data_9COW
# 
_entry.id   9COW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9COW         pdb_00009cow 10.2210/pdb9cow/pdb 
WWPDB D_1000285855 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-01-08 ? 
2 'Structure model' 1 1 2025-03-05 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation.pdbx_database_id_DOI'    
5 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
6 2 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9COW 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              sevrioui@uci.edu 
_pdbx_contact_author.name_first         Irina 
_pdbx_contact_author.name_last          Sevrioukova 
_pdbx_contact_author.name_mi            F 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4498-6057 
# 
_audit_author.name               'Sevrioukova, I.F.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   ? 
# 
_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            'Chem.Biol.Drug Des.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1747-0285 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            105 
_citation.language                  ? 
_citation.page_first                e70043 
_citation.page_last                 e70043 
_citation.title                     
'Evaluation of Larger Side-Group Functionalities and the Side/End-Group Interplay in Ritonavir-Like Inhibitors of CYP3A4.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1111/cbdd.70043 
_citation.pdbx_database_id_PubMed   39792691 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Samuels, E.R.'     1 ?                   
primary 'Sevrioukova, I.F.' 2 0000-0002-4498-6057 
# 
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 'Cytochrome P450 3A4' 55757.812 1  1.14.14.1,1.14.14.56,1.14.14.73,1.14.14.55 
'residues 3-22 deleted, C-terminal 4-histidine tag' ? ? 
2 non-polymer nat 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   1  ?                                          ? ? ? 
3 non-polymer syn GLYCEROL 92.094    1  ?                                          ? ? ? 
4 non-polymer syn 
;N-[(2S)-1-(naphthalen-1-yl)-3-{[(2R)-1-oxo-3-phenyl-1-{[3-(pyridin-3-yl)propyl]amino}propan-2-yl]sulfanyl}propan-2-yl]pyridine-3-carboxamide
;
588.762   1  ?                                          ?                                                   ? ? 
5 water       nat water 18.015    40 ?                                          ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;1,4-cineole 2-exo-monooxygenase,8-cineole 2-exo-monooxygenase,Albendazole monooxygenase (sulfoxide-forming),Albendazole sulfoxidase,CYPIIIA3,CYPIIIA4,Cholesterol 25-hydroxylase,Cytochrome P450 3A3,Cytochrome P450 HLp,Cytochrome P450 NF-25,Cytochrome P450-PCN1,Nifedipine oxidase,Quinine 3-monooxygenase
;
# 
_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       
;MAYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYS
VFTNRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYS
MDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVFPREVTNFLRKSVKRMKESR
LEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLP
NKAPPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFS
KKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGGLLQPEKPVVLKVESRDGTV
SGAHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYS
VFTNRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYS
MDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVFPREVTNFLRKSVKRMKESR
LEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLP
NKAPPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFS
KKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGGLLQPEKPVVLKVESRDGTV
SGAHHHH
;
_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 'PROTOPORPHYRIN IX CONTAINING FE' HEM   
3 GLYCEROL GOL   
4 
;N-[(2S)-1-(naphthalen-1-yl)-3-{[(2R)-1-oxo-3-phenyl-1-{[3-(pyridin-3-yl)propyl]amino}propan-2-yl]sulfanyl}propan-2-yl]pyridine-3-carboxamide
;
A1A4V 
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   ALA n 
1 3   TYR n 
1 4   LEU n 
1 5   TYR n 
1 6   GLY n 
1 7   THR n 
1 8   HIS n 
1 9   SER n 
1 10  HIS n 
1 11  GLY n 
1 12  LEU n 
1 13  PHE n 
1 14  LYS n 
1 15  LYS n 
1 16  LEU n 
1 17  GLY n 
1 18  ILE n 
1 19  PRO n 
1 20  GLY n 
1 21  PRO n 
1 22  THR n 
1 23  PRO n 
1 24  LEU n 
1 25  PRO n 
1 26  PHE n 
1 27  LEU n 
1 28  GLY n 
1 29  ASN n 
1 30  ILE n 
1 31  LEU n 
1 32  SER n 
1 33  TYR n 
1 34  HIS n 
