     1 
ATOM   2701 C CB    . TYR   A 1 354 ? -22.253 18.296 -2.304  1.00 48.79  ?  354 TYR   A CB    1 
ATOM   2702 C CG    . TYR   A 1 354 ? -22.933 18.005 -0.997  1.00 44.30  ?  354 TYR   A CG    1 
ATOM   2703 C CD1   . TYR   A 1 354 ? -24.247 18.372 -0.775  1.00 44.10  ?  354 TYR   A CD1   1 
ATOM   2704 C CD2   . TYR   A 1 354 ? -22.254 17.373 0.022   1.00 46.23  ?  354 TYR   A CD2   1 
ATOM   2705 C CE1   . TYR   A 1 354 ? -24.867 18.109 0.437   1.00 47.08  ?  354 TYR   A CE1   1 
ATOM   2706 C CE2   . TYR   A 1 354 ? -22.858 17.105 1.240   1.00 46.30  ?  354 TYR   A CE2   1 
ATOM   2707 C CZ    . TYR   A 1 354 ? -24.156 17.474 1.452   1.00 47.16  ?  354 TYR   A CZ    1 
ATOM   2708 O OH    . TYR   A 1 354 ? -24.735 17.190 2.681   1.00 44.06  ?  354 TYR   A OH    1 
ATOM   2709 N N     . PHE   A 1 355 ? -22.105 18.187 -5.581  1.00 45.46  ?  355 PHE   A N     1 
ATOM   2710 C CA    . PHE   A 1 355 ? -21.345 18.627 -6.747  1.00 42.42  ?  355 PHE   A CA    1 
ATOM   2711 C C     . PHE   A 1 355 ? -21.281 20.141 -6.748  1.00 40.74  ?  355 PHE   A C     1 
ATOM   2712 O O     . PHE   A 1 355 ? -22.317 20.805 -6.637  1.00 41.39  ?  355 PHE   A O     1 
ATOM   2713 C CB    . PHE   A 1 355 ? -21.989 18.145 -8.048  1.00 37.15  ?  355 PHE   A CB    1 
ATOM   2714 C CG    . PHE   A 1 355 ? -22.029 16.669 -8.173  1.00 43.10  ?  355 PHE   A CG    1 
ATOM   2715 C CD1   . PHE   A 1 355 ? -22.992 15.933 -7.480  1.00 40.24  ?  355 PHE   A CD1   1 
ATOM   2716 C CD2   . PHE   A 1 355 ? -21.095 15.993 -8.970  1.00 40.15  ?  355 PHE   A CD2   1 
ATOM   2717 C CE1   . PHE   A 1 355 ? -23.037 14.554 -7.582  1.00 39.09  ?  355 PHE   A CE1   1 
ATOM   2718 C CE2   . PHE   A 1 355 ? -21.137 14.610 -9.070  1.00 41.63  ?  355 PHE   A CE2   1 
ATOM   2719 C CZ    . PHE   A 1 355 ? -22.116 13.887 -8.366  1.00 39.74  ?  355 PHE   A CZ    1 
ATOM   2720 N N     . VAL   A 1 356 ? -20.076 20.679 -6.895  1.00 40.21  ?  356 VAL   A N     1 
ATOM   2721 C CA    . VAL   A 1 356 ? -19.828 22.114 -6.822  1.00 39.38  ?  356 VAL   A CA    1 
ATOM   2722 C C     . VAL   A 1 356 ? -19.121 22.554 -8.086  1.00 39.94  ?  356 VAL   A C     1 
ATOM   2723 O O     . VAL   A 1 356 ? -18.192 21.884 -8.548  1.00 46.51  ?  356 VAL   A O     1 
ATOM   2724 C CB    . VAL   A 1 356 ? -18.988 22.476 -5.579  1.00 37.99  ?  356 VAL   A CB    1 
ATOM   2725 C CG1   . VAL   A 1 356 ? -18.491 23.908 -5.666  1.00 35.43  ?  356 VAL   A CG1   1 
ATOM   2726 C CG2   . VAL   A 1 356 ? -19.828 22.251 -4.329  1.00 35.96  ?  356 VAL   A CG2   1 
ATOM   2727 N N     . GLY   A 1 357 ? -19.543 23.690 -8.636  1.00 43.64  ?  357 GLY   A N     1 
ATOM   2728 C CA    . GLY   A 1 357 ? -18.942 24.195 -9.855  1.00 43.00  ?  357 GLY   A CA    1 
ATOM   2729 C C     . GLY   A 1 357 ? -19.446 23.549 -11.128 1.00 45.04  ?  357 GLY   A C     1 
ATOM   2730 O O     . GLY   A 1 357 ? -18.967 23.904 -12.212 1.00 52.77  ?  357 GLY   A O     1 
ATOM   2731 N N     . LEU   A 1 358 ? -20.374 22.602 -11.029 1.00 40.43  ?  358 LEU   A N     1 
ATOM   2732 C CA    . LEU   A 1 358 ? -20.952 21.931 -12.188 1.00 47.43  ?  358 LEU   A CA    1 
ATOM   2733 C C     . LEU   A 1 358 ? -22.124 22.749 -12.737 1.00 48.84  ?  358 LEU   A C     1 
ATOM   2734 O O     . LEU   A 1 358 ? -23.295 22.354 -12.736 1.00 50.32  ?  358 LEU   A O     1 
ATOM   2735 C CB    . LEU   A 1 358 ? -21.375 20.519 -11.816 1.00 45.64  ?  358 LEU   A CB    1 
ATOM   2736 C CG    . LEU   A 1 358 ? -21.796 19.646 -12.983 1.00 47.35  ?  358 LEU   A CG    1 
ATOM   2737 C CD1   . LEU   A 1 358 ? -20.739 19.729 -14.087 1.00 50.83  ?  358 LEU   A CD1   1 
ATOM   2738 C CD2   . LEU   A 1 358 ? -21.970 18.237 -12.494 1.00 45.64  ?  358 LEU   A CD2   1 
ATOM   2739 N N     . VAL   A 1 359 ? -21.778 23.946 -13.179 1.00 50.63  ?  359 VAL   A N     1 
ATOM   2740 C CA    . VAL   A 1 359 ? -22.714 24.876 -13.785 1.00 54.05  ?  359 VAL   A CA    1 
ATOM   2741 C C     . VAL   A 1 359 ? -21.938 25.670 -14.825 1.00 59.32  ?  359 VAL   A C     1 
ATOM   2742 O O     . VAL   A 1 359 ? -20.706 25.612 -14.890 1.00 53.03  ?  359 VAL   A O     1 
ATOM   2743 C CB    . VAL   A 1 359 ? -23.369 25.825 -12.758 1.00 54.99  ?  359 VAL   A CB    1 
ATOM   2744 C CG1   . VAL   A 1 359 ? -24.310 25.052 -11.819 1.00 48.93  ?  359 VAL   A CG1   1 
ATOM   2745 C CG2   . VAL   A 1 359 ? -22.302 26.564 -11.986 1.00 49.69  ?  359 VAL   A CG2   1 
ATOM   2746 N N     . ARG   A 1 360 ? -22.674 26.400 -15.663 1.00 65.18  ?  360 ARG   A N     1 
ATOM   2747 C CA    . ARG   A 1 360 ? -22.106 27.189 -16.749 1.00 67.53  ?  360 ARG   A CA    1 
ATOM   2748 C C     . ARG   A 1 360 ? -22.956 28.446 -16.856 1.00 68.21  ?  360 ARG   A C     1 
ATOM   2749 O O     . ARG   A 1 360 ? -24.119 28.377 -17.278 1.00 68.13  ?  360 ARG   A O     1 
ATOM   2750 C CB    . ARG   A 1 360 ? -22.076 26.394 -18.068 1.00 69.12  ?  360 ARG   A CB    1 
ATOM   2751 C CG    . ARG   A 1 360 ? -21.612 27.184 -19.322 1.00 72.03  ?  360 ARG   A CG    1 
ATOM   2752 C CD    . ARG   A 1 360 ? -20.522 26.451 -20.127 1.00 75.44  ?  360 ARG   A CD    1 
ATOM   2753 N NE    . ARG   A 1 360 ? -19.186 26.664 -19.559 1.00 84.69  ?  360 ARG   A NE    1 
ATOM   2754 C CZ    . ARG   A 1 360 ? -18.075 26.018 -19.925 1.00 83.41  ?  360 ARG   A CZ    1 
ATOM   2755 N NH1   . ARG   A 1 360 ? -18.100 25.089 -20.880 1.00 73.69  ?  360 ARG   A NH1   1 
ATOM   2756 N NH2   . ARG   A 1 360 ? -16.924 26.313 -19.332 1.00 75.24  ?  360 ARG   A NH2   1 
ATOM   2757 N N     . PRO   A 1 361 ? -22.437 29.599 -16.448 1.00 70.63  ?  361 PRO   A N     1 
ATOM   2758 C CA    . PRO   A 1 361 ? -23.293 30.786 -16.361 1.00 67.75  ?  361 PRO   A CA    1 
ATOM   2759 C C     . PRO   A 1 361 ? -22.944 31.876 -17.359 1.00 58.79  ?  361 PRO   A C     1 
ATOM   2760 O O     . PRO   A 1 361 ? -21.890 31.864 -18.006 1.00 60.21  ?  361 PRO   A O     1 
ATOM   2761 C CB    . PRO   A 1 361 ? -23.052 31.256 -14.925 1.00 66.42  ?  361 PRO   A CB    1 
ATOM   2762 C CG    . PRO   A 1 361 ? -21.538 30.938 -14.733 1.00 64.75  ?  361 PRO   A CG    1 
ATOM   2763 C CD    . PRO   A 1 361 ? -21.182 29.787 -15.700 1.00 64.08  ?  361 PRO   A CD    1 
ATOM   2764 N N     . VAL   A 1 362 ? -23.868 32.814 -17.505 1.00 64.70  ?  362 VAL   A N     1 
ATOM   2765 C CA    . VAL   A 1 362 ? -23.524 34.126 -18.024 1.00 69.21  ?  362 VAL   A CA    1 
ATOM   2766 C C     . VAL   A 1 362 ? -22.386 34.641 -17.154 1.00 68.77  ?  362 VAL   A C     1 
ATOM   2767 O O     . VAL   A 1 362 ? -22.559 34.835 -15.940 1.00 74.00  ?  362 VAL   A O     1 
ATOM   2768 C CB    . VAL   A 1 362 ? -24.735 35.092 -18.012 1.00 77.01  ?  362 VAL   A CB    1 
ATOM   2769 C CG1   . VAL   A 1 362 ? -25.375 35.234 -16.596 1.00 73.81  ?  362 VAL   A CG1   1 
ATOM   2770 C CG2   . VAL   A 1 362 ? -24.295 36.489 -18.479 1.00 78.58  ?  362 VAL   A CG2   1 
ATOM   2771 N N     . GLY   A 1 363 ? -21.198 34.779 -17.735 1.00 60.78  ?  363 GLY   A N     1 
ATOM   2772 C CA    . GLY   A 1 363 ? -20.159 35.418 -16.963 1.00 59.36  ?  363 GLY   A CA    1 
ATOM   2773 C C     . GLY   A 1 363 ? -19.456 34.510 -15.970 1.00 57.39  ?  363 GLY   A C     1 
ATOM   2774 O O     . GLY   A 1 363 ? -19.394 33.278 -16.105 1.00 60.24  ?  363 GLY   A O     1 
ATOM   2775 N N     . ALA   A 1 364 ? -18.884 35.161 -14.959 1.00 54.04  ?  364 ALA   A N     1 
ATOM   2776 C CA    . ALA   A 1 364 ? -17.930 34.494 -14.091 1.00 46.67  ?  364 ALA   A CA    1 
ATOM   2777 C C     . ALA   A 1 364 ? -18.639 33.546 -13.136 1.00 53.22  ?  364 ALA   A C     1 
ATOM   2778 O O     . ALA   A 1 364 ? -19.786 33.761 -12.725 1.00 54.85  ?  364 ALA   A O     1 
ATOM   2779 C CB    . ALA   A 1 364 ? -17.095 35.510 -13.318 1.00 47.11  ?  364 ALA   A CB    1 
ATOM   2780 N N     . ILE   A 1 365 ? -17.940 32.465 -12.808 1.00 48.06  ?  365 ILE   A N     1 
ATOM   2781 C CA    . ILE   A 1 365 ? -18.517 31.389 -12.015 1.00 49.75  ?  365 ILE   A CA    1 
ATOM   2782 C C     . ILE   A 1 365 ? -18.229 31.546 -10.525 1.00 53.15  ?  365 ILE   A C     1 
ATOM   2783 O O     . ILE   A 1 365 ? -18.764 30.772 -9.712  1.00 52.47  ?  365 ILE   A O     1 
