data_8Z16
# 
_entry.id   8Z16 
# 
_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   8Z16         pdb_00008z16 10.2210/pdb8z16/pdb 
WWPDB D_1300046783 ?            ?                   
# 
_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                        8Z16 
_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'                                             46815.859 1  ? N57A ? 
;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 'FLAVIN-ADENINE DINUCLEOTIDE'                                                785.550   1  ? ?    ? ? 
3 non-polymer syn 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'                           743.405   1  ? ?    ? ? 
4 non-polymer syn '(2~{S})-2-azanyl-3-[6-(3-methylbut-2-enyl)-1~{H}-indol-3-yl]propanoic acid' 272.342   1  ? ?    ? ? 
5 water       nat water                                                                        18.015    43 ? ?    ? ? 
# 
_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       
;MRVCVIGAGLSGLAVGHALKERGISFVCLEKAPDVGGIWRQPGAGERGPGYRTLHLATAKQLTGYADFPMPDAYPLYPRH
SQVAAYLRSFAEWAGLLDHVELRTEVVSVRQDADGPWTVVSRGADGAQVSRRFEQVVVASGHHNEPALPDPLPAGADSFA
GTILHSLDYRDGGDFAGRRVVVVGLGASAVDIAADLSRHAERTLLSVRRGLHIVPKQLFGMSVDEIAEAPWWNEMSFDER
RRWVEQALLVARGRLSDYGLPEPDHPVFSSATTLSDEILSRIRHGAVTPKPAIASFDGDRVVFTDGTSEPADAVVYCTGF
HMTFPFLPAGCPMSADGSVELYRRVVPADRPGLYFVGLVRPVGAITRLVEAQAEWVARLVDGAAVLPAADQMREEIGTYL
TGIVQRYGRTEGASIQVDVGPYLAEFRESLPV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MRVCVIGAGLSGLAVGHALKERGISFVCLEKAPDVGGIWRQPGAGERGPGYRTLHLATAKQLTGYADFPMPDAYPLYPRH
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 'FLAVIN-ADENINE DINUCLEOTIDE'                                                FAD   
3 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'                           NAP   
4 '(2~{S})-2-azanyl-3-[6-(3-methylbut-2-enyl)-1~{H}-indol-3-yl]propanoic acid' A1D7R 
5 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  ALA 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 
NAP   non-polymer         . 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'                           
;2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
;
'C21 H28 N7 O17 P3' 743.405 
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  ALA 57  57  57  ALA ALA 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_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 FAD   1  501 501 FAD   FAD A . 
C 3 NAP   1  502 502 NAP   NAP A . 
D 4 A1D7R 1  503 503 A1D7R DMA A . 
E 5 HOH   1  601 30  HOH   HOH A . 
E 5 HOH   2  602 38  HOH   HOH A . 
E 5 HOH   3  603 36  HOH   HOH A . 
E 5 HOH   4  604 21  HOH   HOH A . 
E 5 HOH   5  605 33  HOH   HOH A . 
E 5 HOH   6  606 11  HOH   HOH A . 
E 5 HOH   7  607 12  HOH   HOH A . 
E 5 HOH   8  608 1   HOH   HOH A . 
E 5 HOH   9  609 15  HOH   HOH A . 
E 5 HOH   10 610 26  HOH   HOH A . 
E 5 HOH   11 611 13  HOH   HOH A . 
E 5 HOH   12 612 25  HOH   HOH A . 
E 5 HOH   13 613 27  HOH   HOH A . 
E 5 HOH   14 614 9   HOH   HOH A . 
E 5 HOH   15 615 16  HOH   HOH A . 
E 5 HOH   16 616 14  HOH   HOH A . 
E 5 HOH   17 617 29  HOH   HOH A . 
E 5 HOH   18 618 18  HOH   HOH A . 
E 5 HOH   19 619 19  HOH   HOH A . 
E 5 HOH   20 620 24  HOH   HOH A . 
E 5 HOH   21 621 4   HOH   HOH A . 
E 5 HOH   22 622 23  HOH   HOH A . 
E 5 HOH   23 623 2   HOH   HOH A . 
E 5 HOH   24 624 40  HOH   HOH A . 
E 5 HOH   25 625 46  HOH   HOH A . 
E 5 HOH   26 626 8   HOH   HOH A . 
E 5 HOH   27 627 31  HOH   HOH A . 
E 5 HOH   28 628 35  HOH   HOH A . 
E 5 HOH   29 629 10  HOH   HOH A . 
E 5 HOH   30 630 7   HOH   HOH A . 
E 5 HOH   31 631 3   HOH   HOH A . 
E 5 HOH   32 632 6   HOH   HOH A . 
E 5 HOH   33 633 17  HOH   HOH A . 
E 5 HOH   34 634 34  HOH   HOH A . 
E 5 HOH   35 635 45  HOH   HOH A . 
E 5 HOH   36 636 39  HOH   HOH A . 
E 5 HOH   37 637 37  HOH   HOH A . 
E 5 HOH   38 638 20  HOH   HOH A . 
E 5 HOH   39 639 41  HOH   HOH A . 
E 5 HOH   40 640 28  HOH   HOH A . 
E 5 HOH   41 641 44  HOH   HOH A . 
E 5 HOH   42 642 42  HOH   HOH A . 
E 5 HOH   43 643 5   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'  ? ? ? ? ? ? ? ? ? ? ? autoPX  ? ? ? .                  2 
? 'data processing' ? ? ? ? ? ? ? ? ? ? ? autoPX  ? ? ? .                  3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                  4 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                  5 
# 
_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                     8Z16 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     67.928 
_cell.length_a_esd                 ? 
_cell.length_b                     67.928 
_cell.length_b_esd                 ? 
_cell.length_c                     381.657 
_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                         8Z16 
_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                   8Z16 
_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             2.57 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          52.21 
_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    '0.2 M Sodium citrate tribasic dihydrate and 18% w/v Polyethylene glycol 3,350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-07-01 
_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   0.97946 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97946 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8Z16 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.419 
_reflns.d_resolution_low                               46.595 
_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                                     21263 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                34.39 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.00 
_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                                0.5610 
_reflns.pdbx_Rpim_I_all                                0.0941 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.9975 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.5528 
_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                                    2.419 
_reflns_shell.d_res_low                                     2.506 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.09 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1500 
_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                               32.79 
_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                               3.3605 
_reflns_shell.pdbx_Rpim_I_all                               0.5768 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.3618 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  3.3094 
_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                                 8Z16 
_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                            2.419 
_refine.ls_d_res_low                             46.595 
_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                     21084 
_refine.ls_number_reflns_R_free                  1029 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.38 
_refine.ls_percent_reflns_R_free                 4.88 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2640 
_refine.ls_R_factor_R_free                       0.3453 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2600 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_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                 41.27 
_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                            0.62 
_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                       2.419 
_refine_hist.d_res_low                        46.595 
_refine_hist.number_atoms_solvent             43 
_refine_hist.number_atoms_total               3416 
_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        3252 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         121 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? 3464 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.055  ? 4741 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.659 ? 1980 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.054  ? 513  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 612  ? 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' 2.419  2.5464 . . 162 2678 97.00  . . . . 0.4297 . . . . . . . . . . . 0.4729 
'X-RAY DIFFRACTION' 2.5464 2.7060 . . 153 2794 100.00 . . . . 0.3927 . . . . . . . . . . . 0.4293 
'X-RAY DIFFRACTION' 2.7060 2.9149 . . 133 2807 100.00 . . . . 0.3544 . . . . . . . . . . . 0.4893 
'X-RAY DIFFRACTION' 2.9149 3.2081 . . 136 2840 100.00 . . . . 0.3241 . . . . . . . . . . . 0.3887 
'X-RAY DIFFRACTION' 3.2081 3.6722 . . 138 2868 100.00 . . . . 0.2708 . . . . . . . . . . . 0.3455 
'X-RAY DIFFRACTION' 3.6722 4.6259 . . 150 2909 100.00 . . . . 0.2195 . . . . . . . . . . . 0.3288 
'X-RAY DIFFRACTION' 4.6259 46.595 . . 157 3159 99.00  . . . . 0.2032 . . . . . . . . . . . 0.2863 
# 
_struct.entry_id                     8Z16 
_struct.title                        'Crystal structure of DiatB mutant N57A' 
_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        8Z16 
_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 ? 
E N N 5 ? 
# 
_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              8Z16 
_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 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8Z16 ALA A 57  ? UNP A0A7T1BYC5 ASN 57  'engineered mutation' 57  1 
1 8Z16 MET A 333 ? UNP A0A7T1BYC5 VAL 333 conflict              333 2 
# 
_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)' 1490  ? 
1 MORE         -10   ? 
1 'SSA (A^2)'  19520 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_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   ? GLY A 23  ? GLY A 9   GLY A 23  1 ? 15 
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  ? THR A 63  ? ALA A 59  THR A 63  5 ? 5  
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 SER A 222 ? ALA A 229 ? SER A 222 ALA A 229 1 ? 8  
HELX_P HELX_P11 AB2 ALA A 229 ? MET A 235 ? ALA A 229 MET A 235 1 ? 7  
HELX_P HELX_P12 AB3 ASP A 238 ? ARG A 252 ? ASP A 238 ARG A 252 1 ? 15 
HELX_P HELX_P13 AB4 ARG A 254 ? GLY A 259 ? ARG A 254 GLY A 259 5 ? 6  
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 ? GLY A 408 ? ALA A 388 GLY A 408 1 ? 21 
HELX_P HELX_P18 AB9 GLU A 411 ? SER A 414 ? GLU A 411 SER A 414 5 ? 4  
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       1.29 
# 
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 ? 3 ? 
AA7 ? 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 
AA6 2 3 ? anti-parallel 
AA7 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 ILE A 213 ? VAL A 214 ? ILE A 213 VAL A 214 
AA5 2 THR A 273 ? LEU A 274 ? THR A 273 LEU A 274 
AA6 1 ILE A 293 ? ASP A 297 ? ILE A 293 ASP A 297 
AA6 2 ARG A 300 ? PHE A 303 ? ARG A 300 PHE A 303 
AA6 3 SER A 308 ? PRO A 310 ? SER A 308 PRO A 310 
AA7 1 ARG A 360 ? PRO A 361 ? ARG A 360 PRO A 361 
AA7 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 VAL A 27  ? O VAL A 27  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 TRP A 117 ? N TRP A 117 O PHE A 133 ? O PHE A 133 
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 VAL A 315 ? O VAL A 315 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 LYS A 290 ? O LYS A 290 
AA5 1 2 N VAL A 214 ? N VAL A 214 O THR A 273 ? O THR A 273 
AA6 1 2 N ALA A 294 ? N ALA A 294 O VAL A 302 ? O VAL A 302 
AA6 2 3 N VAL A 301 ? N VAL A 301 O GLU A 309 ? O GLU A 309 
AA7 1 2 N ARG A 360 ? N ARG A 360 O VAL A 417 ? O VAL A 417 
# 
_pdbx_entry_details.entry_id                   8Z16 
_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     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 N A PRO 291 ? ? CA A PRO 291 ? ? CB A PRO 291 ? ? 91.14 103.30 -12.16 1.20 N 
2 1 N A PRO 332 ? ? CA A PRO 332 ? ? CB A PRO 332 ? ? 89.98 103.30 -13.32 1.20 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 ARG A 52  ? ? -69.36  4.00    
2  1 ALA A 139 ? ? -142.11 52.28   
3  1 HIS A 143 ? ? -110.84 67.68   
4  1 SER A 158 ? ? -91.64  45.95   
5  1 ARG A 170 ? ? -126.51 -65.16  
6  1 HIS A 199 ? ? -131.48 -40.92  
7  1 ARG A 202 ? ? -173.11 135.58  
8  1 GLN A 217 ? ? -173.96 120.58  
9  1 ASP A 264 ? ? -98.42  34.11   
10 1 PHE A 268 ? ? 79.19   -19.47  
11 1 ALA A 271 ? ? -170.30 101.20  
12 1 GLU A 277 ? ? -131.97 -30.60  
13 1 ALA A 292 ? ? 135.35  135.89  
14 1 CYS A 317 ? ? -101.73 58.08   
15 1 PRO A 332 ? ? -4.98   41.93   
16 1 SER A 334 ? ? -106.82 -161.47 
17 1 ALA A 335 ? ? -67.45  -70.66  
18 1 VAL A 345 ? ? -134.43 -42.79  
19 1 ARG A 367 ? ? -49.63  -19.72  
20 1 ARG A 406 ? ? -136.42 -40.93  
21 1 THR A 410 ? ? -156.54 -156.77 
22 1 GLU A 425 ? ? -109.31 42.07   
# 
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 88  ? ? 0.135 'SIDE CHAIN' 
2  1 ARG A 103 ? ? 0.163 'SIDE CHAIN' 
3  1 ARG A 170 ? ? 0.203 'SIDE CHAIN' 
4  1 ARG A 198 ? ? 0.106 'SIDE CHAIN' 
5  1 ARG A 209 ? ? 0.150 'SIDE CHAIN' 
6  1 ARG A 240 ? ? 0.152 'SIDE CHAIN' 
7  1 ARG A 242 ? ? 0.101 'SIDE CHAIN' 
8  1 ARG A 252 ? ? 0.198 'SIDE CHAIN' 
9  1 ARG A 254 ? ? 0.130 'SIDE CHAIN' 
10 1 ARG A 378 ? ? 0.100 'SIDE CHAIN' 
11 1 ARG A 393 ? ? 0.214 'SIDE CHAIN' 
12 1 ARG A 406 ? ? 0.139 'SIDE CHAIN' 
13 1 ARG A 409 ? ? 0.290 '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 
NAP   PA     P N R 376 
NAP   O1A    O N N 377 
NAP   O2A    O N N 378 
NAP   O5B    O N N 379 
NAP   C5B    C N N 380 
NAP   C4B    C N R 381 
NAP   O4B    O N N 382 
NAP   C3B    C N R 383 
NAP   O3B    O N N 384 
NAP   C2B    C N R 385 
NAP   O2B    O N N 386 
NAP   C1B    C N R 387 
NAP   N9A    N Y N 388 
NAP   C8A    C Y N 389 
NAP   N7A    N Y N 390 
NAP   C5A    C Y N 391 
NAP   C6A    C Y N 392 
NAP   N6A    N N N 393 
NAP   N1A    N Y N 394 
NAP   C2A    C Y N 395 
NAP   N3A    N Y N 396 
NAP   C4A    C Y N 397 
NAP   O3     O N N 398 
NAP   PN     P N N 399 
NAP   O1N    O N N 400 
NAP   O2N    O N N 401 
NAP   O5D    O N N 402 
NAP   C5D    C N N 403 
NAP   C4D    C N R 404 
NAP   O4D    O N N 405 
NAP   C3D    C N S 406 
NAP   O3D    O N N 407 
NAP   C2D    C N R 408 
NAP   O2D    O N N 409 
NAP   C1D    C N R 410 
NAP   N1N    N Y N 411 
NAP   C2N    C Y N 412 
NAP   C3N    C Y N 413 
NAP   C7N    C N N 414 
NAP   O7N    O N N 415 
NAP   N7N    N N N 416 
NAP   C4N    C Y N 417 
NAP   C5N    C Y N 418 
NAP   C6N    C Y N 419 
NAP   P2B    P N N 420 
NAP   O1X    O N N 421 
NAP   O2X    O N N 422 
NAP   O3X    O N N 423 
NAP   HOA2   H N N 424 
NAP   H51A   H N N 425 
NAP   H52A   H N N 426 
NAP   H4B    H N N 427 
NAP   H3B    H N N 428 
NAP   HO3A   H N N 429 
NAP   H2B    H N N 430 
NAP   H1B    H N N 431 
NAP   H8A    H N N 432 
NAP   H61A   H N N 433 
NAP   H62A   H N N 434 
NAP   H2A    H N N 435 
NAP   H51N   H N N 436 
NAP   H52N   H N N 437 
NAP   H4D    H N N 438 
NAP   H3D    H N N 439 
NAP   HO3N   H N N 440 
NAP   H2D    H N N 441 
NAP   HO2N   H N N 442 
NAP   H1D    H N N 443 
NAP   H2N    H N N 444 
NAP   H71N   H N N 445 
NAP   H72N   H N N 446 
NAP   H4N    H N N 447 
NAP   H5N    H N N 448 
NAP   H6N    H N N 449 
NAP   HOP2   H N N 450 
NAP   HOP3   H N N 451 
PHE   N      N N N 452 
PHE   CA     C N S 453 
PHE   C      C N N 454 
PHE   O      O N N 455 
PHE   CB     C N N 456 
PHE   CG     C Y N 457 
PHE   CD1    C Y N 458 
PHE   CD2    C Y N 459 
PHE   CE1    C Y N 460 
PHE   CE2    C Y N 461 
PHE   CZ     C Y N 462 
PHE   OXT    O N N 463 
PHE   H      H N N 464 
PHE   H2     H N N 465 
PHE   HA     H N N 466 
PHE   HB2    H N N 467 
PHE   HB3    H N N 468 
PHE   HD1    H N N 469 
PHE   HD2    H N N 470 
PHE   HE1    H N N 471 
PHE   HE2    H N N 472 
PHE   HZ     H N N 473 
PHE   HXT    H N N 474 
PRO   N      N N N 475 
PRO   CA     C N S 476 
PRO   C      C N N 477 
PRO   O      O N N 478 
PRO   CB     C N N 479 
PRO   CG     C N N 480 
PRO   CD     C N N 481 
PRO   OXT    O N N 482 
PRO   H      H N N 483 
PRO   HA     H N N 484 
PRO   HB2    H N N 485 
PRO   HB3    H N N 486 
PRO   HG2    H N N 487 
PRO   HG3    H N N 488 
PRO   HD2    H N N 489 
PRO   HD3    H N N 490 
PRO   HXT    H N N 491 
SER   N      N N N 492 
SER   CA     C N S 493 
SER   C      C N N 494 
SER   O      O N N 495 
SER   CB     C N N 496 
SER   OG     O N N 497 
SER   OXT    O N N 498 
SER   H      H N N 499 
SER   H2     H N N 500 
SER   HA     H N N 501 
SER   HB2    H N N 502 
SER   HB3    H N N 503 
SER   HG     H N N 504 
SER   HXT    H N N 505 
THR   N      N N N 506 
THR   CA     C N S 507 
THR   C      C N N 508 
THR   O      O N N 509 
THR   CB     C N R 510 
THR   OG1    O N N 511 
THR   CG2    C N N 512 
THR   OXT    O N N 513 
THR   H      H N N 514 
THR   H2     H N N 515 
THR   HA     H N N 516 
THR   HB     H N N 517 
THR   HG1    H N N 518 
THR   HG21   H N N 519 
THR   HG22   H N N 520 
THR   HG23   H N N 521 
THR   HXT    H N N 522 
TRP   N      N N N 523 
TRP   CA     C N S 524 
TRP   C      C N N 525 
TRP   O      O N N 526 
TRP   CB     C N N 527 
TRP   CG     C Y N 528 
TRP   CD1    C Y N 529 
TRP   CD2    C Y N 530 
TRP   NE1    N Y N 531 
TRP   CE2    C Y N 532 
TRP   CE3    C Y N 533 
TRP   CZ2    C Y N 534 
TRP   CZ3    C Y N 535 
TRP   CH2    C Y N 536 
TRP   OXT    O N N 537 
TRP   H      H N N 538 
TRP   H2     H N N 539 
TRP   HA     H N N 540 
TRP   HB2    H N N 541 
TRP   HB3    H N N 542 
TRP   HD1    H N N 543 
TRP   HE1    H N N 544 
TRP   HE3    H N N 545 
TRP   HZ2    H N N 546 
TRP   HZ3    H N N 547 
TRP   HH2    H N N 548 
TRP   HXT    H N N 549 
TYR   N      N N N 550 
TYR   CA     C N S 551 
TYR   C      C N N 552 
TYR   O      O N N 553 
TYR   CB     C N N 554 
TYR   CG     C Y N 555 
TYR   CD1    C Y N 556 
TYR   CD2    C Y N 557 
TYR   CE1    C Y N 558 
TYR   CE2    C Y N 559 
TYR   CZ     C Y N 560 
TYR   OH     O N N 561 
TYR   OXT    O N N 562 
TYR   H      H N N 563 
TYR   H2     H N N 564 
TYR   HA     H N N 565 
TYR   HB2    H N N 566 
TYR   HB3    H N N 567 
TYR   HD1    H N N 568 
TYR   HD2    H N N 569 
TYR   HE1    H N N 570 
TYR   HE2    H N N 571 
TYR   HH     H N N 572 
TYR   HXT    H N N 573 
VAL   N      N N N 574 
VAL   CA     C N S 575 
VAL   C      C N N 576 
VAL   O      O N N 577 
VAL   CB     C N N 578 
VAL   CG1    C N N 579 
VAL   CG2    C N N 580 
VAL   OXT    O N N 581 
VAL   H      H N N 582 
VAL   H2     H N N 583 
VAL   HA     H N N 584 
VAL   HB     H N N 585 
VAL   HG11   H N N 586 
VAL   HG12   H N N 587 
VAL   HG13   H N N 588 
VAL   HG21   H N N 589 
VAL   HG22   H N N 590 
VAL   HG23   H N N 591 
VAL   HXT    H N N 592 
# 
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 
NAP   PA    O1A    doub N N 369 
NAP   PA    O2A    sing N N 370 
NAP   PA    O5B    sing N N 371 
NAP   PA    O3     sing N N 372 
NAP   O2A   HOA2   sing N N 373 
NAP   O5B   C5B    sing N N 374 
NAP   C5B   C4B    sing N N 375 
NAP   C5B   H51A   sing N N 376 
NAP   C5B   H52A   sing N N 377 
NAP   C4B   O4B    sing N N 378 
NAP   C4B   C3B    sing N N 379 
NAP   C4B   H4B    sing N N 380 
NAP   O4B   C1B    sing N N 381 
NAP   C3B   O3B    sing N N 382 
NAP   C3B   C2B    sing N N 383 
NAP   C3B   H3B    sing N N 384 
NAP   O3B   HO3A   sing N N 385 
NAP   C2B   O2B    sing N N 386 
NAP   C2B   C1B    sing N N 387 
NAP   C2B   H2B    sing N N 388 
NAP   O2B   P2B    sing N N 389 
NAP   C1B   N9A    sing N N 390 
NAP   C1B   H1B    sing N N 391 
NAP   N9A   C8A    sing Y N 392 
NAP   N9A   C4A    sing Y N 393 
NAP   C8A   N7A    doub Y N 394 
NAP   C8A   H8A    sing N N 395 
NAP   N7A   C5A    sing Y N 396 
NAP   C5A   C6A    sing Y N 397 
NAP   C5A   C4A    doub Y N 398 
NAP   C6A   N6A    sing N N 399 
NAP   C6A   N1A    doub Y N 400 
NAP   N6A   H61A   sing N N 401 
NAP   N6A   H62A   sing N N 402 
NAP   N1A   C2A    sing Y N 403 
NAP   C2A   N3A    doub Y N 404 
NAP   C2A   H2A    sing N N 405 
NAP   N3A   C4A    sing Y N 406 
NAP   O3    PN     sing N N 407 
NAP   PN    O1N    doub N N 408 
NAP   PN    O2N    sing N N 409 
NAP   PN    O5D    sing N N 410 
NAP   O5D   C5D    sing N N 411 
NAP   C5D   C4D    sing N N 412 
NAP   C5D   H51N   sing N N 413 
NAP   C5D   H52N   sing N N 414 
NAP   C4D   O4D    sing N N 415 
NAP   C4D   C3D    sing N N 416 
NAP   C4D   H4D    sing N N 417 
NAP   O4D   C1D    sing N N 418 
NAP   C3D   O3D    sing N N 419 
NAP   C3D   C2D    sing N N 420 
NAP   C3D   H3D    sing N N 421 
NAP   O3D   HO3N   sing N N 422 
NAP   C2D   O2D    sing N N 423 
NAP   C2D   C1D    sing N N 424 
NAP   C2D   H2D    sing N N 425 
NAP   O2D   HO2N   sing N N 426 
NAP   C1D   N1N    sing N N 427 
NAP   C1D   H1D    sing N N 428 
NAP   N1N   C2N    sing Y N 429 
NAP   N1N   C6N    doub Y N 430 
NAP   C2N   C3N    doub Y N 431 
NAP   C2N   H2N    sing N N 432 
NAP   C3N   C7N    sing N N 433 
NAP   C3N   C4N    sing Y N 434 
NAP   C7N   O7N    doub N N 435 
NAP   C7N   N7N    sing N N 436 
NAP   N7N   H71N   sing N N 437 
NAP   N7N   H72N   sing N N 438 
NAP   C4N   C5N    doub Y N 439 
NAP   C4N   H4N    sing N N 440 
NAP   C5N   C6N    sing Y N 441 
NAP   C5N   H5N    sing N N 442 
NAP   C6N   H6N    sing N N 443 
NAP   P2B   O1X    doub N N 444 
NAP   P2B   O2X    sing N N 445 
NAP   P2B   O3X    sing N N 446 
NAP   O2X   HOP2   sing N N 447 
NAP   O3X   HOP3   sing N N 448 
PHE   N     CA     sing N N 449 
PHE   N     H      sing N N 450 
PHE   N     H2     sing N N 451 
PHE   CA    C      sing N N 452 
PHE   CA    CB     sing N N 453 
PHE   CA    HA     sing N N 454 
PHE   C     O      doub N N 455 
PHE   C     OXT    sing N N 456 
PHE   CB    CG     sing N N 457 
PHE   CB    HB2    sing N N 458 
PHE   CB    HB3    sing N N 459 
PHE   CG    CD1    doub Y N 460 
PHE   CG    CD2    sing Y N 461 
PHE   CD1   CE1    sing Y N 462 
PHE   CD1   HD1    sing N N 463 
PHE   CD2   CE2    doub Y N 464 
PHE   CD2   HD2    sing N N 465 
PHE   CE1   CZ     doub Y N 466 
PHE   CE1   HE1    sing N N 467 
PHE   CE2   CZ     sing Y N 468 
PHE   CE2   HE2    sing N N 469 
PHE   CZ    HZ     sing N N 470 
PHE   OXT   HXT    sing N N 471 
PRO   N     CA     sing N N 472 
PRO   N     CD     sing N N 473 
PRO   N     H      sing N N 474 
PRO   CA    C      sing N N 475 
PRO   CA    CB     sing N N 476 
PRO   CA    HA     sing N N 477 
PRO   C     O      doub N N 478 
PRO   C     OXT    sing N N 479 
PRO   CB    CG     sing N N 480 
PRO   CB    HB2    sing N N 481 
PRO   CB    HB3    sing N N 482 
PRO   CG    CD     sing N N 483 
PRO   CG    HG2    sing N N 484 
PRO   CG    HG3    sing N N 485 
PRO   CD    HD2    sing N N 486 
PRO   CD    HD3    sing N N 487 
PRO   OXT   HXT    sing N N 488 
SER   N     CA     sing N N 489 
SER   N     H      sing N N 490 
SER   N     H2     sing N N 491 
SER   CA    C      sing N N 492 
SER   CA    CB     sing N N 493 
SER   CA    HA     sing N N 494 
SER   C     O      doub N N 495 
SER   C     OXT    sing N N 496 
SER   CB    OG     sing N N 497 
SER   CB    HB2    sing N N 498 
SER   CB    HB3    sing N N 499 
SER   OG    HG     sing N N 500 
SER   OXT   HXT    sing N N 501 
THR   N     CA     sing N N 502 
THR   N     H      sing N N 503 
THR   N     H2     sing N N 504 
THR   CA    C      sing N N 505 
THR   CA    CB     sing N N 506 
THR   CA    HA     sing N N 507 
THR   C     O      doub N N 508 
THR   C     OXT    sing N N 509 
THR   CB    OG1    sing N N 510 
THR   CB    CG2    sing N N 511 
THR   CB    HB     sing N N 512 
THR   OG1   HG1    sing N N 513 
THR   CG2   HG21   sing N N 514 
THR   CG2   HG22   sing N N 515 
THR   CG2   HG23   sing N N 516 
THR   OXT   HXT    sing N N 517 
TRP   N     CA     sing N N 518 
TRP   N     H      sing N N 519 
TRP   N     H2     sing N N 520 
TRP   CA    C      sing N N 521 
TRP   CA    CB     sing N N 522 
TRP   CA    HA     sing N N 523 
TRP   C     O      doub N N 524 
TRP   C     OXT    sing N N 525 
TRP   CB    CG     sing N N 526 
TRP   CB    HB2    sing N N 527 
TRP   CB    HB3    sing N N 528 
TRP   CG    CD1    doub Y N 529 
TRP   CG    CD2    sing Y N 530 
TRP   CD1   NE1    sing Y N 531 
TRP   CD1   HD1    sing N N 532 
TRP   CD2   CE2    doub Y N 533 
TRP   CD2   CE3    sing Y N 534 
TRP   NE1   CE2    sing Y N 535 
TRP   NE1   HE1    sing N N 536 
TRP   CE2   CZ2    sing Y N 537 
TRP   CE3   CZ3    doub Y N 538 
TRP   CE3   HE3    sing N N 539 
TRP   CZ2   CH2    doub Y N 540 
TRP   CZ2   HZ2    sing N N 541 
TRP   CZ3   CH2    sing Y N 542 
TRP   CZ3   HZ3    sing N N 543 
TRP   CH2   HH2    sing N N 544 
TRP   OXT   HXT    sing N N 545 
TYR   N     CA     sing N N 546 
TYR   N     H      sing N N 547 
TYR   N     H2     sing N N 548 
TYR   CA    C      sing N N 549 
TYR   CA    CB     sing N N 550 
TYR   CA    HA     sing N N 551 
TYR   C     O      doub N N 552 
TYR   C     OXT    sing N N 553 
TYR   CB    CG     sing N N 554 
TYR   CB    HB2    sing N N 555 
TYR   CB    HB3    sing N N 556 
TYR   CG    CD1    doub Y N 557 
TYR   CG    CD2    sing Y N 558 
TYR   CD1   CE1    sing Y N 559 
TYR   CD1   HD1    sing N N 560 
TYR   CD2   CE2    doub Y N 561 
TYR   CD2   HD2    sing N N 562 
TYR   CE1   CZ     doub Y N 563 
TYR   CE1   HE1    sing N N 564 
TYR   CE2   CZ     sing Y N 565 
TYR   CE2   HE2    sing N N 566 
TYR   CZ    OH     sing N N 567 
TYR   OH    HH     sing N N 568 
TYR   OXT   HXT    sing N N 569 
VAL   N     CA     sing N N 570 
VAL   N     H      sing N N 571 
VAL   N     H2     sing N N 572 
VAL   CA    C      sing N N 573 
VAL   CA    CB     sing N N 574 
VAL   CA    HA     sing N N 575 
VAL   C     O      doub N N 576 
VAL   C     OXT    sing N N 577 
VAL   CB    CG1    sing N N 578 
VAL   CB    CG2    sing N N 579 
VAL   CB    HB     sing N N 580 
VAL   CG1   HG11   sing N N 581 
VAL   CG1   HG12   sing N N 582 
VAL   CG1   HG13   sing N N 583 
VAL   CG2   HG21   sing N N 584 
VAL   CG2   HG22   sing N N 585 
VAL   CG2   HG23   sing N N 586 
VAL   OXT   HXT    sing N N 587 
# 
_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                    8Z16 
_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]   0.014721 
_atom_sites.fract_transf_matrix[1][2]   0.008499 
_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]   0.016999 
_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]   0.002620 
_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   ? 12.409 -13.937 7.613   1.00 61.30  ?  1   MET   A N     1 
ATOM   2    C CA    . MET   A 1 1   ? 13.291 -12.943 8.273   1.00 59.81  ?  1   MET   A CA    1 
ATOM   3    C C     . MET   A 1 1   ? 14.740 -13.231 7.890   1.00 53.58  ?  1   MET   A C     1 
ATOM   4    O O     . MET   A 1 1   ? 15.421 -12.309 7.432   1.00 53.29  ?  1   MET   A O     1 
ATOM   5    C CB    . MET   A 1 1   ? 13.180 -13.031 9.796   1.00 30.00  ?  1   MET   A CB    1 
ATOM   6    C CG    . MET   A 1 1   ? 14.102 -12.093 10.550  1.00 30.00  ?  1   MET   A CG    1 
ATOM   7    S SD    . MET   A 1 1   ? 13.525 -10.384 10.564  1.00 30.00  ?  1   MET   A SD    1 
ATOM   8    C CE    . MET   A 1 1   ? 12.358 -10.433 11.932  1.00 30.00  ?  1   MET   A CE    1 
ATOM   9    N N     . ARG   A 1 2   ? 15.180 -14.469 8.069   1.00 48.31  ?  2   ARG   A N     1 
ATOM   10   C CA    . ARG   A 1 2   ? 16.602 -14.782 7.794   1.00 54.69  ?  2   ARG   A CA    1 
ATOM   11   C C     . ARG   A 1 2   ? 16.838 -14.981 6.283   1.00 54.27  ?  2   ARG   A C     1 
ATOM   12   O O     . ARG   A 1 2   ? 17.893 -14.543 5.804   1.00 50.20  ?  2   ARG   A O     1 
ATOM   13   C CB    . ARG   A 1 2   ? 17.039 -15.997 8.616   1.00 49.11  ?  2   ARG   A CB    1 
ATOM   14   C CG    . ARG   A 1 2   ? 17.425 -15.747 10.063  1.00 51.10  ?  2   ARG   A CG    1 
ATOM   15   C CD    . ARG   A 1 2   ? 18.216 -16.925 10.599  1.00 54.65  ?  2   ARG   A CD    1 
ATOM   16   N NE    . ARG   A 1 2   ? 19.648 -16.786 10.319  1.00 56.66  ?  2   ARG   A NE    1 
ATOM   17   C CZ    . ARG   A 1 2   ? 20.582 -17.620 10.748  1.00 54.53  ?  2   ARG   A CZ    1 
ATOM   18   N NH1   . ARG   A 1 2   ? 20.234 -18.752 11.328  1.00 47.81  ?  2   ARG   A NH1   1 
ATOM   19   N NH2   . ARG   A 1 2   ? 21.857 -17.315 10.597  1.00 51.63  ?  2   ARG   A NH2   1 
ATOM   20   N N     . VAL   A 1 3   ? 15.905 -15.617 5.564   1.00 47.72  ?  3   VAL   A N     1 
ATOM   21   C CA    . VAL   A 1 3   ? 16.198 -15.929 4.134   1.00 51.83  ?  3   VAL   A CA    1 
ATOM   22   C C     . VAL   A 1 3   ? 15.004 -15.738 3.193   1.00 48.10  ?  3   VAL   A C     1 
ATOM   23   O O     . VAL   A 1 3   ? 13.952 -16.318 3.445   1.00 42.31  ?  3   VAL   A O     1 
ATOM   24   C CB    . VAL   A 1 3   ? 16.764 -17.350 3.931   1.00 47.24  ?  3   VAL   A CB    1 
ATOM   25   C CG1   . VAL   A 1 3   ? 17.102 -17.612 2.471   1.00 45.13  ?  3   VAL   A CG1   1 
ATOM   26   C CG2   . VAL   A 1 3   ? 17.966 -17.657 4.811   1.00 46.01  ?  3   VAL   A CG2   1 
ATOM   27   N N     . CYS   A 1 4   ? 15.177 -14.912 2.163   1.00 52.62  ?  4   CYS   A N     1 
ATOM   28   C CA    . CYS   A 1 4   ? 14.195 -14.847 1.071   1.00 53.78  ?  4   CYS   A CA    1 
ATOM   29   C C     . CYS   A 1 4   ? 14.641 -15.785 -0.057  1.00 50.81  ?  4   CYS   A C     1 
ATOM   30   O O     . CYS   A 1 4   ? 15.740 -15.633 -0.609  1.00 47.06  ?  4   CYS   A O     1 
ATOM   31   C CB    . CYS   A 1 4   ? 14.018 -13.416 0.549   1.00 44.43  ?  4   CYS   A CB    1 
ATOM   32   S SG    . CYS   A 1 4   ? 12.741 -13.150 -0.761  1.00 54.52  ?  4   CYS   A SG    1 
ATOM   33   N N     . VAL   A 1 5   ? 13.807 -16.772 -0.359  1.00 43.48  ?  5   VAL   A N     1 
ATOM   34   C CA    . VAL   A 1 5   ? 14.030 -17.709 -1.449  1.00 47.20  ?  5   VAL   A CA    1 
ATOM   35   C C     . VAL   A 1 5   ? 13.096 -17.315 -2.584  1.00 52.07  ?  5   VAL   A C     1 
ATOM   36   O O     . VAL   A 1 5   ? 11.869 -17.407 -2.440  1.00 54.54  ?  5   VAL   A O     1 
ATOM   37   C CB    . VAL   A 1 5   ? 13.781 -19.153 -1.008  1.00 50.46  ?  5   VAL   A CB    1 
ATOM   38   C CG1   . VAL   A 1 5   ? 14.059 -20.119 -2.169  1.00 48.88  ?  5   VAL   A CG1   1 
ATOM   39   C CG2   . VAL   A 1 5   ? 14.634 -19.475 0.217   1.00 46.08  ?  5   VAL   A CG2   1 
ATOM   40   N N     . ILE   A 1 6   ? 13.668 -16.885 -3.710  1.00 44.39  ?  6   ILE   A N     1 
ATOM   41   C CA    . ILE   A 1 6   ? 12.888 -16.440 -4.861  1.00 43.85  ?  6   ILE   A CA    1 
ATOM   42   C C     . ILE   A 1 6   ? 12.590 -17.651 -5.748  1.00 46.44  ?  6   ILE   A C     1 
ATOM   43   O O     . ILE   A 1 6   ? 13.493 -18.242 -6.346  1.00 40.98  ?  6   ILE   A O     1 
ATOM   44   C CB    . ILE   A 1 6   ? 13.610 -15.331 -5.637  1.00 42.55  ?  6   ILE   A CB    1 
ATOM   45   C CG1   . ILE   A 1 6   ? 13.708 -14.055 -4.795  1.00 40.98  ?  6   ILE   A CG1   1 
ATOM   46   C CG2   . ILE   A 1 6   ? 12.867 -15.022 -6.913  1.00 46.67  ?  6   ILE   A CG2   1 
ATOM   47   C CD1   . ILE   A 1 6   ? 14.725 -13.043 -5.289  1.00 38.09  ?  6   ILE   A CD1   1 
ATOM   48   N N     . GLY   A 1 7   ? 11.317 -18.033 -5.810  1.00 48.51  ?  7   GLY   A N     1 
ATOM   49   C CA    . GLY   A 1 7   ? 10.878 -19.097 -6.683  1.00 46.05  ?  7   GLY   A CA    1 
ATOM   50   C C     . GLY   A 1 7   ? 10.585 -20.409 -5.994  1.00 48.88  ?  7   GLY   A C     1 
ATOM   51   O O     . GLY   A 1 7   ? 11.372 -20.886 -5.164  1.00 46.90  ?  7   GLY   A O     1 
ATOM   52   N N     . ALA   A 1 8   ? 9.468  -21.022 -6.375  1.00 48.99  ?  8   ALA   A N     1 
ATOM   53   C CA    . ALA   A 1 8   ? 8.999  -22.278 -5.800  1.00 47.53  ?  8   ALA   A CA    1 
ATOM   54   C C     . ALA   A 1 8   ? 8.975  -23.427 -6.814  1.00 51.21  ?  8   ALA   A C     1 
ATOM   55   O O     . ALA   A 1 8   ? 8.115  -24.318 -6.758  1.00 48.77  ?  8   ALA   A O     1 
ATOM   56   C CB    . ALA   A 1 8   ? 7.617  -22.087 -5.189  1.00 52.53  ?  8   ALA   A CB    1 
ATOM   57   N N     . GLY   A 1 9   ? 9.914  -23.433 -7.756  1.00 49.66  ?  9   GLY   A N     1 
ATOM   58   C CA    . GLY   A 1 9   ? 10.109 -24.589 -8.603  1.00 46.07  ?  9   GLY   A CA    1 
ATOM   59   C C     . GLY   A 1 9   ? 10.825 -25.703 -7.855  1.00 46.60  ?  9   GLY   A C     1 
ATOM   60   O O     . GLY   A 1 9   ? 10.985 -25.684 -6.634  1.00 42.94  ?  9   GLY   A O     1 
ATOM   61   N N     . LEU   A 1 10  ? 11.296 -26.682 -8.630  1.00 48.75  ?  10  LEU   A N     1 
ATOM   62   C CA    . LEU   A 1 10  ? 11.966 -27.849 -8.058  1.00 44.12  ?  10  LEU   A CA    1 
ATOM   63   C C     . LEU   A 1 10  ? 13.123 -27.470 -7.147  1.00 38.50  ?  10  LEU   A C     1 
ATOM   64   O O     . LEU   A 1 10  ? 13.490 -28.245 -6.259  1.00 36.78  ?  10  LEU   A O     1 
ATOM   65   C CB    . LEU   A 1 10  ? 12.474 -28.747 -9.192  1.00 43.77  ?  10  LEU   A CB    1 
ATOM   66   C CG    . LEU   A 1 10  ? 13.392 -29.917 -8.818  1.00 44.42  ?  10  LEU   A CG    1 
ATOM   67   C CD1   . LEU   A 1 10  ? 13.020 -31.137 -9.615  1.00 37.87  ?  10  LEU   A CD1   1 
ATOM   68   C CD2   . LEU   A 1 10  ? 14.874 -29.557 -9.012  1.00 43.45  ?  10  LEU   A CD2   1 
ATOM   69   N N     . SER   A 1 11  ? 13.741 -26.315 -7.384  1.00 37.52  ?  11  SER   A N     1 
ATOM   70   C CA    . SER   A 1 11  ? 14.925 -25.898 -6.640  1.00 42.95  ?  11  SER   A CA    1 
ATOM   71   C C     . SER   A 1 11  ? 14.570 -25.144 -5.361  1.00 42.13  ?  11  SER   A C     1 
ATOM   72   O O     . SER   A 1 11  ? 15.020 -25.528 -4.278  1.00 39.48  ?  11  SER   A O     1 
ATOM   73   C CB    . SER   A 1 11  ? 15.848 -25.055 -7.532  1.00 45.07  ?  11  SER   A CB    1 
ATOM   74   O OG    . SER   A 1 11  ? 16.264 -25.781 -8.662  1.00 45.04  ?  11  SER   A OG    1 
ATOM   75   N N     . GLY   A 1 12  ? 13.782 -24.066 -5.485  1.00 43.99  ?  12  GLY   A N     1 
ATOM   76   C CA    . GLY   A 1 12  ? 13.252 -23.389 -4.309  1.00 42.60  ?  12  GLY   A CA    1 
ATOM   77   C C     . GLY   A 1 12  ? 12.695 -24.363 -3.292  1.00 43.09  ?  12  GLY   A C     1 
ATOM   78   O O     . GLY   A 1 12  ? 12.871 -24.189 -2.086  1.00 42.10  ?  12  GLY   A O     1 
ATOM   79   N N     . LEU   A 1 13  ? 12.053 -25.430 -3.769  1.00 39.67  ?  13  LEU   A N     1 
ATOM   80   C CA    . LEU   A 1 13  ? 11.551 -26.454 -2.861  1.00 40.25  ?  13  LEU   A CA    1 
ATOM   81   C C     . LEU   A 1 13  ? 12.700 -27.182 -2.172  1.00 43.36  ?  13  LEU   A C     1 
ATOM   82   O O     . LEU   A 1 13  ? 12.731 -27.303 -0.945  1.00 42.35  ?  13  LEU   A O     1 
ATOM   83   C CB    . LEU   A 1 13  ? 10.650 -27.440 -3.609  1.00 40.91  ?  13  LEU   A CB    1 
ATOM   84   C CG    . LEU   A 1 13  ? 9.353  -26.904 -4.242  1.00 44.95  ?  13  LEU   A CG    1 
ATOM   85   C CD1   . LEU   A 1 13  ? 8.461  -28.015 -4.848  1.00 42.82  ?  13  LEU   A CD1   1 
ATOM   86   C CD2   . LEU   A 1 13  ? 8.551  -26.074 -3.245  1.00 49.51  ?  13  LEU   A CD2   1 
ATOM   87   N N     . ALA   A 1 14  ? 13.673 -27.662 -2.933  1.00 42.40  ?  14  ALA   A N     1 
ATOM   88   C CA    . ALA   A 1 14  ? 14.793 -28.302 -2.259  1.00 41.56  ?  14  ALA   A CA    1 
ATOM   89   C C     . ALA   A 1 14  ? 15.476 -27.338 -1.287  1.00 43.31  ?  14  ALA   A C     1 
ATOM   90   O O     . ALA   A 1 14  ? 16.085 -27.779 -0.296  1.00 41.77  ?  14  ALA   A O     1 
ATOM   91   C CB    . ALA   A 1 14  ? 15.790 -28.850 -3.275  1.00 36.58  ?  14  ALA   A CB    1 
ATOM   92   N N     . VAL   A 1 15  ? 15.375 -26.028 -1.537  1.00 36.35  ?  15  VAL   A N     1 
ATOM   93   C CA    . VAL   A 1 15  ? 16.029 -25.063 -0.660  1.00 44.24  ?  15  VAL   A CA    1 
ATOM   94   C C     . VAL   A 1 15  ? 15.315 -25.025 0.696   1.00 46.87  ?  15  VAL   A C     1 
ATOM   95   O O     . VAL   A 1 15  ? 15.913 -25.279 1.752   1.00 40.64  ?  15  VAL   A O     1 
ATOM   96   C CB    . VAL   A 1 15  ? 16.084 -23.675 -1.325  1.00 43.05  ?  15  VAL   A CB    1 
ATOM   97   C CG1   . VAL   A 1 15  ? 16.380 -22.632 -0.284  1.00 42.96  ?  15  VAL   A CG1   1 
ATOM   98   C CG2   . VAL   A 1 15  ? 17.150 -23.632 -2.405  1.00 32.74  ?  15  VAL   A CG2   1 
ATOM   99   N N     . GLY   A 1 16  ? 14.004 -24.779 0.672   1.00 44.55  ?  16  GLY   A N     1 
ATOM   100  C CA    . GLY   A 1 16  ? 13.243 -24.748 1.912   1.00 48.69  ?  16  GLY   A CA    1 
ATOM   101  C C     . GLY   A 1 16  ? 13.369 -26.020 2.729   1.00 44.10  ?  16  GLY   A C     1 
ATOM   102  O O     . GLY   A 1 16  ? 13.485 -25.967 3.954   1.00 51.06  ?  16  GLY   A O     1 
ATOM   103  N N     . HIS   A 1 17  ? 13.332 -27.178 2.068   1.00 39.75  ?  17  HIS   A N     1 
ATOM   104  C CA    . HIS   A 1 17  ? 13.608 -28.428 2.761   1.00 41.81  ?  17  HIS   A CA    1 
ATOM   105  C C     . HIS   A 1 17  ? 14.934 -28.366 3.513   1.00 45.98  ?  17  HIS   A C     1 
ATOM   106  O O     . HIS   A 1 17  ? 15.025 -28.819 4.655   1.00 47.66  ?  17  HIS   A O     1 
ATOM   107  C CB    . HIS   A 1 17  ? 13.601 -29.577 1.763   1.00 39.91  ?  17  HIS   A CB    1 
ATOM   108  C CG    . HIS   A 1 17  ? 13.596 -30.943 2.384   1.00 42.64  ?  17  HIS   A CG    1 
ATOM   109  N ND1   . HIS   A 1 17  ? 12.525 -31.438 3.102   1.00 48.43  ?  17  HIS   A ND1   1 
ATOM   110  C CD2   . HIS   A 1 17  ? 14.514 -31.939 2.348   1.00 43.22  ?  17  HIS   A CD2   1 
ATOM   111  C CE1   . HIS   A 1 17  ? 12.787 -32.672 3.490   1.00 46.55  ?  17  HIS   A CE1   1 
ATOM   112  N NE2   . HIS   A 1 17  ? 13.989 -32.999 3.047   1.00 47.72  ?  17  HIS   A NE2   1 
ATOM   113  N N     . ALA   A 1 18  ? 15.966 -27.780 2.904   1.00 46.67  ?  18  ALA   A N     1 
ATOM   114  C CA    . ALA   A 1 18  ? 17.262 -27.706 3.569   1.00 48.13  ?  18  ALA   A CA    1 
ATOM   115  C C     . ALA   A 1 18  ? 17.217 -26.761 4.769   1.00 49.31  ?  18  ALA   A C     1 
ATOM   116  O O     . ALA   A 1 18  ? 17.672 -27.109 5.865   1.00 46.00  ?  18  ALA   A O     1 
ATOM   117  C CB    . ALA   A 1 18  ? 18.332 -27.265 2.573   1.00 36.88  ?  18  ALA   A CB    1 
ATOM   118  N N     . LEU   A 1 19  ? 16.663 -25.564 4.572   1.00 43.86  ?  19  LEU   A N     1 
ATOM   119  C CA    . LEU   A 1 19  ? 16.652 -24.557 5.619   1.00 44.55  ?  19  LEU   A CA    1 
ATOM   120  C C     . LEU   A 1 19  ? 15.766 -24.968 6.778   1.00 49.57  ?  19  LEU   A C     1 
ATOM   121  O O     . LEU   A 1 19  ? 16.085 -24.694 7.941   1.00 46.01  ?  19  LEU   A O     1 
ATOM   122  C CB    . LEU   A 1 19  ? 16.164 -23.239 5.046   1.00 45.93  ?  19  LEU   A CB    1 
ATOM   123  C CG    . LEU   A 1 19  ? 17.124 -22.635 4.040   1.00 40.10  ?  19  LEU   A CG    1 
ATOM   124  C CD1   . LEU   A 1 19  ? 16.602 -21.283 3.628   1.00 39.12  ?  19  LEU   A CD1   1 
ATOM   125  C CD2   . LEU   A 1 19  ? 18.489 -22.534 4.682   1.00 40.98  ?  19  LEU   A CD2   1 
ATOM   126  N N     . LYS   A 1 20  ? 14.634 -25.595 6.472   1.00 47.02  ?  20  LYS   A N     1 
ATOM   127  C CA    . LYS   A 1 20  ? 13.708 -26.005 7.515   1.00 46.02  ?  20  LYS   A CA    1 
ATOM   128  C C     . LYS   A 1 20  ? 14.309 -27.114 8.367   1.00 49.10  ?  20  LYS   A C     1 
ATOM   129  O O     . LYS   A 1 20  ? 14.292 -27.044 9.598   1.00 52.35  ?  20  LYS   A O     1 
ATOM   130  C CB    . LYS   A 1 20  ? 12.403 -26.463 6.887   1.00 45.52  ?  20  LYS   A CB    1 
ATOM   131  C CG    . LYS   A 1 20  ? 11.189 -26.012 7.632   1.00 48.29  ?  20  LYS   A CG    1 
ATOM   132  C CD    . LYS   A 1 20  ? 10.195 -27.145 7.736   1.00 48.50  ?  20  LYS   A CD    1 
ATOM   133  C CE    . LYS   A 1 20  ? 8.793  -26.645 8.029   1.00 40.40  ?  20  LYS   A CE    1 
ATOM   134  N NZ    . LYS   A 1 20  ? 7.923  -27.825 8.219   1.00 41.94  ?  20  LYS   A NZ    1 
ATOM   135  N N     . GLU   A 1 21  ? 14.858 -28.142 7.723   1.00 52.52  ?  21  GLU   A N     1 
ATOM   136  C CA    . GLU   A 1 21  ? 15.558 -29.204 8.428   1.00 50.07  ?  21  GLU   A CA    1 
ATOM   137  C C     . GLU   A 1 21  ? 16.560 -28.666 9.419   1.00 51.07  ?  21  GLU   A C     1 
ATOM   138  O O     . GLU   A 1 21  ? 16.910 -29.355 10.378  1.00 52.91  ?  21  GLU   A O     1 
ATOM   139  C CB    . GLU   A 1 21  ? 16.300 -30.098 7.433   1.00 47.23  ?  21  GLU   A CB    1 
ATOM   140  C CG    . GLU   A 1 21  ? 15.406 -31.015 6.644   1.00 52.25  ?  21  GLU   A CG    1 
ATOM   141  C CD    . GLU   A 1 21  ? 14.588 -31.931 7.524   1.00 63.93  ?  21  GLU   A CD    1 
ATOM   142  O OE1   . GLU   A 1 21  ? 13.488 -31.513 7.966   1.00 67.29  ?  21  GLU   A OE1   1 
ATOM   143  O OE2   . GLU   A 1 21  ? 15.043 -33.073 7.770   1.00 66.97  ?  21  GLU   A OE2   1 
ATOM   144  N N     . ARG   A 1 22  ? 17.051 -27.459 9.197   1.00 51.16  ?  22  ARG   A N     1 
ATOM   145  C CA    . ARG   A 1 22  ? 18.161 -26.954 9.976   1.00 50.99  ?  22  ARG   A CA    1 
ATOM   146  C C     . ARG   A 1 22  ? 17.723 -25.982 11.051  1.00 54.48  ?  22  ARG   A C     1 
ATOM   147  O O     . ARG   A 1 22  ? 18.394 -25.864 12.085  1.00 59.30  ?  22  ARG   A O     1 
ATOM   148  C CB    . ARG   A 1 22  ? 19.160 -26.284 9.046   1.00 50.16  ?  22  ARG   A CB    1 
ATOM   149  C CG    . ARG   A 1 22  ? 20.499 -26.146 9.626   1.00 54.19  ?  22  ARG   A CG    1 
ATOM   150  C CD    . ARG   A 1 22  ? 21.521 -26.157 8.550   1.00 45.09  ?  22  ARG   A CD    1 
ATOM   151  N NE    . ARG   A 1 22  ? 22.792 -26.628 9.073   1.00 53.27  ?  22  ARG   A NE    1 
ATOM   152  C CZ    . ARG   A 1 22  ? 23.071 -27.908 9.265   1.00 56.11  ?  22  ARG   A CZ    1 
ATOM   153  N NH1   . ARG   A 1 22  ? 22.164 -28.830 8.981   1.00 60.80  ?  22  ARG   A NH1   1 
ATOM   154  N NH2   . ARG   A 1 22  ? 24.252 -28.265 9.735   1.00 61.68  ?  22  ARG   A NH2   1 
ATOM   155  N N     . GLY   A 1 23  ? 16.596 -25.314 10.836  1.00 50.25  ?  23  GLY   A N     1 
ATOM   156  C CA    . GLY   A 1 23  ? 16.059 -24.362 11.783  1.00 48.55  ?  23  GLY   A CA    1 
ATOM   157  C C     . GLY   A 1 23  ? 16.046 -22.935 11.291  1.00 52.46  ?  23  GLY   A C     1 
ATOM   158  O O     . GLY   A 1 23  ? 15.644 -22.043 12.053  1.00 53.28  ?  23  GLY   A O     1 
ATOM   159  N N     . ILE   A 1 24  ? 16.463 -22.656 10.062  1.00 46.38  ?  24  ILE   A N     1 
ATOM   160  C CA    . ILE   A 1 24  ? 16.512 -21.276 9.608   1.00 45.99  ?  24  ILE   A CA    1 
ATOM   161  C C     . ILE   A 1 24  ? 15.121 -20.838 9.182   1.00 48.35  ?  24  ILE   A C     1 
ATOM   162  O O     . ILE   A 1 24  ? 14.379 -21.591 8.542   1.00 48.05  ?  24  ILE   A O     1 
ATOM   163  C CB    . ILE   A 1 24  ? 17.537 -21.115 8.474   1.00 48.38  ?  24  ILE   A CB    1 
ATOM   164  C CG1   . ILE   A 1 24  ? 18.904 -21.597 8.946   1.00 46.03  ?  24  ILE   A CG1   1 
ATOM   165  C CG2   . ILE   A 1 24  ? 17.624 -19.654 8.019   1.00 45.55  ?  24  ILE   A CG2   1 
ATOM   166  C CD1   . ILE   A 1 24  ? 19.347 -22.865 8.295   1.00 50.79  ?  24  ILE   A CD1   1 
ATOM   167  N N     . SER   A 1 25  ? 14.756 -19.621 9.571   1.00 48.52  ?  25  SER   A N     1 
ATOM   168  C CA    . SER   A 1 25  ? 13.552 -18.991 9.053   1.00 49.23  ?  25  SER   A CA    1 
ATOM   169  C C     . SER   A 1 25  ? 13.779 -18.531 7.624   1.00 49.79  ?  25  SER   A C     1 
ATOM   170  O O     . SER   A 1 25  ? 14.868 -18.060 7.276   1.00 48.74  ?  25  SER   A O     1 
ATOM   171  C CB    . SER   A 1 25  ? 13.161 -17.791 9.906   1.00 47.88  ?  25  SER   A CB    1 
ATOM   172  O OG    . SER   A 1 25  ? 14.061 -16.712 9.695   1.00 56.31  ?  25  SER   A OG    1 
ATOM   173  N N     . PHE   A 1 26  ? 12.724 -18.639 6.812   1.00 49.37  ?  26  PHE   A N     1 
ATOM   174  C CA    . PHE   A 1 26  ? 12.749 -18.300 5.392   1.00 52.81  ?  26  PHE   A CA    1 
ATOM   175  C C     . PHE   A 1 26  ? 11.321 -18.079 4.914   1.00 55.30  ?  26  PHE   A C     1 
ATOM   176  O O     . PHE   A 1 26  ? 10.358 -18.516 5.548   1.00 55.26  ?  26  PHE   A O     1 
ATOM   177  C CB    . PHE   A 1 26  ? 13.403 -19.403 4.538   1.00 45.66  ?  26  PHE   A CB    1 
ATOM   178  C CG    . PHE   A 1 26  ? 12.619 -20.692 4.509   1.00 46.81  ?  26  PHE   A CG    1 
ATOM   179  C CD1   . PHE   A 1 26  ? 11.552 -20.865 3.629   1.00 49.37  ?  26  PHE   A CD1   1 
ATOM   180  C CD2   . PHE   A 1 26  ? 12.947 -21.739 5.373   1.00 50.88  ?  26  PHE   A CD2   1 
ATOM   181  C CE1   . PHE   A 1 26  ? 10.814 -22.052 3.619   1.00 52.47  ?  26  PHE   A CE1   1 
ATOM   182  C CE2   . PHE   A 1 26  ? 12.224 -22.937 5.374   1.00 48.16  ?  26  PHE   A CE2   1 
ATOM   183  C CZ    . PHE   A 1 26  ? 11.153 -23.095 4.496   1.00 51.75  ?  26  PHE   A CZ    1 
ATOM   184  N N     . VAL   A 1 27  ? 11.198 -17.438 3.755   1.00 56.90  ?  27  VAL   A N     1 
ATOM   185  C CA    . VAL   A 1 27  ? 9.960  -17.477 2.988   1.00 60.20  ?  27  VAL   A CA    1 
ATOM   186  C C     . VAL   A 1 27  ? 10.260 -17.786 1.521   1.00 56.38  ?  27  VAL   A C     1 
ATOM   187  O O     . VAL   A 1 27  ? 11.365 -17.569 1.017   1.00 57.61  ?  27  VAL   A O     1 
ATOM   188  C CB    . VAL   A 1 27  ? 9.157  -16.168 3.099   1.00 58.76  ?  27  VAL   A CB    1 
ATOM   189  C CG1   . VAL   A 1 27  ? 8.355  -16.173 4.364   1.00 61.45  ?  27  VAL   A CG1   1 
ATOM   190  C CG2   . VAL   A 1 27  ? 10.093 -14.979 3.042   1.00 62.51  ?  27  VAL   A CG2   1 
ATOM   191  N N     . CYS   A 1 28  ? 9.248  -18.297 0.832   1.00 52.49  ?  28  CYS   A N     1 