1 35  LYS n 
1 36  GLY n 
1 37  PHE n 
1 38  CYS n 
1 39  MET n 
1 40  PHE n 
1 41  ASP n 
1 42  MET n 
1 43  GLU n 
1 44  CYS n 
1 45  HIS n 
1 46  LYS n 
1 47  LYS n 
1 48  TYR n 
1 49  GLY n 
1 50  LYS n 
1 51  VAL n 
1 52  TRP n 
1 53  GLY n 
1 54  PHE n 
1 55  TYR n 
1 56  ASP n 
1 57  GLY n 
1 58  GLN n 
1 59  GLN n 
1 60  PRO n 
1 61  VAL n 
1 62  LEU n 
1 63  ALA n 
1 64  ILE n 
1 65  THR n 
1 66  ASP n 
1 67  PRO n 
1 68  ASP n 
1 69  MET n 
1 70  ILE n 
1 71  LYS n 
1 72  THR n 
1 73  VAL n 
1 74  LEU n 
1 75  VAL n 
1 76  LYS n 
1 77  GLU n 
1 78  CYS n 
1 79  TYR n 
1 80  SER n 
1 81  VAL n 
1 82  PHE n 
1 83  THR n 
1 84  ASN n 
1 85  ARG n 
1 86  ARG n 
1 87  PRO n 
1 88  PHE n 
1 89  GLY n 
1 90  PRO n 
1 91  VAL n 
1 92  GLY n 
1 93  PHE n 
1 94  MET n 
1 95  LYS n 
1 96  SER n 
1 97  ALA n 
1 98  ILE n 
1 99  SER n 
1 100 ILE n 
1 101 ALA n 
1 102 GLU n 
1 103 ASP n 
1 104 GLU n 
1 105 GLU n 
1 106 TRP n 
1 107 LYS n 
1 108 ARG n 
1 109 LEU n 
1 110 ARG n 
1 111 SER n 
1 112 LEU n 
1 113 LEU n 
1 114 SER n 
1 115 PRO n 
1 116 THR n 
1 117 PHE n 
1 118 THR n 
1 119 SER n 
1 120 GLY n 
1 121 LYS n 
1 122 LEU n 
1 123 LYS n 
1 124 GLU n 
1 125 MET n 
1 126 VAL n 
1 127 PRO n 
1 128 ILE n 
1 129 ILE n 
1 130 ALA n 
1 131 GLN n 
1 132 TYR n 
1 133 GLY n 
1 134 ASP n 
1 135 VAL n 
1 136 LEU n 
1 137 VAL n 
1 138 ARG n 
1 139 ASN n 
1 140 LEU n 
1 141 ARG n 
1 142 ARG n 
1 143 GLU n 
1 144 ALA n 
1 145 GLU n 
1 146 THR n 
1 147 GLY n 
1 148 LYS n 
1 149 PRO n 
1 150 VAL n 
1 151 THR n 
1 152 LEU n 
1 153 LYS n 
1 154 ASP n 
1 155 VAL n 
1 156 PHE n 
1 157 GLY n 
1 158 ALA n 
1 159 TYR n 
1 160 SER n 
1 161 MET n 
1 162 ASP n 
1 163 VAL n 
1 164 ILE n 
1 165 THR n 
1 166 SER n 
1 167 THR n 
1 168 SER n 
1 169 PHE n 
1 170 GLY n 
1 171 VAL n 
1 172 ASN n 
1 173 ILE n 
1 174 ASP n 
1 175 SER n 
1 176 LEU n 
1 177 ASN n 
1 178 ASN n 
1 179 PRO n 
1 180 GLN n 
1 181 ASP n 
1 182 PRO n 
1 183 PHE n 
1 184 VAL n 
1 185 GLU n 
1 186 ASN n 
1 187 THR n 
1 188 LYS n 
1 189 LYS n 
1 190 LEU n 
1 191 LEU n 
1 192 ARG n 
1 193 PHE n 
1 194 ASP n 
1 195 PHE n 
1 196 LEU n 
1 197 ASP n 
1 198 PRO n 
1 199 PHE n 
1 200 PHE n 
1 201 LEU n 
1 202 SER n 
1 203 ILE n 
1 204 THR n 
1 205 VAL n 
1 206 PHE n 
1 207 PRO n 
1 208 PHE n 
1 209 LEU n 
1 210 ILE n 
1 211 PRO n 
1 212 ILE n 
1 213 LEU n 
1 214 GLU n 
1 215 VAL n 
1 216 LEU n 
1 217 ASN n 
1 218 ILE n 
1 219 CYS n 
1 220 VAL n 
1 221 PHE n 
1 222 PRO n 
1 223 ARG n 
1 224 GLU n 
1 225 VAL n 
1 226 THR n 
1 227 ASN n 
1 228 PHE n 
1 229 LEU n 
1 230 ARG n 
1 231 LYS n 
1 232 SER n 
1 233 VAL n 
1 234 LYS n 
1 235 ARG n 
1 236 MET n 
1 237 LYS n 
1 238 GLU n 
1 239 SER n 
1 240 ARG n 
1 241 LEU n 
1 242 GLU n 
1 243 ASP n 
1 244 THR n 
1 245 GLN n 
1 246 LYS n 
1 247 HIS n 
1 248 ARG n 
1 249 VAL n 
1 250 ASP n 
1 251 PHE n 
1 252 LEU n 
1 253 GLN n 
1 254 LEU n 
1 255 MET n 
1 256 ILE n 
1 257 ASP n 
1 258 SER n 
1 259 GLN n 
1 260 ASN n 
1 261 SER n 
1 262 LYS n 
1 263 GLU n 
1 264 THR n 
1 265 GLU n 
1 266 SER n 
1 267 HIS n 
1 268 LYS n 
1 269 ALA n 
1 270 LEU n 
1 271 SER n 
1 272 ASP n 
1 273 LEU n 
1 274 GLU n 
1 275 LEU n 
1 276 VAL n 
1 277 ALA n 
1 278 GLN n 
1 279 SER n 
1 280 ILE n 
1 281 ILE n 
1 282 PHE n 
1 283 ILE n 
1 284 PHE n 
1 285 ALA n 
1 286 GLY n 
1 287 TYR n 
1 288 GLU n 
1 289 THR n 
1 290 THR n 
1 291 SER n 
1 292 SER n 
1 293 VAL n 
1 294 LEU n 
1 295 SER n 
1 296 PHE n 
1 297 ILE n 
1 298 MET n 
1 299 TYR n 
1 300 GLU n 
1 301 LEU n 
1 302 ALA n 
1 303 THR n 
1 304 HIS n 
1 305 PRO n 
1 306 ASP n 
1 307 VAL n 
1 308 GLN n 
1 309 GLN n 
1 310 LYS n 
1 311 LEU n 
1 312 GLN n 
1 313 GLU n 
1 314 GLU n 
1 315 ILE n 
1 316 ASP n 
1 317 ALA n 
1 318 VAL n 
1 319 LEU n 
1 320 PRO n 
1 321 ASN n 
1 322 LYS n 
1 323 ALA n 
1 324 PRO n 
1 325 PRO n 
1 326 THR n 
1 327 TYR n 
1 328 ASP n 
1 329 THR n 
1 330 VAL n 
1 331 LEU n 
1 332 GLN n 
1 333 MET n 
1 334 GLU n 
1 335 TYR n 
1 336 LEU n 
1 337 ASP n 
1 338 MET n 
1 339 VAL n 
1 340 VAL n 
1 341 ASN n 
1 342 GLU n 
1 343 THR n 
1 344 LEU n 
1 345 ARG n 
1 346 LEU n 
1 347 PHE n 
1 348 PRO n 
1 349 ILE n 
1 350 ALA n 
1 351 MET n 
1 352 ARG n 
1 353 LEU n 
1 354 GLU n 
1 355 ARG n 
1 356 VAL n 
1 357 CYS n 
1 358 LYS n 
1 359 LYS n 
1 360 ASP n 
1 361 VAL n 
1 362 GLU n 
1 363 ILE n 
1 364 ASN n 
1 365 GLY n 
1 366 MET n 
1 367 PHE n 
1 368 ILE n 
1 369 PRO n 