ATOM   2784 C CB    . ILE   A 1 365 ? -17.984 30.042 -12.556 1.00 49.25  ?  365 ILE   A CB    1 
ATOM   2785 C CG1   . ILE   A 1 365 ? -18.844 28.870 -12.091 1.00 50.61  ?  365 ILE   A CG1   1 
ATOM   2786 C CG2   . ILE   A 1 365 ? -16.511 29.841 -12.181 1.00 48.40  ?  365 ILE   A CG2   1 
ATOM   2787 C CD1   . ILE   A 1 365 ? -18.198 27.528 -12.322 1.00 46.86  ?  365 ILE   A CD1   1 
ATOM   2788 N N     . THR   A 1 366 ? -17.429 32.543 -10.131 1.00 48.88  ?  366 THR   A N     1 
ATOM   2789 C CA    . THR   A 1 366 ? -16.897 32.540 -8.774  1.00 46.46  ?  366 THR   A CA    1 
ATOM   2790 C C     . THR   A 1 366 ? -17.981 32.800 -7.742  1.00 44.71  ?  366 THR   A C     1 
ATOM   2791 O O     . THR   A 1 366 ? -18.031 32.116 -6.714  1.00 43.78  ?  366 THR   A O     1 
ATOM   2792 C CB    . THR   A 1 366 ? -15.772 33.552 -8.621  1.00 47.44  ?  366 THR   A CB    1 
ATOM   2793 O OG1   . THR   A 1 366 ? -14.765 33.297 -9.604  1.00 50.96  ?  366 THR   A OG1   1 
ATOM   2794 C CG2   . THR   A 1 366 ? -15.147 33.412 -7.251  1.00 39.56  ?  366 THR   A CG2   1 
ATOM   2795 N N     . ARG   A 1 367 ? -18.838 33.799 -7.965  1.00 45.23  ?  367 ARG   A N     1 
ATOM   2796 C CA    . ARG   A 1 367 ? -19.864 34.062 -6.957  1.00 44.88  ?  367 ARG   A CA    1 
ATOM   2797 C C     . ARG   A 1 367 ? -20.775 32.862 -6.786  1.00 49.76  ?  367 ARG   A C     1 
ATOM   2798 O O     . ARG   A 1 367 ? -21.243 32.586 -5.669  1.00 44.92  ?  367 ARG   A O     1 
ATOM   2799 C CB    . ARG   A 1 367 ? -20.706 35.281 -7.313  1.00 44.34  ?  367 ARG   A CB    1 
ATOM   2800 C CG    . ARG   A 1 367 ? -19.932 36.522 -7.536  1.00 43.46  ?  367 ARG   A CG    1 
ATOM   2801 C CD    . ARG   A 1 367 ? -19.308 37.006 -6.277  1.00 47.79  ?  367 ARG   A CD    1 
ATOM   2802 N NE    . ARG   A 1 367 ? -18.314 38.008 -6.616  1.00 53.39  ?  367 ARG   A NE    1 
ATOM   2803 C CZ    . ARG   A 1 367 ? -17.024 37.867 -6.373  1.00 50.41  ?  367 ARG   A CZ    1 
ATOM   2804 N NH1   . ARG   A 1 367 ? -16.589 36.761 -5.773  1.00 45.09  ?  367 ARG   A NH1   1 
ATOM   2805 N NH2   . ARG   A 1 367 ? -16.184 38.828 -6.737  1.00 49.24  ?  367 ARG   A NH2   1 
ATOM   2806 N N     . LEU   A 1 368 ? -21.023 32.128 -7.878  1.00 47.78  ?  368 LEU   A N     1 
ATOM   2807 C CA    . LEU   A 1 368 ? -21.905 30.974 -7.782  1.00 48.50  ?  368 LEU   A CA    1 
ATOM   2808 C C     . LEU   A 1 368 ? -21.247 29.845 -6.996  1.00 45.05  ?  368 LEU   A C     1 
ATOM   2809 O O     . LEU   A 1 368 ? -21.886 29.198 -6.164  1.00 42.97  ?  368 LEU   A O     1 
ATOM   2810 C CB    . LEU   A 1 368 ? -22.298 30.485 -9.167  1.00 47.88  ?  368 LEU   A CB    1 
ATOM   2811 C CG    . LEU   A 1 368 ? -23.116 31.341 -10.138 1.00 57.57  ?  368 LEU   A CG    1 
ATOM   2812 C CD1   . LEU   A 1 368 ? -22.358 32.582 -10.670 1.00 57.09  ?  368 LEU   A CD1   1 
ATOM   2813 C CD2   . LEU   A 1 368 ? -23.615 30.460 -11.259 1.00 54.48  ?  368 LEU   A CD2   1 
ATOM   2814 N N     . VAL   A 1 369 ? -19.964 29.607 -7.242  1.00 41.56  ?  369 VAL   A N     1 
ATOM   2815 C CA    . VAL   A 1 369 ? -19.222 28.580 -6.522  1.00 43.15  ?  369 VAL   A CA    1 
ATOM   2816 C C     . VAL   A 1 369 ? -19.160 28.916 -5.035  1.00 43.63  ?  369 VAL   A C     1 
ATOM   2817 O O     . VAL   A 1 369 ? -19.243 28.029 -4.176  1.00 39.99  ?  369 VAL   A O     1 
ATOM   2818 C CB    . VAL   A 1 369 ? -17.826 28.435 -7.159  1.00 42.90  ?  369 VAL   A CB    1 
ATOM   2819 C CG1   . VAL   A 1 369 ? -16.880 27.705 -6.232  1.00 41.60  ?  369 VAL   A CG1   1 
ATOM   2820 C CG2   . VAL   A 1 369 ? -17.979 27.694 -8.441  1.00 46.40  ?  369 VAL   A CG2   1 
ATOM   2821 N N     . GLU   A 1 370 ? -19.011 30.203 -4.709  1.00 41.51  ?  370 GLU   A N     1 
ATOM   2822 C CA    . GLU   A 1 370 ? -19.003 30.622 -3.317  1.00 40.41  ?  370 GLU   A CA    1 
ATOM   2823 C C     . GLU   A 1 370 ? -20.360 30.360 -2.681  1.00 43.31  ?  370 GLU   A C     1 
ATOM   2824 O O     . GLU   A 1 370 ? -20.445 29.816 -1.571  1.00 44.95  ?  370 GLU   A O     1 
ATOM   2825 C CB    . GLU   A 1 370 ? -18.623 32.102 -3.218  1.00 38.59  ?  370 GLU   A CB    1 
ATOM   2826 C CG    . GLU   A 1 370 ? -17.161 32.392 -3.571  1.00 41.24  ?  370 GLU   A CG    1 
ATOM   2827 C CD    . GLU   A 1 370 ? -16.846 33.887 -3.662  1.00 43.11  ?  370 GLU   A CD    1 
ATOM   2828 O OE1   . GLU   A 1 370 ? -15.755 34.294 -3.211  1.00 47.85  ?  370 GLU   A OE1   1 
ATOM   2829 O OE2   . GLU   A 1 370 ? -17.684 34.668 -4.165  1.00 44.23  ?  370 GLU   A OE2   1 
ATOM   2830 N N     . ALA   A 1 371 ? -21.436 30.738 -3.377  1.00 40.04  ?  371 ALA   A N     1 
ATOM   2831 C CA    . ALA   A 1 371 ? -22.781 30.453 -2.894  1.00 38.16  ?  371 ALA   A CA    1 
ATOM   2832 C C     . ALA   A 1 371 ? -22.978 28.958 -2.674  1.00 44.50  ?  371 ALA   A C     1 
ATOM   2833 O O     . ALA   A 1 371 ? -23.481 28.530 -1.625  1.00 44.65  ?  371 ALA   A O     1 
ATOM   2834 C CB    . ALA   A 1 371 ? -23.809 30.988 -3.882  1.00 44.48  ?  371 ALA   A CB    1 
ATOM   2835 N N     . GLN   A 1 372 ? -22.563 28.145 -3.647  1.00 41.05  ?  372 GLN   A N     1 
ATOM   2836 C CA    . GLN   A 1 372 ? -22.684 26.697 -3.516  1.00 43.86  ?  372 GLN   A CA    1 
ATOM   2837 C C     . GLN   A 1 372 ? -21.868 26.177 -2.337  1.00 43.22  ?  372 GLN   A C     1 
ATOM   2838 O O     . GLN   A 1 372 ? -22.350 25.353 -1.555  1.00 43.00  ?  372 GLN   A O     1 
ATOM   2839 C CB    . GLN   A 1 372 ? -22.249 26.012 -4.816  1.00 41.08  ?  372 GLN   A CB    1 
ATOM   2840 C CG    . GLN   A 1 372 ? -23.206 26.153 -5.973  1.00 40.84  ?  372 GLN   A CG    1 
ATOM   2841 C CD    . GLN   A 1 372 ? -22.709 25.400 -7.189  1.00 49.36  ?  372 GLN   A CD    1 
ATOM   2842 O OE1   . GLN   A 1 372 ? -21.526 25.015 -7.252  1.00 45.00  ?  372 GLN   A OE1   1 
ATOM   2843 N NE2   . GLN   A 1 372 ? -23.600 25.174 -8.167  1.00 43.20  ?  372 GLN   A NE2   1 
ATOM   2844 N N     . ALA   A 1 373 ? -20.620 26.640 -2.202  1.00 42.66  ?  373 ALA   A N     1 
ATOM   2845 C CA    . ALA   A 1 373 ? -19.771 26.194 -1.101  1.00 40.87  ?  373 ALA   A CA    1 
ATOM   2846 C C     . ALA   A 1 373 ? -20.405 26.529 0.243   1.00 43.78  ?  373 ALA   A C     1 
ATOM   2847 O O     . ALA   A 1 373 ? -20.449 25.688 1.154   1.00 39.19  ?  373 ALA   A O     1 
ATOM   2848 C CB    . ALA   A 1 373 ? -18.375 26.815 -1.212  1.00 34.32  ?  373 ALA   A CB    1 
ATOM   2849 N N     . GLU   A 1 374 ? -20.918 27.752 0.379   1.00 40.27  ?  374 GLU   A N     1 
ATOM   2850 C CA    . GLU   A 1 374 ? -21.488 28.157 1.658   1.00 44.32  ?  374 GLU   A CA    1 
ATOM   2851 C C     . GLU   A 1 374 ? -22.706 27.305 2.008   1.00 48.63  ?  374 GLU   A C     1 
ATOM   2852 O O     . GLU   A 1 374 ? -22.897 26.916 3.174   1.00 43.68  ?  374 GLU   A O     1 
ATOM   2853 C CB    . GLU   A 1 374 ? -21.854 29.641 1.618   1.00 44.35  ?  374 GLU   A CB    1 
ATOM   2854 C CG    . GLU   A 1 374 ? -21.748 30.316 2.963   1.00 43.83  ?  374 GLU   A CG    1 
ATOM   2855 C CD    . GLU   A 1 374 ? -22.925 29.985 3.866   1.00 54.15  ?  374 GLU   A CD    1 
ATOM   2856 O OE1   . GLU   A 1 374 ? -22.735 29.906 5.116   1.00 59.04  ?  374 GLU   A OE1   1 
ATOM   2857 O OE2   . GLU   A 1 374 ? -24.040 29.810 3.320   1.00 49.42  ?  374 GLU   A OE2   1 
ATOM   2858 N N     . TRP   A 1 375 ? -23.534 26.990 1.005   1.00 43.99  ?  375 TRP   A N     1 
ATOM   2859 C CA    . TRP   A 1 375 ? -24.707 26.167 1.255   1.00 45.66  ?  375 TRP   A CA    1 
ATOM   2860 C C     . TRP   A 1 375 ? -24.307 24.741 1.641   1.00 47.74  ?  375 TRP   A C     1 
ATOM   2861 O O     . TRP   A 1 375 ? -24.835 24.172 2.610   1.00 44.13  ?  375 TRP   A O     1 
ATOM   2862 C CB    . TRP   A 1 375 ? -25.614 26.185 0.021   1.00 47.24  ?  375 TRP   A CB    1 
ATOM   2863 C CG    . TRP   A 1 375 ? -26.954 25.550 0.235   1.00 45.49  ?  375 TRP   A CG    1 
ATOM   2864 C CD1   . TRP   A 1 375 ? -27.781 25.696 1.318   1.00 46.21  ?  375 TRP   A CD1   1 
ATOM   2865 C CD2   . TRP   A 1 375 ? -27.622 24.663 -0.661  1.00 50.43  ?  375 TRP   A CD2   1 
ATOM   2866 N NE1   . TRP   A 1 375 ? -28.914 24.938 1.157   1.00 45.13  ?  375 TRP   A NE1   1 