ATOM   192  C CA    . CYS   A 1 28  ? 9.350  -18.557 -0.593  1.00 57.36  ?  28  CYS   A CA    1 
ATOM   193  C C     . CYS   A 1 28  ? 8.322  -17.721 -1.332  1.00 55.41  ?  28  CYS   A C     1 
ATOM   194  O O     . CYS   A 1 28  ? 7.117  -17.964 -1.208  1.00 56.79  ?  28  CYS   A O     1 
ATOM   195  C CB    . CYS   A 1 28  ? 9.158  -20.036 -0.903  1.00 56.65  ?  28  CYS   A CB    1 
ATOM   196  S SG    . CYS   A 1 28  ? 9.796  -20.430 -2.518  1.00 68.59  ?  28  CYS   A SG    1 
ATOM   197  N N     . LEU   A 1 29  ? 8.822  -16.845 -2.187  1.00 51.45  ?  29  LEU   A N     1 
ATOM   198  C CA    . LEU   A 1 29  ? 7.923  -16.020 -3.017  1.00 57.57  ?  29  LEU   A CA    1 
ATOM   199  C C     . LEU   A 1 29  ? 7.888  -16.577 -4.446  1.00 51.28  ?  29  LEU   A C     1 
ATOM   200  O O     . LEU   A 1 29  ? 8.963  -16.747 -5.026  1.00 47.59  ?  29  LEU   A O     1 
ATOM   201  C CB    . LEU   A 1 29  ? 8.448  -14.591 -2.959  1.00 55.64  ?  29  LEU   A CB    1 
ATOM   202  C CG    . LEU   A 1 29  ? 8.719  -14.017 -1.566  1.00 56.83  ?  29  LEU   A CG    1 
ATOM   203  C CD1   . LEU   A 1 29  ? 9.090  -12.552 -1.659  1.00 52.19  ?  29  LEU   A CD1   1 
ATOM   204  C CD2   . LEU   A 1 29  ? 7.525  -14.192 -0.656  1.00 54.18  ?  29  LEU   A CD2   1 
ATOM   205  N N     . GLU   A 1 30  ? 6.688  -16.854 -4.967  1.00 55.93  ?  30  GLU   A N     1 
ATOM   206  C CA    . GLU   A 1 30  ? 6.511  -17.343 -6.361  1.00 59.39  ?  30  GLU   A CA    1 
ATOM   207  C C     . GLU   A 1 30  ? 5.391  -16.555 -7.044  1.00 59.02  ?  30  GLU   A C     1 
ATOM   208  O O     . GLU   A 1 30  ? 4.432  -16.192 -6.357  1.00 56.60  ?  30  GLU   A O     1 
ATOM   209  C CB    . GLU   A 1 30  ? 6.180  -18.826 -6.492  1.00 57.77  ?  30  GLU   A CB    1 
ATOM   210  C CG    . GLU   A 1 30  ? 6.834  -19.450 -7.718  1.00 55.36  ?  30  GLU   A CG    1 
ATOM   211  C CD    . GLU   A 1 30  ? 5.835  -20.350 -8.399  1.00 62.23  ?  30  GLU   A CD    1 
ATOM   212  O OE1   . GLU   A 1 30  ? 4.640  -20.123 -8.156  1.00 70.35  ?  30  GLU   A OE1   1 
ATOM   213  O OE2   . GLU   A 1 30  ? 6.231  -21.270 -9.133  1.00 63.04  ?  30  GLU   A OE2   1 
ATOM   214  N N     . LYS   A 1 31  ? 5.492  -16.363 -8.359  1.00 60.99  ?  31  LYS   A N     1 
ATOM   215  C CA    . LYS   A 1 31  ? 4.525  -15.509 -9.092  1.00 60.99  ?  31  LYS   A CA    1 
ATOM   216  C C     . LYS   A 1 31  ? 3.322  -16.313 -9.580  1.00 57.20  ?  31  LYS   A C     1 
ATOM   217  O O     . LYS   A 1 31  ? 2.283  -15.704 -9.857  1.00 55.34  ?  31  LYS   A O     1 
ATOM   218  C CB    . LYS   A 1 31  ? 5.262  -14.920 -10.294 1.00 56.28  ?  31  LYS   A CB    1 
ATOM   219  C CG    . LYS   A 1 31  ? 6.054  -15.880 -11.150 1.00 58.41  ?  31  LYS   A CG    1 
ATOM   220  C CD    . LYS   A 1 31  ? 6.839  -15.132 -12.219 1.00 64.93  ?  31  LYS   A CD    1 
ATOM   221  C CE    . LYS   A 1 31  ? 7.024  -15.932 -13.464 1.00 66.68  ?  31  LYS   A CE    1 
ATOM   222  N NZ    . LYS   A 1 31  ? 7.348  -15.076 -14.606 1.00 69.61  ?  31  LYS   A NZ    1 
ATOM   223  N N     . ALA   A 1 32  ? 3.466  -17.624 -9.664  1.00 55.19  ?  32  ALA   A N     1 
ATOM   224  C CA    . ALA   A 1 32  ? 2.389  -18.466 -10.219 1.00 55.40  ?  32  ALA   A CA    1 
ATOM   225  C C     . ALA   A 1 32  ? 1.372  -18.817 -9.138  1.00 58.99  ?  32  ALA   A C     1 
ATOM   226  O O     . ALA   A 1 32  ? 1.664  -18.643 -7.947  1.00 55.51  ?  32  ALA   A O     1 
ATOM   227  C CB    . ALA   A 1 32  ? 3.013  -19.696 -10.814 1.00 49.35  ?  32  ALA   A CB    1 
ATOM   228  N N     . PRO   A 1 33  ? 0.171  -19.290 -9.519  1.00 58.21  ?  33  PRO   A N     1 
ATOM   229  C CA    . PRO   A 1 33  ? -0.822 -19.710 -8.538  1.00 58.95  ?  33  PRO   A CA    1 
ATOM   230  C C     . PRO   A 1 33  ? -0.587 -20.994 -7.724  1.00 59.01  ?  33  PRO   A C     1 
ATOM   231  O O     . PRO   A 1 33  ? -1.407 -21.282 -6.844  1.00 51.93  ?  33  PRO   A O     1 
ATOM   232  C CB    . PRO   A 1 33  ? -2.018 -19.822 -9.477  1.00 59.85  ?  33  PRO   A CB    1 
ATOM   233  C CG    . PRO   A 1 33  ? -1.439 -20.308 -10.768 1.00 59.70  ?  33  PRO   A CG    1 
ATOM   234  C CD    . PRO   A 1 33  ? -0.293 -19.349 -10.894 1.00 57.44  ?  33  PRO   A CD    1 
ATOM   235  N N     . ASP   A 1 34  ? 0.484  -21.737 -8.009  1.00 56.81  ?  34  ASP   A N     1 
ATOM   236  C CA    . ASP   A 1 34  ? 0.828  -22.933 -7.194  1.00 48.46  ?  34  ASP   A CA    1 
ATOM   237  C C     . ASP   A 1 34  ? 2.300  -23.279 -7.363  1.00 48.41  ?  34  ASP   A C     1 
ATOM   238  O O     . ASP   A 1 34  ? 3.002  -22.544 -8.054  1.00 53.66  ?  34  ASP   A O     1 
ATOM   239  C CB    . ASP   A 1 34  ? -0.033 -24.146 -7.498  1.00 52.32  ?  34  ASP   A CB    1 
ATOM   240  C CG    . ASP   A 1 34  ? -0.312 -25.097 -6.345  1.00 55.48  ?  34  ASP   A CG    1 
ATOM   241  O OD1   . ASP   A 1 34  ? 0.645  -25.465 -5.644  1.00 52.08  ?  34  ASP   A OD1   1 
ATOM   242  O OD2   . ASP   A 1 34  ? -1.483 -25.477 -6.177  1.00 58.02  ?  34  ASP   A OD2   1 
ATOM   243  N N     . VAL   A 1 35  ? 2.726  -24.369 -6.747  1.00 51.20  ?  35  VAL   A N     1 
ATOM   244  C CA    . VAL   A 1 35  ? 4.121  -24.794 -6.767  1.00 51.01  ?  35  VAL   A CA    1 
ATOM   245  C C     . VAL   A 1 35  ? 4.334  -25.704 -7.970  1.00 56.58  ?  35  VAL   A C     1 
ATOM   246  O O     . VAL   A 1 35  ? 3.386  -26.234 -8.563  1.00 55.37  ?  35  VAL   A O     1 
ATOM   247  C CB    . VAL   A 1 35  ? 4.537  -25.496 -5.447  1.00 56.03  ?  35  VAL   A CB    1 
ATOM   248  C CG1   . VAL   A 1 35  ? 4.050  -24.708 -4.227  1.00 52.67  ?  35  VAL   A CG1   1 
ATOM   249  C CG2   . VAL   A 1 35  ? 4.039  -26.939 -5.391  1.00 54.63  ?  35  VAL   A CG2   1 
ATOM   250  N N     . GLY   A 1 36  ? 5.595  -25.870 -8.361  1.00 58.14  ?  36  GLY   A N     1 
ATOM   251  C CA    . GLY   A 1 36  ? 5.890  -26.795 -9.445  1.00 51.77  ?  36  GLY   A CA    1 
ATOM   252  C C     . GLY   A 1 36  ? 6.822  -26.298 -10.532 1.00 44.40  ?  36  GLY   A C     1 
ATOM   253  O O     . GLY   A 1 36  ? 7.420  -27.108 -11.240 1.00 46.80  ?  36  GLY   A O     1 
ATOM   254  N N     . GLY   A 1 37  ? 6.961  -24.985 -10.681 1.00 46.45  ?  37  GLY   A N     1 
ATOM   255  C CA    . GLY   A 1 37  ? 7.836  -24.485 -11.726 1.00 52.32  ?  37  GLY   A CA    1 
ATOM   256  C C     . GLY   A 1 37  ? 7.187  -24.599 -13.097 1.00 55.69  ?  37  GLY   A C     1 
ATOM   257  O O     . GLY   A 1 37  ? 6.002  -24.289 -13.294 1.00 56.50  ?  37  GLY   A O     1 
ATOM   258  N N     . ILE   A 1 38  ? 7.975  -25.057 -14.068 1.00 49.59  ?  38  ILE   A N     1 
ATOM   259  C CA    . ILE   A 1 38  ? 7.433  -25.164 -15.415 1.00 51.62  ?  38  ILE   A CA    1 
ATOM   260  C C     . ILE   A 1 38  ? 6.403  -26.284 -15.486 1.00 54.14  ?  38  ILE   A C     1 
ATOM   261  O O     . ILE   A 1 38  ? 5.445  -26.206 -16.270 1.00 55.63  ?  38  ILE   A O     1 
ATOM   262  C CB    . ILE   A 1 38  ? 8.570  -25.348 -16.440 1.00 50.42  ?  38  ILE   A CB    1 
ATOM   263  C CG1   . ILE   A 1 38  ? 9.310  -26.665 -16.180 1.00 47.10  ?  38  ILE   A CG1   1 
ATOM   264  C CG2   . ILE   A 1 38  ? 9.514  -24.142 -16.412 1.00 45.80  ?  38  ILE   A CG2   1 
ATOM   265  C CD1   . ILE   A 1 38  ? 10.707 -26.731 -16.768 1.00 48.34  ?  38  ILE   A CD1   1 
ATOM   266  N N     . TRP   A 1 39  ? 6.543  -27.316 -14.643 1.00 50.78  ?  39  TRP   A N     1 
ATOM   267  C CA    . TRP   A 1 39  ? 5.698  -28.506 -14.754 1.00 46.89  ?  39  TRP   A CA    1 
ATOM   268  C C     . TRP   A 1 39  ? 4.242  -28.242 -14.389 1.00 50.82  ?  39  TRP   A C     1 
ATOM   269  O O     . TRP   A 1 39  ? 3.385  -29.085 -14.677 1.00 52.20  ?  39  TRP   A O     1 
ATOM   270  C CB    . TRP   A 1 39  ? 6.270  -29.634 -13.898 1.00 41.96  ?  39  TRP   A CB    1 
ATOM   271  C CG    . TRP   A 1 39  ? 7.679  -29.996 -14.288 1.00 46.44  ?  39  TRP   A CG    1 
ATOM   272  C CD1   . TRP   A 1 39  ? 8.828  -29.402 -13.859 1.00 45.00  ?  39  TRP   A CD1   1 
ATOM   273  C CD2   . TRP   A 1 39  ? 8.084  -31.018 -15.211 1.00 53.72  ?  39  TRP   A CD2   1 
ATOM   274  N NE1   . TRP   A 1 39  ? 9.923  -29.995 -14.433 1.00 42.21  ?  39  TRP   A NE1   1 
ATOM   275  C CE2   . TRP   A 1 39  ? 9.496  -30.988 -15.274 1.00 53.00  ?  39  TRP   A CE2   1 
ATOM   276  C CE3   . TRP   A 1 39  ? 7.388  -31.954 -15.999 1.00 53.17  ?  39  TRP   A CE3   1 
ATOM   277  C CZ2   . TRP   A 1 39  ? 10.229 -31.857 -16.092 1.00 61.00  ?  39  TRP   A CZ2   1 
ATOM   278  C CZ3   . TRP   A 1 39  ? 8.116  -32.821 -16.810 1.00 54.43  ?  39  TRP   A CZ3   1 
ATOM   279  C CH2   . TRP   A 1 39  ? 9.525  -32.768 -16.847 1.00 57.30  ?  39  TRP   A CH2   1 
ATOM   280  N N     . ARG   A 1 40  ? 3.947  -27.097 -13.775 1.00 53.69  ?  40  ARG   A N     1 
ATOM   281  C CA    . ARG   A 1 40  ? 2.574  -26.698 -13.515 1.00 52.66  ?  40  ARG   A CA    1 
ATOM   282  C C     . ARG   A 1 40  ? 1.887  -26.171 -14.777 1.00 56.63  ?  40  ARG   A C     1 
ATOM   283  O O     . ARG   A 1 40  ? 0.666  -26.303 -14.910 1.00 55.15  ?  40  ARG   A O     1 
ATOM   284  C CB    . ARG   A 1 40  ? 2.564  -25.631 -12.412 1.00 47.41  ?  40  ARG   A CB    1 
ATOM   285  C CG    . ARG   A 1 40  ? 1.265  -25.499 -11.605 1.00 46.93  ?  40  ARG   A CG    1 
ATOM   286  C CD    . ARG   A 1 40  ? 1.212  -24.167 -10.929 1.00 43.26  ?  40  ARG   A CD    1 
ATOM   287  N NE    . ARG   A 1 40  ? 1.573  -23.170 -11.909 1.00 54.13  ?  40  ARG   A NE    1 
ATOM   288  C CZ    . ARG   A 1 40  ? 0.716  -22.673 -12.792 1.00 58.48  ?  40  ARG   A CZ    1 
ATOM   289  N NH1   . ARG   A 1 40  ? -0.548 -23.071 -12.771 1.00 57.25  ?  40  ARG   A NH1   1 
ATOM   290  N NH2   . ARG   A 1 40  ? 1.120  -21.781 -13.688 1.00 57.94  ?  40  ARG   A NH2   1 
ATOM   291  N N     . GLN   A 1 41  ? 2.653  -25.611 -15.727 1.00 49.12  ?  41  GLN   A N     1 
ATOM   292  C CA    . GLN   A 1 41  ? 2.060  -24.688 -16.696 1.00 56.82  ?  41  GLN   A CA    1 
ATOM   293  C C     . GLN   A 1 41  ? 1.187  -25.356 -17.763 1.00 63.37  ?  41  GLN   A C     1 
ATOM   294  O O     . GLN   A 1 41  ? 0.066  -24.868 -18.000 1.00 61.96  ?  41  GLN   A O     1 
ATOM   295  C CB    . GLN   A 1 41  ? 3.166  -23.842 -17.328 1.00 60.20  ?  41  GLN   A CB    1 
ATOM   296  C CG    . GLN   A 1 41  ? 4.151  -23.272 -16.339 1.00 55.13  ?  41  GLN   A CG    1 
ATOM   297  C CD    . GLN   A 1 41  ? 4.873  -22.070 -16.891 1.00 57.81  ?  41  GLN   A CD    1 
ATOM   298  O OE1   . GLN   A 1 41  ? 5.979  -22.184 -17.424 1.00 55.22  ?  41  GLN   A OE1   1 
ATOM   299  N NE2   . GLN   A 1 41  ? 4.241  -20.904 -16.785 1.00 58.61  ?  41  GLN   A NE2   1 
ATOM   300  N N     . PRO   A 1 42  ? 1.618  -26.412 -18.470 1.00 61.43  ?  42  PRO   A N     1 
ATOM   301  C CA    . PRO   A 1 42  ? 0.773  -26.917 -19.566 1.00 60.96  ?  42  PRO   A CA    1 
ATOM   302  C C     . PRO   A 1 42  ? -0.490 -27.617 -19.088 1.00 62.10  ?  42  PRO   A C     1 
ATOM   303  O O     . PRO   A 1 42  ? -1.516 -27.563 -19.778 1.00 55.72  ?  42  PRO   A O     1 
ATOM   304  C CB    . PRO   A 1 42  ? 1.708  -27.871 -20.326 1.00 54.86  ?  42  PRO   A CB    1 
ATOM   305  C CG    . PRO   A 1 42  ? 2.653  -28.330 -19.329 1.00 55.35  ?  42  PRO   A CG    1 
ATOM   306  C CD    . PRO   A 1 42  ? 2.888  -27.157 -18.402 1.00 59.91  ?  42  PRO   A CD    1 
ATOM   307  N N     . GLY   A 1 43  ? -0.465 -28.253 -17.918 1.00 62.15  ?  43  GLY   A N     1 
ATOM   308  C CA    . GLY   A 1 43  ? -1.693 -28.740 -17.322 1.00 62.43  ?  43  GLY   A CA    1 
ATOM   309  C C     . GLY   A 1 43  ? -2.651 -27.607 -16.991 1.00 65.12  ?  43  GLY   A C     1 
ATOM   310  O O     . GLY   A 1 43  ? -3.783 -27.840 -16.555 1.00 68.61  ?  43  GLY   A O     1 
ATOM   311  N N     . ALA   A 1 44  ? -2.247 -26.378 -17.279 1.00 65.34  ?  44  ALA   A N     1 
ATOM   312  C CA    . ALA   A 1 44  ? -3.101 -25.224 -16.931 1.00 65.62  ?  44  ALA   A CA    1 
ATOM   313  C C     . ALA   A 1 44  ? -3.128 -24.216 -18.073 1.00 72.57  ?  44  ALA   A C     1 
ATOM   314  O O     . ALA   A 1 44  ? -3.555 -23.073 -17.853 1.00 76.63  ?  44  ALA   A O     1 
ATOM   315  C CB    . ALA   A 1 44  ? -2.592 -24.596 -15.673 1.00 69.95  ?  44  ALA   A CB    1 
ATOM   316  N N     . GLY   A 1 45  ? -2.673 -24.623 -19.252 1.00 71.23  ?  45  GLY   A N     1 
ATOM   317  C CA    . GLY   A 1 45  ? -2.745 -23.740 -20.425 1.00 69.72  ?  45  GLY   A CA    1 
ATOM   318  C C     . GLY   A 1 45  ? -1.938 -22.479 -20.247 1.00 74.18  ?  45  GLY   A C     1 
ATOM   319  O O     . GLY   A 1 45  ? -2.283 -21.465 -20.866 1.00 82.46  ?  45  GLY   A O     1 
ATOM   320  N N     . GLU   A 1 46  ? -0.884 -22.534 -19.446 1.00 72.47  ?  46  GLU   A N     1 
ATOM   321  C CA    . GLU   A 1 46  ? -0.117 -21.297 -19.178 1.00 72.72  ?  46  GLU   A CA    1 
ATOM   322  C C     . GLU   A 1 46  ? 1.032  -21.181 -20.184 1.00 66.17  ?  46  GLU   A C     1 
ATOM   323  O O     . GLU   A 1 46  ? 1.606  -22.211 -20.560 1.00 66.70  ?  46  GLU   A O     1 
ATOM   324  C CB    . GLU   A 1 46  ? 0.381  -21.278 -17.738 1.00 68.49  ?  46  GLU   A CB    1 
ATOM   325  C CG    . GLU   A 1 46  ? -0.686 -21.695 -16.732 1.00 74.87  ?  46  GLU   A CG    1 
ATOM   326  C CD    . GLU   A 1 46  ? -0.940 -20.658 -15.658 1.00 75.90  ?  46  GLU   A CD    1 
ATOM   327  O OE1   . GLU   A 1 46  ? 0.023  -19.958 -15.290 1.00 70.17  ?  46  GLU   A OE1   1 
ATOM   328  O OE2   . GLU   A 1 46  ? -2.089 -20.557 -15.187 1.00 73.77  ?  46  GLU   A OE2   1 
ATOM   329  N N     . ARG   A 1 47  ? 1.340  -19.958 -20.592 1.00 63.39  ?  47  ARG   A N     1 
ATOM   330  C CA    . ARG   A 1 47  ? 2.449  -19.722 -21.538 1.00 66.82  ?  47  ARG   A CA    1 
ATOM   331  C C     . ARG   A 1 47  ? 3.760  -20.118 -20.869 1.00 64.25  ?  47  ARG   A C     1 
ATOM   332  O O     . ARG   A 1 47  ? 4.103  -19.512 -19.847 1.00 70.60  ?  47  ARG   A O     1 
ATOM   333  C CB    . ARG   A 1 47  ? 2.506  -18.235 -21.887 1.00 68.13  ?  47  ARG   A CB    1 
ATOM   334  C CG    . ARG   A 1 47  ? 2.292  -17.903 -23.356 1.00 71.22  ?  47  ARG   A CG    1 
ATOM   335  C CD    . ARG   A 1 47  ? 2.153  -16.404 -23.549 1.00 73.39  ?  47  ARG   A CD    1 
ATOM   336  N NE    . ARG   A 1 47  ? 3.370  -15.794 -24.095 1.00 75.57  ?  47  ARG   A NE    1 
ATOM   337  C CZ    . ARG   A 1 47  ? 4.231  -15.075 -23.389 1.00 76.30  ?  47  ARG   A CZ    1 
ATOM   338  N NH1   . ARG   A 1 47  ? 5.219  -14.444 -23.995 1.00 65.65  ?  47  ARG   A NH1   1 
ATOM   339  N NH2   . ARG   A 1 47  ? 4.107  -14.999 -22.078 1.00 77.63  ?  47  ARG   A NH2   1 
ATOM   340  N N     . GLY   A 1 48  ? 4.464  -21.083 -21.444 1.00 61.61  ?  48  GLY   A N     1 
ATOM   341  C CA    . GLY   A 1 48  ? 5.762  -21.466 -20.880 1.00 59.66  ?  48  GLY   A CA    1 
ATOM   342  C C     . GLY   A 1 48  ? 6.555  -22.369 -21.781 1.00 55.84  ?  48  GLY   A C     1 
ATOM   343  O O     . GLY   A 1 48  ? 6.056  -22.763 -22.838 1.00 60.20  ?  48  GLY   A O     1 
ATOM   344  N N     . PRO   A 1 49  ? 7.783  -22.722 -21.378 1.00 56.23  ?  49  PRO   A N     1 
ATOM   345  C CA    . PRO   A 1 49  ? 8.618  -23.583 -22.192 1.00 53.77  ?  49  PRO   A CA    1 
ATOM   346  C C     . PRO   A 1 49  ? 8.000  -24.916 -22.567 1.00 51.69  ?  49  PRO   A C     1 
ATOM   347  O O     . PRO   A 1 49  ? 8.409  -25.499 -23.571 1.00 53.98  ?  49  PRO   A O     1 
ATOM   348  C CB    . PRO   A 1 49  ? 9.770  -23.745 -21.213 1.00 52.20  ?  49  PRO   A CB    1 
ATOM   349  C CG    . PRO   A 1 49  ? 9.836  -22.440 -20.485 1.00 56.30  ?  49  PRO   A CG    1 
ATOM   350  C CD    . PRO   A 1 49  ? 8.384  -22.267 -20.146 1.00 55.86  ?  49  PRO   A CD    1 
ATOM   351  N N     . GLY   A 1 50  ? 7.009  -25.372 -21.816 1.00 50.76  ?  50  GLY   A N     1 
ATOM   352  C CA    . GLY   A 1 50  ? 6.466  -26.692 -22.034 1.00 50.50  ?  50  GLY   A CA    1 
ATOM   353  C C     . GLY   A 1 50  ? 5.259  -26.717 -22.955 1.00 51.48  ?  50  GLY   A C     1 
ATOM   354  O O     . GLY   A 1 50  ? 4.841  -25.716 -23.542 1.00 51.52  ?  50  GLY   A O     1 
ATOM   355  N N     . TYR   A 1 51  ? 4.683  -27.911 -23.057 1.00 46.45  ?  51  TYR   A N     1 
ATOM   356  C CA    . TYR   A 1 51  ? 3.619  -28.180 -24.008 1.00 48.25  ?  51  TYR   A CA    1 
ATOM   357  C C     . TYR   A 1 51  ? 2.859  -29.411 -23.548 1.00 52.47  ?  51  TYR   A C     1 
ATOM   358  O O     . TYR   A 1 51  ? 3.373  -30.230 -22.780 1.00 48.79  ?  51  TYR   A O     1 
ATOM   359  C CB    . TYR   A 1 51  ? 4.182  -28.391 -25.410 1.00 49.95  ?  51  TYR   A CB    1 
ATOM   360  C CG    . TYR   A 1 51  ? 5.559  -29.025 -25.408 1.00 47.51  ?  51  TYR   A CG    1 
ATOM   361  C CD1   . TYR   A 1 51  ? 5.715  -30.408 -25.352 1.00 45.08  ?  51  TYR   A CD1   1 
ATOM   362  C CD2   . TYR   A 1 51  ? 6.702  -28.234 -25.454 1.00 47.05  ?  51  TYR   A CD2   1 
ATOM   363  C CE1   . TYR   A 1 51  ? 6.970  -30.978 -25.348 1.00 43.97  ?  51  TYR   A CE1   1 
ATOM   364  C CE2   . TYR   A 1 51  ? 7.960  -28.795 -25.446 1.00 47.05  ?  51  TYR   A CE2   1 
ATOM   365  C CZ    . TYR   A 1 51  ? 8.094  -30.162 -25.391 1.00 42.97  ?  51  TYR   A CZ    1 
ATOM   366  O OH    . TYR   A 1 51  ? 9.357  -30.697 -25.394 1.00 38.83  ?  51  TYR   A OH    1 
ATOM   367  N N     . ARG   A 1 52  ? 1.646  -29.555 -24.067 1.00 52.52  ?  52  ARG   A N     1 
ATOM   368  C CA    . ARG   A 1 52  ? 0.739  -30.550 -23.510 1.00 56.43  ?  52  ARG   A CA    1 
ATOM   369  C C     . ARG   A 1 52  ? 1.166  -31.996 -23.785 1.00 55.54  ?  52  ARG   A C     1 
ATOM   370  O O     . ARG   A 1 52  ? 0.406  -32.900 -23.397 1.00 59.81  ?  52  ARG   A O     1 
ATOM   371  C CB    . ARG   A 1 52  ? -0.678 -30.303 -24.029 1.00 63.06  ?  52  ARG   A CB    1 
ATOM   372  C CG    . ARG   A 1 52  ? -1.785 -30.668 -23.018 1.00 70.17  ?  52  ARG   A CG    1 
ATOM   373  C CD    . ARG   A 1 52  ? -3.117 -30.921 -23.728 1.00 79.85  ?  52  ARG   A CD    1 
ATOM   374  N NE    . ARG   A 1 52  ? -2.914 -31.537 -25.040 1.00 73.66  ?  52  ARG   A NE    1 
ATOM   375  C CZ    . ARG   A 1 52  ? -3.110 -32.825 -25.310 1.00 74.59  ?  52  ARG   A CZ    1 
ATOM   376  N NH1   . ARG   A 1 52  ? -3.540 -33.664 -24.370 1.00 68.78  ?  52  ARG   A NH1   1 
ATOM   377  N NH2   . ARG   A 1 52  ? -2.882 -33.270 -26.538 1.00 82.41  ?  52  ARG   A NH2   1 
ATOM   378  N N     . THR   A 1 53  ? 2.316  -32.253 -24.407 1.00 49.81  ?  53  THR   A N     1 
ATOM   379  C CA    . THR   A 1 53  ? 2.793  -33.609 -24.668 1.00 52.26  ?  53  THR   A CA    1 
ATOM   380  C C     . THR   A 1 53  ? 4.130  -33.884 -23.993 1.00 51.99  ?  53  THR   A C     1 
ATOM   381  O O     . THR   A 1 53  ? 4.774  -34.898 -24.296 1.00 50.86  ?  53  THR   A O     1 
ATOM   382  C CB    . THR   A 1 53  ? 2.925  -33.870 -26.187 1.00 57.95  ?  53  THR   A CB    1 
ATOM   383  O OG1   . THR   A 1 53  ? 4.114  -33.247 -26.712 1.00 50.91  ?  53  THR   A OG1   1 
ATOM   384  C CG2   . THR   A 1 53  ? 1.715  -33.336 -26.946 1.00 49.78  ?  53  THR   A CG2   1 
ATOM   385  N N     . LEU   A 1 54  ? 4.575  -33.006 -23.098 1.00 54.10  ?  54  LEU   A N     1 
ATOM   386  C CA    . LEU   A 1 54  ? 5.928  -33.129 -22.573 1.00 50.99  ?  54  LEU   A CA    1 
ATOM   387  C C     . LEU   A 1 54  ? 5.995  -34.182 -21.472 1.00 47.89  ?  54  LEU   A C     1 
ATOM   388  O O     . LEU   A 1 54  ? 5.068  -34.330 -20.671 1.00 41.83  ?  54  LEU   A O     1 
ATOM   389  C CB    . LEU   A 1 54  ? 6.423  -31.779 -22.068 1.00 46.68  ?  54  LEU   A CB    1 
ATOM   390  C CG    . LEU   A 1 54  ? 7.767  -31.729 -21.359 1.00 42.12  ?  54  LEU   A CG    1 
ATOM   391  C CD1   . LEU   A 1 54  ? 8.857  -31.522 -22.335 1.00 48.81  ?  54  LEU   A CD1   1 
ATOM   392  C CD2   . LEU   A 1 54  ? 7.719  -30.562 -20.447 1.00 44.28  ?  54  LEU   A CD2   1 
ATOM   393  N N     . HIS   A 1 55  ? 7.096  -34.937 -21.482 1.00 48.15  ?  55  HIS   A N     1 
ATOM   394  C CA    . HIS   A 1 55  ? 7.412  -35.959 -20.506 1.00 42.87  ?  55  HIS   A CA    1 
ATOM   395  C C     . HIS   A 1 55  ? 8.842  -35.759 -20.033 1.00 46.39  ?  55  HIS   A C     1 
ATOM   396  O O     . HIS   A 1 55  ? 9.606  -34.959 -20.584 1.00 49.32  ?  55  HIS   A O     1 
ATOM   397  C CB    . HIS   A 1 55  ? 7.291  -37.358 -21.095 1.00 40.93  ?  55  HIS   A CB    1 
ATOM   398  C CG    . HIS   A 1 55  ? 5.896  -37.873 -21.152 1.00 45.23  ?  55  HIS   A CG    1 
ATOM   399  N ND1   . HIS   A 1 55  ? 5.549  -39.134 -20.713 1.00 44.13  ?  55  HIS   A ND1   1 
ATOM   400  C CD2   . HIS   A 1 55  ? 4.755  -37.294 -21.587 1.00 45.37  ?  55  HIS   A CD2   1 
ATOM   401  C CE1   . HIS   A 1 55  ? 4.252  -39.310 -20.882 1.00 43.28  ?  55  HIS   A CE1   1 
ATOM   402  N NE2   . HIS   A 1 55  ? 3.748  -38.211 -21.417 1.00 43.54  ?  55  HIS   A NE2   1 
ATOM   403  N N     . LEU   A 1 56  ? 9.198  -36.518 -19.006 1.00 47.08  ?  56  LEU   A N     1 
ATOM   404  C CA    . LEU   A 1 56  ? 10.578 -36.592 -18.559 1.00 47.10  ?  56  LEU   A CA    1 
ATOM   405  C C     . LEU   A 1 56  ? 11.415 -37.369 -19.565 1.00 52.31  ?  56  LEU   A C     1 
ATOM   406  O O     . LEU   A 1 56  ? 10.962 -38.368 -20.134 1.00 46.51  ?  56  LEU   A O     1 
ATOM   407  C CB    . LEU   A 1 56  ? 10.657 -37.278 -17.196 1.00 49.78  ?  56  LEU   A CB    1 
ATOM   408  C CG    . LEU   A 1 56  ? 10.432 -36.442 -15.934 1.00 51.93  ?  56  LEU   A CG    1 
ATOM   409  C CD1   . LEU   A 1 56  ? 10.262 -37.371 -14.747 1.00 40.91  ?  56  LEU   A CD1   1 
ATOM   410  C CD2   . LEU   A 1 56  ? 11.588 -35.471 -15.731 1.00 48.93  ?  56  LEU   A CD2   1 
ATOM   411  N N     . ALA   A 1 57  ? 12.646 -36.912 -19.777 1.00 52.46  ?  57  ALA   A N     1 
ATOM   412  C CA    . ALA   A 1 57  ? 13.612 -37.673 -20.549 1.00 51.20  ?  57  ALA   A CA    1 
ATOM   413  C C     . ALA   A 1 57  ? 14.576 -38.455 -19.666 1.00 54.82  ?  57  ALA   A C     1 
ATOM   414  O O     . ALA   A 1 57  ? 15.382 -39.230 -20.197 1.00 54.83  ?  57  ALA   A O     1 
ATOM   415  C CB    . ALA   A 1 57  ? 14.391 -36.747 -21.487 1.00 51.06  ?  57  ALA   A CB    1 
ATOM   416  N N     . THR   A 1 58  ? 14.506 -38.276 -18.341 1.00 52.49  ?  58  THR   A N     1 
ATOM   417  C CA    . THR   A 1 58  ? 15.354 -38.952 -17.361 1.00 51.80  ?  58  THR   A CA    1 
ATOM   418  C C     . THR   A 1 58  ? 14.551 -39.950 -16.527 1.00 51.67  ?  58  THR   A C     1 
ATOM   419  O O     . THR   A 1 58  ? 13.359 -39.750 -16.280 1.00 52.31  ?  58  THR   A O     1 
ATOM   420  C CB    . THR   A 1 58  ? 16.014 -37.931 -16.435 1.00 55.98  ?  58  THR   A CB    1 
ATOM   421  O OG1   . THR   A 1 58  ? 14.994 -37.177 -15.757 1.00 51.52  ?  58  THR   A OG1   1 
ATOM   422  C CG2   . THR   A 1 58  ? 16.937 -36.988 -17.238 1.00 51.34  ?  58  THR   A CG2   1 
ATOM   423  N N     . ALA   A 1 59  ? 15.215 -41.023 -16.079 1.00 52.30  ?  59  ALA   A N     1 
ATOM   424  C CA    . ALA   A 1 59  ? 14.535 -42.077 -15.319 1.00 51.65  ?  59  ALA   A CA    1 
ATOM   425  C C     . ALA   A 1 59  ? 13.973 -41.547 -14.005 1.00 48.20  ?  59  ALA   A C     1 
ATOM   426  O O     . ALA   A 1 59  ? 14.605 -40.736 -13.326 1.00 48.89  ?  59  ALA   A O     1 
ATOM   427  C CB    . ALA   A 1 59  ? 15.491 -43.233 -15.029 1.00 52.39  ?  59  ALA   A CB    1 
ATOM   428  N N     . LYS   A 1 60  ? 12.789 -42.044 -13.633 1.00 49.03  ?  60  LYS   A N     1 
ATOM   429  C CA    . LYS   A 1 60  ? 12.065 -41.498 -12.480 1.00 51.59  ?  60  LYS   A CA    1 
ATOM   430  C C     . LYS   A 1 60  ? 12.862 -41.650 -11.185 1.00 50.75  ?  60  LYS   A C     1 
ATOM   431  O O     . LYS   A 1 60  ? 12.998 -40.693 -10.413 1.00 51.18  ?  60  LYS   A O     1 
ATOM   432  C CB    . LYS   A 1 60  ? 10.679 -42.149 -12.354 1.00 44.80  ?  60  LYS   A CB    1 
ATOM   433  C CG    . LYS   A 1 60  ? 10.672 -43.631 -11.981 1.00 50.65  ?  60  LYS   A CG    1 
ATOM   434  C CD    . LYS   A 1 60  ? 9.406  -44.031 -11.203 1.00 49.10  ?  60  LYS   A CD    1 
ATOM   435  C CE    . LYS   A 1 60  ? 9.289  -45.546 -11.053 1.00 46.73  ?  60  LYS   A CE    1 
ATOM   436  N NZ    . LYS   A 1 60  ? 7.939  -45.967 -10.588 1.00 45.66  ?  60  LYS   A NZ    1 
ATOM   437  N N     . GLN   A 1 61  ? 13.427 -42.837 -10.947 1.00 48.88  ?  61  GLN   A N     1 
ATOM   438  C CA    . GLN   A 1 61  ? 14.182 -43.076 -9.723  1.00 48.57  ?  61  GLN   A CA    1 
ATOM   439  C C     . GLN   A 1 61  ? 15.386 -42.146 -9.594  1.00 53.88  ?  61  GLN   A C     1 
ATOM   440  O O     . GLN   A 1 61  ? 15.777 -41.796 -8.473  1.00 53.26  ?  61  GLN   A O     1 
ATOM   441  C CB    . GLN   A 1 61  ? 14.637 -44.530 -9.681  1.00 45.25  ?  61  GLN   A CB    1 
ATOM   442  C CG    . GLN   A 1 61  ? 15.746 -44.844 -10.666 1.00 52.59  ?  61  GLN   A CG    1 
ATOM   443  C CD    . GLN   A 1 61  ? 15.239 -45.221 -12.056 1.00 57.08  ?  61  GLN   A CD    1 
ATOM   444  O OE1   . GLN   A 1 61  ? 14.091 -44.937 -12.422 1.00 56.45  ?  61  GLN   A OE1   1 
ATOM   445  N NE2   . GLN   A 1 61  ? 16.093 -45.891 -12.826 1.00 55.76  ?  61  GLN   A NE2   1 
ATOM   446  N N     . LEU   A 1 62  ? 15.994 -41.744 -10.716 1.00 54.60  ?  62  LEU   A N     1 
ATOM   447  C CA    . LEU   A 1 62  ? 17.128 -40.823 -10.711 1.00 54.52  ?  62  LEU   A CA    1 
ATOM   448  C C     . LEU   A 1 62  ? 16.696 -39.371 -10.710 1.00 48.89  ?  62  LEU   A C     1 
ATOM   449  O O     . LEU   A 1 62  ? 17.547 -38.478 -10.739 1.00 49.62  ?  62  LEU   A O     1 
ATOM   450  C CB    . LEU   A 1 62  ? 18.034 -41.050 -11.927 1.00 53.55  ?  62  LEU   A CB    1 
ATOM   451  C CG    . LEU   A 1 62  ? 18.425 -42.449 -12.414 1.00 58.66  ?  62  LEU   A CG    1 
ATOM   452  C CD1   . LEU   A 1 62  ? 19.427 -42.338 -13.570 1.00 58.08  ?  62  LEU   A CD1   1 
ATOM   453  C CD2   . LEU   A 1 62  ? 18.991 -43.266 -11.273 1.00 57.04  ?  62  LEU   A CD2   1 
ATOM   454  N N     . THR   A 1 63  ? 15.413 -39.111 -10.709 1.00 42.64  ?  63  THR   A N     1 
ATOM   455  C CA    . THR   A 1 63  ? 14.941 -37.749 -10.819 1.00 45.98  ?  63  THR   A CA    1 
ATOM   456  C C     . THR   A 1 63  ? 14.157 -37.303 -9.605  1.00 47.62  ?  63  THR   A C     1 
ATOM   457  O O     . THR   A 1 63  ? 14.143 -36.107 -9.310  1.00 44.04  ?  63  THR   A O     1 
ATOM   458  C CB    . THR   A 1 63  ? 14.063 -37.585 -12.076 1.00 50.43  ?  63  THR   A CB    1 
ATOM   459  O OG1   . THR   A 1 63  ? 14.573 -38.407 -13.134 1.00 54.11  ?  63  THR   A OG1   1 
ATOM   460  C CG2   . THR   A 1 63  ? 14.066 -36.149 -12.541 1.00 48.81  ?  63  THR   A CG2   1 
ATOM   461  N N     . GLY   A 1 64  ? 13.524 -38.233 -8.887  1.00 44.37  ?  64  GLY   A N     1 
ATOM   462  C CA    . GLY   A 1 64  ? 12.803 -37.870 -7.676  1.00 43.11  ?  64  GLY   A CA    1 
ATOM   463  C C     . GLY   A 1 64  ? 13.726 -37.522 -6.517  1.00 48.91  ?  64  GLY   A C     1 
ATOM   464  O O     . GLY   A 1 64  ? 14.869 -37.992 -6.424  1.00 49.58  ?  64  GLY   A O     1 
ATOM   465  N N     . TYR   A 1 65  ? 13.212 -36.666 -5.620  1.00 43.84  ?  65  TYR   A N     1 
ATOM   466  C CA    . TYR   A 1 65  ? 13.888 -36.369 -4.356  1.00 41.34  ?  65  TYR   A CA    1 
ATOM   467  C C     . TYR   A 1 65  ? 14.235 -37.666 -3.640  1.00 46.17  ?  65  TYR   A C     1 
ATOM   468  O O     . TYR   A 1 65  ? 13.402 -38.575 -3.529  1.00 47.14  ?  65  TYR   A O     1 
ATOM   469  C CB    . TYR   A 1 65  ? 13.002 -35.504 -3.462  1.00 37.14  ?  65  TYR   A CB    1 
ATOM   470  C CG    . TYR   A 1 65  ? 12.770 -34.097 -3.952  1.00 32.90  ?  65  TYR   A CG    1 
ATOM   471  C CD1   . TYR   A 1 65  ? 13.830 -33.258 -4.262  1.00 31.39  ?  65  TYR   A CD1   1 
ATOM   472  C CD2   . TYR   A 1 65  ? 11.480 -33.613 -4.105  1.00 29.26  ?  65  TYR   A CD2   1 
ATOM   473  C CE1   . TYR   A 1 65  ? 13.612 -31.973 -4.703  1.00 30.11  ?  65  TYR   A CE1   1 
ATOM   474  C CE2   . TYR   A 1 65  ? 11.250 -32.350 -4.546  1.00 28.90  ?  65  TYR   A CE2   1 
ATOM   475  C CZ    . TYR   A 1 65  ? 12.312 -31.524 -4.842  1.00 32.46  ?  65  TYR   A CZ    1 
ATOM   476  O OH    . TYR   A 1 65  ? 12.046 -30.252 -5.292  1.00 37.17  ?  65  TYR   A OH    1 
ATOM   477  N N     . ALA   A 1 66  ? 15.466 -37.769 -3.150  1.00 42.39  ?  66  ALA   A N     1 
ATOM   478  C CA    . ALA   A 1 66  ? 15.943 -39.049 -2.575  1.00 44.21  ?  66  ALA   A CA    1 
ATOM   479  C C     . ALA   A 1 66  ? 15.266 -39.429 -1.255  1.00 50.30  ?  66  ALA   A C     1 
ATOM   480  O O     . ALA   A 1 66  ? 15.462 -40.558 -0.791  1.00 57.65  ?  66  ALA   A O     1 
ATOM   481  C CB    . ALA   A 1 66  ? 17.434 -38.966 -2.422  1.00 44.28  ?  66  ALA   A CB    1 
ATOM   482  N N     . ASP   A 1 67  ? 14.489 -38.528 -0.674  1.00 47.45  ?  67  ASP   A N     1 
ATOM   483  C CA    . ASP   A 1 67  ? 13.756 -38.829 0.580   1.00 52.64  ?  67  ASP   A CA    1 
ATOM   484  C C     . ASP   A 1 67  ? 12.271 -39.043 0.279   1.00 51.62  ?  67  ASP   A C     1 
ATOM   485  O O     . ASP   A 1 67  ? 11.557 -39.505 1.177   1.00 48.83  ?  67  ASP   A O     1 
ATOM   486  C CB    . ASP   A 1 67  ? 13.971 -37.723 1.597   1.00 55.33  ?  67  ASP   A CB    1 
ATOM   487  C CG    . ASP   A 1 67  ? 13.777 -36.300 1.104   1.00 56.80  ?  67  ASP   A CG    1 
ATOM   488  O OD1   . ASP   A 1 67  ? 13.903 -36.076 -0.112  1.00 55.08  ?  67  ASP   A OD1   1 
ATOM   489  O OD2   . ASP   A 1 67  ? 13.513 -35.429 1.950   1.00 52.78  ?  67  ASP   A OD2   1 
ATOM   490  N N     . PHE   A 1 68  ? 11.835 -38.705 -0.931  1.00 46.21  ?  68  PHE   A N     1 
ATOM   491  C CA    . PHE   A 1 68  ? 10.401 -38.797 -1.303  1.00 48.65  ?  68  PHE   A CA    1 
ATOM   492  C C     . PHE   A 1 68  ? 10.296 -39.492 -2.636  1.00 48.87  ?  68  PHE   A C     1 
ATOM   493  O O     . PHE   A 1 68  ? 10.306 -38.848 -3.693  1.00 44.20  ?  68  PHE   A O     1 
ATOM   494  C CB    . PHE   A 1 68  ? 9.826  -37.383 -1.354  1.00 48.17  ?  68  PHE   A CB    1 
ATOM   495  C CG    . PHE   A 1 68  ? 8.321  -37.249 -1.209  1.00 48.75  ?  68  PHE   A CG    1 
ATOM   496  C CD1   . PHE   A 1 68  ? 7.681  -37.636 -0.042  1.00 48.00  ?  68  PHE   A CD1   1 
ATOM   497  C CD2   . PHE   A 1 68  ? 7.557  -36.716 -2.237  1.00 48.39  ?  68  PHE   A CD2   1 
ATOM   498  C CE1   . PHE   A 1 68  ? 6.310  -37.506 0.083   1.00 48.49  ?  68  PHE   A CE1   1 
ATOM   499  C CE2   . PHE   A 1 68  ? 6.187  -36.589 -2.106  1.00 46.36  ?  68  PHE   A CE2   1 
ATOM   500  C CZ    . PHE   A 1 68  ? 5.569  -36.982 -0.946  1.00 48.27  ?  68  PHE   A CZ    1 
ATOM   501  N N     . PRO   A 1 69  ? 10.202 -40.829 -2.628  1.00 47.28  ?  69  PRO   A N     1 
ATOM   502  C CA    . PRO   A 1 69  ? 10.056 -41.575 -3.862  1.00 48.23  ?  69  PRO   A CA    1 
ATOM   503  C C     . PRO   A 1 69  ? 8.734  -41.336 -4.574  1.00 45.86  ?  69  PRO   A C     1 
ATOM   504  O O     . PRO   A 1 69  ? 7.724  -41.065 -3.913  1.00 43.59  ?  69  PRO   A O     1 
ATOM   505  C CB    . PRO   A 1 69  ? 10.196 -43.007 -3.344  1.00 49.19  ?  69  PRO   A CB    1 
ATOM   506  C CG    . PRO   A 1 69  ? 9.662  -42.950 -1.943  1.00 48.71  ?  69  PRO   A CG    1 
ATOM   507  C CD    . PRO   A 1 69  ? 10.230 -41.646 -1.437  1.00 48.48  ?  69  PRO   A CD    1 
ATOM   508  N N     . MET   A 1 70  ? 8.744  -41.437 -5.906  1.00 48.16  ?  70  MET   A N     1 
ATOM   509  C CA    . MET   A 1 70  ? 7.536  -41.226 -6.682  1.00 43.01  ?  70  MET   A CA    1 
ATOM   510  C C     . MET   A 1 70  ? 6.620  -42.432 -6.560  1.00 37.24  ?  70  MET   A C     1 
ATOM   511  O O     . MET   A 1 70  ? 7.069  -43.536 -6.245  1.00 40.10  ?  70  MET   A O     1 
ATOM   512  C CB    . MET   A 1 70  ? 7.883  -40.977 -8.152  1.00 42.45  ?  70  MET   A CB    1 
ATOM   513  C CG    . MET   A 1 70  ? 8.474  -39.596 -8.464  1.00 46.51  ?  70  MET   A CG    1 
ATOM   514  S SD    . MET   A 1 70  ? 8.434  -39.232 -10.257 1.00 50.03  ?  70  MET   A SD    1 
ATOM   515  C CE    . MET   A 1 70  ? 9.916  -38.256 -10.517 1.00 39.16  ?  70  MET   A CE    1 
ATOM   516  N N     . PRO   A 1 71  ? 5.331  -42.246 -6.818  1.00 34.81  ?  71  PRO   A N     1 
ATOM   517  C CA    . PRO   A 1 71  ? 4.384  -43.364 -6.732  1.00 34.18  ?  71  PRO   A CA    1 
ATOM   518  C C     . PRO   A 1 71  ? 4.796  -44.548 -7.598  1.00 43.31  ?  71  PRO   A C     1 
ATOM   519  O O     . PRO   A 1 71  ? 5.127  -44.400 -8.775  1.00 44.53  ?  71  PRO   A O     1 
ATOM   520  C CB    . PRO   A 1 71  ? 3.072  -42.744 -7.210  1.00 33.28  ?  71  PRO   A CB    1 
ATOM   521  C CG    . PRO   A 1 71  ? 3.204  -41.300 -6.926  1.00 33.91  ?  71  PRO   A CG    1 
ATOM   522  C CD    . PRO   A 1 71  ? 4.657  -40.966 -7.093  1.00 36.56  ?  71  PRO   A CD    1 
ATOM   523  N N     . ASP   A 1 72  ? 4.764  -45.743 -7.007  1.00 44.41  ?  72  ASP   A N     1 
ATOM   524  C CA    . ASP   A 1 72  ? 5.336  -46.904 -7.680  1.00 50.26  ?  72  ASP   A CA    1 
ATOM   525  C C     . ASP   A 1 72  ? 4.673  -47.213 -9.019  1.00 50.10  ?  72  ASP   A C     1 
ATOM   526  O O     . ASP   A 1 72  ? 5.274  -47.909 -9.845  1.00 50.00  ?  72  ASP   A O     1 
ATOM   527  C CB    . ASP   A 1 72  ? 5.269  -48.122 -6.763  1.00 48.82  ?  72  ASP   A CB    1 
ATOM   528  C CG    . ASP   A 1 72  ? 6.604  -48.422 -6.114  1.00 62.07  ?  72  ASP   A CG    1 
ATOM   529  O OD1   . ASP   A 1 72  ? 7.612  -48.543 -6.851  1.00 64.75  ?  72  ASP   A OD1   1 
ATOM   530  O OD2   . ASP   A 1 72  ? 6.654  -48.513 -4.865  1.00 82.59  ?  72  ASP   A OD2   1 
ATOM   531  N N     . ALA   A 1 73  ? 3.457  -46.726 -9.250  1.00 46.00  ?  73  ALA   A N     1 
ATOM   532  C CA    . ALA   A 1 73  ? 2.793  -46.944 -10.527 1.00 48.81  ?  73  ALA   A CA    1 
ATOM   533  C C     . ALA   A 1 73  ? 3.225  -45.956 -11.605 1.00 47.91  ?  73  ALA   A C     1 
ATOM   534  O O     . ALA   A 1 73  ? 2.836  -46.130 -12.766 1.00 53.33  ?  73  ALA   A O     1 
ATOM   535  C CB    . ALA   A 1 73  ? 1.280  -46.866 -10.352 1.00 57.18  ?  73  ALA   A CB    1 
ATOM   536  N N     . TYR   A 1 74  ? 4.001  -44.934 -11.255 1.00 42.66  ?  74  TYR   A N     1 
ATOM   537  C CA    . TYR   A 1 74  ? 4.552  -44.051 -12.264 1.00 43.95  ?  74  TYR   A CA    1 
ATOM   538  C C     . TYR   A 1 74  ? 5.445  -44.850 -13.215 1.00 49.11  ?  74  TYR   A C     1 
ATOM   539  O O     . TYR   A 1 74  ? 6.116  -45.809 -12.798 1.00 50.59  ?  74  TYR   A O     1 
ATOM   540  C CB    . TYR   A 1 74  ? 5.352  -42.916 -11.625 1.00 39.86  ?  74  TYR   A CB    1 
ATOM   541  C CG    . TYR   A 1 74  ? 4.531  -41.713 -11.206 1.00 39.95  ?  74  TYR   A CG    1 
ATOM   542  C CD1   . TYR   A 1 74  ? 3.194  -41.846 -10.831 1.00 39.97  ?  74  TYR   A CD1   1 
ATOM   543  C CD2   . TYR   A 1 74  ? 5.101  -40.441 -11.159 1.00 39.74  ?  74  TYR   A CD2   1 
ATOM   544  C CE1   . TYR   A 1 74  ? 2.452  -40.744 -10.422 1.00 36.52  ?  74  TYR   A CE1   1 
ATOM   545  C CE2   . TYR   A 1 74  ? 4.363  -39.329 -10.750 1.00 40.52  ?  74  TYR   A CE2   1 
ATOM   546  C CZ    . TYR   A 1 74  ? 3.041  -39.489 -10.386 1.00 38.71  ?  74  TYR   A CZ    1 
ATOM   547  O OH    . TYR   A 1 74  ? 2.306  -38.395 -10.004 1.00 33.51  ?  74  TYR   A OH    1 
ATOM   548  N N     . PRO   A 1 75  ? 5.472  -44.502 -14.488 1.00 45.20  ?  75  PRO   A N     1 
ATOM   549  C CA    . PRO   A 1 75  ? 6.373  -45.165 -15.421 1.00 43.64  ?  75  PRO   A CA    1 
ATOM   550  C C     . PRO   A 1 75  ? 7.740  -44.500 -15.346 1.00 44.10  ?  75  PRO   A C     1 
ATOM   551  O O     . PRO   A 1 75  ? 7.938  -43.506 -14.644 1.00 46.17  ?  75  PRO   A O     1 
ATOM   552  C CB    . PRO   A 1 75  ? 5.694  -44.917 -16.766 1.00 46.29  ?  75  PRO   A CB    1 
ATOM   553  C CG    . PRO   A 1 75  ? 5.132  -43.519 -16.602 1.00 39.71  ?  75  PRO   A CG    1 
ATOM   554  C CD    . PRO   A 1 75  ? 4.734  -43.400 -15.136 1.00 46.85  ?  75  PRO   A CD    1 
ATOM   555  N N     . LEU   A 1 76  ? 8.670  -45.057 -16.117 1.00 42.41  ?  76  LEU   A N     1 
ATOM   556  C CA    . LEU   A 1 76  ? 10.010 -44.502 -16.226 1.00 39.68  ?  76  LEU   A CA    1 
ATOM   557  C C     . LEU   A 1 76  ? 10.014 -43.053 -16.695 1.00 40.24  ?  76  LEU   A C     1 
ATOM   558  O O     . LEU   A 1 76  ? 10.956 -42.320 -16.396 1.00 44.84  ?  76  LEU   A O     1 
ATOM   559  C CB    . LEU   A 1 76  ? 10.818 -45.348 -17.188 1.00 41.21  ?  76  LEU   A CB    1 
ATOM   560  C CG    . LEU   A 1 76  ? 12.319 -45.227 -17.044 1.00 48.83  ?  76  LEU   A CG    1 
ATOM   561  C CD1   . LEU   A 1 76  ? 12.748 -45.861 -15.739 1.00 46.29  ?  76  LEU   A CD1   1 
ATOM   562  C CD2   . LEU   A 1 76  ? 12.987 -45.876 -18.244 1.00 48.08  ?  76  LEU   A CD2   1 
ATOM   563  N N     . TYR   A 1 77  ? 9.014  -42.621 -17.454 1.00 41.29  ?  77  TYR   A N     1 
ATOM   564  C CA    . TYR   A 1 77  ? 8.958  -41.247 -17.967 1.00 44.54  ?  77  TYR   A CA    1 
ATOM   565  C C     . TYR   A 1 77  ? 7.560  -40.706 -17.738 1.00 47.99  ?  77  TYR   A C     1 
ATOM   566  O O     . TYR   A 1 77  ? 6.708  -40.755 -18.637 1.00 48.76  ?  77  TYR   A O     1 
ATOM   567  C CB    . TYR   A 1 77  ? 9.297  -41.147 -19.460 1.00 42.65  ?  77  TYR   A CB    1 
ATOM   568  C CG    . TYR   A 1 77  ? 10.582 -41.802 -19.901 1.00 43.12  ?  77  TYR   A CG    1 
ATOM   569  C CD1   . TYR   A 1 77  ? 11.812 -41.265 -19.556 1.00 46.00  ?  77  TYR   A CD1   1 
ATOM   570  C CD2   . TYR   A 1 77  ? 10.563 -42.949 -20.681 1.00 46.05  ?  77  TYR   A CD2   1 
ATOM   571  C CE1   . TYR   A 1 77  ? 12.984 -41.858 -19.956 1.00 47.37  ?  77  TYR   A CE1   1 
ATOM   572  C CE2   . TYR   A 1 77  ? 11.737 -43.554 -21.091 1.00 48.20  ?  77  TYR   A CE2   1 
ATOM   573  C CZ    . TYR   A 1 77  ? 12.949 -43.003 -20.721 1.00 50.93  ?  77  TYR   A CZ    1 
ATOM   574  O OH    . TYR   A 1 77  ? 14.125 -43.598 -21.126 1.00 51.37  ?  77  TYR   A OH    1 
ATOM   575  N N     . PRO   A 1 78  ? 7.284  -40.191 -16.547 1.00 49.27  ?  78  PRO   A N     1 
ATOM   576  C CA    . PRO   A 1 78  ? 5.948  -39.659 -16.274 1.00 45.38  ?  78  PRO   A CA    1 
ATOM   577  C C     . PRO   A 1 78  ? 5.625  -38.424 -17.104 1.00 40.21  ?  78  PRO   A C     1 
ATOM   578  O O     . PRO   A 1 78  ? 6.508  -37.655 -17.487 1.00 39.94  ?  78  PRO   A O     1 
ATOM   579  C CB    . PRO   A 1 78  ? 6.011  -39.326 -14.773 1.00 45.30  ?  78  PRO   A CB    1 
ATOM   580  C CG    . PRO   A 1 78  ? 7.009  -40.297 -14.249 1.00 42.62  ?  78  PRO   A CG    1 
ATOM   581  C CD    . PRO   A 1 78  ? 8.062  -40.369 -15.307 1.00 45.78  ?  78  PRO   A CD    1 
ATOM   582  N N     . ARG   A 1 79  ? 4.327  -38.241 -17.348 1.00 41.23  ?  79  ARG   A N     1 
ATOM   583  C CA    . ARG   A 1 79  ? 3.797  -37.060 -18.021 1.00 44.71  ?  79  ARG   A CA    1 
ATOM   584  C C     . ARG   A 1 79  ? 3.922  -35.826 -17.122 1.00 48.37  ?  79  ARG   A C     1 
ATOM   585  O O     . ARG   A 1 79  ? 3.940  -35.923 -15.890 1.00 45.43  ?  79  ARG   A O     1 
ATOM   586  C CB    . ARG   A 1 79  ? 2.328  -37.306 -18.419 1.00 41.38  ?  79  ARG   A CB    1 
ATOM   587  C CG    . ARG   A 1 79  ? 1.589  -36.147 -19.105 1.00 49.82  ?  79  ARG   A CG    1 
ATOM   588  C CD    . ARG   A 1 79  ? 0.160  -36.509 -19.611 1.00 47.55  ?  79  ARG   A CD    1 
ATOM   589  N NE    . ARG   A 1 79  ? -0.809 -35.415 -19.414 1.00 56.61  ?  79  ARG   A NE    1 
ATOM   590  C CZ    . ARG   A 1 79  ? -1.379 -34.709 -20.396 1.00 59.19  ?  79  ARG   A CZ    1 
ATOM   591  N NH1   . ARG   A 1 79  ? -1.092 -34.978 -21.663 1.00 60.75  ?  79  ARG   A NH1   1 
ATOM   592  N NH2   . ARG   A 1 79  ? -2.242 -33.730 -20.123 1.00 58.62  ?  79  ARG   A NH2   1 
ATOM   593  N N     . HIS   A 1 80  ? 4.001  -34.654 -17.763 1.00 48.72  ?  80  HIS   A N     1 
ATOM   594  C CA    . HIS   A 1 80  ? 4.170  -33.383 -17.069 1.00 44.55  ?  80  HIS   A CA    1 
ATOM   595  C C     . HIS   A 1 80  ? 3.124  -33.155 -15.999 1.00 50.96  ?  80  HIS   A C     1 
ATOM   596  O O     . HIS   A 1 80  ? 3.359  -32.362 -15.077 1.00 47.43  ?  80  HIS   A O     1 
ATOM   597  C CB    . HIS   A 1 80  ? 4.096  -32.231 -18.066 1.00 52.53  ?  80  HIS   A CB    1 
ATOM   598  C CG    . HIS   A 1 80  ? 2.747  -32.067 -18.706 1.00 57.49  ?  80  HIS   A CG    1 
ATOM   599  N ND1   . HIS   A 1 80  ? 1.728  -31.337 -18.127 1.00 57.06  ?  80  HIS   A ND1   1 
ATOM   600  C CD2   . HIS   A 1 80  ? 2.253  -32.537 -19.879 1.00 53.38  ?  80  HIS   A CD2   1 
ATOM   601  C CE1   . HIS   A 1 80  ? 0.667  -31.365 -18.916 1.00 57.16  ?  80  HIS   A CE1   1 
ATOM   602  N NE2   . HIS   A 1 80  ? 0.958  -32.088 -19.984 1.00 51.76  ?  80  HIS   A NE2   1 
ATOM   603  N N     . SER   A 1 81  ? 1.957  -33.789 -16.124 1.00 53.54  ?  81  SER   A N     1 
ATOM   604  C CA    . SER   A 1 81  ? 0.943  -33.689 -15.077 1.00 53.87  ?  81  SER   A CA    1 
ATOM   605  C C     . SER   A 1 81  ? 1.312  -34.551 -13.866 1.00 51.07  ?  81  SER   A C     1 
ATOM   606  O O     . SER   A 1 81  ? 1.256  -34.078 -12.724 1.00 49.14  ?  81  SER   A O     1 
ATOM   607  C CB    . SER   A 1 81  ? -0.439 -34.070 -15.630 1.00 58.69  ?  81  SER   A CB    1 
ATOM   608  O OG    . SER   A 1 81  ? -0.494 -35.424 -16.062 1.00 63.14  ?  81  SER   A OG    1 
ATOM   609  N N     . GLN   A 1 82  ? 1.714  -35.811 -14.097 1.00 45.34  ?  82  GLN   A N     1 
ATOM   610  C CA    . GLN   A 1 82  ? 2.202  -36.651 -13.008 1.00 44.08  ?  82  GLN   A CA    1 
ATOM   611  C C     . GLN   A 1 82  ? 3.309  -35.968 -12.215 1.00 45.90  ?  82  GLN   A C     1 
ATOM   612  O O     . GLN   A 1 82  ? 3.388  -36.108 -10.985 1.00 46.57  ?  82  GLN   A O     1 
ATOM   613  C CB    . GLN   A 1 82  ? 2.714  -37.969 -13.556 1.00 41.56  ?  82  GLN   A CB    1 
ATOM   614  C CG    . GLN   A 1 82  ? 1.636  -38.919 -13.940 1.00 41.95  ?  82  GLN   A CG    1 
ATOM   615  C CD    . GLN   A 1 82  ? 2.131  -39.884 -14.969 1.00 44.76  ?  82  GLN   A CD    1 
ATOM   616  O OE1   . GLN   A 1 82  ? 2.815  -39.484 -15.916 1.00 50.97  ?  82  GLN   A OE1   1 
ATOM   617  N NE2   . GLN   A 1 82  ? 1.798  -41.156 -14.810 1.00 44.46  ?  82  GLN   A NE2   1 
ATOM   618  N N     . VAL   A 1 83  ? 4.176  -35.233 -12.905 1.00 41.12  ?  83  VAL   A N     1 
ATOM   619  C CA    . VAL   A 1 83  ? 5.314  -34.615 -12.244 1.00 40.83  ?  83  VAL   A CA    1 
ATOM   620  C C     . VAL   A 1 83  ? 4.854  -33.471 -11.353 1.00 44.62  ?  83  VAL   A C     1 
ATOM   621  O O     . VAL   A 1 83  ? 5.261  -33.367 -10.186 1.00 43.39  ?  83  VAL   A O     1 
ATOM   622  C CB    . VAL   A 1 83  ? 6.335  -34.147 -13.290 1.00 45.06  ?  83  VAL   A CB    1 
ATOM   623  C CG1   . VAL   A 1 83  ? 7.264  -33.120 -12.706 1.00 39.92  ?  83  VAL   A CG1   1 
ATOM   624  C CG2   . VAL   A 1 83  ? 7.092  -35.348 -13.850 1.00 46.94  ?  83  VAL   A CG2   1 
ATOM   625  N N     . ALA   A 1 84  ? 3.990  -32.604 -11.882 1.00 40.32  ?  84  ALA   A N     1 
ATOM   626  C CA    . ALA   A 1 84  ? 3.542  -31.452 -11.107 1.00 44.75  ?  84  ALA   A CA    1 
ATOM   627  C C     . ALA   A 1 84  ? 2.782  -31.889 -9.855  1.00 48.33  ?  84  ALA   A C     1 
ATOM   628  O O     . ALA   A 1 84  ? 2.939  -31.298 -8.781  1.00 39.84  ?  84  ALA   A O     1 
ATOM   629  C CB    . ALA   A 1 84  ? 2.673  -30.537 -11.967 1.00 41.37  ?  84  ALA   A CB    1 
ATOM   630  N N     . ALA   A 1 85  ? 1.947  -32.922 -9.982  1.00 49.53  ?  85  ALA   A N     1 
ATOM   631  C CA    . ALA   A 1 85  ? 1.183  -33.398 -8.844  1.00 46.40  ?  85  ALA   A CA    1 
ATOM   632  C C     . ALA   A 1 85  ? 2.092  -34.008 -7.803  1.00 44.06  ?  85  ALA   A C     1 
ATOM   633  O O     . ALA   A 1 85  ? 1.763  -33.987 -6.618  1.00 49.29  ?  85  ALA   A O     1 
ATOM   634  C CB    . ALA   A 1 85  ? 0.137  -34.417 -9.287  1.00 42.07  ?  85  ALA   A CB    1 
ATOM   635  N N     . TYR   A 1 86  ? 3.237  -34.542 -8.226  1.00 43.53  ?  86  TYR   A N     1 
ATOM   636  C CA    . TYR   A 1 86  ? 4.194  -35.087 -7.272  1.00 45.75  ?  86  TYR   A CA    1 
ATOM   637  C C     . TYR   A 1 86  ? 4.913  -33.972 -6.517  1.00 46.15  ?  86  TYR   A C     1 
ATOM   638  O O     . TYR   A 1 86  ? 5.163  -34.100 -5.318  1.00 47.22  ?  86  TYR   A O     1 
ATOM   639  C CB    . TYR   A 1 86  ? 5.182  -36.004 -7.993  1.00 39.98  ?  86  TYR   A CB    1 
ATOM   640  C CG    . TYR   A 1 86  ? 6.517  -36.173 -7.320  1.00 37.01  ?  86  TYR   A CG    1 
ATOM   641  C CD1   . TYR   A 1 86  ? 7.586  -35.335 -7.626  1.00 40.53  ?  86  TYR   A CD1   1 
ATOM   642  C CD2   . TYR   A 1 86  ? 6.729  -37.200 -6.409  1.00 42.15  ?  86  TYR   A CD2   1 
ATOM   643  C CE1   . TYR   A 1 86  ? 8.837  -35.501 -7.025  1.00 41.43  ?  86  TYR   A CE1   1 
ATOM   644  C CE2   . TYR   A 1 86  ? 7.972  -37.380 -5.788  1.00 42.90  ?  86  TYR   A CE2   1 
ATOM   645  C CZ    . TYR   A 1 86  ? 9.028  -36.527 -6.104  1.00 45.80  ?  86  TYR   A CZ    1 
ATOM   646  O OH    . TYR   A 1 86  ? 10.267 -36.699 -5.492  1.00 47.49  ?  86  TYR   A OH    1 
ATOM   647  N N     . LEU   A 1 87  ? 5.204  -32.865 -7.182  1.00 46.03  ?  87  LEU   A N     1 
ATOM   648  C CA    . LEU   A 1 87  ? 6.009  -31.802 -6.534  1.00 45.56  ?  87  LEU   A CA    1 
ATOM   649  C C     . LEU   A 1 87  ? 5.206  -31.100 -5.424  1.00 47.50  ?  87  LEU   A C     1 
ATOM   650  O O     . LEU   A 1 87  ? 5.814  -30.660 -4.442  1.00 47.36  ?  87  LEU   A O     1 
ATOM   651  C CB    . LEU   A 1 87  ? 6.501  -30.842 -7.616  1.00 44.37  ?  87  LEU   A CB    1 
ATOM   652  C CG    . LEU   A 1 87  ? 7.663  -31.314 -8.493  1.00 40.86  ?  87  LEU   A CG    1 