1 370 LYS n 
1 371 GLY n 
1 372 VAL n 
1 373 VAL n 
1 374 VAL n 
1 375 MET n 
1 376 ILE n 
1 377 PRO n 
1 378 SER n 
1 379 TYR n 
1 380 ALA n 
1 381 LEU n 
1 382 HIS n 
1 383 ARG n 
1 384 ASP n 
1 385 PRO n 
1 386 LYS n 
1 387 TYR n 
1 388 TRP n 
1 389 THR n 
1 390 GLU n 
1 391 PRO n 
1 392 GLU n 
1 393 LYS n 
1 394 PHE n 
1 395 LEU n 
1 396 PRO n 
1 397 GLU n 
1 398 ARG n 
1 399 PHE n 
1 400 SER n 
1 401 LYS n 
1 402 LYS n 
1 403 ASN n 
1 404 LYS n 
1 405 ASP n 
1 406 ASN n 
1 407 ILE n 
1 408 ASP n 
1 409 PRO n 
1 410 TYR n 
1 411 ILE n 
1 412 TYR n 
1 413 THR n 
1 414 PRO n 
1 415 PHE n 
1 416 GLY n 
1 417 SER n 
1 418 GLY n 
1 419 PRO n 
1 420 ARG n 
1 421 ASN n 
1 422 CYS n 
1 423 ILE n 
1 424 GLY n 
1 425 MET n 
1 426 ARG n 
1 427 PHE n 
1 428 ALA n 
1 429 LEU n 
1 430 MET n 
1 431 ASN n 
1 432 MET n 
1 433 LYS n 
1 434 LEU n 
1 435 ALA n 
1 436 LEU n 
1 437 ILE n 
1 438 ARG n 
1 439 VAL n 
1 440 LEU n 
1 441 GLN n 
1 442 ASN n 
1 443 PHE n 
1 444 SER n 
1 445 PHE n 
1 446 LYS n 
1 447 PRO n 
1 448 CYS n 
1 449 LYS n 
1 450 GLU n 
1 451 THR n 
1 452 GLN n 
1 453 ILE n 
1 454 PRO n 
1 455 LEU n 
1 456 LYS n 
1 457 LEU n 
1 458 SER n 
1 459 LEU n 
1 460 GLY n 
1 461 GLY n 
1 462 LEU n 
1 463 LEU n 
1 464 GLN n 
1 465 PRO n 
1 466 GLU n 
1 467 LYS n 
1 468 PRO n 
1 469 VAL n 
1 470 VAL n 
1 471 LEU n 
1 472 LYS n 
1 473 VAL n 
1 474 GLU n 
1 475 SER n 
1 476 ARG n 
1 477 ASP n 
1 478 GLY n 
1 479 THR n 
1 480 VAL n 
1 481 SER n 
1 482 GLY n 
1 483 ALA n 
1 484 HIS n 
1 485 HIS n 
1 486 HIS n 
1 487 HIS 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                   487 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'CYP3A4, CYP3A3' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      '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               'C41 (De3)' 
_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          pcWori 
_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 
A1A4V non-polymer         . 
;N-[(2S)-1-(naphthalen-1-yl)-3-{[(2R)-1-oxo-3-phenyl-1-{[3-(pyridin-3-yl)propyl]amino}propan-2-yl]sulfanyl}propan-2-yl]pyridine-3-carboxamide
;
?                               'C36 H36 N4 O2 S'  588.762 
ALA   'L-peptide linking' y ALANINE ?                               'C3 H7 N O2'       89.093  
ARG   'L-peptide linking' y ARGININE ?                               'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE ?                               'C4 H8 N2 O3'      132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'       133.103 
CYS   'L-peptide linking' y CYSTEINE ?                               'C3 H7 N O2 S'     121.158 
GLN   'L-peptide linking' y GLUTAMINE ?                               'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE ?                               'C2 H5 N O2'       75.067  
GOL   non-polymer         . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'         92.094  
HEM   non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME                            'C34 H32 Fe N4 O4' 616.487 
HIS   'L-peptide linking' y HISTIDINE ?                               'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER ?                               'H2 O'             18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                               'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE ?                               'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE ?                               'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE ?                               'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE ?                               'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE ?                               'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE ?                               'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE ?                               'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?                               'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE ?                               'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE ?                               'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   TYR 3   23  ?   ?   ?   A . n 
A 1 4   LEU 4   24  ?   ?   ?   A . n 
A 1 5   TYR 5   25  ?   ?   ?   A . n 