ATOM   2867 C CE2   . TRP   A 1 375 ? -28.846 24.300 -0.056  1.00 50.91  ?  375 TRP   A CE2   1 
ATOM   2868 C CE3   . TRP   A 1 375 ? -27.309 24.138 -1.920  1.00 45.36  ?  375 TRP   A CE3   1 
ATOM   2869 C CZ2   . TRP   A 1 375 ? -29.745 23.422 -0.668  1.00 44.11  ?  375 TRP   A CZ2   1 
ATOM   2870 C CZ3   . TRP   A 1 375 ? -28.215 23.288 -2.526  1.00 47.61  ?  375 TRP   A CZ3   1 
ATOM   2871 C CH2   . TRP   A 1 375 ? -29.409 22.932 -1.895  1.00 42.67  ?  375 TRP   A CH2   1 
ATOM   2872 N N     . VAL   A 1 376 ? -23.353 24.164 0.913   1.00 47.94  ?  376 VAL   A N     1 
ATOM   2873 C CA    . VAL   A 1 376 ? -22.949 22.791 1.177   1.00 43.11  ?  376 VAL   A CA    1 
ATOM   2874 C C     . VAL   A 1 376 ? -22.396 22.669 2.582   1.00 42.01  ?  376 VAL   A C     1 
ATOM   2875 O O     . VAL   A 1 376 ? -22.671 21.691 3.287   1.00 46.89  ?  376 VAL   A O     1 
ATOM   2876 C CB    . VAL   A 1 376 ? -21.940 22.322 0.113   1.00 39.51  ?  376 VAL   A CB    1 
ATOM   2877 C CG1   . VAL   A 1 376 ? -21.267 21.008 0.515   1.00 31.85  ?  376 VAL   A CG1   1 
ATOM   2878 C CG2   . VAL   A 1 376 ? -22.654 22.178 -1.187  1.00 40.87  ?  376 VAL   A CG2   1 
ATOM   2879 N N     . ALA   A 1 377 ? -21.618 23.659 3.022   1.00 44.11  ?  377 ALA   A N     1 
ATOM   2880 C CA    . ALA   A 1 377 ? -21.020 23.568 4.352   1.00 44.41  ?  377 ALA   A CA    1 
ATOM   2881 C C     . ALA   A 1 377 ? -22.099 23.552 5.430   1.00 46.13  ?  377 ALA   A C     1 
ATOM   2882 O O     . ALA   A 1 377 ? -21.962 22.852 6.444   1.00 42.19  ?  377 ALA   A O     1 
ATOM   2883 C CB    . ALA   A 1 377 ? -20.034 24.717 4.573   1.00 38.25  ?  377 ALA   A CB    1 
ATOM   2884 N N     . ARG   A 1 378 ? -23.204 24.265 5.195   1.00 43.63  ?  378 ARG   A N     1 
ATOM   2885 C CA    . ARG   A 1 378 ? -24.295 24.275 6.156   1.00 46.36  ?  378 ARG   A CA    1 
ATOM   2886 C C     . ARG   A 1 378 ? -25.168 23.029 6.049   1.00 47.53  ?  378 ARG   A C     1 
ATOM   2887 O O     . ARG   A 1 378 ? -25.810 22.648 7.038   1.00 44.19  ?  378 ARG   A O     1 
ATOM   2888 C CB    . ARG   A 1 378 ? -25.125 25.550 5.994   1.00 43.30  ?  378 ARG   A CB    1 
ATOM   2889 C CG    . ARG   A 1 378 ? -24.444 26.783 6.603   1.00 47.12  ?  378 ARG   A CG    1 
ATOM   2890 C CD    . ARG   A 1 378 ? -25.333 28.002 6.521   1.00 45.96  ?  378 ARG   A CD    1 
ATOM   2891 N NE    . ARG   A 1 378 ? -26.238 27.826 5.392   1.00 53.66  ?  378 ARG   A NE    1 
ATOM   2892 C CZ    . ARG   A 1 378 ? -27.058 28.744 4.910   1.00 52.00  ?  378 ARG   A CZ    1 
ATOM   2893 N NH1   . ARG   A 1 378 ? -27.133 29.954 5.465   1.00 70.11  ?  378 ARG   A NH1   1 
ATOM   2894 N NH2   . ARG   A 1 378 ? -27.821 28.435 3.877   1.00 54.53  ?  378 ARG   A NH2   1 
ATOM   2895 N N     . LEU   A 1 379 ? -25.199 22.383 4.877   1.00 44.56  ?  379 LEU   A N     1 
ATOM   2896 C CA    . LEU   A 1 379 ? -25.818 21.066 4.767   1.00 40.93  ?  379 LEU   A CA    1 
ATOM   2897 C C     . LEU   A 1 379 ? -24.989 20.013 5.497   1.00 45.64  ?  379 LEU   A C     1 
ATOM   2898 O O     . LEU   A 1 379 ? -25.544 19.114 6.146   1.00 50.24  ?  379 LEU   A O     1 
ATOM   2899 C CB    . LEU   A 1 379 ? -25.984 20.677 3.300   1.00 40.61  ?  379 LEU   A CB    1 
ATOM   2900 C CG    . LEU   A 1 379 ? -26.907 21.529 2.422   1.00 43.74  ?  379 LEU   A CG    1 
ATOM   2901 C CD1   . LEU   A 1 379 ? -26.846 21.126 0.929   1.00 40.60  ?  379 LEU   A CD1   1 
ATOM   2902 C CD2   . LEU   A 1 379 ? -28.313 21.394 2.958   1.00 45.34  ?  379 LEU   A CD2   1 
ATOM   2903 N N     . VAL   A 1 380 ? -23.660 20.115 5.422   1.00 39.37  ?  380 VAL   A N     1 
ATOM   2904 C CA    . VAL   A 1 380 ? -22.813 19.104 6.049   1.00 44.04  ?  380 VAL   A CA    1 
ATOM   2905 C C     . VAL   A 1 380 ? -23.018 19.081 7.568   1.00 52.40  ?  380 VAL   A C     1 
ATOM   2906 O O     . VAL   A 1 380 ? -22.994 18.010 8.195   1.00 50.02  ?  380 VAL   A O     1 
ATOM   2907 C CB    . VAL   A 1 380 ? -21.337 19.338 5.679   1.00 48.02  ?  380 VAL   A CB    1 
ATOM   2908 C CG1   . VAL   A 1 380 ? -20.421 18.449 6.525   1.00 44.60  ?  380 VAL   A CG1   1 
ATOM   2909 C CG2   . VAL   A 1 380 ? -21.113 19.087 4.189   1.00 43.42  ?  380 VAL   A CG2   1 
ATOM   2910 N N     . ASP   A 1 381 ? -23.223 20.246 8.195   1.00 45.55  ?  381 ASP   A N     1 
ATOM   2911 C CA    . ASP   A 1 381 ? -23.330 20.264 9.650   1.00 48.58  ?  381 ASP   A CA    1 
ATOM   2912 C C     . ASP   A 1 381 ? -24.733 20.600 10.140  1.00 48.69  ?  381 ASP   A C     1 
ATOM   2913 O O     . ASP   A 1 381 ? -24.910 20.936 11.316  1.00 51.31  ?  381 ASP   A O     1 
ATOM   2914 C CB    . ASP   A 1 381 ? -22.291 21.202 10.283  1.00 48.17  ?  381 ASP   A CB    1 
ATOM   2915 C CG    . ASP   A 1 381 ? -22.526 22.654 9.960   1.00 47.90  ?  381 ASP   A CG    1 
ATOM   2916 O OD1   . ASP   A 1 381 ? -23.452 22.961 9.166   1.00 49.46  ?  381 ASP   A OD1   1 
ATOM   2917 O OD2   . ASP   A 1 381 ? -21.772 23.487 10.503  1.00 44.29  ?  381 ASP   A OD2   1 
ATOM   2918 N N     . GLY   A 1 382 ? -25.739 20.503 9.274   1.00 46.64  ?  382 GLY   A N     1 
ATOM   2919 C CA    . GLY   A 1 382 ? -27.105 20.547 9.739   1.00 43.39  ?  382 GLY   A CA    1 
ATOM   2920 C C     . GLY   A 1 382 ? -27.710 21.918 9.913   1.00 47.24  ?  382 GLY   A C     1 
ATOM   2921 O O     . GLY   A 1 382 ? -28.912 22.010 10.207  1.00 55.50  ?  382 GLY   A O     1 
ATOM   2922 N N     . ALA   A 1 383 ? -26.938 22.988 9.734   1.00 45.13  ?  383 ALA   A N     1 
ATOM   2923 C CA    . ALA   A 1 383 ? -27.544 24.315 9.687   1.00 41.41  ?  383 ALA   A CA    1 
ATOM   2924 C C     . ALA   A 1 383 ? -28.574 24.436 8.553   1.00 45.24  ?  383 ALA   A C     1 
ATOM   2925 O O     . ALA   A 1 383 ? -29.520 25.222 8.652   1.00 45.41  ?  383 ALA   A O     1 
ATOM   2926 C CB    . ALA   A 1 383 ? -26.445 25.364 9.543   1.00 42.54  ?  383 ALA   A CB    1 
ATOM   2927 N N     . ALA   A 1 384 ? -28.413 23.677 7.475   1.00 43.59  ?  384 ALA   A N     1 
ATOM   2928 C CA    . ALA   A 1 384 ? -29.351 23.679 6.361   1.00 45.54  ?  384 ALA   A CA    1 
ATOM   2929 C C     . ALA   A 1 384 ? -29.825 22.258 6.118   1.00 43.55  ?  384 ALA   A C     1 
ATOM   2930 O O     . ALA   A 1 384 ? -29.108 21.294 6.399   1.00 47.76  ?  384 ALA   A O     1 
ATOM   2931 C CB    . ALA   A 1 384 ? -28.722 24.252 5.073   1.00 38.95  ?  384 ALA   A CB    1 
ATOM   2932 N N     . VAL   A 1 385 ? -31.055 22.133 5.622   1.00 43.08  ?  385 VAL   A N     1 
ATOM   2933 C CA    . VAL   A 1 385 ? -31.660 20.835 5.356   1.00 44.95  ?  385 VAL   A CA    1 
ATOM   2934 C C     . VAL   A 1 385 ? -32.200 20.857 3.934   1.00 44.60  ?  385 VAL   A C     1 
ATOM   2935 O O     . VAL   A 1 385 ? -32.401 21.919 3.343   1.00 45.93  ?  385 VAL   A O     1 
ATOM   2936 C CB    . VAL   A 1 385 ? -32.788 20.466 6.357   1.00 43.34  ?  385 VAL   A CB    1 
ATOM   2937 C CG1   . VAL   A 1 385 ? -32.287 20.514 7.802   1.00 40.87  ?  385 VAL   A CG1   1 
ATOM   2938 C CG2   . VAL   A 1 385 ? -34.000 21.361 6.156   1.00 41.22  ?  385 VAL   A CG2   1 
ATOM   2939 N N     . LEU   A 1 386 ? -32.426 19.666 3.387   1.00 45.92  ?  386 LEU   A N     1 
ATOM   2940 C CA    . LEU   A 1 386 ? -32.907 19.489 2.024   1.00 45.53  ?  386 LEU   A CA    1 
ATOM   2941 C C     . LEU   A 1 386 ? -34.365 19.079 2.028   1.00 48.22  ?  386 LEU   A C     1 
ATOM   2942 O O     . LEU   A 1 386 ? -34.870 18.552 3.027   1.00 51.36  ?  386 LEU   A O     1 
ATOM   2943 C CB    . LEU   A 1 386 ? -32.109 18.417 1.270   1.00 43.36  ?  386 LEU   A CB    1 
ATOM   2944 C CG    . LEU   A 1 386 ? -30.587 18.407 1.317   1.00 43.18  ?  386 LEU   A CG    1 
ATOM   2945 C CD1   . LEU   A 1 386 ? -30.106 16.995 0.955   1.00 45.74  ?  386 LEU   A CD1   1 
ATOM   2946 C CD2   . LEU   A 1 386 ? -30.041 19.405 0.346   1.00 39.88  ?  386 LEU   A CD2   1 
ATOM   2947 N N     . PRO   A 1 387 ? -35.083 19.321 0.932   1.00 50.34  ?  387 PRO   A N     1 
ATOM   2948 C CA    . PRO   A 1 387 ? -36.427 18.750 0.775   1.00 46.00  ?  387 PRO   A CA    1 
ATOM   2949 C C     . PRO   A 1 387 ? -36.375 17.240 0.644   1.00 45.74  ?  387 PRO   A C     1 
ATOM   2950 O O     . PRO   A 1 387 ? -35.358 16.655 0.275   1.00 50.81  ?  387 PRO   A O     1 