ATOM   653  C CD1   . LEU   A 1 87  ? 7.969  -30.239 -9.513  1.00 46.66  ?  87  LEU   A CD1   1 
ATOM   654  C CD2   . LEU   A 1 87  ? 8.893  -31.610 -7.666  1.00 36.26  ?  87  LEU   A CD2   1 
ATOM   655  N N     . ARG   A 1 88  ? 3.889  -31.033 -5.565  1.00 44.53  ?  88  ARG   A N     1 
ATOM   656  C CA    . ARG   A 1 88  ? 3.041  -30.432 -4.510  1.00 50.49  ?  88  ARG   A CA    1 
ATOM   657  C C     . ARG   A 1 88  ? 2.911  -31.423 -3.349  1.00 48.01  ?  88  ARG   A C     1 
ATOM   658  O O     . ARG   A 1 88  ? 2.823  -30.972 -2.209  1.00 52.01  ?  88  ARG   A O     1 
ATOM   659  C CB    . ARG   A 1 88  ? 1.689  -30.049 -5.113  1.00 46.08  ?  88  ARG   A CB    1 
ATOM   660  C CG    . ARG   A 1 88  ? 0.530  -29.918 -4.138  1.00 57.07  ?  88  ARG   A CG    1 
ATOM   661  C CD    . ARG   A 1 88  ? -0.439 -28.831 -4.553  1.00 57.75  ?  88  ARG   A CD    1 
ATOM   662  N NE    . ARG   A 1 88  ? -0.215 -27.594 -3.800  1.00 56.60  ?  88  ARG   A NE    1 
ATOM   663  C CZ    . ARG   A 1 88  ? -0.945 -27.207 -2.769  1.00 61.58  ?  88  ARG   A CZ    1 
ATOM   664  N NH1   . ARG   A 1 88  ? -1.545 -28.104 -2.011  1.00 61.02  ?  88  ARG   A NH1   1 
ATOM   665  N NH2   . ARG   A 1 88  ? -1.071 -25.923 -2.497  1.00 66.09  ?  88  ARG   A NH2   1 
ATOM   666  N N     . SER   A 1 89  ? 2.963  -32.718 -3.635  1.00 42.23  ?  89  SER   A N     1 
ATOM   667  C CA    . SER   A 1 89  ? 2.861  -33.745 -2.576  1.00 42.51  ?  89  SER   A CA    1 
ATOM   668  C C     . SER   A 1 89  ? 4.096  -33.675 -1.682  1.00 46.39  ?  89  SER   A C     1 
ATOM   669  O O     . SER   A 1 89  ? 3.987  -34.059 -0.520  1.00 52.16  ?  89  SER   A O     1 
ATOM   670  C CB    . SER   A 1 89  ? 2.668  -35.112 -3.150  1.00 44.96  ?  89  SER   A CB    1 
ATOM   671  O OG    . SER   A 1 89  ? 2.178  -36.020 -2.178  1.00 45.46  ?  89  SER   A OG    1 
ATOM   672  N N     . PHE   A 1 90  ? 5.231  -33.200 -2.183  1.00 47.34  ?  90  PHE   A N     1 
ATOM   673  C CA    . PHE   A 1 90  ? 6.448  -33.043 -1.337  1.00 49.20  ?  90  PHE   A CA    1 
ATOM   674  C C     . PHE   A 1 90  ? 6.291  -31.830 -0.442  1.00 45.52  ?  90  PHE   A C     1 
ATOM   675  O O     . PHE   A 1 90  ? 6.670  -31.883 0.723   1.00 42.85  ?  90  PHE   A O     1 
ATOM   676  C CB    . PHE   A 1 90  ? 7.663  -32.922 -2.258  1.00 45.13  ?  90  PHE   A CB    1 
ATOM   677  C CG    . PHE   A 1 90  ? 9.012  -32.615 -1.626  1.00 41.60  ?  90  PHE   A CG    1 
ATOM   678  C CD1   . PHE   A 1 90  ? 9.757  -33.612 -1.013  1.00 37.39  ?  90  PHE   A CD1   1 
ATOM   679  C CD2   . PHE   A 1 90  ? 9.551  -31.337 -1.689  1.00 38.69  ?  90  PHE   A CD2   1 
ATOM   680  C CE1   . PHE   A 1 90  ? 10.996 -33.332 -0.465  1.00 36.57  ?  90  PHE   A CE1   1 
ATOM   681  C CE2   . PHE   A 1 90  ? 10.789 -31.063 -1.135  1.00 35.24  ?  90  PHE   A CE2   1 
ATOM   682  C CZ    . PHE   A 1 90  ? 11.507 -32.061 -0.526  1.00 34.30  ?  90  PHE   A CZ    1 
ATOM   683  N N     . ALA   A 1 91  ? 5.713  -30.770 -0.985  1.00 48.62  ?  91  ALA   A N     1 
ATOM   684  C CA    . ALA   A 1 91  ? 5.545  -29.511 -0.233  1.00 51.66  ?  91  ALA   A CA    1 
ATOM   685  C C     . ALA   A 1 91  ? 4.568  -29.746 0.909   1.00 47.99  ?  91  ALA   A C     1 
ATOM   686  O O     . ALA   A 1 91  ? 4.727  -29.144 1.977   1.00 48.19  ?  91  ALA   A O     1 
ATOM   687  C CB    . ALA   A 1 91  ? 5.085  -28.415 -1.167  1.00 45.85  ?  91  ALA   A CB    1 
ATOM   688  N N     . GLU   A 1 92  ? 3.613  -30.627 0.676   1.00 43.46  ?  92  GLU   A N     1 
ATOM   689  C CA    . GLU   A 1 92  ? 2.655  -30.977 1.742   1.00 47.58  ?  92  GLU   A CA    1 
ATOM   690  C C     . GLU   A 1 92  ? 3.369  -31.827 2.807   1.00 50.21  ?  92  GLU   A C     1 
ATOM   691  O O     . GLU   A 1 92  ? 3.258  -31.492 3.991   1.00 47.69  ?  92  GLU   A O     1 
ATOM   692  C CB    . GLU   A 1 92  ? 1.479  -31.663 1.060   1.00 45.16  ?  92  GLU   A CB    1 
ATOM   693  C CG    . GLU   A 1 92  ? 0.649  -30.718 0.197   1.00 51.58  ?  92  GLU   A CG    1 
ATOM   694  C CD    . GLU   A 1 92  ? -0.356 -31.374 -0.731  1.00 43.46  ?  92  GLU   A CD    1 
ATOM   695  O OE1   . GLU   A 1 92  ? -0.385 -32.612 -0.808  1.00 40.82  ?  92  GLU   A OE1   1 
ATOM   696  O OE2   . GLU   A 1 92  ? -1.118 -30.639 -1.380  1.00 48.23  ?  92  GLU   A OE2   1 
ATOM   697  N N     . TRP   A 1 93  ? 4.074  -32.874 2.394   1.00 46.16  ?  93  TRP   A N     1 
ATOM   698  C CA    . TRP   A 1 93  ? 4.788  -33.768 3.335   1.00 45.40  ?  93  TRP   A CA    1 
ATOM   699  C C     . TRP   A 1 93  ? 5.849  -32.977 4.089   1.00 45.13  ?  93  TRP   A C     1 
ATOM   700  O O     . TRP   A 1 93  ? 5.880  -33.040 5.323   1.00 48.30  ?  93  TRP   A O     1 
ATOM   701  C CB    . TRP   A 1 93  ? 5.382  -34.938 2.544   1.00 39.00  ?  93  TRP   A CB    1 
ATOM   702  C CG    . TRP   A 1 93  ? 6.315  -35.862 3.275   1.00 43.65  ?  93  TRP   A CG    1 
ATOM   703  C CD1   . TRP   A 1 93  ? 5.981  -36.893 4.100   1.00 47.43  ?  93  TRP   A CD1   1 
ATOM   704  C CD2   . TRP   A 1 93  ? 7.753  -35.881 3.172   1.00 44.96  ?  93  TRP   A CD2   1 
ATOM   705  N NE1   . TRP   A 1 93  ? 7.107  -37.531 4.541   1.00 43.62  ?  93  TRP   A NE1   1 
ATOM   706  C CE2   . TRP   A 1 93  ? 8.208  -36.938 3.985   1.00 39.59  ?  93  TRP   A CE2   1 
ATOM   707  C CE3   . TRP   A 1 93  ? 8.692  -35.109 2.482   1.00 45.89  ?  93  TRP   A CE3   1 
ATOM   708  C CZ2   . TRP   A 1 93  ? 9.559  -37.236 4.126   1.00 41.94  ?  93  TRP   A CZ2   1 
ATOM   709  C CZ3   . TRP   A 1 93  ? 10.027 -35.408 2.620   1.00 47.36  ?  93  TRP   A CZ3   1 
ATOM   710  C CH2   . TRP   A 1 93  ? 10.452 -36.459 3.427   1.00 41.44  ?  93  TRP   A CH2   1 
ATOM   711  N N     . ALA   A 1 94  ? 6.804  -32.440 3.323   1.00 41.30  ?  94  ALA   A N     1 
ATOM   712  C CA    . ALA   A 1 94  ? 7.998  -31.775 3.892   1.00 46.68  ?  94  ALA   A CA    1 
ATOM   713  C C     . ALA   A 1 94  ? 7.618  -30.572 4.720   1.00 49.72  ?  94  ALA   A C     1 
ATOM   714  O O     . ALA   A 1 94  ? 8.460  -29.963 5.390   1.00 46.69  ?  94  ALA   A O     1 
ATOM   715  C CB    . ALA   A 1 94  ? 8.942  -31.371 2.793   1.00 45.75  ?  94  ALA   A CB    1 
ATOM   716  N N     . GLY   A 1 95  ? 6.376  -30.189 4.599   1.00 51.20  ?  95  GLY   A N     1 
ATOM   717  C CA    . GLY   A 1 95  ? 5.979  -29.151 5.527   1.00 45.33  ?  95  GLY   A CA    1 
ATOM   718  C C     . GLY   A 1 95  ? 6.271  -27.719 5.137   1.00 51.15  ?  95  GLY   A C     1 
ATOM   719  O O     . GLY   A 1 95  ? 6.600  -26.960 6.043   1.00 54.35  ?  95  GLY   A O     1 
ATOM   720  N N     . LEU   A 1 96  ? 6.003  -27.276 3.910   1.00 48.19  ?  96  LEU   A N     1 
ATOM   721  C CA    . LEU   A 1 96  ? 6.517  -25.937 3.517   1.00 46.81  ?  96  LEU   A CA    1 
ATOM   722  C C     . LEU   A 1 96  ? 5.507  -24.867 3.071   1.00 50.83  ?  96  LEU   A C     1 
ATOM   723  O O     . LEU   A 1 96  ? 5.907  -23.702 3.084   1.00 50.60  ?  96  LEU   A O     1 
ATOM   724  C CB    . LEU   A 1 96  ? 7.511  -26.234 2.394   1.00 51.79  ?  96  LEU   A CB    1 
ATOM   725  C CG    . LEU   A 1 96  ? 8.584  -27.290 2.668   1.00 49.70  ?  96  LEU   A CG    1 
ATOM   726  C CD1   . LEU   A 1 96  ? 9.142  -27.777 1.348   1.00 45.06  ?  96  LEU   A CD1   1 
ATOM   727  C CD2   . LEU   A 1 96  ? 9.689  -26.713 3.528   1.00 46.30  ?  96  LEU   A CD2   1 
ATOM   728  N N     . LEU   A 1 97  ? 4.270  -25.202 2.726   1.00 49.85  ?  97  LEU   A N     1 
ATOM   729  C CA    . LEU   A 1 97  ? 3.340  -24.197 2.128   1.00 58.14  ?  97  LEU   A CA    1 
ATOM   730  C C     . LEU   A 1 97  ? 3.113  -22.946 3.001   1.00 59.23  ?  97  LEU   A C     1 
ATOM   731  O O     . LEU   A 1 97  ? 2.876  -21.874 2.425   1.00 60.81  ?  97  LEU   A O     1 
ATOM   732  C CB    . LEU   A 1 97  ? 2.034  -24.881 1.734   1.00 64.68  ?  97  LEU   A CB    1 
ATOM   733  C CG    . LEU   A 1 97  ? 2.153  -25.952 0.645   1.00 58.23  ?  97  LEU   A CG    1 
ATOM   734  C CD1   . LEU   A 1 97  ? 0.880  -26.764 0.536   1.00 56.42  ?  97  LEU   A CD1   1 
ATOM   735  C CD2   . LEU   A 1 97  ? 2.510  -25.331 -0.688  1.00 54.14  ?  97  LEU   A CD2   1 
ATOM   736  N N     . ASP   A 1 98  ? 3.168  -23.078 4.321   1.00 62.49  ?  98  ASP   A N     1 
ATOM   737  C CA    . ASP   A 1 98  ? 2.967  -21.931 5.240   1.00 68.36  ?  98  ASP   A CA    1 
ATOM   738  C C     . ASP   A 1 98  ? 4.092  -20.932 5.022   1.00 65.57  ?  98  ASP   A C     1 
ATOM   739  O O     . ASP   A 1 98  ? 3.941  -19.769 5.430   1.00 67.52  ?  98  ASP   A O     1 
ATOM   740  C CB    . ASP   A 1 98  ? 2.902  -22.377 6.688   1.00 70.30  ?  98  ASP   A CB    1 
ATOM   741  C CG    . ASP   A 1 98  ? 2.058  -21.501 7.599   1.00 81.95  ?  98  ASP   A CG    1 
ATOM   742  O OD1   . ASP   A 1 98  ? 1.559  -20.465 7.116   1.00 92.34  ?  98  ASP   A OD1   1 
ATOM   743  O OD2   . ASP   A 1 98  ? 1.906  -21.863 8.781   1.00 98.43  ?  98  ASP   A OD2   1 
ATOM   744  N N     . HIS   A 1 99  ? 5.174  -21.381 4.401   1.00 60.07  ?  99  HIS   A N     1 
ATOM   745  C CA    . HIS   A 1 99  ? 6.238  -20.446 4.101   1.00 55.91  ?  99  HIS   A CA    1 
ATOM   746  C C     . HIS   A 1 99  ? 6.131  -19.878 2.689   1.00 57.98  ?  99  HIS   A C     1 
ATOM   747  O O     . HIS   A 1 99  ? 6.937  -19.020 2.331   1.00 57.02  ?  99  HIS   A O     1 
ATOM   748  C CB    . HIS   A 1 99  ? 7.595  -21.126 4.290   1.00 56.82  ?  99  HIS   A CB    1 
ATOM   749  C CG    . HIS   A 1 99  ? 7.769  -21.808 5.621   1.00 60.00  ?  99  HIS   A CG    1 
ATOM   750  N ND1   . HIS   A 1 99  ? 6.959  -22.841 6.047   1.00 59.91  ?  99  HIS   A ND1   1 
ATOM   751  C CD2   . HIS   A 1 99  ? 8.694  -21.633 6.600   1.00 56.49  ?  99  HIS   A CD2   1 
ATOM   752  C CE1   . HIS   A 1 99  ? 7.359  -23.251 7.241   1.00 58.41  ?  99  HIS   A CE1   1 
ATOM   753  N NE2   . HIS   A 1 99  ? 8.412  -22.537 7.596   1.00 50.71  ?  99  HIS   A NE2   1 
ATOM   754  N N     . VAL   A 1 100 ? 5.136  -20.296 1.900   1.00 53.96  ?  100 VAL   A N     1 
ATOM   755  C CA    . VAL   A 1 100 ? 5.075  -20.007 0.469   1.00 58.65  ?  100 VAL   A CA    1 
ATOM   756  C C     . VAL   A 1 100 ? 3.981  -18.987 0.179   1.00 58.74  ?  100 VAL   A C     1 
ATOM   757  O O     . VAL   A 1 100 ? 2.796  -19.240 0.431   1.00 62.99  ?  100 VAL   A O     1 
ATOM   758  C CB    . VAL   A 1 100 ? 4.822  -21.275 -0.358  1.00 59.24  ?  100 VAL   A CB    1 
ATOM   759  C CG1   . VAL   A 1 100 ? 5.054  -20.977 -1.837  1.00 58.12  ?  100 VAL   A CG1   1 
ATOM   760  C CG2   . VAL   A 1 100 ? 5.680  -22.433 0.131   1.00 56.02  ?  100 VAL   A CG2   1 
ATOM   761  N N     . GLU   A 1 101 ? 4.371  -17.872 -0.420  1.00 51.12  ?  101 GLU   A N     1 
ATOM   762  C CA    . GLU   A 1 101 ? 3.445  -16.842 -0.867  1.00 52.56  ?  101 GLU   A CA    1 
ATOM   763  C C     . GLU   A 1 101 ? 3.202  -17.031 -2.358  1.00 59.80  ?  101 GLU   A C     1 
ATOM   764  O O     . GLU   A 1 101 ? 4.025  -16.626 -3.184  1.00 58.15  ?  101 GLU   A O     1 
ATOM   765  C CB    . GLU   A 1 101 ? 4.016  -15.457 -0.584  1.00 56.24  ?  101 GLU   A CB    1 
ATOM   766  C CG    . GLU   A 1 101 ? 3.714  -14.940 0.799   1.00 55.82  ?  101 GLU   A CG    1 
ATOM   767  C CD    . GLU   A 1 101 ? 4.474  -13.680 1.136   1.00 59.47  ?  101 GLU   A CD    1 
ATOM   768  O OE1   . GLU   A 1 101 ? 4.927  -13.571 2.303   1.00 55.05  ?  101 GLU   A OE1   1 
ATOM   769  O OE2   . GLU   A 1 101 ? 4.609  -12.799 0.250   1.00 56.68  ?  101 GLU   A OE2   1 
ATOM   770  N N     . LEU   A 1 102 ? 2.076  -17.641 -2.710  1.00 61.26  ?  102 LEU   A N     1 
ATOM   771  C CA    . LEU   A 1 102 ? 1.745  -17.753 -4.123  1.00 59.67  ?  102 LEU   A CA    1 
ATOM   772  C C     . LEU   A 1 102 ? 1.284  -16.412 -4.672  1.00 56.99  ?  102 LEU   A C     1 
ATOM   773  O O     . LEU   A 1 102 ? 0.861  -15.517 -3.938  1.00 56.65  ?  102 LEU   A O     1 
ATOM   774  C CB    . LEU   A 1 102 ? 0.659  -18.797 -4.350  1.00 56.30  ?  102 LEU   A CB    1 
ATOM   775  C CG    . LEU   A 1 102 ? 0.919  -20.074 -3.573  1.00 54.76  ?  102 LEU   A CG    1 
ATOM   776  C CD1   . LEU   A 1 102 ? -0.291 -20.973 -3.635  1.00 61.07  ?  102 LEU   A CD1   1 
ATOM   777  C CD2   . LEU   A 1 102 ? 2.124  -20.758 -4.151  1.00 49.90  ?  102 LEU   A CD2   1 
ATOM   778  N N     . ARG   A 1 103 ? 1.298  -16.321 -5.997  1.00 59.94  ?  103 ARG   A N     1 
ATOM   779  C CA    . ARG   A 1 103 ? 0.853  -15.099 -6.713  1.00 62.53  ?  103 ARG   A CA    1 
ATOM   780  C C     . ARG   A 1 103 ? 1.597  -13.873 -6.178  1.00 63.18  ?  103 ARG   A C     1 
ATOM   781  O O     . ARG   A 1 103 ? 1.059  -12.768 -6.290  1.00 71.93  ?  103 ARG   A O     1 
ATOM   782  C CB    . ARG   A 1 103 ? -0.674 -15.000 -6.679  1.00 67.31  ?  103 ARG   A CB    1 
ATOM   783  C CG    . ARG   A 1 103 ? -1.378 -16.299 -7.035  1.00 67.96  ?  103 ARG   A CG    1 
ATOM   784  C CD    . ARG   A 1 103 ? -2.797 -16.301 -6.506  1.00 71.86  ?  103 ARG   A CD    1 
ATOM   785  N NE    . ARG   A 1 103 ? -3.733 -15.777 -7.504  1.00 87.06  ?  103 ARG   A NE    1 
ATOM   786  C CZ    . ARG   A 1 103 ? -4.294 -16.504 -8.461  1.00 84.15  ?  103 ARG   A CZ    1 
ATOM   787  N NH1   . ARG   A 1 103 ? -4.617 -17.763 -8.231  1.00 82.17  ?  103 ARG   A NH1   1 
ATOM   788  N NH2   . ARG   A 1 103 ? -4.536 -15.970 -9.642  1.00 77.06  ?  103 ARG   A NH2   1 
ATOM   789  N N     . THR   A 1 104 ? 2.804  -14.075 -5.667  1.00 62.03  ?  104 THR   A N     1 
ATOM   790  C CA    . THR   A 1 104 ? 3.613  -12.941 -5.188  1.00 61.57  ?  104 THR   A CA    1 
ATOM   791  C C     . THR   A 1 104 ? 4.880  -12.883 -6.004  1.00 59.56  ?  104 THR   A C     1 
ATOM   792  O O     . THR   A 1 104 ? 5.752  -13.724 -5.784  1.00 56.78  ?  104 THR   A O     1 
ATOM   793  C CB    . THR   A 1 104 ? 3.862  -13.083 -3.689  1.00 62.25  ?  104 THR   A CB    1 
ATOM   794  O OG1   . THR   A 1 104 ? 2.687  -13.663 -3.136  1.00 55.54  ?  104 THR   A OG1   1 
ATOM   795  C CG2   . THR   A 1 104 ? 4.124  -11.743 -3.027  1.00 64.29  ?  104 THR   A CG2   1 
ATOM   796  N N     . GLU   A 1 105 ? 4.987  -11.906 -6.901  1.00 63.91  ?  105 GLU   A N     1 
ATOM   797  C CA    . GLU   A 1 105 ? 6.145  -11.812 -7.823  1.00 62.35  ?  105 GLU   A CA    1 
ATOM   798  C C     . GLU   A 1 105 ? 7.187  -10.801 -7.340  1.00 60.55  ?  105 GLU   A C     1 
ATOM   799  O O     . GLU   A 1 105 ? 6.817  -9.651  -7.094  1.00 60.96  ?  105 GLU   A O     1 
ATOM   800  C CB    . GLU   A 1 105 ? 5.607  -11.358 -9.171  1.00 65.94  ?  105 GLU   A CB    1 
ATOM   801  C CG    . GLU   A 1 105 ? 6.687  -11.029 -10.195 1.00 68.52  ?  105 GLU   A CG    1 
ATOM   802  C CD    . GLU   A 1 105 ? 6.103  -10.286 -11.380 1.00 78.01  ?  105 GLU   A CD    1 
ATOM   803  O OE1   . GLU   A 1 105 ? 5.126  -9.540  -11.175 1.00 77.09  ?  105 GLU   A OE1   1 
ATOM   804  O OE2   . GLU   A 1 105 ? 6.612  -10.461 -12.503 1.00 82.42  ?  105 GLU   A OE2   1 
ATOM   805  N N     . VAL   A 1 106 ? 8.447  -11.222 -7.253  1.00 59.37  ?  106 VAL   A N     1 
ATOM   806  C CA    . VAL   A 1 106 ? 9.552  -10.326 -6.798  1.00 62.97  ?  106 VAL   A CA    1 
ATOM   807  C C     . VAL   A 1 106 ? 9.883  -9.380  -7.953  1.00 57.45  ?  106 VAL   A C     1 
ATOM   808  O O     . VAL   A 1 106 ? 9.941  -9.846  -9.099  1.00 57.22  ?  106 VAL   A O     1 
ATOM   809  C CB    . VAL   A 1 106 ? 10.802 -11.067 -6.283  1.00 56.33  ?  106 VAL   A CB    1 
ATOM   810  C CG1   . VAL   A 1 106 ? 11.929 -10.107 -5.930  1.00 50.32  ?  106 VAL   A CG1   1 
ATOM   811  C CG2   . VAL   A 1 106 ? 10.474 -11.966 -5.101  1.00 48.77  ?  106 VAL   A CG2   1 
ATOM   812  N N     . VAL   A 1 107 ? 10.092 -8.107  -7.644  1.00 56.57  ?  107 VAL   A N     1 
ATOM   813  C CA    . VAL   A 1 107 ? 10.299 -7.120  -8.693  1.00 56.06  ?  107 VAL   A CA    1 
ATOM   814  C C     . VAL   A 1 107 ? 11.655 -6.434  -8.548  1.00 59.10  ?  107 VAL   A C     1 
ATOM   815  O O     . VAL   A 1 107 ? 12.228 -5.962  -9.543  1.00 51.46  ?  107 VAL   A O     1 
ATOM   816  C CB    . VAL   A 1 107 ? 9.142  -6.100  -8.705  1.00 57.99  ?  107 VAL   A CB    1 
ATOM   817  C CG1   . VAL   A 1 107 ? 7.801  -6.810  -8.556  1.00 63.00  ?  107 VAL   A CG1   1 
ATOM   818  C CG2   . VAL   A 1 107 ? 9.314  -5.024  -7.652  1.00 59.86  ?  107 VAL   A CG2   1 
ATOM   819  N N     . SER   A 1 108 ? 12.189 -6.383  -7.321  1.00 58.53  ?  108 SER   A N     1 
ATOM   820  C CA    . SER   A 1 108 ? 13.437 -5.670  -7.062  1.00 55.15  ?  108 SER   A CA    1 
ATOM   821  C C     . SER   A 1 108 ? 14.202 -6.322  -5.922  1.00 53.30  ?  108 SER   A C     1 
ATOM   822  O O     . SER   A 1 108 ? 13.609 -6.885  -5.001  1.00 58.57  ?  108 SER   A O     1 
ATOM   823  C CB    . SER   A 1 108 ? 13.203 -4.198  -6.723  1.00 50.64  ?  108 SER   A CB    1 
ATOM   824  O OG    . SER   A 1 108 ? 14.452 -3.542  -6.690  1.00 52.28  ?  108 SER   A OG    1 
ATOM   825  N N     . VAL   A 1 109 ? 15.530 -6.230  -5.989  1.00 55.19  ?  109 VAL   A N     1 
ATOM   826  C CA    . VAL   A 1 109 ? 16.429 -6.779  -4.972  1.00 52.48  ?  109 VAL   A CA    1 
ATOM   827  C C     . VAL   A 1 109 ? 17.712 -5.961  -4.985  1.00 54.22  ?  109 VAL   A C     1 
ATOM   828  O O     . VAL   A 1 109 ? 18.377 -5.860  -6.023  1.00 55.72  ?  109 VAL   A O     1 
ATOM   829  C CB    . VAL   A 1 109 ? 16.745 -8.268  -5.214  1.00 47.92  ?  109 VAL   A CB    1 
ATOM   830  C CG1   . VAL   A 1 109 ? 18.022 -8.634  -4.528  1.00 41.76  ?  109 VAL   A CG1   1 
ATOM   831  C CG2   . VAL   A 1 109 ? 15.620 -9.171  -4.738  1.00 46.72  ?  109 VAL   A CG2   1 
ATOM   832  N N     . ARG   A 1 110 ? 18.074 -5.385  -3.838  1.00 52.66  ?  110 ARG   A N     1 
ATOM   833  C CA    . ARG   A 1 110 ? 19.210 -4.478  -3.729  1.00 54.19  ?  110 ARG   A CA    1 
ATOM   834  C C     . ARG   A 1 110 ? 19.934 -4.675  -2.400  1.00 55.41  ?  110 ARG   A C     1 
ATOM   835  O O     . ARG   A 1 110 ? 19.297 -4.793  -1.347  1.00 64.86  ?  110 ARG   A O     1 
ATOM   836  C CB    . ARG   A 1 110 ? 18.753 -3.022  -3.872  1.00 55.98  ?  110 ARG   A CB    1 
ATOM   837  C CG    . ARG   A 1 110 ? 19.711 -2.168  -4.675  1.00 62.81  ?  110 ARG   A CG    1 
ATOM   838  C CD    . ARG   A 1 110 ? 19.201 -0.749  -4.810  1.00 66.84  ?  110 ARG   A CD    1 
ATOM   839  N NE    . ARG   A 1 110 ? 17.930 -0.675  -5.526  1.00 70.81  ?  110 ARG   A NE    1 
ATOM   840  C CZ    . ARG   A 1 110 ? 17.825 -0.550  -6.849  1.00 70.95  ?  110 ARG   A CZ    1 
ATOM   841  N NH1   . ARG   A 1 110 ? 18.925 -0.498  -7.595  1.00 69.38  ?  110 ARG   A NH1   1 
ATOM   842  N NH2   . ARG   A 1 110 ? 16.625 -0.478  -7.425  1.00 69.43  ?  110 ARG   A NH2   1 
ATOM   843  N N     . GLN   A 1 111 ? 21.265 -4.700  -2.446  1.00 54.69  ?  111 GLN   A N     1 
ATOM   844  C CA    . GLN   A 1 111 ? 22.077 -4.874  -1.246  1.00 56.08  ?  111 GLN   A CA    1 
ATOM   845  C C     . GLN   A 1 111 ? 22.277 -3.543  -0.520  1.00 60.38  ?  111 GLN   A C     1 
ATOM   846  O O     . GLN   A 1 111 ? 22.642 -2.528  -1.135  1.00 58.81  ?  111 GLN   A O     1 
ATOM   847  C CB    . GLN   A 1 111 ? 23.424 -5.489  -1.609  1.00 52.31  ?  111 GLN   A CB    1 
ATOM   848  C CG    . GLN   A 1 111 ? 24.483 -5.241  -0.592  1.00 55.47  ?  111 GLN   A CG    1 
ATOM   849  C CD    . GLN   A 1 111 ? 25.365 -6.443  -0.379  1.00 59.30  ?  111 GLN   A CD    1 
ATOM   850  O OE1   . GLN   A 1 111 ? 25.040 -7.328  0.423   1.00 55.48  ?  111 GLN   A OE1   1 
ATOM   851  N NE2   . GLN   A 1 111 ? 26.499 -6.483  -1.090  1.00 57.87  ?  111 GLN   A NE2   1 
ATOM   852  N N     . ASP   A 1 112 ? 22.049 -3.552  0.794   1.00 54.43  ?  112 ASP   A N     1 
ATOM   853  C CA    . ASP   A 1 112 ? 22.166 -2.342  1.598   1.00 57.61  ?  112 ASP   A CA    1 
ATOM   854  C C     . ASP   A 1 112 ? 23.547 -2.220  2.205   1.00 58.89  ?  112 ASP   A C     1 
ATOM   855  O O     . ASP   A 1 112 ? 24.195 -3.216  2.536   1.00 63.63  ?  112 ASP   A O     1 
ATOM   856  C CB    . ASP   A 1 112 ? 21.128 -2.319  2.706   1.00 56.12  ?  112 ASP   A CB    1 
ATOM   857  C CG    . ASP   A 1 112 ? 19.788 -1.885  2.209   1.00 62.76  ?  112 ASP   A CG    1 
ATOM   858  O OD1   . ASP   A 1 112 ? 19.749 -1.010  1.310   1.00 68.68  ?  112 ASP   A OD1   1 
ATOM   859  O OD2   . ASP   A 1 112 ? 18.783 -2.442  2.694   1.00 58.98  ?  112 ASP   A OD2   1 
ATOM   860  N N     . ALA   A 1 113 ? 23.985 -0.978  2.371   1.00 59.18  ?  113 ALA   A N     1 
ATOM   861  C CA    . ALA   A 1 113 ? 25.352 -0.741  2.813   1.00 60.56  ?  113 ALA   A CA    1 
ATOM   862  C C     . ALA   A 1 113 ? 25.688 -1.513  4.093   1.00 58.96  ?  113 ALA   A C     1 
ATOM   863  O O     . ALA   A 1 113 ? 26.840 -1.905  4.290   1.00 59.37  ?  113 ALA   A O     1 
ATOM   864  C CB    . ALA   A 1 113 ? 25.574 0.761   2.988   1.00 52.55  ?  113 ALA   A CB    1 
ATOM   865  N N     . ASP   A 1 114 ? 24.707 -1.798  4.939   1.00 58.94  ?  114 ASP   A N     1 
ATOM   866  C CA    . ASP   A 1 114 ? 25.007 -2.427  6.217   1.00 59.62  ?  114 ASP   A CA    1 
ATOM   867  C C     . ASP   A 1 114 ? 24.888 -3.946  6.212   1.00 61.80  ?  114 ASP   A C     1 
ATOM   868  O O     . ASP   A 1 114 ? 25.049 -4.563  7.274   1.00 62.29  ?  114 ASP   A O     1 
ATOM   869  C CB    . ASP   A 1 114 ? 24.106 -1.856  7.318   1.00 65.97  ?  114 ASP   A CB    1 
ATOM   870  C CG    . ASP   A 1 114 ? 22.695 -2.411  7.273   1.00 69.66  ?  114 ASP   A CG    1 
ATOM   871  O OD1   . ASP   A 1 114 ? 21.996 -2.219  6.250   1.00 68.56  ?  114 ASP   A OD1   1 
ATOM   872  O OD2   . ASP   A 1 114 ? 22.286 -3.045  8.273   1.00 74.04  ?  114 ASP   A OD2   1 
ATOM   873  N N     . GLY   A 1 115 ? 24.596 -4.576  5.077   1.00 58.86  ?  115 GLY   A N     1 
ATOM   874  C CA    . GLY   A 1 115 ? 24.616 -6.020  5.040   1.00 56.77  ?  115 GLY   A CA    1 
ATOM   875  C C     . GLY   A 1 115 ? 23.328 -6.714  4.634   1.00 56.72  ?  115 GLY   A C     1 
ATOM   876  O O     . GLY   A 1 115 ? 23.335 -7.625  3.807   1.00 55.63  ?  115 GLY   A O     1 
ATOM   877  N N     . PRO   A 1 116 ? 22.203 -6.358  5.233   1.00 60.61  ?  116 PRO   A N     1 
ATOM   878  C CA    . PRO   A 1 116 ? 20.944 -6.984  4.819   1.00 60.01  ?  116 PRO   A CA    1 
ATOM   879  C C     . PRO   A 1 116 ? 20.543 -6.524  3.424   1.00 52.15  ?  116 PRO   A C     1 
ATOM   880  O O     . PRO   A 1 116 ? 21.091 -5.572  2.867   1.00 52.74  ?  116 PRO   A O     1 
ATOM   881  C CB    . PRO   A 1 116 ? 19.945 -6.515  5.889   1.00 58.22  ?  116 PRO   A CB    1 
ATOM   882  C CG    . PRO   A 1 116 ? 20.778 -6.169  7.041   1.00 59.80  ?  116 PRO   A CG    1 
ATOM   883  C CD    . PRO   A 1 116 ? 22.015 -5.568  6.457   1.00 58.31  ?  116 PRO   A CD    1 
ATOM   884  N N     . TRP   A 1 117 ? 19.531 -7.200  2.885   1.00 54.67  ?  117 TRP   A N     1 
ATOM   885  C CA    . TRP   A 1 117 ? 19.050 -6.915  1.520   1.00 55.40  ?  117 TRP   A CA    1 
ATOM   886  C C     . TRP   A 1 117 ? 17.601 -6.448  1.571   1.00 57.32  ?  117 TRP   A C     1 
ATOM   887  O O     . TRP   A 1 117 ? 16.875 -6.873  2.470   1.00 55.33  ?  117 TRP   A O     1 
ATOM   888  C CB    . TRP   A 1 117 ? 19.152 -8.193  0.686   1.00 52.60  ?  117 TRP   A CB    1 
ATOM   889  C CG    . TRP   A 1 117 ? 20.530 -8.776  0.530   1.00 53.50  ?  117 TRP   A CG    1 
ATOM   890  C CD1   . TRP   A 1 117 ? 21.269 -9.430  1.469   1.00 51.11  ?  117 TRP   A CD1   1 
ATOM   891  C CD2   . TRP   A 1 117 ? 21.314 -8.795  -0.680  1.00 59.54  ?  117 TRP   A CD2   1 
ATOM   892  N NE1   . TRP   A 1 117 ? 22.463 -9.832  0.938   1.00 53.69  ?  117 TRP   A NE1   1 
ATOM   893  C CE2   . TRP   A 1 117 ? 22.518 -9.462  -0.378  1.00 58.03  ?  117 TRP   A CE2   1 
ATOM   894  C CE3   . TRP   A 1 117 ? 21.117 -8.313  -1.977  1.00 55.92  ?  117 TRP   A CE3   1 
ATOM   895  C CZ2   . TRP   A 1 117 ? 23.516 -9.655  -1.326  1.00 54.27  ?  117 TRP   A CZ2   1 
ATOM   896  C CZ3   . TRP   A 1 117 ? 22.105 -8.507  -2.913  1.00 51.36  ?  117 TRP   A CZ3   1 
ATOM   897  C CH2   . TRP   A 1 117 ? 23.286 -9.169  -2.590  1.00 53.07  ?  117 TRP   A CH2   1 
ATOM   898  N N     . THR   A 1 118 ? 17.196 -5.618  0.611   1.00 55.86  ?  118 THR   A N     1 
ATOM   899  C CA    . THR   A 1 118 ? 15.817 -5.101  0.571   1.00 53.96  ?  118 THR   A CA    1 
ATOM   900  C C     . THR   A 1 118 ? 15.101 -5.664  -0.644  1.00 56.10  ?  118 THR   A C     1 
ATOM   901  O O     . THR   A 1 118 ? 15.521 -5.361  -1.767  1.00 51.06  ?  118 THR   A O     1 
ATOM   902  C CB    . THR   A 1 118 ? 15.837 -3.573  0.614   1.00 54.68  ?  118 THR   A CB    1 
ATOM   903  O OG1   . THR   A 1 118 ? 16.311 -3.222  1.908   1.00 55.51  ?  118 THR   A OG1   1 
ATOM   904  C CG2   . THR   A 1 118 ? 14.465 -2.963  0.399   1.00 55.69  ?  118 THR   A CG2   1 
ATOM   905  N N     . VAL   A 1 119 ? 14.060 -6.472  -0.423  1.00 55.78  ?  119 VAL   A N     1 
ATOM   906  C CA    . VAL   A 1 119 ? 13.296 -7.134  -1.519  1.00 52.91  ?  119 VAL   A CA    1 
ATOM   907  C C     . VAL   A 1 119 ? 11.930 -6.452  -1.676  1.00 60.45  ?  119 VAL   A C     1 
ATOM   908  O O     . VAL   A 1 119 ? 11.203 -6.349  -0.675  1.00 63.41  ?  119 VAL   A O     1 
ATOM   909  C CB    . VAL   A 1 119 ? 13.129 -8.637  -1.237  1.00 52.67  ?  119 VAL   A CB    1 
ATOM   910  C CG1   . VAL   A 1 119 ? 12.251 -9.327  -2.270  1.00 47.99  ?  119 VAL   A CG1   1 
ATOM   911  C CG2   . VAL   A 1 119 ? 14.470 -9.342  -1.095  1.00 51.05  ?  119 VAL   A CG2   1 
ATOM   912  N N     . VAL   A 1 120 ? 11.612 -6.000  -2.886  1.00 54.89  ?  120 VAL   A N     1 
ATOM   913  C CA    . VAL   A 1 120 ? 10.299 -5.361  -3.164  1.00 57.16  ?  120 VAL   A CA    1 
ATOM   914  C C     . VAL   A 1 120 ? 9.475  -6.352  -3.984  1.00 63.08  ?  120 VAL   A C     1 
ATOM   915  O O     . VAL   A 1 120 ? 9.942  -6.772  -5.047  1.00 59.68  ?  120 VAL   A O     1 
ATOM   916  C CB    . VAL   A 1 120 ? 10.457 -4.029  -3.912  1.00 59.10  ?  120 VAL   A CB    1 
ATOM   917  C CG1   . VAL   A 1 120 ? 9.128  -3.298  -4.033  1.00 67.16  ?  120 VAL   A CG1   1 
ATOM   918  C CG2   . VAL   A 1 120 ? 11.501 -3.137  -3.257  1.00 60.39  ?  120 VAL   A CG2   1 
ATOM   919  N N     . SER   A 1 121 ? 8.298  -6.708  -3.491  1.00 65.16  ?  121 SER   A N     1 
ATOM   920  C CA    . SER   A 1 121 ? 7.485  -7.730  -4.183  1.00 65.47  ?  121 SER   A CA    1 
ATOM   921  C C     . SER   A 1 121 ? 6.101  -7.183  -4.503  1.00 72.80  ?  121 SER   A C     1 
ATOM   922  O O     . SER   A 1 121 ? 5.518  -6.518  -3.635  1.00 74.02  ?  121 SER   A O     1 
ATOM   923  C CB    . SER   A 1 121 ? 7.357  -8.958  -3.345  1.00 62.68  ?  121 SER   A CB    1 
ATOM   924  O OG    . SER   A 1 121 ? 6.924  -8.635  -2.034  1.00 59.03  ?  121 SER   A OG    1 
ATOM   925  N N     . ARG   A 1 122 ? 5.628  -7.409  -5.723  1.00 74.59  ?  122 ARG   A N     1 
ATOM   926  C CA    . ARG   A 1 122 ? 4.253  -7.066  -6.034  1.00 82.45  ?  122 ARG   A CA    1 
ATOM   927  C C     . ARG   A 1 122 ? 3.396  -8.327  -5.981  1.00 85.61  ?  122 ARG   A C     1 
ATOM   928  O O     . ARG   A 1 122 ? 3.834  -9.411  -6.382  1.00 81.77  ?  122 ARG   A O     1 
ATOM   929  C CB    . ARG   A 1 122 ? 4.138  -6.371  -7.395  1.00 79.73  ?  122 ARG   A CB    1 
ATOM   930  C CG    . ARG   A 1 122 ? 4.108  -7.266  -8.605  1.00 84.15  ?  122 ARG   A CG    1 
ATOM   931  C CD    . ARG   A 1 122 ? 3.452  -6.532  -9.770  1.00 91.38  ?  122 ARG   A CD    1 
ATOM   932  N NE    . ARG   A 1 122 ? 3.927  -6.997  -11.067 1.00 84.17  ?  122 ARG   A NE    1 
ATOM   933  C CZ    . ARG   A 1 122 ? 4.626  -6.239  -11.904 1.00 88.52  ?  122 ARG   A CZ    1 
ATOM   934  N NH1   . ARG   A 1 122 ? 4.925  -4.987  -11.562 1.00 83.61  ?  122 ARG   A NH1   1 
ATOM   935  N NH2   . ARG   A 1 122 ? 5.029  -6.730  -13.073 1.00 89.79  ?  122 ARG   A NH2   1 
ATOM   936  N N     . GLY   A 1 123 ? 2.181  -8.181  -5.456  1.00 89.85  ?  123 GLY   A N     1 
ATOM   937  C CA    . GLY   A 1 123 ? 1.326  -9.325  -5.177  1.00 89.60  ?  123 GLY   A CA    1 
ATOM   938  C C     . GLY   A 1 123 ? 0.119  -9.484  -6.086  1.00 102.05 ?  123 GLY   A C     1 
ATOM   939  O O     . GLY   A 1 123 ? 0.168  -9.146  -7.280  1.00 96.32  ?  123 GLY   A O     1 
ATOM   940  N N     . ALA   A 1 124 ? -1.034 -9.885  -5.544  1.00 100.55 ?  124 ALA   A N     1 
ATOM   941  C CA    . ALA   A 1 124 ? -2.210 -10.134 -6.417  1.00 100.83 ?  124 ALA   A CA    1 
ATOM   942  C C     . ALA   A 1 124 ? -2.983 -8.836  -6.671  1.00 101.72 ?  124 ALA   A C     1 
ATOM   943  O O     . ALA   A 1 124 ? -3.586 -8.703  -7.752  1.00 102.78 ?  124 ALA   A O     1 
ATOM   944  C CB    . ALA   A 1 124 ? -3.091 -11.195 -5.805  1.00 93.98  ?  124 ALA   A CB    1 
ATOM   945  N N     . ASP   A 1 125 ? -2.950 -7.900  -5.723  1.00 99.69  ?  125 ASP   A N     1 
ATOM   946  C CA    . ASP   A 1 125 ? -3.667 -6.604  -5.864  1.00 99.20  ?  125 ASP   A CA    1 
ATOM   947  C C     . ASP   A 1 125 ? -2.926 -5.670  -6.828  1.00 102.68 ?  125 ASP   A C     1 
ATOM   948  O O     . ASP   A 1 125 ? -3.326 -4.495  -6.908  1.00 94.34  ?  125 ASP   A O     1 
ATOM   949  C CB    . ASP   A 1 125 ? -3.810 -5.956  -4.501  1.00 97.71  ?  125 ASP   A CB    1 
ATOM   950  C CG    . ASP   A 1 125 ? -2.926 -6.548  -3.416  1.00 96.53  ?  125 ASP   A CG    1 
ATOM   951  O OD1   . ASP   A 1 125 ? -1.692 -6.410  -3.524  1.00 95.76  ?  125 ASP   A OD1   1 
ATOM   952  O OD2   . ASP   A 1 125 ? -3.483 -7.149  -2.478  1.00 95.29  ?  125 ASP   A OD2   1 
ATOM   953  N N     . GLY   A 1 126 ? -1.881 -6.154  -7.512  1.00 104.27 ?  126 GLY   A N     1 
ATOM   954  C CA    . GLY   A 1 126 ? -1.053 -5.322  -8.411  1.00 97.43  ?  126 GLY   A CA    1 
ATOM   955  C C     . GLY   A 1 126 ? -0.309 -4.272  -7.623  1.00 94.66  ?  126 GLY   A C     1 
ATOM   956  O O     . GLY   A 1 126 ? 0.246  -3.355  -8.248  1.00 90.91  ?  126 GLY   A O     1 
ATOM   957  N N     . ALA   A 1 127 ? -0.269 -4.415  -6.300  1.00 98.38  ?  127 ALA   A N     1 
ATOM   958  C CA    . ALA   A 1 127 ? 0.318  -3.375  -5.432  1.00 95.54  ?  127 ALA   A CA    1 
ATOM   959  C C     . ALA   A 1 127 ? 1.747  -3.728  -5.040  1.00 94.59  ?  127 ALA   A C     1 
ATOM   960  O O     . ALA   A 1 127 ? 2.277  -4.709  -5.570  1.00 94.90  ?  127 ALA   A O     1 
ATOM   961  C CB    . ALA   A 1 127 ? -0.545 -3.242  -4.216  1.00 97.68  ?  127 ALA   A CB    1 
ATOM   962  N N     . GLN   A 1 128 ? 2.323  -2.982  -4.097  1.00 89.40  ?  128 GLN   A N     1 
ATOM   963  C CA    . GLN   A 1 128 ? 3.752  -3.194  -3.778  1.00 84.85  ?  128 GLN   A CA    1 
ATOM   964  C C     . GLN   A 1 128 ? 4.056  -3.124  -2.280  1.00 82.56  ?  128 GLN   A C     1 
ATOM   965  O O     . GLN   A 1 128 ? 3.326  -2.418  -1.567  1.00 80.51  ?  128 GLN   A O     1 
ATOM   966  C CB    . GLN   A 1 128 ? 4.537  -2.090  -4.481  1.00 86.70  ?  128 GLN   A CB    1 
ATOM   967  C CG    . GLN   A 1 128 ? 4.436  -2.113  -6.002  1.00 93.58  ?  128 GLN   A CG    1 
ATOM   968  C CD    . GLN   A 1 128 ? 5.779  -2.095  -6.695  1.00 89.34  ?  128 GLN   A CD    1 
ATOM   969  O OE1   . GLN   A 1 128 ? 6.708  -1.400  -6.275  1.00 95.69  ?  128 GLN   A OE1   1 
ATOM   970  N NE2   . GLN   A 1 128 ? 5.890  -2.857  -7.772  1.00 86.20  ?  128 GLN   A NE2   1 
ATOM   971  N N     . VAL   A 1 129 ? 5.096  -3.833  -1.840  1.00 76.45  ?  129 VAL   A N     1 
ATOM   972  C CA    . VAL   A 1 129 ? 5.566  -3.806  -0.457  1.00 71.01  ?  129 VAL   A CA    1 
ATOM   973  C C     . VAL   A 1 129 ? 7.070  -4.005  -0.454  1.00 70.33  ?  129 VAL   A C     1 
ATOM   974  O O     . VAL   A 1 129 ? 7.601  -4.814  -1.221  1.00 70.03  ?  129 VAL   A O     1 
ATOM   975  C CB    . VAL   A 1 129 ? 4.892  -4.887  0.404   1.00 74.19  ?  129 VAL   A CB    1 
ATOM   976  C CG1   . VAL   A 1 129 ? 3.542  -4.407  0.885   1.00 78.40  ?  129 VAL   A CG1   1 
ATOM   977  C CG2   . VAL   A 1 129 ? 4.771  -6.176  -0.385  1.00 74.30  ?  129 VAL   A CG2   1 
ATOM   978  N N     . SER   A 1 130 ? 7.754  -3.282  0.427   1.00 67.12  ?  130 SER   A N     1 
ATOM   979  C CA    . SER   A 1 130 ? 9.199  -3.387  0.568   1.00 67.60  ?  130 SER   A CA    1 
ATOM   980  C C     . SER   A 1 130 ? 9.543  -4.091  1.880   1.00 68.32  ?  130 SER   A C     1 
ATOM   981  O O     . SER   A 1 130 ? 8.851  -3.905  2.885   1.00 69.04  ?  130 SER   A O     1 
ATOM   982  C CB    . SER   A 1 130 ? 9.840  -2.000  0.517   1.00 68.29  ?  130 SER   A CB    1 
ATOM   983  O OG    . SER   A 1 130 ? 11.143 -2.016  1.073   1.00 70.37  ?  130 SER   A OG    1 
ATOM   984  N N     . ARG   A 1 131 ? 10.606 -4.907  1.869   1.00 64.09  ?  131 ARG   A N     1 
ATOM   985  C CA    . ARG   A 1 131 ? 10.974 -5.719  3.028   1.00 61.32  ?  131 ARG   A CA    1 
ATOM   986  C C     . ARG   A 1 131 ? 12.492 -5.876  3.112   1.00 56.40  ?  131 ARG   A C     1 
ATOM   987  O O     . ARG   A 1 131 ? 13.214 -5.610  2.155   1.00 60.94  ?  131 ARG   A O     1 
ATOM   988  C CB    . ARG   A 1 131 ? 10.309 -7.101  2.974   1.00 59.52  ?  131 ARG   A CB    1 
ATOM   989  C CG    . ARG   A 1 131 ? 8.795  -7.081  3.013   1.00 58.27  ?  131 ARG   A CG    1 
ATOM   990  C CD    . ARG   A 1 131 ? 8.227  -8.491  2.910   1.00 65.25  ?  131 ARG   A CD    1 
ATOM   991  N NE    . ARG   A 1 131 ? 7.873  -8.887  1.541   1.00 63.45  ?  131 ARG   A NE    1 
ATOM   992  C CZ    . ARG   A 1 131 ? 7.094  -9.930  1.250   1.00 60.71  ?  131 ARG   A CZ    1 
ATOM   993  N NH1   . ARG   A 1 131 ? 6.594  -10.674 2.229   1.00 50.67  ?  131 ARG   A NH1   1 
ATOM   994  N NH2   . ARG   A 1 131 ? 6.811  -10.234 -0.017  1.00 63.00  ?  131 ARG   A NH2   1 
ATOM   995  N N     . ARG   A 1 132 ? 12.970 -6.344  4.271   1.00 55.97  ?  132 ARG   A N     1 
ATOM   996  C CA    . ARG   A 1 132 ? 14.390 -6.559  4.533   1.00 57.84  ?  132 ARG   A CA    1 
ATOM   997  C C     . ARG   A 1 132 ? 14.632 -7.986  5.003   1.00 55.64  ?  132 ARG   A C     1 
ATOM   998  O O     . ARG   A 1 132 ? 13.833 -8.535  5.767   1.00 56.81  ?  132 ARG   A O     1 
ATOM   999  C CB    . ARG   A 1 132 ? 14.934 -5.582  5.593   1.00 63.45  ?  132 ARG   A CB    1 
ATOM   1000 C CG    . ARG   A 1 132 ? 15.932 -4.563  5.064   1.00 61.56  ?  132 ARG   A CG    1 
ATOM   1001 C CD    . ARG   A 1 132 ? 16.071 -3.358  5.995   1.00 68.99  ?  132 ARG   A CD    1 
ATOM   1002 N NE    . ARG   A 1 132 ? 17.218 -3.438  6.908   1.00 74.88  ?  132 ARG   A NE    1 
ATOM   1003 C CZ    . ARG   A 1 132 ? 18.460 -3.057  6.601   1.00 73.33  ?  132 ARG   A CZ    1 
ATOM   1004 N NH1   . ARG   A 1 132 ? 18.736 -2.565  5.400   1.00 69.34  ?  132 ARG   A NH1   1 
ATOM   1005 N NH2   . ARG   A 1 132 ? 19.431 -3.156  7.505   1.00 73.69  ?  132 ARG   A NH2   1 
ATOM   1006 N N     . PHE   A 1 133 ? 15.750 -8.570  4.557   1.00 56.03  ?  133 PHE   A N     1 
ATOM   1007 C CA    . PHE   A 1 133 ? 16.116 -9.949  4.859   1.00 51.78  ?  133 PHE   A CA    1 
ATOM   1008 C C     . PHE   A 1 133 ? 17.617 -10.066 5.058   1.00 50.78  ?  133 PHE   A C     1 
ATOM   1009 O O     . PHE   A 1 133 ? 18.405 -9.268  4.541   1.00 46.47  ?  133 PHE   A O     1 
ATOM   1010 C CB    . PHE   A 1 133 ? 15.734 -10.924 3.743   1.00 53.61  ?  133 PHE   A CB    1 
ATOM   1011 C CG    . PHE   A 1 133 ? 14.269 -11.081 3.543   1.00 52.52  ?  133 PHE   A CG    1 
ATOM   1012 C CD1   . PHE   A 1 133 ? 13.556 -10.152 2.796   1.00 48.78  ?  133 PHE   A CD1   1 
ATOM   1013 C CD2   . PHE   A 1 133 ? 13.605 -12.175 4.081   1.00 54.01  ?  133 PHE   A CD2   1 
ATOM   1014 C CE1   . PHE   A 1 133 ? 12.207 -10.296 2.596   1.00 51.17  ?  133 PHE   A CE1   1 
ATOM   1015 C CE2   . PHE   A 1 133 ? 12.249 -12.329 3.894   1.00 55.20  ?  133 PHE   A CE2   1 
ATOM   1016 C CZ    . PHE   A 1 133 ? 11.545 -11.386 3.144   1.00 59.93  ?  133 PHE   A CZ    1 
ATOM   1017 N N     . GLU   A 1 134 ? 18.007 -11.123 5.768   1.00 46.53  ?  134 GLU   A N     1 
ATOM   1018 C CA    . GLU   A 1 134 ? 19.419 -11.327 6.050   1.00 49.89  ?  134 GLU   A CA    1 
ATOM   1019 C C     . GLU   A 1 134 ? 20.130 -11.871 4.827   1.00 46.47  ?  134 GLU   A C     1 
ATOM   1020 O O     . GLU   A 1 134 ? 21.113 -11.291 4.360   1.00 46.95  ?  134 GLU   A O     1 
ATOM   1021 C CB    . GLU   A 1 134 ? 19.592 -12.263 7.254   1.00 55.96  ?  134 GLU   A CB    1 
ATOM   1022 C CG    . GLU   A 1 134 ? 21.039 -12.347 7.735   1.00 65.96  ?  134 GLU   A CG    1 
ATOM   1023 C CD    . GLU   A 1 134 ? 21.194 -13.097 9.043   1.00 62.57  ?  134 GLU   A CD    1 
ATOM   1024 O OE1   . GLU   A 1 134 ? 20.763 -12.541 10.084  1.00 67.26  ?  134 GLU   A OE1   1 
ATOM   1025 O OE2   . GLU   A 1 134 ? 21.765 -14.216 9.033   1.00 61.43  ?  134 GLU   A OE2   1 
ATOM   1026 N N     . GLN   A 1 135 ? 19.627 -12.976 4.284   1.00 49.28  ?  135 GLN   A N     1 
ATOM   1027 C CA    . GLN   A 1 135 ? 20.173 -13.568 3.073   1.00 54.74  ?  135 GLN   A CA    1 
ATOM   1028 C C     . GLN   A 1 135 ? 19.071 -13.836 2.056   1.00 55.47  ?  135 GLN   A C     1 
ATOM   1029 O O     . GLN   A 1 135 ? 17.876 -13.849 2.381   1.00 53.40  ?  135 GLN   A O     1 
ATOM   1030 C CB    . GLN   A 1 135 ? 20.938 -14.856 3.382   1.00 53.72  ?  135 GLN   A CB    1 
ATOM   1031 C CG    . GLN   A 1 135 ? 22.355 -14.556 3.781   1.00 53.30  ?  135 GLN   A CG    1 
ATOM   1032 C CD    . GLN   A 1 135 ? 22.881 -15.543 4.766   1.00 54.08  ?  135 GLN   A CD    1 
ATOM   1033 O OE1   . GLN   A 1 135 ? 23.567 -16.488 4.391   1.00 50.34  ?  135 GLN   A OE1   1 
ATOM   1034 N NE2   . GLN   A 1 135 ? 22.545 -15.345 6.048   1.00 46.90  ?  135 GLN   A NE2   1 
ATOM   1035 N N     . VAL   A 1 136 ? 19.503 -14.039 0.807   1.00 49.44  ?  136 VAL   A N     1 
ATOM   1036 C CA    . VAL   A 1 136 ? 18.610 -14.285 -0.323  1.00 50.37  ?  136 VAL   A CA    1 
ATOM   1037 C C     . VAL   A 1 136 ? 19.186 -15.411 -1.179  1.00 51.54  ?  136 VAL   A C     1 
ATOM   1038 O O     . VAL   A 1 136 ? 20.376 -15.392 -1.516  1.00 48.27  ?  136 VAL   A O     1 
ATOM   1039 C CB    . VAL   A 1 136 ? 18.415 -13.019 -1.180  1.00 49.15  ?  136 VAL   A CB    1 
ATOM   1040 C CG1   . VAL   A 1 136 ? 17.467 -13.299 -2.307  1.00 49.58  ?  136 VAL   A CG1   1 
ATOM   1041 C CG2   . VAL   A 1 136 ? 17.885 -11.877 -0.347  1.00 55.04  ?  136 VAL   A CG2   1 
ATOM   1042 N N     . VAL   A 1 137 ? 18.343 -16.386 -1.540  1.00 51.23  ?  137 VAL   A N     1 
ATOM   1043 C CA    . VAL   A 1 137 ? 18.692 -17.421 -2.515  1.00 50.51  ?  137 VAL   A CA    1 
ATOM   1044 C C     . VAL   A 1 137 ? 17.811 -17.249 -3.742  1.00 48.91  ?  137 VAL   A C     1 
ATOM   1045 O O     . VAL   A 1 137 ? 16.578 -17.177 -3.624  1.00 46.99  ?  137 VAL   A O     1 
ATOM   1046 C CB    . VAL   A 1 137 ? 18.544 -18.843 -1.947  1.00 49.01  ?  137 VAL   A CB    1 
ATOM   1047 C CG1   . VAL   A 1 137 ? 19.226 -19.832 -2.878  1.00 40.80  ?  137 VAL   A CG1   1 
ATOM   1048 C CG2   . VAL   A 1 137 ? 19.139 -18.919 -0.559  1.00 47.44  ?  137 VAL   A CG2   1 
ATOM   1049 N N     . VAL   A 1 138 ? 18.449 -17.185 -4.917  1.00 46.61  ?  138 VAL   A N     1 
ATOM   1050 C CA    . VAL   A 1 138 ? 17.753 -17.142 -6.202  1.00 44.31  ?  138 VAL   A CA    1 
ATOM   1051 C C     . VAL   A 1 138 ? 17.518 -18.562 -6.691  1.00 42.59  ?  138 VAL   A C     1 
ATOM   1052 O O     . VAL   A 1 138 ? 18.461 -19.358 -6.783  1.00 44.82  ?  138 VAL   A O     1 
ATOM   1053 C CB    . VAL   A 1 138 ? 18.561 -16.350 -7.238  1.00 44.24  ?  138 VAL   A CB    1 
ATOM   1054 C CG1   . VAL   A 1 138 ? 17.768 -16.213 -8.516  1.00 45.18  ?  138 VAL   A CG1   1 
ATOM   1055 C CG2   . VAL   A 1 138 ? 18.961 -15.000 -6.682  1.00 45.84  ?  138 VAL   A CG2   1 
ATOM   1056 N N     . ALA   A 1 139 ? 16.266 -18.873 -7.023  1.00 42.42  ?  139 ALA   A N     1 
ATOM   1057 C CA    . ALA   A 1 139 ? 15.875 -20.176 -7.561  1.00 40.97  ?  139 ALA   A CA    1 
ATOM   1058 C C     . ALA   A 1 139 ? 14.800 -19.996 -8.638  1.00 45.30  ?  139 ALA   A C     1 
ATOM   1059 O O     . ALA   A 1 139 ? 13.731 -20.605 -8.600  1.00 46.69  ?  139 ALA   A O     1 
ATOM   1060 C CB    . ALA   A 1 139 ? 15.391 -21.093 -6.441  1.00 43.19  ?  139 ALA   A CB    1 
ATOM   1061 N N     . SER   A 1 140 ? 15.094 -19.130 -9.606  1.00 45.08  ?  140 SER   A N     1 
ATOM   1062 C CA    . SER   A 1 140 ? 14.066 -18.677 -10.574 1.00 49.57  ?  140 SER   A CA    1 
ATOM   1063 C C     . SER   A 1 140 ? 14.070 -19.374 -11.940 1.00 50.21  ?  140 SER   A C     1 
ATOM   1064 O O     . SER   A 1 140 ? 13.124 -19.153 -12.697 1.00 50.23  ?  140 SER   A O     1 
ATOM   1065 C CB    . SER   A 1 140 ? 14.279 -17.219 -10.756 1.00 46.70  ?  140 SER   A CB    1 
ATOM   1066 O OG    . SER   A 1 140 ? 15.660 -16.910 -10.713 1.00 45.24  ?  140 SER   A OG    1 
ATOM   1067 N N     . GLY   A 1 141 ? 15.103 -20.133 -12.255 1.00 50.76  ?  141 GLY   A N     1 
ATOM   1068 C CA    . GLY   A 1 141 ? 15.163 -20.824 -13.549 1.00 50.11  ?  141 GLY   A CA    1 
ATOM   1069 C C     . GLY   A 1 141 ? 16.006 -20.083 -14.553 1.00 50.83  ?  141 GLY   A C     1 
ATOM   1070 O O     . GLY   A 1 141 ? 16.386 -18.940 -14.273 1.00 54.01  ?  141 GLY   A O     1 
ATOM   1071 N N     . HIS   A 1 142 ? 16.278 -20.717 -15.688 1.00 57.44  ?  142 HIS   A N     1 
ATOM   1072 C CA    . HIS   A 1 142 ? 17.076 -20.071 -16.766 1.00 63.80  ?  142 HIS   A CA    1 
ATOM   1073 C C     . HIS   A 1 142 ? 16.319 -20.169 -18.106 1.00 59.09  ?  142 HIS   A C     1 
ATOM   1074 O O     . HIS   A 1 142 ? 16.852 -19.715 -19.127 1.00 60.28  ?  142 HIS   A O     1 
ATOM   1075 C CB    . HIS   A 1 142 ? 18.514 -20.609 -16.741 1.00 55.60  ?  142 HIS   A CB    1 
ATOM   1076 C CG    . HIS   A 1 142 ? 18.668 -22.079 -16.616 1.00 56.05  ?  142 HIS   A CG    1 
ATOM   1077 N ND1   . HIS   A 1 142 ? 19.476 -22.649 -15.661 1.00 51.73  ?  142 HIS   A ND1   1 
ATOM   1078 C CD2   . HIS   A 1 142 ? 18.172 -23.084 -17.326 1.00 62.33  ?  142 HIS   A CD2   1 
ATOM   1079 C CE1   . HIS   A 1 142 ? 19.443 -23.963 -15.791 1.00 53.50  ?  142 HIS   A CE1   1 
ATOM   1080 N NE2   . HIS   A 1 142 ? 18.654 -24.249 -16.797 1.00 62.20  ?  142 HIS   A NE2   1 
ATOM   1081 N N     . HIS   A 1 143 ? 15.106 -20.719 -18.099 1.00 57.58  ?  143 HIS   A N     1 
ATOM   1082 C CA    . HIS   A 1 143 ? 14.270 -20.806 -19.324 1.00 55.00  ?  143 HIS   A CA    1 
ATOM   1083 C C     . HIS   A 1 143 ? 13.067 -19.867 -19.194 1.00 55.26  ?  143 HIS   A C     1 
ATOM   1084 O O     . HIS   A 1 143 ? 11.929 -20.336 -19.126 1.00 51.08  ?  143 HIS   A O     1 
ATOM   1085 C CB    . HIS   A 1 143 ? 13.790 -22.237 -19.555 1.00 52.85  ?  143 HIS   A CB    1 
ATOM   1086 C CG    . HIS   A 1 143 ? 14.720 -23.328 -19.171 1.00 60.30  ?  143 HIS   A CG    1 
ATOM   1087 N ND1   . HIS   A 1 143 ? 15.651 -23.856 -20.035 1.00 62.81  ?  143 HIS   A ND1   1 
ATOM   1088 C CD2   . HIS   A 1 143 ? 14.823 -24.026 -18.040 1.00 66.44  ?  143 HIS   A CD2   1 
ATOM   1089 C CE1   . HIS   A 1 143 ? 16.302 -24.828 -19.422 1.00 67.24  ?  143 HIS   A CE1   1 
ATOM   1090 N NE2   . HIS   A 1 143 ? 15.814 -24.952 -18.214 1.00 62.19  ?  143 HIS   A NE2   1 
ATOM   1091 N N     . ASN   A 1 144 ? 13.316 -18.563 -19.190 1.00 57.90  ?  144 ASN   A N     1 
ATOM   1092 C CA    . ASN   A 1 144 ? 12.224 -17.584 -18.969 1.00 57.28  ?  144 ASN   A CA    1 
ATOM   1093 C C     . ASN   A 1 144 ? 12.169 -16.571 -20.115 1.00 61.40  ?  144 ASN   A C     1 
ATOM   1094 O O     . ASN   A 1 144 ? 11.061 -16.133 -20.445 1.00 60.59  ?  144 ASN   A O     1 
ATOM   1095 C CB    . ASN   A 1 144 ? 12.402 -16.868 -17.637 1.00 64.20  ?  144 ASN   A CB    1 
ATOM   1096 C CG    . ASN   A 1 144 ? 12.127 -17.747 -16.440 1.00 63.85  ?  144 ASN   A CG    1 
ATOM   1097 O OD1   . ASN   A 1 144 ? 10.966 -17.981 -16.092 1.00 64.56  ?  144 ASN   A OD1   1 
ATOM   1098 N ND2   . ASN   A 1 144 ? 13.175 -18.224 -15.787 1.00 63.57  ?  144 ASN   A ND2   1 
ATOM   1099 N N     . GLU   A 1 145 ? 13.311 -16.197 -20.697 1.00 63.32  ?  145 GLU   A N     1 
ATOM   1100 C CA    . GLU   A 1 145 ? 13.216 -15.285 -21.831 1.00 58.81  ?  145 GLU   A CA    1 
ATOM   1101 C C     . GLU   A 1 145 ? 13.542 -16.006 -23.128 1.00 55.86  ?  145 GLU   A C     1 
ATOM   1102 O O     . GLU   A 1 145 ? 14.685 -16.461 -23.301 1.00 54.86  ?  145 GLU   A O     1 
ATOM   1103 C CB    . GLU   A 1 145 ? 14.152 -14.103 -21.650 1.00 63.92  ?  145 GLU   A CB    1 
ATOM   1104 C CG    . GLU   A 1 145 ? 13.518 -13.012 -20.866 1.00 67.67  ?  145 GLU   A CG    1 
ATOM   1105 C CD    . GLU   A 1 145 ? 12.747 -12.108 -21.761 1.00 70.61  ?  145 GLU   A CD    1 
ATOM   1106 O OE1   . GLU   A 1 145 ? 11.676 -11.617 -21.335 1.00 78.23  ?  145 GLU   A OE1   1 
ATOM   1107 O OE2   . GLU   A 1 145 ? 13.220 -11.903 -22.900 1.00 72.94  ?  145 GLU   A OE2   1 
ATOM   1108 N N     . PRO   A 1 146 ? 12.608 -16.081 -24.078 1.00 63.03  ?  146 PRO   A N     1 
ATOM   1109 C CA    . PRO   A 1 146 ? 12.867 -16.820 -25.320 1.00 59.07  ?  146 PRO   A CA    1 
ATOM   1110 C C     . PRO   A 1 146 ? 13.859 -16.095 -26.212 1.00 57.47  ?  146 PRO   A C     1 
ATOM   1111 O O     . PRO   A 1 146 ? 13.924 -14.864 -26.247 1.00 55.50  ?  146 PRO   A O     1 
ATOM   1112 C CB    . PRO   A 1 146 ? 11.487 -16.891 -25.978 1.00 52.87  ?  146 PRO   A CB    1 
ATOM   1113 C CG    . PRO   A 1 146 ? 10.848 -15.640 -25.581 1.00 55.67  ?  146 PRO   A CG    1 