A 1 6   GLY 6   26  ?   ?   ?   A . n 
A 1 7   THR 7   27  ?   ?   ?   A . n 
A 1 8   HIS 8   28  28  HIS HIS A . n 
A 1 9   SER 9   29  29  SER SER A . n 
A 1 10  HIS 10  30  30  HIS HIS A . n 
A 1 11  GLY 11  31  31  GLY GLY A . n 
A 1 12  LEU 12  32  32  LEU LEU A . n 
A 1 13  PHE 13  33  33  PHE PHE A . n 
A 1 14  LYS 14  34  34  LYS LYS A . n 
A 1 15  LYS 15  35  35  LYS LYS A . n 
A 1 16  LEU 16  36  36  LEU LEU A . n 
A 1 17  GLY 17  37  37  GLY GLY A . n 
A 1 18  ILE 18  38  38  ILE ILE A . n 
A 1 19  PRO 19  39  39  PRO PRO A . n 
A 1 20  GLY 20  40  40  GLY GLY A . n 
A 1 21  PRO 21  41  41  PRO PRO A . n 
A 1 22  THR 22  42  42  THR THR A . n 
A 1 23  PRO 23  43  43  PRO PRO A . n 
A 1 24  LEU 24  44  44  LEU LEU A . n 
A 1 25  PRO 25  45  45  PRO PRO A . n 
A 1 26  PHE 26  46  46  PHE PHE A . n 
A 1 27  LEU 27  47  47  LEU LEU A . n 
A 1 28  GLY 28  48  48  GLY GLY A . n 
A 1 29  ASN 29  49  49  ASN ASN A . n 
A 1 30  ILE 30  50  50  ILE ILE A . n 
A 1 31  LEU 31  51  51  LEU LEU A . n 
A 1 32  SER 32  52  52  SER SER A . n 
A 1 33  TYR 33  53  53  TYR TYR A . n 
A 1 34  HIS 34  54  54  HIS HIS A . n 
A 1 35  LYS 35  55  55  LYS LYS A . n 
A 1 36  GLY 36  56  56  GLY GLY A . n 
A 1 37  PHE 37  57  57  PHE PHE A . n 
A 1 38  CYS 38  58  58  CYS CYS A . n 
A 1 39  MET 39  59  59  MET MET A . n 
A 1 40  PHE 40  60  60  PHE PHE A . n 
A 1 41  ASP 41  61  61  ASP ASP A . n 
A 1 42  MET 42  62  62  MET MET A . n 
A 1 43  GLU 43  63  63  GLU GLU A . n 
A 1 44  CYS 44  64  64  CYS CYS A . n 
A 1 45  HIS 45  65  65  HIS HIS A . n 
A 1 46  LYS 46  66  66  LYS LYS A . n 
A 1 47  LYS 47  67  67  LYS LYS A . n 
A 1 48  TYR 48  68  68  TYR TYR A . n 
A 1 49  GLY 49  69  69  GLY GLY A . n 
A 1 50  LYS 50  70  70  LYS LYS A . n 
A 1 51  VAL 51  71  71  VAL VAL A . n 
A 1 52  TRP 52  72  72  TRP TRP A . n 
A 1 53  GLY 53  73  73  GLY GLY A . n 
A 1 54  PHE 54  74  74  PHE PHE A . n 
A 1 55  TYR 55  75  75  TYR TYR A . n 
A 1 56  ASP 56  76  76  ASP ASP A . n 
A 1 57  GLY 57  77  77  GLY GLY A . n 
A 1 58  GLN 58  78  78  GLN GLN A . n 
A 1 59  GLN 59  79  79  GLN GLN A . n 
A 1 60  PRO 60  80  80  PRO PRO A . n 
A 1 61  VAL 61  81  81  VAL VAL A . n 
A 1 62  LEU 62  82  82  LEU LEU A . n 
A 1 63  ALA 63  83  83  ALA ALA A . n 
A 1 64  ILE 64  84  84  ILE ILE A . n 
A 1 65  THR 65  85  85  THR THR A . n 
A 1 66  ASP 66  86  86  ASP ASP A . n 
A 1 67  PRO 67  87  87  PRO PRO A . n 
A 1 68  ASP 68  88  88  ASP ASP A . n 
A 1 69  MET 69  89  89  MET MET A . n 
A 1 70  ILE 70  90  90  ILE ILE A . n 
A 1 71  LYS 71  91  91  LYS LYS A . n 
A 1 72  THR 72  92  92  THR THR A . n 
A 1 73  VAL 73  93  93  VAL VAL A . n 
A 1 74  LEU 74  94  94  LEU LEU A . n 
A 1 75  VAL 75  95  95  VAL VAL A . n 
A 1 76  LYS 76  96  96  LYS LYS A . n 
A 1 77  GLU 77  97  97  GLU GLU A . n 
A 1 78  CYS 78  98  98  CYS CYS A . n 
A 1 79  TYR 79  99  99  TYR TYR A . n 
A 1 80  SER 80  100 100 SER SER A . n 
A 1 81  VAL 81  101 101 VAL VAL A . n 
A 1 82  PHE 82  102 102 PHE PHE A . n 
A 1 83  THR 83  103 103 THR THR A . n 
A 1 84  ASN 84  104 104 ASN ASN A . n 
A 1 85  ARG 85  105 105 ARG ARG A . n 
A 1 86  ARG 86  106 106 ARG ARG A . n 
A 1 87  PRO 87  107 107 PRO PRO A . n 
A 1 88  PHE 88  108 108 PHE PHE A . n 
A 1 89  GLY 89  109 109 GLY GLY A . n 
A 1 90  PRO 90  110 110 PRO PRO A . n 
A 1 91  VAL 91  111 111 VAL VAL A . n 
A 1 92  GLY 92  112 112 GLY GLY A . n 
A 1 93  PHE 93  113 113 PHE PHE A . n 
A 1 94  MET 94  114 114 MET MET A . n 
A 1 95  LYS 95  115 115 LYS LYS A . n 
A 1 96  SER 96  116 116 SER SER A . n 
A 1 97  ALA 97  117 117 ALA ALA A . n 
A 1 98  ILE 98  118 118 ILE ILE A . n 
A 1 99  SER 99  119 119 SER SER A . n 
A 1 100 ILE 100 120 120 ILE ILE A . n 
A 1 101 ALA 101 121 121 ALA ALA A . n 
A 1 102 GLU 102 122 122 GLU GLU A . n 
A 1 103 ASP 103 123 123 ASP ASP A . n 
A 1 104 GLU 104 124 124 GLU GLU A . n 
A 1 105 GLU 105 125 125 GLU GLU A . n 
A 1 106 TRP 106 126 126 TRP TRP A . n 
A 1 107 LYS 107 127 127 LYS LYS A . n 
A 1 108 ARG 108 128 128 ARG ARG A . n 
A 1 109 LEU 109 129 129 LEU LEU A . n 
A 1 110 ARG 110 130 130 ARG ARG A . n 
A 1 111 SER 111 131 131 SER SER A . n 
A 1 112 LEU 112 132 132 LEU LEU A . n 
A 1 113 LEU 113 133 133 LEU LEU A . n 
A 1 114 SER 114 134 134 SER SER A . n 
A 1 115 PRO 115 135 135 PRO PRO A . n 
A 1 116 THR 116 136 136 THR THR A . n 
A 1 117 PHE 117 137 137 PHE PHE A . n 