ATOM   2951 C CB    . PRO   A 1 387 ? -36.937 19.378 -0.526  1.00 49.75  ?  387 PRO   A CB    1 
ATOM   2952 C CG    . PRO   A 1 387 ? -35.754 20.014 -1.173  1.00 48.52  ?  387 PRO   A CG    1 
ATOM   2953 C CD    . PRO   A 1 387 ? -34.775 20.328 -0.096  1.00 47.51  ?  387 PRO   A CD    1 
ATOM   2954 N N     . ALA   A 1 388 ? -37.509 16.606 0.918   1.00 49.38  ?  388 ALA   A N     1 
ATOM   2955 C CA    . ALA   A 1 388 ? -37.618 15.173 0.662   1.00 48.65  ?  388 ALA   A CA    1 
ATOM   2956 C C     . ALA   A 1 388 ? -37.304 14.898 -0.809  1.00 45.54  ?  388 ALA   A C     1 
ATOM   2957 O O     . ALA   A 1 388 ? -37.400 15.805 -1.641  1.00 49.14  ?  388 ALA   A O     1 
ATOM   2958 C CB    . ALA   A 1 388 ? -39.004 14.663 1.051   1.00 40.74  ?  388 ALA   A CB    1 
ATOM   2959 N N     . ALA   A 1 389 ? -36.918 13.661 -1.139  1.00 44.13  ?  389 ALA   A N     1 
ATOM   2960 C CA    . ALA   A 1 389 ? -36.359 13.385 -2.462  1.00 48.63  ?  389 ALA   A CA    1 
ATOM   2961 C C     . ALA   A 1 389 ? -37.357 13.667 -3.577  1.00 52.78  ?  389 ALA   A C     1 
ATOM   2962 O O     . ALA   A 1 389 ? -36.989 14.240 -4.611  1.00 48.66  ?  389 ALA   A O     1 
ATOM   2963 C CB    . ALA   A 1 389 ? -35.870 11.946 -2.548  1.00 41.45  ?  389 ALA   A CB    1 
ATOM   2964 N N     . ASP   A 1 390 ? -38.617 13.262 -3.398  1.00 53.67  ?  390 ASP   A N     1 
ATOM   2965 C CA    . ASP   A 1 390 ? -39.625 13.555 -4.409  1.00 52.12  ?  390 ASP   A CA    1 
ATOM   2966 C C     . ASP   A 1 390 ? -39.699 15.052 -4.691  1.00 56.21  ?  390 ASP   A C     1 
ATOM   2967 O O     . ASP   A 1 390 ? -39.806 15.470 -5.852  1.00 54.97  ?  390 ASP   A O     1 
ATOM   2968 C CB    . ASP   A 1 390 ? -40.983 13.010 -3.966  1.00 56.07  ?  390 ASP   A CB    1 
ATOM   2969 C CG    . ASP   A 1 390 ? -40.970 11.500 -3.782  1.00 66.12  ?  390 ASP   A CG    1 
ATOM   2970 O OD1   . ASP   A 1 390 ? -40.124 10.839 -4.428  1.00 67.96  ?  390 ASP   A OD1   1 
ATOM   2971 O OD2   . ASP   A 1 390 ? -41.789 10.975 -2.989  1.00 67.26  ?  390 ASP   A OD2   1 
ATOM   2972 N N     . GLN   A 1 391 ? -39.595 15.877 -3.644  1.00 55.56  ?  391 GLN   A N     1 
ATOM   2973 C CA    . GLN   A 1 391 ? -39.615 17.325 -3.837  1.00 53.28  ?  391 GLN   A CA    1 
ATOM   2974 C C     . GLN   A 1 391 ? -38.358 17.808 -4.552  1.00 51.05  ?  391 GLN   A C     1 
ATOM   2975 O O     . GLN   A 1 391 ? -38.418 18.725 -5.378  1.00 51.90  ?  391 GLN   A O     1 
ATOM   2976 C CB    . GLN   A 1 391 ? -39.765 18.030 -2.491  1.00 51.45  ?  391 GLN   A CB    1 
ATOM   2977 C CG    . GLN   A 1 391 ? -41.189 18.159 -2.022  1.00 48.60  ?  391 GLN   A CG    1 
ATOM   2978 C CD    . GLN   A 1 391 ? -41.951 16.857 -2.112  1.00 54.06  ?  391 GLN   A CD    1 
ATOM   2979 O OE1   . GLN   A 1 391 ? -41.542 15.836 -1.540  1.00 50.79  ?  391 GLN   A OE1   1 
ATOM   2980 N NE2   . GLN   A 1 391 ? -43.070 16.878 -2.843  1.00 56.41  ?  391 GLN   A NE2   1 
ATOM   2981 N N     . MET   A 1 392 ? -37.208 17.211 -4.246  1.00 50.21  ?  392 MET   A N     1 
ATOM   2982 C CA    . MET   A 1 392 ? -35.984 17.615 -4.919  1.00 49.79  ?  392 MET   A CA    1 
ATOM   2983 C C     . MET   A 1 392 ? -36.090 17.392 -6.426  1.00 53.06  ?  392 MET   A C     1 
ATOM   2984 O O     . MET   A 1 392 ? -35.798 18.299 -7.218  1.00 49.00  ?  392 MET   A O     1 
ATOM   2985 C CB    . MET   A 1 392 ? -34.794 16.866 -4.321  1.00 47.13  ?  392 MET   A CB    1 
ATOM   2986 C CG    . MET   A 1 392 ? -34.091 17.662 -3.236  1.00 48.30  ?  392 MET   A CG    1 
ATOM   2987 S SD    . MET   A 1 392 ? -32.464 17.049 -2.757  1.00 57.09  ?  392 MET   A SD    1 
ATOM   2988 C CE    . MET   A 1 392 ? -32.934 15.465 -2.054  1.00 34.83  ?  392 MET   A CE    1 
ATOM   2989 N N     . ARG   A 1 393 ? -36.542 16.202 -6.850  1.00 49.36  ?  393 ARG   A N     1 
ATOM   2990 C CA    . ARG   A 1 393 ? -36.618 15.985 -8.290  1.00 54.70  ?  393 ARG   A CA    1 
ATOM   2991 C C     . ARG   A 1 393 ? -37.759 16.747 -8.949  1.00 56.48  ?  393 ARG   A C     1 
ATOM   2992 O O     . ARG   A 1 393 ? -37.770 16.854 -10.184 1.00 57.23  ?  393 ARG   A O     1 
ATOM   2993 C CB    . ARG   A 1 393 ? -36.732 14.503 -8.644  1.00 56.14  ?  393 ARG   A CB    1 
ATOM   2994 C CG    . ARG   A 1 393 ? -37.360 13.631 -7.640  1.00 53.41  ?  393 ARG   A CG    1 
ATOM   2995 C CD    . ARG   A 1 393 ? -37.094 12.182 -8.006  1.00 49.59  ?  393 ARG   A CD    1 
ATOM   2996 N NE    . ARG   A 1 393 ? -37.612 11.315 -6.958  1.00 57.69  ?  393 ARG   A NE    1 
ATOM   2997 C CZ    . ARG   A 1 393 ? -36.861 10.491 -6.245  1.00 54.18  ?  393 ARG   A CZ    1 
ATOM   2998 N NH1   . ARG   A 1 393 ? -35.564 10.412 -6.501  1.00 56.44  ?  393 ARG   A NH1   1 
ATOM   2999 N NH2   . ARG   A 1 393 ? -37.407 9.753  -5.287  1.00 54.66  ?  393 ARG   A NH2   1 
ATOM   3000 N N     . GLU   A 1 394 ? -38.702 17.285 -8.173  1.00 55.05  ?  394 GLU   A N     1 
ATOM   3001 C CA    . GLU   A 1 394 ? -39.641 18.246 -8.744  1.00 54.52  ?  394 GLU   A CA    1 
ATOM   3002 C C     . GLU   A 1 394 ? -38.931 19.518 -9.199  1.00 56.49  ?  394 GLU   A C     1 
ATOM   3003 O O     . GLU   A 1 394 ? -39.216 20.038 -10.288 1.00 58.29  ?  394 GLU   A O     1 
ATOM   3004 C CB    . GLU   A 1 394 ? -40.741 18.557 -7.740  1.00 49.86  ?  394 GLU   A CB    1 
ATOM   3005 C CG    . GLU   A 1 394 ? -41.536 17.320 -7.417  1.00 54.73  ?  394 GLU   A CG    1 
ATOM   3006 C CD    . GLU   A 1 394 ? -42.720 17.584 -6.514  1.00 60.62  ?  394 GLU   A CD    1 
ATOM   3007 O OE1   . GLU   A 1 394 ? -43.249 18.714 -6.552  1.00 60.34  ?  394 GLU   A OE1   1 
ATOM   3008 O OE2   . GLU   A 1 394 ? -43.125 16.651 -5.775  1.00 63.38  ?  394 GLU   A OE2   1 
ATOM   3009 N N     . GLU   A 1 395 ? -37.993 20.032 -8.397  1.00 51.91  ?  395 GLU   A N     1 
ATOM   3010 C CA    . GLU   A 1 395 ? -37.252 21.208 -8.843  1.00 50.03  ?  395 GLU   A CA    1 
ATOM   3011 C C     . GLU   A 1 395 ? -36.353 20.868 -10.026 1.00 52.93  ?  395 GLU   A C     1 
ATOM   3012 O O     . GLU   A 1 395 ? -36.187 21.687 -10.939 1.00 53.87  ?  395 GLU   A O     1 
ATOM   3013 C CB    . GLU   A 1 395 ? -36.449 21.803 -7.685  1.00 44.38  ?  395 GLU   A CB    1 
ATOM   3014 C CG    . GLU   A 1 395 ? -35.759 23.112 -8.011  1.00 45.29  ?  395 GLU   A CG    1 
ATOM   3015 C CD    . GLU   A 1 395 ? -34.380 22.896 -8.607  1.00 48.71  ?  395 GLU   A CD    1 
ATOM   3016 O OE1   . GLU   A 1 395 ? -33.862 23.805 -9.298  1.00 43.57  ?  395 GLU   A OE1   1 
ATOM   3017 O OE2   . GLU   A 1 395 ? -33.823 21.796 -8.385  1.00 48.90  ?  395 GLU   A OE2   1 
ATOM   3018 N N     . ILE   A 1 396 ? -35.781 19.659 -10.044 1.00 51.97  ?  396 ILE   A N     1 
ATOM   3019 C CA    . ILE   A 1 396 ? -34.986 19.247 -11.200 1.00 53.03  ?  396 ILE   A CA    1 
ATOM   3020 C C     . ILE   A 1 396 ? -35.862 19.191 -12.448 1.00 56.90  ?  396 ILE   A C     1 
ATOM   3021 O O     . ILE   A 1 396 ? -35.444 19.598 -13.541 1.00 56.73  ?  396 ILE   A O     1 
ATOM   3022 C CB    . ILE   A 1 396 ? -34.289 17.900 -10.927 1.00 53.48  ?  396 ILE   A CB    1 
ATOM   3023 C CG1   . ILE   A 1 396 ? -33.272 18.031 -9.793  1.00 52.06  ?  396 ILE   A CG1   1 
ATOM   3024 C CG2   . ILE   A 1 396 ? -33.574 17.394 -12.177 1.00 53.33  ?  396 ILE   A CG2   1 
ATOM   3025 C CD1   . ILE   A 1 396 ? -32.901 16.705 -9.167  1.00 45.19  ?  396 ILE   A CD1   1 
ATOM   3026 N N     . GLY   A 1 397 ? -37.100 18.707 -12.298 1.00 59.66  ?  397 GLY   A N     1 
ATOM   3027 C CA    . GLY   A 1 397 ? -38.023 18.674 -13.424 1.00 56.60  ?  397 GLY   A CA    1 
ATOM   3028 C C     . GLY   A 1 397 ? -38.307 20.055 -13.982 1.00 59.93  ?  397 GLY   A C     1 
ATOM   3029 O O     . GLY   A 1 397 ? -38.227 20.278 -15.195 1.00 64.07  ?  397 GLY   A O     1 
ATOM   3030 N N     . THR   A 1 398 ? -38.632 21.007 -13.103 1.00 52.36  ?  398 THR   A N     1 
ATOM   3031 C CA    . THR   A 1 398 ? -38.854 22.378 -13.558 1.00 57.59  ?  398 THR   A CA    1 
ATOM   3032 C C     . THR   A 1 398 ? -37.609 22.976 -14.213 1.00 62.33  ?  398 THR   A C     1 
ATOM   3033 O O     . THR   A 1 398 ? -37.713 23.638 -15.251 1.00 63.18  ?  398 THR   A O     1 