ATOM   1114 C CD    . PRO   A 1 146 ? 11.345 -15.329 -24.160 1.00 63.29  ?  146 PRO   A CD    1 
ATOM   1115 N N     . ALA   A 1 147 ? 14.641 -16.881 -26.932 1.00 59.33  ?  147 ALA   A N     1 
ATOM   1116 C CA    . ALA   A 1 147 ? 15.686 -16.365 -27.804 1.00 61.05  ?  147 ALA   A CA    1 
ATOM   1117 C C     . ALA   A 1 147 ? 15.232 -16.583 -29.240 1.00 69.44  ?  147 ALA   A C     1 
ATOM   1118 O O     . ALA   A 1 147 ? 15.378 -17.683 -29.781 1.00 67.63  ?  147 ALA   A O     1 
ATOM   1119 C CB    . ALA   A 1 147 ? 17.012 -17.059 -27.528 1.00 60.98  ?  147 ALA   A CB    1 
ATOM   1120 N N     . LEU   A 1 148 ? 14.659 -15.544 -29.849 1.00 74.26  ?  148 LEU   A N     1 
ATOM   1121 C CA    . LEU   A 1 148 ? 14.390 -15.586 -31.279 1.00 71.87  ?  148 LEU   A CA    1 
ATOM   1122 C C     . LEU   A 1 148 ? 15.671 -15.312 -32.051 1.00 70.25  ?  148 LEU   A C     1 
ATOM   1123 O O     . LEU   A 1 148 ? 16.597 -14.682 -31.531 1.00 77.24  ?  148 LEU   A O     1 
ATOM   1124 C CB    . LEU   A 1 148 ? 13.339 -14.554 -31.669 1.00 70.15  ?  148 LEU   A CB    1 
ATOM   1125 C CG    . LEU   A 1 148 ? 11.874 -14.992 -31.700 1.00 75.42  ?  148 LEU   A CG    1 
ATOM   1126 C CD1   . LEU   A 1 148 ? 10.968 -13.804 -32.043 1.00 81.75  ?  148 LEU   A CD1   1 
ATOM   1127 C CD2   . LEU   A 1 148 ? 11.644 -16.158 -32.649 1.00 70.63  ?  148 LEU   A CD2   1 
ATOM   1128 N N     . PRO   A 1 149 ? 15.751 -15.771 -33.297 1.00 76.02  ?  149 PRO   A N     1 
ATOM   1129 C CA    . PRO   A 1 149 ? 16.928 -15.456 -34.119 1.00 78.52  ?  149 PRO   A CA    1 
ATOM   1130 C C     . PRO   A 1 149 ? 16.973 -13.974 -34.461 1.00 71.58  ?  149 PRO   A C     1 
ATOM   1131 O O     . PRO   A 1 149 ? 15.938 -13.338 -34.683 1.00 70.07  ?  149 PRO   A O     1 
ATOM   1132 C CB    . PRO   A 1 149 ? 16.722 -16.314 -35.370 1.00 75.59  ?  149 PRO   A CB    1 
ATOM   1133 C CG    . PRO   A 1 149 ? 15.217 -16.491 -35.444 1.00 72.90  ?  149 PRO   A CG    1 
ATOM   1134 C CD    . PRO   A 1 149 ? 14.779 -16.613 -34.020 1.00 72.32  ?  149 PRO   A CD    1 
ATOM   1135 N N     . ASP   A 1 150 ? 18.180 -13.415 -34.471 1.00 68.99  ?  150 ASP   A N     1 
ATOM   1136 C CA    . ASP   A 1 150 ? 18.354 -12.030 -34.897 1.00 76.76  ?  150 ASP   A CA    1 
ATOM   1137 C C     . ASP   A 1 150 ? 19.214 -12.003 -36.151 1.00 80.52  ?  150 ASP   A C     1 
ATOM   1138 O O     . ASP   A 1 150 ? 20.394 -12.403 -36.097 1.00 79.66  ?  150 ASP   A O     1 
ATOM   1139 C CB    . ASP   A 1 150 ? 18.973 -11.141 -33.814 1.00 75.11  ?  150 ASP   A CB    1 
ATOM   1140 C CG    . ASP   A 1 150 ? 18.716 -9.656  -34.075 1.00 73.99  ?  150 ASP   A CG    1 
ATOM   1141 O OD1   . ASP   A 1 150 ? 17.526 -9.269  -34.165 1.00 68.89  ?  150 ASP   A OD1   1 
ATOM   1142 O OD2   . ASP   A 1 150 ? 19.697 -8.885  -34.199 1.00 73.57  ?  150 ASP   A OD2   1 
ATOM   1143 N N     . PRO   A 1 151 ? 18.673 -11.532 -37.298 1.00 76.58  ?  151 PRO   A N     1 
ATOM   1144 C CA    . PRO   A 1 151 ? 17.296 -11.023 -37.360 1.00 69.96  ?  151 PRO   A CA    1 
ATOM   1145 C C     . PRO   A 1 151 ? 16.310 -12.073 -37.851 1.00 67.58  ?  151 PRO   A C     1 
ATOM   1146 O O     . PRO   A 1 151 ? 16.706 -13.220 -38.082 1.00 67.62  ?  151 PRO   A O     1 
ATOM   1147 C CB    . PRO   A 1 151 ? 17.405 -9.884  -38.371 1.00 72.91  ?  151 PRO   A CB    1 
ATOM   1148 C CG    . PRO   A 1 151 ? 18.397 -10.431 -39.380 1.00 71.73  ?  151 PRO   A CG    1 
ATOM   1149 C CD    . PRO   A 1 151 ? 19.364 -11.337 -38.587 1.00 76.41  ?  151 PRO   A CD    1 
ATOM   1150 N N     . LEU   A 1 152 ? 15.045 -11.688 -38.004 1.00 63.23  ?  152 LEU   A N     1 
ATOM   1151 C CA    . LEU   A 1 152 ? 14.102 -12.536 -38.707 1.00 59.40  ?  152 LEU   A CA    1 
ATOM   1152 C C     . LEU   A 1 152 ? 14.492 -12.621 -40.187 1.00 58.95  ?  152 LEU   A C     1 
ATOM   1153 O O     . LEU   A 1 152 ? 15.141 -11.718 -40.725 1.00 59.59  ?  152 LEU   A O     1 
ATOM   1154 C CB    . LEU   A 1 152 ? 12.682 -11.989 -38.558 1.00 58.64  ?  152 LEU   A CB    1 
ATOM   1155 C CG    . LEU   A 1 152 ? 12.090 -12.082 -37.145 1.00 64.24  ?  152 LEU   A CG    1 
ATOM   1156 C CD1   . LEU   A 1 152 ? 11.095 -10.956 -36.853 1.00 59.47  ?  152 LEU   A CD1   1 
ATOM   1157 C CD2   . LEU   A 1 152 ? 11.444 -13.450 -36.900 1.00 56.52  ?  152 LEU   A CD2   1 
ATOM   1158 N N     . PRO   A 1 153 ? 14.142 -13.708 -40.867 1.00 58.33  ?  153 PRO   A N     1 
ATOM   1159 C CA    . PRO   A 1 153 ? 14.355 -13.740 -42.319 1.00 56.88  ?  153 PRO   A CA    1 
ATOM   1160 C C     . PRO   A 1 153 ? 13.508 -12.683 -43.027 1.00 56.85  ?  153 PRO   A C     1 
ATOM   1161 O O     . PRO   A 1 153 ? 12.402 -12.345 -42.593 1.00 55.74  ?  153 PRO   A O     1 
ATOM   1162 C CB    . PRO   A 1 153 ? 13.949 -15.166 -42.704 1.00 52.99  ?  153 PRO   A CB    1 
ATOM   1163 C CG    . PRO   A 1 153 ? 14.093 -15.945 -41.442 1.00 53.98  ?  153 PRO   A CG    1 
ATOM   1164 C CD    . PRO   A 1 153 ? 13.700 -15.010 -40.348 1.00 56.42  ?  153 PRO   A CD    1 
ATOM   1165 N N     . ALA   A 1 154 ? 14.054 -12.166 -44.130 1.00 56.45  ?  154 ALA   A N     1 
ATOM   1166 C CA    . ALA   A 1 154 ? 13.469 -11.040 -44.853 1.00 55.74  ?  154 ALA   A CA    1 
ATOM   1167 C C     . ALA   A 1 154 ? 12.010 -11.281 -45.237 1.00 54.96  ?  154 ALA   A C     1 
ATOM   1168 O O     . ALA   A 1 154 ? 11.621 -12.378 -45.650 1.00 50.51  ?  154 ALA   A O     1 
ATOM   1169 C CB    . ALA   A 1 154 ? 14.300 -10.763 -46.110 1.00 54.30  ?  154 ALA   A CB    1 
ATOM   1170 N N     . GLY   A 1 155 ? 11.203 -10.232 -45.113 1.00 53.65  ?  155 GLY   A N     1 
ATOM   1171 C CA    . GLY   A 1 155 ? 9.802  -10.317 -45.461 1.00 57.12  ?  155 GLY   A CA    1 
ATOM   1172 C C     . GLY   A 1 155 ? 8.891  -10.832 -44.373 1.00 64.35  ?  155 GLY   A C     1 
ATOM   1173 O O     . GLY   A 1 155 ? 7.709  -11.082 -44.644 1.00 66.09  ?  155 GLY   A O     1 
ATOM   1174 N N     . ALA   A 1 156 ? 9.394  -10.986 -43.143 1.00 65.97  ?  156 ALA   A N     1 
ATOM   1175 C CA    . ALA   A 1 156 ? 8.589  -11.543 -42.061 1.00 62.66  ?  156 ALA   A CA    1 
ATOM   1176 C C     . ALA   A 1 156 ? 7.383  -10.677 -41.719 1.00 63.46  ?  156 ALA   A C     1 
ATOM   1177 O O     . ALA   A 1 156 ? 6.389  -11.197 -41.206 1.00 61.18  ?  156 ALA   A O     1 
ATOM   1178 C CB    . ALA   A 1 156 ? 9.459  -11.750 -40.824 1.00 56.18  ?  156 ALA   A CB    1 
ATOM   1179 N N     . ASP   A 1 157 ? 7.434  -9.379  -42.015 1.00 70.34  ?  157 ASP   A N     1 
ATOM   1180 C CA    . ASP   A 1 157 ? 6.308  -8.498  -41.710 1.00 72.75  ?  157 ASP   A CA    1 
ATOM   1181 C C     . ASP   A 1 157 ? 5.183  -8.629  -42.729 1.00 75.23  ?  157 ASP   A C     1 
ATOM   1182 O O     . ASP   A 1 157 ? 4.009  -8.446  -42.382 1.00 75.55  ?  157 ASP   A O     1 
ATOM   1183 C CB    . ASP   A 1 157 ? 6.800  -7.057  -41.639 1.00 71.60  ?  157 ASP   A CB    1 
ATOM   1184 C CG    . ASP   A 1 157 ? 8.162  -6.956  -40.992 1.00 83.74  ?  157 ASP   A CG    1 
ATOM   1185 O OD1   . ASP   A 1 157 ? 9.154  -7.341  -41.667 1.00 75.02  ?  157 ASP   A OD1   1 
ATOM   1186 O OD2   . ASP   A 1 157 ? 8.232  -6.528  -39.809 1.00 90.31  ?  157 ASP   A OD2   1 
ATOM   1187 N N     . SER   A 1 158 ? 5.517  -8.939  -43.980 1.00 72.04  ?  158 SER   A N     1 
ATOM   1188 C CA    . SER   A 1 158 ? 4.532  -9.318  -44.990 1.00 71.49  ?  158 SER   A CA    1 
ATOM   1189 C C     . SER   A 1 158 ? 4.317  -10.821 -45.038 1.00 68.71  ?  158 SER   A C     1 
ATOM   1190 O O     . SER   A 1 158 ? 4.334  -11.410 -46.117 1.00 72.64  ?  158 SER   A O     1 
ATOM   1191 C CB    . SER   A 1 158 ? 4.970  -8.797  -46.354 1.00 71.89  ?  158 SER   A CB    1 
ATOM   1192 O OG    . SER   A 1 158 ? 5.945  -9.656  -46.926 1.00 70.04  ?  158 SER   A OG    1 
ATOM   1193 N N     . PHE   A 1 159 ? 4.159  -11.483 -43.901 1.00 69.35  ?  159 PHE   A N     1 
ATOM   1194 C CA    . PHE   A 1 159 ? 3.854  -12.902 -43.884 1.00 69.40  ?  159 PHE   A CA    1 
ATOM   1195 C C     . PHE   A 1 159 ? 2.354  -13.060 -43.719 1.00 69.74  ?  159 PHE   A C     1 
ATOM   1196 O O     . PHE   A 1 159 ? 1.717  -12.295 -42.991 1.00 74.52  ?  159 PHE   A O     1 
ATOM   1197 C CB    . PHE   A 1 159 ? 4.602  -13.630 -42.762 1.00 66.75  ?  159 PHE   A CB    1 
ATOM   1198 C CG    . PHE   A 1 159 ? 4.370  -15.123 -42.732 1.00 67.20  ?  159 PHE   A CG    1 
ATOM   1199 C CD1   . PHE   A 1 159 ? 4.575  -15.900 -43.865 1.00 73.48  ?  159 PHE   A CD1   1 
ATOM   1200 C CD2   . PHE   A 1 159 ? 3.957  -15.752 -41.572 1.00 66.37  ?  159 PHE   A CD2   1 
ATOM   1201 C CE1   . PHE   A 1 159 ? 4.369  -17.282 -43.837 1.00 68.30  ?  159 PHE   A CE1   1 
ATOM   1202 C CE2   . PHE   A 1 159 ? 3.746  -17.125 -41.539 1.00 67.56  ?  159 PHE   A CE2   1 
ATOM   1203 C CZ    . PHE   A 1 159 ? 3.952  -17.889 -42.675 1.00 67.30  ?  159 PHE   A CZ    1 
ATOM   1204 N N     . ALA   A 1 160 ? 1.793  -14.045 -44.413 1.00 68.41  ?  160 ALA   A N     1 
ATOM   1205 C CA    . ALA   A 1 160 ? 0.355  -14.255 -44.343 1.00 71.58  ?  160 ALA   A CA    1 
ATOM   1206 C C     . ALA   A 1 160 ? -0.067 -14.794 -42.982 1.00 79.14  ?  160 ALA   A C     1 
ATOM   1207 O O     . ALA   A 1 160 ? -1.108 -14.389 -42.447 1.00 83.11  ?  160 ALA   A O     1 
ATOM   1208 C CB    . ALA   A 1 160 ? -0.086 -15.208 -45.449 1.00 78.51  ?  160 ALA   A CB    1 
ATOM   1209 N N     . GLY   A 1 161 ? 0.719  -15.709 -42.406 1.00 76.76  ?  161 GLY   A N     1 
ATOM   1210 C CA    . GLY   A 1 161 ? 0.340  -16.405 -41.195 1.00 70.50  ?  161 GLY   A CA    1 
ATOM   1211 C C     . GLY   A 1 161 ? 1.040  -15.875 -39.958 1.00 69.09  ?  161 GLY   A C     1 
ATOM   1212 O O     . GLY   A 1 161 ? 1.632  -14.794 -39.947 1.00 72.25  ?  161 GLY   A O     1 
ATOM   1213 N N     . THR   A 1 162 ? 0.973  -16.668 -38.895 1.00 64.26  ?  162 THR   A N     1 
ATOM   1214 C CA    . THR   A 1 162 ? 1.525  -16.259 -37.612 1.00 65.97  ?  162 THR   A CA    1 
ATOM   1215 C C     . THR   A 1 162 ? 2.919  -16.841 -37.408 1.00 62.10  ?  162 THR   A C     1 
ATOM   1216 O O     . THR   A 1 162 ? 3.212  -17.968 -37.815 1.00 57.73  ?  162 THR   A O     1 
ATOM   1217 C CB    . THR   A 1 162 ? 0.630  -16.689 -36.444 1.00 60.33  ?  162 THR   A CB    1 
ATOM   1218 O OG1   . THR   A 1 162 ? 0.544  -18.110 -36.424 1.00 57.68  ?  162 THR   A OG1   1 
ATOM   1219 C CG2   . THR   A 1 162 ? -0.779 -16.108 -36.563 1.00 64.36  ?  162 THR   A CG2   1 
ATOM   1220 N N     . ILE   A 1 163 ? 3.769  -16.060 -36.745 1.00 60.32  ?  163 ILE   A N     1 
ATOM   1221 C CA    . ILE   A 1 163 ? 5.119  -16.468 -36.378 1.00 58.71  ?  163 ILE   A CA    1 
ATOM   1222 C C     . ILE   A 1 163 ? 5.216  -16.458 -34.853 1.00 64.77  ?  163 ILE   A C     1 
ATOM   1223 O O     . ILE   A 1 163 ? 5.014  -15.409 -34.227 1.00 69.03  ?  163 ILE   A O     1 
ATOM   1224 C CB    . ILE   A 1 163 ? 6.170  -15.546 -37.012 1.00 59.42  ?  163 ILE   A CB    1 
ATOM   1225 C CG1   . ILE   A 1 163 ? 5.962  -15.466 -38.539 1.00 53.53  ?  163 ILE   A CG1   1 
ATOM   1226 C CG2   . ILE   A 1 163 ? 7.559  -16.036 -36.669 1.00 59.78  ?  163 ILE   A CG2   1 
ATOM   1227 C CD1   . ILE   A 1 163 ? 6.530  -14.223 -39.167 1.00 38.09  ?  163 ILE   A CD1   1 
ATOM   1228 N N     . LEU   A 1 164 ? 5.516  -17.620 -34.252 1.00 57.65  ?  164 LEU   A N     1 
ATOM   1229 C CA    . LEU   A 1 164 ? 5.480  -17.772 -32.797 1.00 53.95  ?  164 LEU   A CA    1 
ATOM   1230 C C     . LEU   A 1 164 ? 6.671  -18.596 -32.310 1.00 54.96  ?  164 LEU   A C     1 
ATOM   1231 O O     . LEU   A 1 164 ? 7.364  -19.250 -33.100 1.00 49.82  ?  164 LEU   A O     1 
ATOM   1232 C CB    . LEU   A 1 164 ? 4.164  -18.414 -32.336 1.00 53.25  ?  164 LEU   A CB    1 
ATOM   1233 C CG    . LEU   A 1 164 ? 4.051  -19.931 -32.479 1.00 55.32  ?  164 LEU   A CG    1 
ATOM   1234 C CD1   . LEU   A 1 164 ? 2.923  -20.475 -31.613 1.00 52.66  ?  164 LEU   A CD1   1 
ATOM   1235 C CD2   . LEU   A 1 164 ? 3.843  -20.318 -33.930 1.00 55.99  ?  164 LEU   A CD2   1 
ATOM   1236 N N     . HIS   A 1 165 ? 6.906  -18.541 -30.984 1.00 54.84  ?  165 HIS   A N     1 
ATOM   1237 C CA    . HIS   A 1 165 ? 7.983  -19.242 -30.282 1.00 49.89  ?  165 HIS   A CA    1 
ATOM   1238 C C     . HIS   A 1 165 ? 7.420  -20.438 -29.524 1.00 51.39  ?  165 HIS   A C     1 
ATOM   1239 O O     . HIS   A 1 165 ? 6.243  -20.471 -29.144 1.00 50.03  ?  165 HIS   A O     1 
ATOM   1240 C CB    . HIS   A 1 165 ? 8.713  -18.299 -29.304 1.00 56.90  ?  165 HIS   A CB    1 
ATOM   1241 C CG    . HIS   A 1 165 ? 10.002 -18.839 -28.741 1.00 55.13  ?  165 HIS   A CG    1 
ATOM   1242 N ND1   . HIS   A 1 165 ? 10.046 -19.806 -27.756 1.00 54.02  ?  165 HIS   A ND1   1 
ATOM   1243 C CD2   . HIS   A 1 165 ? 11.291 -18.501 -28.988 1.00 53.59  ?  165 HIS   A CD2   1 
ATOM   1244 C CE1   . HIS   A 1 165 ? 11.305 -20.073 -27.457 1.00 49.51  ?  165 HIS   A CE1   1 
ATOM   1245 N NE2   . HIS   A 1 165 ? 12.080 -19.287 -28.183 1.00 52.40  ?  165 HIS   A NE2   1 
ATOM   1246 N N     . SER   A 1 166 ? 8.289  -21.428 -29.302 1.00 48.36  ?  166 SER   A N     1 
ATOM   1247 C CA    . SER   A 1 166 ? 7.903  -22.628 -28.567 1.00 50.73  ?  166 SER   A CA    1 
ATOM   1248 C C     . SER   A 1 166 ? 7.286  -22.312 -27.216 1.00 57.20  ?  166 SER   A C     1 
ATOM   1249 O O     . SER   A 1 166 ? 6.544  -23.140 -26.674 1.00 57.46  ?  166 SER   A O     1 
ATOM   1250 C CB    . SER   A 1 166 ? 9.112  -23.534 -28.366 1.00 50.13  ?  166 SER   A CB    1 
ATOM   1251 O OG    . SER   A 1 166 ? 9.983  -22.975 -27.400 1.00 54.25  ?  166 SER   A OG    1 
ATOM   1252 N N     . LEU   A 1 167 ? 7.579  -21.139 -26.657 1.00 52.14  ?  167 LEU   A N     1 
ATOM   1253 C CA    . LEU   A 1 167 ? 6.954  -20.753 -25.405 1.00 57.68  ?  167 LEU   A CA    1 
ATOM   1254 C C     . LEU   A 1 167 ? 5.450  -20.550 -25.561 1.00 59.28  ?  167 LEU   A C     1 
ATOM   1255 O O     . LEU   A 1 167 ? 4.677  -20.822 -24.630 1.00 62.23  ?  167 LEU   A O     1 
ATOM   1256 C CB    . LEU   A 1 167 ? 7.617  -19.486 -24.897 1.00 62.21  ?  167 LEU   A CB    1 
ATOM   1257 C CG    . LEU   A 1 167 ? 7.153  -19.013 -23.534 1.00 59.35  ?  167 LEU   A CG    1 
ATOM   1258 C CD1   . LEU   A 1 167 ? 8.362  -18.610 -22.737 1.00 58.13  ?  167 LEU   A CD1   1 
ATOM   1259 C CD2   . LEU   A 1 167 ? 6.197  -17.852 -23.722 1.00 63.09  ?  167 LEU   A CD2   1 
ATOM   1260 N N     . ASP   A 1 168 ? 5.023  -20.066 -26.721 1.00 59.22  ?  168 ASP   A N     1 
ATOM   1261 C CA    . ASP   A 1 168 ? 3.614  -19.859 -27.018 1.00 54.78  ?  168 ASP   A CA    1 
ATOM   1262 C C     . ASP   A 1 168 ? 2.911  -21.133 -27.470 1.00 57.75  ?  168 ASP   A C     1 
ATOM   1263 O O     . ASP   A 1 168 ? 1.686  -21.135 -27.619 1.00 60.40  ?  168 ASP   A O     1 
ATOM   1264 C CB    . ASP   A 1 168 ? 3.489  -18.793 -28.099 1.00 56.01  ?  168 ASP   A CB    1 
ATOM   1265 C CG    . ASP   A 1 168 ? 4.036  -17.445 -27.663 1.00 58.29  ?  168 ASP   A CG    1 
ATOM   1266 O OD1   . ASP   A 1 168 ? 3.426  -16.830 -26.761 1.00 55.84  ?  168 ASP   A OD1   1 
ATOM   1267 O OD2   . ASP   A 1 168 ? 5.072  -17.010 -28.228 1.00 56.18  ?  168 ASP   A OD2   1 
ATOM   1268 N N     . TYR   A 1 169 ? 3.627  -22.237 -27.654 1.00 56.54  ?  169 TYR   A N     1 
ATOM   1269 C CA    . TYR   A 1 169 ? 2.952  -23.454 -28.172 1.00 54.06  ?  169 TYR   A CA    1 
ATOM   1270 C C     . TYR   A 1 169 ? 2.345  -24.233 -27.017 1.00 55.06  ?  169 TYR   A C     1 
ATOM   1271 O O     . TYR   A 1 169 ? 2.936  -24.304 -25.944 1.00 60.19  ?  169 TYR   A O     1 
ATOM   1272 C CB    . TYR   A 1 169 ? 3.962  -24.274 -28.978 1.00 53.82  ?  169 TYR   A CB    1 
ATOM   1273 C CG    . TYR   A 1 169 ? 3.451  -25.541 -29.649 1.00 53.61  ?  169 TYR   A CG    1 
ATOM   1274 C CD1   . TYR   A 1 169 ? 3.302  -26.724 -28.938 1.00 56.22  ?  169 TYR   A CD1   1 
ATOM   1275 C CD2   . TYR   A 1 169 ? 3.149  -25.556 -31.002 1.00 53.23  ?  169 TYR   A CD2   1 
ATOM   1276 C CE1   . TYR   A 1 169 ? 2.844  -27.879 -29.546 1.00 54.32  ?  169 TYR   A CE1   1 
ATOM   1277 C CE2   . TYR   A 1 169 ? 2.691  -26.703 -31.623 1.00 52.70  ?  169 TYR   A CE2   1 
ATOM   1278 C CZ    . TYR   A 1 169 ? 2.541  -27.866 -30.893 1.00 56.84  ?  169 TYR   A CZ    1 
ATOM   1279 O OH    . TYR   A 1 169 ? 2.097  -28.995 -31.505 1.00 54.41  ?  169 TYR   A OH    1 
ATOM   1280 N N     . ARG   A 1 170 ? 1.174  -24.817 -27.229 1.00 55.94  ?  170 ARG   A N     1 
ATOM   1281 C CA    . ARG   A 1 170 ? 0.579  -25.688 -26.185 1.00 59.64  ?  170 ARG   A CA    1 
ATOM   1282 C C     . ARG   A 1 170 ? 0.238  -27.055 -26.795 1.00 60.89  ?  170 ARG   A C     1 
ATOM   1283 O O     . ARG   A 1 170 ? 0.845  -28.047 -26.384 1.00 62.19  ?  170 ARG   A O     1 
ATOM   1284 C CB    . ARG   A 1 170 ? -0.647 -25.025 -25.555 1.00 66.13  ?  170 ARG   A CB    1 
ATOM   1285 C CG    . ARG   A 1 170 ? -1.445 -25.908 -24.607 1.00 71.20  ?  170 ARG   A CG    1 
ATOM   1286 C CD    . ARG   A 1 170 ? -2.906 -25.490 -24.565 1.00 78.95  ?  170 ARG   A CD    1 
ATOM   1287 N NE    . ARG   A 1 170 ? -3.500 -25.381 -25.902 1.00 81.48  ?  170 ARG   A NE    1 
ATOM   1288 C CZ    . ARG   A 1 170 ? -4.005 -24.274 -26.429 1.00 85.44  ?  170 ARG   A CZ    1 
ATOM   1289 N NH1   . ARG   A 1 170 ? -5.164 -24.314 -27.056 1.00 83.39  ?  170 ARG   A NH1   1 
ATOM   1290 N NH2   . ARG   A 1 170 ? -3.344 -23.134 -26.354 1.00 81.35  ?  170 ARG   A NH2   1 
ATOM   1291 N N     . ASP   A 1 171 ? -0.700 -27.090 -27.733 1.00 63.10  ?  171 ASP   A N     1 
ATOM   1292 C CA    . ASP   A 1 171 ? -1.085 -28.361 -28.388 1.00 65.06  ?  171 ASP   A CA    1 
ATOM   1293 C C     . ASP   A 1 171 ? -1.236 -28.129 -29.883 1.00 60.11  ?  171 ASP   A C     1 
ATOM   1294 O O     . ASP   A 1 171 ? -1.555 -27.007 -30.289 1.00 60.22  ?  171 ASP   A O     1 
ATOM   1295 C CB    . ASP   A 1 171 ? -2.364 -28.949 -27.820 1.00 67.50  ?  171 ASP   A CB    1 
ATOM   1296 C CG    . ASP   A 1 171 ? -2.781 -30.289 -28.407 1.00 69.85  ?  171 ASP   A CG    1 
ATOM   1297 O OD1   . ASP   A 1 171 ? -1.925 -31.191 -28.476 1.00 71.87  ?  171 ASP   A OD1   1 
ATOM   1298 O OD2   . ASP   A 1 171 ? -3.952 -30.412 -28.803 1.00 71.42  ?  171 ASP   A OD2   1 
ATOM   1299 N N     . GLY   A 1 172 ? -0.995 -29.173 -30.658 1.00 57.05  ?  172 GLY   A N     1 
ATOM   1300 C CA    . GLY   A 1 172 ? -1.161 -29.067 -32.112 1.00 66.16  ?  172 GLY   A CA    1 
ATOM   1301 C C     . GLY   A 1 172 ? -2.616 -29.099 -32.492 1.00 66.10  ?  172 GLY   A C     1 
ATOM   1302 O O     . GLY   A 1 172 ? -2.922 -28.764 -33.640 1.00 60.82  ?  172 GLY   A O     1 
ATOM   1303 N N     . GLY   A 1 173 ? -3.485 -29.507 -31.568 1.00 68.70  ?  173 GLY   A N     1 
ATOM   1304 C CA    . GLY   A 1 173 ? -4.889 -29.441 -31.949 1.00 66.41  ?  173 GLY   A CA    1 
ATOM   1305 C C     . GLY   A 1 173 ? -5.340 -28.071 -32.410 1.00 65.93  ?  173 GLY   A C     1 
ATOM   1306 O O     . GLY   A 1 173 ? -6.454 -27.944 -32.931 1.00 64.06  ?  173 GLY   A O     1 
ATOM   1307 N N     . ASP   A 1 174 ? -4.514 -27.052 -32.210 1.00 65.38  ?  174 ASP   A N     1 
ATOM   1308 C CA    . ASP   A 1 174 ? -4.772 -25.705 -32.674 1.00 66.58  ?  174 ASP   A CA    1 
ATOM   1309 C C     . ASP   A 1 174 ? -4.253 -25.479 -34.077 1.00 69.16  ?  174 ASP   A C     1 
ATOM   1310 O O     . ASP   A 1 174 ? -4.492 -24.409 -34.648 1.00 75.31  ?  174 ASP   A O     1 
ATOM   1311 C CB    . ASP   A 1 174 ? -4.130 -24.706 -31.725 1.00 67.90  ?  174 ASP   A CB    1 
ATOM   1312 C CG    . ASP   A 1 174 ? -4.361 -25.067 -30.281 1.00 76.65  ?  174 ASP   A CG    1 
ATOM   1313 O OD1   . ASP   A 1 174 ? -5.218 -25.938 -30.021 1.00 76.41  ?  174 ASP   A OD1   1 
ATOM   1314 O OD2   . ASP   A 1 174 ? -3.679 -24.501 -29.401 1.00 83.14  ?  174 ASP   A OD2   1 
ATOM   1315 N N     . PHE   A 1 175 ? -3.542 -26.460 -34.634 1.00 67.47  ?  175 PHE   A N     1 
ATOM   1316 C CA    . PHE   A 1 175 ? -3.009 -26.401 -35.991 1.00 66.73  ?  175 PHE   A CA    1 
ATOM   1317 C C     . PHE   A 1 175 ? -3.592 -27.509 -36.848 1.00 66.30  ?  175 PHE   A C     1 
ATOM   1318 O O     . PHE   A 1 175 ? -2.969 -27.933 -37.828 1.00 66.19  ?  175 PHE   A O     1 
ATOM   1319 C CB    . PHE   A 1 175 ? -1.486 -26.497 -35.978 1.00 64.64  ?  175 PHE   A CB    1 
ATOM   1320 C CG    . PHE   A 1 175 ? -0.841 -25.534 -35.045 1.00 66.79  ?  175 PHE   A CG    1 
ATOM   1321 C CD1   . PHE   A 1 175 ? -0.834 -25.775 -33.671 1.00 64.75  ?  175 PHE   A CD1   1 
ATOM   1322 C CD2   . PHE   A 1 175 ? -0.254 -24.378 -35.532 1.00 63.47  ?  175 PHE   A CD2   1 
ATOM   1323 C CE1   . PHE   A 1 175 ? -0.253 -24.876 -32.804 1.00 66.77  ?  175 PHE   A CE1   1 
ATOM   1324 C CE2   . PHE   A 1 175 ? 0.337  -23.474 -34.672 1.00 63.51  ?  175 PHE   A CE2   1 
ATOM   1325 C CZ    . PHE   A 1 175 ? 0.338  -23.720 -33.306 1.00 63.72  ?  175 PHE   A CZ    1 
ATOM   1326 N N     . ALA   A 1 176 ? -4.767 -27.997 -36.471 1.00 63.12  ?  176 ALA   A N     1 
ATOM   1327 C CA    . ALA   A 1 176 ? -5.376 -29.113 -37.166 1.00 68.52  ?  176 ALA   A CA    1 
ATOM   1328 C C     . ALA   A 1 176 ? -5.636 -28.753 -38.631 1.00 74.07  ?  176 ALA   A C     1 
ATOM   1329 O O     . ALA   A 1 176 ? -6.268 -27.734 -38.939 1.00 72.59  ?  176 ALA   A O     1 
ATOM   1330 C CB    . ALA   A 1 176 ? -6.665 -29.512 -36.447 1.00 62.81  ?  176 ALA   A CB    1 
ATOM   1331 N N     . GLY   A 1 177 ? -5.116 -29.580 -39.535 1.00 67.99  ?  177 GLY   A N     1 
ATOM   1332 C CA    . GLY   A 1 177 ? -5.321 -29.351 -40.948 1.00 66.56  ?  177 GLY   A CA    1 
ATOM   1333 C C     . GLY   A 1 177 ? -4.679 -28.087 -41.458 1.00 68.80  ?  177 GLY   A C     1 
ATOM   1334 O O     . GLY   A 1 177 ? -5.180 -27.484 -42.412 1.00 78.02  ?  177 GLY   A O     1 
ATOM   1335 N N     . ARG   A 1 178 ? -3.592 -27.659 -40.849 1.00 64.68  ?  178 ARG   A N     1 
ATOM   1336 C CA    . ARG   A 1 178 ? -2.824 -26.555 -41.391 1.00 66.91  ?  178 ARG   A CA    1 
ATOM   1337 C C     . ARG   A 1 178 ? -1.448 -27.059 -41.785 1.00 63.25  ?  178 ARG   A C     1 
ATOM   1338 O O     . ARG   A 1 178 ? -1.140 -28.253 -41.671 1.00 61.97  ?  178 ARG   A O     1 
ATOM   1339 C CB    . ARG   A 1 178 ? -2.735 -25.403 -40.391 1.00 68.88  ?  178 ARG   A CB    1 
ATOM   1340 C CG    . ARG   A 1 178 ? -4.006 -25.181 -39.614 1.00 67.81  ?  178 ARG   A CG    1 
ATOM   1341 C CD    . ARG   A 1 178 ? -4.943 -24.245 -40.342 1.00 71.50  ?  178 ARG   A CD    1 
ATOM   1342 N NE    . ARG   A 1 178 ? -6.269 -24.244 -39.728 1.00 83.83  ?  178 ARG   A NE    1 
ATOM   1343 C CZ    . ARG   A 1 178 ? -6.566 -23.679 -38.557 1.00 83.52  ?  178 ARG   A CZ    1 
ATOM   1344 N NH1   . ARG   A 1 178 ? -5.633 -23.051 -37.846 1.00 78.62  ?  178 ARG   A NH1   1 
ATOM   1345 N NH2   . ARG   A 1 178 ? -7.808 -23.741 -38.095 1.00 83.80  ?  178 ARG   A NH2   1 
ATOM   1346 N N     . ARG   A 1 179 ? -0.619 -26.126 -42.248 1.00 61.54  ?  179 ARG   A N     1 
ATOM   1347 C CA    . ARG   A 1 179 ? 0.737  -26.413 -42.697 1.00 60.18  ?  179 ARG   A CA    1 
ATOM   1348 C C     . ARG   A 1 179 ? 1.702  -25.528 -41.914 1.00 60.15  ?  179 ARG   A C     1 
ATOM   1349 O O     . ARG   A 1 179 ? 1.528  -24.304 -41.887 1.00 57.52  ?  179 ARG   A O     1 
ATOM   1350 C CB    . ARG   A 1 179 ? 0.847  -26.185 -44.203 1.00 58.94  ?  179 ARG   A CB    1 
ATOM   1351 C CG    . ARG   A 1 179 ? -0.091 -27.090 -44.998 1.00 68.03  ?  179 ARG   A CG    1 
ATOM   1352 C CD    . ARG   A 1 179 ? -0.639 -26.396 -46.237 1.00 71.59  ?  179 ARG   A CD    1 
ATOM   1353 N NE    . ARG   A 1 179 ? -1.304 -25.140 -45.899 1.00 75.85  ?  179 ARG   A NE    1 
ATOM   1354 C CZ    . ARG   A 1 179 ? -2.128 -24.484 -46.712 1.00 76.38  ?  179 ARG   A CZ    1 
ATOM   1355 N NH1   . ARG   A 1 179 ? -2.680 -23.339 -46.320 1.00 72.85  ?  179 ARG   A NH1   1 
ATOM   1356 N NH2   . ARG   A 1 179 ? -2.399 -24.972 -47.918 1.00 75.37  ?  179 ARG   A NH2   1 
ATOM   1357 N N     . VAL   A 1 180 ? 2.713  -26.155 -41.271 1.00 58.07  ?  180 VAL   A N     1 
ATOM   1358 C CA    . VAL   A 1 180 ? 3.550  -25.529 -40.238 1.00 51.28  ?  180 VAL   A CA    1 
ATOM   1359 C C     . VAL   A 1 180 ? 5.038  -25.820 -40.470 1.00 46.83  ?  180 VAL   A C     1 
ATOM   1360 O O     . VAL   A 1 180 ? 5.423  -26.957 -40.765 1.00 44.83  ?  180 VAL   A O     1 
ATOM   1361 C CB    . VAL   A 1 180 ? 3.140  -26.016 -38.825 1.00 51.08  ?  180 VAL   A CB    1 
ATOM   1362 C CG1   . VAL   A 1 180 ? 3.608  -25.041 -37.755 1.00 53.05  ?  180 VAL   A CG1   1 
ATOM   1363 C CG2   . VAL   A 1 180 ? 1.637  -26.241 -38.733 1.00 53.52  ?  180 VAL   A CG2   1 
ATOM   1364 N N     . VAL   A 1 181 ? 5.883  -24.793 -40.290 1.00 48.76  ?  181 VAL   A N     1 
ATOM   1365 C CA    . VAL   A 1 181 ? 7.336  -24.954 -40.164 1.00 46.99  ?  181 VAL   A CA    1 
ATOM   1366 C C     . VAL   A 1 181 ? 7.731  -24.988 -38.684 1.00 51.82  ?  181 VAL   A C     1 
ATOM   1367 O O     . VAL   A 1 181 ? 7.140  -24.283 -37.853 1.00 51.11  ?  181 VAL   A O     1 
ATOM   1368 C CB    . VAL   A 1 181 ? 8.065  -23.811 -40.886 1.00 45.98  ?  181 VAL   A CB    1 
ATOM   1369 C CG1   . VAL   A 1 181 ? 9.527  -24.173 -41.149 1.00 48.81  ?  181 VAL   A CG1   1 
ATOM   1370 C CG2   . VAL   A 1 181 ? 7.331  -23.464 -42.158 1.00 45.86  ?  181 VAL   A CG2   1 
ATOM   1371 N N     . VAL   A 1 182 ? 8.736  -25.804 -38.351 1.00 50.07  ?  182 VAL   A N     1 
ATOM   1372 C CA    . VAL   A 1 182 ? 9.344  -25.860 -37.019 1.00 46.47  ?  182 VAL   A CA    1 
ATOM   1373 C C     . VAL   A 1 182 ? 10.832 -25.576 -37.187 1.00 45.46  ?  182 VAL   A C     1 
ATOM   1374 O O     . VAL   A 1 182 ? 11.515 -26.299 -37.924 1.00 47.07  ?  182 VAL   A O     1 
ATOM   1375 C CB    . VAL   A 1 182 ? 9.135  -27.227 -36.338 1.00 45.64  ?  182 VAL   A CB    1 
ATOM   1376 C CG1   . VAL   A 1 182 ? 10.026 -27.350 -35.121 1.00 43.55  ?  182 VAL   A CG1   1 
ATOM   1377 C CG2   . VAL   A 1 182 ? 7.690  -27.438 -35.957 1.00 42.82  ?  182 VAL   A CG2   1 
ATOM   1378 N N     . VAL   A 1 183 ? 11.336 -24.548 -36.493 1.00 38.34  ?  183 VAL   A N     1 
ATOM   1379 C CA    . VAL   A 1 183 ? 12.711 -24.071 -36.656 1.00 42.75  ?  183 VAL   A CA    1 
ATOM   1380 C C     . VAL   A 1 183 ? 13.541 -24.541 -35.475 1.00 44.33  ?  183 VAL   A C     1 
ATOM   1381 O O     . VAL   A 1 183 ? 13.393 -24.040 -34.357 1.00 47.99  ?  183 VAL   A O     1 
ATOM   1382 C CB    . VAL   A 1 183 ? 12.794 -22.540 -36.788 1.00 47.36  ?  183 VAL   A CB    1 
ATOM   1383 C CG1   . VAL   A 1 183 ? 14.198 -22.116 -37.257 1.00 42.62  ?  183 VAL   A CG1   1 
ATOM   1384 C CG2   . VAL   A 1 183 ? 11.753 -22.019 -37.756 1.00 50.82  ?  183 VAL   A CG2   1 
ATOM   1385 N N     . GLY   A 1 184 ? 14.452 -25.467 -35.728 1.00 45.83  ?  184 GLY   A N     1 
ATOM   1386 C CA    . GLY   A 1 184 ? 15.369 -25.899 -34.703 1.00 46.64  ?  184 GLY   A CA    1 
ATOM   1387 C C     . GLY   A 1 184 ? 15.519 -27.395 -34.604 1.00 49.09  ?  184 GLY   A C     1 
ATOM   1388 O O     . GLY   A 1 184 ? 14.631 -28.160 -34.981 1.00 52.98  ?  184 GLY   A O     1 
ATOM   1389 N N     . LEU   A 1 185 ? 16.656 -27.831 -34.092 1.00 47.02  ?  185 LEU   A N     1 
ATOM   1390 C CA    . LEU   A 1 185 ? 16.872 -29.240 -33.828 1.00 48.87  ?  185 LEU   A CA    1 
ATOM   1391 C C     . LEU   A 1 185 ? 17.002 -29.539 -32.330 1.00 52.40  ?  185 LEU   A C     1 
ATOM   1392 O O     . LEU   A 1 185 ? 17.594 -30.556 -31.948 1.00 48.01  ?  185 LEU   A O     1 
ATOM   1393 C CB    . LEU   A 1 185 ? 18.105 -29.713 -34.593 1.00 47.30  ?  185 LEU   A CB    1 
ATOM   1394 C CG    . LEU   A 1 185 ? 17.981 -31.177 -34.992 1.00 47.08  ?  185 LEU   A CG    1 
ATOM   1395 C CD1   . LEU   A 1 185 ? 16.581 -31.427 -35.501 1.00 38.40  ?  185 LEU   A CD1   1 
ATOM   1396 C CD2   . LEU   A 1 185 ? 19.035 -31.557 -36.000 1.00 51.39  ?  185 LEU   A CD2   1 
ATOM   1397 N N     . GLY   A 1 186 ? 16.456 -28.674 -31.479 1.00 50.94  ?  186 GLY   A N     1 
ATOM   1398 C CA    . GLY   A 1 186 ? 16.610 -28.800 -30.051 1.00 54.91  ?  186 GLY   A CA    1 
ATOM   1399 C C     . GLY   A 1 186 ? 15.623 -29.772 -29.432 1.00 57.63  ?  186 GLY   A C     1 
ATOM   1400 O O     . GLY   A 1 186 ? 14.883 -30.490 -30.107 1.00 51.73  ?  186 GLY   A O     1 
ATOM   1401 N N     . ALA   A 1 187 ? 15.615 -29.773 -28.095 1.00 60.69  ?  187 ALA   A N     1 
ATOM   1402 C CA    . ALA   A 1 187 ? 14.742 -30.678 -27.348 1.00 57.06  ?  187 ALA   A CA    1 
ATOM   1403 C C     . ALA   A 1 187 ? 13.274 -30.353 -27.575 1.00 57.49  ?  187 ALA   A C     1 
ATOM   1404 O O     . ALA   A 1 187 ? 12.440 -31.256 -27.720 1.00 53.14  ?  187 ALA   A O     1 
ATOM   1405 C CB    . ALA   A 1 187 ? 15.072 -30.607 -25.863 1.00 68.05  ?  187 ALA   A CB    1 
ATOM   1406 N N     . SER   A 1 188 ? 12.935 -29.066 -27.591 1.00 55.25  ?  188 SER   A N     1 
ATOM   1407 C CA    . SER   A 1 188 ? 11.571 -28.670 -27.912 1.00 53.10  ?  188 SER   A CA    1 
ATOM   1408 C C     . SER   A 1 188 ? 11.237 -28.897 -29.389 1.00 56.77  ?  188 SER   A C     1 
ATOM   1409 O O     . SER   A 1 188 ? 10.095 -29.254 -29.721 1.00 52.12  ?  188 SER   A O     1 
ATOM   1410 C CB    . SER   A 1 188 ? 11.367 -27.207 -27.549 1.00 52.63  ?  188 SER   A CB    1 
ATOM   1411 O OG    . SER   A 1 188 ? 12.056 -26.885 -26.358 1.00 57.98  ?  188 SER   A OG    1 
ATOM   1412 N N     . ALA   A 1 189 ? 12.223 -28.724 -30.280 1.00 57.56  ?  189 ALA   A N     1 
ATOM   1413 C CA    . ALA   A 1 189 ? 11.970 -28.763 -31.717 1.00 53.33  ?  189 ALA   A CA    1 
ATOM   1414 C C     . ALA   A 1 189 ? 11.447 -30.120 -32.161 1.00 48.16  ?  189 ALA   A C     1 
ATOM   1415 O O     . ALA   A 1 189 ? 10.397 -30.208 -32.807 1.00 45.16  ?  189 ALA   A O     1 
ATOM   1416 C CB    . ALA   A 1 189 ? 13.241 -28.414 -32.468 1.00 54.98  ?  189 ALA   A CB    1 
ATOM   1417 N N     . VAL   A 1 190 ? 12.167 -31.193 -31.819 1.00 46.67  ?  190 VAL   A N     1 
ATOM   1418 C CA    . VAL   A 1 190 ? 11.753 -32.525 -32.252 1.00 44.85  ?  190 VAL   A CA    1 
ATOM   1419 C C     . VAL   A 1 190 ? 10.444 -32.934 -31.582 1.00 50.23  ?  190 VAL   A C     1 
ATOM   1420 O O     . VAL   A 1 190 ? 9.663  -33.708 -32.156 1.00 44.88  ?  190 VAL   A O     1 
ATOM   1421 C CB    . VAL   A 1 190 ? 12.862 -33.564 -31.989 1.00 39.98  ?  190 VAL   A CB    1 
ATOM   1422 C CG1   . VAL   A 1 190 ? 14.158 -33.125 -32.609 1.00 44.12  ?  190 VAL   A CG1   1 
ATOM   1423 C CG2   . VAL   A 1 190 ? 13.041 -33.790 -30.514 1.00 52.07  ?  190 VAL   A CG2   1 
ATOM   1424 N N     . ASP   A 1 191 ? 10.179 -32.421 -30.369 1.00 50.12  ?  191 ASP   A N     1 
ATOM   1425 C CA    . ASP   A 1 191 ? 8.964  -32.772 -29.630 1.00 49.32  ?  191 ASP   A CA    1 
ATOM   1426 C C     . ASP   A 1 191 ? 7.725  -32.146 -30.272 1.00 49.40  ?  191 ASP   A C     1 
ATOM   1427 O O     . ASP   A 1 191 ? 6.678  -32.794 -30.413 1.00 42.41  ?  191 ASP   A O     1 
ATOM   1428 C CB    . ASP   A 1 191 ? 9.089  -32.300 -28.173 1.00 52.68  ?  191 ASP   A CB    1 
ATOM   1429 C CG    . ASP   A 1 191 ? 9.535  -33.394 -27.210 1.00 55.64  ?  191 ASP   A CG    1 
ATOM   1430 O OD1   . ASP   A 1 191 ? 9.718  -34.556 -27.632 1.00 56.23  ?  191 ASP   A OD1   1 
ATOM   1431 O OD2   . ASP   A 1 191 ? 9.703  -33.071 -26.011 1.00 56.38  ?  191 ASP   A OD2   1 
ATOM   1432 N N     . ILE   A 1 192 ? 7.823  -30.864 -30.630 1.00 50.39  ?  192 ILE   A N     1 
ATOM   1433 C CA    . ILE   A 1 192 ? 6.697  -30.147 -31.220 1.00 48.18  ?  192 ILE   A CA    1 
ATOM   1434 C C     . ILE   A 1 192 ? 6.448  -30.614 -32.659 1.00 50.08  ?  192 ILE   A C     1 
ATOM   1435 O O     . ILE   A 1 192 ? 5.297  -30.815 -33.069 1.00 42.79  ?  192 ILE   A O     1 
ATOM   1436 C CB    . ILE   A 1 192 ? 6.964  -28.635 -31.123 1.00 48.77  ?  192 ILE   A CB    1 
ATOM   1437 C CG1   . ILE   A 1 192 ? 6.719  -28.152 -29.683 1.00 48.50  ?  192 ILE   A CG1   1 
ATOM   1438 C CG2   . ILE   A 1 192 ? 6.128  -27.882 -32.122 1.00 49.82  ?  192 ILE   A CG2   1 
ATOM   1439 C CD1   . ILE   A 1 192 ? 7.179  -26.741 -29.412 1.00 47.28  ?  192 ILE   A CD1   1 
ATOM   1440 N N     . ALA   A 1 193 ? 7.524  -30.821 -33.435 1.00 52.29  ?  193 ALA   A N     1 
ATOM   1441 C CA    . ALA   A 1 193 ? 7.410  -31.452 -34.750 1.00 45.11  ?  193 ALA   A CA    1 
ATOM   1442 C C     . ALA   A 1 193 ? 6.631  -32.762 -34.673 1.00 45.26  ?  193 ALA   A C     1 
ATOM   1443 O O     . ALA   A 1 193 ? 5.622  -32.936 -35.361 1.00 42.08  ?  193 ALA   A O     1 
ATOM   1444 C CB    . ALA   A 1 193 ? 8.799  -31.686 -35.334 1.00 41.72  ?  193 ALA   A CB    1 
ATOM   1445 N N     . ALA   A 1 194 ? 7.076  -33.688 -33.817 1.00 44.76  ?  194 ALA   A N     1 
ATOM   1446 C CA    . ALA   A 1 194 ? 6.378  -34.966 -33.658 1.00 44.62  ?  194 ALA   A CA    1 
ATOM   1447 C C     . ALA   A 1 194 ? 4.939  -34.777 -33.194 1.00 47.74  ?  194 ALA   A C     1 
ATOM   1448 O O     . ALA   A 1 194 ? 4.049  -35.547 -33.580 1.00 48.69  ?  194 ALA   A O     1 
ATOM   1449 C CB    . ALA   A 1 194 ? 7.122  -35.871 -32.674 1.00 36.66  ?  194 ALA   A CB    1 
ATOM   1450 N N     . ASP   A 1 195 ? 4.682  -33.794 -32.332 1.00 45.27  ?  195 ASP   A N     1 
ATOM   1451 C CA    . ASP   A 1 195 ? 3.288  -33.506 -32.014 1.00 46.29  ?  195 ASP   A CA    1 
ATOM   1452 C C     . ASP   A 1 195 ? 2.576  -32.948 -33.248 1.00 50.50  ?  195 ASP   A C     1 
ATOM   1453 O O     . ASP   A 1 195 ? 1.513  -33.446 -33.645 1.00 52.12  ?  195 ASP   A O     1 
ATOM   1454 C CB    . ASP   A 1 195 ? 3.182  -32.541 -30.821 1.00 43.57  ?  195 ASP   A CB    1 
ATOM   1455 C CG    . ASP   A 1 195 ? 1.729  -32.229 -30.437 1.00 45.10  ?  195 ASP   A CG    1 
ATOM   1456 O OD1   . ASP   A 1 195 ? 0.932  -33.180 -30.349 1.00 50.68  ?  195 ASP   A OD1   1 
ATOM   1457 O OD2   . ASP   A 1 195 ? 1.371  -31.045 -30.236 1.00 42.33  ?  195 ASP   A OD2   1 
ATOM   1458 N N     . LEU   A 1 196 ? 3.168  -31.993 -33.951 1.00 47.45  ?  196 LEU   A N     1 
ATOM   1459 C CA    . LEU   A 1 196 ? 2.445  -31.426 -35.111 1.00 50.31  ?  196 LEU   A CA    1 
ATOM   1460 C C     . LEU   A 1 196 ? 2.302  -32.488 -36.213 1.00 50.35  ?  196 LEU   A C     1 
ATOM   1461 O O     . LEU   A 1 196 ? 1.435  -32.317 -37.073 1.00 47.88  ?  196 LEU   A O     1 
ATOM   1462 C CB    . LEU   A 1 196 ? 3.195  -30.188 -35.591 1.00 46.70  ?  196 LEU   A CB    1 
ATOM   1463 C CG    . LEU   A 1 196 ? 2.919  -28.899 -34.817 1.00 45.57  ?  196 LEU   A CG    1 
ATOM   1464 C CD1   . LEU   A 1 196 ? 3.954  -27.856 -35.173 1.00 44.65  ?  196 LEU   A CD1   1 
ATOM   1465 C CD2   . LEU   A 1 196 ? 1.527  -28.408 -35.136 1.00 46.52  ?  196 LEU   A CD2   1 
ATOM   1466 N N     . SER   A 1 197 ? 3.083  -33.566 -36.149 1.00 51.60  ?  197 SER   A N     1 
ATOM   1467 C CA    . SER   A 1 197 ? 3.079  -34.630 -37.188 1.00 51.48  ?  197 SER   A CA    1 
ATOM   1468 C C     . SER   A 1 197 ? 1.835  -35.507 -37.083 1.00 49.10  ?  197 SER   A C     1 
ATOM   1469 O O     . SER   A 1 197 ? 1.776  -36.514 -37.793 1.00 51.31  ?  197 SER   A O     1 
ATOM   1470 C CB    . SER   A 1 197 ? 4.307  -35.473 -37.081 1.00 47.30  ?  197 SER   A CB    1 
ATOM   1471 O OG    . SER   A 1 197 ? 4.021  -36.736 -36.500 1.00 53.63  ?  197 SER   A OG    1 
ATOM   1472 N N     . ARG   A 1 198 ? 0.903  -35.146 -36.215 1.00 47.20  ?  198 ARG   A N     1 
ATOM   1473 C CA    . ARG   A 1 198 ? -0.310 -35.966 -36.003 1.00 49.21  ?  198 ARG   A CA    1 
ATOM   1474 C C     . ARG   A 1 198 ? -1.534 -35.044 -35.983 1.00 52.27  ?  198 ARG   A C     1 
ATOM   1475 O O     . ARG   A 1 198 ? -2.638 -35.559 -35.771 1.00 50.60  ?  198 ARG   A O     1 
ATOM   1476 C CB    . ARG   A 1 198 ? -0.147 -36.796 -34.728 1.00 52.68  ?  198 ARG   A CB    1 
ATOM   1477 C CG    . ARG   A 1 198 ? 1.198  -37.479 -34.522 1.00 57.28  ?  198 ARG   A CG    1 
ATOM   1478 C CD    . ARG   A 1 198 ? 1.073  -38.856 -33.891 1.00 57.54  ?  198 ARG   A CD    1 
ATOM   1479 N NE    . ARG   A 1 198 ? 2.227  -39.716 -34.167 1.00 58.46  ?  198 ARG   A NE    1 
ATOM   1480 C CZ    . ARG   A 1 198 ? 3.275  -39.850 -33.367 1.00 60.43  ?  198 ARG   A CZ    1 
ATOM   1481 N NH1   . ARG   A 1 198 ? 3.556  -38.915 -32.479 1.00 55.34  ?  198 ARG   A NH1   1 
ATOM   1482 N NH2   . ARG   A 1 198 ? 4.042  -40.919 -33.457 1.00 54.56  ?  198 ARG   A NH2   1 
ATOM   1483 N N     . HIS   A 1 199 ? -1.333 -33.748 -36.250 1.00 56.67  ?  199 HIS   A N     1 
ATOM   1484 C CA    . HIS   A 1 199 ? -2.437 -32.791 -36.275 1.00 58.06  ?  199 HIS   A CA    1 
ATOM   1485 C C     . HIS   A 1 199 ? -2.427 -31.906 -37.526 1.00 59.42  ?  199 HIS   A C     1 
ATOM   1486 O O     . HIS   A 1 199 ? -3.495 -31.629 -38.091 1.00 58.83  ?  199 HIS   A O     1 
ATOM   1487 C CB    . HIS   A 1 199 ? -2.402 -31.900 -34.992 1.00 59.92  ?  199 HIS   A CB    1 
ATOM   1488 C CG    . HIS   A 1 199 ? -2.881 -32.583 -33.740 1.00 62.16  ?  199 HIS   A CG    1 
ATOM   1489 N ND1   . HIS   A 1 199 ? -2.658 -32.066 -32.480 1.00 68.01  ?  199 HIS   A ND1   1 
ATOM   1490 C CD2   . HIS   A 1 199 ? -3.566 -33.735 -33.550 1.00 62.35  ?  199 HIS   A CD2   1 
ATOM   1491 C CE1   . HIS   A 1 199 ? -3.188 -32.861 -31.569 1.00 64.50  ?  199 HIS   A CE1   1 
ATOM   1492 N NE2   . HIS   A 1 199 ? -3.743 -33.885 -32.192 1.00 65.08  ?  199 HIS   A NE2   1 
ATOM   1493 N N     . ALA   A 1 200 ? -1.258 -31.439 -37.966 1.00 55.23  ?  200 ALA   A N     1 
ATOM   1494 C CA    . ALA   A 1 200 ? -1.181 -30.568 -39.134 1.00 60.25  ?  200 ALA   A CA    1 
ATOM   1495 C C     . ALA   A 1 200 ? -1.219 -31.389 -40.414 1.00 63.93  ?  200 ALA   A C     1 
ATOM   1496 O O     . ALA   A 1 200 ? -0.708 -32.511 -40.472 1.00 60.18  ?  200 ALA   A O     1 
ATOM   1497 C CB    . ALA   A 1 200 ? 0.097  -29.727 -39.100 1.00 55.39  ?  200 ALA   A CB    1 
ATOM   1498 N N     . GLU   A 1 201 ? -1.821 -30.817 -41.459 1.00 64.07  ?  201 GLU   A N     1 
ATOM   1499 C CA    . GLU   A 1 201 ? -1.869 -31.548 -42.720 1.00 66.05  ?  201 GLU   A CA    1 
ATOM   1500 C C     . GLU   A 1 201 ? -0.473 -31.871 -43.241 1.00 65.98  ?  201 GLU   A C     1 
ATOM   1501 O O     . GLU   A 1 201 ? -0.320 -32.774 -44.073 1.00 65.73  ?  201 GLU   A O     1 
ATOM   1502 C CB    . GLU   A 1 201 ? -2.653 -30.761 -43.772 1.00 72.88  ?  201 GLU   A CB    1 
ATOM   1503 C CG    . GLU   A 1 201 ? -2.961 -31.575 -45.031 1.00 79.96  ?  201 GLU   A CG    1 
ATOM   1504 C CD    . GLU   A 1 201 ? -3.847 -30.847 -46.027 1.00 81.29  ?  201 GLU   A CD    1 
ATOM   1505 O OE1   . GLU   A 1 201 ? -3.588 -29.655 -46.316 1.00 83.25  ?  201 GLU   A OE1   1 
ATOM   1506 O OE2   . GLU   A 1 201 ? -4.798 -31.483 -46.530 1.00 83.65  ?  201 GLU   A OE2   1 
ATOM   1507 N N     . ARG   A 1 202 ? 0.551  -31.191 -42.728 1.00 64.49  ?  202 ARG   A N     1 
ATOM   1508 C CA    . ARG   A 1 202 ? 1.921  -31.320 -43.206 1.00 61.71  ?  202 ARG   A CA    1 
ATOM   1509 C C     . ARG   A 1 202 ? 2.811  -30.520 -42.260 1.00 57.01  ?  202 ARG   A C     1 
ATOM   1510 O O     . ARG   A 1 202 ? 2.439  -29.406 -41.864 1.00 52.67  ?  202 ARG   A O     1 
ATOM   1511 C CB    . ARG   A 1 202 ? 2.027  -30.814 -44.660 1.00 62.39  ?  202 ARG   A CB    1 
ATOM   1512 C CG    . ARG   A 1 202 ? 3.390  -30.909 -45.302 1.00 60.13  ?  202 ARG   A CG    1 
ATOM   1513 C CD    . ARG   A 1 202 ? 3.256  -31.128 -46.791 1.00 52.12  ?  202 ARG   A CD    1 
ATOM   1514 N NE    . ARG   A 1 202 ? 4.365  -31.927 -47.306 1.00 44.19  ?  202 ARG   A NE    1 
ATOM   1515 C CZ    . ARG   A 1 202 ? 5.420  -31.420 -47.935 1.00 51.47  ?  202 ARG   A CZ    1 
ATOM   1516 N NH1   . ARG   A 1 202 ? 5.511  -30.113 -48.147 1.00 56.66  ?  202 ARG   A NH1   1 
ATOM   1517 N NH2   . ARG   A 1 202 ? 6.385  -32.222 -48.363 1.00 50.12  ?  202 ARG   A NH2   1 
ATOM   1518 N N     . THR   A 1 203 ? 3.960  -31.108 -41.865 1.00 57.32  ?  203 THR   A N     1 
ATOM   1519 C CA    . THR   A 1 203 ? 4.914  -30.470 -40.954 1.00 51.60  ?  203 THR   A CA    1 
ATOM   1520 C C     . THR   A 1 203 ? 6.333  -30.494 -41.519 1.00 49.16  ?  203 THR   A C     1 
ATOM   1521 O O     . THR   A 1 203 ? 6.766  -31.494 -42.108 1.00 49.65  ?  203 THR   A O     1 
ATOM   1522 C CB    . THR   A 1 203 ? 4.946  -31.135 -39.545 1.00 49.83  ?  203 THR   A CB    1 
ATOM   1523 O OG1   . THR   A 1 203 ? 3.654  -31.601 -39.136 1.00 50.75  ?  203 THR   A OG1   1 
ATOM   1524 C CG2   . THR   A 1 203 ? 5.423  -30.131 -38.536 1.00 49.82  ?  203 THR   A CG2   1 
ATOM   1525 N N     . LEU   A 1 204 ? 7.075  -29.410 -41.286 1.00 48.55  ?  204 LEU   A N     1 
ATOM   1526 C CA    . LEU   A 1 204 ? 8.410  -29.256 -41.853 1.00 51.76  ?  204 LEU   A CA    1 
ATOM   1527 C C     . LEU   A 1 204 ? 9.391  -28.753 -40.808 1.00 53.02  ?  204 LEU   A C     1 
ATOM   1528 O O     . LEU   A 1 204 ? 9.129  -27.738 -40.154 1.00 55.17  ?  204 LEU   A O     1 
ATOM   1529 C CB    . LEU   A 1 204 ? 8.399  -28.275 -43.026 1.00 55.41  ?  204 LEU   A CB    1 
ATOM   1530 C CG    . LEU   A 1 204 ? 7.533  -28.637 -44.212 1.00 46.81  ?  204 LEU   A CG    1 
ATOM   1531 C CD1   . LEU   A 1 204 ? 6.943  -27.352 -44.721 1.00 46.66  ?  204 LEU   A CD1   1 
ATOM   1532 C CD2   . LEU   A 1 204 ? 8.428  -29.305 -45.212 1.00 45.74  ?  204 LEU   A CD2   1 
ATOM   1533 N N     . LEU   A 1 205 ? 10.545 -29.431 -40.713 1.00 49.90  ?  205 LEU   A N     1 
ATOM   1534 C CA    . LEU   A 1 205 ? 11.605 -29.153 -39.746 1.00 49.61  ?  205 LEU   A CA    1 
ATOM   1535 C C     . LEU   A 1 205 ? 12.772 -28.457 -40.452 1.00 50.17  ?  205 LEU   A C     1 
ATOM   1536 O O     . LEU   A 1 205 ? 13.566 -29.097 -41.152 1.00 49.13  ?  205 LEU   A O     1 
ATOM   1537 C CB    . LEU   A 1 205 ? 12.054 -30.451 -39.072 1.00 45.28  ?  205 LEU   A CB    1 
ATOM   1538 C CG    . LEU   A 1 205 ? 12.856 -30.375 -37.757 1.00 49.77  ?  205 LEU   A CG    1 
ATOM   1539 C CD1   . LEU   A 1 205 ? 12.005 -29.928 -36.542 1.00 44.57  ?  205 LEU   A CD1   1 
ATOM   1540 C CD2   . LEU   A 1 205 ? 13.526 -31.715 -37.489 1.00 43.05  ?  205 LEU   A CD2   1 
ATOM   1541 N N     . SER   A 1 206 ? 12.894 -27.151 -40.239 1.00 46.37  ?  206 SER   A N     1 
ATOM   1542 C CA    . SER   A 1 206 ? 13.946 -26.362 -40.869 1.00 48.22  ?  206 SER   A CA    1 
ATOM   1543 C C     . SER   A 1 206 ? 15.165 -26.341 -39.949 1.00 55.34  ?  206 SER   A C     1 
ATOM   1544 O O     . SER   A 1 206 ? 15.051 -25.962 -38.775 1.00 45.54  ?  206 SER   A O     1 
ATOM   1545 C CB    . SER   A 1 206 ? 13.448 -24.946 -41.161 1.00 47.50  ?  206 SER   A CB    1 
ATOM   1546 O OG    . SER   A 1 206 ? 14.465 -24.174 -41.777 1.00 50.05  ?  206 SER   A OG    1 
ATOM   1547 N N     . VAL   A 1 207 ? 16.317 -26.801 -40.474 1.00 53.93  ?  207 VAL   A N     1 
ATOM   1548 C CA    . VAL   A 1 207 ? 17.554 -26.986 -39.659 1.00 49.61  ?  207 VAL   A CA    1 
ATOM   1549 C C     . VAL   A 1 207 ? 18.787 -26.350 -40.312 1.00 49.10  ?  207 VAL   A C     1 
ATOM   1550 O O     . VAL   A 1 207 ? 18.958 -26.525 -41.512 1.00 54.87  ?  207 VAL   A O     1 
ATOM   1551 C CB    . VAL   A 1 207 ? 17.726 -28.512 -39.575 1.00 48.96  ?  207 VAL   A CB    1 
ATOM   1552 C CG1   . VAL   A 1 207 ? 19.052 -28.914 -38.950 1.00 52.48  ?  207 VAL   A CG1   1 
ATOM   1553 C CG2   . VAL   A 1 207 ? 16.568 -29.190 -38.855 1.00 48.20  ?  207 VAL   A CG2   1 
ATOM   1554 N N     . ARG   A 1 208 ? 19.664 -25.734 -39.523 1.00 54.93  ?  208 ARG   A N     1 
ATOM   1555 C CA    . ARG   A 1 208 ? 20.846 -25.021 -40.076 1.00 58.03  ?  208 ARG   A CA    1 
ATOM   1556 C C     . ARG   A 1 208 ? 22.147 -25.752 -39.732 1.00 60.74  ?  208 ARG   A C     1 
ATOM   1557 O O     . ARG   A 1 208 ? 23.139 -25.550 -40.446 1.00 66.09  ?  208 ARG   A O     1 
ATOM   1558 C CB    . ARG   A 1 208 ? 20.867 -23.583 -39.544 1.00 66.26  ?  208 ARG   A CB    1 
ATOM   1559 C CG    . ARG   A 1 208 ? 22.129 -23.053 -38.882 1.00 69.86  ?  208 ARG   A CG    1 
ATOM   1560 C CD    . ARG   A 1 208 ? 21.921 -21.642 -38.369 1.00 79.65  ?  208 ARG   A CD    1 
ATOM   1561 N NE    . ARG   A 1 208 ? 21.900 -21.609 -36.904 1.00 85.12  ?  208 ARG   A NE    1 
ATOM   1562 C CZ    . ARG   A 1 208 ? 22.175 -20.537 -36.180 1.00 87.68  ?  208 ARG   A CZ    1 
ATOM   1563 N NH1   . ARG   A 1 208 ? 22.356 -20.647 -34.877 1.00 86.22  ?  208 ARG   A NH1   1 
ATOM   1564 N NH2   . ARG   A 1 208 ? 22.266 -19.358 -36.765 1.00 86.25  ?  208 ARG   A NH2   1 
ATOM   1565 N N     . ARG   A 1 209 ? 22.132 -26.577 -38.698 1.00 63.84  ?  209 ARG   A N     1 
ATOM   1566 C CA    . ARG   A 1 209 ? 23.346 -27.295 -38.253 1.00 64.27  ?  209 ARG   A CA    1 
ATOM   1567 C C     . ARG   A 1 209 ? 22.928 -28.660 -37.709 1.00 61.86  ?  209 ARG   A C     1 
ATOM   1568 O O     . ARG   A 1 209 ? 21.822 -28.764 -37.176 1.00 65.58  ?  209 ARG   A O     1 
ATOM   1569 C CB    . ARG   A 1 209 ? 24.030 -26.475 -37.160 1.00 68.55  ?  209 ARG   A CB    1 
ATOM   1570 C CG    . ARG   A 1 209 ? 25.516 -26.704 -36.936 1.00 74.84  ?  209 ARG   A CG    1 
ATOM   1571 C CD    . ARG   A 1 209 ? 26.136 -25.435 -36.379 1.00 85.28  ?  209 ARG   A CD    1 
ATOM   1572 N NE    . ARG   A 1 209 ? 25.431 -24.240 -36.857 1.00 90.08  ?  209 ARG   A NE    1 
ATOM   1573 C CZ    . ARG   A 1 209 ? 25.283 -23.121 -36.165 1.00 91.03  ?  209 ARG   A CZ    1 