A 1 118 THR 118 138 138 THR THR A . n 
A 1 119 SER 119 139 139 SER SER A . n 
A 1 120 GLY 120 140 140 GLY GLY A . n 
A 1 121 LYS 121 141 141 LYS LYS A . n 
A 1 122 LEU 122 142 142 LEU LEU A . n 
A 1 123 LYS 123 143 143 LYS LYS A . n 
A 1 124 GLU 124 144 144 GLU GLU A . n 
A 1 125 MET 125 145 145 MET MET A . n 
A 1 126 VAL 126 146 146 VAL VAL A . n 
A 1 127 PRO 127 147 147 PRO PRO A . n 
A 1 128 ILE 128 148 148 ILE ILE A . n 
A 1 129 ILE 129 149 149 ILE ILE A . n 
A 1 130 ALA 130 150 150 ALA ALA A . n 
A 1 131 GLN 131 151 151 GLN GLN A . n 
A 1 132 TYR 132 152 152 TYR TYR A . n 
A 1 133 GLY 133 153 153 GLY GLY A . n 
A 1 134 ASP 134 154 154 ASP ASP A . n 
A 1 135 VAL 135 155 155 VAL VAL A . n 
A 1 136 LEU 136 156 156 LEU LEU A . n 
A 1 137 VAL 137 157 157 VAL VAL A . n 
A 1 138 ARG 138 158 158 ARG ARG A . n 
A 1 139 ASN 139 159 159 ASN ASN A . n 
A 1 140 LEU 140 160 160 LEU LEU A . n 
A 1 141 ARG 141 161 161 ARG ARG A . n 
A 1 142 ARG 142 162 162 ARG ARG A . n 
A 1 143 GLU 143 163 163 GLU GLU A . n 
A 1 144 ALA 144 164 164 ALA ALA A . n 
A 1 145 GLU 145 165 165 GLU GLU A . n 
A 1 146 THR 146 166 ?   ?   ?   A . n 
A 1 147 GLY 147 167 ?   ?   ?   A . n 
A 1 148 LYS 148 168 ?   ?   ?   A . n 
A 1 149 PRO 149 169 169 PRO PRO A . n 
A 1 150 VAL 150 170 170 VAL VAL A . n 
A 1 151 THR 151 171 171 THR THR A . n 
A 1 152 LEU 152 172 172 LEU LEU A . n 
A 1 153 LYS 153 173 173 LYS LYS A . n 
A 1 154 ASP 154 174 174 ASP ASP A . n 
A 1 155 VAL 155 175 175 VAL VAL A . n 
A 1 156 PHE 156 176 176 PHE PHE A . n 
A 1 157 GLY 157 177 177 GLY GLY A . n 
A 1 158 ALA 158 178 178 ALA ALA A . n 
A 1 159 TYR 159 179 179 TYR TYR A . n 
A 1 160 SER 160 180 180 SER SER A . n 
A 1 161 MET 161 181 181 MET MET A . n 
A 1 162 ASP 162 182 182 ASP ASP A . n 
A 1 163 VAL 163 183 183 VAL VAL A . n 
A 1 164 ILE 164 184 184 ILE ILE A . n 
A 1 165 THR 165 185 185 THR THR A . n 
A 1 166 SER 166 186 186 SER SER A . n 
A 1 167 THR 167 187 187 THR THR A . n 
A 1 168 SER 168 188 188 SER SER A . n 
A 1 169 PHE 169 189 189 PHE PHE A . n 
A 1 170 GLY 170 190 190 GLY GLY A . n 
A 1 171 VAL 171 191 191 VAL VAL A . n 
A 1 172 ASN 172 192 192 ASN ASN A . n 
A 1 173 ILE 173 193 193 ILE ILE A . n 
A 1 174 ASP 174 194 194 ASP ASP A . n 
A 1 175 SER 175 195 195 SER SER A . n 
A 1 176 LEU 176 196 196 LEU LEU A . n 
A 1 177 ASN 177 197 197 ASN ASN A . n 
A 1 178 ASN 178 198 198 ASN ASN A . n 
A 1 179 PRO 179 199 199 PRO PRO A . n 
A 1 180 GLN 180 200 200 GLN GLN A . n 
A 1 181 ASP 181 201 201 ASP ASP A . n 
A 1 182 PRO 182 202 202 PRO PRO A . n 
A 1 183 PHE 183 203 203 PHE PHE A . n 
A 1 184 VAL 184 204 ?   ?   ?   A . n 
A 1 185 GLU 185 205 ?   ?   ?   A . n 
A 1 186 ASN 186 206 ?   ?   ?   A . n 
A 1 187 THR 187 207 ?   ?   ?   A . n 
A 1 188 LYS 188 208 ?   ?   ?   A . n 
A 1 189 LYS 189 209 ?   ?   ?   A . n 
A 1 190 LEU 190 210 ?   ?   ?   A . n 
A 1 191 LEU 191 211 ?   ?   ?   A . n 
A 1 192 ARG 192 212 ?   ?   ?   A . n 
A 1 193 PHE 193 213 ?   ?   ?   A . n 
A 1 194 ASP 194 214 ?   ?   ?   A . n 
A 1 195 PHE 195 215 ?   ?   ?   A . n 
A 1 196 LEU 196 216 ?   ?   ?   A . n 
A 1 197 ASP 197 217 ?   ?   ?   A . n 
A 1 198 PRO 198 218 218 PRO PRO A . n 
A 1 199 PHE 199 219 219 PHE PHE A . n 
A 1 200 PHE 200 220 220 PHE PHE A . n 
A 1 201 LEU 201 221 221 LEU LEU A . n 
A 1 202 SER 202 222 222 SER SER A . n 
A 1 203 ILE 203 223 223 ILE ILE A . n 
A 1 204 THR 204 224 224 THR THR A . n 
A 1 205 VAL 205 225 225 VAL VAL A . n 
A 1 206 PHE 206 226 226 PHE PHE A . n 
A 1 207 PRO 207 227 227 PRO PRO A . n 
A 1 208 PHE 208 228 228 PHE PHE A . n 
A 1 209 LEU 209 229 229 LEU LEU A . n 
A 1 210 ILE 210 230 230 ILE ILE A . n 
A 1 211 PRO 211 231 231 PRO PRO A . n 
A 1 212 ILE 212 232 232 ILE ILE A . n 
A 1 213 LEU 213 233 233 LEU LEU A . n 
A 1 214 GLU 214 234 234 GLU GLU A . n 
A 1 215 VAL 215 235 235 VAL VAL A . n 
A 1 216 LEU 216 236 236 LEU LEU A . n 
A 1 217 ASN 217 237 237 ASN ASN A . n 
A 1 218 ILE 218 238 238 ILE ILE A . n 
A 1 219 CYS 219 239 239 CYS CYS A . n 
A 1 220 VAL 220 240 ?   ?   ?   A . n 
A 1 221 PHE 221 241 ?   ?   ?   A . n 
A 1 222 PRO 222 242 ?   ?   ?   A . n 
A 1 223 ARG 223 243 ?   ?   ?   A . n 
A 1 224 GLU 224 244 ?   ?   ?   A . n 
A 1 225 VAL 225 245 ?   ?   ?   A . n 
A 1 226 THR 226 246 246 THR THR A . n 
A 1 227 ASN 227 247 247 ASN ASN A . n 
A 1 228 PHE 228 248 248 PHE PHE A . n 
A 1 229 LEU 229 249 249 LEU LEU A . n 