ATOM   3034 C CB    . THR   A 1 398 ? -39.304 23.256 -12.397 1.00 56.84  ?  398 THR   A CB    1 
ATOM   3035 O OG1   . THR   A 1 398 ? -40.523 22.738 -11.855 1.00 59.81  ?  398 THR   A OG1   1 
ATOM   3036 C CG2   . THR   A 1 398 ? -39.506 24.686 -12.876 1.00 49.86  ?  398 THR   A CG2   1 
ATOM   3037 N N     . TYR   A 1 399 ? -36.428 22.783 -13.611 1.00 59.11  ?  399 TYR   A N     1 
ATOM   3038 C CA    . TYR   A 1 399 ? -35.203 23.287 -14.232 1.00 60.32  ?  399 TYR   A CA    1 
ATOM   3039 C C     . TYR   A 1 399 ? -35.025 22.713 -15.628 1.00 61.20  ?  399 TYR   A C     1 
ATOM   3040 O O     . TYR   A 1 399 ? -34.693 23.445 -16.572 1.00 62.06  ?  399 TYR   A O     1 
ATOM   3041 C CB    . TYR   A 1 399 ? -33.971 22.953 -13.372 1.00 56.13  ?  399 TYR   A CB    1 
ATOM   3042 C CG    . TYR   A 1 399 ? -32.641 23.241 -14.067 1.00 52.63  ?  399 TYR   A CG    1 
ATOM   3043 C CD1   . TYR   A 1 399 ? -32.167 24.550 -14.187 1.00 50.81  ?  399 TYR   A CD1   1 
ATOM   3044 C CD2   . TYR   A 1 399 ? -31.865 22.207 -14.611 1.00 49.96  ?  399 TYR   A CD2   1 
ATOM   3045 C CE1   . TYR   A 1 399 ? -30.961 24.831 -14.822 1.00 52.13  ?  399 TYR   A CE1   1 
ATOM   3046 C CE2   . TYR   A 1 399 ? -30.650 22.473 -15.254 1.00 51.71  ?  399 TYR   A CE2   1 
ATOM   3047 C CZ    . TYR   A 1 399 ? -30.200 23.793 -15.359 1.00 61.57  ?  399 TYR   A CZ    1 
ATOM   3048 O OH    . TYR   A 1 399 ? -28.997 24.092 -15.999 1.00 60.28  ?  399 TYR   A OH    1 
ATOM   3049 N N     . LEU   A 1 400 ? -35.260 21.402 -15.776 1.00 60.43  ?  400 LEU   A N     1 
ATOM   3050 C CA    . LEU   A 1 400 ? -34.891 20.681 -16.991 1.00 62.74  ?  400 LEU   A CA    1 
ATOM   3051 C C     . LEU   A 1 400 ? -35.832 21.005 -18.141 1.00 67.46  ?  400 LEU   A C     1 
ATOM   3052 O O     . LEU   A 1 400 ? -35.380 21.293 -19.256 1.00 67.44  ?  400 LEU   A O     1 
ATOM   3053 C CB    . LEU   A 1 400 ? -34.867 19.171 -16.729 1.00 60.13  ?  400 LEU   A CB    1 
ATOM   3054 C CG    . LEU   A 1 400 ? -33.590 18.585 -16.126 1.00 57.42  ?  400 LEU   A CG    1 
ATOM   3055 C CD1   . LEU   A 1 400 ? -33.622 17.073 -16.123 1.00 56.45  ?  400 LEU   A CD1   1 
ATOM   3056 C CD2   . LEU   A 1 400 ? -32.394 19.083 -16.907 1.00 62.15  ?  400 LEU   A CD2   1 
ATOM   3057 N N     . THR   A 1 401 ? -37.144 20.956 -17.893 1.00 64.53  ?  401 THR   A N     1 
ATOM   3058 C CA    . THR   A 1 401 ? -38.091 21.292 -18.949 1.00 70.90  ?  401 THR   A CA    1 
ATOM   3059 C C     . THR   A 1 401 ? -37.888 22.732 -19.413 1.00 75.34  ?  401 THR   A C     1 
ATOM   3060 O O     . THR   A 1 401 ? -37.962 23.027 -20.614 1.00 72.98  ?  401 THR   A O     1 
ATOM   3061 C CB    . THR   A 1 401 ? -39.523 21.060 -18.466 1.00 69.46  ?  401 THR   A CB    1 
ATOM   3062 O OG1   . THR   A 1 401 ? -39.732 21.782 -17.250 1.00 67.86  ?  401 THR   A OG1   1 
ATOM   3063 C CG2   . THR   A 1 401 ? -39.795 19.552 -18.235 1.00 59.28  ?  401 THR   A CG2   1 
ATOM   3064 N N     . GLY   A 1 402 ? -37.593 23.633 -18.475 1.00 71.86  ?  402 GLY   A N     1 
ATOM   3065 C CA    . GLY   A 1 402 ? -37.209 24.981 -18.848 1.00 64.17  ?  402 GLY   A CA    1 
ATOM   3066 C C     . GLY   A 1 402 ? -35.907 25.029 -19.614 1.00 69.06  ?  402 GLY   A C     1 
ATOM   3067 O O     . GLY   A 1 402 ? -35.697 25.926 -20.430 1.00 80.51  ?  402 GLY   A O     1 
ATOM   3068 N N     . ILE   A 1 403 ? -35.020 24.065 -19.381 1.00 71.12  ?  403 ILE   A N     1 
ATOM   3069 C CA    . ILE   A 1 403 ? -33.775 24.022 -20.146 1.00 76.52  ?  403 ILE   A CA    1 
ATOM   3070 C C     . ILE   A 1 403 ? -34.041 23.587 -21.584 1.00 79.69  ?  403 ILE   A C     1 
ATOM   3071 O O     . ILE   A 1 403 ? -33.539 24.202 -22.533 1.00 79.83  ?  403 ILE   A O     1 
ATOM   3072 C CB    . ILE   A 1 403 ? -32.744 23.106 -19.463 1.00 70.14  ?  403 ILE   A CB    1 
ATOM   3073 C CG1   . ILE   A 1 403 ? -32.074 23.834 -18.298 1.00 65.78  ?  403 ILE   A CG1   1 
ATOM   3074 C CG2   . ILE   A 1 403 ? -31.702 22.666 -20.458 1.00 72.72  ?  403 ILE   A CG2   1 
ATOM   3075 C CD1   . ILE   A 1 403 ? -31.304 25.076 -18.719 1.00 69.28  ?  403 ILE   A CD1   1 
ATOM   3076 N N     . VAL   A 1 404 ? -34.817 22.509 -21.769 1.00 82.80  ?  404 VAL   A N     1 
ATOM   3077 C CA    . VAL   A 1 404 ? -35.127 22.046 -23.124 1.00 84.71  ?  404 VAL   A CA    1 
ATOM   3078 C C     . VAL   A 1 404 ? -35.896 23.116 -23.884 1.00 81.75  ?  404 VAL   A C     1 
ATOM   3079 O O     . VAL   A 1 404 ? -35.713 23.277 -25.095 1.00 80.78  ?  404 VAL   A O     1 
ATOM   3080 C CB    . VAL   A 1 404 ? -35.892 20.695 -23.108 1.00 78.85  ?  404 VAL   A CB    1 
ATOM   3081 C CG1   . VAL   A 1 404 ? -35.256 19.707 -22.126 1.00 68.82  ?  404 VAL   A CG1   1 
ATOM   3082 C CG2   . VAL   A 1 404 ? -37.386 20.882 -22.816 1.00 76.41  ?  404 VAL   A CG2   1 
ATOM   3083 N N     . GLN   A 1 405 ? -36.732 23.891 -23.186 1.00 78.09  ?  405 GLN   A N     1 
ATOM   3084 C CA    . GLN   A 1 405 ? -37.458 24.974 -23.837 1.00 79.16  ?  405 GLN   A CA    1 
ATOM   3085 C C     . GLN   A 1 405 ? -36.512 26.066 -24.319 1.00 81.13  ?  405 GLN   A C     1 
ATOM   3086 O O     . GLN   A 1 405 ? -36.593 26.510 -25.467 1.00 86.68  ?  405 GLN   A O     1 
ATOM   3087 C CB    . GLN   A 1 405 ? -38.502 25.558 -22.885 1.00 76.88  ?  405 GLN   A CB    1 
ATOM   3088 C CG    . GLN   A 1 405 ? -39.692 24.657 -22.644 1.00 80.98  ?  405 GLN   A CG    1 
ATOM   3089 C CD    . GLN   A 1 405 ? -40.593 25.176 -21.545 1.00 87.15  ?  405 GLN   A CD    1 
ATOM   3090 O OE1   . GLN   A 1 405 ? -40.739 26.389 -21.370 1.00 86.16  ?  405 GLN   A OE1   1 
ATOM   3091 N NE2   . GLN   A 1 405 ? -41.187 24.260 -20.780 1.00 84.71  ?  405 GLN   A NE2   1 
ATOM   3092 N N     . ARG   A 1 406 ? -35.612 26.525 -23.457 1.00 88.28  ?  406 ARG   A N     1 
ATOM   3093 C CA    . ARG   A 1 406 ? -34.806 27.694 -23.812 1.00 95.47  ?  406 ARG   A CA    1 
ATOM   3094 C C     . ARG   A 1 406 ? -33.593 27.293 -24.650 1.00 93.05  ?  406 ARG   A C     1 
ATOM   3095 O O     . ARG   A 1 406 ? -33.528 27.582 -25.847 1.00 93.09  ?  406 ARG   A O     1 
ATOM   3096 C CB    . ARG   A 1 406 ? -34.394 28.448 -22.542 1.00 92.92  ?  406 ARG   A CB    1 
ATOM   3097 C CG    . ARG   A 1 406 ? -33.469 29.630 -22.780 1.00 94.70  ?  406 ARG   A CG    1 
ATOM   3098 C CD    . ARG   A 1 406 ? -33.413 30.564 -21.572 1.00 102.13 ?  406 ARG   A CD    1 
ATOM   3099 N NE    . ARG   A 1 406 ? -34.725 30.966 -21.049 1.00 107.58 ?  406 ARG   A NE    1 
ATOM   3100 C CZ    . ARG   A 1 406 ? -35.413 32.023 -21.480 1.00 110.15 ?  406 ARG   A CZ    1 
ATOM   3101 N NH1   . ARG   A 1 406 ? -34.927 32.766 -22.463 1.00 112.31 ?  406 ARG   A NH1   1 
ATOM   3102 N NH2   . ARG   A 1 406 ? -36.591 32.332 -20.940 1.00 104.53 ?  406 ARG   A NH2   1 
ATOM   3103 N N     . TYR   A 1 407 ? -32.683 26.480 -24.125 1.00 97.98  ?  407 TYR   A N     1 
ATOM   3104 C CA    . TYR   A 1 407 ? -31.410 26.207 -24.857 1.00 98.04  ?  407 TYR   A CA    1 
ATOM   3105 C C     . TYR   A 1 407 ? -31.521 24.974 -25.717 1.00 92.47  ?  407 TYR   A C     1 
ATOM   3106 O O     . TYR   A 1 407 ? -30.600 24.693 -26.500 1.00 90.47  ?  407 TYR   A O     1 
ATOM   3107 C CB    . TYR   A 1 407 ? -30.302 26.091 -23.805 1.00 96.25  ?  407 TYR   A CB    1 
ATOM   3108 C CG    . TYR   A 1 407 ? -30.136 27.379 -23.018 1.00 90.35  ?  407 TYR   A CG    1 
ATOM   3109 C CD1   . TYR   A 1 407 ? -29.505 28.476 -23.582 1.00 92.90  ?  407 TYR   A CD1   1 
ATOM   3110 C CD2   . TYR   A 1 407 ? -30.647 27.509 -21.737 1.00 87.85  ?  407 TYR   A CD2   1 
ATOM   3111 C CE1   . TYR   A 1 407 ? -29.368 29.663 -22.886 1.00 100.18 ?  407 TYR   A CE1   1 
ATOM   3112 C CE2   . TYR   A 1 407 ? -30.518 28.690 -21.030 1.00 93.52  ?  407 TYR   A CE2   1 
ATOM   3113 C CZ    . TYR   A 1 407 ? -29.883 29.772 -21.609 1.00 95.06  ?  407 TYR   A CZ    1 
ATOM   3114 O OH    . TYR   A 1 407 ? -29.754 30.941 -20.921 1.00 90.87  ?  407 TYR   A OH    1 
ATOM   3115 N N     . GLY   A 1 408 ? -32.615 24.241 -25.563 1.00 90.56  ?  408 GLY   A N     1 
ATOM   3116 C CA    . GLY   A 1 408 ? -32.839 23.062 -26.408 1.00 91.76  ?  408 GLY   A CA    1 