ATOM   1574 N NH1   . ARG   A 1 209 ? 25.223 -21.960 -36.788 1.00 86.67  ?  209 ARG   A NH1   1 
ATOM   1575 N NH2   . ARG   A 1 209 ? 25.189 -23.166 -34.851 1.00 93.48  ?  209 ARG   A NH2   1 
ATOM   1576 N N     . GLY   A 1 210 ? 23.800 -29.650 -37.807 1.00 56.67  ?  210 GLY   A N     1 
ATOM   1577 C CA    . GLY   A 1 210 ? 23.439 -31.006 -37.384 1.00 58.30  ?  210 GLY   A CA    1 
ATOM   1578 C C     . GLY   A 1 210 ? 23.751 -31.319 -35.942 1.00 61.69  ?  210 GLY   A C     1 
ATOM   1579 O O     . GLY   A 1 210 ? 24.822 -30.918 -35.467 1.00 59.19  ?  210 GLY   A O     1 
ATOM   1580 N N     . LEU   A 1 211 ? 22.832 -32.004 -35.274 1.00 60.15  ?  211 LEU   A N     1 
ATOM   1581 C CA    . LEU   A 1 211 ? 23.053 -32.433 -33.879 1.00 57.56  ?  211 LEU   A CA    1 
ATOM   1582 C C     . LEU   A 1 211 ? 22.900 -33.954 -33.862 1.00 54.50  ?  211 LEU   A C     1 
ATOM   1583 O O     . LEU   A 1 211 ? 22.242 -34.487 -34.756 1.00 57.17  ?  211 LEU   A O     1 
ATOM   1584 C CB    . LEU   A 1 211 ? 22.043 -31.753 -32.960 1.00 52.96  ?  211 LEU   A CB    1 
ATOM   1585 C CG    . LEU   A 1 211 ? 22.117 -30.229 -32.856 1.00 54.45  ?  211 LEU   A CG    1 
ATOM   1586 C CD1   . LEU   A 1 211 ? 21.132 -29.752 -31.810 1.00 49.27  ?  211 LEU   A CD1   1 
ATOM   1587 C CD2   . LEU   A 1 211 ? 23.520 -29.781 -32.509 1.00 60.38  ?  211 LEU   A CD2   1 
ATOM   1588 N N     . HIS   A 1 212 ? 23.499 -34.617 -32.886 1.00 60.67  ?  212 HIS   A N     1 
ATOM   1589 C CA    . HIS   A 1 212 ? 23.391 -36.090 -32.764 1.00 61.82  ?  212 HIS   A CA    1 
ATOM   1590 C C     . HIS   A 1 212 ? 22.026 -36.452 -32.182 1.00 60.84  ?  212 HIS   A C     1 
ATOM   1591 O O     . HIS   A 1 212 ? 21.722 -36.044 -31.054 1.00 62.36  ?  212 HIS   A O     1 
ATOM   1592 C CB    . HIS   A 1 212 ? 24.552 -36.626 -31.928 1.00 59.92  ?  212 HIS   A CB    1 
ATOM   1593 C CG    . HIS   A 1 212 ? 25.895 -36.348 -32.506 1.00 63.29  ?  212 HIS   A CG    1 
ATOM   1594 N ND1   . HIS   A 1 212 ? 26.481 -37.169 -33.441 1.00 62.91  ?  212 HIS   A ND1   1 
ATOM   1595 C CD2   . HIS   A 1 212 ? 26.761 -35.360 -32.285 1.00 62.74  ?  212 HIS   A CD2   1 
ATOM   1596 C CE1   . HIS   A 1 212 ? 27.664 -36.679 -33.766 1.00 69.57  ?  212 HIS   A CE1   1 
ATOM   1597 N NE2   . HIS   A 1 212 ? 27.853 -35.581 -33.075 1.00 67.49  ?  212 HIS   A NE2   1 
ATOM   1598 N N     . ILE   A 1 213 ? 21.225 -37.183 -32.954 1.00 57.89  ?  213 ILE   A N     1 
ATOM   1599 C CA    . ILE   A 1 213 ? 19.877 -37.612 -32.488 1.00 53.42  ?  213 ILE   A CA    1 
ATOM   1600 C C     . ILE   A 1 213 ? 20.029 -38.984 -31.828 1.00 51.01  ?  213 ILE   A C     1 
ATOM   1601 O O     . ILE   A 1 213 ? 20.439 -39.913 -32.507 1.00 55.70  ?  213 ILE   A O     1 
ATOM   1602 C CB    . ILE   A 1 213 ? 18.858 -37.590 -33.636 1.00 53.72  ?  213 ILE   A CB    1 
ATOM   1603 C CG1   . ILE   A 1 213 ? 18.807 -36.219 -34.306 1.00 53.70  ?  213 ILE   A CG1   1 
ATOM   1604 C CG2   . ILE   A 1 213 ? 17.484 -38.043 -33.148 1.00 50.58  ?  213 ILE   A CG2   1 
ATOM   1605 C CD1   . ILE   A 1 213 ? 17.743 -35.292 -33.752 1.00 45.65  ?  213 ILE   A CD1   1 
ATOM   1606 N N     . VAL   A 1 214 ? 19.637 -39.102 -30.575 1.00 55.30  ?  214 VAL   A N     1 
ATOM   1607 C CA    . VAL   A 1 214 ? 19.875 -40.301 -29.762 1.00 51.10  ?  214 VAL   A CA    1 
ATOM   1608 C C     . VAL   A 1 214 ? 18.576 -40.822 -29.153 1.00 45.46  ?  214 VAL   A C     1 
ATOM   1609 O O     . VAL   A 1 214 ? 17.762 -40.015 -28.687 1.00 48.98  ?  214 VAL   A O     1 
ATOM   1610 C CB    . VAL   A 1 214 ? 20.917 -39.988 -28.673 1.00 50.18  ?  214 VAL   A CB    1 
ATOM   1611 C CG1   . VAL   A 1 214 ? 21.143 -41.172 -27.795 1.00 49.39  ?  214 VAL   A CG1   1 
ATOM   1612 C CG2   . VAL   A 1 214 ? 22.230 -39.572 -29.311 1.00 50.09  ?  214 VAL   A CG2   1 
ATOM   1613 N N     . PRO   A 1 215 ? 18.326 -42.136 -29.135 1.00 44.02  ?  215 PRO   A N     1 
ATOM   1614 C CA    . PRO   A 1 215 ? 17.119 -42.642 -28.476 1.00 45.94  ?  215 PRO   A CA    1 
ATOM   1615 C C     . PRO   A 1 215 ? 17.293 -42.657 -26.964 1.00 49.90  ?  215 PRO   A C     1 
ATOM   1616 O O     . PRO   A 1 215 ? 18.397 -42.525 -26.432 1.00 51.03  ?  215 PRO   A O     1 
ATOM   1617 C CB    . PRO   A 1 215 ? 16.983 -44.062 -29.033 1.00 44.77  ?  215 PRO   A CB    1 
ATOM   1618 C CG    . PRO   A 1 215 ? 18.385 -44.495 -29.206 1.00 45.80  ?  215 PRO   A CG    1 
ATOM   1619 C CD    . PRO   A 1 215 ? 19.153 -43.247 -29.640 1.00 45.12  ?  215 PRO   A CD    1 
ATOM   1620 N N     . LYS   A 1 216 ? 16.191 -42.829 -26.244 1.00 51.76  ?  216 LYS   A N     1 
ATOM   1621 C CA    . LYS   A 1 216 ? 16.230 -42.732 -24.766 1.00 48.97  ?  216 LYS   A CA    1 
ATOM   1622 C C     . LYS   A 1 216 ? 16.436 -44.106 -24.147 1.00 49.12  ?  216 LYS   A C     1 
ATOM   1623 O O     . LYS   A 1 216 ? 15.983 -44.309 -23.018 1.00 56.89  ?  216 LYS   A O     1 
ATOM   1624 C CB    . LYS   A 1 216 ? 14.888 -42.178 -24.286 1.00 46.80  ?  216 LYS   A CB    1 
ATOM   1625 C CG    . LYS   A 1 216 ? 14.457 -40.830 -24.823 1.00 45.31  ?  216 LYS   A CG    1 
ATOM   1626 C CD    . LYS   A 1 216 ? 12.954 -40.647 -24.669 1.00 48.93  ?  216 LYS   A CD    1 
ATOM   1627 C CE    . LYS   A 1 216 ? 12.587 -39.505 -23.779 1.00 47.96  ?  216 LYS   A CE    1 
ATOM   1628 N NZ    . LYS   A 1 216 ? 11.329 -39.741 -23.069 1.00 39.12  ?  216 LYS   A NZ    1 
ATOM   1629 N N     . GLN   A 1 217 ? 17.116 -44.994 -24.855 1.00 51.12  ?  217 GLN   A N     1 
ATOM   1630 C CA    . GLN   A 1 217 ? 17.230 -46.379 -24.354 1.00 55.53  ?  217 GLN   A CA    1 
ATOM   1631 C C     . GLN   A 1 217 ? 18.167 -47.202 -25.227 1.00 54.39  ?  217 GLN   A C     1 
ATOM   1632 O O     . GLN   A 1 217 ? 17.893 -47.330 -26.425 1.00 60.97  ?  217 GLN   A O     1 
ATOM   1633 C CB    . GLN   A 1 217 ? 15.875 -47.084 -24.379 1.00 54.82  ?  217 GLN   A CB    1 
ATOM   1634 C CG    . GLN   A 1 217 ? 15.935 -48.575 -24.075 1.00 55.71  ?  217 GLN   A CG    1 
ATOM   1635 C CD    . GLN   A 1 217 ? 15.926 -49.443 -25.313 1.00 57.86  ?  217 GLN   A CD    1 
ATOM   1636 O OE1   . GLN   A 1 217 ? 16.871 -50.191 -25.581 1.00 57.88  ?  217 GLN   A OE1   1 
ATOM   1637 N NE2   . GLN   A 1 217 ? 14.860 -49.342 -26.088 1.00 59.81  ?  217 GLN   A NE2   1 
ATOM   1638 N N     . LEU   A 1 218 ? 19.228 -47.728 -24.635 1.00 52.17  ?  218 LEU   A N     1 
ATOM   1639 C CA    . LEU   A 1 218 ? 20.108 -48.663 -25.361 1.00 54.44  ?  218 LEU   A CA    1 
ATOM   1640 C C     . LEU   A 1 218 ? 20.237 -49.891 -24.453 1.00 55.03  ?  218 LEU   A C     1 
ATOM   1641 O O     . LEU   A 1 218 ? 20.505 -49.700 -23.266 1.00 58.77  ?  218 LEU   A O     1 
ATOM   1642 C CB    . LEU   A 1 218 ? 21.445 -48.008 -25.688 1.00 55.37  ?  218 LEU   A CB    1 
ATOM   1643 C CG    . LEU   A 1 218 ? 21.383 -46.727 -26.522 1.00 57.06  ?  218 LEU   A CG    1 
ATOM   1644 C CD1   . LEU   A 1 218 ? 22.737 -46.051 -26.552 1.00 53.54  ?  218 LEU   A CD1   1 
ATOM   1645 C CD2   . LEU   A 1 218 ? 20.909 -47.024 -27.927 1.00 48.81  ?  218 LEU   A CD2   1 
ATOM   1646 N N     . PHE   A 1 219 ? 19.992 -51.085 -24.983 1.00 55.93  ?  219 PHE   A N     1 
ATOM   1647 C CA    . PHE   A 1 219 ? 20.019 -52.336 -24.182 1.00 60.51  ?  219 PHE   A CA    1 
ATOM   1648 C C     . PHE   A 1 219 ? 18.951 -52.259 -23.084 1.00 60.08  ?  219 PHE   A C     1 
ATOM   1649 O O     . PHE   A 1 219 ? 19.188 -52.797 -21.994 1.00 62.17  ?  219 PHE   A O     1 
ATOM   1650 C CB    . PHE   A 1 219 ? 21.401 -52.637 -23.597 1.00 62.77  ?  219 PHE   A CB    1 
ATOM   1651 C CG    . PHE   A 1 219 ? 22.593 -52.701 -24.538 1.00 63.25  ?  219 PHE   A CG    1 
ATOM   1652 C CD1   . PHE   A 1 219 ? 23.116 -51.551 -25.116 1.00 65.32  ?  219 PHE   A CD1   1 
ATOM   1653 C CD2   . PHE   A 1 219 ? 23.221 -53.911 -24.800 1.00 61.03  ?  219 PHE   A CD2   1 
ATOM   1654 C CE1   . PHE   A 1 219 ? 24.209 -51.618 -25.962 1.00 67.16  ?  219 PHE   A CE1   1 
ATOM   1655 C CE2   . PHE   A 1 219 ? 24.318 -53.970 -25.642 1.00 70.27  ?  219 PHE   A CE2   1 
ATOM   1656 C CZ    . PHE   A 1 219 ? 24.810 -52.824 -26.220 1.00 69.37  ?  219 PHE   A CZ    1 
ATOM   1657 N N     . GLY   A 1 220 ? 17.806 -51.637 -23.368 1.00 56.97  ?  220 GLY   A N     1 
ATOM   1658 C CA    . GLY   A 1 220 ? 16.706 -51.519 -22.391 1.00 56.17  ?  220 GLY   A CA    1 
ATOM   1659 C C     . GLY   A 1 220 ? 17.013 -50.476 -21.351 1.00 55.72  ?  220 GLY   A C     1 
ATOM   1660 O O     . GLY   A 1 220 ? 16.112 -50.139 -20.575 1.00 54.34  ?  220 GLY   A O     1 
ATOM   1661 N N     . MET   A 1 221 ? 18.212 -49.919 -21.387 1.00 55.71  ?  221 MET   A N     1 
ATOM   1662 C CA    . MET   A 1 221 ? 18.664 -49.023 -20.337 1.00 54.12  ?  221 MET   A CA    1 
ATOM   1663 C C     . MET   A 1 221 ? 18.522 -47.570 -20.763 1.00 56.24  ?  221 MET   A C     1 
ATOM   1664 O O     . MET   A 1 221 ? 18.987 -47.187 -21.839 1.00 51.30  ?  221 MET   A O     1 
ATOM   1665 C CB    . MET   A 1 221 ? 20.121 -49.318 -20.002 1.00 52.35  ?  221 MET   A CB    1 
ATOM   1666 C CG    . MET   A 1 221 ? 20.376 -50.689 -19.436 1.00 54.98  ?  221 MET   A CG    1 
ATOM   1667 S SD    . MET   A 1 221 ? 21.926 -50.727 -18.507 1.00 76.55  ?  221 MET   A SD    1 
ATOM   1668 C CE    . MET   A 1 221 ? 21.794 -49.241 -17.505 1.00 54.16  ?  221 MET   A CE    1 
ATOM   1669 N N     . SER   A 1 222 ? 17.898 -46.759 -19.911 1.00 56.88  ?  222 SER   A N     1 
ATOM   1670 C CA    . SER   A 1 222 ? 17.917 -45.323 -20.141 1.00 56.51  ?  222 SER   A CA    1 
ATOM   1671 C C     . SER   A 1 222 ? 19.345 -44.814 -20.241 1.00 58.28  ?  222 SER   A C     1 
ATOM   1672 O O     . SER   A 1 222 ? 20.254 -45.321 -19.581 1.00 60.03  ?  222 SER   A O     1 
ATOM   1673 C CB    . SER   A 1 222 ? 17.199 -44.584 -19.026 1.00 56.83  ?  222 SER   A CB    1 
ATOM   1674 O OG    . SER   A 1 222 ? 15.855 -44.353 -19.385 1.00 61.65  ?  222 SER   A OG    1 
ATOM   1675 N N     . VAL   A 1 223 ? 19.531 -43.782 -21.066 1.00 59.59  ?  223 VAL   A N     1 
ATOM   1676 C CA    . VAL   A 1 223 ? 20.869 -43.249 -21.294 1.00 62.14  ?  223 VAL   A CA    1 
ATOM   1677 C C     . VAL   A 1 223 ? 21.518 -42.789 -19.989 1.00 61.54  ?  223 VAL   A C     1 
ATOM   1678 O O     . VAL   A 1 223 ? 22.743 -42.882 -19.829 1.00 65.22  ?  223 VAL   A O     1 
ATOM   1679 C CB    . VAL   A 1 223 ? 20.810 -42.124 -22.347 1.00 63.28  ?  223 VAL   A CB    1 
ATOM   1680 C CG1   . VAL   A 1 223 ? 20.778 -42.717 -23.747 1.00 55.12  ?  223 VAL   A CG1   1 
ATOM   1681 C CG2   . VAL   A 1 223 ? 19.587 -41.238 -22.120 1.00 63.72  ?  223 VAL   A CG2   1 
ATOM   1682 N N     . ASP   A 1 224 ? 20.722 -42.326 -19.024 1.00 60.29  ?  224 ASP   A N     1 
ATOM   1683 C CA    . ASP   A 1 224 ? 21.281 -41.907 -17.740 1.00 60.10  ?  224 ASP   A CA    1 
ATOM   1684 C C     . ASP   A 1 224 ? 21.471 -43.068 -16.761 1.00 59.63  ?  224 ASP   A C     1 
ATOM   1685 O O     . ASP   A 1 224 ? 22.310 -42.967 -15.862 1.00 62.92  ?  224 ASP   A O     1 
ATOM   1686 C CB    . ASP   A 1 224 ? 20.411 -40.796 -17.124 1.00 60.15  ?  224 ASP   A CB    1 
ATOM   1687 C CG    . ASP   A 1 224 ? 18.926 -41.170 -17.031 1.00 63.27  ?  224 ASP   A CG    1 
ATOM   1688 O OD1   . ASP   A 1 224 ? 18.553 -42.260 -17.524 1.00 64.66  ?  224 ASP   A OD1   1 
ATOM   1689 O OD2   . ASP   A 1 224 ? 18.127 -40.365 -16.481 1.00 57.88  ?  224 ASP   A OD2   1 
ATOM   1690 N N     . GLU   A 1 225 ? 20.723 -44.165 -16.914 1.00 59.23  ?  225 GLU   A N     1 
ATOM   1691 C CA    . GLU   A 1 225 ? 21.032 -45.385 -16.169 1.00 59.54  ?  225 GLU   A CA    1 
ATOM   1692 C C     . GLU   A 1 225 ? 22.345 -46.007 -16.641 1.00 63.65  ?  225 GLU   A C     1 
ATOM   1693 O O     . GLU   A 1 225 ? 23.133 -46.501 -15.829 1.00 65.52  ?  225 GLU   A O     1 
ATOM   1694 C CB    . GLU   A 1 225 ? 19.895 -46.399 -16.308 1.00 58.60  ?  225 GLU   A CB    1 
ATOM   1695 C CG    . GLU   A 1 225 ? 18.585 -46.024 -15.621 1.00 60.21  ?  225 GLU   A CG    1 
ATOM   1696 C CD    . GLU   A 1 225 ? 17.585 -47.177 -15.591 1.00 64.21  ?  225 GLU   A CD    1 
ATOM   1697 O OE1   . GLU   A 1 225 ? 17.993 -48.337 -15.849 1.00 67.45  ?  225 GLU   A OE1   1 
ATOM   1698 O OE2   . GLU   A 1 225 ? 16.387 -46.921 -15.325 1.00 61.97  ?  225 GLU   A OE2   1 
ATOM   1699 N N     . ILE   A 1 226 ? 22.583 -46.028 -17.955 1.00 65.20  ?  226 ILE   A N     1 
ATOM   1700 C CA    . ILE   A 1 226 ? 23.888 -46.439 -18.473 1.00 67.76  ?  226 ILE   A CA    1 
ATOM   1701 C C     . ILE   A 1 226 ? 24.987 -45.637 -17.796 1.00 64.39  ?  226 ILE   A C     1 
ATOM   1702 O O     . ILE   A 1 226 ? 26.045 -46.169 -17.438 1.00 59.53  ?  226 ILE   A O     1 
ATOM   1703 C CB    . ILE   A 1 226 ? 23.930 -46.277 -20.011 1.00 62.47  ?  226 ILE   A CB    1 
ATOM   1704 C CG1   . ILE   A 1 226 ? 23.103 -47.366 -20.690 1.00 57.81  ?  226 ILE   A CG1   1 
ATOM   1705 C CG2   . ILE   A 1 226 ? 25.355 -46.325 -20.544 1.00 60.75  ?  226 ILE   A CG2   1 
ATOM   1706 C CD1   . ILE   A 1 226 ? 22.095 -46.824 -21.684 1.00 57.91  ?  226 ILE   A CD1   1 
ATOM   1707 N N     . ALA   A 1 227 ? 24.733 -44.347 -17.591 1.00 63.71  ?  227 ALA   A N     1 
ATOM   1708 C CA    . ALA   A 1 227 ? 25.747 -43.456 -17.051 1.00 67.81  ?  227 ALA   A CA    1 
ATOM   1709 C C     . ALA   A 1 227 ? 26.250 -43.932 -15.694 1.00 74.91  ?  227 ALA   A C     1 
ATOM   1710 O O     . ALA   A 1 227 ? 27.437 -43.787 -15.379 1.00 78.80  ?  227 ALA   A O     1 
ATOM   1711 C CB    . ALA   A 1 227 ? 25.181 -42.044 -16.948 1.00 63.31  ?  227 ALA   A CB    1 
ATOM   1712 N N     . GLU   A 1 228 ? 25.370 -44.506 -14.875 1.00 74.96  ?  228 GLU   A N     1 
ATOM   1713 C CA    . GLU   A 1 228 ? 25.745 -44.831 -13.506 1.00 80.07  ?  228 GLU   A CA    1 
ATOM   1714 C C     . GLU   A 1 228 ? 26.324 -46.230 -13.352 1.00 85.11  ?  228 GLU   A C     1 
ATOM   1715 O O     . GLU   A 1 228 ? 26.979 -46.501 -12.336 1.00 85.98  ?  228 GLU   A O     1 
ATOM   1716 C CB    . GLU   A 1 228 ? 24.541 -44.668 -12.575 1.00 79.98  ?  228 GLU   A CB    1 
ATOM   1717 C CG    . GLU   A 1 228 ? 24.721 -43.535 -11.581 1.00 89.30  ?  228 GLU   A CG    1 
ATOM   1718 C CD    . GLU   A 1 228 ? 23.582 -43.442 -10.596 1.00 95.20  ?  228 GLU   A CD    1 
ATOM   1719 O OE1   . GLU   A 1 228 ? 23.843 -43.479 -9.369  1.00 102.54 ?  228 GLU   A OE1   1 
ATOM   1720 O OE2   . GLU   A 1 228 ? 22.423 -43.336 -11.051 1.00 89.80  ?  228 GLU   A OE2   1 
ATOM   1721 N N     . ALA   A 1 229 ? 26.102 -47.112 -14.326 1.00 83.04  ?  229 ALA   A N     1 
ATOM   1722 C CA    . ALA   A 1 229 ? 26.653 -48.455 -14.265 1.00 84.41  ?  229 ALA   A CA    1 
ATOM   1723 C C     . ALA   A 1 229 ? 28.175 -48.392 -14.196 1.00 87.83  ?  229 ALA   A C     1 
ATOM   1724 O O     . ALA   A 1 229 ? 28.796 -47.506 -14.786 1.00 87.90  ?  229 ALA   A O     1 
ATOM   1725 C CB    . ALA   A 1 229 ? 26.225 -49.275 -15.478 1.00 86.00  ?  229 ALA   A CB    1 
ATOM   1726 N N     . PRO   A 1 230 ? 28.803 -49.320 -13.475 1.00 91.58  ?  230 PRO   A N     1 
ATOM   1727 C CA    . PRO   A 1 230 ? 30.257 -49.227 -13.294 1.00 93.25  ?  230 PRO   A CA    1 
ATOM   1728 C C     . PRO   A 1 230 ? 31.038 -49.573 -14.545 1.00 93.53  ?  230 PRO   A C     1 
ATOM   1729 O O     . PRO   A 1 230 ? 32.125 -49.017 -14.746 1.00 93.17  ?  230 PRO   A O     1 
ATOM   1730 C CB    . PRO   A 1 230 ? 30.535 -50.221 -12.158 1.00 96.26  ?  230 PRO   A CB    1 
ATOM   1731 C CG    . PRO   A 1 230 ? 29.181 -50.470 -11.518 1.00 99.62  ?  230 PRO   A CG    1 
ATOM   1732 C CD    . PRO   A 1 230 ? 28.216 -50.388 -12.656 1.00 92.52  ?  230 PRO   A CD    1 
ATOM   1733 N N     . TRP   A 1 231 ? 30.518 -50.462 -15.398 1.00 92.25  ?  231 TRP   A N     1 
ATOM   1734 C CA    . TRP   A 1 231 ? 31.238 -50.806 -16.620 1.00 91.24  ?  231 TRP   A CA    1 
ATOM   1735 C C     . TRP   A 1 231 ? 31.345 -49.613 -17.565 1.00 91.81  ?  231 TRP   A C     1 
ATOM   1736 O O     . TRP   A 1 231 ? 32.285 -49.543 -18.366 1.00 91.78  ?  231 TRP   A O     1 
ATOM   1737 C CB    . TRP   A 1 231 ? 30.573 -51.997 -17.311 1.00 88.56  ?  231 TRP   A CB    1 
ATOM   1738 C CG    . TRP   A 1 231 ? 29.132 -51.787 -17.683 1.00 93.83  ?  231 TRP   A CG    1 
ATOM   1739 C CD1   . TRP   A 1 231 ? 28.032 -52.185 -16.974 1.00 96.46  ?  231 TRP   A CD1   1 
ATOM   1740 C CD2   . TRP   A 1 231 ? 28.633 -51.144 -18.867 1.00 94.51  ?  231 TRP   A CD2   1 
ATOM   1741 N NE1   . TRP   A 1 231 ? 26.880 -51.824 -17.639 1.00 93.66  ?  231 TRP   A NE1   1 
ATOM   1742 C CE2   . TRP   A 1 231 ? 27.224 -51.185 -18.803 1.00 94.76  ?  231 TRP   A CE2   1 
ATOM   1743 C CE3   . TRP   A 1 231 ? 29.241 -50.538 -19.973 1.00 92.87  ?  231 TRP   A CE3   1 
ATOM   1744 C CZ2   . TRP   A 1 231 ? 26.419 -50.642 -19.798 1.00 92.35  ?  231 TRP   A CZ2   1 
ATOM   1745 C CZ3   . TRP   A 1 231 ? 28.442 -50.001 -20.957 1.00 90.18  ?  231 TRP   A CZ3   1 
ATOM   1746 C CH2   . TRP   A 1 231 ? 27.046 -50.056 -20.864 1.00 90.54  ?  231 TRP   A CH2   1 
ATOM   1747 N N     . TRP   A 1 232 ? 30.405 -48.666 -17.485 1.00 89.73  ?  232 TRP   A N     1 
ATOM   1748 C CA    . TRP   A 1 232 ? 30.555 -47.414 -18.223 1.00 88.92  ?  232 TRP   A CA    1 
ATOM   1749 C C     . TRP   A 1 232 ? 31.655 -46.552 -17.606 1.00 92.09  ?  232 TRP   A C     1 
ATOM   1750 O O     . TRP   A 1 232 ? 32.578 -46.111 -18.301 1.00 93.35  ?  232 TRP   A O     1 
ATOM   1751 C CB    . TRP   A 1 232 ? 29.221 -46.665 -18.258 1.00 82.27  ?  232 TRP   A CB    1 
ATOM   1752 C CG    . TRP   A 1 232 ? 29.296 -45.299 -18.884 1.00 81.93  ?  232 TRP   A CG    1 
ATOM   1753 C CD1   . TRP   A 1 232 ? 29.425 -44.110 -18.235 1.00 83.51  ?  232 TRP   A CD1   1 
ATOM   1754 C CD2   . TRP   A 1 232 ? 29.230 -44.983 -20.278 1.00 81.63  ?  232 TRP   A CD2   1 
ATOM   1755 N NE1   . TRP   A 1 232 ? 29.450 -43.072 -19.133 1.00 81.17  ?  232 TRP   A NE1   1 
ATOM   1756 C CE2   . TRP   A 1 232 ? 29.331 -43.581 -20.395 1.00 79.89  ?  232 TRP   A CE2   1 
ATOM   1757 C CE3   . TRP   A 1 232 ? 29.099 -45.750 -21.439 1.00 88.84  ?  232 TRP   A CE3   1 
ATOM   1758 C CZ2   . TRP   A 1 232 ? 29.309 -42.928 -21.623 1.00 84.02  ?  232 TRP   A CZ2   1 
ATOM   1759 C CZ3   . TRP   A 1 232 ? 29.072 -45.100 -22.664 1.00 90.98  ?  232 TRP   A CZ3   1 
ATOM   1760 C CH2   . TRP   A 1 232 ? 29.176 -43.699 -22.745 1.00 89.58  ?  232 TRP   A CH2   1 
ATOM   1761 N N     . ASN   A 1 233 ? 31.579 -46.316 -16.292 1.00 91.24  ?  233 ASN   A N     1 
ATOM   1762 C CA    . ASN   A 1 233 ? 32.630 -45.623 -15.553 1.00 92.61  ?  233 ASN   A CA    1 
ATOM   1763 C C     . ASN   A 1 233 ? 33.958 -46.368 -15.586 1.00 95.33  ?  233 ASN   A C     1 
ATOM   1764 O O     . ASN   A 1 233 ? 34.986 -45.790 -15.206 1.00 93.31  ?  233 ASN   A O     1 
ATOM   1765 C CB    . ASN   A 1 233 ? 32.206 -45.422 -14.091 1.00 97.16  ?  233 ASN   A CB    1 
ATOM   1766 C CG    . ASN   A 1 233 ? 30.771 -44.929 -13.951 1.00 94.83  ?  233 ASN   A CG    1 
ATOM   1767 O OD1   . ASN   A 1 233 ? 30.331 -44.048 -14.695 1.00 91.80  ?  233 ASN   A OD1   1 
ATOM   1768 N ND2   . ASN   A 1 233 ? 30.038 -45.488 -12.985 1.00 90.10  ?  233 ASN   A ND2   1 
ATOM   1769 N N     . GLU   A 1 234 ? 33.952 -47.639 -16.004 1.00 96.53  ?  234 GLU   A N     1 
ATOM   1770 C CA    . GLU   A 1 234 ? 35.174 -48.420 -16.166 1.00 95.01  ?  234 GLU   A CA    1 
ATOM   1771 C C     . GLU   A 1 234 ? 35.928 -48.042 -17.434 1.00 96.55  ?  234 GLU   A C     1 
ATOM   1772 O O     . GLU   A 1 234 ? 37.165 -48.031 -17.440 1.00 99.01  ?  234 GLU   A O     1 
ATOM   1773 C CB    . GLU   A 1 234 ? 34.843 -49.909 -16.204 1.00 90.98  ?  234 GLU   A CB    1 
ATOM   1774 C CG    . GLU   A 1 234 ? 35.144 -50.662 -14.944 1.00 96.79  ?  234 GLU   A CG    1 
ATOM   1775 C CD    . GLU   A 1 234 ? 34.881 -52.144 -15.101 1.00 100.14 ?  234 GLU   A CD    1 
ATOM   1776 O OE1   . GLU   A 1 234 ? 34.402 -52.547 -16.182 1.00 103.33 ?  234 GLU   A OE1   1 
ATOM   1777 O OE2   . GLU   A 1 234 ? 35.143 -52.907 -14.146 1.00 101.73 ?  234 GLU   A OE2   1 
ATOM   1778 N N     . MET   A 1 235 ? 35.183 -47.704 -18.481 1.00 94.69  ?  235 MET   A N     1 
ATOM   1779 C CA    . MET   A 1 235 ? 35.808 -47.403 -19.790 1.00 94.41  ?  235 MET   A CA    1 
ATOM   1780 C C     . MET   A 1 235 ? 36.456 -46.021 -19.780 1.00 92.57  ?  235 MET   A C     1 
ATOM   1781 O O     . MET   A 1 235 ? 36.125 -45.199 -18.910 1.00 92.48  ?  235 MET   A O     1 
ATOM   1782 C CB    . MET   A 1 235 ? 34.759 -47.456 -20.902 1.00 92.49  ?  235 MET   A CB    1 
ATOM   1783 C CG    . MET   A 1 235 ? 34.319 -48.863 -21.245 1.00 91.07  ?  235 MET   A CG    1 
ATOM   1784 S SD    . MET   A 1 235 ? 32.694 -48.935 -22.020 1.00 85.31  ?  235 MET   A SD    1 
ATOM   1785 C CE    . MET   A 1 235 ? 32.351 -50.692 -21.870 1.00 83.89  ?  235 MET   A CE    1 
ATOM   1786 N N     . SER   A 1 236 ? 37.352 -45.798 -20.734 1.00 90.62  ?  236 SER   A N     1 
ATOM   1787 C CA    . SER   A 1 236 ? 38.043 -44.495 -20.835 1.00 95.01  ?  236 SER   A CA    1 
ATOM   1788 C C     . SER   A 1 236 ? 37.159 -43.508 -21.598 1.00 94.83  ?  236 SER   A C     1 
ATOM   1789 O O     . SER   A 1 236 ? 36.112 -43.929 -22.116 1.00 93.61  ?  236 SER   A O     1 
ATOM   1790 C CB    . SER   A 1 236 ? 39.358 -44.660 -21.513 1.00 93.99  ?  236 SER   A CB    1 
ATOM   1791 O OG    . SER   A 1 236 ? 39.594 -46.023 -21.833 1.00 93.33  ?  236 SER   A OG    1 
ATOM   1792 N N     . PHE   A 1 237 ? 37.601 -42.259 -21.704 1.00 93.78  ?  237 PHE   A N     1 
ATOM   1793 C CA    . PHE   A 1 237 ? 36.772 -41.214 -22.350 1.00 91.69  ?  237 PHE   A CA    1 
ATOM   1794 C C     . PHE   A 1 237 ? 36.779 -41.401 -23.861 1.00 95.45  ?  237 PHE   A C     1 
ATOM   1795 O O     . PHE   A 1 237 ? 35.981 -40.734 -24.535 1.00 94.68  ?  237 PHE   A O     1 
ATOM   1796 C CB    . PHE   A 1 237 ? 37.354 -39.899 -21.840 1.00 94.50  ?  237 PHE   A CB    1 
ATOM   1797 C CG    . PHE   A 1 237 ? 37.907 -39.977 -20.423 1.00 101.95 ?  237 PHE   A CG    1 
ATOM   1798 C CD1   . PHE   A 1 237 ? 37.069 -40.219 -19.342 1.00 102.77 ?  237 PHE   A CD1   1 
ATOM   1799 C CD2   . PHE   A 1 237 ? 39.264 -39.807 -20.177 1.00 104.01 ?  237 PHE   A CD2   1 
ATOM   1800 C CE1   . PHE   A 1 237 ? 37.575 -40.292 -18.055 1.00 101.65 ?  237 PHE   A CE1   1 
ATOM   1801 C CE2   . PHE   A 1 237 ? 39.765 -39.880 -18.887 1.00 98.06  ?  237 PHE   A CE2   1 
ATOM   1802 C CZ    . PHE   A 1 237 ? 38.920 -40.121 -17.831 1.00 103.09 ?  237 PHE   A CZ    1 
ATOM   1803 N N     . ASP   A 1 238 ? 37.648 -42.270 -24.378 1.00 95.83  ?  238 ASP   A N     1 
ATOM   1804 C CA    . ASP   A 1 238 ? 37.657 -42.577 -25.833 1.00 91.09  ?  238 ASP   A CA    1 
ATOM   1805 C C     . ASP   A 1 238 ? 37.034 -43.957 -26.017 1.00 89.69  ?  238 ASP   A C     1 
ATOM   1806 O O     . ASP   A 1 238 ? 36.423 -44.196 -27.067 1.00 93.12  ?  238 ASP   A O     1 
ATOM   1807 C CB    . ASP   A 1 238 ? 39.046 -42.464 -26.434 1.00 89.93  ?  238 ASP   A CB    1 
ATOM   1808 C CG    . ASP   A 1 238 ? 39.139 -42.731 -27.929 1.00 102.33 ?  238 ASP   A CG    1 
ATOM   1809 O OD1   . ASP   A 1 238 ? 38.285 -42.205 -28.672 1.00 99.91  ?  238 ASP   A OD1   1 
ATOM   1810 O OD2   . ASP   A 1 238 ? 40.064 -43.464 -28.335 1.00 100.42 ?  238 ASP   A OD2   1 
ATOM   1811 N N     . GLU   A 1 239 ? 37.171 -44.825 -25.023 1.00 90.21  ?  239 GLU   A N     1 
ATOM   1812 C CA    . GLU   A 1 239 ? 36.499 -46.117 -25.133 1.00 93.51  ?  239 GLU   A CA    1 
ATOM   1813 C C     . GLU   A 1 239 ? 34.989 -45.947 -25.208 1.00 91.90  ?  239 GLU   A C     1 
ATOM   1814 O O     . GLU   A 1 239 ? 34.338 -46.460 -26.125 1.00 92.17  ?  239 GLU   A O     1 
ATOM   1815 C CB    . GLU   A 1 239 ? 36.883 -47.015 -23.954 1.00 97.27  ?  239 GLU   A CB    1 
ATOM   1816 C CG    . GLU   A 1 239 ? 38.203 -47.802 -24.105 1.00 97.13  ?  239 GLU   A CG    1 
ATOM   1817 C CD    . GLU   A 1 239 ? 38.189 -49.083 -23.286 1.00 98.44  ?  239 GLU   A CD    1 
ATOM   1818 O OE1   . GLU   A 1 239 ? 38.875 -50.070 -23.644 1.00 98.07  ?  239 GLU   A OE1   1 
ATOM   1819 O OE2   . GLU   A 1 239 ? 37.475 -49.084 -22.268 1.00 99.83  ?  239 GLU   A OE2   1 
ATOM   1820 N N     . ARG   A 1 240 ? 34.430 -45.173 -24.285 1.00 90.63  ?  240 ARG   A N     1 
ATOM   1821 C CA    . ARG   A 1 240 ? 32.952 -45.067 -24.230 1.00 89.03  ?  240 ARG   A CA    1 
ATOM   1822 C C     . ARG   A 1 240 ? 32.441 -44.171 -25.364 1.00 88.89  ?  240 ARG   A C     1 
ATOM   1823 O O     . ARG   A 1 240 ? 31.297 -44.374 -25.800 1.00 87.38  ?  240 ARG   A O     1 
ATOM   1824 C CB    . ARG   A 1 240 ? 32.516 -44.600 -22.838 1.00 90.18  ?  240 ARG   A CB    1 
ATOM   1825 C CG    . ARG   A 1 240 ? 33.071 -43.329 -22.218 1.00 90.84  ?  240 ARG   A CG    1 
ATOM   1826 C CD    . ARG   A 1 240 ? 33.174 -43.615 -20.732 1.00 91.91  ?  240 ARG   A CD    1 
ATOM   1827 N NE    . ARG   A 1 240 ? 33.066 -42.435 -19.871 1.00 94.84  ?  240 ARG   A NE    1 
ATOM   1828 C CZ    . ARG   A 1 240 ? 33.541 -42.402 -18.636 1.00 90.87  ?  240 ARG   A CZ    1 
ATOM   1829 N NH1   . ARG   A 1 240 ? 33.581 -43.507 -17.919 1.00 89.47  ?  240 ARG   A NH1   1 
ATOM   1830 N NH2   . ARG   A 1 240 ? 33.985 -41.270 -18.126 1.00 91.97  ?  240 ARG   A NH2   1 
ATOM   1831 N N     . ARG   A 1 241 ? 33.270 -43.245 -25.840 1.00 92.18  ?  241 ARG   A N     1 
ATOM   1832 C CA    . ARG   A 1 241 ? 32.861 -42.376 -26.970 1.00 90.31  ?  241 ARG   A CA    1 
ATOM   1833 C C     . ARG   A 1 241 ? 32.554 -43.259 -28.179 1.00 87.16  ?  241 ARG   A C     1 
ATOM   1834 O O     . ARG   A 1 241 ? 31.566 -42.991 -28.874 1.00 87.88  ?  241 ARG   A O     1 
ATOM   1835 C CB    . ARG   A 1 241 ? 33.953 -41.360 -27.302 1.00 93.15  ?  241 ARG   A CB    1 
ATOM   1836 C CG    . ARG   A 1 241 ? 33.522 -40.210 -28.200 1.00 91.49  ?  241 ARG   A CG    1 
ATOM   1837 C CD    . ARG   A 1 241 ? 34.628 -39.777 -29.143 1.00 89.86  ?  241 ARG   A CD    1 
ATOM   1838 N NE    . ARG   A 1 241 ? 35.182 -40.913 -29.885 1.00 95.38  ?  241 ARG   A NE    1 
ATOM   1839 C CZ    . ARG   A 1 241 ? 35.207 -40.991 -31.207 1.00 96.38  ?  241 ARG   A CZ    1 
ATOM   1840 N NH1   . ARG   A 1 241 ? 34.732 -39.997 -31.932 1.00 99.00  ?  241 ARG   A NH1   1 
ATOM   1841 N NH2   . ARG   A 1 241 ? 35.701 -42.059 -31.804 1.00 91.54  ?  241 ARG   A NH2   1 
ATOM   1842 N N     . ARG   A 1 242 ? 33.361 -44.287 -28.395 1.00 89.40  ?  242 ARG   A N     1 
ATOM   1843 C CA    . ARG   A 1 242 ? 33.157 -45.185 -29.554 1.00 90.02  ?  242 ARG   A CA    1 
ATOM   1844 C C     . ARG   A 1 242 ? 32.081 -46.218 -29.214 1.00 86.58  ?  242 ARG   A C     1 
ATOM   1845 O O     . ARG   A 1 242 ? 31.218 -46.470 -30.068 1.00 82.60  ?  242 ARG   A O     1 
ATOM   1846 C CB    . ARG   A 1 242 ? 34.493 -45.853 -29.883 1.00 94.83  ?  242 ARG   A CB    1 
ATOM   1847 C CG    . ARG   A 1 242 ? 34.449 -46.750 -31.111 1.00 104.36 ?  242 ARG   A CG    1 
ATOM   1848 C CD    . ARG   A 1 242 ? 35.347 -47.966 -30.962 1.00 112.97 ?  242 ARG   A CD    1 
ATOM   1849 N NE    . ARG   A 1 242 ? 34.980 -49.045 -31.885 1.00 120.61 ?  242 ARG   A NE    1 
ATOM   1850 C CZ    . ARG   A 1 242 ? 35.833 -49.684 -32.675 1.00 125.32 ?  242 ARG   A CZ    1 
ATOM   1851 N NH1   . ARG   A 1 242 ? 37.124 -49.670 -32.399 1.00 126.07 ?  242 ARG   A NH1   1 
ATOM   1852 N NH2   . ARG   A 1 242 ? 35.392 -50.331 -33.738 1.00 116.26 ?  242 ARG   A NH2   1 
ATOM   1853 N N     . TRP   A 1 243 ? 32.156 -46.809 -28.025 1.00 84.09  ?  243 TRP   A N     1 
ATOM   1854 C CA    . TRP   A 1 243 ? 31.106 -47.761 -27.607 1.00 80.12  ?  243 TRP   A CA    1 
ATOM   1855 C C     . TRP   A 1 243 ? 29.777 -47.200 -28.050 1.00 76.72  ?  243 TRP   A C     1 
ATOM   1856 O O     . TRP   A 1 243 ? 28.911 -47.967 -28.494 1.00 71.02  ?  243 TRP   A O     1 
ATOM   1857 C CB    . TRP   A 1 243 ? 31.117 -47.922 -26.085 1.00 85.66  ?  243 TRP   A CB    1 
ATOM   1858 C CG    . TRP   A 1 243 ? 30.094 -48.904 -25.578 1.00 88.02  ?  243 TRP   A CG    1 
ATOM   1859 C CD1   . TRP   A 1 243 ? 30.274 -50.241 -25.388 1.00 88.27  ?  243 TRP   A CD1   1 
ATOM   1860 C CD2   . TRP   A 1 243 ? 28.723 -48.630 -25.216 1.00 84.50  ?  243 TRP   A CD2   1 
ATOM   1861 N NE1   . TRP   A 1 243 ? 29.120 -50.817 -24.931 1.00 88.22  ?  243 TRP   A NE1   1 
ATOM   1862 C CE2   . TRP   A 1 243 ? 28.152 -49.856 -24.818 1.00 83.74  ?  243 TRP   A CE2   1 
ATOM   1863 C CE3   . TRP   A 1 243 ? 27.929 -47.481 -25.189 1.00 79.89  ?  243 TRP   A CE3   1 
ATOM   1864 C CZ2   . TRP   A 1 243 ? 26.829 -49.959 -24.400 1.00 78.46  ?  243 TRP   A CZ2   1 
ATOM   1865 C CZ3   . TRP   A 1 243 ? 26.621 -47.585 -24.778 1.00 75.85  ?  243 TRP   A CZ3   1 
ATOM   1866 C CH2   . TRP   A 1 243 ? 26.080 -48.808 -24.392 1.00 72.98  ?  243 TRP   A CH2   1 
ATOM   1867 N N     . VAL   A 1 244 ? 29.629 -45.883 -27.928 1.00 78.12  ?  244 VAL   A N     1 
ATOM   1868 C CA    . VAL   A 1 244 ? 28.333 -45.296 -28.233 1.00 76.38  ?  244 VAL   A CA    1 
ATOM   1869 C C     . VAL   A 1 244 ? 28.117 -45.227 -29.739 1.00 73.98  ?  244 VAL   A C     1 
ATOM   1870 O O     . VAL   A 1 244 ? 27.073 -45.646 -30.252 1.00 65.54  ?  244 VAL   A O     1 
ATOM   1871 C CB    . VAL   A 1 244 ? 28.241 -43.906 -27.578 1.00 77.23  ?  244 VAL   A CB    1 
ATOM   1872 C CG1   . VAL   A 1 244 ? 27.114 -43.121 -28.166 1.00 76.82  ?  244 VAL   A CG1   1 
ATOM   1873 C CG2   . VAL   A 1 244 ? 28.068 -44.024 -26.066 1.00 81.49  ?  244 VAL   A CG2   1 
ATOM   1874 N N     . GLU   A 1 245 ? 29.116 -44.707 -30.463 1.00 77.63  ?  245 GLU   A N     1 
ATOM   1875 C CA    . GLU   A 1 245 ? 29.059 -44.619 -31.921 1.00 70.73  ?  245 GLU   A CA    1 
ATOM   1876 C C     . GLU   A 1 245 ? 28.666 -45.947 -32.549 1.00 69.18  ?  245 GLU   A C     1 
ATOM   1877 O O     . GLU   A 1 245 ? 27.796 -45.997 -33.426 1.00 65.56  ?  245 GLU   A O     1 
ATOM   1878 C CB    . GLU   A 1 245 ? 30.411 -44.156 -32.465 1.00 74.17  ?  245 GLU   A CB    1 
ATOM   1879 C CG    . GLU   A 1 245 ? 30.814 -42.763 -32.028 1.00 76.20  ?  245 GLU   A CG    1 
ATOM   1880 C CD    . GLU   A 1 245 ? 32.176 -42.353 -32.563 1.00 77.67  ?  245 GLU   A CD    1 
ATOM   1881 O OE1   . GLU   A 1 245 ? 33.058 -43.224 -32.711 1.00 73.27  ?  245 GLU   A OE1   1 
ATOM   1882 O OE2   . GLU   A 1 245 ? 32.366 -41.148 -32.823 1.00 84.79  ?  245 GLU   A OE2   1 
ATOM   1883 N N     . GLN   A 1 246 ? 29.279 -47.038 -32.098 1.00 69.75  ?  246 GLN   A N     1 
ATOM   1884 C CA    . GLN   A 1 246 ? 28.933 -48.334 -32.653 1.00 67.75  ?  246 GLN   A CA    1 
ATOM   1885 C C     . GLN   A 1 246 ? 27.480 -48.679 -32.378 1.00 66.52  ?  246 GLN   A C     1 
ATOM   1886 O O     . GLN   A 1 246 ? 26.771 -49.172 -33.261 1.00 62.48  ?  246 GLN   A O     1 
ATOM   1887 C CB    . GLN   A 1 246 ? 29.857 -49.411 -32.098 1.00 76.63  ?  246 GLN   A CB    1 
ATOM   1888 C CG    . GLN   A 1 246 ? 31.013 -49.701 -33.028 1.00 88.08  ?  246 GLN   A CG    1 
ATOM   1889 C CD    . GLN   A 1 246 ? 30.615 -49.539 -34.496 1.00 88.28  ?  246 GLN   A CD    1 
ATOM   1890 O OE1   . GLN   A 1 246 ? 31.003 -48.566 -35.154 1.00 90.70  ?  246 GLN   A OE1   1 
ATOM   1891 N NE2   . GLN   A 1 246 ? 29.831 -50.489 -35.012 1.00 86.35  ?  246 GLN   A NE2   1 
ATOM   1892 N N     . ALA   A 1 247 ? 27.019 -48.447 -31.148 1.00 66.71  ?  247 ALA   A N     1 
ATOM   1893 C CA    . ALA   A 1 247 ? 25.655 -48.829 -30.794 1.00 64.77  ?  247 ALA   A CA    1 
ATOM   1894 C C     . ALA   A 1 247 ? 24.643 -48.033 -31.601 1.00 63.77  ?  247 ALA   A C     1 
ATOM   1895 O O     . ALA   A 1 247 ? 23.732 -48.605 -32.210 1.00 59.73  ?  247 ALA   A O     1 
ATOM   1896 C CB    . ALA   A 1 247 ? 25.412 -48.637 -29.296 1.00 59.68  ?  247 ALA   A CB    1 
ATOM   1897 N N     . LEU   A 1 248 ? 24.802 -46.706 -31.619 1.00 62.13  ?  248 LEU   A N     1 
ATOM   1898 C CA    . LEU   A 1 248 ? 23.910 -45.833 -32.376 1.00 56.65  ?  248 LEU   A CA    1 
ATOM   1899 C C     . LEU   A 1 248 ? 23.708 -46.349 -33.790 1.00 62.04  ?  248 LEU   A C     1 
ATOM   1900 O O     . LEU   A 1 248 ? 22.576 -46.425 -34.289 1.00 59.31  ?  248 LEU   A O     1 
ATOM   1901 C CB    . LEU   A 1 248 ? 24.490 -44.422 -32.412 1.00 62.01  ?  248 LEU   A CB    1 
ATOM   1902 C CG    . LEU   A 1 248 ? 24.537 -43.657 -31.088 1.00 61.46  ?  248 LEU   A CG    1 
ATOM   1903 C CD1   . LEU   A 1 248 ? 25.345 -42.378 -31.244 1.00 59.00  ?  248 LEU   A CD1   1 
ATOM   1904 C CD2   . LEU   A 1 248 ? 23.116 -43.349 -30.609 1.00 58.84  ?  248 LEU   A CD2   1 
ATOM   1905 N N     . LEU   A 1 249 ? 24.811 -46.717 -34.445 1.00 65.47  ?  249 LEU   A N     1 
ATOM   1906 C CA    . LEU   A 1 249 ? 24.755 -47.209 -35.816 1.00 57.03  ?  249 LEU   A CA    1 
ATOM   1907 C C     . LEU   A 1 249 ? 23.822 -48.402 -35.925 1.00 58.66  ?  249 LEU   A C     1 
ATOM   1908 O O     . LEU   A 1 249 ? 22.978 -48.466 -36.830 1.00 59.20  ?  249 LEU   A O     1 
ATOM   1909 C CB    . LEU   A 1 249 ? 26.162 -47.577 -36.279 1.00 57.23  ?  249 LEU   A CB    1 
ATOM   1910 C CG    . LEU   A 1 249 ? 26.915 -46.438 -36.955 1.00 65.59  ?  249 LEU   A CG    1 
ATOM   1911 C CD1   . LEU   A 1 249 ? 26.452 -46.354 -38.392 1.00 69.55  ?  249 LEU   A CD1   1 
ATOM   1912 C CD2   . LEU   A 1 249 ? 26.695 -45.092 -36.259 1.00 64.62  ?  249 LEU   A CD2   1 
ATOM   1913 N N     . VAL   A 1 250 ? 23.935 -49.344 -34.988 1.00 55.85  ?  250 VAL   A N     1 
ATOM   1914 C CA    . VAL   A 1 250 ? 23.068 -50.511 -35.020 1.00 57.52  ?  250 VAL   A CA    1 
ATOM   1915 C C     . VAL   A 1 250 ? 21.616 -50.123 -34.782 1.00 57.86  ?  250 VAL   A C     1 
ATOM   1916 O O     . VAL   A 1 250 ? 20.710 -50.714 -35.378 1.00 57.88  ?  250 VAL   A O     1 
ATOM   1917 C CB    . VAL   A 1 250 ? 23.546 -51.547 -33.993 1.00 56.87  ?  250 VAL   A CB    1 
ATOM   1918 C CG1   . VAL   A 1 250 ? 22.782 -52.848 -34.171 1.00 58.90  ?  250 VAL   A CG1   1 
ATOM   1919 C CG2   . VAL   A 1 250 ? 25.047 -51.750 -34.107 1.00 49.75  ?  250 VAL   A CG2   1 
ATOM   1920 N N     . ALA   A 1 251 ? 21.363 -49.120 -33.931 1.00 52.79  ?  251 ALA   A N     1 
ATOM   1921 C CA    . ALA   A 1 251 ? 19.993 -48.808 -33.529 1.00 48.77  ?  251 ALA   A CA    1 
ATOM   1922 C C     . ALA   A 1 251 ? 19.247 -48.003 -34.584 1.00 55.02  ?  251 ALA   A C     1 
ATOM   1923 O O     . ALA   A 1 251 ? 18.087 -48.305 -34.904 1.00 49.54  ?  251 ALA   A O     1 
ATOM   1924 C CB    . ALA   A 1 251 ? 19.998 -48.028 -32.213 1.00 49.62  ?  251 ALA   A CB    1 
ATOM   1925 N N     . ARG   A 1 252 ? 19.896 -46.953 -35.094 1.00 54.43  ?  252 ARG   A N     1 
ATOM   1926 C CA    . ARG   A 1 252 ? 19.236 -46.009 -36.027 1.00 54.05  ?  252 ARG   A CA    1 
ATOM   1927 C C     . ARG   A 1 252 ? 19.960 -45.949 -37.378 1.00 54.72  ?  252 ARG   A C     1 
ATOM   1928 O O     . ARG   A 1 252 ? 19.293 -45.684 -38.381 1.00 52.55  ?  252 ARG   A O     1 
ATOM   1929 C CB    . ARG   A 1 252 ? 19.262 -44.654 -35.314 1.00 44.46  ?  252 ARG   A CB    1 
ATOM   1930 C CG    . ARG   A 1 252 ? 20.183 -43.572 -35.858 1.00 55.52  ?  252 ARG   A CG    1 
ATOM   1931 C CD    . ARG   A 1 252 ? 21.289 -43.229 -34.879 1.00 54.88  ?  252 ARG   A CD    1 
ATOM   1932 N NE    . ARG   A 1 252 ? 21.495 -41.785 -34.737 1.00 57.82  ?  252 ARG   A NE    1 
ATOM   1933 C CZ    . ARG   A 1 252 ? 22.673 -41.218 -34.548 1.00 55.43  ?  252 ARG   A CZ    1 
ATOM   1934 N NH1   . ARG   A 1 252 ? 22.807 -40.245 -33.671 1.00 52.59  ?  252 ARG   A NH1   1 
ATOM   1935 N NH2   . ARG   A 1 252 ? 23.715 -41.627 -35.240 1.00 64.25  ?  252 ARG   A NH2   1 
ATOM   1936 N N     . GLY   A 1 253 ? 21.269 -46.176 -37.398 1.00 55.76  ?  253 GLY   A N     1 
ATOM   1937 C CA    . GLY   A 1 253 ? 22.046 -46.054 -38.639 1.00 54.36  ?  253 GLY   A CA    1 
ATOM   1938 C C     . GLY   A 1 253 ? 22.726 -44.710 -38.713 1.00 62.01  ?  253 GLY   A C     1 
ATOM   1939 O O     . GLY   A 1 253 ? 23.130 -44.202 -37.657 1.00 63.25  ?  253 GLY   A O     1 
ATOM   1940 N N     . ARG   A 1 254 ? 22.838 -44.150 -39.916 1.00 58.49  ?  254 ARG   A N     1 
ATOM   1941 C CA    . ARG   A 1 254 ? 23.503 -42.840 -40.105 1.00 61.88  ?  254 ARG   A CA    1 
ATOM   1942 C C     . ARG   A 1 254 ? 22.438 -41.755 -40.276 1.00 63.91  ?  254 ARG   A C     1 
ATOM   1943 O O     . ARG   A 1 254 ? 21.363 -42.062 -40.806 1.00 62.66  ?  254 ARG   A O     1 
ATOM   1944 C CB    . ARG   A 1 254 ? 24.469 -42.914 -41.285 1.00 67.91  ?  254 ARG   A CB    1 
ATOM   1945 C CG    . ARG   A 1 254 ? 25.276 -44.202 -41.320 1.00 75.12  ?  254 ARG   A CG    1 
ATOM   1946 C CD    . ARG   A 1 254 ? 26.515 -44.071 -42.185 1.00 84.08  ?  254 ARG   A CD    1 
ATOM   1947 N NE    . ARG   A 1 254 ? 27.555 -43.253 -41.554 1.00 85.66  ?  254 ARG   A NE    1 
ATOM   1948 C CZ    . ARG   A 1 254 ? 28.851 -43.393 -41.787 1.00 85.02  ?  254 ARG   A CZ    1 
ATOM   1949 N NH1   . ARG   A 1 254 ? 29.330 -44.561 -42.175 1.00 81.58  ?  254 ARG   A NH1   1 
ATOM   1950 N NH2   . ARG   A 1 254 ? 29.664 -42.365 -41.636 1.00 87.14  ?  254 ARG   A NH2   1 
ATOM   1951 N N     . LEU   A 1 255 ? 22.747 -40.531 -39.859 1.00 64.82  ?  255 LEU   A N     1 
ATOM   1952 C CA    . LEU   A 1 255 ? 21.729 -39.452 -39.864 1.00 64.03  ?  255 LEU   A CA    1 
ATOM   1953 C C     . LEU   A 1 255 ? 21.489 -38.902 -41.279 1.00 60.75  ?  255 LEU   A C     1 
ATOM   1954 O O     . LEU   A 1 255 ? 20.332 -38.585 -41.582 1.00 58.12  ?  255 LEU   A O     1 
ATOM   1955 C CB    . LEU   A 1 255 ? 22.205 -38.378 -38.890 1.00 62.39  ?  255 LEU   A CB    1 
ATOM   1956 C CG    . LEU   A 1 255 ? 22.102 -38.715 -37.402 1.00 59.70  ?  255 LEU   A CG    1 
ATOM   1957 C CD1   . LEU   A 1 255 ? 23.042 -37.829 -36.610 1.00 60.92  ?  255 LEU   A CD1   1 
ATOM   1958 C CD2   . LEU   A 1 255 ? 20.675 -38.526 -36.933 1.00 55.47  ?  255 LEU   A CD2   1 
ATOM   1959 N N     . SER   A 1 256 ? 22.524 -38.792 -42.110 1.00 63.74  ?  256 SER   A N     1 
ATOM   1960 C CA    . SER   A 1 256 ? 22.265 -38.263 -43.452 1.00 62.69  ?  256 SER   A CA    1 
ATOM   1961 C C     . SER   A 1 256 ? 21.286 -39.131 -44.252 1.00 59.81  ?  256 SER   A C     1 
ATOM   1962 O O     . SER   A 1 256 ? 20.686 -38.639 -45.216 1.00 58.46  ?  256 SER   A O     1 
ATOM   1963 C CB    . SER   A 1 256 ? 23.593 -38.099 -44.204 1.00 59.28  ?  256 SER   A CB    1 
ATOM   1964 O OG    . SER   A 1 256 ? 24.395 -39.269 -44.108 1.00 59.12  ?  256 SER   A OG    1 
ATOM   1965 N N     . ASP   A 1 257 ? 21.098 -40.397 -43.859 1.00 58.89  ?  257 ASP   A N     1 
ATOM   1966 C CA    . ASP   A 1 257 ? 20.109 -41.288 -44.457 1.00 59.80  ?  257 ASP   A CA    1 
ATOM   1967 C C     . ASP   A 1 257 ? 18.664 -40.910 -44.131 1.00 60.24  ?  257 ASP   A C     1 
ATOM   1968 O O     . ASP   A 1 257 ? 17.741 -41.537 -44.671 1.00 59.54  ?  257 ASP   A O     1 
ATOM   1969 C CB    . ASP   A 1 257 ? 20.342 -42.726 -43.994 1.00 64.10  ?  257 ASP   A CB    1 
ATOM   1970 C CG    . ASP   A 1 257 ? 21.759 -43.209 -44.241 1.00 77.20  ?  257 ASP   A CG    1 
ATOM   1971 O OD1   . ASP   A 1 257 ? 22.414 -42.712 -45.188 1.00 78.27  ?  257 ASP   A OD1   1 
ATOM   1972 O OD2   . ASP   A 1 257 ? 22.209 -44.104 -43.486 1.00 82.51  ?  257 ASP   A OD2   1 
ATOM   1973 N N     . TYR   A 1 258 ? 18.433 -39.939 -43.250 1.00 54.06  ?  258 TYR   A N     1 
ATOM   1974 C CA    . TYR   A 1 258 ? 17.085 -39.465 -42.970 1.00 51.27  ?  258 TYR   A CA    1 
ATOM   1975 C C     . TYR   A 1 258 ? 16.844 -38.074 -43.532 1.00 50.59  ?  258 TYR   A C     1 
ATOM   1976 O O     . TYR   A 1 258 ? 15.787 -37.491 -43.286 1.00 49.25  ?  258 TYR   A O     1 
ATOM   1977 C CB    . TYR   A 1 258 ? 16.801 -39.468 -41.465 1.00 49.11  ?  258 TYR   A CB    1 
ATOM   1978 C CG    . TYR   A 1 258 ? 16.837 -40.826 -40.816 1.00 47.25  ?  258 TYR   A CG    1 
ATOM   1979 C CD1   . TYR   A 1 258 ? 18.035 -41.372 -40.357 1.00 49.35  ?  258 TYR   A CD1   1 
ATOM   1980 C CD2   . TYR   A 1 258 ? 15.670 -41.571 -40.658 1.00 47.17  ?  258 TYR   A CD2   1 
ATOM   1981 C CE1   . TYR   A 1 258 ? 18.069 -42.620 -39.757 1.00 49.21  ?  258 TYR   A CE1   1 
ATOM   1982 C CE2   . TYR   A 1 258 ? 15.693 -42.818 -40.050 1.00 45.89  ?  258 TYR   A CE2   1 
ATOM   1983 C CZ    . TYR   A 1 258 ? 16.892 -43.334 -39.601 1.00 46.18  ?  258 TYR   A CZ    1 
ATOM   1984 O OH    . TYR   A 1 258 ? 16.903 -44.569 -39.009 1.00 41.37  ?  258 TYR   A OH    1 
ATOM   1985 N N     . GLY   A 1 259 ? 17.792 -37.532 -44.282 1.00 52.74  ?  259 GLY   A N     1 
ATOM   1986 C CA    . GLY   A 1 259 ? 17.648 -36.199 -44.810 1.00 48.62  ?  259 GLY   A CA    1 
ATOM   1987 C C     . GLY   A 1 259 ? 18.193 -35.122 -43.920 1.00 52.65  ?  259 GLY   A C     1 
ATOM   1988 O O     . GLY   A 1 259 ? 17.830 -33.956 -44.100 1.00 53.43  ?  259 GLY   A O     1 
ATOM   1989 N N     . LEU   A 1 260 ? 19.074 -35.470 -42.975 1.00 54.41  ?  260 LEU   A N     1 
ATOM   1990 C CA    . LEU   A 1 260 ? 19.518 -34.588 -41.903 1.00 49.00  ?  260 LEU   A CA    1 
ATOM   1991 C C     . LEU   A 1 260 ? 21.016 -34.312 -41.974 1.00 50.01  ?  260 LEU   A C     1 
ATOM   1992 O O     . LEU   A 1 260 ? 21.800 -35.221 -42.266 1.00 52.64  ?  260 LEU   A O     1 
ATOM   1993 C CB    . LEU   A 1 260 ? 19.192 -35.205 -40.538 1.00 52.43  ?  260 LEU   A CB    1 
ATOM   1994 C CG    . LEU   A 1 260 ? 17.736 -35.208 -40.097 1.00 48.91  ?  260 LEU   A CG    1 
ATOM   1995 C CD1   . LEU   A 1 260 ? 17.501 -36.242 -39.024 1.00 47.86  ?  260 LEU   A CD1   1 
ATOM   1996 C CD2   . LEU   A 1 260 ? 17.369 -33.830 -39.602 1.00 48.63  ?  260 LEU   A CD2   1 
ATOM   1997 N N     . PRO   A 1 261 ? 21.443 -33.084 -41.669 1.00 47.39  ?  261 PRO   A N     1 
ATOM   1998 C CA    . PRO   A 1 261 ? 22.870 -32.748 -41.768 1.00 50.48  ?  261 PRO   A CA    1 
ATOM   1999 C C     . PRO   A 1 261 ? 23.701 -33.495 -40.746 1.00 52.93  ?  261 PRO   A C     1 
ATOM   2000 O O     . PRO   A 1 261 ? 23.314 -33.637 -39.584 1.00 62.23  ?  261 PRO   A O     1 
ATOM   2001 C CB    . PRO   A 1 261 ? 22.902 -31.237 -41.505 1.00 50.57  ?  261 PRO   A CB    1 
ATOM   2002 C CG    . PRO   A 1 261 ? 21.674 -30.967 -40.729 1.00 53.69  ?  261 PRO   A CG    1 
ATOM   2003 C CD    . PRO   A 1 261 ? 20.638 -31.942 -41.212 1.00 48.98  ?  261 PRO   A CD    1 
ATOM   2004 N N     . GLU   A 1 262 ? 24.853 -33.960 -41.174 1.00 52.27  ?  262 GLU   A N     1 
ATOM   2005 C CA    . GLU   A 1 262 ? 25.774 -34.552 -40.227 1.00 60.52  ?  262 GLU   A CA    1 
ATOM   2006 C C     . GLU   A 1 262 ? 26.307 -33.470 -39.292 1.00 67.39  ?  262 GLU   A C     1 
ATOM   2007 O O     . GLU   A 1 262 ? 26.671 -32.375 -39.752 1.00 60.34  ?  262 GLU   A O     1 
ATOM   2008 C CB    . GLU   A 1 262 ? 26.910 -35.257 -40.935 1.00 54.83  ?  262 GLU   A CB    1 
ATOM   2009 C CG    . GLU   A 1 262 ? 26.505 -36.614 -41.447 1.00 59.06  ?  262 GLU   A CG    1 
ATOM   2010 C CD    . GLU   A 1 262 ? 26.434 -37.666 -40.365 1.00 66.97  ?  262 GLU   A CD    1 
ATOM   2011 O OE1   . GLU   A 1 262 ? 27.164 -37.538 -39.345 1.00 72.38  ?  262 GLU   A OE1   1 
ATOM   2012 O OE2   . GLU   A 1 262 ? 25.634 -38.620 -40.541 1.00 65.37  ?  262 GLU   A OE2   1 
ATOM   2013 N N     . PRO   A 1 263 ? 26.317 -33.713 -37.982 1.00 66.19  ?  263 PRO   A N     1 
ATOM   2014 C CA    . PRO   A 1 263 ? 27.028 -32.815 -37.070 1.00 68.97  ?  263 PRO   A CA    1 
ATOM   2015 C C     . PRO   A 1 263 ? 28.512 -32.794 -37.407 1.00 72.36  ?  263 PRO   A C     1 
ATOM   2016 O O     . PRO   A 1 263 ? 29.053 -33.728 -38.005 1.00 69.91  ?  263 PRO   A O     1 
ATOM   2017 C CB    . PRO   A 1 263 ? 26.770 -33.431 -35.690 1.00 66.41  ?  263 PRO   A CB    1 
ATOM   2018 C CG    . PRO   A 1 263 ? 25.626 -34.386 -35.888 1.00 62.91  ?  263 PRO   A CG    1 
ATOM   2019 C CD    . PRO   A 1 263 ? 25.704 -34.859 -37.285 1.00 62.66  ?  263 PRO   A CD    1 
ATOM   2020 N N     . ASP   A 1 264 ? 29.123 -31.640 -37.118 1.00 72.98  ?  264 ASP   A N     1 
ATOM   2021 C CA    . ASP   A 1 264 ? 30.553 -31.419 -37.453 1.00 77.78  ?  264 ASP   A CA    1 
ATOM   2022 C C     . ASP   A 1 264 ? 31.407 -31.667 -36.219 1.00 81.82  ?  264 ASP   A C     1 
ATOM   2023 O O     . ASP   A 1 264 ? 32.432 -30.985 -36.058 1.00 83.66  ?  264 ASP   A O     1 
ATOM   2024 C CB    . ASP   A 1 264 ? 30.771 -30.009 -37.972 1.00 81.92  ?  264 ASP   A CB    1 
ATOM   2025 C CG    . ASP   A 1 264 ? 30.017 -28.900 -37.251 1.00 87.59  ?  264 ASP   A CG    1 
ATOM   2026 O OD1   . ASP   A 1 264 ? 29.865 -28.993 -36.018 1.00 89.64  ?  264 ASP   A OD1   1 
ATOM   2027 O OD2   . ASP   A 1 264 ? 29.599 -27.943 -37.931 1.00 83.82  ?  264 ASP   A OD2   1 
ATOM   2028 N N     . HIS   A 1 265 ? 30.989 -32.616 -35.393 1.00 87.78  ?  265 HIS   A N     1 
ATOM   2029 C CA    . HIS   A 1 265 ? 31.714 -32.914 -34.137 1.00 84.62  ?  265 HIS   A CA    1 
ATOM   2030 C C     . HIS   A 1 265 ? 31.248 -34.276 -33.636 1.00 79.94  ?  265 HIS   A C     1 
ATOM   2031 O O     . HIS   A 1 265 ? 30.079 -34.627 -33.805 1.00 73.28  ?  265 HIS   A O     1 
ATOM   2032 C CB    . HIS   A 1 265 ? 31.433 -31.820 -33.113 1.00 80.52  ?  265 HIS   A CB    1 
ATOM   2033 C CG    . HIS   A 1 265 ? 29.992 -31.469 -33.028 1.00 81.49  ?  265 HIS   A CG    1 
ATOM   2034 N ND1   . HIS   A 1 265 ? 29.476 -30.332 -33.606 1.00 83.17  ?  265 HIS   A ND1   1 