A 1 230 ARG 230 250 250 ARG ARG A . n 
A 1 231 LYS 231 251 251 LYS LYS A . n 
A 1 232 SER 232 252 252 SER SER A . n 
A 1 233 VAL 233 253 253 VAL VAL A . n 
A 1 234 LYS 234 254 254 LYS LYS A . n 
A 1 235 ARG 235 255 255 ARG ARG A . n 
A 1 236 MET 236 256 256 MET MET A . n 
A 1 237 LYS 237 257 257 LYS LYS A . n 
A 1 238 GLU 238 258 258 GLU GLU A . n 
A 1 239 SER 239 259 259 SER SER A . n 
A 1 240 ARG 240 260 ?   ?   ?   A . n 
A 1 241 LEU 241 261 ?   ?   ?   A . n 
A 1 242 GLU 242 262 ?   ?   ?   A . n 
A 1 243 ASP 243 263 ?   ?   ?   A . n 
A 1 244 THR 244 264 ?   ?   ?   A . n 
A 1 245 GLN 245 265 ?   ?   ?   A . n 
A 1 246 LYS 246 266 ?   ?   ?   A . n 
A 1 247 HIS 247 267 ?   ?   ?   A . n 
A 1 248 ARG 248 268 ?   ?   ?   A . n 
A 1 249 VAL 249 269 ?   ?   ?   A . n 
A 1 250 ASP 250 270 270 ASP ASP A . n 
A 1 251 PHE 251 271 271 PHE PHE A . n 
A 1 252 LEU 252 272 272 LEU LEU A . n 
A 1 253 GLN 253 273 273 GLN GLN A . n 
A 1 254 LEU 254 274 274 LEU LEU A . n 
A 1 255 MET 255 275 275 MET MET A . n 
A 1 256 ILE 256 276 276 ILE ILE A . n 
A 1 257 ASP 257 277 277 ASP ASP A . n 
A 1 258 SER 258 278 278 SER SER A . n 
A 1 259 GLN 259 279 ?   ?   ?   A . n 
A 1 260 ASN 260 280 ?   ?   ?   A . n 
A 1 261 SER 261 281 ?   ?   ?   A . n 
A 1 262 LYS 262 282 ?   ?   ?   A . n 
A 1 263 GLU 263 283 ?   ?   ?   A . n 
A 1 264 THR 264 284 ?   ?   ?   A . n 
A 1 265 GLU 265 285 ?   ?   ?   A . n 
A 1 266 SER 266 286 286 SER SER A . n 
A 1 267 HIS 267 287 287 HIS HIS A . n 
A 1 268 LYS 268 288 288 LYS LYS A . n 
A 1 269 ALA 269 289 289 ALA ALA A . n 
A 1 270 LEU 270 290 290 LEU LEU A . n 
A 1 271 SER 271 291 291 SER SER A . n 
A 1 272 ASP 272 292 292 ASP ASP A . n 
A 1 273 LEU 273 293 293 LEU LEU A . n 
A 1 274 GLU 274 294 294 GLU GLU A . n 
A 1 275 LEU 275 295 295 LEU LEU A . n 
A 1 276 VAL 276 296 296 VAL VAL A . n 
A 1 277 ALA 277 297 297 ALA ALA A . n 
A 1 278 GLN 278 298 298 GLN GLN A . n 
A 1 279 SER 279 299 299 SER SER A . n 
A 1 280 ILE 280 300 300 ILE ILE A . n 
A 1 281 ILE 281 301 301 ILE ILE A . n 
A 1 282 PHE 282 302 302 PHE PHE A . n 
A 1 283 ILE 283 303 303 ILE ILE A . n 
A 1 284 PHE 284 304 304 PHE PHE A . n 
A 1 285 ALA 285 305 305 ALA ALA A . n 
A 1 286 GLY 286 306 306 GLY GLY A . n 
A 1 287 TYR 287 307 307 TYR TYR A . n 
A 1 288 GLU 288 308 308 GLU GLU A . n 
A 1 289 THR 289 309 309 THR THR A . n 
A 1 290 THR 290 310 310 THR THR A . n 
A 1 291 SER 291 311 311 SER SER A . n 
A 1 292 SER 292 312 312 SER SER A . n 
A 1 293 VAL 293 313 313 VAL VAL A . n 
A 1 294 LEU 294 314 314 LEU LEU A . n 
A 1 295 SER 295 315 315 SER SER A . n 
A 1 296 PHE 296 316 316 PHE PHE A . n 
A 1 297 ILE 297 317 317 ILE ILE A . n 
A 1 298 MET 298 318 318 MET MET A . n 
A 1 299 TYR 299 319 319 TYR TYR A . n 
A 1 300 GLU 300 320 320 GLU GLU A . n 
A 1 301 LEU 301 321 321 LEU LEU A . n 
A 1 302 ALA 302 322 322 ALA ALA A . n 
A 1 303 THR 303 323 323 THR THR A . n 
A 1 304 HIS 304 324 324 HIS HIS A . n 
A 1 305 PRO 305 325 325 PRO PRO A . n 
A 1 306 ASP 306 326 326 ASP ASP A . n 
A 1 307 VAL 307 327 327 VAL VAL A . n 
A 1 308 GLN 308 328 328 GLN GLN A . n 
A 1 309 GLN 309 329 329 GLN GLN A . n 
A 1 310 LYS 310 330 330 LYS LYS A . n 
A 1 311 LEU 311 331 331 LEU LEU A . n 
A 1 312 GLN 312 332 332 GLN GLN A . n 
A 1 313 GLU 313 333 333 GLU GLU A . n 
A 1 314 GLU 314 334 334 GLU GLU A . n 
A 1 315 ILE 315 335 335 ILE ILE A . n 
A 1 316 ASP 316 336 336 ASP ASP A . n 
A 1 317 ALA 317 337 337 ALA ALA A . n 
A 1 318 VAL 318 338 338 VAL VAL A . n 
A 1 319 LEU 319 339 339 LEU LEU A . n 
A 1 320 PRO 320 340 340 PRO PRO A . n 
A 1 321 ASN 321 341 341 ASN ASN A . n 
A 1 322 LYS 322 342 342 LYS LYS A . n 
A 1 323 ALA 323 343 343 ALA ALA A . n 
A 1 324 PRO 324 344 344 PRO PRO A . n 
A 1 325 PRO 325 345 345 PRO PRO A . n 
A 1 326 THR 326 346 346 THR THR A . n 
A 1 327 TYR 327 347 347 TYR TYR A . n 
A 1 328 ASP 328 348 348 ASP ASP A . n 
A 1 329 THR 329 349 349 THR THR A . n 
A 1 330 VAL 330 350 350 VAL VAL A . n 
A 1 331 LEU 331 351 351 LEU LEU A . n 
A 1 332 GLN 332 352 352 GLN GLN A . n 
A 1 333 MET 333 353 353 MET MET A . n 
A 1 334 GLU 334 354 354 GLU GLU A . n 
A 1 335 TYR 335 355 355 TYR TYR A . n 
A 1 336 LEU 336 356 356 LEU LEU A . n 
A 1 337 ASP 337 357 357 ASP ASP A . n 
A 1 338 MET 338 358 358 MET MET A . n 
A 1 339 VAL 339 359 359 VAL VAL A . n 
A 1 340 VAL 340 360 360 VAL VAL A . n 