ATOM   3117 C C     . GLY   A 1 408 ? -32.100 21.857 -25.899 1.00 96.59  ?  408 GLY   A C     1 
ATOM   3118 O O     . GLY   A 1 408 ? -31.417 21.975 -24.873 1.00 98.19  ?  408 GLY   A O     1 
ATOM   3119 N N     . ARG   A 1 409 ? -32.226 20.736 -26.603 1.00 99.47  ?  409 ARG   A N     1 
ATOM   3120 C CA    . ARG   A 1 409 ? -31.597 19.473 -26.149 1.00 105.00 ?  409 ARG   A CA    1 
ATOM   3121 C C     . ARG   A 1 409 ? -30.153 19.447 -26.647 1.00 105.59 ?  409 ARG   A C     1 
ATOM   3122 O O     . ARG   A 1 409 ? -29.709 18.396 -27.138 1.00 106.13 ?  409 ARG   A O     1 
ATOM   3123 C CB    . ARG   A 1 409 ? -32.389 18.249 -26.619 1.00 105.85 ?  409 ARG   A CB    1 
ATOM   3124 C CG    . ARG   A 1 409 ? -32.888 18.310 -28.055 1.00 113.59 ?  409 ARG   A CG    1 
ATOM   3125 C CD    . ARG   A 1 409 ? -33.024 16.916 -28.645 1.00 112.11 ?  409 ARG   A CD    1 
ATOM   3126 N NE    . ARG   A 1 409 ? -33.278 16.939 -30.089 1.00 122.24 ?  409 ARG   A NE    1 
ATOM   3127 C CZ    . ARG   A 1 409 ? -34.402 17.366 -30.650 1.00 125.23 ?  409 ARG   A CZ    1 
ATOM   3128 N NH1   . ARG   A 1 409 ? -35.543 17.297 -29.988 1.00 123.69 ?  409 ARG   A NH1   1 
ATOM   3129 N NH2   . ARG   A 1 409 ? -34.380 17.859 -31.875 1.00 114.68 ?  409 ARG   A NH2   1 
ATOM   3130 N N     . THR   A 1 410 ? -29.446 20.563 -26.491 1.00 109.11 ?  410 THR   A N     1 
ATOM   3131 C CA    . THR   A 1 410 ? -28.020 20.612 -26.861 1.00 105.81 ?  410 THR   A CA    1 
ATOM   3132 C C     . THR   A 1 410 ? -27.234 19.855 -25.817 1.00 104.28 ?  410 THR   A C     1 
ATOM   3133 O O     . THR   A 1 410 ? -27.838 19.318 -24.877 1.00 104.47 ?  410 THR   A O     1 
ATOM   3134 C CB    . THR   A 1 410 ? -27.598 22.072 -26.989 1.00 101.33 ?  410 THR   A CB    1 
ATOM   3135 O OG1   . THR   A 1 410 ? -26.422 22.026 -27.788 1.00 105.92 ?  410 THR   A OG1   1 
ATOM   3136 C CG2   . THR   A 1 410 ? -27.303 22.725 -25.652 1.00 101.19 ?  410 THR   A CG2   1 
ATOM   3137 N N     . GLU   A 1 411 ? -25.925 19.789 -25.978 1.00 101.89 ?  411 GLU   A N     1 
ATOM   3138 C CA    . GLU   A 1 411 ? -25.076 19.098 -24.994 1.00 97.69  ?  411 GLU   A CA    1 
ATOM   3139 C C     . GLU   A 1 411 ? -24.557 20.103 -23.977 1.00 98.31  ?  411 GLU   A C     1 
ATOM   3140 O O     . GLU   A 1 411 ? -23.807 21.001 -24.391 1.00 100.16 ?  411 GLU   A O     1 
ATOM   3141 C CB    . GLU   A 1 411 ? -23.886 18.561 -25.769 1.00 107.92 ?  411 GLU   A CB    1 
ATOM   3142 C CG    . GLU   A 1 411 ? -24.281 17.759 -27.007 1.00 118.29 ?  411 GLU   A CG    1 
ATOM   3143 C CD    . GLU   A 1 411 ? -24.440 18.525 -28.310 1.00 119.55 ?  411 GLU   A CD    1 
ATOM   3144 O OE1   . GLU   A 1 411 ? -25.597 18.837 -28.656 1.00 119.67 ?  411 GLU   A OE1   1 
ATOM   3145 O OE2   . GLU   A 1 411 ? -23.425 18.807 -28.979 1.00 120.75 ?  411 GLU   A OE2   1 
ATOM   3146 N N     . GLY   A 1 412 ? -24.960 19.985 -22.714 1.00 87.84  ?  412 GLY   A N     1 
ATOM   3147 C CA    . GLY   A 1 412 ? -24.401 20.857 -21.673 1.00 81.62  ?  412 GLY   A CA    1 
ATOM   3148 C C     . GLY   A 1 412 ? -25.322 21.992 -21.320 1.00 79.13  ?  412 GLY   A C     1 
ATOM   3149 O O     . GLY   A 1 412 ? -24.850 22.982 -20.745 1.00 79.68  ?  412 GLY   A O     1 
ATOM   3150 N N     . ALA   A 1 413 ? -26.592 21.854 -21.647 1.00 80.28  ?  413 ALA   A N     1 
ATOM   3151 C CA    . ALA   A 1 413 ? -27.558 22.886 -21.242 1.00 79.09  ?  413 ALA   A CA    1 
ATOM   3152 C C     . ALA   A 1 413 ? -28.096 22.497 -19.873 1.00 72.42  ?  413 ALA   A C     1 
ATOM   3153 O O     . ALA   A 1 413 ? -28.701 23.332 -19.205 1.00 69.35  ?  413 ALA   A O     1 
ATOM   3154 C CB    . ALA   A 1 413 ? -28.625 22.953 -22.282 1.00 84.05  ?  413 ALA   A CB    1 
ATOM   3155 N N     . SER   A 1 414 ? -27.834 21.261 -19.469 1.00 67.03  ?  414 SER   A N     1 
ATOM   3156 C CA    . SER   A 1 414 ? -28.256 20.795 -18.149 1.00 69.13  ?  414 SER   A CA    1 
ATOM   3157 C C     . SER   A 1 414 ? -27.502 21.465 -17.011 1.00 62.46  ?  414 SER   A C     1 
ATOM   3158 O O     . SER   A 1 414 ? -27.763 21.133 -15.854 1.00 62.52  ?  414 SER   A O     1 
ATOM   3159 C CB    . SER   A 1 414 ? -28.061 19.281 -18.018 1.00 66.59  ?  414 SER   A CB    1 
ATOM   3160 O OG    . SER   A 1 414 ? -28.341 18.648 -19.247 1.00 76.00  ?  414 SER   A OG    1 
ATOM   3161 N N     . ILE   A 1 415 ? -26.550 22.350 -17.288 1.00 60.81  ?  415 ILE   A N     1 
ATOM   3162 C CA    . ILE   A 1 415 ? -25.804 23.001 -16.219 1.00 62.57  ?  415 ILE   A CA    1 
ATOM   3163 C C     . ILE   A 1 415 ? -25.830 24.507 -16.451 1.00 65.27  ?  415 ILE   A C     1 
ATOM   3164 O O     . ILE   A 1 415 ? -25.042 25.260 -15.867 1.00 66.37  ?  415 ILE   A O     1 
ATOM   3165 C CB    . ILE   A 1 415 ? -24.360 22.462 -16.119 1.00 54.52  ?  415 ILE   A CB    1 
ATOM   3166 C CG1   . ILE   A 1 415 ? -23.565 22.767 -17.394 1.00 55.80  ?  415 ILE   A CG1   1 
ATOM   3167 C CG2   . ILE   A 1 415 ? -24.367 20.964 -15.797 1.00 49.71  ?  415 ILE   A CG2   1 
ATOM   3168 C CD1   . ILE   A 1 415 ? -22.075 22.554 -17.256 1.00 51.88  ?  415 ILE   A CD1   1 
ATOM   3169 N N     . GLN   A 1 416 ? -26.746 24.967 -17.288 1.00 63.49  ?  416 GLN   A N     1 
ATOM   3170 C CA    . GLN   A 1 416 ? -26.795 26.379 -17.624 1.00 66.80  ?  416 GLN   A CA    1 
ATOM   3171 C C     . GLN   A 1 416 ? -27.656 27.123 -16.612 1.00 63.44  ?  416 GLN   A C     1 
ATOM   3172 O O     . GLN   A 1 416 ? -28.743 26.660 -16.250 1.00 62.15  ?  416 GLN   A O     1 
ATOM   3173 C CB    . GLN   A 1 416 ? -27.314 26.578 -19.050 1.00 77.57  ?  416 GLN   A CB    1 
ATOM   3174 C CG    . GLN   A 1 416 ? -26.396 25.953 -20.104 1.00 79.55  ?  416 GLN   A CG    1 
ATOM   3175 C CD    . GLN   A 1 416 ? -25.640 26.986 -20.902 1.00 78.52  ?  416 GLN   A CD    1 
ATOM   3176 O OE1   . GLN   A 1 416 ? -24.468 27.271 -20.633 1.00 70.99  ?  416 GLN   A OE1   1 
ATOM   3177 N NE2   . GLN   A 1 416 ? -26.306 27.556 -21.895 1.00 88.07  ?  416 GLN   A NE2   1 
ATOM   3178 N N     . VAL   A 1 417 ? -27.148 28.270 -16.152 1.00 67.07  ?  417 VAL   A N     1 
ATOM   3179 C CA    . VAL   A 1 417 ? -27.771 29.104 -15.130 1.00 70.24  ?  417 VAL   A CA    1 
ATOM   3180 C C     . VAL   A 1 417 ? -27.434 30.554 -15.449 1.00 69.04  ?  417 VAL   A C     1 
ATOM   3181 O O     . VAL   A 1 417 ? -26.367 30.853 -15.994 1.00 75.69  ?  417 VAL   A O     1 
ATOM   3182 C CB    . VAL   A 1 417 ? -27.272 28.766 -13.696 1.00 68.72  ?  417 VAL   A CB    1 
ATOM   3183 C CG1   . VAL   A 1 417 ? -27.689 27.371 -13.263 1.00 64.48  ?  417 VAL   A CG1   1 
ATOM   3184 C CG2   . VAL   A 1 417 ? -25.772 28.921 -13.613 1.00 69.34  ?  417 VAL   A CG2   1 
ATOM   3185 N N     . ASP   A 1 418 ? -28.327 31.467 -15.086 1.00 71.07  ?  418 ASP   A N     1 
ATOM   3186 C CA    . ASP   A 1 418 ? -28.005 32.890 -15.142 1.00 75.70  ?  418 ASP   A CA    1 
ATOM   3187 C C     . ASP   A 1 418 ? -27.565 33.380 -13.761 1.00 76.40  ?  418 ASP   A C     1 
ATOM   3188 O O     . ASP   A 1 418 ? -28.165 33.006 -12.746 1.00 70.14  ?  418 ASP   A O     1 
ATOM   3189 C CB    . ASP   A 1 418 ? -29.208 33.691 -15.649 1.00 81.15  ?  418 ASP   A CB    1 
ATOM   3190 C CG    . ASP   A 1 418 ? -29.781 33.128 -16.954 1.00 81.36  ?  418 ASP   A CG    1 
ATOM   3191 O OD1   . ASP   A 1 418 ? -29.036 33.049 -17.965 1.00 77.58  ?  418 ASP   A OD1   1 
ATOM   3192 O OD2   . ASP   A 1 418 ? -30.981 32.772 -16.962 1.00 77.40  ?  418 ASP   A OD2   1 
ATOM   3193 N N     . VAL   A 1 419 ? -26.429 34.065 -13.686 1.00 74.87  ?  419 VAL   A N     1 
ATOM   3194 C CA    . VAL   A 1 419 ? -25.862 34.444 -12.355 1.00 73.87  ?  419 VAL   A CA    1 
ATOM   3195 C C     . VAL   A 1 419 ? -26.952 35.001 -11.440 1.00 73.25  ?  419 VAL   A C     1 
ATOM   3196 O O     . VAL   A 1 419 ? -27.085 34.486 -10.331 1.00 67.59  ?  419 VAL   A O     1 
ATOM   3197 C CB    . VAL   A 1 419 ? -24.715 35.461 -12.492 1.00 72.82  ?  419 VAL   A CB    1 
ATOM   3198 C CG1   . VAL   A 1 419 ? -23.429 34.808 -12.962 1.00 72.30  ?  419 VAL   A CG1   1 
ATOM   3199 C CG2   . VAL   A 1 419 ? -25.070 36.626 -13.404 1.00 73.99  ?  419 VAL   A CG2   1 
ATOM   3200 N N     . GLY   A 1 420 ? -27.707 35.983 -11.910 1.00 71.84  ?  420 GLY   A N     1 