ATOM   2035 C CD2   . HIS   A 1 265 ? 28.965 -32.094 -32.452 1.00 84.33  ?  265 HIS   A CD2   1 
ATOM   2036 C CE1   . HIS   A 1 265 ? 28.176 -30.281 -33.375 1.00 83.87  ?  265 HIS   A CE1   1 
ATOM   2037 N NE2   . HIS   A 1 265 ? 27.848 -31.342 -32.677 1.00 84.21  ?  265 HIS   A NE2   1 
ATOM   2038 N N     . PRO   A 1 266 ? 32.144 -35.075 -33.034 1.00 82.00  ?  266 PRO   A N     1 
ATOM   2039 C CA    . PRO   A 1 266 ? 31.760 -36.366 -32.494 1.00 83.37  ?  266 PRO   A CA    1 
ATOM   2040 C C     . PRO   A 1 266 ? 30.761 -36.264 -31.365 1.00 81.83  ?  266 PRO   A C     1 
ATOM   2041 O O     . PRO   A 1 266 ? 30.429 -35.165 -30.898 1.00 82.29  ?  266 PRO   A O     1 
ATOM   2042 C CB    . PRO   A 1 266 ? 33.097 -36.889 -31.989 1.00 86.26  ?  266 PRO   A CB    1 
ATOM   2043 C CG    . PRO   A 1 266 ? 34.118 -36.168 -32.824 1.00 92.71  ?  266 PRO   A CG    1 
ATOM   2044 C CD    . PRO   A 1 266 ? 33.547 -34.772 -32.891 1.00 88.65  ?  266 PRO   A CD    1 
ATOM   2045 N N     . VAL   A 1 267 ? 30.306 -37.412 -30.892 1.00 81.25  ?  267 VAL   A N     1 
ATOM   2046 C CA    . VAL   A 1 267 ? 29.382 -37.414 -29.728 1.00 79.69  ?  267 VAL   A CA    1 
ATOM   2047 C C     . VAL   A 1 267 ? 30.072 -36.727 -28.546 1.00 83.50  ?  267 VAL   A C     1 
ATOM   2048 O O     . VAL   A 1 267 ? 31.318 -36.738 -28.516 1.00 84.29  ?  267 VAL   A O     1 
ATOM   2049 C CB    . VAL   A 1 267 ? 28.983 -38.855 -29.376 1.00 77.01  ?  267 VAL   A CB    1 
ATOM   2050 C CG1   . VAL   A 1 267 ? 27.805 -39.326 -30.214 1.00 76.02  ?  267 VAL   A CG1   1 
ATOM   2051 C CG2   . VAL   A 1 267 ? 30.156 -39.814 -29.511 1.00 76.03  ?  267 VAL   A CG2   1 
ATOM   2052 N N     . PHE   A 1 268 ? 29.294 -36.126 -27.647 1.00 87.52  ?  268 PHE   A N     1 
ATOM   2053 C CA    . PHE   A 1 268 ? 29.825 -35.472 -26.414 1.00 91.25  ?  268 PHE   A CA    1 
ATOM   2054 C C     . PHE   A 1 268 ? 30.392 -34.093 -26.753 1.00 92.46  ?  268 PHE   A C     1 
ATOM   2055 O O     . PHE   A 1 268 ? 30.498 -33.265 -25.832 1.00 94.94  ?  268 PHE   A O     1 
ATOM   2056 C CB    . PHE   A 1 268 ? 30.777 -36.395 -25.645 1.00 88.65  ?  268 PHE   A CB    1 
ATOM   2057 C CG    . PHE   A 1 268 ? 30.249 -37.809 -25.449 1.00 84.35  ?  268 PHE   A CG    1 
ATOM   2058 C CD1   . PHE   A 1 268 ? 28.963 -38.030 -24.974 1.00 79.65  ?  268 PHE   A CD1   1 
ATOM   2059 C CD2   . PHE   A 1 268 ? 31.035 -38.911 -25.754 1.00 81.73  ?  268 PHE   A CD2   1 
ATOM   2060 C CE1   . PHE   A 1 268 ? 28.484 -39.317 -24.805 1.00 82.79  ?  268 PHE   A CE1   1 
ATOM   2061 C CE2   . PHE   A 1 268 ? 30.549 -40.195 -25.582 1.00 84.85  ?  268 PHE   A CE2   1 
ATOM   2062 C CZ    . PHE   A 1 268 ? 29.277 -40.396 -25.109 1.00 83.26  ?  268 PHE   A CZ    1 
ATOM   2063 N N     . SER   A 1 269 ? 30.706 -33.841 -28.023 1.00 95.45  ?  269 SER   A N     1 
ATOM   2064 C CA    . SER   A 1 269 ? 31.150 -32.482 -28.426 1.00 93.08  ?  269 SER   A CA    1 
ATOM   2065 C C     . SER   A 1 269 ? 29.931 -31.559 -28.577 1.00 95.28  ?  269 SER   A C     1 
ATOM   2066 O O     . SER   A 1 269 ? 29.671 -31.108 -29.700 1.00 87.85  ?  269 SER   A O     1 
ATOM   2067 C CB    . SER   A 1 269 ? 31.972 -32.546 -29.663 1.00 85.66  ?  269 SER   A CB    1 
ATOM   2068 O OG    . SER   A 1 269 ? 32.564 -33.829 -29.800 1.00 85.49  ?  269 SER   A OG    1 
ATOM   2069 N N     . SER   A 1 270 ? 29.191 -31.331 -27.493 1.00 103.20 ?  270 SER   A N     1 
ATOM   2070 C CA    . SER   A 1 270 ? 28.028 -30.393 -27.469 1.00 101.20 ?  270 SER   A CA    1 
ATOM   2071 C C     . SER   A 1 270 ? 26.919 -30.732 -28.477 1.00 96.18  ?  270 SER   A C     1 
ATOM   2072 O O     . SER   A 1 270 ? 26.565 -29.821 -29.251 1.00 98.07  ?  270 SER   A O     1 
ATOM   2073 C CB    . SER   A 1 270 ? 28.483 -28.966 -27.628 1.00 99.99  ?  270 SER   A CB    1 
ATOM   2074 O OG    . SER   A 1 270 ? 28.294 -28.241 -26.421 1.00 101.50 ?  270 SER   A OG    1 
ATOM   2075 N N     . ALA   A 1 271 ? 26.336 -31.938 -28.418 1.00 91.87  ?  271 ALA   A N     1 
ATOM   2076 C CA    . ALA   A 1 271 ? 25.186 -32.235 -29.306 1.00 83.08  ?  271 ALA   A CA    1 
ATOM   2077 C C     . ALA   A 1 271 ? 24.484 -33.540 -28.971 1.00 78.30  ?  271 ALA   A C     1 
ATOM   2078 O O     . ALA   A 1 271 ? 25.039 -34.582 -29.322 1.00 81.28  ?  271 ALA   A O     1 
ATOM   2079 C CB    . ALA   A 1 271 ? 25.633 -32.310 -30.731 1.00 77.80  ?  271 ALA   A CB    1 
ATOM   2080 N N     . THR   A 1 272 ? 23.348 -33.488 -28.285 1.00 76.60  ?  272 THR   A N     1 
ATOM   2081 C CA    . THR   A 1 272 ? 22.519 -34.678 -28.123 1.00 68.82  ?  272 THR   A CA    1 
ATOM   2082 C C     . THR   A 1 272 ? 21.084 -34.280 -27.819 1.00 67.71  ?  272 THR   A C     1 
ATOM   2083 O O     . THR   A 1 272 ? 20.762 -33.884 -26.692 1.00 71.15  ?  272 THR   A O     1 
ATOM   2084 C CB    . THR   A 1 272 ? 23.028 -35.610 -27.015 1.00 73.80  ?  272 THR   A CB    1 
ATOM   2085 O OG1   . THR   A 1 272 ? 24.434 -35.826 -27.162 1.00 74.87  ?  272 THR   A OG1   1 
ATOM   2086 C CG2   . THR   A 1 272 ? 22.323 -36.951 -27.094 1.00 69.88  ?  272 THR   A CG2   1 
ATOM   2087 N N     . THR   A 1 273 ? 20.218 -34.384 -28.819 1.00 61.05  ?  273 THR   A N     1 
ATOM   2088 C CA    . THR   A 1 273 ? 18.781 -34.329 -28.606 1.00 60.37  ?  273 THR   A CA    1 
ATOM   2089 C C     . THR   A 1 273 ? 18.307 -35.768 -28.430 1.00 57.35  ?  273 THR   A C     1 
ATOM   2090 O O     . THR   A 1 273 ? 18.707 -36.650 -29.191 1.00 55.19  ?  273 THR   A O     1 
ATOM   2091 C CB    . THR   A 1 273 ? 18.087 -33.626 -29.787 1.00 54.15  ?  273 THR   A CB    1 
ATOM   2092 O OG1   . THR   A 1 273 ? 18.736 -32.378 -30.041 1.00 49.74  ?  273 THR   A OG1   1 
ATOM   2093 C CG2   . THR   A 1 273 ? 16.620 -33.310 -29.509 1.00 48.62  ?  273 THR   A CG2   1 
ATOM   2094 N N     . LEU   A 1 274 ? 17.524 -36.020 -27.386 1.00 59.41  ?  274 LEU   A N     1 
ATOM   2095 C CA    . LEU   A 1 274 ? 16.977 -37.348 -27.128 1.00 57.40  ?  274 LEU   A CA    1 
ATOM   2096 C C     . LEU   A 1 274 ? 15.578 -37.417 -27.724 1.00 55.77  ?  274 LEU   A C     1 
ATOM   2097 O O     . LEU   A 1 274 ? 14.790 -36.483 -27.555 1.00 60.84  ?  274 LEU   A O     1 
ATOM   2098 C CB    . LEU   A 1 274 ? 16.933 -37.649 -25.626 1.00 54.96  ?  274 LEU   A CB    1 
ATOM   2099 C CG    . LEU   A 1 274 ? 18.284 -37.858 -24.934 1.00 64.90  ?  274 LEU   A CG    1 
ATOM   2100 C CD1   . LEU   A 1 274 ? 18.149 -37.724 -23.421 1.00 59.99  ?  274 LEU   A CD1   1 
ATOM   2101 C CD2   . LEU   A 1 274 ? 18.897 -39.205 -25.318 1.00 54.10  ?  274 LEU   A CD2   1 
ATOM   2102 N N     . SER   A 1 275 ? 15.277 -38.504 -28.440 1.00 51.29  ?  275 SER   A N     1 
ATOM   2103 C CA    . SER   A 1 275 ? 13.928 -38.703 -28.976 1.00 48.84  ?  275 SER   A CA    1 
ATOM   2104 C C     . SER   A 1 275 ? 13.730 -40.139 -29.430 1.00 45.58  ?  275 SER   A C     1 
ATOM   2105 O O     . SER   A 1 275 ? 14.611 -40.703 -30.071 1.00 50.96  ?  275 SER   A O     1 
ATOM   2106 C CB    . SER   A 1 275 ? 13.639 -37.759 -30.151 1.00 47.15  ?  275 SER   A CB    1 
ATOM   2107 O OG    . SER   A 1 275 ? 12.444 -38.125 -30.844 1.00 47.30  ?  275 SER   A OG    1 
ATOM   2108 N N     . ASP   A 1 276 ? 12.593 -40.744 -29.102 1.00 48.40  ?  276 ASP   A N     1 
ATOM   2109 C CA    . ASP   A 1 276 ? 12.241 -42.074 -29.593 1.00 49.42  ?  276 ASP   A CA    1 
ATOM   2110 C C     . ASP   A 1 276 ? 11.422 -42.024 -30.877 1.00 46.97  ?  276 ASP   A C     1 
ATOM   2111 O O     . ASP   A 1 276 ? 10.954 -43.071 -31.340 1.00 46.62  ?  276 ASP   A O     1 
ATOM   2112 C CB    . ASP   A 1 276 ? 11.439 -42.853 -28.534 1.00 46.70  ?  276 ASP   A CB    1 
ATOM   2113 C CG    . ASP   A 1 276 ? 12.310 -43.435 -27.436 1.00 53.74  ?  276 ASP   A CG    1 
ATOM   2114 O OD1   . ASP   A 1 276 ? 13.547 -43.536 -27.647 1.00 51.73  ?  276 ASP   A OD1   1 
ATOM   2115 O OD2   . ASP   A 1 276 ? 11.740 -43.803 -26.370 1.00 57.27  ?  276 ASP   A OD2   1 
ATOM   2116 N N     . GLU   A 1 277 ? 11.229 -40.838 -31.453 1.00 43.38  ?  277 GLU   A N     1 
ATOM   2117 C CA    . GLU   A 1 277 ? 10.136 -40.661 -32.392 1.00 44.06  ?  277 GLU   A CA    1 
ATOM   2118 C C     . GLU   A 1 277 ? 10.510 -39.971 -33.707 1.00 49.21  ?  277 GLU   A C     1 
ATOM   2119 O O     . GLU   A 1 277 ? 9.898  -40.267 -34.743 1.00 47.88  ?  277 GLU   A O     1 
ATOM   2120 C CB    . GLU   A 1 277 ? 9.019  -39.882 -31.702 1.00 38.98  ?  277 GLU   A CB    1 
ATOM   2121 C CG    . GLU   A 1 277 ? 7.895  -40.767 -31.216 1.00 48.56  ?  277 GLU   A CG    1 
ATOM   2122 C CD    . GLU   A 1 277 ? 6.699  -39.987 -30.683 1.00 53.64  ?  277 GLU   A CD    1 
ATOM   2123 O OE1   . GLU   A 1 277 ? 6.270  -40.271 -29.546 1.00 54.51  ?  277 GLU   A OE1   1 
ATOM   2124 O OE2   . GLU   A 1 277 ? 6.179  -39.107 -31.403 1.00 53.06  ?  277 GLU   A OE2   1 
ATOM   2125 N N     . ILE   A 1 278 ? 11.504 -39.072 -33.690 1.00 40.94  ?  278 ILE   A N     1 
ATOM   2126 C CA    . ILE   A 1 278 ? 11.591 -38.081 -34.757 1.00 40.17  ?  278 ILE   A CA    1 
ATOM   2127 C C     . ILE   A 1 278 ? 12.003 -38.729 -36.067 1.00 43.23  ?  278 ILE   A C     1 
ATOM   2128 O O     . ILE   A 1 278 ? 11.428 -38.423 -37.114 1.00 46.00  ?  278 ILE   A O     1 
ATOM   2129 C CB    . ILE   A 1 278 ? 12.519 -36.907 -34.375 1.00 42.66  ?  278 ILE   A CB    1 
ATOM   2130 C CG1   . ILE   A 1 278 ? 12.312 -35.730 -35.344 1.00 36.19  ?  278 ILE   A CG1   1 
ATOM   2131 C CG2   . ILE   A 1 278 ? 13.994 -37.311 -34.325 1.00 38.72  ?  278 ILE   A CG2   1 
ATOM   2132 C CD1   . ILE   A 1 278 ? 10.879 -35.407 -35.657 1.00 32.47  ?  278 ILE   A CD1   1 
ATOM   2133 N N     . LEU   A 1 279 ? 12.969 -39.655 -36.034 1.00 45.65  ?  279 LEU   A N     1 
ATOM   2134 C CA    . LEU   A 1 279 ? 13.360 -40.344 -37.259 1.00 42.68  ?  279 LEU   A CA    1 
ATOM   2135 C C     . LEU   A 1 279 ? 12.185 -41.110 -37.842 1.00 44.83  ?  279 LEU   A C     1 
ATOM   2136 O O     . LEU   A 1 279 ? 11.931 -41.033 -39.051 1.00 45.01  ?  279 LEU   A O     1 
ATOM   2137 C CB    . LEU   A 1 279 ? 14.536 -41.287 -37.004 1.00 43.89  ?  279 LEU   A CB    1 
ATOM   2138 C CG    . LEU   A 1 279 ? 15.836 -40.729 -36.389 1.00 46.51  ?  279 LEU   A CG    1 
ATOM   2139 C CD1   . LEU   A 1 279 ? 16.828 -41.870 -36.079 1.00 42.28  ?  279 LEU   A CD1   1 
ATOM   2140 C CD2   . LEU   A 1 279 ? 16.498 -39.632 -37.232 1.00 35.33  ?  279 LEU   A CD2   1 
ATOM   2141 N N     . SER   A 1 280 ? 11.426 -41.821 -37.002 1.00 40.77  ?  280 SER   A N     1 
ATOM   2142 C CA    . SER   A 1 280 ? 10.352 -42.632 -37.559 1.00 41.74  ?  280 SER   A CA    1 
ATOM   2143 C C     . SER   A 1 280 ? 9.254  -41.760 -38.151 1.00 44.17  ?  280 SER   A C     1 
ATOM   2144 O O     . SER   A 1 280 ? 8.603  -42.166 -39.118 1.00 43.85  ?  280 SER   A O     1 
ATOM   2145 C CB    . SER   A 1 280 ? 9.772  -43.584 -36.519 1.00 36.60  ?  280 SER   A CB    1 
ATOM   2146 O OG    . SER   A 1 280 ? 8.460  -43.997 -36.887 1.00 40.92  ?  280 SER   A OG    1 
ATOM   2147 N N     . ARG   A 1 281 ? 9.029  -40.566 -37.602 1.00 42.83  ?  281 ARG   A N     1 
ATOM   2148 C CA    . ARG   A 1 281 ? 8.097  -39.657 -38.261 1.00 44.08  ?  281 ARG   A CA    1 
ATOM   2149 C C     . ARG   A 1 281 ? 8.580  -39.310 -39.665 1.00 45.45  ?  281 ARG   A C     1 
ATOM   2150 O O     . ARG   A 1 281 ? 7.765  -39.131 -40.586 1.00 41.39  ?  281 ARG   A O     1 
ATOM   2151 C CB    . ARG   A 1 281 ? 7.908  -38.374 -37.444 1.00 43.53  ?  281 ARG   A CB    1 
ATOM   2152 C CG    . ARG   A 1 281 ? 7.504  -38.566 -35.999 1.00 43.99  ?  281 ARG   A CG    1 
ATOM   2153 C CD    . ARG   A 1 281 ? 6.543  -39.702 -35.823 1.00 44.70  ?  281 ARG   A CD    1 
ATOM   2154 N NE    . ARG   A 1 281 ? 5.293  -39.488 -36.531 1.00 47.96  ?  281 ARG   A NE    1 
ATOM   2155 C CZ    . ARG   A 1 281 ? 4.554  -40.480 -37.007 1.00 54.59  ?  281 ARG   A CZ    1 
ATOM   2156 N NH1   . ARG   A 1 281 ? 4.963  -41.739 -36.844 1.00 54.78  ?  281 ARG   A NH1   1 
ATOM   2157 N NH2   . ARG   A 1 281 ? 3.418  -40.220 -37.642 1.00 51.04  ?  281 ARG   A NH2   1 
ATOM   2158 N N     . ILE   A 1 282 ? 9.902  -39.217 -39.844 1.00 42.07  ?  282 ILE   A N     1 
ATOM   2159 C CA    . ILE   A 1 282 ? 10.461 -38.892 -41.151 1.00 44.56  ?  282 ILE   A CA    1 
ATOM   2160 C C     . ILE   A 1 282 ? 10.294 -40.064 -42.107 1.00 42.17  ?  282 ILE   A C     1 
ATOM   2161 O O     . ILE   A 1 282 ? 9.796  -39.899 -43.221 1.00 45.50  ?  282 ILE   A O     1 
ATOM   2162 C CB    . ILE   A 1 282 ? 11.931 -38.477 -41.012 1.00 46.28  ?  282 ILE   A CB    1 
ATOM   2163 C CG1   . ILE   A 1 282 ? 12.018 -37.091 -40.398 1.00 47.69  ?  282 ILE   A CG1   1 
ATOM   2164 C CG2   . ILE   A 1 282 ? 12.633 -38.507 -42.347 1.00 43.59  ?  282 ILE   A CG2   1 
ATOM   2165 C CD1   . ILE   A 1 282 ? 13.398 -36.482 -40.498 1.00 51.40  ?  282 ILE   A CD1   1 
ATOM   2166 N N     . ARG   A 1 283 ? 10.674 -41.271 -41.678 1.00 41.11  ?  283 ARG   A N     1 
ATOM   2167 C CA    . ARG   A 1 283 ? 10.465 -42.445 -42.517 1.00 39.04  ?  283 ARG   A CA    1 
ATOM   2168 C C     . ARG   A 1 283 ? 8.991  -42.744 -42.785 1.00 42.39  ?  283 ARG   A C     1 
ATOM   2169 O O     . ARG   A 1 283 ? 8.699  -43.515 -43.708 1.00 51.90  ?  283 ARG   A O     1 
ATOM   2170 C CB    . ARG   A 1 283 ? 11.129 -43.674 -41.912 1.00 38.03  ?  283 ARG   A CB    1 
ATOM   2171 C CG    . ARG   A 1 283 ? 12.635 -43.619 -41.883 1.00 38.13  ?  283 ARG   A CG    1 
ATOM   2172 C CD    . ARG   A 1 283 ? 13.237 -44.372 -43.054 1.00 43.43  ?  283 ARG   A CD    1 
ATOM   2173 N NE    . ARG   A 1 283 ? 14.570 -43.884 -43.379 1.00 40.26  ?  283 ARG   A NE    1 
ATOM   2174 C CZ    . ARG   A 1 283 ? 15.681 -44.564 -43.138 1.00 44.32  ?  283 ARG   A CZ    1 
ATOM   2175 N NH1   . ARG   A 1 283 ? 15.613 -45.766 -42.586 1.00 42.90  ?  283 ARG   A NH1   1 
ATOM   2176 N NH2   . ARG   A 1 283 ? 16.854 -44.039 -43.456 1.00 48.11  ?  283 ARG   A NH2   1 
ATOM   2177 N N     . HIS   A 1 284 ? 8.056  -42.148 -42.053 1.00 37.76  ?  284 HIS   A N     1 
ATOM   2178 C CA    . HIS   A 1 284 ? 6.642  -42.344 -42.342 1.00 39.94  ?  284 HIS   A CA    1 
ATOM   2179 C C     . HIS   A 1 284 ? 6.064  -41.218 -43.195 1.00 45.36  ?  284 HIS   A C     1 
ATOM   2180 O O     . HIS   A 1 284 ? 4.887  -41.280 -43.585 1.00 41.83  ?  284 HIS   A O     1 
ATOM   2181 C CB    . HIS   A 1 284 ? 5.844  -42.503 -41.037 1.00 41.24  ?  284 HIS   A CB    1 
ATOM   2182 C CG    . HIS   A 1 284 ? 5.921  -43.879 -40.464 1.00 40.66  ?  284 HIS   A CG    1 
ATOM   2183 N ND1   . HIS   A 1 284 ? 7.066  -44.377 -39.881 1.00 42.52  ?  284 HIS   A ND1   1 
ATOM   2184 C CD2   . HIS   A 1 284 ? 5.013  -44.882 -40.429 1.00 42.11  ?  284 HIS   A CD2   1 
ATOM   2185 C CE1   . HIS   A 1 284 ? 6.852  -45.623 -39.494 1.00 43.75  ?  284 HIS   A CE1   1 
ATOM   2186 N NE2   . HIS   A 1 284 ? 5.613  -45.951 -39.810 1.00 43.11  ?  284 HIS   A NE2   1 
ATOM   2187 N N     . GLY   A 1 285 ? 6.880  -40.215 -43.527 1.00 41.75  ?  285 GLY   A N     1 
ATOM   2188 C CA    . GLY   A 1 285 ? 6.443  -39.061 -44.272 1.00 38.33  ?  285 GLY   A CA    1 
ATOM   2189 C C     . GLY   A 1 285 ? 5.760  -38.003 -43.440 1.00 50.54  ?  285 GLY   A C     1 
ATOM   2190 O O     . GLY   A 1 285 ? 5.427  -36.940 -43.980 1.00 53.73  ?  285 GLY   A O     1 
ATOM   2191 N N     . ALA   A 1 286 ? 5.569  -38.247 -42.133 1.00 50.65  ?  286 ALA   A N     1 
ATOM   2192 C CA    . ALA   A 1 286 ? 4.789  -37.355 -41.283 1.00 48.19  ?  286 ALA   A CA    1 
ATOM   2193 C C     . ALA   A 1 286 ? 5.484  -36.026 -41.039 1.00 46.62  ?  286 ALA   A C     1 
ATOM   2194 O O     . ALA   A 1 286 ? 4.807  -35.050 -40.710 1.00 52.84  ?  286 ALA   A O     1 
ATOM   2195 C CB    . ALA   A 1 286 ? 4.479  -38.036 -39.948 1.00 53.50  ?  286 ALA   A CB    1 
ATOM   2196 N N     . VAL   A 1 287 ? 6.801  -36.014 -41.166 1.00 42.25  ?  287 VAL   A N     1 
ATOM   2197 C CA    . VAL   A 1 287 ? 7.552  -34.733 -41.082 1.00 44.10  ?  287 VAL   A CA    1 
ATOM   2198 C C     . VAL   A 1 287 ? 8.599  -34.775 -42.201 1.00 49.26  ?  287 VAL   A C     1 
ATOM   2199 O O     . VAL   A 1 287 ? 9.121  -35.871 -42.472 1.00 46.13  ?  287 VAL   A O     1 
ATOM   2200 C CB    . VAL   A 1 287 ? 8.218  -34.402 -39.735 1.00 45.25  ?  287 VAL   A CB    1 
ATOM   2201 C CG1   . VAL   A 1 287 ? 7.255  -33.778 -38.739 1.00 51.33  ?  287 VAL   A CG1   1 
ATOM   2202 C CG2   . VAL   A 1 287 ? 8.951  -35.591 -39.137 1.00 46.61  ?  287 VAL   A CG2   1 
ATOM   2203 N N     . THR   A 1 288 ? 8.895  -33.626 -42.803 1.00 49.33  ?  288 THR   A N     1 
ATOM   2204 C CA    . THR   A 1 288 ? 9.822  -33.581 -43.951 1.00 50.34  ?  288 THR   A CA    1 
ATOM   2205 C C     . THR   A 1 288 ? 10.971 -32.657 -43.640 1.00 49.04  ?  288 THR   A C     1 
ATOM   2206 O O     . THR   A 1 288 ? 10.728 -31.493 -43.297 1.00 47.22  ?  288 THR   A O     1 
ATOM   2207 C CB    . THR   A 1 288 ? 9.050  -33.148 -45.199 1.00 52.97  ?  288 THR   A CB    1 
ATOM   2208 O OG1   . THR   A 1 288 ? 8.137  -34.201 -45.493 1.00 51.34  ?  288 THR   A OG1   1 
ATOM   2209 C CG2   . THR   A 1 288 ? 9.955  -32.892 -46.389 1.00 53.86  ?  288 THR   A CG2   1 
ATOM   2210 N N     . PRO   A 1 289 ? 12.221 -33.144 -43.736 1.00 50.23  ?  289 PRO   A N     1 
ATOM   2211 C CA    . PRO   A 1 289 ? 13.383 -32.306 -43.494 1.00 48.13  ?  289 PRO   A CA    1 
ATOM   2212 C C     . PRO   A 1 289 ? 13.639 -31.191 -44.498 1.00 50.07  ?  289 PRO   A C     1 
ATOM   2213 O O     . PRO   A 1 289 ? 13.641 -31.439 -45.705 1.00 53.09  ?  289 PRO   A O     1 
ATOM   2214 C CB    . PRO   A 1 289 ? 14.498 -33.349 -43.494 1.00 44.88  ?  289 PRO   A CB    1 
ATOM   2215 C CG    . PRO   A 1 289 ? 13.994 -34.438 -44.393 1.00 50.26  ?  289 PRO   A CG    1 
ATOM   2216 C CD    . PRO   A 1 289 ? 12.532 -34.523 -44.035 1.00 47.21  ?  289 PRO   A CD    1 
ATOM   2217 N N     . LYS   A 1 290 ? 13.855 -29.979 -44.001 1.00 50.70  ?  290 LYS   A N     1 
ATOM   2218 C CA    . LYS   A 1 290 ? 14.156 -28.819 -44.872 1.00 49.57  ?  290 LYS   A CA    1 
ATOM   2219 C C     . LYS   A 1 290 ? 15.524 -28.251 -44.464 1.00 51.45  ?  290 LYS   A C     1 
ATOM   2220 O O     . LYS   A 1 290 ? 16.136 -28.821 -43.554 1.00 52.94  ?  290 LYS   A O     1 
ATOM   2221 C CB    . LYS   A 1 290 ? 12.960 -27.875 -44.737 1.00 54.39  ?  290 LYS   A CB    1 
ATOM   2222 C CG    . LYS   A 1 290 ? 11.818 -28.117 -45.701 1.00 56.02  ?  290 LYS   A CG    1 
ATOM   2223 C CD    . LYS   A 1 290 ? 12.156 -27.707 -47.126 1.00 57.90  ?  290 LYS   A CD    1 
ATOM   2224 C CE    . LYS   A 1 290 ? 11.146 -28.179 -48.118 1.00 59.20  ?  290 LYS   A CE    1 
ATOM   2225 N NZ    . LYS   A 1 290 ? 11.796 -28.882 -49.224 1.00 53.16  ?  290 LYS   A NZ    1 
ATOM   2226 N N     . PRO   A 1 291 ? 16.050 -27.183 -45.101 1.00 55.68  ?  291 PRO   A N     1 
ATOM   2227 C CA    . PRO   A 1 291 ? 17.394 -26.713 -44.793 1.00 54.21  ?  291 PRO   A CA    1 
ATOM   2228 C C     . PRO   A 1 291 ? 17.750 -25.359 -44.181 1.00 52.40  ?  291 PRO   A C     1 
ATOM   2229 O O     . PRO   A 1 291 ? 18.976 -25.213 -44.067 1.00 55.96  ?  291 PRO   A O     1 
ATOM   2230 C CB    . PRO   A 1 291 ? 17.774 -26.734 -46.275 1.00 51.90  ?  291 PRO   A CB    1 
ATOM   2231 C CG    . PRO   A 1 291 ? 16.679 -25.944 -46.934 1.00 47.18  ?  291 PRO   A CG    1 
ATOM   2232 C CD    . PRO   A 1 291 ? 15.457 -26.453 -46.210 1.00 50.14  ?  291 PRO   A CD    1 
ATOM   2233 N N     . ALA   A 1 292 ? 16.802 -24.486 -43.835 1.00 45.92  ?  292 ALA   A N     1 
ATOM   2234 C CA    . ALA   A 1 292 ? 17.015 -23.121 -43.277 1.00 45.41  ?  292 ALA   A CA    1 
ATOM   2235 C C     . ALA   A 1 292 ? 16.074 -22.175 -43.997 1.00 48.15  ?  292 ALA   A C     1 
ATOM   2236 O O     . ALA   A 1 292 ? 15.978 -22.250 -45.219 1.00 55.01  ?  292 ALA   A O     1 
ATOM   2237 C CB    . ALA   A 1 292 ? 18.409 -22.591 -43.373 1.00 41.55  ?  292 ALA   A CB    1 
ATOM   2238 N N     . ILE   A 1 293 ? 15.423 -21.300 -43.255 1.00 44.39  ?  293 ILE   A N     1 
ATOM   2239 C CA    . ILE   A 1 293 ? 14.393 -20.420 -43.873 1.00 42.83  ?  293 ILE   A CA    1 
ATOM   2240 C C     . ILE   A 1 293 ? 15.137 -19.213 -44.443 1.00 47.12  ?  293 ILE   A C     1 
ATOM   2241 O O     . ILE   A 1 293 ? 16.038 -18.719 -43.755 1.00 48.20  ?  293 ILE   A O     1 
ATOM   2242 C CB    . ILE   A 1 293 ? 13.328 -20.012 -42.844 1.00 44.61  ?  293 ILE   A CB    1 
ATOM   2243 C CG1   . ILE   A 1 293 ? 12.506 -21.202 -42.376 1.00 40.16  ?  293 ILE   A CG1   1 
ATOM   2244 C CG2   . ILE   A 1 293 ? 12.436 -18.894 -43.383 1.00 47.01  ?  293 ILE   A CG2   1 
ATOM   2245 C CD1   . ILE   A 1 293 ? 11.231 -20.811 -41.655 1.00 42.04  ?  293 ILE   A CD1   1 
ATOM   2246 N N     . ALA   A 1 294 ? 14.773 -18.758 -45.643 1.00 54.45  ?  294 ALA   A N     1 
ATOM   2247 C CA    . ALA   A 1 294 ? 15.557 -17.690 -46.308 1.00 51.36  ?  294 ALA   A CA    1 
ATOM   2248 C C     . ALA   A 1 294 ? 14.696 -16.463 -46.581 1.00 43.47  ?  294 ALA   A C     1 
ATOM   2249 O O     . ALA   A 1 294 ? 15.272 -15.375 -46.611 1.00 43.97  ?  294 ALA   A O     1 
ATOM   2250 C CB    . ALA   A 1 294 ? 16.167 -18.222 -47.570 1.00 48.12  ?  294 ALA   A CB    1 
ATOM   2251 N N     . SER   A 1 295 ? 13.386 -16.632 -46.760 1.00 44.50  ?  295 SER   A N     1 
ATOM   2252 C CA    . SER   A 1 295 ? 12.577 -15.426 -46.910 1.00 47.62  ?  295 SER   A CA    1 
ATOM   2253 C C     . SER   A 1 295 ? 11.116 -15.805 -46.721 1.00 49.18  ?  295 SER   A C     1 
ATOM   2254 O O     . SER   A 1 295 ? 10.745 -16.975 -46.835 1.00 50.70  ?  295 SER   A O     1 
ATOM   2255 C CB    . SER   A 1 295 ? 12.803 -14.756 -48.275 1.00 56.67  ?  295 SER   A CB    1 
ATOM   2256 O OG    . SER   A 1 295 ? 11.627 -14.125 -48.762 1.00 62.46  ?  295 SER   A OG    1 
ATOM   2257 N N     . PHE   A 1 296 ? 10.295 -14.809 -46.413 1.00 47.70  ?  296 PHE   A N     1 
ATOM   2258 C CA    . PHE   A 1 296 ? 8.849  -14.991 -46.300 1.00 57.55  ?  296 PHE   A CA    1 
ATOM   2259 C C     . PHE   A 1 296 ? 8.180  -14.366 -47.530 1.00 65.33  ?  296 PHE   A C     1 
ATOM   2260 O O     . PHE   A 1 296 ? 7.948  -13.151 -47.576 1.00 64.19  ?  296 PHE   A O     1 
ATOM   2261 C CB    . PHE   A 1 296 ? 8.314  -14.381 -45.002 1.00 63.89  ?  296 PHE   A CB    1 
ATOM   2262 C CG    . PHE   A 1 296 ? 8.684  -15.155 -43.772 1.00 61.10  ?  296 PHE   A CG    1 
ATOM   2263 C CD1   . PHE   A 1 296 ? 9.883  -14.897 -43.115 1.00 59.76  ?  296 PHE   A CD1   1 
ATOM   2264 C CD2   . PHE   A 1 296 ? 7.843  -16.146 -43.273 1.00 57.21  ?  296 PHE   A CD2   1 
ATOM   2265 C CE1   . PHE   A 1 296 ? 10.232 -15.613 -41.979 1.00 57.32  ?  296 PHE   A CE1   1 
ATOM   2266 C CE2   . PHE   A 1 296 ? 8.185  -16.872 -42.145 1.00 53.04  ?  296 PHE   A CE2   1 
ATOM   2267 C CZ    . PHE   A 1 296 ? 9.378  -16.606 -41.495 1.00 53.77  ?  296 PHE   A CZ    1 
ATOM   2268 N N     . ASP   A 1 297 ? 7.858  -15.213 -48.520 1.00 68.56  ?  297 ASP   A N     1 
ATOM   2269 C CA    . ASP   A 1 297 ? 7.201  -14.814 -49.771 1.00 64.17  ?  297 ASP   A CA    1 
ATOM   2270 C C     . ASP   A 1 297 ? 5.694  -14.958 -49.569 1.00 62.14  ?  297 ASP   A C     1 
ATOM   2271 O O     . ASP   A 1 297 ? 5.106  -16.001 -49.845 1.00 62.76  ?  297 ASP   A O     1 
ATOM   2272 C CB    . ASP   A 1 297 ? 7.724  -15.669 -50.927 1.00 65.67  ?  297 ASP   A CB    1 
ATOM   2273 C CG    . ASP   A 1 297 ? 7.418  -15.078 -52.336 1.00 69.99  ?  297 ASP   A CG    1 
ATOM   2274 O OD1   . ASP   A 1 297 ? 6.349  -14.457 -52.525 1.00 68.18  ?  297 ASP   A OD1   1 
ATOM   2275 O OD2   . ASP   A 1 297 ? 8.252  -15.262 -53.264 1.00 62.89  ?  297 ASP   A OD2   1 
ATOM   2276 N N     . GLY   A 1 298 ? 5.063  -13.910 -49.044 1.00 58.15  ?  298 GLY   A N     1 
ATOM   2277 C CA    . GLY   A 1 298 ? 3.610  -13.865 -48.958 1.00 62.27  ?  298 GLY   A CA    1 
ATOM   2278 C C     . GLY   A 1 298 ? 2.919  -14.883 -48.061 1.00 70.82  ?  298 GLY   A C     1 
ATOM   2279 O O     . GLY   A 1 298 ? 2.888  -14.724 -46.834 1.00 69.98  ?  298 GLY   A O     1 
ATOM   2280 N N     . ASP   A 1 299 ? 2.311  -15.914 -48.653 1.00 71.19  ?  299 ASP   A N     1 
ATOM   2281 C CA    . ASP   A 1 299 ? 1.776  -17.025 -47.877 1.00 67.43  ?  299 ASP   A CA    1 
ATOM   2282 C C     . ASP   A 1 299 ? 2.684  -18.246 -47.935 1.00 70.11  ?  299 ASP   A C     1 
ATOM   2283 O O     . ASP   A 1 299 ? 2.318  -19.317 -47.438 1.00 71.74  ?  299 ASP   A O     1 
ATOM   2284 C CB    . ASP   A 1 299 ? 0.343  -17.379 -48.323 1.00 68.88  ?  299 ASP   A CB    1 
ATOM   2285 C CG    . ASP   A 1 299 ? 0.236  -17.805 -49.792 1.00 72.04  ?  299 ASP   A CG    1 
ATOM   2286 O OD1   . ASP   A 1 299 ? 1.253  -17.831 -50.527 1.00 65.29  ?  299 ASP   A OD1   1 
ATOM   2287 O OD2   . ASP   A 1 299 ? -0.908 -18.110 -50.205 1.00 73.36  ?  299 ASP   A OD2   1 
ATOM   2288 N N     . ARG   A 1 300 ? 3.871  -18.099 -48.507 1.00 65.05  ?  300 ARG   A N     1 
ATOM   2289 C CA    . ARG   A 1 300 ? 4.794  -19.206 -48.662 1.00 66.19  ?  300 ARG   A CA    1 
ATOM   2290 C C     . ARG   A 1 300 ? 6.085  -18.908 -47.902 1.00 68.10  ?  300 ARG   A C     1 
ATOM   2291 O O     . ARG   A 1 300 ? 6.352  -17.765 -47.514 1.00 68.68  ?  300 ARG   A O     1 
ATOM   2292 C CB    . ARG   A 1 300 ? 5.071  -19.485 -50.158 1.00 68.79  ?  300 ARG   A CB    1 
ATOM   2293 C CG    . ARG   A 1 300 ? 3.799  -19.654 -51.029 1.00 68.22  ?  300 ARG   A CG    1 
ATOM   2294 C CD    . ARG   A 1 300 ? 4.117  -19.749 -52.514 1.00 58.24  ?  300 ARG   A CD    1 
ATOM   2295 N NE    . ARG   A 1 300 ? 4.884  -20.950 -52.841 1.00 59.77  ?  300 ARG   A NE    1 
ATOM   2296 C CZ    . ARG   A 1 300 ? 4.347  -22.110 -53.218 1.00 60.48  ?  300 ARG   A CZ    1 
ATOM   2297 N NH1   . ARG   A 1 300 ? 3.029  -22.234 -53.322 1.00 62.14  ?  300 ARG   A NH1   1 
ATOM   2298 N NH2   . ARG   A 1 300 ? 5.128  -23.148 -53.491 1.00 55.95  ?  300 ARG   A NH2   1 
ATOM   2299 N N     . VAL   A 1 301 ? 6.876  -19.962 -47.674 1.00 61.22  ?  301 VAL   A N     1 
ATOM   2300 C CA    . VAL   A 1 301 ? 8.165  -19.878 -46.987 1.00 57.76  ?  301 VAL   A CA    1 
ATOM   2301 C C     . VAL   A 1 301 ? 9.248  -20.367 -47.946 1.00 53.30  ?  301 VAL   A C     1 
ATOM   2302 O O     . VAL   A 1 301 ? 9.247  -21.538 -48.346 1.00 50.46  ?  301 VAL   A O     1 
ATOM   2303 C CB    . VAL   A 1 301 ? 8.174  -20.694 -45.675 1.00 52.96  ?  301 VAL   A CB    1 
ATOM   2304 C CG1   . VAL   A 1 301 ? 9.583  -20.864 -45.157 1.00 47.07  ?  301 VAL   A CG1   1 
ATOM   2305 C CG2   . VAL   A 1 301 ? 7.327  -20.021 -44.620 1.00 48.66  ?  301 VAL   A CG2   1 
ATOM   2306 N N     . VAL   A 1 302 ? 10.170 -19.470 -48.308 1.00 53.21  ?  302 VAL   A N     1 
ATOM   2307 C CA    . VAL   A 1 302 ? 11.293 -19.795 -49.182 1.00 47.88  ?  302 VAL   A CA    1 
ATOM   2308 C C     . VAL   A 1 302 ? 12.462 -20.244 -48.322 1.00 50.80  ?  302 VAL   A C     1 
ATOM   2309 O O     . VAL   A 1 302 ? 12.804 -19.579 -47.335 1.00 56.43  ?  302 VAL   A O     1 
ATOM   2310 C CB    . VAL   A 1 302 ? 11.691 -18.585 -50.052 1.00 54.45  ?  302 VAL   A CB    1 
ATOM   2311 C CG1   . VAL   A 1 302 ? 12.780 -18.983 -51.045 1.00 51.47  ?  302 VAL   A CG1   1 
ATOM   2312 C CG2   . VAL   A 1 302 ? 10.473 -17.990 -50.784 1.00 54.07  ?  302 VAL   A CG2   1 
ATOM   2313 N N     . PHE   A 1 303 ? 13.086 -21.363 -48.695 1.00 51.44  ?  303 PHE   A N     1 
ATOM   2314 C CA    . PHE   A 1 303 ? 14.235 -21.910 -47.981 1.00 50.99  ?  303 PHE   A CA    1 
ATOM   2315 C C     . PHE   A 1 303 ? 15.527 -21.639 -48.744 1.00 50.61  ?  303 PHE   A C     1 
ATOM   2316 O O     . PHE   A 1 303 ? 15.534 -21.014 -49.804 1.00 57.26  ?  303 PHE   A O     1 
ATOM   2317 C CB    . PHE   A 1 303 ? 14.058 -23.406 -47.733 1.00 45.52  ?  303 PHE   A CB    1 
ATOM   2318 C CG    . PHE   A 1 303 ? 12.838 -23.730 -46.956 1.00 51.43  ?  303 PHE   A CG    1 
ATOM   2319 C CD1   . PHE   A 1 303 ? 12.844 -23.659 -45.572 1.00 57.72  ?  303 PHE   A CD1   1 
ATOM   2320 C CD2   . PHE   A 1 303 ? 11.673 -24.088 -47.593 1.00 52.00  ?  303 PHE   A CD2   1 
ATOM   2321 C CE1   . PHE   A 1 303 ? 11.702 -23.955 -44.842 1.00 54.14  ?  303 PHE   A CE1   1 
ATOM   2322 C CE2   . PHE   A 1 303 ? 10.538 -24.387 -46.869 1.00 56.99  ?  303 PHE   A CE2   1 
ATOM   2323 C CZ    . PHE   A 1 303 ? 10.552 -24.319 -45.492 1.00 54.91  ?  303 PHE   A CZ    1 
ATOM   2324 N N     . THR   A 1 304 ? 16.639 -22.134 -48.198 1.00 54.33  ?  304 THR   A N     1 
ATOM   2325 C CA    . THR   A 1 304 ? 17.964 -21.706 -48.646 1.00 57.17  ?  304 THR   A CA    1 
ATOM   2326 C C     . THR   A 1 304 ? 18.487 -22.505 -49.829 1.00 52.53  ?  304 THR   A C     1 
ATOM   2327 O O     . THR   A 1 304 ? 19.469 -22.081 -50.455 1.00 47.90  ?  304 THR   A O     1 
ATOM   2328 C CB    . THR   A 1 304 ? 18.997 -21.773 -47.492 1.00 49.34  ?  304 THR   A CB    1 
ATOM   2329 O OG1   . THR   A 1 304 ? 19.080 -23.103 -46.963 1.00 47.96  ?  304 THR   A OG1   1 
ATOM   2330 C CG2   . THR   A 1 304 ? 18.625 -20.787 -46.383 1.00 47.50  ?  304 THR   A CG2   1 
ATOM   2331 N N     . ASP   A 1 305 ? 17.871 -23.648 -50.130 1.00 54.61  ?  305 ASP   A N     1 
ATOM   2332 C CA    . ASP   A 1 305 ? 18.216 -24.448 -51.298 1.00 53.69  ?  305 ASP   A CA    1 
ATOM   2333 C C     . ASP   A 1 305 ? 17.298 -24.156 -52.481 1.00 54.54  ?  305 ASP   A C     1 
ATOM   2334 O O     . ASP   A 1 305 ? 17.341 -24.882 -53.479 1.00 53.50  ?  305 ASP   A O     1 
ATOM   2335 C CB    . ASP   A 1 305 ? 18.193 -25.947 -50.947 1.00 48.61  ?  305 ASP   A CB    1 
ATOM   2336 C CG    . ASP   A 1 305 ? 16.808 -26.444 -50.548 1.00 48.54  ?  305 ASP   A CG    1 
ATOM   2337 O OD1   . ASP   A 1 305 ? 15.864 -25.627 -50.469 1.00 47.96  ?  305 ASP   A OD1   1 
ATOM   2338 O OD2   . ASP   A 1 305 ? 16.669 -27.665 -50.322 1.00 46.05  ?  305 ASP   A OD2   1 
ATOM   2339 N N     . GLY   A 1 306 ? 16.463 -23.119 -52.382 1.00 56.39  ?  306 GLY   A N     1 
ATOM   2340 C CA    . GLY   A 1 306 ? 15.603 -22.698 -53.465 1.00 54.16  ?  306 GLY   A CA    1 
ATOM   2341 C C     . GLY   A 1 306 ? 14.173 -23.178 -53.366 1.00 57.54  ?  306 GLY   A C     1 
ATOM   2342 O O     . GLY   A 1 306 ? 13.328 -22.721 -54.143 1.00 56.57  ?  306 GLY   A O     1 
ATOM   2343 N N     . THR   A 1 307 ? 13.867 -24.055 -52.422 1.00 55.79  ?  307 THR   A N     1 
ATOM   2344 C CA    . THR   A 1 307 ? 12.547 -24.654 -52.390 1.00 53.53  ?  307 THR   A CA    1 
ATOM   2345 C C     . THR   A 1 307 ? 11.551 -23.769 -51.632 1.00 52.48  ?  307 THR   A C     1 
ATOM   2346 O O     . THR   A 1 307 ? 11.910 -22.773 -51.000 1.00 56.78  ?  307 THR   A O     1 
ATOM   2347 C CB    . THR   A 1 307 ? 12.669 -26.041 -51.803 1.00 58.77  ?  307 THR   A CB    1 
ATOM   2348 O OG1   . THR   A 1 307 ? 13.064 -25.945 -50.431 1.00 55.68  ?  307 THR   A OG1   1 
ATOM   2349 C CG2   . THR   A 1 307 ? 13.764 -26.766 -52.574 1.00 55.47  ?  307 THR   A CG2   1 
ATOM   2350 N N     . SER   A 1 308 ? 10.275 -24.077 -51.811 1.00 47.58  ?  308 SER   A N     1 
ATOM   2351 C CA    . SER   A 1 308 ? 9.241  -23.195 -51.233 1.00 54.20  ?  308 SER   A CA    1 
ATOM   2352 C C     . SER   A 1 308 ? 8.004  -24.015 -50.880 1.00 60.80  ?  308 SER   A C     1 
ATOM   2353 O O     . SER   A 1 308 ? 7.856  -25.117 -51.422 1.00 63.68  ?  308 SER   A O     1 
ATOM   2354 C CB    . SER   A 1 308 ? 8.896  -22.085 -52.184 1.00 61.46  ?  308 SER   A CB    1 
ATOM   2355 O OG    . SER   A 1 308 ? 7.537  -22.137 -52.591 1.00 63.71  ?  308 SER   A OG    1 
ATOM   2356 N N     . GLU   A 1 309 ? 7.155  -23.468 -50.018 1.00 58.25  ?  309 GLU   A N     1 
ATOM   2357 C CA    . GLU   A 1 309 ? 5.984  -24.232 -49.561 1.00 60.84  ?  309 GLU   A CA    1 
ATOM   2358 C C     . GLU   A 1 309 ? 4.942  -23.306 -48.960 1.00 64.54  ?  309 GLU   A C     1 
ATOM   2359 O O     . GLU   A 1 309 ? 5.319  -22.333 -48.305 1.00 64.66  ?  309 GLU   A O     1 
ATOM   2360 C CB    . GLU   A 1 309 ? 6.401  -25.150 -48.420 1.00 59.66  ?  309 GLU   A CB    1 
ATOM   2361 C CG    . GLU   A 1 309 ? 5.754  -26.528 -48.470 1.00 58.40  ?  309 GLU   A CG    1 
ATOM   2362 C CD    . GLU   A 1 309 ? 6.706  -27.531 -49.080 1.00 59.35  ?  309 GLU   A CD    1 
ATOM   2363 O OE1   . GLU   A 1 309 ? 7.922  -27.425 -48.847 1.00 59.66  ?  309 GLU   A OE1   1 
ATOM   2364 O OE2   . GLU   A 1 309 ? 6.222  -28.423 -49.791 1.00 62.71  ?  309 GLU   A OE2   1 
ATOM   2365 N N     . PRO   A 1 310 ? 3.643  -23.571 -49.170 1.00 67.50  ?  310 PRO   A N     1 
ATOM   2366 C CA    . PRO   A 1 310 ? 2.625  -22.802 -48.490 1.00 67.83  ?  310 PRO   A CA    1 
ATOM   2367 C C     . PRO   A 1 310 ? 2.656  -23.142 -47.010 1.00 67.05  ?  310 PRO   A C     1 
ATOM   2368 O O     . PRO   A 1 310 ? 2.770  -24.328 -46.658 1.00 59.23  ?  310 PRO   A O     1 
ATOM   2369 C CB    . PRO   A 1 310 ? 1.356  -23.278 -49.183 1.00 66.02  ?  310 PRO   A CB    1 
ATOM   2370 C CG    . PRO   A 1 310 ? 1.693  -24.660 -49.677 1.00 67.96  ?  310 PRO   A CG    1 
ATOM   2371 C CD    . PRO   A 1 310 ? 3.137  -24.550 -50.107 1.00 60.61  ?  310 PRO   A CD    1 
ATOM   2372 N N     . ALA   A 1 311 ? 2.543  -22.118 -46.159 1.00 69.85  ?  311 ALA   A N     1 
ATOM   2373 C CA    . ALA   A 1 311 ? 2.568  -22.315 -44.692 1.00 63.19  ?  311 ALA   A CA    1 
ATOM   2374 C C     . ALA   A 1 311 ? 1.679  -21.292 -44.001 1.00 62.47  ?  311 ALA   A C     1 
ATOM   2375 O O     . ALA   A 1 311 ? 1.632  -20.145 -44.448 1.00 63.16  ?  311 ALA   A O     1 
ATOM   2376 C CB    . ALA   A 1 311 ? 3.975  -22.196 -44.191 1.00 57.22  ?  311 ALA   A CB    1 
ATOM   2377 N N     . ASP   A 1 312 ? 1.001  -21.711 -42.937 1.00 61.02  ?  312 ASP   A N     1 
ATOM   2378 C CA    . ASP   A 1 312 ? 0.180  -20.792 -42.155 1.00 62.32  ?  312 ASP   A CA    1 
ATOM   2379 C C     . ASP   A 1 312 ? 0.805  -20.394 -40.814 1.00 64.69  ?  312 ASP   A C     1 
ATOM   2380 O O     . ASP   A 1 312 ? 0.269  -19.505 -40.138 1.00 62.77  ?  312 ASP   A O     1 
ATOM   2381 C CB    . ASP   A 1 312 ? -1.194 -21.410 -41.871 1.00 65.56  ?  312 ASP   A CB    1 
ATOM   2382 C CG    . ASP   A 1 312 ? -1.790 -22.092 -43.066 1.00 67.38  ?  312 ASP   A CG    1 
ATOM   2383 O OD1   . ASP   A 1 312 ? -1.170 -23.052 -43.567 1.00 67.35  ?  312 ASP   A OD1   1 
ATOM   2384 O OD2   . ASP   A 1 312 ? -2.894 -21.686 -43.481 1.00 73.25  ?  312 ASP   A OD2   1 
ATOM   2385 N N     . ALA   A 1 313 ? 1.894  -21.040 -40.395 1.00 58.87  ?  313 ALA   A N     1 
ATOM   2386 C CA    . ALA   A 1 313 ? 2.535  -20.709 -39.129 1.00 63.93  ?  313 ALA   A CA    1 
ATOM   2387 C C     . ALA   A 1 313 ? 3.976  -21.199 -39.132 1.00 62.22  ?  313 ALA   A C     1 
ATOM   2388 O O     . ALA   A 1 313 ? 4.320  -22.166 -39.827 1.00 53.47  ?  313 ALA   A O     1 
ATOM   2389 C CB    . ALA   A 1 313 ? 1.787  -21.307 -37.933 1.00 57.67  ?  313 ALA   A CB    1 
ATOM   2390 N N     . VAL   A 1 314 ? 4.811  -20.511 -38.344 1.00 57.43  ?  314 VAL   A N     1 
ATOM   2391 C CA    . VAL   A 1 314 ? 6.202  -20.897 -38.101 1.00 55.32  ?  314 VAL   A CA    1 
ATOM   2392 C C     . VAL   A 1 314 ? 6.433  -20.834 -36.594 1.00 57.68  ?  314 VAL   A C     1 
ATOM   2393 O O     . VAL   A 1 314 ? 6.383  -19.747 -36.006 1.00 59.71  ?  314 VAL   A O     1 
ATOM   2394 C CB    . VAL   A 1 314 ? 7.205  -19.989 -38.844 1.00 51.92  ?  314 VAL   A CB    1 
ATOM   2395 C CG1   . VAL   A 1 314 ? 8.618  -20.541 -38.736 1.00 45.98  ?  314 VAL   A CG1   1 
ATOM   2396 C CG2   . VAL   A 1 314 ? 6.812  -19.821 -40.320 1.00 57.98  ?  314 VAL   A CG2   1 
ATOM   2397 N N     . VAL   A 1 315 ? 6.676  -21.986 -35.968 1.00 51.99  ?  315 VAL   A N     1 
ATOM   2398 C CA    . VAL   A 1 315 ? 6.942  -22.055 -34.531 1.00 47.79  ?  315 VAL   A CA    1 
ATOM   2399 C C     . VAL   A 1 315 ? 8.453  -22.136 -34.304 1.00 50.32  ?  315 VAL   A C     1 
ATOM   2400 O O     . VAL   A 1 315 ? 9.135  -23.048 -34.796 1.00 49.92  ?  315 VAL   A O     1 
ATOM   2401 C CB    . VAL   A 1 315 ? 6.191  -23.226 -33.878 1.00 50.07  ?  315 VAL   A CB    1 
ATOM   2402 C CG1   . VAL   A 1 315 ? 6.769  -24.560 -34.272 1.00 52.94  ?  315 VAL   A CG1   1 
ATOM   2403 C CG2   . VAL   A 1 315 ? 6.190  -23.084 -32.378 1.00 48.92  ?  315 VAL   A CG2   1 
ATOM   2404 N N     . TYR   A 1 316 ? 8.993  -21.169 -33.564 1.00 49.89  ?  316 TYR   A N     1 
ATOM   2405 C CA    . TYR   A 1 316 ? 10.440 -21.004 -33.443 1.00 51.23  ?  316 TYR   A CA    1 
ATOM   2406 C C     . TYR   A 1 316 ? 10.929 -21.682 -32.161 1.00 51.03  ?  316 TYR   A C     1 
ATOM   2407 O O     . TYR   A 1 316 ? 10.649 -21.216 -31.052 1.00 48.47  ?  316 TYR   A O     1 
ATOM   2408 C CB    . TYR   A 1 316 ? 10.811 -19.521 -33.506 1.00 53.03  ?  316 TYR   A CB    1 
ATOM   2409 C CG    . TYR   A 1 316 ? 11.225 -19.061 -34.910 1.00 52.57  ?  316 TYR   A CG    1 
ATOM   2410 C CD1   . TYR   A 1 316 ? 12.510 -19.308 -35.384 1.00 57.38  ?  316 TYR   A CD1   1 
ATOM   2411 C CD2   . TYR   A 1 316 ? 10.337 -18.393 -35.762 1.00 53.02  ?  316 TYR   A CD2   1 
ATOM   2412 C CE1   . TYR   A 1 316 ? 12.915 -18.909 -36.668 1.00 64.11  ?  316 TYR   A CE1   1 
ATOM   2413 C CE2   . TYR   A 1 316 ? 10.735 -17.987 -37.061 1.00 60.52  ?  316 TYR   A CE2   1 
ATOM   2414 C CZ    . TYR   A 1 316 ? 12.031 -18.252 -37.503 1.00 62.74  ?  316 TYR   A CZ    1 
ATOM   2415 O OH    . TYR   A 1 316 ? 12.485 -17.875 -38.758 1.00 57.20  ?  316 TYR   A OH    1 
ATOM   2416 N N     . CYS   A 1 317 ? 11.624 -22.806 -32.323 1.00 52.02  ?  317 CYS   A N     1 
ATOM   2417 C CA    . CYS   A 1 317 ? 12.195 -23.574 -31.209 1.00 45.53  ?  317 CYS   A CA    1 
ATOM   2418 C C     . CYS   A 1 317 ? 13.691 -23.303 -31.085 1.00 49.67  ?  317 CYS   A C     1 
ATOM   2419 O O     . CYS   A 1 317 ? 14.533 -24.198 -31.115 1.00 51.26  ?  317 CYS   A O     1 
ATOM   2420 C CB    . CYS   A 1 317 ? 11.909 -25.060 -31.379 1.00 40.97  ?  317 CYS   A CB    1 
ATOM   2421 S SG    . CYS   A 1 317 ? 10.142 -25.305 -31.527 1.00 44.44  ?  317 CYS   A SG    1 
ATOM   2422 N N     . THR   A 1 318 ? 14.000 -22.023 -30.901 1.00 51.61  ?  318 THR   A N     1 
ATOM   2423 C CA    . THR   A 1 318 ? 15.367 -21.520 -30.944 1.00 58.32  ?  318 THR   A CA    1 
ATOM   2424 C C     . THR   A 1 318 ? 16.019 -21.358 -29.562 1.00 59.18  ?  318 THR   A C     1 
ATOM   2425 O O     . THR   A 1 318 ? 17.152 -20.871 -29.479 1.00 57.99  ?  318 THR   A O     1 
ATOM   2426 C CB    . THR   A 1 318 ? 15.378 -20.194 -31.719 1.00 60.54  ?  318 THR   A CB    1 
ATOM   2427 O OG1   . THR   A 1 318 ? 14.324 -19.350 -31.250 1.00 59.62  ?  318 THR   A OG1   1 
ATOM   2428 C CG2   . THR   A 1 318 ? 15.153 -20.455 -33.203 1.00 62.25  ?  318 THR   A CG2   1 
ATOM   2429 N N     . GLY   A 1 319 ? 15.346 -21.746 -28.485 1.00 54.32  ?  319 GLY   A N     1 
ATOM   2430 C CA    . GLY   A 1 319 ? 15.954 -21.712 -27.167 1.00 57.02  ?  319 GLY   A CA    1 
ATOM   2431 C C     . GLY   A 1 319 ? 15.507 -20.529 -26.326 1.00 55.87  ?  319 GLY   A C     1 
ATOM   2432 O O     . GLY   A 1 319 ? 14.546 -19.816 -26.637 1.00 57.16  ?  319 GLY   A O     1 
ATOM   2433 N N     . PHE   A 1 320 ? 16.235 -20.325 -25.225 1.00 54.88  ?  320 PHE   A N     1 
ATOM   2434 C CA    . PHE   A 1 320 ? 15.923 -19.275 -24.261 1.00 56.89  ?  320 PHE   A CA    1 
ATOM   2435 C C     . PHE   A 1 320 ? 17.180 -18.518 -23.850 1.00 58.69  ?  320 PHE   A C     1 
ATOM   2436 O O     . PHE   A 1 320 ? 18.310 -19.008 -23.963 1.00 55.46  ?  320 PHE   A O     1 
ATOM   2437 C CB    . PHE   A 1 320 ? 15.254 -19.825 -22.983 1.00 57.45  ?  320 PHE   A CB    1 
ATOM   2438 C CG    . PHE   A 1 320 ? 13.930 -20.482 -23.218 1.00 55.35  ?  320 PHE   A CG    1 
ATOM   2439 C CD1   . PHE   A 1 320 ? 13.859 -21.817 -23.589 1.00 54.21  ?  320 PHE   A CD1   1 
ATOM   2440 C CD2   . PHE   A 1 320 ? 12.753 -19.768 -23.071 1.00 54.72  ?  320 PHE   A CD2   1 
ATOM   2441 C CE1   . PHE   A 1 320 ? 12.627 -22.427 -23.812 1.00 55.42  ?  320 PHE   A CE1   1 
ATOM   2442 C CE2   . PHE   A 1 320 ? 11.522 -20.371 -23.295 1.00 54.68  ?  320 PHE   A CE2   1 
ATOM   2443 C CZ    . PHE   A 1 320 ? 11.455 -21.698 -23.661 1.00 54.51  ?  320 PHE   A CZ    1 
ATOM   2444 N N     . HIS   A 1 321 ? 16.958 -17.338 -23.280 1.00 59.31  ?  321 HIS   A N     1 
ATOM   2445 C CA    . HIS   A 1 321 ? 18.087 -16.530 -22.767 1.00 61.16  ?  321 HIS   A CA    1 
ATOM   2446 C C     . HIS   A 1 321 ? 18.056 -16.572 -21.238 1.00 62.23  ?  321 HIS   A C     1 
ATOM   2447 O O     . HIS   A 1 321 ? 16.969 -16.762 -20.665 1.00 59.93  ?  321 HIS   A O     1 
ATOM   2448 C CB    . HIS   A 1 321 ? 17.959 -15.088 -23.255 1.00 63.14  ?  321 HIS   A CB    1 
ATOM   2449 C CG    . HIS   A 1 321 ? 18.358 -14.824 -24.661 1.00 64.97  ?  321 HIS   A CG    1 
ATOM   2450 N ND1   . HIS   A 1 321 ? 19.539 -15.262 -25.214 1.00 66.29  ?  321 HIS   A ND1   1 
ATOM   2451 C CD2   . HIS   A 1 321 ? 17.734 -14.131 -25.613 1.00 64.42  ?  321 HIS   A CD2   1 
ATOM   2452 C CE1   . HIS   A 1 321 ? 19.607 -14.849 -26.468 1.00 65.37  ?  321 HIS   A CE1   1 
ATOM   2453 N NE2   . HIS   A 1 321 ? 18.520 -14.161 -26.730 1.00 66.77  ?  321 HIS   A NE2   1 
ATOM   2454 N N     . MET   A 1 322 ? 19.209 -16.381 -20.598 1.00 61.96  ?  322 MET   A N     1 
ATOM   2455 C CA    . MET   A 1 322 ? 19.301 -16.381 -19.115 1.00 58.87  ?  322 MET   A CA    1 
ATOM   2456 C C     . MET   A 1 322 ? 19.281 -14.933 -18.616 1.00 59.75  ?  322 MET   A C     1 
ATOM   2457 O O     . MET   A 1 322 ? 20.232 -14.193 -18.917 1.00 58.55  ?  322 MET   A O     1 
ATOM   2458 C CB    . MET   A 1 322 ? 20.580 -17.091 -18.669 1.00 53.48  ?  322 MET   A CB    1 
ATOM   2459 C CG    . MET   A 1 322 ? 20.839 -17.078 -17.181 1.00 70.32  ?  322 MET   A CG    1 
ATOM   2460 S SD    . MET   A 1 322 ? 22.589 -17.346 -16.841 1.00 72.26  ?  322 MET   A SD    1 
ATOM   2461 C CE    . MET   A 1 322 ? 23.119 -15.657 -16.532 1.00 56.49  ?  322 MET   A CE    1 
ATOM   2462 N N     . THR   A 1 323 ? 18.220 -14.547 -17.910 1.00 56.58  ?  323 THR   A N     1 
ATOM   2463 C CA    . THR   A 1 323 ? 18.076 -13.159 -17.424 1.00 57.50  ?  323 THR   A CA    1 
ATOM   2464 C C     . THR   A 1 323 ? 17.536 -13.141 -16.008 1.00 60.96  ?  323 THR   A C     1 
ATOM   2465 O O     . THR   A 1 323 ? 16.725 -14.022 -15.676 1.00 57.30  ?  323 THR   A O     1 
ATOM   2466 C CB    . THR   A 1 323 ? 17.167 -12.366 -18.363 1.00 54.81  ?  323 THR   A CB    1 
ATOM   2467 O OG1   . THR   A 1 323 ? 15.968 -13.123 -18.466 1.00 57.44  ?  323 THR   A OG1   1 
ATOM   2468 C CG2   . THR   A 1 323 ? 17.772 -12.145 -19.737 1.00 57.15  ?  323 THR   A CG2   1 
ATOM   2469 N N     . PHE   A 1 324 ? 17.987 -12.194 -15.187 1.00 59.46  ?  324 PHE   A N     1 
ATOM   2470 C CA    . PHE   A 1 324 ? 17.461 -12.003 -13.837 1.00 58.82  ?  324 PHE   A CA    1 
ATOM   2471 C C     . PHE   A 1 324 ? 17.129 -10.523 -13.682 1.00 56.44  ?  324 PHE   A C     1 
ATOM   2472 O O     . PHE   A 1 324 ? 17.964 -9.723  -13.240 1.00 57.57  ?  324 PHE   A O     1 
ATOM   2473 C CB    . PHE   A 1 324 ? 18.465 -12.460 -12.775 1.00 57.18  ?  324 PHE   A CB    1 
ATOM   2474 C CG    . PHE   A 1 324 ? 18.810 -13.927 -12.832 1.00 50.54  ?  324 PHE   A CG    1 
ATOM   2475 C CD1   . PHE   A 1 324 ? 17.953 -14.883 -12.303 1.00 50.83  ?  324 PHE   A CD1   1 
ATOM   2476 C CD2   . PHE   A 1 324 ? 20.004 -14.348 -13.385 1.00 53.13  ?  324 PHE   A CD2   1 
ATOM   2477 C CE1   . PHE   A 1 324 ? 18.282 -16.237 -12.336 1.00 47.10  ?  324 PHE   A CE1   1 
ATOM   2478 C CE2   . PHE   A 1 324 ? 20.351 -15.690 -13.414 1.00 51.30  ?  324 PHE   A CE2   1 
ATOM   2479 C CZ    . PHE   A 1 324 ? 19.490 -16.636 -12.891 1.00 49.15  ?  324 PHE   A CZ    1 
ATOM   2480 N N     . PRO   A 1 325 ? 15.891 -10.083 -14.014 1.00 54.95  ?  325 PRO   A N     1 
ATOM   2481 C CA    . PRO   A 1 325 ? 15.579 -8.663  -13.983 1.00 56.30  ?  325 PRO   A CA    1 
ATOM   2482 C C     . PRO   A 1 325 ? 15.428 -8.014  -12.624 1.00 56.45  ?  325 PRO   A C     1 
ATOM   2483 O O     . PRO   A 1 325 ? 15.580 -6.785  -12.535 1.00 52.88  ?  325 PRO   A O     1 
ATOM   2484 C CB    . PRO   A 1 325 ? 14.259 -8.645  -14.752 1.00 55.24  ?  325 PRO   A CB    1 
ATOM   2485 C CG    . PRO   A 1 325 ? 13.575 -9.910  -14.337 1.00 59.06  ?  325 PRO   A CG    1 
ATOM   2486 C CD    . PRO   A 1 325 ? 14.718 -10.883 -14.441 1.00 58.58  ?  325 PRO   A CD    1 
ATOM   2487 N N     . PHE   A 1 326 ? 15.128 -8.810  -11.602 1.00 55.85  ?  326 PHE   A N     1 
ATOM   2488 C CA    . PHE   A 1 326 ? 14.920 -8.280  -10.234 1.00 55.01  ?  326 PHE   A CA    1 
ATOM   2489 C C     . PHE   A 1 326 ? 16.272 -8.022  -9.630  1.00 55.73  ?  326 PHE   A C     1 
ATOM   2490 O O     . PHE   A 1 326 ? 16.335 -7.631  -8.465  1.00 59.39  ?  326 PHE   A O     1 
ATOM   2491 C CB    . PHE   A 1 326 ? 14.100 -9.317  -9.468  1.00 53.86  ?  326 PHE   A CB    1 
ATOM   2492 C CG    . PHE   A 1 326 ? 14.561 -10.757 -9.632  1.00 52.12  ?  326 PHE   A CG    1 
ATOM   2493 C CD1   . PHE   A 1 326 ? 15.628 -11.252 -8.897  1.00 45.86  ?  326 PHE   A CD1   1 
ATOM   2494 C CD2   . PHE   A 1 326 ? 13.917 -11.614 -10.513 1.00 50.62  ?  326 PHE   A CD2   1 
ATOM   2495 C CE1   . PHE   A 1 326 ? 16.044 -12.561 -9.052  1.00 51.57  ?  326 PHE   A CE1   1 