A 1 341 ASN 341 361 361 ASN ASN A . n 
A 1 342 GLU 342 362 362 GLU GLU A . n 
A 1 343 THR 343 363 363 THR THR A . n 
A 1 344 LEU 344 364 364 LEU LEU A . n 
A 1 345 ARG 345 365 365 ARG ARG A . n 
A 1 346 LEU 346 366 366 LEU LEU A . n 
A 1 347 PHE 347 367 367 PHE PHE A . n 
A 1 348 PRO 348 368 368 PRO PRO A . n 
A 1 349 ILE 349 369 369 ILE ILE A . n 
A 1 350 ALA 350 370 370 ALA ALA A . n 
A 1 351 MET 351 371 371 MET MET A . n 
A 1 352 ARG 352 372 372 ARG ARG A . n 
A 1 353 LEU 353 373 373 LEU LEU A . n 
A 1 354 GLU 354 374 374 GLU GLU A . n 
A 1 355 ARG 355 375 375 ARG ARG A . n 
A 1 356 VAL 356 376 376 VAL VAL A . n 
A 1 357 CYS 357 377 377 CYS CYS A . n 
A 1 358 LYS 358 378 378 LYS LYS A . n 
A 1 359 LYS 359 379 379 LYS LYS A . n 
A 1 360 ASP 360 380 380 ASP ASP A . n 
A 1 361 VAL 361 381 381 VAL VAL A . n 
A 1 362 GLU 362 382 382 GLU GLU A . n 
A 1 363 ILE 363 383 383 ILE ILE A . n 
A 1 364 ASN 364 384 384 ASN ASN A . n 
A 1 365 GLY 365 385 385 GLY GLY A . n 
A 1 366 MET 366 386 386 MET MET A . n 
A 1 367 PHE 367 387 387 PHE PHE A . n 
A 1 368 ILE 368 388 388 ILE ILE A . n 
A 1 369 PRO 369 389 389 PRO PRO A . n 
A 1 370 LYS 370 390 390 LYS LYS A . n 
A 1 371 GLY 371 391 391 GLY GLY A . n 
A 1 372 VAL 372 392 392 VAL VAL A . n 
A 1 373 VAL 373 393 393 VAL VAL A . n 
A 1 374 VAL 374 394 394 VAL VAL A . n 
A 1 375 MET 375 395 395 MET MET A . n 
A 1 376 ILE 376 396 396 ILE ILE A . n 
A 1 377 PRO 377 397 397 PRO PRO A . n 
A 1 378 SER 378 398 398 SER SER A . n 
A 1 379 TYR 379 399 399 TYR TYR A . n 
A 1 380 ALA 380 400 400 ALA ALA A . n 
A 1 381 LEU 381 401 401 LEU LEU A . n 
A 1 382 HIS 382 402 402 HIS HIS A . n 
A 1 383 ARG 383 403 403 ARG ARG A . n 
A 1 384 ASP 384 404 404 ASP ASP A . n 
A 1 385 PRO 385 405 405 PRO PRO A . n 
A 1 386 LYS 386 406 406 LYS LYS A . n 
A 1 387 TYR 387 407 407 TYR TYR A . n 
A 1 388 TRP 388 408 408 TRP TRP A . n 
A 1 389 THR 389 409 409 THR THR A . n 
A 1 390 GLU 390 410 410 GLU GLU A . n 
A 1 391 PRO 391 411 411 PRO PRO A . n 
A 1 392 GLU 392 412 412 GLU GLU A . n 
A 1 393 LYS 393 413 413 LYS LYS A . n 
A 1 394 PHE 394 414 414 PHE PHE A . n 
A 1 395 LEU 395 415 415 LEU LEU A . n 
A 1 396 PRO 396 416 416 PRO PRO A . n 
A 1 397 GLU 397 417 417 GLU GLU A . n 
A 1 398 ARG 398 418 418 ARG ARG A . n 
A 1 399 PHE 399 419 419 PHE PHE A . n 
A 1 400 SER 400 420 420 SER SER A . n 
A 1 401 LYS 401 421 421 LYS LYS A . n 
A 1 402 LYS 402 422 422 LYS LYS A . n 
A 1 403 ASN 403 423 423 ASN ASN A . n 
A 1 404 LYS 404 424 424 LYS LYS A . n 
A 1 405 ASP 405 425 425 ASP ASP A . n 
A 1 406 ASN 406 426 426 ASN ASN A . n 
A 1 407 ILE 407 427 427 ILE ILE A . n 
A 1 408 ASP 408 428 428 ASP ASP A . n 
A 1 409 PRO 409 429 429 PRO PRO A . n 
A 1 410 TYR 410 430 430 TYR TYR A . n 
A 1 411 ILE 411 431 431 ILE ILE A . n 
A 1 412 TYR 412 432 432 TYR TYR A . n 
A 1 413 THR 413 433 433 THR THR A . n 
A 1 414 PRO 414 434 434 PRO PRO A . n 
A 1 415 PHE 415 435 435 PHE PHE A . n 
A 1 416 GLY 416 436 436 GLY GLY A . n 
A 1 417 SER 417 437 437 SER SER A . n 
A 1 418 GLY 418 438 438 GLY GLY A . n 
A 1 419 PRO 419 439 439 PRO PRO A . n 
A 1 420 ARG 420 440 440 ARG ARG A . n 
A 1 421 ASN 421 441 441 ASN ASN A . n 
A 1 422 CYS 422 442 442 CYS CYS A . n 
A 1 423 ILE 423 443 443 ILE ILE A . n 
A 1 424 GLY 424 444 444 GLY GLY A . n 
A 1 425 MET 425 445 445 MET MET A . n 
A 1 426 ARG 426 446 446 ARG ARG A . n 
A 1 427 PHE 427 447 447 PHE PHE A . n 
A 1 428 ALA 428 448 448 ALA ALA A . n 
A 1 429 LEU 429 449 449 LEU LEU A . n 
A 1 430 MET 430 450 450 MET MET A . n 
A 1 431 ASN 431 451 451 ASN ASN A . n 
A 1 432 MET 432 452 452 MET MET A . n 
A 1 433 LYS 433 453 453 LYS LYS A . n 
A 1 434 LEU 434 454 454 LEU LEU A . n 
A 1 435 ALA 435 455 455 ALA ALA A . n 
A 1 436 LEU 436 456 456 LEU LEU A . n 
A 1 437 ILE 437 457 457 ILE ILE A . n 
A 1 438 ARG 438 458 458 ARG ARG A . n 
A 1 439 VAL 439 459 459 VAL VAL A . n 
A 1 440 LEU 440 460 460 LEU LEU A . n 
A 1 441 GLN 441 461 461 GLN GLN A . n 
A 1 442 ASN 442 462 462 ASN ASN A . n 
A 1 443 PHE 443 463 463 PHE PHE A . n 
A 1 444 SER 444 464 464 SER SER A . n 
A 1 445 PHE 445 465 465 PHE PHE A . n 
A 1 446 LYS 446 466 466 LYS LYS A . n 
A 1 447 PRO 447 467 467 PRO PRO A . n 
A 1 448 CYS 448 468 468 CYS CYS A . n 
A 1 449 LYS 449 469 469 LYS LYS A . n 
A 1 450 GLU 450 470 470 GLU GLU A . n 
A 1 451 THR 451 471 471 THR THR A . n 
A 1 452 GLN 452 472 472 GLN GLN A . n 