ATOM   3201 C CA    . GLY   A 1 420 ? -28.686 36.667 -11.054 1.00 73.42  ?  420 GLY   A CA    1 
ATOM   3202 C C     . GLY   A 1 420 ? -29.766 35.932 -10.314 1.00 71.28  ?  420 GLY   A C     1 
ATOM   3203 O O     . GLY   A 1 420 ? -29.835 36.068 -9.090  1.00 69.51  ?  420 GLY   A O     1 
ATOM   3204 N N     . PRO   A 1 421 ? -30.673 35.230 -11.004 1.00 71.42  ?  421 PRO   A N     1 
ATOM   3205 C CA    . PRO   A 1 421 ? -31.685 34.468 -10.296 1.00 70.54  ?  421 PRO   A CA    1 
ATOM   3206 C C     . PRO   A 1 421 ? -31.127 33.284 -9.525  1.00 73.15  ?  421 PRO   A C     1 
ATOM   3207 O O     . PRO   A 1 421 ? -31.756 32.833 -8.560  1.00 76.02  ?  421 PRO   A O     1 
ATOM   3208 C CB    . PRO   A 1 421 ? -32.617 34.064 -11.435 1.00 71.61  ?  421 PRO   A CB    1 
ATOM   3209 C CG    . PRO   A 1 421 ? -31.758 34.145 -12.675 1.00 75.80  ?  421 PRO   A CG    1 
ATOM   3210 C CD    . PRO   A 1 421 ? -30.880 35.348 -12.429 1.00 70.40  ?  421 PRO   A CD    1 
ATOM   3211 N N     . TYR   A 1 422 ? -29.951 32.809 -9.914  1.00 69.13  ?  422 TYR   A N     1 
ATOM   3212 C CA    . TYR   A 1 422 ? -29.331 31.710 -9.185  1.00 67.78  ?  422 TYR   A CA    1 
ATOM   3213 C C     . TYR   A 1 422 ? -28.764 32.182 -7.852  1.00 63.22  ?  422 TYR   A C     1 
ATOM   3214 O O     . TYR   A 1 422 ? -29.105 31.640 -6.800  1.00 59.39  ?  422 TYR   A O     1 
ATOM   3215 C CB    . TYR   A 1 422 ? -28.248 31.054 -10.034 1.00 66.50  ?  422 TYR   A CB    1 
ATOM   3216 C CG    . TYR   A 1 422 ? -27.768 29.756 -9.450  1.00 61.22  ?  422 TYR   A CG    1 
ATOM   3217 C CD1   . TYR   A 1 422 ? -28.568 28.620 -9.488  1.00 55.05  ?  422 TYR   A CD1   1 
ATOM   3218 C CD2   . TYR   A 1 422 ? -26.511 29.668 -8.846  1.00 61.28  ?  422 TYR   A CD2   1 
ATOM   3219 C CE1   . TYR   A 1 422 ? -28.133 27.433 -8.941  1.00 56.86  ?  422 TYR   A CE1   1 
ATOM   3220 C CE2   . TYR   A 1 422 ? -26.066 28.486 -8.305  1.00 54.65  ?  422 TYR   A CE2   1 
ATOM   3221 C CZ    . TYR   A 1 422 ? -26.879 27.374 -8.347  1.00 56.40  ?  422 TYR   A CZ    1 
ATOM   3222 O OH    . TYR   A 1 422 ? -26.428 26.200 -7.794  1.00 52.89  ?  422 TYR   A OH    1 
ATOM   3223 N N     . LEU   A 1 423 ? -27.882 33.190 -7.876  1.00 67.24  ?  423 LEU   A N     1 
ATOM   3224 C CA    . LEU   A 1 423 ? -27.401 33.778 -6.625  1.00 67.36  ?  423 LEU   A CA    1 
ATOM   3225 C C     . LEU   A 1 423 ? -28.554 34.310 -5.782  1.00 65.03  ?  423 LEU   A C     1 
ATOM   3226 O O     . LEU   A 1 423 ? -28.471 34.306 -4.549  1.00 65.77  ?  423 LEU   A O     1 
ATOM   3227 C CB    . LEU   A 1 423 ? -26.389 34.899 -6.899  1.00 60.16  ?  423 LEU   A CB    1 
ATOM   3228 C CG    . LEU   A 1 423 ? -25.109 34.529 -7.663  1.00 63.47  ?  423 LEU   A CG    1 
ATOM   3229 C CD1   . LEU   A 1 423 ? -24.236 35.752 -7.944  1.00 53.74  ?  423 LEU   A CD1   1 
ATOM   3230 C CD2   . LEU   A 1 423 ? -24.306 33.453 -6.930  1.00 58.79  ?  423 LEU   A CD2   1 
ATOM   3231 N N     . ALA   A 1 424 ? -29.648 34.726 -6.426  1.00 65.46  ?  424 ALA   A N     1 
ATOM   3232 C CA    . ALA   A 1 424 ? -30.758 35.364 -5.730  1.00 69.32  ?  424 ALA   A CA    1 
ATOM   3233 C C     . ALA   A 1 424 ? -31.444 34.443 -4.727  1.00 68.43  ?  424 ALA   A C     1 
ATOM   3234 O O     . ALA   A 1 424 ? -32.177 34.933 -3.858  1.00 58.79  ?  424 ALA   A O     1 
ATOM   3235 C CB    . ALA   A 1 424 ? -31.784 35.869 -6.744  1.00 71.37  ?  424 ALA   A CB    1 
ATOM   3236 N N     . GLU   A 1 425 ? -31.238 33.132 -4.822  1.00 64.80  ?  425 GLU   A N     1 
ATOM   3237 C CA    . GLU   A 1 425 ? -31.849 32.214 -3.875  1.00 61.24  ?  425 GLU   A CA    1 
ATOM   3238 C C     . GLU   A 1 425 ? -30.876 31.716 -2.816  1.00 64.79  ?  425 GLU   A C     1 
ATOM   3239 O O     . GLU   A 1 425 ? -31.257 30.904 -1.971  1.00 64.29  ?  425 GLU   A O     1 
ATOM   3240 C CB    . GLU   A 1 425 ? -32.482 31.048 -4.621  1.00 61.09  ?  425 GLU   A CB    1 
ATOM   3241 C CG    . GLU   A 1 425 ? -33.669 31.502 -5.444  1.00 62.39  ?  425 GLU   A CG    1 
ATOM   3242 C CD    . GLU   A 1 425 ? -34.301 30.365 -6.219  1.00 66.83  ?  425 GLU   A CD    1 
ATOM   3243 O OE1   . GLU   A 1 425 ? -33.942 29.179 -5.971  1.00 64.88  ?  425 GLU   A OE1   1 
ATOM   3244 O OE2   . GLU   A 1 425 ? -35.146 30.669 -7.087  1.00 57.49  ?  425 GLU   A OE2   1 
ATOM   3245 N N     . PHE   A 1 426 ? -29.642 32.199 -2.822  1.00 66.05  ?  426 PHE   A N     1 
ATOM   3246 C CA    . PHE   A 1 426 ? -28.742 31.939 -1.709  1.00 65.02  ?  426 PHE   A CA    1 
ATOM   3247 C C     . PHE   A 1 426 ? -28.646 33.209 -0.861  1.00 56.54  ?  426 PHE   A C     1 
ATOM   3248 O O     . PHE   A 1 426 ? -27.658 33.941 -0.913  1.00 66.19  ?  426 PHE   A O     1 
ATOM   3249 C CB    . PHE   A 1 426 ? -27.357 31.469 -2.210  1.00 65.30  ?  426 PHE   A CB    1 
ATOM   3250 C CG    . PHE   A 1 426 ? -27.407 30.241 -3.118  1.00 57.71  ?  426 PHE   A CG    1 
ATOM   3251 C CD1   . PHE   A 1 426 ? -27.719 30.365 -4.472  1.00 59.35  ?  426 PHE   A CD1   1 
ATOM   3252 C CD2   . PHE   A 1 426 ? -27.123 28.969 -2.619  1.00 51.39  ?  426 PHE   A CD2   1 
ATOM   3253 C CE1   . PHE   A 1 426 ? -27.769 29.249 -5.315  1.00 54.69  ?  426 PHE   A CE1   1 
ATOM   3254 C CE2   . PHE   A 1 426 ? -27.169 27.847 -3.452  1.00 55.50  ?  426 PHE   A CE2   1 
ATOM   3255 C CZ    . PHE   A 1 426 ? -27.493 27.994 -4.814  1.00 53.38  ?  426 PHE   A CZ    1 
HETATM 3256 C CZ3   . A1D7R B 2 .   ? -21.509 35.211 -21.224 1.00 80.80  ?  501 A1D7R A CZ3   1 
HETATM 3257 C CH2   . A1D7R B 2 .   ? -21.295 36.512 -20.799 1.00 81.81  ?  501 A1D7R A CH2   1 
HETATM 3258 C CZ2   . A1D7R B 2 .   ? -20.099 36.873 -20.209 1.00 75.07  ?  501 A1D7R A CZ2   1 
HETATM 3259 C CE2   . A1D7R B 2 .   ? -19.102 35.910 -20.035 1.00 76.64  ?  501 A1D7R A CE2   1 
HETATM 3260 C CD2   . A1D7R B 2 .   ? -19.314 34.620 -20.448 1.00 77.87  ?  501 A1D7R A CD2   1 
HETATM 3261 C CE3   . A1D7R B 2 .   ? -20.520 34.257 -21.048 1.00 79.97  ?  501 A1D7R A CE3   1 
HETATM 3262 C CD1   . A1D7R B 2 .   ? -17.287 34.816 -19.550 1.00 74.51  ?  501 A1D7R A CD1   1 
HETATM 3263 C CG    . A1D7R B 2 .   ? -18.150 33.914 -20.142 1.00 76.46  ?  501 A1D7R A CG    1 
HETATM 3264 C CB    . A1D7R B 2 .   ? -17.888 32.443 -20.394 1.00 77.44  ?  501 A1D7R A CB    1 
HETATM 3265 C CA    . A1D7R B 2 .   ? -17.259 31.822 -19.158 1.00 77.78  ?  501 A1D7R A CA    1 
HETATM 3266 C C     . A1D7R B 2 .   ? -18.021 30.559 -18.788 1.00 87.23  ?  501 A1D7R A C     1 
HETATM 3267 C C12   . A1D7R B 2 .   ? -22.383 37.550 -20.996 1.00 80.63  ?  501 A1D7R A C12   1 
HETATM 3268 C C13   . A1D7R B 2 .   ? -22.728 37.585 -22.477 1.00 77.29  ?  501 A1D7R A C13   1 
HETATM 3269 C C14   . A1D7R B 2 .   ? -23.148 38.714 -22.984 1.00 76.16  ?  501 A1D7R A C14   1 
HETATM 3270 C C15   . A1D7R B 2 .   ? -23.511 38.807 -24.460 1.00 72.87  ?  501 A1D7R A C15   1 
HETATM 3271 C C16   . A1D7R B 2 .   ? -23.273 39.930 -22.075 1.00 67.09  ?  501 A1D7R A C16   1 
HETATM 3272 N NE1   . A1D7R B 2 .   ? -17.880 35.985 -19.504 1.00 75.40  ?  501 A1D7R A NE1   1 
HETATM 3273 N N     . A1D7R B 2 .   ? -15.885 31.482 -19.452 1.00 70.05  ?  501 A1D7R A N     1 
HETATM 3274 O O     . A1D7R B 2 .   ? -18.134 30.237 -17.583 1.00 89.42  ?  501 A1D7R A O     1 
HETATM 3275 O OXT   . A1D7R B 2 .   ? -18.530 29.835 -19.678 1.00 87.07  -1 501 A1D7R A OXT   1 
HETATM 3276 P PA    . FAD   C 3 .   ? -10.902 22.592 -12.330 1.00 46.82  ?  502 FAD   A PA    1 
HETATM 3277 O O1A   . FAD   C 3 .   ? -10.163 23.846 -12.583 1.00 47.91  ?  502 FAD   A O1A   1 
HETATM 3278 O O2A   . FAD   C 3 .   ? -11.041 21.623 -13.437 1.00 51.65  ?  502 FAD   A O2A   1 
HETATM 3279 O O5B   . FAD   C 3 .   ? -10.266 21.878 -11.059 1.00 41.49  ?  502 FAD   A O5B   1 
HETATM 3280 C C5B   . FAD   C 3 .   ? -10.747 20.574 -10.741 1.00 39.08  ?  502 FAD   A C5B   1 
HETATM 3281 C C4B   . FAD   C 3 .   ? -9.609  19.797 -10.135 1.00 45.28  ?  502 FAD   A C4B   1 
HETATM 3282 O O4B   . FAD   C 3 .   ? -10.032 18.458 -9.792  1.00 44.31  ?  502 FAD   A O4B   1 
HETATM 3283 C C3B   . FAD   C 3 .   ? -8.391  19.644 -11.052 1.00 47.92  ?  502 FAD   A C3B   1 