ATOM   2496 C CE2   . PHE   A 1 326 ? 14.338 -12.922 -10.660 1.00 49.31  ?  326 PHE   A CE2   1 
ATOM   2497 C CZ    . PHE   A 1 326 ? 15.397 -13.392 -9.930  1.00 45.91  ?  326 PHE   A CZ    1 
ATOM   2498 N N     . LEU   A 1 327 ? 17.324 -8.274  -10.397 1.00 54.81  ?  327 LEU   A N     1 
ATOM   2499 C CA    . LEU   A 1 327 ? 18.693 -7.978  -9.929  1.00 58.59  ?  327 LEU   A CA    1 
ATOM   2500 C C     . LEU   A 1 327 ? 19.173 -6.754  -10.703 1.00 62.55  ?  327 LEU   A C     1 
ATOM   2501 O O     . LEU   A 1 327 ? 19.759 -6.938  -11.772 1.00 59.32  ?  327 LEU   A O     1 
ATOM   2502 C CB    . LEU   A 1 327 ? 19.607 -9.173  -10.172 1.00 54.42  ?  327 LEU   A CB    1 
ATOM   2503 C CG    . LEU   A 1 327 ? 19.435 -10.355 -9.221  1.00 51.04  ?  327 LEU   A CG    1 
ATOM   2504 C CD1   . LEU   A 1 327 ? 20.481 -11.401 -9.537  1.00 51.87  ?  327 LEU   A CD1   1 
ATOM   2505 C CD2   . LEU   A 1 327 ? 19.567 -9.873  -7.793  1.00 56.05  ?  327 LEU   A CD2   1 
ATOM   2506 N N     . PRO   A 1 328 ? 18.888 -5.520  -10.245 1.00 63.61  ?  328 PRO   A N     1 
ATOM   2507 C CA    . PRO   A 1 328 ? 19.272 -4.344  -10.994 1.00 64.41  ?  328 PRO   A CA    1 
ATOM   2508 C C     . PRO   A 1 328 ? 20.695 -4.535  -11.463 1.00 68.76  ?  328 PRO   A C     1 
ATOM   2509 O O     . PRO   A 1 328 ? 20.971 -4.473  -12.670 1.00 73.50  ?  328 PRO   A O     1 
ATOM   2510 C CB    . PRO   A 1 328 ? 19.116 -3.297  -9.920  1.00 64.61  ?  328 PRO   A CB    1 
ATOM   2511 C CG    . PRO   A 1 328 ? 17.890 -3.740  -9.178  1.00 64.71  ?  328 PRO   A CG    1 
ATOM   2512 C CD    . PRO   A 1 328 ? 18.169 -5.216  -9.033  1.00 61.35  ?  328 PRO   A CD    1 
ATOM   2513 N N     . ALA   A 1 329 ? 21.603 -4.761  -10.529 1.00 59.54  ?  329 ALA   A N     1 
ATOM   2514 C CA    . ALA   A 1 329 ? 22.998 -5.049  -10.905 1.00 64.82  ?  329 ALA   A CA    1 
ATOM   2515 C C     . ALA   A 1 329 ? 23.034 -6.358  -11.682 1.00 68.25  ?  329 ALA   A C     1 
ATOM   2516 O O     . ALA   A 1 329 ? 22.347 -7.302  -11.268 1.00 69.05  ?  329 ALA   A O     1 
ATOM   2517 C CB    . ALA   A 1 329 ? 23.799 -5.174  -9.644  1.00 63.23  ?  329 ALA   A CB    1 
ATOM   2518 N N     . GLY   A 1 330 ? 23.865 -6.455  -12.710 1.00 64.86  ?  330 GLY   A N     1 
ATOM   2519 C CA    . GLY   A 1 330 ? 23.853 -7.663  -13.550 1.00 59.31  ?  330 GLY   A CA    1 
ATOM   2520 C C     . GLY   A 1 330 ? 24.169 -8.938  -12.803 1.00 67.13  ?  330 GLY   A C     1 
ATOM   2521 O O     . GLY   A 1 330 ? 25.106 -8.934  -11.997 1.00 72.13  ?  330 GLY   A O     1 
ATOM   2522 N N     . CYS   A 1 331 ? 23.455 -10.012 -13.111 1.00 65.70  ?  331 CYS   A N     1 
ATOM   2523 C CA    . CYS   A 1 331 ? 23.693 -11.331 -12.491 1.00 64.15  ?  331 CYS   A CA    1 
ATOM   2524 C C     . CYS   A 1 331 ? 25.037 -11.905 -12.916 1.00 68.16  ?  331 CYS   A C     1 
ATOM   2525 O O     . CYS   A 1 331 ? 25.462 -11.581 -14.021 1.00 74.69  ?  331 CYS   A O     1 
ATOM   2526 C CB    . CYS   A 1 331 ? 22.712 -12.326 -13.073 1.00 69.66  ?  331 CYS   A CB    1 
ATOM   2527 S SG    . CYS   A 1 331 ? 22.537 -12.187 -14.872 1.00 96.42  ?  331 CYS   A SG    1 
ATOM   2528 N N     . PRO   A 1 332 ? 25.676 -12.804 -12.124 1.00 67.54  ?  332 PRO   A N     1 
ATOM   2529 C CA    . PRO   A 1 332 ? 26.961 -13.422 -12.410 1.00 67.34  ?  332 PRO   A CA    1 
ATOM   2530 C C     . PRO   A 1 332 ? 27.718 -13.228 -13.687 1.00 72.92  ?  332 PRO   A C     1 
ATOM   2531 O O     . PRO   A 1 332 ? 28.333 -14.208 -14.130 1.00 76.08  ?  332 PRO   A O     1 
ATOM   2532 C CB    . PRO   A 1 332 ? 26.278 -14.806 -12.486 1.00 61.28  ?  332 PRO   A CB    1 
ATOM   2533 C CG    . PRO   A 1 332 ? 25.181 -14.807 -11.455 1.00 53.89  ?  332 PRO   A CG    1 
ATOM   2534 C CD    . PRO   A 1 332 ? 25.229 -13.419 -10.889 1.00 66.31  ?  332 PRO   A CD    1 
ATOM   2535 N N     . MET   A 1 333 ? 27.784 -12.018 -14.224 1.00 79.24  ?  333 MET   A N     1 
ATOM   2536 C CA    . MET   A 1 333 ? 28.329 -11.929 -15.600 1.00 78.76  ?  333 MET   A CA    1 
ATOM   2537 C C     . MET   A 1 333 ? 29.774 -11.461 -15.727 1.00 78.93  ?  333 MET   A C     1 
ATOM   2538 O O     . MET   A 1 333 ? 30.247 -10.699 -14.873 1.00 83.21  ?  333 MET   A O     1 
ATOM   2539 C CB    . MET   A 1 333 ? 27.418 -11.064 -16.468 1.00 83.82  ?  333 MET   A CB    1 
ATOM   2540 C CG    . MET   A 1 333 ? 26.099 -11.762 -16.703 1.00 88.72  ?  333 MET   A CG    1 
ATOM   2541 S SD    . MET   A 1 333 ? 26.146 -13.262 -17.702 1.00 94.30  ?  333 MET   A SD    1 
ATOM   2542 C CE    . MET   A 1 333 ? 25.614 -12.611 -19.290 1.00 80.41  ?  333 MET   A CE    1 
ATOM   2543 N N     . SER   A 1 334 ? 30.415 -11.933 -16.792 1.00 80.23  ?  334 SER   A N     1 
ATOM   2544 C CA    . SER   A 1 334 ? 31.811 -11.552 -17.076 1.00 80.85  ?  334 SER   A CA    1 
ATOM   2545 C C     . SER   A 1 334 ? 31.822 -10.591 -18.255 1.00 83.84  ?  334 SER   A C     1 
ATOM   2546 O O     . SER   A 1 334 ? 30.764 -10.028 -18.587 1.00 84.17  ?  334 SER   A O     1 
ATOM   2547 C CB    . SER   A 1 334 ? 32.610 -12.749 -17.447 1.00 78.96  ?  334 SER   A CB    1 
ATOM   2548 O OG    . SER   A 1 334 ? 32.183 -13.269 -18.698 1.00 80.17  ?  334 SER   A OG    1 
ATOM   2549 N N     . ALA   A 1 335 ? 32.984 -10.455 -18.871 1.00 85.20  ?  335 ALA   A N     1 
ATOM   2550 C CA    . ALA   A 1 335 ? 33.107 -9.599  -20.063 1.00 79.37  ?  335 ALA   A CA    1 
ATOM   2551 C C     . ALA   A 1 335 ? 32.318 -10.238 -21.196 1.00 77.55  ?  335 ALA   A C     1 
ATOM   2552 O O     . ALA   A 1 335 ? 31.253 -9.723  -21.564 1.00 75.75  ?  335 ALA   A O     1 
ATOM   2553 C CB    . ALA   A 1 335 ? 34.561 -9.492  -20.414 1.00 73.68  ?  335 ALA   A CB    1 
ATOM   2554 N N     . ASP   A 1 336 ? 32.826 -11.352 -21.710 1.00 78.97  ?  336 ASP   A N     1 
ATOM   2555 C CA    . ASP   A 1 336 ? 32.163 -12.053 -22.833 1.00 78.88  ?  336 ASP   A CA    1 
ATOM   2556 C C     . ASP   A 1 336 ? 30.776 -12.521 -22.404 1.00 83.66  ?  336 ASP   A C     1 
ATOM   2557 O O     . ASP   A 1 336 ? 30.043 -13.040 -23.264 1.00 77.57  ?  336 ASP   A O     1 
ATOM   2558 C CB    . ASP   A 1 336 ? 32.993 -13.242 -23.262 1.00 80.20  ?  336 ASP   A CB    1 
ATOM   2559 C CG    . ASP   A 1 336 ? 33.319 -14.233 -22.157 1.00 84.91  ?  336 ASP   A CG    1 
ATOM   2560 O OD1   . ASP   A 1 336 ? 34.020 -13.839 -21.205 1.00 82.25  ?  336 ASP   A OD1   1 
ATOM   2561 O OD2   . ASP   A 1 336 ? 32.867 -15.390 -22.263 1.00 85.30  ?  336 ASP   A OD2   1 
ATOM   2562 N N     . GLY   A 1 337 ? 30.451 -12.377 -21.119 1.00 81.13  ?  337 GLY   A N     1 
ATOM   2563 C CA    . GLY   A 1 337 ? 29.125 -12.782 -20.612 1.00 78.49  ?  337 GLY   A CA    1 
ATOM   2564 C C     . GLY   A 1 337 ? 29.112 -14.197 -20.071 1.00 76.41  ?  337 GLY   A C     1 
ATOM   2565 O O     . GLY   A 1 337 ? 28.020 -14.779 -19.965 1.00 66.88  ?  337 GLY   A O     1 
ATOM   2566 N N     . SER   A 1 338 ? 30.283 -14.737 -19.742 1.00 77.62  ?  338 SER   A N     1 
ATOM   2567 C CA    . SER   A 1 338 ? 30.332 -16.079 -19.116 1.00 78.59  ?  338 SER   A CA    1 
ATOM   2568 C C     . SER   A 1 338 ? 29.933 -15.969 -17.638 1.00 75.35  ?  338 SER   A C     1 
ATOM   2569 O O     . SER   A 1 338 ? 30.229 -14.930 -17.026 1.00 73.39  ?  338 SER   A O     1 
ATOM   2570 C CB    . SER   A 1 338 ? 31.685 -16.696 -19.291 1.00 78.00  ?  338 SER   A CB    1 
ATOM   2571 O OG    . SER   A 1 338 ? 31.826 -17.243 -20.595 1.00 83.13  ?  338 SER   A OG    1 
ATOM   2572 N N     . VAL   A 1 339 ? 29.275 -16.993 -17.101 1.00 70.07  ?  339 VAL   A N     1 
ATOM   2573 C CA    . VAL   A 1 339 ? 28.774 -16.948 -15.697 1.00 67.53  ?  339 VAL   A CA    1 
ATOM   2574 C C     . VAL   A 1 339 ? 29.940 -17.122 -14.721 1.00 67.24  ?  339 VAL   A C     1 
ATOM   2575 O O     . VAL   A 1 339 ? 30.703 -18.086 -14.878 1.00 61.30  ?  339 VAL   A O     1 
ATOM   2576 C CB    . VAL   A 1 339 ? 27.708 -18.029 -15.467 1.00 69.96  ?  339 VAL   A CB    1 
ATOM   2577 C CG1   . VAL   A 1 339 ? 27.159 -18.000 -14.049 1.00 63.46  ?  339 VAL   A CG1   1 
ATOM   2578 C CG2   . VAL   A 1 339 ? 26.583 -17.933 -16.486 1.00 70.65  ?  339 VAL   A CG2   1 
ATOM   2579 N N     . GLU   A 1 340 ? 30.037 -16.225 -13.741 1.00 66.37  ?  340 GLU   A N     1 
ATOM   2580 C CA    . GLU   A 1 340 ? 31.114 -16.316 -12.726 1.00 60.08  ?  340 GLU   A CA    1 
ATOM   2581 C C     . GLU   A 1 340 ? 30.524 -16.592 -11.337 1.00 58.73  ?  340 GLU   A C     1 
ATOM   2582 O O     . GLU   A 1 340 ? 30.269 -15.629 -10.615 1.00 57.30  ?  340 GLU   A O     1 
ATOM   2583 C CB    . GLU   A 1 340 ? 31.932 -15.034 -12.784 1.00 64.19  ?  340 GLU   A CB    1 
ATOM   2584 C CG    . GLU   A 1 340 ? 32.683 -14.848 -14.097 1.00 67.97  ?  340 GLU   A CG    1 
ATOM   2585 C CD    . GLU   A 1 340 ? 33.281 -13.460 -14.192 1.00 69.52  ?  340 GLU   A CD    1 
ATOM   2586 O OE1   . GLU   A 1 340 ? 32.546 -12.494 -13.925 1.00 71.65  ?  340 GLU   A OE1   1 
ATOM   2587 O OE2   . GLU   A 1 340 ? 34.475 -13.344 -14.523 1.00 72.75  ?  340 GLU   A OE2   1 
ATOM   2588 N N     . LEU   A 1 341 ? 30.323 -17.857 -10.993 1.00 52.23  ?  341 LEU   A N     1 
ATOM   2589 C CA    . LEU   A 1 341 ? 29.829 -18.287 -9.696  1.00 47.97  ?  341 LEU   A CA    1 
ATOM   2590 C C     . LEU   A 1 341 ? 30.788 -19.326 -9.145  1.00 46.14  ?  341 LEU   A C     1 
ATOM   2591 O O     . LEU   A 1 341 ? 30.984 -20.377 -9.763  1.00 47.87  ?  341 LEU   A O     1 
ATOM   2592 C CB    . LEU   A 1 341 ? 28.418 -18.866 -9.806  1.00 49.60  ?  341 LEU   A CB    1 
ATOM   2593 C CG    . LEU   A 1 341 ? 27.300 -17.904 -10.225 1.00 50.50  ?  341 LEU   A CG    1 
ATOM   2594 C CD1   . LEU   A 1 341 ? 26.016 -18.674 -10.494 1.00 44.18  ?  341 LEU   A CD1   1 
ATOM   2595 C CD2   . LEU   A 1 341 ? 27.084 -16.829 -9.175  1.00 45.07  ?  341 LEU   A CD2   1 
ATOM   2596 N N     . TYR   A 1 342 ? 31.386 -19.028 -7.993  1.00 46.70  ?  342 TYR   A N     1 
ATOM   2597 C CA    . TYR   A 1 342 ? 32.272 -19.973 -7.320  1.00 48.51  ?  342 TYR   A CA    1 
ATOM   2598 C C     . TYR   A 1 342 ? 31.551 -21.293 -7.081  1.00 46.62  ?  342 TYR   A C     1 
ATOM   2599 O O     . TYR   A 1 342 ? 30.527 -21.332 -6.399  1.00 44.08  ?  342 TYR   A O     1 
ATOM   2600 C CB    . TYR   A 1 342 ? 32.771 -19.378 -5.995  1.00 46.62  ?  342 TYR   A CB    1 
ATOM   2601 C CG    . TYR   A 1 342 ? 33.451 -20.389 -5.106  1.00 46.53  ?  342 TYR   A CG    1 
ATOM   2602 C CD1   . TYR   A 1 342 ? 34.630 -21.000 -5.497  1.00 44.11  ?  342 TYR   A CD1   1 
ATOM   2603 C CD2   . TYR   A 1 342 ? 32.895 -20.758 -3.882  1.00 51.12  ?  342 TYR   A CD2   1 
ATOM   2604 C CE1   . TYR   A 1 342 ? 35.246 -21.946 -4.701  1.00 45.59  ?  342 TYR   A CE1   1 
ATOM   2605 C CE2   . TYR   A 1 342 ? 33.514 -21.702 -3.067  1.00 47.25  ?  342 TYR   A CE2   1 
ATOM   2606 C CZ    . TYR   A 1 342 ? 34.687 -22.288 -3.489  1.00 46.93  ?  342 TYR   A CZ    1 
ATOM   2607 O OH    . TYR   A 1 342 ? 35.304 -23.224 -2.712  1.00 45.10  ?  342 TYR   A OH    1 
ATOM   2608 N N     . ARG   A 1 343 ? 32.031 -22.387 -7.667  1.00 48.13  ?  343 ARG   A N     1 
ATOM   2609 C CA    . ARG   A 1 343 ? 31.350 -23.710 -7.576  1.00 42.11  ?  343 ARG   A CA    1 
ATOM   2610 C C     . ARG   A 1 343 ? 29.955 -23.585 -8.199  1.00 45.95  ?  343 ARG   A C     1 
ATOM   2611 O O     . ARG   A 1 343 ? 29.073 -24.356 -7.807  1.00 45.17  ?  343 ARG   A O     1 
ATOM   2612 C CB    . ARG   A 1 343 ? 31.366 -24.288 -6.160  1.00 48.55  ?  343 ARG   A CB    1 
ATOM   2613 C CG    . ARG   A 1 343 ? 32.754 -24.640 -5.652  1.00 53.29  ?  343 ARG   A CG    1 
ATOM   2614 C CD    . ARG   A 1 343 ? 32.714 -25.066 -4.198  1.00 53.31  ?  343 ARG   A CD    1 
ATOM   2615 N NE    . ARG   A 1 343 ? 32.855 -26.515 -4.031  1.00 48.95  ?  343 ARG   A NE    1 
ATOM   2616 C CZ    . ARG   A 1 343 ? 32.099 -27.237 -3.223  1.00 53.00  ?  343 ARG   A CZ    1 
ATOM   2617 N NH1   . ARG   A 1 343 ? 31.227 -26.646 -2.433  1.00 56.69  ?  343 ARG   A NH1   1 
ATOM   2618 N NH2   . ARG   A 1 343 ? 32.218 -28.548 -3.207  1.00 54.05  ?  343 ARG   A NH2   1 
ATOM   2619 N N     . ARG   A 1 344 ? 29.782 -22.649 -9.131  1.00 47.73  ?  344 ARG   A N     1 
ATOM   2620 C CA    . ARG   A 1 344 ? 28.520 -22.485 -9.899  1.00 44.80  ?  344 ARG   A CA    1 
ATOM   2621 C C     . ARG   A 1 344 ? 27.354 -22.086 -8.983  1.00 47.65  ?  344 ARG   A C     1 
ATOM   2622 O O     . ARG   A 1 344 ? 26.201 -22.290 -9.384  1.00 43.09  ?  344 ARG   A O     1 
ATOM   2623 C CB    . ARG   A 1 344 ? 28.265 -23.750 -10.730 1.00 48.77  ?  344 ARG   A CB    1 
ATOM   2624 C CG    . ARG   A 1 344 ? 29.437 -24.578 -11.236 1.00 49.09  ?  344 ARG   A CG    1 
ATOM   2625 C CD    . ARG   A 1 344 ? 30.199 -23.947 -12.383 1.00 45.60  ?  344 ARG   A CD    1 
ATOM   2626 N NE    . ARG   A 1 344 ? 31.179 -22.947 -11.950 1.00 45.37  ?  344 ARG   A NE    1 
ATOM   2627 C CZ    . ARG   A 1 344 ? 32.311 -23.204 -11.316 1.00 46.22  ?  344 ARG   A CZ    1 
ATOM   2628 N NH1   . ARG   A 1 344 ? 32.680 -24.448 -11.087 1.00 48.77  ?  344 ARG   A NH1   1 
ATOM   2629 N NH2   . ARG   A 1 344 ? 33.077 -22.209 -10.921 1.00 50.56  ?  344 ARG   A NH2   1 
ATOM   2630 N N     . VAL   A 1 345 ? 27.655 -21.511 -7.818  1.00 51.02  ?  345 VAL   A N     1 
ATOM   2631 C CA    . VAL   A 1 345 ? 26.607 -21.108 -6.871  1.00 44.64  ?  345 VAL   A CA    1 
ATOM   2632 C C     . VAL   A 1 345 ? 26.813 -19.705 -6.291  1.00 46.61  ?  345 VAL   A C     1 
ATOM   2633 O O     . VAL   A 1 345 ? 25.848 -18.939 -6.179  1.00 46.88  ?  345 VAL   A O     1 
ATOM   2634 C CB    . VAL   A 1 345 ? 26.448 -22.117 -5.716  1.00 42.94  ?  345 VAL   A CB    1 
ATOM   2635 C CG1   . VAL   A 1 345 ? 25.498 -21.543 -4.657  1.00 40.50  ?  345 VAL   A CG1   1 
ATOM   2636 C CG2   . VAL   A 1 345 ? 25.902 -23.458 -6.211  1.00 41.30  ?  345 VAL   A CG2   1 
ATOM   2637 N N     . VAL   A 1 346 ? 28.032 -19.343 -5.914  1.00 44.21  ?  346 VAL   A N     1 
ATOM   2638 C CA    . VAL   A 1 346 ? 28.260 -18.205 -5.018  1.00 45.68  ?  346 VAL   A CA    1 
ATOM   2639 C C     . VAL   A 1 346 ? 28.965 -17.077 -5.753  1.00 44.14  ?  346 VAL   A C     1 
ATOM   2640 O O     . VAL   A 1 346 ? 30.029 -17.299 -6.337  1.00 52.14  ?  346 VAL   A O     1 
ATOM   2641 C CB    . VAL   A 1 346 ? 29.063 -18.604 -3.767  1.00 44.83  ?  346 VAL   A CB    1 
ATOM   2642 C CG1   . VAL   A 1 346 ? 28.822 -17.579 -2.689  1.00 40.35  ?  346 VAL   A CG1   1 
ATOM   2643 C CG2   . VAL   A 1 346 ? 28.658 -20.003 -3.278  1.00 49.66  ?  346 VAL   A CG2   1 
ATOM   2644 N N     . PRO   A 1 347 ? 28.450 -15.855 -5.698  1.00 43.16  ?  347 PRO   A N     1 
ATOM   2645 C CA    . PRO   A 1 347 ? 29.212 -14.698 -6.181  1.00 50.56  ?  347 PRO   A CA    1 
ATOM   2646 C C     . PRO   A 1 347 ? 30.399 -14.389 -5.284  1.00 52.58  ?  347 PRO   A C     1 
ATOM   2647 O O     . PRO   A 1 347 ? 30.413 -14.711 -4.099  1.00 56.30  ?  347 PRO   A O     1 
ATOM   2648 C CB    . PRO   A 1 347 ? 28.185 -13.561 -6.137  1.00 56.35  ?  347 PRO   A CB    1 
ATOM   2649 C CG    . PRO   A 1 347 ? 27.170 -14.004 -5.138  1.00 49.73  ?  347 PRO   A CG    1 
ATOM   2650 C CD    . PRO   A 1 347 ? 27.078 -15.489 -5.316  1.00 45.26  ?  347 PRO   A CD    1 
ATOM   2651 N N     . ALA   A 1 348 ? 31.406 -13.727 -5.852  1.00 56.72  ?  348 ALA   A N     1 
ATOM   2652 C CA    . ALA   A 1 348 ? 32.611 -13.477 -5.069  1.00 55.20  ?  348 ALA   A CA    1 
ATOM   2653 C C     . ALA   A 1 348 ? 32.604 -12.146 -4.345  1.00 59.64  ?  348 ALA   A C     1 
ATOM   2654 O O     . ALA   A 1 348 ? 33.350 -11.984 -3.373  1.00 66.74  ?  348 ALA   A O     1 
ATOM   2655 C CB    . ALA   A 1 348 ? 33.859 -13.536 -5.942  1.00 54.32  ?  348 ALA   A CB    1 
ATOM   2656 N N     . ASP   A 1 349 ? 31.782 -11.202 -4.778  1.00 61.83  ?  349 ASP   A N     1 
ATOM   2657 C CA    . ASP   A 1 349 ? 31.821 -9.838  -4.275  1.00 62.55  ?  349 ASP   A CA    1 
ATOM   2658 C C     . ASP   A 1 349 ? 30.539 -9.451  -3.557  1.00 58.32  ?  349 ASP   A C     1 
ATOM   2659 O O     . ASP   A 1 349 ? 30.355 -8.281  -3.230  1.00 65.05  ?  349 ASP   A O     1 
ATOM   2660 C CB    . ASP   A 1 349 ? 32.070 -8.875  -5.437  1.00 71.03  ?  349 ASP   A CB    1 
ATOM   2661 C CG    . ASP   A 1 349 ? 31.085 -9.097  -6.603  1.00 77.39  ?  349 ASP   A CG    1 
ATOM   2662 O OD1   . ASP   A 1 349 ? 30.495 -10.205 -6.693  1.00 74.17  ?  349 ASP   A OD1   1 
ATOM   2663 O OD2   . ASP   A 1 349 ? 30.885 -8.160  -7.416  1.00 80.38  ?  349 ASP   A OD2   1 
ATOM   2664 N N     . ARG   A 1 350 ? 29.629 -10.391 -3.344  1.00 57.79  ?  350 ARG   A N     1 
ATOM   2665 C CA    . ARG   A 1 350 ? 28.282 -10.088 -2.864  1.00 60.94  ?  350 ARG   A CA    1 
ATOM   2666 C C     . ARG   A 1 350 ? 27.966 -11.073 -1.744  1.00 56.76  ?  350 ARG   A C     1 
ATOM   2667 O O     . ARG   A 1 350 ? 27.371 -12.134 -1.980  1.00 53.85  ?  350 ARG   A O     1 
ATOM   2668 C CB    . ARG   A 1 350 ? 27.239 -10.177 -3.993  1.00 68.71  ?  350 ARG   A CB    1 
ATOM   2669 C CG    . ARG   A 1 350 ? 27.448 -9.300  -5.275  1.00 68.86  ?  350 ARG   A CG    1 
ATOM   2670 C CD    . ARG   A 1 350 ? 27.024 -10.070 -6.568  1.00 75.20  ?  350 ARG   A CD    1 
ATOM   2671 N NE    . ARG   A 1 350 ? 26.396 -9.240  -7.616  1.00 76.73  ?  350 ARG   A NE    1 
ATOM   2672 C CZ    . ARG   A 1 350 ? 25.835 -9.701  -8.743  1.00 64.04  ?  350 ARG   A CZ    1 
ATOM   2673 N NH1   . ARG   A 1 350 ? 25.802 -11.003 -9.014  1.00 62.53  ?  350 ARG   A NH1   1 
ATOM   2674 N NH2   . ARG   A 1 350 ? 25.293 -8.847  -9.608  1.00 61.74  ?  350 ARG   A NH2   1 
ATOM   2675 N N     . PRO   A 1 351 ? 28.372 -10.768 -0.512  1.00 60.85  ?  351 PRO   A N     1 
ATOM   2676 C CA    . PRO   A 1 351 ? 28.028 -11.649 0.621   1.00 59.17  ?  351 PRO   A CA    1 
ATOM   2677 C C     . PRO   A 1 351 ? 26.523 -11.706 0.844   1.00 54.89  ?  351 PRO   A C     1 
ATOM   2678 O O     . PRO   A 1 351 ? 25.837 -10.679 0.863   1.00 55.61  ?  351 PRO   A O     1 
ATOM   2679 C CB    . PRO   A 1 351 ? 28.747 -11.005 1.815   1.00 48.41  ?  351 PRO   A CB    1 
ATOM   2680 C CG    . PRO   A 1 351 ? 29.053 -9.595  1.383   1.00 55.83  ?  351 PRO   A CG    1 
ATOM   2681 C CD    . PRO   A 1 351 ? 29.234 -9.641  -0.112  1.00 61.19  ?  351 PRO   A CD    1 
ATOM   2682 N N     . GLY   A 1 352 ? 26.013 -12.916 1.020   1.00 50.93  ?  352 GLY   A N     1 
ATOM   2683 C CA    . GLY   A 1 352 ? 24.622 -13.086 1.366   1.00 50.63  ?  352 GLY   A CA    1 
ATOM   2684 C C     . GLY   A 1 352 ? 23.714 -13.511 0.240   1.00 52.22  ?  352 GLY   A C     1 
ATOM   2685 O O     . GLY   A 1 352 ? 22.515 -13.682 0.488   1.00 50.07  ?  352 GLY   A O     1 
ATOM   2686 N N     . LEU   A 1 353 ? 24.251 -13.704 -0.981  1.00 48.65  ?  353 LEU   A N     1 
ATOM   2687 C CA    . LEU   A 1 353 ? 23.494 -14.092 -2.171  1.00 47.15  ?  353 LEU   A CA    1 
ATOM   2688 C C     . LEU   A 1 353 ? 23.918 -15.472 -2.669  1.00 46.56  ?  353 LEU   A C     1 
ATOM   2689 O O     . LEU   A 1 353 ? 25.094 -15.835 -2.603  1.00 48.79  ?  353 LEU   A O     1 
ATOM   2690 C CB    . LEU   A 1 353 ? 23.678 -13.070 -3.299  1.00 47.28  ?  353 LEU   A CB    1 
ATOM   2691 C CG    . LEU   A 1 353 ? 22.943 -13.347 -4.618  1.00 48.52  ?  353 LEU   A CG    1 
ATOM   2692 C CD1   . LEU   A 1 353 ? 21.442 -13.457 -4.378  1.00 48.23  ?  353 LEU   A CD1   1 
ATOM   2693 C CD2   . LEU   A 1 353 ? 23.235 -12.296 -5.690  1.00 45.26  ?  353 LEU   A CD2   1 
ATOM   2694 N N     . TYR   A 1 354 ? 22.952 -16.245 -3.160  1.00 46.92  ?  354 TYR   A N     1 
ATOM   2695 C CA    . TYR   A 1 354 ? 23.187 -17.604 -3.630  1.00 44.05  ?  354 TYR   A CA    1 
ATOM   2696 C C     . TYR   A 1 354 ? 22.259 -17.901 -4.799  1.00 46.38  ?  354 TYR   A C     1 
ATOM   2697 O O     . TYR   A 1 354 ? 21.103 -17.455 -4.818  1.00 45.15  ?  354 TYR   A O     1 
ATOM   2698 C CB    . TYR   A 1 354 ? 22.951 -18.654 -2.521  1.00 47.92  ?  354 TYR   A CB    1 
ATOM   2699 C CG    . TYR   A 1 354 ? 23.660 -18.356 -1.218  1.00 51.44  ?  354 TYR   A CG    1 
ATOM   2700 C CD1   . TYR   A 1 354 ? 23.091 -17.513 -0.261  1.00 51.10  ?  354 TYR   A CD1   1 
ATOM   2701 C CD2   . TYR   A 1 354 ? 24.896 -18.910 -0.938  1.00 51.20  ?  354 TYR   A CD2   1 
ATOM   2702 C CE1   . TYR   A 1 354 ? 23.734 -17.231 0.915   1.00 47.89  ?  354 TYR   A CE1   1 
ATOM   2703 C CE2   . TYR   A 1 354 ? 25.547 -18.628 0.240   1.00 44.60  ?  354 TYR   A CE2   1 
ATOM   2704 C CZ    . TYR   A 1 354 ? 24.959 -17.795 1.164   1.00 50.17  ?  354 TYR   A CZ    1 
ATOM   2705 O OH    . TYR   A 1 354 ? 25.606 -17.523 2.346   1.00 52.94  ?  354 TYR   A OH    1 
ATOM   2706 N N     . PHE   A 1 355 ? 22.776 -18.667 -5.770  1.00 45.24  ?  355 PHE   A N     1 
ATOM   2707 C CA    . PHE   A 1 355 ? 22.008 -19.172 -6.906  1.00 40.57  ?  355 PHE   A CA    1 
ATOM   2708 C C     . PHE   A 1 355 ? 21.976 -20.693 -6.880  1.00 38.55  ?  355 PHE   A C     1 
ATOM   2709 O O     . PHE   A 1 355 ? 23.029 -21.333 -6.843  1.00 41.18  ?  355 PHE   A O     1 
ATOM   2710 C CB    . PHE   A 1 355 ? 22.611 -18.720 -8.221  1.00 40.08  ?  355 PHE   A CB    1 
ATOM   2711 C CG    . PHE   A 1 355 ? 22.753 -17.250 -8.350  1.00 42.90  ?  355 PHE   A CG    1 
ATOM   2712 C CD1   . PHE   A 1 355 ? 23.854 -16.602 -7.821  1.00 45.14  ?  355 PHE   A CD1   1 
ATOM   2713 C CD2   . PHE   A 1 355 ? 21.806 -16.512 -9.044  1.00 44.76  ?  355 PHE   A CD2   1 
ATOM   2714 C CE1   . PHE   A 1 355 ? 24.001 -15.239 -7.963  1.00 49.54  ?  355 PHE   A CE1   1 
ATOM   2715 C CE2   . PHE   A 1 355 ? 21.939 -15.141 -9.198  1.00 42.65  ?  355 PHE   A CE2   1 
ATOM   2716 C CZ    . PHE   A 1 355 ? 23.036 -14.501 -8.656  1.00 48.16  ?  355 PHE   A CZ    1 
ATOM   2717 N N     . VAL   A 1 356 ? 20.780 -21.267 -6.936  1.00 37.93  ?  356 VAL   A N     1 
ATOM   2718 C CA    . VAL   A 1 356 ? 20.584 -22.718 -6.927  1.00 42.94  ?  356 VAL   A CA    1 
ATOM   2719 C C     . VAL   A 1 356 ? 19.892 -23.134 -8.224  1.00 44.94  ?  356 VAL   A C     1 
ATOM   2720 O O     . VAL   A 1 356 ? 18.877 -22.537 -8.609  1.00 44.45  ?  356 VAL   A O     1 
ATOM   2721 C CB    . VAL   A 1 356 ? 19.750 -23.169 -5.709  1.00 42.20  ?  356 VAL   A CB    1 
ATOM   2722 C CG1   . VAL   A 1 356 ? 19.305 -24.624 -5.861  1.00 43.65  ?  356 VAL   A CG1   1 
ATOM   2723 C CG2   . VAL   A 1 356 ? 20.530 -22.971 -4.431  1.00 37.06  ?  356 VAL   A CG2   1 
ATOM   2724 N N     . GLY   A 1 357 ? 20.433 -24.166 -8.889  1.00 48.64  ?  357 GLY   A N     1 
ATOM   2725 C CA    . GLY   A 1 357 ? 19.825 -24.745 -10.092 1.00 44.25  ?  357 GLY   A CA    1 
ATOM   2726 C C     . GLY   A 1 357 ? 20.289 -24.165 -11.420 1.00 45.35  ?  357 GLY   A C     1 
ATOM   2727 O O     . GLY   A 1 357 ? 19.780 -24.577 -12.478 1.00 43.00  ?  357 GLY   A O     1 
ATOM   2728 N N     . LEU   A 1 358 ? 21.217 -23.215 -11.387 1.00 41.39  ?  358 LEU   A N     1 
ATOM   2729 C CA    . LEU   A 1 358 ? 21.825 -22.623 -12.567 1.00 40.10  ?  358 LEU   A CA    1 
ATOM   2730 C C     . LEU   A 1 358 ? 23.020 -23.468 -13.012 1.00 41.59  ?  358 LEU   A C     1 
ATOM   2731 O O     . LEU   A 1 358 ? 24.167 -23.029 -13.095 1.00 37.32  ?  358 LEU   A O     1 
ATOM   2732 C CB    . LEU   A 1 358 ? 22.222 -21.192 -12.257 1.00 35.77  ?  358 LEU   A CB    1 
ATOM   2733 C CG    . LEU   A 1 358 ? 22.725 -20.311 -13.386 1.00 40.00  ?  358 LEU   A CG    1 
ATOM   2734 C CD1   . LEU   A 1 358 ? 21.850 -20.528 -14.594 1.00 51.13  ?  358 LEU   A CD1   1 
ATOM   2735 C CD2   . LEU   A 1 358 ? 22.693 -18.859 -12.959 1.00 39.18  ?  358 LEU   A CD2   1 
ATOM   2736 N N     . VAL   A 1 359 ? 22.716 -24.730 -13.261 1.00 41.66  ?  359 VAL   A N     1 
ATOM   2737 C CA    . VAL   A 1 359 ? 23.686 -25.712 -13.724 1.00 49.31  ?  359 VAL   A CA    1 
ATOM   2738 C C     . VAL   A 1 359 ? 23.005 -26.598 -14.768 1.00 58.90  ?  359 VAL   A C     1 
ATOM   2739 O O     . VAL   A 1 359 ? 21.837 -26.968 -14.599 1.00 58.72  ?  359 VAL   A O     1 
ATOM   2740 C CB    . VAL   A 1 359 ? 24.226 -26.550 -12.550 1.00 45.59  ?  359 VAL   A CB    1 
ATOM   2741 C CG1   . VAL   A 1 359 ? 25.250 -25.755 -11.780 1.00 46.48  ?  359 VAL   A CG1   1 
ATOM   2742 C CG2   . VAL   A 1 359 ? 23.077 -26.978 -11.642 1.00 42.51  ?  359 VAL   A CG2   1 
ATOM   2743 N N     . ARG   A 1 360 ? 23.717 -26.926 -15.867 1.00 55.92  ?  360 ARG   A N     1 
ATOM   2744 C CA    . ARG   A 1 360 ? 23.178 -27.890 -16.835 1.00 65.01  ?  360 ARG   A CA    1 
ATOM   2745 C C     . ARG   A 1 360 ? 23.987 -29.180 -16.797 1.00 62.58  ?  360 ARG   A C     1 
ATOM   2746 O O     . ARG   A 1 360 ? 25.152 -29.192 -17.224 1.00 66.39  ?  360 ARG   A O     1 
ATOM   2747 C CB    . ARG   A 1 360 ? 23.140 -27.339 -18.269 1.00 69.42  ?  360 ARG   A CB    1 
ATOM   2748 C CG    . ARG   A 1 360 ? 22.707 -28.425 -19.306 1.00 74.47  ?  360 ARG   A CG    1 
ATOM   2749 C CD    . ARG   A 1 360 ? 22.637 -27.951 -20.769 1.00 77.93  ?  360 ARG   A CD    1 
ATOM   2750 N NE    . ARG   A 1 360 ? 21.757 -26.799 -20.942 1.00 80.43  ?  360 ARG   A NE    1 
ATOM   2751 C CZ    . ARG   A 1 360 ? 22.183 -25.538 -21.043 1.00 86.64  ?  360 ARG   A CZ    1 
ATOM   2752 N NH1   . ARG   A 1 360 ? 21.308 -24.549 -21.188 1.00 86.62  ?  360 ARG   A NH1   1 
ATOM   2753 N NH2   . ARG   A 1 360 ? 23.487 -25.256 -20.998 1.00 84.06  ?  360 ARG   A NH2   1 
ATOM   2754 N N     . PRO   A 1 361 ? 23.444 -30.267 -16.295 1.00 66.25  ?  361 PRO   A N     1 
ATOM   2755 C CA    . PRO   A 1 361 ? 24.218 -31.507 -16.267 1.00 66.33  ?  361 PRO   A CA    1 
ATOM   2756 C C     . PRO   A 1 361 ? 23.706 -32.486 -17.296 1.00 63.92  ?  361 PRO   A C     1 
ATOM   2757 O O     . PRO   A 1 361 ? 22.647 -32.286 -17.901 1.00 63.68  ?  361 PRO   A O     1 
ATOM   2758 C CB    . PRO   A 1 361 ? 24.003 -32.015 -14.833 1.00 67.43  ?  361 PRO   A CB    1 
ATOM   2759 C CG    . PRO   A 1 361 ? 22.606 -31.504 -14.465 1.00 62.66  ?  361 PRO   A CG    1 
ATOM   2760 C CD    . PRO   A 1 361 ? 22.264 -30.348 -15.411 1.00 65.59  ?  361 PRO   A CD    1 
ATOM   2761 N N     . VAL   A 1 362 ? 24.454 -33.557 -17.509 1.00 58.63  ?  362 VAL   A N     1 
ATOM   2762 C CA    . VAL   A 1 362 ? 23.980 -34.601 -18.396 1.00 67.95  ?  362 VAL   A CA    1 
ATOM   2763 C C     . VAL   A 1 362 ? 23.064 -35.494 -17.570 1.00 69.95  ?  362 VAL   A C     1 
ATOM   2764 O O     . VAL   A 1 362 ? 23.519 -36.256 -16.716 1.00 67.68  ?  362 VAL   A O     1 
ATOM   2765 C CB    . VAL   A 1 362 ? 25.137 -35.382 -19.020 1.00 71.03  ?  362 VAL   A CB    1 
ATOM   2766 C CG1   . VAL   A 1 362 ? 26.170 -35.755 -17.957 1.00 71.76  ?  362 VAL   A CG1   1 
ATOM   2767 C CG2   . VAL   A 1 362 ? 24.609 -36.590 -19.776 1.00 69.90  ?  362 VAL   A CG2   1 
ATOM   2768 N N     . GLY   A 1 363 ? 21.767 -35.361 -17.782 1.00 69.15  ?  363 GLY   A N     1 
ATOM   2769 C CA    . GLY   A 1 363 ? 20.793 -36.111 -17.028 1.00 62.71  ?  363 GLY   A CA    1 
ATOM   2770 C C     . GLY   A 1 363 ? 20.070 -35.260 -16.008 1.00 53.67  ?  363 GLY   A C     1 
ATOM   2771 O O     . GLY   A 1 363 ? 19.969 -34.036 -16.127 1.00 49.71  ?  363 GLY   A O     1 
ATOM   2772 N N     . ALA   A 1 364 ? 19.567 -35.935 -14.977 1.00 54.76  ?  364 ALA   A N     1 
ATOM   2773 C CA    . ALA   A 1 364 ? 18.726 -35.276 -13.987 1.00 50.97  ?  364 ALA   A CA    1 
ATOM   2774 C C     . ALA   A 1 364 ? 19.495 -34.203 -13.227 1.00 49.07  ?  364 ALA   A C     1 
ATOM   2775 O O     . ALA   A 1 364 ? 20.689 -34.345 -12.948 1.00 51.78  ?  364 ALA   A O     1 
ATOM   2776 C CB    . ALA   A 1 364 ? 18.156 -36.304 -13.017 1.00 47.78  ?  364 ALA   A CB    1 
ATOM   2777 N N     . ILE   A 1 365 ? 18.793 -33.110 -12.907 1.00 50.08  ?  365 ILE   A N     1 
ATOM   2778 C CA    . ILE   A 1 365 ? 19.377 -32.001 -12.155 1.00 50.33  ?  365 ILE   A CA    1 
ATOM   2779 C C     . ILE   A 1 365 ? 19.230 -32.177 -10.650 1.00 39.78  ?  365 ILE   A C     1 
ATOM   2780 O O     . ILE   A 1 365 ? 19.866 -31.443 -9.895  1.00 40.66  ?  365 ILE   A O     1 
ATOM   2781 C CB    . ILE   A 1 365 ? 18.731 -30.656 -12.562 1.00 47.59  ?  365 ILE   A CB    1 
ATOM   2782 C CG1   . ILE   A 1 365 ? 19.684 -29.479 -12.324 1.00 41.57  ?  365 ILE   A CG1   1 
ATOM   2783 C CG2   . ILE   A 1 365 ? 17.426 -30.426 -11.798 1.00 41.59  ?  365 ILE   A CG2   1 
ATOM   2784 C CD1   . ILE   A 1 365 ? 19.019 -28.096 -12.501 1.00 38.70  ?  365 ILE   A CD1   1 
ATOM   2785 N N     . THR   A 1 366 ? 18.442 -33.148 -10.200 1.00 41.44  ?  366 THR   A N     1 
ATOM   2786 C CA    . THR   A 1 366 ? 17.921 -33.154 -8.831  1.00 46.57  ?  366 THR   A CA    1 
ATOM   2787 C C     . THR   A 1 366 ? 19.020 -33.324 -7.781  1.00 45.47  ?  366 THR   A C     1 
ATOM   2788 O O     . THR   A 1 366 ? 19.258 -32.425 -6.966  1.00 48.70  ?  366 THR   A O     1 
ATOM   2789 C CB    . THR   A 1 366 ? 16.880 -34.257 -8.681  1.00 45.72  ?  366 THR   A CB    1 
ATOM   2790 O OG1   . THR   A 1 366 ? 15.883 -34.111 -9.699  1.00 45.13  ?  366 THR   A OG1   1 
ATOM   2791 C CG2   . THR   A 1 366 ? 16.234 -34.180 -7.318  1.00 41.14  ?  366 THR   A CG2   1 
ATOM   2792 N N     . ARG   A 1 367 ? 19.687 -34.481 -7.765  1.00 42.26  ?  367 ARG   A N     1 
ATOM   2793 C CA    . ARG   A 1 367 ? 20.810 -34.664 -6.852  1.00 44.70  ?  367 ARG   A CA    1 
ATOM   2794 C C     . ARG   A 1 367 ? 21.821 -33.522 -6.905  1.00 49.82  ?  367 ARG   A C     1 
ATOM   2795 O O     . ARG   A 1 367 ? 22.589 -33.350 -5.952  1.00 54.87  ?  367 ARG   A O     1 
ATOM   2796 C CB    . ARG   A 1 367 ? 21.504 -35.987 -7.148  1.00 42.29  ?  367 ARG   A CB    1 
ATOM   2797 C CG    . ARG   A 1 367 ? 20.524 -37.092 -7.432  1.00 44.64  ?  367 ARG   A CG    1 
ATOM   2798 C CD    . ARG   A 1 367 ? 20.157 -37.862 -6.184  1.00 45.67  ?  367 ARG   A CD    1 
ATOM   2799 N NE    . ARG   A 1 367 ? 19.085 -38.821 -6.431  1.00 47.58  ?  367 ARG   A NE    1 
ATOM   2800 C CZ    . ARG   A 1 367 ? 17.795 -38.563 -6.238  1.00 48.38  ?  367 ARG   A CZ    1 
ATOM   2801 N NH1   . ARG   A 1 367 ? 17.411 -37.369 -5.792  1.00 41.51  ?  367 ARG   A NH1   1 
ATOM   2802 N NH2   . ARG   A 1 367 ? 16.889 -39.502 -6.491  1.00 46.94  ?  367 ARG   A NH2   1 
ATOM   2803 N N     . LEU   A 1 368 ? 21.839 -32.724 -7.977  1.00 46.37  ?  368 LEU   A N     1 
ATOM   2804 C CA    . LEU   A 1 368 ? 22.745 -31.583 -8.005  1.00 47.88  ?  368 LEU   A CA    1 
ATOM   2805 C C     . LEU   A 1 368 ? 22.212 -30.418 -7.187  1.00 47.15  ?  368 LEU   A C     1 
ATOM   2806 O O     . LEU   A 1 368 ? 22.973 -29.764 -6.464  1.00 48.41  ?  368 LEU   A O     1 
ATOM   2807 C CB    . LEU   A 1 368 ? 22.982 -31.121 -9.435  1.00 49.28  ?  368 LEU   A CB    1 
ATOM   2808 C CG    . LEU   A 1 368 ? 24.052 -31.878 -10.195 1.00 55.58  ?  368 LEU   A CG    1 
ATOM   2809 C CD1   . LEU   A 1 368 ? 23.380 -32.939 -11.025 1.00 54.65  ?  368 LEU   A CD1   1 
ATOM   2810 C CD2   . LEU   A 1 368 ? 24.781 -30.882 -11.051 1.00 61.02  ?  368 LEU   A CD2   1 
ATOM   2811 N N     . VAL   A 1 369 ? 20.919 -30.118 -7.312  1.00 43.80  ?  369 VAL   A N     1 
ATOM   2812 C CA    . VAL   A 1 369 ? 20.372 -29.039 -6.503  1.00 45.54  ?  369 VAL   A CA    1 
ATOM   2813 C C     . VAL   A 1 369 ? 20.315 -29.468 -5.039  1.00 47.00  ?  369 VAL   A C     1 
ATOM   2814 O O     . VAL   A 1 369 ? 20.462 -28.629 -4.143  1.00 43.73  ?  369 VAL   A O     1 
ATOM   2815 C CB    . VAL   A 1 369 ? 18.991 -28.583 -7.031  1.00 46.50  ?  369 VAL   A CB    1 
ATOM   2816 C CG1   . VAL   A 1 369 ? 19.062 -28.229 -8.508  1.00 47.17  ?  369 VAL   A CG1   1 
ATOM   2817 C CG2   . VAL   A 1 369 ? 17.922 -29.653 -6.820  1.00 41.57  ?  369 VAL   A CG2   1 
ATOM   2818 N N     . GLU   A 1 370 ? 20.122 -30.771 -4.775  1.00 44.74  ?  370 GLU   A N     1 
ATOM   2819 C CA    . GLU   A 1 370 ? 20.052 -31.245 -3.400  1.00 41.57  ?  370 GLU   A CA    1 
ATOM   2820 C C     . GLU   A 1 370 ? 21.352 -30.938 -2.673  1.00 46.65  ?  370 GLU   A C     1 
ATOM   2821 O O     . GLU   A 1 370 ? 21.339 -30.400 -1.560  1.00 50.38  ?  370 GLU   A O     1 
ATOM   2822 C CB    . GLU   A 1 370 ? 19.735 -32.744 -3.351  1.00 40.50  ?  370 GLU   A CB    1 
ATOM   2823 C CG    . GLU   A 1 370 ? 18.231 -33.079 -3.357  1.00 40.22  ?  370 GLU   A CG    1 
ATOM   2824 C CD    . GLU   A 1 370 ? 17.920 -34.577 -3.611  1.00 46.88  ?  370 GLU   A CD    1 
ATOM   2825 O OE1   . GLU   A 1 370 ? 16.760 -35.015 -3.400  1.00 44.76  ?  370 GLU   A OE1   1 
ATOM   2826 O OE2   . GLU   A 1 370 ? 18.836 -35.324 -4.021  1.00 47.33  ?  370 GLU   A OE2   1 
ATOM   2827 N N     . ALA   A 1 371 ? 22.491 -31.232 -3.305  1.00 45.73  ?  371 ALA   A N     1 
ATOM   2828 C CA    . ALA   A 1 371 ? 23.775 -30.881 -2.703  1.00 46.03  ?  371 ALA   A CA    1 
ATOM   2829 C C     . ALA   A 1 371 ? 23.926 -29.369 -2.561  1.00 48.58  ?  371 ALA   A C     1 
ATOM   2830 O O     . ALA   A 1 371 ? 24.377 -28.877 -1.519  1.00 50.21  ?  371 ALA   A O     1 
ATOM   2831 C CB    . ALA   A 1 371 ? 24.920 -31.459 -3.522  1.00 46.28  ?  371 ALA   A CB    1 
ATOM   2832 N N     . GLN   A 1 372 ? 23.547 -28.617 -3.599  1.00 41.45  ?  372 GLN   A N     1 
ATOM   2833 C CA    . GLN   A 1 372 ? 23.662 -27.161 -3.555  1.00 43.62  ?  372 GLN   A CA    1 
ATOM   2834 C C     . GLN   A 1 372 ? 22.871 -26.598 -2.386  1.00 44.68  ?  372 GLN   A C     1 
ATOM   2835 O O     . GLN   A 1 372 ? 23.321 -25.675 -1.696  1.00 42.28  ?  372 GLN   A O     1 
ATOM   2836 C CB    . GLN   A 1 372 ? 23.161 -26.536 -4.874  1.00 41.09  ?  372 GLN   A CB    1 
ATOM   2837 C CG    . GLN   A 1 372 ? 24.009 -26.809 -6.125  1.00 43.14  ?  372 GLN   A CG    1 
ATOM   2838 C CD    . GLN   A 1 372 ? 23.509 -26.063 -7.378  1.00 48.73  ?  372 GLN   A CD    1 
ATOM   2839 O OE1   . GLN   A 1 372 ? 22.314 -25.798 -7.531  1.00 46.23  ?  372 GLN   A OE1   1 
ATOM   2840 N NE2   . GLN   A 1 372 ? 24.438 -25.700 -8.264  1.00 45.27  ?  372 GLN   A NE2   1 
ATOM   2841 N N     . ALA   A 1 373 ? 21.683 -27.148 -2.158  1.00 42.90  ?  373 ALA   A N     1 
ATOM   2842 C CA    . ALA   A 1 373 ? 20.819 -26.671 -1.092  1.00 42.46  ?  373 ALA   A CA    1 
ATOM   2843 C C     . ALA   A 1 373 ? 21.404 -27.019 0.273   1.00 47.82  ?  373 ALA   A C     1 
ATOM   2844 O O     . ALA   A 1 373 ? 21.453 -26.176 1.176   1.00 45.67  ?  373 ALA   A O     1 
ATOM   2845 C CB    . ALA   A 1 373 ? 19.423 -27.277 -1.256  1.00 39.76  ?  373 ALA   A CB    1 
ATOM   2846 N N     . GLU   A 1 374 ? 21.866 -28.261 0.427   1.00 44.67  ?  374 GLU   A N     1 
ATOM   2847 C CA    . GLU   A 1 374 ? 22.364 -28.717 1.712   1.00 43.94  ?  374 GLU   A CA    1 
ATOM   2848 C C     . GLU   A 1 374 ? 23.600 -27.930 2.123   1.00 49.62  ?  374 GLU   A C     1 
ATOM   2849 O O     . GLU   A 1 374 ? 23.757 -27.575 3.297   1.00 48.73  ?  374 GLU   A O     1 
ATOM   2850 C CB    . GLU   A 1 374 ? 22.640 -30.216 1.639   1.00 46.48  ?  374 GLU   A CB    1 
ATOM   2851 C CG    . GLU   A 1 374 ? 22.738 -30.895 2.973   1.00 51.44  ?  374 GLU   A CG    1 
ATOM   2852 C CD    . GLU   A 1 374 ? 24.096 -30.717 3.560   1.00 51.77  ?  374 GLU   A CD    1 
ATOM   2853 O OE1   . GLU   A 1 374 ? 24.206 -30.601 4.801   1.00 61.36  ?  374 GLU   A OE1   1 
ATOM   2854 O OE2   . GLU   A 1 374 ? 25.054 -30.663 2.757   1.00 54.26  ?  374 GLU   A OE2   1 
ATOM   2855 N N     . TRP   A 1 375 ? 24.466 -27.607 1.165   1.00 47.47  ?  375 TRP   A N     1 
ATOM   2856 C CA    . TRP   A 1 375 ? 25.639 -26.795 1.476   1.00 49.15  ?  375 TRP   A CA    1 
ATOM   2857 C C     . TRP   A 1 375 ? 25.237 -25.371 1.845   1.00 48.63  ?  375 TRP   A C     1 
ATOM   2858 O O     . TRP   A 1 375 ? 25.689 -24.826 2.859   1.00 45.11  ?  375 TRP   A O     1 
ATOM   2859 C CB    . TRP   A 1 375 ? 26.605 -26.804 0.282   1.00 48.63  ?  375 TRP   A CB    1 
ATOM   2860 C CG    . TRP   A 1 375 ? 27.902 -26.056 0.481   1.00 48.22  ?  375 TRP   A CG    1 
ATOM   2861 C CD1   . TRP   A 1 375 ? 28.737 -26.131 1.564   1.00 52.16  ?  375 TRP   A CD1   1 
ATOM   2862 C CD2   . TRP   A 1 375 ? 28.524 -25.145 -0.443  1.00 50.15  ?  375 TRP   A CD2   1 
ATOM   2863 N NE1   . TRP   A 1 375 ? 29.825 -25.309 1.375   1.00 51.90  ?  375 TRP   A NE1   1 
ATOM   2864 C CE2   . TRP   A 1 375 ? 29.716 -24.691 0.156   1.00 50.08  ?  375 TRP   A CE2   1 
ATOM   2865 C CE3   . TRP   A 1 375 ? 28.187 -24.668 -1.726  1.00 54.44  ?  375 TRP   A CE3   1 
ATOM   2866 C CZ2   . TRP   A 1 375 ? 30.580 -23.784 -0.483  1.00 54.43  ?  375 TRP   A CZ2   1 
ATOM   2867 C CZ3   . TRP   A 1 375 ? 29.039 -23.756 -2.357  1.00 49.10  ?  375 TRP   A CZ3   1 
ATOM   2868 C CH2   . TRP   A 1 375 ? 30.222 -23.328 -1.735  1.00 53.25  ?  375 TRP   A CH2   1 
ATOM   2869 N N     . VAL   A 1 376 ? 24.396 -24.746 1.021   1.00 49.30  ?  376 VAL   A N     1 
ATOM   2870 C CA    . VAL   A 1 376 ? 24.006 -23.366 1.276   1.00 48.15  ?  376 VAL   A CA    1 
ATOM   2871 C C     . VAL   A 1 376 ? 23.292 -23.248 2.623   1.00 49.32  ?  376 VAL   A C     1 
ATOM   2872 O O     . VAL   A 1 376 ? 23.419 -22.227 3.308   1.00 48.25  ?  376 VAL   A O     1 
ATOM   2873 C CB    . VAL   A 1 376 ? 23.153 -22.835 0.100   1.00 47.10  ?  376 VAL   A CB    1 
ATOM   2874 C CG1   . VAL   A 1 376 ? 22.528 -21.498 0.427   1.00 45.23  ?  376 VAL   A CG1   1 
ATOM   2875 C CG2   . VAL   A 1 376 ? 24.007 -22.693 -1.157  1.00 48.01  ?  376 VAL   A CG2   1 
ATOM   2876 N N     . ALA   A 1 377 ? 22.615 -24.303 3.062   1.00 46.56  ?  377 ALA   A N     1 
ATOM   2877 C CA    . ALA   A 1 377 ? 21.939 -24.266 4.381   1.00 50.75  ?  377 ALA   A CA    1 
ATOM   2878 C C     . ALA   A 1 377 ? 22.941 -24.126 5.527   1.00 46.06  ?  377 ALA   A C     1 
ATOM   2879 O O     . ALA   A 1 377 ? 22.561 -23.626 6.590   1.00 51.75  ?  377 ALA   A O     1 
ATOM   2880 C CB    . ALA   A 1 377 ? 21.090 -25.487 4.571   1.00 47.94  ?  377 ALA   A CB    1 
ATOM   2881 N N     . ARG   A 1 378 ? 24.184 -24.528 5.303   1.00 44.33  ?  378 ARG   A N     1 
ATOM   2882 C CA    . ARG   A 1 378 ? 25.221 -24.432 6.352   1.00 43.35  ?  378 ARG   A CA    1 
ATOM   2883 C C     . ARG   A 1 378 ? 26.002 -23.116 6.214   1.00 44.56  ?  378 ARG   A C     1 
ATOM   2884 O O     . ARG   A 1 378 ? 26.605 -22.696 7.202   1.00 48.33  ?  378 ARG   A O     1 
ATOM   2885 C CB    . ARG   A 1 378 ? 26.081 -25.692 6.262   1.00 45.33  ?  378 ARG   A CB    1 
ATOM   2886 C CG    . ARG   A 1 378 ? 25.252 -26.967 6.268   1.00 50.91  ?  378 ARG   A CG    1 
ATOM   2887 C CD    . ARG   A 1 378 ? 26.073 -28.172 6.679   1.00 53.95  ?  378 ARG   A CD    1 
ATOM   2888 N NE    . ARG   A 1 378 ? 27.420 -28.131 6.102   1.00 56.47  ?  378 ARG   A NE    1 
ATOM   2889 C CZ    . ARG   A 1 378 ? 27.720 -28.544 4.881   1.00 63.84  ?  378 ARG   A CZ    1 
ATOM   2890 N NH1   . ARG   A 1 378 ? 26.915 -29.377 4.255   1.00 61.54  ?  378 ARG   A NH1   1 
ATOM   2891 N NH2   . ARG   A 1 378 ? 28.824 -28.126 4.291   1.00 65.62  ?  378 ARG   A NH2   1 
ATOM   2892 N N     . LEU   A 1 379 ? 25.976 -22.483 5.051   1.00 45.38  ?  379 LEU   A N     1 
ATOM   2893 C CA    . LEU   A 1 379 ? 26.645 -21.169 4.904   1.00 44.53  ?  379 LEU   A CA    1 
ATOM   2894 C C     . LEU   A 1 379 ? 25.750 -20.065 5.486   1.00 46.83  ?  379 LEU   A C     1 
ATOM   2895 O O     . LEU   A 1 379 ? 26.267 -18.967 5.686   1.00 46.51  ?  379 LEU   A O     1 
ATOM   2896 C CB    . LEU   A 1 379 ? 27.000 -20.871 3.451   1.00 45.58  ?  379 LEU   A CB    1 
ATOM   2897 C CG    . LEU   A 1 379 ? 27.901 -21.873 2.727   1.00 51.95  ?  379 LEU   A CG    1 
ATOM   2898 C CD1   . LEU   A 1 379 ? 27.523 -21.917 1.262   1.00 46.60  ?  379 LEU   A CD1   1 
ATOM   2899 C CD2   . LEU   A 1 379 ? 29.344 -21.445 2.869   1.00 48.70  ?  379 LEU   A CD2   1 
ATOM   2900 N N     . VAL   A 1 380 ? 24.470 -20.342 5.757   1.00 48.80  ?  380 VAL   A N     1 
ATOM   2901 C CA    . VAL   A 1 380 ? 23.601 -19.259 6.237   1.00 49.38  ?  380 VAL   A CA    1 
ATOM   2902 C C     . VAL   A 1 380 ? 23.681 -19.085 7.762   1.00 54.67  ?  380 VAL   A C     1 
ATOM   2903 O O     . VAL   A 1 380 ? 23.621 -17.958 8.277   1.00 52.01  ?  380 VAL   A O     1 
ATOM   2904 C CB    . VAL   A 1 380 ? 22.148 -19.512 5.777   1.00 50.21  ?  380 VAL   A CB    1 
ATOM   2905 C CG1   . VAL   A 1 380 ? 21.158 -18.708 6.623   1.00 50.46  ?  380 VAL   A CG1   1 
ATOM   2906 C CG2   . VAL   A 1 380 ? 21.982 -19.152 4.324   1.00 53.14  ?  380 VAL   A CG2   1 
ATOM   2907 N N     . ASP   A 1 381 ? 23.787 -20.177 8.516   1.00 46.32  ?  381 ASP   A N     1 
ATOM   2908 C CA    . ASP   A 1 381 ? 23.900 -20.075 9.961   1.00 55.01  ?  381 ASP   A CA    1 
ATOM   2909 C C     . ASP   A 1 381 ? 25.319 -20.305 10.439  1.00 54.56  ?  381 ASP   A C     1 
ATOM   2910 O O     . ASP   A 1 381 ? 25.543 -20.433 11.645  1.00 61.79  ?  381 ASP   A O     1 
ATOM   2911 C CB    . ASP   A 1 381 ? 22.923 -21.030 10.665  1.00 56.58  ?  381 ASP   A CB    1 
ATOM   2912 C CG    . ASP   A 1 381 ? 23.252 -22.498 10.448  1.00 58.52  ?  381 ASP   A CG    1 
ATOM   2913 O OD1   . ASP   A 1 381 ? 24.150 -22.811 9.630   1.00 55.28  ?  381 ASP   A OD1   1 
ATOM   2914 O OD2   . ASP   A 1 381 ? 22.589 -23.348 11.097  1.00 63.72  ?  381 ASP   A OD2   1 
ATOM   2915 N N     . GLY   A 1 382 ? 26.276 -20.362 9.528   1.00 50.85  ?  382 GLY   A N     1 
ATOM   2916 C CA    . GLY   A 1 382 ? 27.670 -20.320 9.897   1.00 50.61  ?  382 GLY   A CA    1 
ATOM   2917 C C     . GLY   A 1 382 ? 28.383 -21.655 9.963   1.00 49.71  ?  382 GLY   A C     1 
ATOM   2918 O O     . GLY   A 1 382 ? 29.618 -21.667 10.046  1.00 47.62  ?  382 GLY   A O     1 
ATOM   2919 N N     . ALA   A 1 383 ? 27.660 -22.774 9.927   1.00 47.78  ?  383 ALA   A N     1 
ATOM   2920 C CA    . ALA   A 1 383 ? 28.320 -24.077 9.902   1.00 42.60  ?  383 ALA   A CA    1 
ATOM   2921 C C     . ALA   A 1 383 ? 29.247 -24.270 8.695   1.00 48.18  ?  383 ALA   A C     1 
ATOM   2922 O O     . ALA   A 1 383 ? 30.008 -25.248 8.669   1.00 48.13  ?  383 ALA   A O     1 
ATOM   2923 C CB    . ALA   A 1 383 ? 27.267 -25.182 9.921   1.00 48.07  ?  383 ALA   A CB    1 
ATOM   2924 N N     . ALA   A 1 384 ? 29.192 -23.390 7.692   1.00 44.59  ?  384 ALA   A N     1 
ATOM   2925 C CA    . ALA   A 1 384 ? 30.043 -23.493 6.517   1.00 41.89  ?  384 ALA   A CA    1 
ATOM   2926 C C     . ALA   A 1 384 ? 30.703 -22.146 6.229   1.00 42.32  ?  384 ALA   A C     1 
ATOM   2927 O O     . ALA   A 1 384 ? 30.125 -21.080 6.479   1.00 42.28  ?  384 ALA   A O     1 
ATOM   2928 C CB    . ALA   A 1 384 ? 29.233 -23.976 5.320   1.00 45.30  ?  384 ALA   A CB    1 
ATOM   2929 N N     . VAL   A 1 385 ? 31.931 -22.201 5.716   1.00 42.44  ?  385 VAL   A N     1 
ATOM   2930 C CA    . VAL   A 1 385 ? 32.690 -21.002 5.383   1.00 43.95  ?  385 VAL   A CA    1 
ATOM   2931 C C     . VAL   A 1 385 ? 33.115 -21.035 3.896   1.00 46.37  ?  385 VAL   A C     1 
ATOM   2932 O O     . VAL   A 1 385 ? 33.058 -22.067 3.212   1.00 42.22  ?  385 VAL   A O     1 
ATOM   2933 C CB    . VAL   A 1 385 ? 33.917 -20.817 6.300   1.00 44.59  ?  385 VAL   A CB    1 
ATOM   2934 C CG1   . VAL   A 1 385 ? 33.486 -20.580 7.758   1.00 40.14  ?  385 VAL   A CG1   1 
ATOM   2935 C CG2   . VAL   A 1 385 ? 34.826 -22.013 6.203   1.00 39.63  ?  385 VAL   A CG2   1 
ATOM   2936 N N     . LEU   A 1 386 ? 33.549 -19.873 3.415   1.00 40.15  ?  386 LEU   A N     1 
ATOM   2937 C CA    . LEU   A 1 386 ? 33.955 -19.630 2.046   1.00 46.86  ?  386 LEU   A CA    1 
ATOM   2938 C C     . LEU   A 1 386 ? 35.405 -19.161 2.013   1.00 50.47  ?  386 LEU   A C     1 
ATOM   2939 O O     . LEU   A 1 386 ? 35.923 -18.640 3.010   1.00 47.06  ?  386 LEU   A O     1 
ATOM   2940 C CB    . LEU   A 1 386 ? 33.058 -18.569 1.377   1.00 45.39  ?  386 LEU   A CB    1 
ATOM   2941 C CG    . LEU   A 1 386 ? 31.567 -18.867 1.164   1.00 48.46  ?  386 LEU   A CG    1 
ATOM   2942 C CD1   . LEU   A 1 386 ? 30.780 -17.615 0.737   1.00 39.77  ?  386 LEU   A CD1   1 
ATOM   2943 C CD2   . LEU   A 1 386 ? 31.369 -19.999 0.164   1.00 46.57  ?  386 LEU   A CD2   1 
ATOM   2944 N N     . PRO   A 1 387 ? 36.093 -19.341 0.886   1.00 48.57  ?  387 PRO   A N     1 
ATOM   2945 C CA    . PRO   A 1 387 ? 37.435 -18.761 0.734   1.00 45.81  ?  387 PRO   A CA    1 
ATOM   2946 C C     . PRO   A 1 387 ? 37.398 -17.243 0.646   1.00 47.83  ?  387 PRO   A C     1 
ATOM   2947 O O     . PRO   A 1 387 ? 36.358 -16.623 0.425   1.00 48.03  ?  387 PRO   A O     1 
ATOM   2948 C CB    . PRO   A 1 387 ? 37.953 -19.368 -0.578  1.00 46.39  ?  387 PRO   A CB    1 
ATOM   2949 C CG    . PRO   A 1 387 ? 36.801 -20.117 -1.171  1.00 47.24  ?  387 PRO   A CG    1 
ATOM   2950 C CD    . PRO   A 1 387 ? 35.804 -20.382 -0.117  1.00 47.08  ?  387 PRO   A CD    1 
ATOM   2951 N N     . ALA   A 1 388 ? 38.567 -16.640 0.825   1.00 46.05  ?  388 ALA   A N     1 
ATOM   2952 C CA    . ALA   A 1 388 ? 38.693 -15.223 0.533   1.00 45.14  ?  388 ALA   A CA    1 
ATOM   2953 C C     . ALA   A 1 388 ? 38.370 -14.983 -0.937  1.00 51.64  ?  388 ALA   A C     1 
ATOM   2954 O O     . ALA   A 1 388 ? 38.565 -15.859 -1.785  1.00 47.12  ?  388 ALA   A O     1 
ATOM   2955 C CB    . ALA   A 1 388 ? 40.104 -14.723 0.859   1.00 43.46  ?  388 ALA   A CB    1 
ATOM   2956 N N     . ALA   A 1 389 ? 37.902 -13.764 -1.230  1.00 52.26  ?  389 ALA   A N     1 
ATOM   2957 C CA    . ALA   A 1 389 ? 37.329 -13.448 -2.536  1.00 51.36  ?  389 ALA   A CA    1 
ATOM   2958 C C     . ALA   A 1 389 ? 38.323 -13.677 -3.676  1.00 54.49  ?  389 ALA   A C     1 
ATOM   2959 O O     . ALA   A 1 389 ? 37.955 -14.223 -4.723  1.00 49.81  ?  389 ALA   A O     1 
ATOM   2960 C CB    . ALA   A 1 389 ? 36.814 -12.009 -2.543  1.00 47.51  ?  389 ALA   A CB    1 
ATOM   2961 N N     . ASP   A 1 390 ? 39.583 -13.271 -3.500  1.00 56.61  ?  390 ASP   A N     1 
ATOM   2962 C CA    . ASP   A 1 390 ? 40.604 -13.612 -4.490  1.00 56.25  ?  390 ASP   A CA    1 
ATOM   2963 C C     . ASP   A 1 390 ? 40.666 -15.112 -4.717  1.00 53.07  ?  390 ASP   A C     1 
ATOM   2964 O O     . ASP   A 1 390 ? 40.564 -15.582 -5.853  1.00 57.13  ?  390 ASP   A O     1 
ATOM   2965 C CB    . ASP   A 1 390 ? 41.977 -13.108 -4.057  1.00 59.76  ?  390 ASP   A CB    1 
ATOM   2966 C CG    . ASP   A 1 390 ? 42.114 -11.620 -4.190  1.00 67.36  ?  390 ASP   A CG    1 
ATOM   2967 O OD1   . ASP   A 1 390 ? 41.283 -11.012 -4.902  1.00 67.73  ?  390 ASP   A OD1   1 
ATOM   2968 O OD2   . ASP   A 1 390 ? 43.063 -11.061 -3.597  1.00 67.30  ?  390 ASP   A OD2   1 
ATOM   2969 N N     . GLN   A 1 391 ? 40.828 -15.886 -3.644  1.00 50.27  ?  391 GLN   A N     1 
ATOM   2970 C CA    . GLN   A 1 391 ? 40.941 -17.325 -3.808  1.00 52.98  ?  391 GLN   A CA    1 
ATOM   2971 C C     . GLN   A 1 391 ? 39.687 -17.918 -4.432  1.00 55.01  ?  391 GLN   A C     1 
ATOM   2972 O O     . GLN   A 1 391 ? 39.742 -19.029 -4.968  1.00 52.59  ?  391 GLN   A O     1 
ATOM   2973 C CB    . GLN   A 1 391 ? 41.230 -17.993 -2.466  1.00 48.35  ?  391 GLN   A CB    1 
ATOM   2974 C CG    . GLN   A 1 391 ? 42.701 -17.959 -2.044  1.00 52.37  ?  391 GLN   A CG    1 
ATOM   2975 C CD    . GLN   A 1 391 ? 43.258 -16.551 -1.931  1.00 53.01  ?  391 GLN   A CD    1 
ATOM   2976 O OE1   . GLN   A 1 391 ? 42.652 -15.676 -1.315  1.00 50.08  ?  391 GLN   A OE1   1 
ATOM   2977 N NE2   . GLN   A 1 391 ? 44.422 -16.330 -2.520  1.00 52.76  ?  391 GLN   A NE2   1 
ATOM   2978 N N     . MET   A 1 392 ? 38.594 -17.166 -4.450  1.00 50.74  ?  392 MET   A N     1 
ATOM   2979 C CA    . MET   A 1 392 ? 37.324 -17.682 -5.013  1.00 49.70  ?  392 MET   A CA    1 
ATOM   2980 C C     . MET   A 1 392 ? 37.320 -17.396 -6.518  1.00 58.71  ?  392 MET   A C     1 
ATOM   2981 O O     . MET   A 1 392 ? 36.854 -18.261 -7.280  1.00 51.85  ?  392 MET   A O     1 
ATOM   2982 C CB    . MET   A 1 392 ? 36.126 -17.007 -4.345  1.00 50.90  ?  392 MET   A CB    1 
ATOM   2983 C CG    . MET   A 1 392 ? 35.384 -17.871 -3.350  1.00 50.80  ?  392 MET   A CG    1 
ATOM   2984 S SD    . MET   A 1 392 ? 33.805 -17.203 -2.789  1.00 56.33  ?  392 MET   A SD    1 
ATOM   2985 C CE    . MET   A 1 392 ? 34.268 -15.542 -2.288  1.00 49.09  ?  392 MET   A CE    1 
ATOM   2986 N N     . ARG   A 1 393 ? 37.885 -16.253 -6.917  1.00 57.66  ?  393 ARG   A N     1 
ATOM   2987 C CA    . ARG   A 1 393 ? 37.909 -15.824 -8.335  1.00 54.59  ?  393 ARG   A CA    1 
ATOM   2988 C C     . ARG   A 1 393 ? 38.871 -16.715 -9.117  1.00 58.13  ?  393 ARG   A C     1 
ATOM   2989 O O     . ARG   A 1 393 ? 38.844 -16.670 -10.355 1.00 64.77  ?  393 ARG   A O     1 
ATOM   2990 C CB    . ARG   A 1 393 ? 38.355 -14.362 -8.349  1.00 52.19  ?  393 ARG   A CB    1 
ATOM   2991 C CG    . ARG   A 1 393 ? 37.245 -13.395 -7.969  1.00 49.87  ?  393 ARG   A CG    1 
ATOM   2992 C CD    . ARG   A 1 393 ? 37.625 -11.964 -8.286  1.00 54.40  ?  393 ARG   A CD    1 
ATOM   2993 N NE    . ARG   A 1 393 ? 38.717 -11.496 -7.430  1.00 61.95  ?  393 ARG   A NE    1 
ATOM   2994 C CZ    . ARG   A 1 393 ? 38.567 -10.617 -6.455  1.00 64.53  ?  393 ARG   A CZ    1 
ATOM   2995 N NH1   . ARG   A 1 393 ? 37.583 -10.754 -5.592  1.00 64.33  ?  393 ARG   A NH1   1 
ATOM   2996 N NH2   . ARG   A 1 393 ? 39.403 -9.603  -6.343  1.00 63.38  ?  393 ARG   A NH2   1 
ATOM   2997 N N     . GLU   A 1 394 ? 39.674 -17.495 -8.406  1.00 53.11  ?  394 GLU   A N     1 
ATOM   2998 C CA    . GLU   A 1 394 ? 40.655 -18.380 -9.065  1.00 51.02  ?  394 GLU   A CA    1 
ATOM   2999 C C     . GLU   A 1 394 ? 39.968 -19.684 -9.468  1.00 51.97  ?  394 GLU   A C     1 
ATOM   3000 O O     . GLU   A 1 394 ? 40.240 -20.179 -10.565 1.00 50.33  ?  394 GLU   A O     1 
ATOM   3001 C CB    . GLU   A 1 394 ? 41.803 -18.633 -8.098  1.00 52.48  ?  394 GLU   A CB    1 
ATOM   3002 C CG    . GLU   A 1 394 ? 42.710 -17.425 -7.894  1.00 53.77  ?  394 GLU   A CG    1 
ATOM   3003 C CD    . GLU   A 1 394 ? 43.647 -17.576 -6.712  1.00 65.60  ?  394 GLU   A CD    1 
ATOM   3004 O OE1   . GLU   A 1 394 ? 43.749 -18.691 -6.165  1.00 65.15  ?  394 GLU   A OE1   1 
ATOM   3005 O OE2   . GLU   A 1 394 ? 44.281 -16.572 -6.338  1.00 72.74  ?  394 GLU   A OE2   1 
ATOM   3006 N N     . GLU   A 1 395 ? 39.110 -20.209 -8.599  1.00 51.77  ?  395 GLU   A N     1 
ATOM   3007 C CA    . GLU   A 1 395 ? 38.393 -21.465 -8.926  1.00 55.20  ?  395 GLU   A CA    1 
ATOM   3008 C C     . GLU   A 1 395 ? 37.558 -21.189 -10.169 1.00 55.85  ?  395 GLU   A C     1 
ATOM   3009 O O     . GLU   A 1 395 ? 37.511 -22.042 -11.068 1.00 51.18  ?  395 GLU   A O     1 
ATOM   3010 C CB    . GLU   A 1 395 ? 37.454 -21.972 -7.835  1.00 43.56  ?  395 GLU   A CB    1 
ATOM   3011 C CG    . GLU   A 1 395 ? 36.829 -23.330 -8.137  1.00 41.34  ?  395 GLU   A CG    1 
ATOM   3012 C CD    . GLU   A 1 395 ? 35.461 -23.268 -8.787  1.00 46.62  ?  395 GLU   A CD    1 
ATOM   3013 O OE1   . GLU   A 1 395 ? 35.060 -24.275 -9.394  1.00 46.29  ?  395 GLU   A OE1   1 
ATOM   3014 O OE2   . GLU   A 1 395 ? 34.805 -22.214 -8.698  1.00 47.54  ?  395 GLU   A OE2   1 
ATOM   3015 N N     . ILE   A 1 396 ? 36.934 -20.019 -10.191 1.00 55.06  ?  396 ILE   A N     1 
ATOM   3016 C CA    . ILE   A 1 396 ? 36.116 -19.670 -11.349 1.00 57.77  ?  396 ILE   A CA    1 
ATOM   3017 C C     . ILE   A 1 396 ? 36.981 -19.608 -12.614 1.00 58.18  ?  396 ILE   A C     1 
ATOM   3018 O O     . ILE   A 1 396 ? 36.644 -20.201 -13.647 1.00 51.43  ?  396 ILE   A O     1 
ATOM   3019 C CB    . ILE   A 1 396 ? 35.365 -18.345 -11.078 1.00 56.32  ?  396 ILE   A CB    1 
ATOM   3020 C CG1   . ILE   A 1 396 ? 34.255 -18.554 -10.031 1.00 51.13  ?  396 ILE   A CG1   1 
ATOM   3021 C CG2   . ILE   A 1 396 ? 34.797 -17.743 -12.367 1.00 58.48  ?  396 ILE   A CG2   1 
ATOM   3022 C CD1   . ILE   A 1 396 ? 33.503 -17.295 -9.675  1.00 47.57  ?  396 ILE   A CD1   1 
ATOM   3023 N N     . GLY   A 1 397 ? 38.128 -18.921 -12.534 1.00 57.42  ?  397 GLY   A N     1 
ATOM   3024 C CA    . GLY   A 1 397 ? 39.028 -18.852 -13.673 1.00 53.04  ?  397 GLY   A CA    1 
ATOM   3025 C C     . GLY   A 1 397 ? 39.484 -20.214 -14.152 1.00 54.48  ?  397 GLY   A C     1 
ATOM   3026 O O     . GLY   A 1 397 ? 39.642 -20.438 -15.354 1.00 67.46  ?  397 GLY   A O     1 
ATOM   3027 N N     . THR   A 1 398 ? 39.688 -21.146 -13.222 1.00 46.21  ?  398 THR   A N     1 
ATOM   3028 C CA    . THR   A 1 398 ? 40.046 -22.509 -13.596 1.00 51.34  ?  398 THR   A CA    1 
ATOM   3029 C C     . THR   A 1 398 ? 38.885 -23.224 -14.288 1.00 58.98  ?  398 THR   A C     1 
ATOM   3030 O O     . THR   A 1 398 ? 39.093 -23.945 -15.273 1.00 63.19  ?  398 THR   A O     1 
ATOM   3031 C CB    . THR   A 1 398 ? 40.517 -23.285 -12.360 1.00 50.78  ?  398 THR   A CB    1 
ATOM   3032 O OG1   . THR   A 1 398 ? 41.891 -22.973 -12.103 1.00 50.62  ?  398 THR   A OG1   1 
ATOM   3033 C CG2   . THR   A 1 398 ? 40.379 -24.794 -12.549 1.00 44.32  ?  398 THR   A CG2   1 
ATOM   3034 N N     . TYR   A 1 399 ? 37.656 -23.031 -13.805 1.00 59.07  ?  399 TYR   A N     1 
ATOM   3035 C CA    . TYR   A 1 399 ? 36.517 -23.710 -14.422 1.00 63.45  ?  399 TYR   A CA    1 
ATOM   3036 C C     . TYR   A 1 399 ? 36.314 -23.252 -15.860 1.00 63.04  ?  399 TYR   A C     1 
ATOM   3037 O O     . TYR   A 1 399 ? 35.989 -24.057 -16.742 1.00 58.21  ?  399 TYR   A O     1 
ATOM   3038 C CB    . TYR   A 1 399 ? 35.242 -23.461 -13.615 1.00 58.89  ?  399 TYR   A CB    1 
ATOM   3039 C CG    . TYR   A 1 399 ? 33.973 -23.837 -14.349 1.00 58.76  ?  399 TYR   A CG    1 
ATOM   3040 C CD1   . TYR   A 1 399 ? 33.560 -25.166 -14.410 1.00 58.10  ?  399 TYR   A CD1   1 
ATOM   3041 C CD2   . TYR   A 1 399 ? 33.184 -22.867 -14.984 1.00 54.71  ?  399 TYR   A CD2   1 
ATOM   3042 C CE1   . TYR   A 1 399 ? 32.411 -25.526 -15.074 1.00 56.85  ?  399 TYR   A CE1   1 
ATOM   3043 C CE2   . TYR   A 1 399 ? 32.020 -23.222 -15.648 1.00 54.15  ?  399 TYR   A CE2   1 
ATOM   3044 C CZ    . TYR   A 1 399 ? 31.644 -24.557 -15.688 1.00 56.92  ?  399 TYR   A CZ    1 
ATOM   3045 O OH    . TYR   A 1 399 ? 30.496 -24.947 -16.340 1.00 59.37  ?  399 TYR   A OH    1 
ATOM   3046 N N     . LEU   A 1 400 ? 36.504 -21.956 -16.103 1.00 63.36  ?  400 LEU   A N     1 
ATOM   3047 C CA    . LEU   A 1 400 ? 36.190 -21.357 -17.390 1.00 66.36  ?  400 LEU   A CA    1 
ATOM   3048 C C     . LEU   A 1 400 ? 37.269 -21.668 -18.420 1.00 74.86  ?  400 LEU   A C     1 
ATOM   3049 O O     . LEU   A 1 400 ? 36.980 -22.210 -19.498 1.00 78.76  ?  400 LEU   A O     1 
ATOM   3050 C CB    . LEU   A 1 400 ? 36.009 -19.844 -17.224 1.00 59.99  ?  400 LEU   A CB    1 
ATOM   3051 C CG    . LEU   A 1 400 ? 34.640 -19.345 -16.737 1.00 60.18  ?  400 LEU   A CG    1 
ATOM   3052 C CD1   . LEU   A 1 400 ? 34.628 -17.822 -16.570 1.00 63.35  ?  400 LEU   A CD1   1 
ATOM   3053 C CD2   . LEU   A 1 400 ? 33.479 -19.803 -17.629 1.00 60.33  ?  400 LEU   A CD2   1 
ATOM   3054 N N     . THR   A 1 401 ? 38.525 -21.342 -18.101 1.00 69.50  ?  401 THR   A N     1 
ATOM   3055 C CA    . THR   A 1 401 ? 39.601 -21.627 -19.041 1.00 75.45  ?  401 THR   A CA    1 
ATOM   3056 C C     . THR   A 1 401 ? 39.696 -23.117 -19.359 1.00 75.53  ?  401 THR   A C     1 
ATOM   3057 O O     . THR   A 1 401 ? 40.277 -23.490 -20.382 1.00 82.67  ?  401 THR   A O     1 
ATOM   3058 C CB    . THR   A 1 401 ? 40.927 -21.086 -18.497 1.00 75.95  ?  401 THR   A CB    1 
ATOM   3059 O OG1   . THR   A 1 401 ? 41.197 -21.663 -17.216 1.00 70.95  ?  401 THR   A OG1   1 
ATOM   3060 C CG2   . THR   A 1 401 ? 40.857 -19.566 -18.353 1.00 73.57  ?  401 THR   A CG2   1 
ATOM   3061 N N     . GLY   A 1 402 ? 39.090 -23.969 -18.546 1.00 72.60  ?  402 GLY   A N     1 
ATOM   3062 C CA    . GLY   A 1 402 ? 39.106 -25.391 -18.814 1.00 76.70  ?  402 GLY   A CA    1 
ATOM   3063 C C     . GLY   A 1 402 ? 37.891 -25.916 -19.547 1.00 78.33  ?  402 GLY   A C     1 
ATOM   3064 O O     . GLY   A 1 402 ? 37.953 -27.009 -20.112 1.00 82.74  ?  402 GLY   A O     1 
ATOM   3065 N N     . ILE   A 1 403 ? 36.775 -25.180 -19.536 1.00 80.52  ?  403 ILE   A N     1 
ATOM   3066 C CA    . ILE   A 1 403 ? 35.618 -25.627 -20.310 1.00 83.04  ?  403 ILE   A CA    1 
ATOM   3067 C C     . ILE   A 1 403 ? 35.708 -25.167 -21.747 1.00 87.25  ?  403 ILE   A C     1 
ATOM   3068 O O     . ILE   A 1 403 ? 34.930 -25.637 -22.584 1.00 91.84  ?  403 ILE   A O     1 
ATOM   3069 C CB    . ILE   A 1 403 ? 34.251 -25.154 -19.777 1.00 79.28  ?  403 ILE   A CB    1 
ATOM   3070 C CG1   . ILE   A 1 403 ? 34.087 -23.638 -19.949 1.00 74.38  ?  403 ILE   A CG1   1 
ATOM   3071 C CG2   . ILE   A 1 403 ? 34.010 -25.661 -18.352 1.00 76.49  ?  403 ILE   A CG2   1 
ATOM   3072 C CD1   . ILE   A 1 403 ? 33.065 -23.246 -20.991 1.00 82.33  ?  403 ILE   A CD1   1 
ATOM   3073 N N     . VAL   A 1 404 ? 36.684 -24.325 -22.069 1.00 85.99  ?  404 VAL   A N     1 
ATOM   3074 C CA    . VAL   A 1 404 ? 36.876 -23.933 -23.497 1.00 85.74  ?  404 VAL   A CA    1 
ATOM   3075 C C     . VAL   A 1 404 ? 37.643 -25.062 -24.197 1.00 87.79  ?  404 VAL   A C     1 
ATOM   3076 O O     . VAL   A 1 404 ? 37.598 -25.135 -25.425 1.00 92.69  ?  404 VAL   A O     1 
ATOM   3077 C CB    . VAL   A 1 404 ? 37.598 -22.582 -23.650 1.00 83.48  ?  404 VAL   A CB    1 
ATOM   3078 C CG1   . VAL   A 1 404 ? 37.002 -21.518 -22.738 1.00 77.55  ?  404 VAL   A CG1   1 
ATOM   3079 C CG2   . VAL   A 1 404 ? 39.100 -22.704 -23.437 1.00 82.95  ?  404 VAL   A CG2   1 
ATOM   3080 N N     . GLN   A 1 405 ? 38.289 -25.933 -23.428 1.00 88.38  ?  405 GLN   A N     1 
ATOM   3081 C CA    . GLN   A 1 405 ? 39.032 -27.076 -24.006 1.00 91.01  ?  405 GLN   A CA    1 
ATOM   3082 C C     . GLN   A 1 405 ? 38.070 -28.240 -24.254 1.00 92.60  ?  405 GLN   A C     1 
ATOM   3083 O O     . GLN   A 1 405 ? 38.547 -29.369 -24.491 1.00 88.12  ?  405 GLN   A O     1 
ATOM   3084 C CB    . GLN   A 1 405 ? 40.115 -27.490 -23.015 1.00 87.55  ?  405 GLN   A CB    1 
ATOM   3085 C CG    . GLN   A 1 405 ? 40.828 -26.307 -22.374 1.00 88.03  ?  405 GLN   A CG    1 
ATOM   3086 C CD    . GLN   A 1 405 ? 41.708 -26.710 -21.215 1.00 91.11  ?  405 GLN   A CD    1 
ATOM   3087 O OE1   . GLN   A 1 405 ? 41.610 -27.825 -20.692 1.00 95.42  ?  405 GLN   A OE1   1 
ATOM   3088 N NE2   . GLN   A 1 405 ? 42.580 -25.802 -20.805 1.00 91.31  ?  405 GLN   A NE2   1 
ATOM   3089 N N     . ARG   A 1 406 ? 36.768 -27.974 -24.200 1.00 94.80  ?  406 ARG   A N     1 
ATOM   3090 C CA    . ARG   A 1 406 ? 35.784 -29.071 -24.322 1.00 96.05  ?  406 ARG   A CA    1 
ATOM   3091 C C     . ARG   A 1 406 ? 34.663 -28.622 -25.250 1.00 93.65  ?  406 ARG   A C     1 
ATOM   3092 O O     . ARG   A 1 406 ? 34.218 -29.438 -26.070 1.00 95.02  ?  406 ARG   A O     1 
ATOM   3093 C CB    . ARG   A 1 406 ? 35.234 -29.386 -22.931 1.00 95.83  ?  406 ARG   A CB    1 
ATOM   3094 C CG    . ARG   A 1 406 ? 34.274 -30.564 -22.855 1.00 97.39  ?  406 ARG   A CG    1 
ATOM   3095 C CD    . ARG   A 1 406 ? 33.888 -30.849 -21.414 1.00 100.03 ?  406 ARG   A CD    1 
ATOM   3096 N NE    . ARG   A 1 406 ? 32.868 -31.894 -21.284 1.00 100.24 ?  406 ARG   A NE    1 
ATOM   3097 C CZ    . ARG   A 1 406 ? 32.701 -32.643 -20.202 1.00 99.39  ?  406 ARG   A CZ    1 
ATOM   3098 N NH1   . ARG   A 1 406 ? 33.022 -32.167 -19.013 1.00 93.13  ?  406 ARG   A NH1   1 
ATOM   3099 N NH2   . ARG   A 1 406 ? 32.215 -33.865 -20.312 1.00 96.75  ?  406 ARG   A NH2   1 
ATOM   3100 N N     . TYR   A 1 407 ? 34.236 -27.370 -25.114 1.00 93.83  ?  407 TYR   A N     1 
ATOM   3101 C CA    . TYR   A 1 407 ? 33.145 -26.843 -25.972 1.00 95.45  ?  407 TYR   A CA    1 
ATOM   3102 C C     . TYR   A 1 407 ? 33.656 -25.630 -26.728 1.00 97.95  ?  407 TYR   A C     1 
ATOM   3103 O O     . TYR   A 1 407 ? 32.880 -24.996 -27.472 1.00 98.62  ?  407 TYR   A O     1 
ATOM   3104 C CB    . TYR   A 1 407 ? 31.905 -26.456 -25.163 1.00 95.08  ?  407 TYR   A CB    1 
ATOM   3105 C CG    . TYR   A 1 407 ? 31.491 -27.435 -24.073 1.00 97.82  ?  407 TYR   A CG    1 
ATOM   3106 C CD1   . TYR   A 1 407 ? 31.103 -28.732 -24.379 1.00 95.61  ?  407 TYR   A CD1   1 
ATOM   3107 C CD2   . TYR   A 1 407 ? 31.483 -27.053 -22.740 1.00 94.25  ?  407 TYR   A CD2   1 
ATOM   3108 C CE1   . TYR   A 1 407 ? 30.723 -29.620 -23.388 1.00 97.56  ?  407 TYR   A CE1   1 
ATOM   3109 C CE2   . TYR   A 1 407 ? 31.105 -27.931 -21.741 1.00 92.34  ?  407 TYR   A CE2   1 
ATOM   3110 C CZ    . TYR   A 1 407 ? 30.723 -29.218 -22.066 1.00 93.32  ?  407 TYR   A CZ    1 
ATOM   3111 O OH    . TYR   A 1 407 ? 30.352 -30.079 -21.078 1.00 89.97  ?  407 TYR   A OH    1 
ATOM   3112 N N     . GLY   A 1 408 ? 34.930 -25.295 -26.540 1.00 95.20  ?  408 GLY   A N     1 
ATOM   3113 C CA    . GLY   A 1 408 ? 35.427 -24.068 -27.182 1.00 90.94  ?  408 GLY   A CA    1 
ATOM   3114 C C     . GLY   A 1 408 ? 34.662 -22.855 -26.711 1.00 96.34  ?  408 GLY   A C     1 
ATOM   3115 O O     . GLY   A 1 408 ? 34.172 -22.867 -25.568 1.00 95.95  ?  408 GLY   A O     1 
ATOM   3116 N N     . ARG   A 1 409 ? 34.546 -21.844 -27.570 1.00 102.85 ?  409 ARG   A N     1 
ATOM   3117 C CA    . ARG   A 1 409 ? 33.857 -20.588 -27.190 1.00 108.17 ?  409 ARG   A CA    1 
ATOM   3118 C C     . ARG   A 1 409 ? 32.393 -20.618 -27.645 1.00 114.39 ?  409 ARG   A C     1 
ATOM   3119 O O     . ARG   A 1 409 ? 32.166 -20.848 -28.845 1.00 113.71 ?  409 ARG   A O     1 
ATOM   3120 C CB    . ARG   A 1 409 ? 34.581 -19.397 -27.823 1.00 107.11 ?  409 ARG   A CB    1 
ATOM   3121 C CG    . ARG   A 1 409 ? 33.818 -18.082 -27.765 1.00 114.92 ?  409 ARG   A CG    1 
ATOM   3122 C CD    . ARG   A 1 409 ? 33.212 -17.683 -29.102 1.00 121.98 ?  409 ARG   A CD    1 
ATOM   3123 N NE    . ARG   A 1 409 ? 32.218 -16.611 -28.978 1.00 125.11 ?  409 ARG   A NE    1 
ATOM   3124 C CZ    . ARG   A 1 409 ? 30.954 -16.782 -28.613 1.00 126.48 ?  409 ARG   A CZ    1 
ATOM   3125 N NH1   . ARG   A 1 409 ? 30.636 -16.827 -27.332 1.00 125.52 ?  409 ARG   A NH1   1 
ATOM   3126 N NH2   . ARG   A 1 409 ? 30.013 -16.897 -29.530 1.00 125.20 ?  409 ARG   A NH2   1 
ATOM   3127 N N     . THR   A 1 410 ? 31.447 -20.418 -26.723 1.00 123.67 ?  410 THR   A N     1 
ATOM   3128 C CA    . THR   A 1 410 ? 30.008 -20.302 -27.087 1.00 125.28 ?  410 THR   A CA    1 
ATOM   3129 C C     . THR   A 1 410 ? 29.314 -19.528 -25.983 1.00 123.63 ?  410 THR   A C     1 
ATOM   3130 O O     . THR   A 1 410 ? 30.015 -18.785 -25.266 1.00 123.30 ?  410 THR   A O     1 
ATOM   3131 C CB    . THR   A 1 410 ? 29.363 -21.660 -27.361 1.00 123.99 ?  410 THR   A CB    1 
ATOM   3132 O OG1   . THR   A 1 410 ? 28.016 -21.364 -27.717 1.00 125.56 ?  410 THR   A OG1   1 
ATOM   3133 C CG2   . THR   A 1 410 ? 29.415 -22.590 -26.162 1.00 122.65 ?  410 THR   A CG2   1 
ATOM   3134 N N     . GLU   A 1 411 ? 28.003 -19.682 -25.820 1.00 119.97 ?  411 GLU   A N     1 
ATOM   3135 C CA    . GLU   A 1 411 ? 27.284 -18.868 -24.850 1.00 124.51 ?  411 GLU   A CA    1 
ATOM   3136 C C     . GLU   A 1 411 ? 26.841 -19.623 -23.595 1.00 117.52 ?  411 GLU   A C     1 
ATOM   3137 O O     . GLU   A 1 411 ? 27.029 -19.113 -22.483 1.00 115.40 ?  411 GLU   A O     1 
ATOM   3138 C CB    . GLU   A 1 411 ? 26.073 -18.216 -25.530 1.00 126.92 ?  411 GLU   A CB    1 
ATOM   3139 C CG    . GLU   A 1 411 ? 26.332 -17.775 -26.989 1.00 125.61 ?  411 GLU   A CG    1 
ATOM   3140 C CD    . GLU   A 1 411 ? 27.160 -16.495 -27.121 1.00 126.62 ?  411 GLU   A CD    1 
ATOM   3141 O OE1   . GLU   A 1 411 ? 28.199 -16.358 -26.436 1.00 123.98 ?  411 GLU   A OE1   1 
ATOM   3142 O OE2   . GLU   A 1 411 ? 26.773 -15.622 -27.929 1.00 128.96 ?  411 GLU   A OE2   1 
ATOM   3143 N N     . GLY   A 1 412 ? 26.271 -20.821 -23.727 1.00 110.23 ?  412 GLY   A N     1 
ATOM   3144 C CA    . GLY   A 1 412 ? 25.679 -21.486 -22.576 1.00 102.58 ?  412 GLY   A CA    1 
ATOM   3145 C C     . GLY   A 1 412 ? 26.519 -22.597 -21.974 1.00 92.57  ?  412 GLY   A C     1 
ATOM   3146 O O     . GLY   A 1 412 ? 26.020 -23.423 -21.197 1.00 80.50  ?  412 GLY   A O     1 
ATOM   3147 N N     . ALA   A 1 413 ? 27.801 -22.637 -22.339 1.00 93.98  ?  413 ALA   A N     1 
ATOM   3148 C CA    . ALA   A 1 413 ? 28.714 -23.624 -21.779 1.00 89.58  ?  413 ALA   A CA    1 
ATOM   3149 C C     . ALA   A 1 413 ? 29.149 -23.299 -20.360 1.00 77.41  ?  413 ALA   A C     1 
ATOM   3150 O O     . ALA   A 1 413 ? 29.715 -24.178 -19.690 1.00 74.29  ?  413 ALA   A O     1 
ATOM   3151 C CB    . ALA   A 1 413 ? 29.952 -23.753 -22.664 1.00 93.97  ?  413 ALA   A CB    1 
ATOM   3152 N N     . SER   A 1 414 ? 28.906 -22.066 -19.901 1.00 75.61  ?  414 SER   A N     1 
ATOM   3153 C CA    . SER   A 1 414 ? 29.405 -21.590 -18.614 1.00 72.17  ?  414 SER   A CA    1 
ATOM   3154 C C     . SER   A 1 414 ? 28.644 -22.150 -17.412 1.00 66.96  ?  414 SER   A C     1 
ATOM   3155 O O     . SER   A 1 414 ? 28.968 -21.776 -16.286 1.00 69.02  ?  414 SER   A O     1 
ATOM   3156 C CB    . SER   A 1 414 ? 29.386 -20.050 -18.580 1.00 71.67  ?  414 SER   A CB    1 
ATOM   3157 O OG    . SER   A 1 414 ? 28.264 -19.551 -19.293 1.00 81.35  ?  414 SER   A OG    1 
ATOM   3158 N N     . ILE   A 1 415 ? 27.691 -23.062 -17.607 1.00 66.72  ?  415 ILE   A N     1 
ATOM   3159 C CA    . ILE   A 1 415 ? 26.974 -23.696 -16.503 1.00 61.85  ?  415 ILE   A CA    1 
ATOM   3160 C C     . ILE   A 1 415 ? 26.926 -25.198 -16.750 1.00 62.45  ?  415 ILE   A C     1 
ATOM   3161 O O     . ILE   A 1 415 ? 26.060 -25.909 -16.219 1.00 56.50  ?  415 ILE   A O     1 
ATOM   3162 C CB    . ILE   A 1 415 ? 25.555 -23.119 -16.307 1.00 57.90  ?  415 ILE   A CB    1 
ATOM   3163 C CG1   . ILE   A 1 415 ? 24.608 -23.572 -17.424 1.00 56.71  ?  415 ILE   A CG1   1 
ATOM   3164 C CG2   . ILE   A 1 415 ? 25.597 -21.609 -16.238 1.00 59.32  ?  415 ILE   A CG2   1 
ATOM   3165 C CD1   . ILE   A 1 415 ? 23.156 -23.363 -17.087 1.00 54.27  ?  415 ILE   A CD1   1 
ATOM   3166 N N     . GLN   A 1 416 ? 27.867 -25.692 -17.549 1.00 61.64  ?  416 GLN   A N     1 
ATOM   3167 C CA    . GLN   A 1 416 ? 27.909 -27.100 -17.916 1.00 67.18  ?  416 GLN   A CA    1 
ATOM   3168 C C     . GLN   A 1 416 ? 28.735 -27.878 -16.905 1.00 62.45  ?  416 GLN   A C     1 
ATOM   3169 O O     . GLN   A 1 416 ? 29.871 -27.500 -16.609 1.00 59.45  ?  416 GLN   A O     1 
ATOM   3170 C CB    . GLN   A 1 416 ? 28.495 -27.261 -19.318 1.00 73.35  ?  416 GLN   A CB    1 
ATOM   3171 C CG    . GLN   A 1 416 ? 27.619 -26.656 -20.386 1.00 76.85  ?  416 GLN   A CG    1 
ATOM   3172 C CD    . GLN   A 1 416 ? 27.175 -27.687 -21.385 1.00 83.64  ?  416 GLN   A CD    1 
ATOM   3173 O OE1   . GLN   A 1 416 ? 27.763 -27.836 -22.458 1.00 89.69  ?  416 GLN   A OE1   1 
ATOM   3174 N NE2   . GLN   A 1 416 ? 26.149 -28.447 -21.015 1.00 79.64  ?  416 GLN   A NE2   1 
ATOM   3175 N N     . VAL   A 1 417 ? 28.175 -28.979 -16.410 1.00 61.94  ?  417 VAL   A N     1 
ATOM   3176 C CA    . VAL   A 1 417 ? 28.877 -29.742 -15.335 1.00 71.96  ?  417 VAL   A CA    1 
ATOM   3177 C C     . VAL   A 1 417 ? 28.815 -31.258 -15.572 1.00 73.59  ?  417 VAL   A C     1 
ATOM   3178 O O     . VAL   A 1 417 ? 27.926 -31.712 -16.314 1.00 68.48  ?  417 VAL   A O     1 
ATOM   3179 C CB    . VAL   A 1 417 ? 28.311 -29.413 -13.940 1.00 63.96  ?  417 VAL   A CB    1 
ATOM   3180 C CG1   . VAL   A 1 417 ? 28.933 -28.155 -13.349 1.00 59.45  ?  417 VAL   A CG1   1 
ATOM   3181 C CG2   . VAL   A 1 417 ? 26.794 -29.306 -13.951 1.00 65.05  ?  417 VAL   A CG2   1 
ATOM   3182 N N     . ASP   A 1 418 ? 29.724 -31.997 -14.933 1.00 77.61  ?  418 ASP   A N     1 
ATOM   3183 C CA    . ASP   A 1 418 ? 29.727 -33.479 -15.006 1.00 82.68  ?  418 ASP   A CA    1 
ATOM   3184 C C     . ASP   A 1 418 ? 29.150 -34.012 -13.691 1.00 87.05  ?  418 ASP   A C     1 
ATOM   3185 O O     . ASP   A 1 418 ? 29.816 -33.874 -12.653 1.00 83.07  ?  418 ASP   A O     1 
ATOM   3186 C CB    . ASP   A 1 418 ? 31.128 -33.999 -15.286 1.00 89.34  ?  418 ASP   A CB    1 
ATOM   3187 C CG    . ASP   A 1 418 ? 32.258 -33.337 -14.513 1.00 90.37  ?  418 ASP   A CG    1 
ATOM   3188 O OD1   . ASP   A 1 418 ? 31.977 -32.393 -13.746 1.00 89.22  ?  418 ASP   A OD1   1 
ATOM   3189 O OD2   . ASP   A 1 418 ? 33.411 -33.777 -14.684 1.00 95.59  ?  418 ASP   A OD2   1 
ATOM   3190 N N     . VAL   A 1 419 ? 27.966 -34.617 -13.733 1.00 89.49  ?  419 VAL   A N     1 
ATOM   3191 C CA    . VAL   A 1 419 ? 27.276 -35.097 -12.495 1.00 88.40  ?  419 VAL   A CA    1 
ATOM   3192 C C     . VAL   A 1 419 ? 28.252 -35.835 -11.570 1.00 88.36  ?  419 VAL   A C     1 
ATOM   3193 O O     . VAL   A 1 419 ? 28.254 -35.523 -10.367 1.00 85.46  ?  419 VAL   A O     1 
ATOM   3194 C CB    . VAL   A 1 419 ? 26.086 -35.997 -12.876 1.00 84.08  ?  419 VAL   A CB    1 
ATOM   3195 C CG1   . VAL   A 1 419 ? 25.063 -36.100 -11.754 1.00 71.52  ?  419 VAL   A CG1   1 
ATOM   3196 C CG2   . VAL   A 1 419 ? 25.424 -35.536 -14.166 1.00 75.97  ?  419 VAL   A CG2   1 
ATOM   3197 N N     . GLY   A 1 420 ? 29.040 -36.761 -12.104 1.00 90.19  ?  420 GLY   A N     1 
ATOM   3198 C CA    . GLY   A 1 420 ? 29.937 -37.582 -11.269 1.00 89.57  ?  420 GLY   A CA    1 
ATOM   3199 C C     . GLY   A 1 420 ? 30.780 -36.770 -10.316 1.00 89.69  ?  420 GLY   A C     1 
ATOM   3200 O O     . GLY   A 1 420 ? 30.496 -36.785 -9.108  1.00 85.83  ?  420 GLY   A O     1 
ATOM   3201 N N     . PRO   A 1 421 ? 31.849 -36.111 -10.792 1.00 91.32  ?  421 PRO   A N     1 
ATOM   3202 C CA    . PRO   A 1 421 ? 32.738 -35.381 -9.903  1.00 90.44  ?  421 PRO   A CA    1 
ATOM   3203 C C     . PRO   A 1 421 ? 32.107 -34.225 -9.137  1.00 87.66  ?  421 PRO   A C     1 
ATOM   3204 O O     . PRO   A 1 421 ? 32.549 -33.929 -8.018  1.00 87.04  ?  421 PRO   A O     1 
ATOM   3205 C CB    . PRO   A 1 421 ? 33.807 -34.901 -10.886 1.00 92.00  ?  421 PRO   A CB    1 
ATOM   3206 C CG    . PRO   A 1 421 ? 33.761 -35.917 -11.994 1.00 94.40  ?  421 PRO   A CG    1 
ATOM   3207 C CD    . PRO   A 1 421 ? 32.272 -36.110 -12.173 1.00 93.76  ?  421 PRO   A CD    1 
ATOM   3208 N N     . TYR   A 1 422 ? 31.104 -33.578 -9.721  1.00 84.84  ?  422 TYR   A N     1 
ATOM   3209 C CA    . TYR   A 1 422 ? 30.487 -32.404 -9.049  1.00 85.81  ?  422 TYR   A CA    1 
ATOM   3210 C C     . TYR   A 1 422 ? 29.920 -32.836 -7.710  1.00 83.44  ?  422 TYR   A C     1 
ATOM   3211 O O     . TYR   A 1 422 ? 30.268 -32.219 -6.693  1.00 78.24  ?  422 TYR   A O     1 
ATOM   3212 C CB    . TYR   A 1 422 ? 29.368 -31.788 -9.891  1.00 80.32  ?  422 TYR   A CB    1 
ATOM   3213 C CG    . TYR   A 1 422 ? 28.781 -30.499 -9.334  1.00 79.34  ?  422 TYR   A CG    1 
ATOM   3214 C CD1   . TYR   A 1 422 ? 29.473 -29.299 -9.425  1.00 76.17  ?  422 TYR   A CD1   1 
ATOM   3215 C CD2   . TYR   A 1 422 ? 27.535 -30.484 -8.721  1.00 74.47  ?  422 TYR   A CD2   1 
ATOM   3216 C CE1   . TYR   A 1 422 ? 28.945 -28.122 -8.923  1.00 70.79  ?  422 TYR   A CE1   1 
ATOM   3217 C CE2   . TYR   A 1 422 ? 26.995 -29.314 -8.217  1.00 67.66  ?  422 TYR   A CE2   1 
ATOM   3218 C CZ    . TYR   A 1 422 ? 27.702 -28.131 -8.318  1.00 69.27  ?  422 TYR   A CZ    1 
ATOM   3219 O OH    . TYR   A 1 422 ? 27.178 -26.976 -7.822  1.00 63.32  ?  422 TYR   A OH    1 
ATOM   3220 N N     . LEU   A 1 423 ? 29.099 -33.886 -7.705  1.00 86.11  ?  423 LEU   A N     1 
ATOM   3221 C CA    . LEU   A 1 423 ? 28.419 -34.349 -6.470  1.00 80.52  ?  423 LEU   A CA    1 
ATOM   3222 C C     . LEU   A 1 423 ? 29.411 -35.004 -5.507  1.00 78.85  ?  423 LEU   A C     1 
ATOM   3223 O O     . LEU   A 1 423 ? 29.052 -35.172 -4.333  1.00 81.79  ?  423 LEU   A O     1 
ATOM   3224 C CB    . LEU   A 1 423 ? 27.326 -35.335 -6.875  1.00 79.40  ?  423 LEU   A CB    1 
ATOM   3225 C CG    . LEU   A 1 423 ? 25.886 -34.841 -6.739  1.00 75.78  ?  423 LEU   A CG    1 
ATOM   3226 C CD1   . LEU   A 1 423 ? 25.156 -35.029 -8.053  1.00 80.00  ?  423 LEU   A CD1   1 
ATOM   3227 C CD2   . LEU   A 1 423 ? 25.197 -35.617 -5.635  1.00 73.77  ?  423 LEU   A CD2   1 
ATOM   3228 N N     . ALA   A 1 424 ? 30.602 -35.356 -5.980  1.00 79.42  ?  424 ALA   A N     1 
ATOM   3229 C CA    . ALA   A 1 424 ? 31.586 -36.055 -5.121  1.00 80.89  ?  424 ALA   A CA    1 
ATOM   3230 C C     . ALA   A 1 424 ? 32.164 -35.096 -4.087  1.00 81.78  ?  424 ALA   A C     1 
ATOM   3231 O O     . ALA   A 1 424 ? 32.788 -35.570 -3.127  1.00 76.89  ?  424 ALA   A O     1 
ATOM   3232 C CB    . ALA   A 1 424 ? 32.685 -36.627 -5.965  1.00 78.46  ?  424 ALA   A CB    1 
ATOM   3233 N N     . GLU   A 1 425 ? 31.951 -33.797 -4.274  1.00 79.72  ?  425 GLU   A N     1 
ATOM   3234 C CA    . GLU   A 1 425 ? 32.566 -32.803 -3.362  1.00 78.74  ?  425 GLU   A CA    1 
ATOM   3235 C C     . GLU   A 1 425 ? 31.499 -32.148 -2.469  1.00 79.05  ?  425 GLU   A C     1 
ATOM   3236 O O     . GLU   A 1 425 ? 31.593 -30.927 -2.242  1.00 76.71  ?  425 GLU   A O     1 
ATOM   3237 C CB    . GLU   A 1 425 ? 33.344 -31.822 -4.239  1.00 76.38  ?  425 GLU   A CB    1 
ATOM   3238 C CG    . GLU   A 1 425 ? 34.180 -32.513 -5.312  1.00 74.49  ?  425 GLU   A CG    1 
ATOM   3239 C CD    . GLU   A 1 425 ? 34.728 -31.570 -6.364  1.00 80.76  ?  425 GLU   A CD    1 
ATOM   3240 O OE1   . GLU   A 1 425 ? 33.921 -30.973 -7.103  1.00 87.64  ?  425 GLU   A OE1   1 
ATOM   3241 O OE2   . GLU   A 1 425 ? 35.964 -31.432 -6.441  1.00 68.04  ?  425 GLU   A OE2   1 
ATOM   3242 N N     . PHE   A 1 426 ? 30.555 -32.931 -1.947  1.00 78.00  ?  426 PHE   A N     1 
ATOM   3243 C CA    . PHE   A 1 426 ? 29.486 -32.387 -1.119  1.00 77.33  ?  426 PHE   A CA    1 
ATOM   3244 C C     . PHE   A 1 426 ? 29.095 -33.373 -0.011  1.00 71.54  ?  426 PHE   A C     1 
ATOM   3245 O O     . PHE   A 1 426 ? 29.008 -34.585 -0.233  1.00 69.64  ?  426 PHE   A O     1 
ATOM   3246 C CB    . PHE   A 1 426 ? 28.265 -32.034 -1.993  1.00 75.72  ?  426 PHE   A CB    1 
ATOM   3247 C CG    . PHE   A 1 426 ? 28.440 -30.779 -2.848  1.00 69.88  ?  426 PHE   A CG    1 
ATOM   3248 C CD1   . PHE   A 1 426 ? 29.041 -30.842 -4.106  1.00 71.60  ?  426 PHE   A CD1   1 
ATOM   3249 C CD2   . PHE   A 1 426 ? 27.967 -29.544 -2.405  1.00 63.11  ?  426 PHE   A CD2   1 
ATOM   3250 C CE1   . PHE   A 1 426 ? 29.192 -29.687 -4.897  1.00 66.69  ?  426 PHE   A CE1   1 
ATOM   3251 C CE2   . PHE   A 1 426 ? 28.120 -28.388 -3.182  1.00 62.37  ?  426 PHE   A CE2   1 
ATOM   3252 C CZ    . PHE   A 1 426 ? 28.733 -28.465 -4.434  1.00 61.89  ?  426 PHE   A CZ    1 
HETATM 3253 P PA    . FAD   B 2 .   ? 11.690 -23.425 -12.757 1.00 46.00  ?  501 FAD   A PA    1 
HETATM 3254 O O1A   . FAD   B 2 .   ? 11.823 -22.338 -13.753 1.00 56.14  -1 501 FAD   A O1A   1 
HETATM 3255 O O2A   . FAD   B 2 .   ? 11.003 -24.675 -13.156 1.00 45.68  ?  501 FAD   A O2A   1 
HETATM 3256 O O5B   . FAD   B 2 .   ? 10.997 -22.831 -11.451 1.00 50.39  ?  501 FAD   A O5B   1 
HETATM 3257 C C5B   . FAD   B 2 .   ? 11.372 -21.494 -11.086 1.00 48.67  ?  501 FAD   A C5B   1 
HETATM 3258 C C4B   . FAD   B 2 .   ? 10.181 -20.766 -10.516 1.00 47.69  ?  501 FAD   A C4B   1 
HETATM 3259 O O4B   . FAD   B 2 .   ? 10.547 -19.399 -10.244 1.00 50.09  ?  501 FAD   A O4B   1 
HETATM 3260 C C3B   . FAD   B 2 .   ? 8.961  -20.699 -11.439 1.00 50.41  ?  501 FAD   A C3B   1 
HETATM 3261 O O3B   . FAD   B 2 .   ? 7.913  -21.458 -10.857 1.00 51.06  ?  501 FAD   A O3B   1 
HETATM 3262 C C2B   . FAD   B 2 .   ? 8.603  -19.210 -11.525 1.00 52.26  ?  501 FAD   A C2B   1 
HETATM 3263 O O2B   . FAD   B 2 .   ? 7.219  -18.986 -11.369 1.00 53.60  ?  501 FAD   A O2B   1 
HETATM 3264 C C1B   . FAD   B 2 .   ? 9.367  -18.620 -10.346 1.00 54.16  ?  501 FAD   A C1B   1 
HETATM 3265 N N9A   . FAD   B 2 .   ? 9.759  -17.227 -10.528 1.00 56.38  ?  501 FAD   A N9A   1 
HETATM 3266 C C8A   . FAD   B 2 .   ? 10.530 -16.717 -11.537 1.00 55.61  ?  501 FAD   A C8A   1 
HETATM 3267 N N7A   . FAD   B 2 .   ? 10.739 -15.427 -11.438 1.00 57.29  ?  501 FAD   A N7A   1 
HETATM 3268 C C5A   . FAD   B 2 .   ? 10.058 -15.066 -10.285 1.00 58.99  ?  501 FAD   A C5A   1 
HETATM 3269 C C6A   . FAD   B 2 .   ? 9.893  -13.829 -9.638  1.00 61.01  ?  501 FAD   A C6A   1 
HETATM 3270 N N6A   . FAD   B 2 .   ? 10.425 -12.689 -10.072 1.00 57.52  ?  501 FAD   A N6A   1 
HETATM 3271 N N1A   . FAD   B 2 .   ? 9.153  -13.810 -8.506  1.00 59.87  ?  501 FAD   A N1A   1 
HETATM 3272 C C2A   . FAD   B 2 .   ? 8.624  -14.957 -8.072  1.00 58.07  ?  501 FAD   A C2A   1 
HETATM 3273 N N3A   . FAD   B 2 .   ? 8.714  -16.173 -8.595  1.00 57.81  ?  501 FAD   A N3A   1 
HETATM 3274 C C4A   . FAD   B 2 .   ? 9.452  -16.166 -9.715  1.00 56.43  ?  501 FAD   A C4A   1 
HETATM 3275 N N1    . FAD   B 2 .   ? 15.337 -32.084 -16.221 1.00 60.70  ?  501 FAD   A N1    1 
HETATM 3276 C C2    . FAD   B 2 .   ? 15.351 -33.438 -16.056 1.00 61.48  ?  501 FAD   A C2    1 
HETATM 3277 O O2    . FAD   B 2 .   ? 15.947 -33.975 -15.120 1.00 57.21  ?  501 FAD   A O2    1 
HETATM 3278 N N3    . FAD   B 2 .   ? 14.682 -34.236 -16.973 1.00 61.59  ?  501 FAD   A N3    1 
HETATM 3279 C C4    . FAD   B 2 .   ? 13.971 -33.799 -18.064 1.00 61.59  ?  501 FAD   A C4    1 
HETATM 3280 O O4    . FAD   B 2 .   ? 13.411 -34.569 -18.820 1.00 58.96  ?  501 FAD   A O4    1 
HETATM 3281 C C4X   . FAD   B 2 .   ? 13.962 -32.411 -18.211 1.00 65.16  ?  501 FAD   A C4X   1 
HETATM 3282 N N5    . FAD   B 2 .   ? 13.306 -31.935 -19.231 1.00 70.99  ?  501 FAD   A N5    1 
HETATM 3283 C C5X   . FAD   B 2 .   ? 13.283 -30.580 -19.397 1.00 70.31  ?  501 FAD   A C5X   1 
HETATM 3284 C C6    . FAD   B 2 .   ? 12.576 -30.065 -20.497 1.00 69.88  ?  501 FAD   A C6    1 
HETATM 3285 C C7    . FAD   B 2 .   ? 12.513 -28.713 -20.732 1.00 68.73  ?  501 FAD   A C7    1 
HETATM 3286 C C7M   . FAD   B 2 .   ? 11.750 -28.187 -21.918 1.00 64.66  ?  501 FAD   A C7M   1 
HETATM 3287 C C8    . FAD   B 2 .   ? 13.164 -27.825 -19.851 1.00 73.00  ?  501 FAD   A C8    1 
HETATM 3288 C C8M   . FAD   B 2 .   ? 13.095 -26.345 -20.099 1.00 67.17  ?  501 FAD   A C8M   1 
HETATM 3289 C C9    . FAD   B 2 .   ? 13.863 -28.317 -18.769 1.00 66.32  ?  501 FAD   A C9    1 
HETATM 3290 C C9A   . FAD   B 2 .   ? 13.938 -29.696 -18.519 1.00 66.46  ?  501 FAD   A C9A   1 
HETATM 3291 N N10   . FAD   B 2 .   ? 14.627 -30.235 -17.438 1.00 66.34  ?  501 FAD   A N10   1 
HETATM 3292 C C10   . FAD   B 2 .   ? 14.673 -31.606 -17.249 1.00 66.52  ?  501 FAD   A C10   1 
HETATM 3293 C "C1'" . FAD   B 2 .   ? 15.350 -29.355 -16.501 1.00 64.94  ?  501 FAD   A "C1'" 1 
HETATM 3294 C "C2'" . FAD   B 2 .   ? 14.766 -29.175 -15.111 1.00 62.41  ?  501 FAD   A "C2'" 1 
HETATM 3295 O "O2'" . FAD   B 2 .   ? 13.884 -30.234 -14.742 1.00 62.62  ?  501 FAD   A "O2'" 1 
HETATM 3296 C "C3'" . FAD   B 2 .   ? 13.960 -27.889 -15.007 1.00 57.57  ?  501 FAD   A "C3'" 1 
HETATM 3297 O "O3'" . FAD   B 2 .   ? 14.810 -26.771 -15.244 1.00 49.00  ?  501 FAD   A "O3'" 1 
HETATM 3298 C "C4'" . FAD   B 2 .   ? 13.295 -27.828 -13.637 1.00 52.13  ?  501 FAD   A "C4'" 1 
HETATM 3299 O "O4'" . FAD   B 2 .   ? 11.971 -27.310 -13.760 1.00 52.41  ?  501 FAD   A "O4'" 1 
HETATM 3300 C "C5'" . FAD   B 2 .   ? 14.096 -26.978 -12.675 1.00 47.98  ?  501 FAD   A "C5'" 1 
HETATM 3301 O "O5'" . FAD   B 2 .   ? 13.191 -26.202 -11.887 1.00 44.00  ?  501 FAD   A "O5'" 1 
HETATM 3302 P P     . FAD   B 2 .   ? 13.741 -24.873 -11.236 1.00 52.48  ?  501 FAD   A P     1 
HETATM 3303 O O1P   . FAD   B 2 .   ? 15.215 -24.886 -11.376 1.00 47.19  -1 501 FAD   A O1P   1 
HETATM 3304 O O2P   . FAD   B 2 .   ? 13.146 -24.723 -9.889  1.00 46.15  ?  501 FAD   A O2P   1 
HETATM 3305 O O3P   . FAD   B 2 .   ? 13.142 -23.775 -12.216 1.00 51.22  ?  501 FAD   A O3P   1 
HETATM 3306 P PA    . NAP   C 3 .   ? 18.047 -25.627 -27.514 1.00 70.22  ?  502 NAP   A PA    1 
HETATM 3307 O O1A   . NAP   C 3 .   ? 18.972 -24.482 -27.289 1.00 63.09  -1 502 NAP   A O1A   1 
HETATM 3308 O O2A   . NAP   C 3 .   ? 18.484 -26.981 -27.070 1.00 69.99  ?  502 NAP   A O2A   1 
HETATM 3309 O O5B   . NAP   C 3 .   ? 17.636 -25.684 -29.059 1.00 60.53  ?  502 NAP   A O5B   1 
HETATM 3310 C C5B   . NAP   C 3 .   ? 17.971 -24.564 -29.911 1.00 64.17  ?  502 NAP   A C5B   1 
HETATM 3311 C C4B   . NAP   C 3 .   ? 17.872 -24.990 -31.354 1.00 66.84  ?  502 NAP   A C4B   1 
HETATM 3312 O O4B   . NAP   C 3 .   ? 17.584 -23.828 -32.171 1.00 67.07  ?  502 NAP   A O4B   1 
HETATM 3313 C C3B   . NAP   C 3 .   ? 19.135 -25.615 -31.958 1.00 67.81  ?  502 NAP   A C3B   1 
HETATM 3314 O O3B   . NAP   C 3 .   ? 18.800 -26.633 -32.889 1.00 60.99  ?  502 NAP   A O3B   1 
HETATM 3315 C C2B   . NAP   C 3 .   ? 19.806 -24.423 -32.624 1.00 75.16  ?  502 NAP   A C2B   1 
HETATM 3316 O O2B   . NAP   C 3 .   ? 20.618 -24.847 -33.712 1.00 81.76  ?  502 NAP   A O2B   1 
HETATM 3317 C C1B   . NAP   C 3 .   ? 18.595 -23.659 -33.135 1.00 71.85  ?  502 NAP   A C1B   1 
HETATM 3318 N N9A   . NAP   C 3 .   ? 18.849 -22.235 -33.292 1.00 79.36  ?  502 NAP   A N9A   1 
HETATM 3319 C C8A   . NAP   C 3 .   ? 19.224 -21.361 -32.306 1.00 77.90  ?  502 NAP   A C8A   1 
HETATM 3320 N N7A   . NAP   C 3 .   ? 19.393 -20.137 -32.735 1.00 83.74  ?  502 NAP   A N7A   1 
HETATM 3321 C C5A   . NAP   C 3 .   ? 19.118 -20.209 -34.092 1.00 85.25  ?  502 NAP   A C5A   1 
HETATM 3322 C C6A   . NAP   C 3 .   ? 19.123 -19.238 -35.108 1.00 84.85  ?  502 NAP   A C6A   1 
HETATM 3323 N N6A   . NAP   C 3 .   ? 19.436 -17.962 -34.905 1.00 78.36  ?  502 NAP   A N6A   1 
HETATM 3324 N N1A   . NAP   C 3 .   ? 18.799 -19.641 -36.359 1.00 82.23  ?  502 NAP   A N1A   1 
HETATM 3325 C C2A   . NAP   C 3 .   ? 18.493 -20.929 -36.554 1.00 76.39  ?  502 NAP   A C2A   1 
HETATM 3326 N N3A   . NAP   C 3 .   ? 18.458 -21.927 -35.678 1.00 74.65  ?  502 NAP   A N3A   1 
HETATM 3327 C C4A   . NAP   C 3 .   ? 18.784 -21.499 -34.449 1.00 82.14  ?  502 NAP   A C4A   1 
HETATM 3328 O O3    . NAP   C 3 .   ? 16.639 -25.298 -26.833 1.00 58.01  ?  502 NAP   A O3    1 
HETATM 3329 P PN    . NAP   C 3 .   ? 15.339 -26.185 -26.543 1.00 65.30  ?  502 NAP   A PN    1 
HETATM 3330 O O1N   . NAP   C 3 .   ? 14.194 -25.269 -26.292 1.00 55.10  -1 502 NAP   A O1N   1 
HETATM 3331 O O2N   . NAP   C 3 .   ? 15.186 -27.210 -27.609 1.00 63.76  ?  502 NAP   A O2N   1 
HETATM 3332 O O5D   . NAP   C 3 .   ? 15.753 -26.920 -25.186 1.00 72.50  ?  502 NAP   A O5D   1 
HETATM 3333 C C5D   . NAP   C 3 .   ? 15.036 -26.587 -23.976 1.00 76.24  ?  502 NAP   A C5D   1 
HETATM 3334 C C4D   . NAP   C 3 .   ? 16.029 -26.145 -22.935 1.00 78.06  ?  502 NAP   A C4D   1 
HETATM 3335 O O4D   . NAP   C 3 .   ? 16.149 -27.168 -21.926 1.00 74.65  ?  502 NAP   A O4D   1 
HETATM 3336 C C3D   . NAP   C 3 .   ? 17.450 -25.904 -23.462 1.00 79.53  ?  502 NAP   A C3D   1 
HETATM 3337 O O3D   . NAP   C 3 .   ? 17.614 -24.543 -23.832 1.00 68.44  ?  502 NAP   A O3D   1 
HETATM 3338 C C2D   . NAP   C 3 .   ? 18.339 -26.292 -22.276 1.00 83.78  ?  502 NAP   A C2D   1 
HETATM 3339 O O2D   . NAP   C 3 .   ? 18.551 -25.217 -21.375 1.00 74.82  ?  502 NAP   A O2D   1 
HETATM 3340 C C1D   . NAP   C 3 .   ? 17.515 -27.400 -21.611 1.00 79.79  ?  502 NAP   A C1D   1 
HETATM 3341 N N1N   . NAP   C 3 .   ? 17.862 -28.740 -22.103 1.00 87.27  ?  502 NAP   A N1N   1 
HETATM 3342 C C2N   . NAP   C 3 .   ? 17.026 -29.801 -21.846 1.00 85.83  ?  502 NAP   A C2N   1 
HETATM 3343 C C3N   . NAP   C 3 .   ? 17.371 -31.061 -22.321 1.00 93.21  ?  502 NAP   A C3N   1 
HETATM 3344 C C7N   . NAP   C 3 .   ? 16.484 -32.229 -22.039 1.00 90.72  ?  502 NAP   A C7N   1 
HETATM 3345 O O7N   . NAP   C 3 .   ? 16.562 -33.242 -22.751 1.00 84.55  ?  502 NAP   A O7N   1 
HETATM 3346 N N7N   . NAP   C 3 .   ? 15.656 -32.146 -21.009 1.00 85.85  ?  502 NAP   A N7N   1 
HETATM 3347 C C4N   . NAP   C 3 .   ? 18.538 -31.243 -23.046 1.00 93.83  ?  502 NAP   A C4N   1 
HETATM 3348 C C5N   . NAP   C 3 .   ? 19.363 -30.167 -23.295 1.00 92.27  ?  502 NAP   A C5N   1 
HETATM 3349 C C6N   . NAP   C 3 .   ? 19.018 -28.922 -22.821 1.00 90.51  ?  502 NAP   A C6N   1 
HETATM 3350 P P2B   . NAP   C 3 .   ? 22.027 -24.065 -33.796 1.00 94.48  ?  502 NAP   A P2B   1 
HETATM 3351 O O1X   . NAP   C 3 .   ? 22.220 -23.758 -35.261 1.00 93.04  -1 502 NAP   A O1X   1 
HETATM 3352 O O2X   . NAP   C 3 .   ? 21.930 -22.806 -32.969 1.00 86.85  -1 502 NAP   A O2X   1 
HETATM 3353 O O3X   . NAP   C 3 .   ? 23.087 -25.008 -33.274 1.00 82.52  ?  502 NAP   A O3X   1 
HETATM 3354 C CZ3   . A1D7R D 4 .   ? 21.673 -36.527 -22.413 0.89 84.93  ?  503 A1D7R A CZ3   1 
HETATM 3355 C CH2   . A1D7R D 4 .   ? 22.897 -36.039 -22.846 0.89 82.92  ?  503 A1D7R A CH2   1 
HETATM 3356 C CZ2   . A1D7R D 4 .   ? 23.226 -34.705 -22.652 0.89 84.70  ?  503 A1D7R A CZ2   1 
HETATM 3357 C CE2   . A1D7R D 4 .   ? 22.318 -33.845 -22.018 0.89 85.34  ?  503 A1D7R A CE2   1 
HETATM 3358 C CD2   . A1D7R D 4 .   ? 21.108 -34.331 -21.594 0.89 86.34  ?  503 A1D7R A CD2   1 
HETATM 3359 C CE3   . A1D7R D 4 .   ? 20.778 -35.676 -21.786 0.89 87.93  ?  503 A1D7R A CE3   1 
HETATM 3360 C CD1   . A1D7R D 4 .   ? 21.268 -32.163 -21.112 0.89 80.92  ?  503 A1D7R A CD1   1 
HETATM 3361 C CG    . A1D7R D 4 .   ? 20.430 -33.263 -20.996 0.89 85.13  ?  503 A1D7R A CG    1 
HETATM 3362 C CB    . A1D7R D 4 .   ? 19.025 -33.351 -20.407 0.89 81.22  ?  503 A1D7R A CB    1 
HETATM 3363 C CA    . A1D7R D 4 .   ? 18.761 -33.052 -18.941 0.89 79.39  ?  503 A1D7R A CA    1 
HETATM 3364 C C     . A1D7R D 4 .   ? 18.744 -31.563 -18.610 0.89 82.97  ?  503 A1D7R A C     1 
HETATM 3365 C C12   . A1D7R D 4 .   ? 23.883 -36.979 -23.531 0.89 80.65  ?  503 A1D7R A C12   1 
HETATM 3366 C C13   . A1D7R D 4 .   ? 23.430 -38.438 -23.517 0.89 73.72  ?  503 A1D7R A C13   1 
HETATM 3367 C C14   . A1D7R D 4 .   ? 24.513 -39.347 -24.097 0.89 71.81  ?  503 A1D7R A C14   1 
HETATM 3368 C C15   . A1D7R D 4 .   ? 25.143 -38.709 -25.328 0.89 66.14  ?  503 A1D7R A C15   1 
HETATM 3369 C C16   . A1D7R D 4 .   ? 23.976 -40.732 -24.439 0.89 62.83  ?  503 A1D7R A C16   1 
HETATM 3370 N NE1   . A1D7R D 4 .   ? 22.377 -32.544 -21.714 0.89 82.54  ?  503 A1D7R A NE1   1 
HETATM 3371 N N     . A1D7R D 4 .   ? 17.429 -33.545 -18.680 0.89 75.42  ?  503 A1D7R A N     1 
HETATM 3372 O O     . A1D7R D 4 .   ? 18.574 -31.202 -17.417 0.89 80.39  -1 503 A1D7R A O     1 
HETATM 3373 O OXT   . A1D7R D 4 .   ? 18.888 -30.694 -19.502 0.89 87.19  ?  503 A1D7R A OXT   1 
HETATM 3374 O O     . HOH   E 5 .   ? 4.785  -23.554 -24.892 1.00 49.80  ?  601 HOH   A O     1 
HETATM 3375 O O     . HOH   E 5 .   ? 30.728 -13.723 -9.377  1.00 54.09  ?  602 HOH   A O     1 
HETATM 3376 O O     . HOH   E 5 .   ? -0.852 -10.981 -3.498  1.00 74.25  ?  603 HOH   A O     1 
HETATM 3377 O O     . HOH   E 5 .   ? 4.289  -11.767 -40.344 1.00 66.46  ?  604 HOH   A O     1 
HETATM 3378 O O     . HOH   E 5 .   ? 17.421 -22.155 -24.311 1.00 57.78  ?  605 HOH   A O     1 
HETATM 3379 O O     . HOH   E 5 .   ? 0.469  -34.716 -0.102  1.00 44.33  ?  606 HOH   A O     1 
HETATM 3380 O O     . HOH   E 5 .   ? 20.585 -3.619  9.873   1.00 60.50  ?  607 HOH   A O     1 
HETATM 3381 O O     . HOH   E 5 .   ? 10.048 -25.035 -25.284 1.00 43.40  ?  608 HOH   A O     1 
HETATM 3382 O O     . HOH   E 5 .   ? 21.123 -27.288 -35.376 1.00 62.13  ?  609 HOH   A O     1 
HETATM 3383 O O     . HOH   E 5 .   ? 25.699 -29.428 -39.363 1.00 63.28  ?  610 HOH   A O     1 
HETATM 3384 O O     . HOH   E 5 .   ? 20.717 0.444   -9.005  1.00 61.63  ?  611 HOH   A O     1 
HETATM 3385 O O     . HOH   E 5 .   ? 16.442 -30.202 0.052   1.00 35.58  ?  612 HOH   A O     1 
HETATM 3386 O O     . HOH   E 5 .   ? 16.307 -22.823 -10.534 1.00 43.97  ?  613 HOH   A O     1 
HETATM 3387 O O     . HOH   E 5 .   ? 28.167 -14.366 -1.217  1.00 48.44  ?  614 HOH   A O     1 
HETATM 3388 O O     . HOH   E 5 .   ? 14.480 -45.857 -27.741 1.00 49.26  ?  615 HOH   A O     1 
HETATM 3389 O O     . HOH   E 5 .   ? 15.089 -33.922 -0.713  1.00 42.53  ?  616 HOH   A O     1 
HETATM 3390 O O     . HOH   E 5 .   ? 30.509 -30.728 -18.620 1.00 75.61  ?  617 HOH   A O     1 
HETATM 3391 O O     . HOH   E 5 .   ? -3.722 -32.935 -18.194 1.00 51.28  ?  618 HOH   A O     1 
HETATM 3392 O O     . HOH   E 5 .   ? -2.706 -6.525  -0.095  1.00 73.61  ?  619 HOH   A O     1 
HETATM 3393 O O     . HOH   E 5 .   ? 14.475 -28.944 -49.789 1.00 45.18  ?  620 HOH   A O     1 
HETATM 3394 O O     . HOH   E 5 .   ? 12.513 -22.863 -8.135  1.00 42.54  ?  621 HOH   A O     1 
HETATM 3395 O O     . HOH   E 5 .   ? 1.096  -29.014 -15.950 1.00 55.08  ?  622 HOH   A O     1 
HETATM 3396 O O     . HOH   E 5 .   ? 23.652 -22.921 -9.481  1.00 36.43  ?  623 HOH   A O     1 
HETATM 3397 O O     . HOH   E 5 .   ? 26.661 -39.768 -33.971 1.00 58.92  ?  624 HOH   A O     1 
HETATM 3398 O O     . HOH   E 5 .   ? 31.610 -35.225 -0.067  1.00 63.82  ?  625 HOH   A O     1 
HETATM 3399 O O     . HOH   E 5 .   ? 2.958  -27.463 3.374   1.00 47.18  ?  626 HOH   A O     1 
HETATM 3400 O O     . HOH   E 5 .   ? 1.788  -33.547 -40.696 1.00 53.58  ?  627 HOH   A O     1 
HETATM 3401 O O     . HOH   E 5 .   ? 18.634 -24.459 -36.638 1.00 57.06  ?  628 HOH   A O     1 
HETATM 3402 O O     . HOH   E 5 .   ? 8.049  -48.649 -10.092 1.00 50.81  ?  629 HOH   A O     1 
HETATM 3403 O O     . HOH   E 5 .   ? 13.030 -33.169 -47.765 1.00 46.27  ?  630 HOH   A O     1 
HETATM 3404 O O     . HOH   E 5 .   ? 10.163 -26.824 -11.393 1.00 44.89  ?  631 HOH   A O     1 
HETATM 3405 O O     . HOH   E 5 .   ? 12.760 -23.321 -27.998 1.00 42.39  ?  632 HOH   A O     1 
HETATM 3406 O O     . HOH   E 5 .   ? 15.889 -48.840 -17.994 1.00 50.31  ?  633 HOH   A O     1 
HETATM 3407 O O     . HOH   E 5 .   ? 4.482  -21.758 -12.864 1.00 50.66  ?  634 HOH   A O     1 
HETATM 3408 O O     . HOH   E 5 .   ? 26.011 -16.221 7.225   1.00 49.63  ?  635 HOH   A O     1 
HETATM 3409 O O     . HOH   E 5 .   ? 32.495 -44.480 -41.715 1.00 58.65  ?  636 HOH   A O     1 
HETATM 3410 O O     . HOH   E 5 .   ? 15.467 -20.900 -39.987 1.00 44.38  ?  637 HOH   A O     1 
HETATM 3411 O O     . HOH   E 5 .   ? 2.846  -34.389 -43.358 1.00 51.08  ?  638 HOH   A O     1 
HETATM 3412 O O     . HOH   E 5 .   ? 23.412 -23.113 14.394  1.00 62.32  ?  639 HOH   A O     1 
HETATM 3413 O O     . HOH   E 5 .   ? 27.020 -42.244 -34.651 1.00 58.84  ?  640 HOH   A O     1 
HETATM 3414 O O     . HOH   E 5 .   ? 25.696 -15.840 9.992   1.00 45.71  ?  641 HOH   A O     1 
HETATM 3415 O O     . HOH   E 5 .   ? 23.172 -20.629 14.140  1.00 54.82  ?  642 HOH   A O     1 
HETATM 3416 O O     . HOH   E 5 .   ? 15.047 -31.602 -1.512  1.00 41.97  ?  643 HOH   A O     1 
# 