HETATM 3284 O O3B   . FAD   C 3 .   ? -7.321  20.389 -10.495 1.00 42.04  ?  502 FAD   A O3B   1 
HETATM 3285 C C2B   . FAD   C 3 .   ? -8.121  18.141 -11.007 1.00 43.54  ?  502 FAD   A C2B   1 
HETATM 3286 O O2B   . FAD   C 3 .   ? -6.747  17.829 -10.995 1.00 49.41  ?  502 FAD   A O2B   1 
HETATM 3287 C C1B   . FAD   C 3 .   ? -8.762  17.844 -9.661  1.00 45.70  ?  502 FAD   A C1B   1 
HETATM 3288 N N9A   . FAD   C 3 .   ? -8.887  16.435 -9.296  1.00 54.59  ?  502 FAD   A N9A   1 
HETATM 3289 C C8A   . FAD   C 3 .   ? -8.337  15.869 -8.178  1.00 52.51  ?  502 FAD   A C8A   1 
HETATM 3290 N N7A   . FAD   C 3 .   ? -8.561  14.586 -8.066  1.00 51.81  ?  502 FAD   A N7A   1 
HETATM 3291 C C5A   . FAD   C 3 .   ? -9.304  14.289 -9.196  1.00 49.94  ?  502 FAD   A C5A   1 
HETATM 3292 C C6A   . FAD   C 3 .   ? -9.849  13.086 -9.662  1.00 51.66  ?  502 FAD   A C6A   1 
HETATM 3293 N N6A   . FAD   C 3 .   ? -9.722  11.928 -9.030  1.00 50.98  ?  502 FAD   A N6A   1 
HETATM 3294 N N1A   . FAD   C 3 .   ? -10.530 13.121 -10.828 1.00 64.06  ?  502 FAD   A N1A   1 
HETATM 3295 C C2A   . FAD   C 3 .   ? -10.653 14.291 -11.462 1.00 59.23  ?  502 FAD   A C2A   1 
HETATM 3296 N N3A   . FAD   C 3 .   ? -10.183 15.482 -11.120 1.00 51.49  ?  502 FAD   A N3A   1 
HETATM 3297 C C4A   . FAD   C 3 .   ? -9.510  15.416 -9.964  1.00 47.83  ?  502 FAD   A C4A   1 
HETATM 3298 N N1    . FAD   C 3 .   ? -14.398 30.796 -15.930 1.00 58.85  ?  502 FAD   A N1    1 
HETATM 3299 C C2    . FAD   C 3 .   ? -14.435 32.127 -15.637 1.00 56.53  ?  502 FAD   A C2    1 
HETATM 3300 O O2    . FAD   C 3 .   ? -15.153 32.576 -14.743 1.00 60.97  ?  502 FAD   A O2    1 
HETATM 3301 N N3    . FAD   C 3 .   ? -13.639 33.001 -16.365 1.00 59.86  ?  502 FAD   A N3    1 
HETATM 3302 C C4    . FAD   C 3 .   ? -12.791 32.663 -17.390 1.00 62.22  ?  502 FAD   A C4    1 
HETATM 3303 O O4    . FAD   C 3 .   ? -12.113 33.490 -17.963 1.00 60.20  ?  502 FAD   A O4    1 
HETATM 3304 C C4X   . FAD   C 3 .   ? -12.763 31.296 -17.673 1.00 62.22  ?  502 FAD   A C4X   1 
HETATM 3305 N N5    . FAD   C 3 .   ? -11.972 30.909 -18.636 1.00 57.79  ?  502 FAD   A N5    1 
HETATM 3306 C C5X   . FAD   C 3 .   ? -11.923 29.574 -18.920 1.00 55.09  ?  502 FAD   A C5X   1 
HETATM 3307 C C6    . FAD   C 3 .   ? -11.067 29.145 -19.948 1.00 53.31  ?  502 FAD   A C6    1 
HETATM 3308 C C7    . FAD   C 3 .   ? -10.959 27.816 -20.278 1.00 58.44  ?  502 FAD   A C7    1 
HETATM 3309 C C7M   . FAD   C 3 .   ? -10.027 27.384 -21.379 1.00 53.41  ?  502 FAD   A C7M   1 
HETATM 3310 C C8    . FAD   C 3 .   ? -11.733 26.864 -19.581 1.00 56.41  ?  502 FAD   A C8    1 
HETATM 3311 C C8M   . FAD   C 3 .   ? -11.642 25.406 -19.927 1.00 58.74  ?  502 FAD   A C8M   1 
HETATM 3312 C C9    . FAD   C 3 .   ? -12.584 27.274 -18.581 1.00 55.32  ?  502 FAD   A C9    1 
HETATM 3313 C C9A   . FAD   C 3 .   ? -12.692 28.623 -18.224 1.00 55.93  ?  502 FAD   A C9A   1 
HETATM 3314 N N10   . FAD   C 3 .   ? -13.533 29.070 -17.215 1.00 58.25  ?  502 FAD   A N10   1 
HETATM 3315 C C10   . FAD   C 3 .   ? -13.598 30.413 -16.900 1.00 62.18  ?  502 FAD   A C10   1 
HETATM 3316 C "C1'" . FAD   C 3 .   ? -14.339 28.115 -16.435 1.00 55.71  ?  502 FAD   A "C1'" 1 
HETATM 3317 C "C2'" . FAD   C 3 .   ? -13.477 27.356 -15.436 1.00 52.82  ?  502 FAD   A "C2'" 1 
HETATM 3318 O "O2'" . FAD   C 3 .   ? -13.937 26.009 -15.369 1.00 50.82  ?  502 FAD   A "O2'" 1 
HETATM 3319 C "C3'" . FAD   C 3 .   ? -13.480 27.980 -14.041 1.00 52.22  ?  502 FAD   A "C3'" 1 
HETATM 3320 O "O3'" . FAD   C 3 .   ? -12.906 29.279 -14.115 1.00 50.40  ?  502 FAD   A "O3'" 1 
HETATM 3321 C "C4'" . FAD   C 3 .   ? -12.676 27.237 -12.982 1.00 49.52  ?  502 FAD   A "C4'" 1 
HETATM 3322 O "O4'" . FAD   C 3 .   ? -11.572 26.592 -13.610 1.00 53.95  ?  502 FAD   A "O4'" 1 
HETATM 3323 C "C5'" . FAD   C 3 .   ? -13.469 26.194 -12.225 1.00 42.80  ?  502 FAD   A "C5'" 1 
HETATM 3324 O "O5'" . FAD   C 3 .   ? -12.501 25.354 -11.595 1.00 48.85  ?  502 FAD   A "O5'" 1 
HETATM 3325 P P     . FAD   C 3 .   ? -12.993 24.039 -10.883 1.00 42.82  ?  502 FAD   A P     1 
HETATM 3326 O O1P   . FAD   C 3 .   ? -12.380 23.991 -9.539  1.00 47.22  ?  502 FAD   A O1P   1 
HETATM 3327 O O2P   . FAD   C 3 .   ? -14.461 23.998 -11.040 1.00 47.46  ?  502 FAD   A O2P   1 
HETATM 3328 O O3P   . FAD   C 3 .   ? -12.352 22.923 -11.797 1.00 51.25  ?  502 FAD   A O3P   1 
HETATM 3329 O O     . HOH   D 4 .   ? -23.155 42.847 -40.776 1.00 62.92  ?  601 HOH   A O     1 
HETATM 3330 O O     . HOH   D 4 .   ? -0.680  9.668  -7.735  1.00 68.56  ?  602 HOH   A O     1 
HETATM 3331 O O     . HOH   D 4 .   ? -14.581 16.537 -18.143 1.00 54.25  ?  603 HOH   A O     1 
HETATM 3332 O O     . HOH   D 4 .   ? -11.645 22.432 -27.432 1.00 48.31  ?  604 HOH   A O     1 
HETATM 3333 O O     . HOH   D 4 .   ? 1.747   33.118 -2.552  1.00 39.39  ?  605 HOH   A O     1 
HETATM 3334 O O     . HOH   D 4 .   ? -2.992  26.688 3.614   1.00 49.99  ?  606 HOH   A O     1 
HETATM 3335 O O     . HOH   D 4 .   ? -15.807 22.170 -10.257 1.00 45.95  ?  607 HOH   A O     1 
HETATM 3336 O O     . HOH   D 4 .   ? -0.043  33.767 0.029   1.00 43.59  ?  608 HOH   A O     1 
HETATM 3337 O O     . HOH   D 4 .   ? -8.767  7.477  0.496   1.00 44.50  ?  609 HOH   A O     1 
HETATM 3338 O O     . HOH   D 4 .   ? -28.178 30.057 -19.198 1.00 71.44  ?  610 HOH   A O     1 
HETATM 3339 O O     . HOH   D 4 .   ? -1.793  27.466 -8.619  1.00 43.75  ?  611 HOH   A O     1 
HETATM 3340 O O     . HOH   D 4 .   ? -27.883 25.026 -36.278 1.00 83.52  ?  612 HOH   A O     1 
HETATM 3341 O O     . HOH   D 4 .   ? -1.363  32.227 -39.909 1.00 47.34  ?  613 HOH   A O     1 
HETATM 3342 O O     . HOH   D 4 .   ? -15.960 25.898 -22.085 1.00 69.16  ?  614 HOH   A O     1 
HETATM 3343 O O     . HOH   D 4 .   ? -21.094 20.938 -49.795 1.00 56.69  ?  615 HOH   A O     1 
HETATM 3344 O O     . HOH   D 4 .   ? -5.259  21.967 -9.127  1.00 52.27  ?  616 HOH   A O     1 
HETATM 3345 O O     . HOH   D 4 .   ? -10.452 29.213 5.129   1.00 38.26  ?  617 HOH   A O     1 
HETATM 3346 O O     . HOH   D 4 .   ? -13.143 24.456 -24.920 1.00 56.12  ?  618 HOH   A O     1 
HETATM 3347 O O     . HOH   D 4 .   ? -20.568 45.666 -42.290 1.00 61.42  ?  619 HOH   A O     1 
HETATM 3348 O O     . HOH   D 4 .   ? -3.959  32.995 -42.782 1.00 47.22  ?  620 HOH   A O     1 
HETATM 3349 O O     . HOH   D 4 .   ? -24.941 30.308 -0.030  1.00 45.30  ?  621 HOH   A O     1 
HETATM 3350 O O     . HOH   D 4 .   ? -25.241 30.073 10.936  1.00 41.81  ?  622 HOH   A O     1 
HETATM 3351 O O     . HOH   D 4 .   ? -14.223 3.263  -3.094  1.00 42.37  ?  623 HOH   A O     1 
HETATM 3352 O O     . HOH   D 4 .   ? -26.293 35.897 0.652   1.00 55.59  ?  624 HOH   A O     1 
HETATM 3353 O O     . HOH   D 4 .   ? -35.248 10.382 -18.088 1.00 74.01  ?  625 HOH   A O     1 
HETATM 3354 O O     . HOH   D 4 .   ? 5.915   28.377 -14.566 1.00 57.04  ?  626 HOH   A O     1 
HETATM 3355 O O     . HOH   D 4 .   ? 2.278   32.169 -28.224 1.00 51.39  ?  627 HOH   A O     1 
HETATM 3356 O O     . HOH   D 4 .   ? -9.475  26.237 -11.104 1.00 47.07  ?  628 HOH   A O     1 
HETATM 3357 O O     . HOH   D 4 .   ? -24.869 34.288 -0.123  1.00 63.19  ?  629 HOH   A O     1 
HETATM 3358 O O     . HOH   D 4 .   ? -15.870 30.092 -0.322  1.00 32.98  ?  630 HOH   A O     1 
HETATM 3359 O O     . HOH   D 4 .   ? -19.046 35.674 -10.565 1.00 41.87  ?  631 HOH   A O     1 
HETATM 3360 O O     . HOH   D 4 .   ? -5.121  19.775 -12.569 1.00 58.14  ?  632 HOH   A O     1 
HETATM 3361 O O     . HOH   D 4 .   ? -15.038 22.920 -14.644 1.00 53.02  ?  633 HOH   A O     1 
HETATM 3362 O O     . HOH   D 4 .   ? -33.534 26.712 -8.537  1.00 46.30  ?  634 HOH   A O     1 
HETATM 3363 O O     . HOH   D 4 .   ? -4.263  14.633 5.193   1.00 50.36  ?  635 HOH   A O     1 
HETATM 3364 O O     . HOH   D 4 .   ? -5.301  48.904 -11.572 1.00 55.03  ?  636 HOH   A O     1 
HETATM 3365 O O     . HOH   D 4 .   ? -25.509 35.236 -2.718  1.00 52.63  ?  637 HOH   A O     1 
HETATM 3366 O O     . HOH   D 4 .   ? -14.760 25.918 -25.847 1.00 44.07  ?  638 HOH   A O     1 
# 