A 1 453 ILE 453 473 473 ILE ILE A . n 
A 1 454 PRO 454 474 474 PRO PRO A . n 
A 1 455 LEU 455 475 475 LEU LEU A . n 
A 1 456 LYS 456 476 476 LYS LYS A . n 
A 1 457 LEU 457 477 477 LEU LEU A . n 
A 1 458 SER 458 478 478 SER SER A . n 
A 1 459 LEU 459 479 479 LEU LEU A . n 
A 1 460 GLY 460 480 480 GLY GLY A . n 
A 1 461 GLY 461 481 481 GLY GLY A . n 
A 1 462 LEU 462 482 482 LEU LEU A . n 
A 1 463 LEU 463 483 483 LEU LEU A . n 
A 1 464 GLN 464 484 484 GLN GLN A . n 
A 1 465 PRO 465 485 485 PRO PRO A . n 
A 1 466 GLU 466 486 486 GLU GLU A . n 
A 1 467 LYS 467 487 487 LYS LYS A . n 
A 1 468 PRO 468 488 488 PRO PRO A . n 
A 1 469 VAL 469 489 489 VAL VAL A . n 
A 1 470 VAL 470 490 490 VAL VAL A . n 
A 1 471 LEU 471 491 491 LEU LEU A . n 
A 1 472 LYS 472 492 492 LYS LYS A . n 
A 1 473 VAL 473 493 493 VAL VAL A . n 
A 1 474 GLU 474 494 494 GLU GLU A . n 
A 1 475 SER 475 495 495 SER SER A . n 
A 1 476 ARG 476 496 496 ARG ARG A . n 
A 1 477 ASP 477 497 ?   ?   ?   A . n 
A 1 478 GLY 478 498 ?   ?   ?   A . n 
A 1 479 THR 479 499 ?   ?   ?   A . n 
A 1 480 VAL 480 500 ?   ?   ?   A . n 
A 1 481 SER 481 501 ?   ?   ?   A . n 
A 1 482 GLY 482 502 ?   ?   ?   A . n 
A 1 483 ALA 483 503 ?   ?   ?   A . n 
A 1 484 HIS 484 504 ?   ?   ?   A . n 
A 1 485 HIS 485 505 ?   ?   ?   A . n 
A 1 486 HIS 486 506 ?   ?   ?   A . n 
A 1 487 HIS 487 507 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A4V 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A4V 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 HEM   1  601 500 HEM   HEM A . 
C 3 GOL   1  602 600 GOL   GOL A . 
D 4 A1A4V 1  603 700 A1A4V 422 A . 
E 5 HOH   1  701 1   HOH   HOH A . 
E 5 HOH   2  702 33  HOH   HOH A . 
E 5 HOH   3  703 13  HOH   HOH A . 
E 5 HOH   4  704 27  HOH   HOH A . 
E 5 HOH   5  705 6   HOH   HOH A . 
E 5 HOH   6  706 16  HOH   HOH A . 
E 5 HOH   7  707 39  HOH   HOH A . 
E 5 HOH   8  708 40  HOH   HOH A . 
E 5 HOH   9  709 11  HOH   HOH A . 
E 5 HOH   10 710 24  HOH   HOH A . 
E 5 HOH   11 711 2   HOH   HOH A . 
E 5 HOH   12 712 20  HOH   HOH A . 
E 5 HOH   13 713 29  HOH   HOH A . 
E 5 HOH   14 714 3   HOH   HOH A . 
E 5 HOH   15 715 41  HOH   HOH A . 
E 5 HOH   16 716 31  HOH   HOH A . 
E 5 HOH   17 717 38  HOH   HOH A . 
E 5 HOH   18 718 17  HOH   HOH A . 
E 5 HOH   19 719 21  HOH   HOH A . 
E 5 HOH   20 720 25  HOH   HOH A . 
E 5 HOH   21 721 37  HOH   HOH A . 
E 5 HOH   22 722 5   HOH   HOH A . 
E 5 HOH   23 723 18  HOH   HOH A . 
E 5 HOH   24 724 8   HOH   HOH A . 
E 5 HOH   25 725 22  HOH   HOH A . 
E 5 HOH   26 726 14  HOH   HOH A . 
E 5 HOH   27 727 7   HOH   HOH A . 
E 5 HOH   28 728 30  HOH   HOH A . 
E 5 HOH   29 729 12  HOH   HOH A . 
E 5 HOH   30 730 19  HOH   HOH A . 
E 5 HOH   31 731 10  HOH   HOH A . 
E 5 HOH   32 732 28  HOH   HOH A . 
E 5 HOH   33 733 4   HOH   HOH A . 
E 5 HOH   34 734 32  HOH   HOH A . 
E 5 HOH   35 735 23  HOH   HOH A . 
E 5 HOH   36 736 35  HOH   HOH A . 
E 5 HOH   37 737 36  HOH   HOH A . 
E 5 HOH   38 738 26  HOH   HOH A . 
E 5 HOH   39 739 15  HOH   HOH A . 
E 5 HOH   40 740 34  HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9COW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     76.190 
_cell.length_a_esd                 ? 
_cell.length_b                     100.090 
_cell.length_b_esd                 ? 
_cell.length_c                     121.460 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9COW 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 2 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                   9COW 
_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             2.08 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.76 
_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              7.5 
_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    'PEG 8000, 1,5-pentanediol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     103 
_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                      mirrors 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 300K' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-05-15 
_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   0.98 
_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                        'SSRL BEAMLINE BL12-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.98 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9COW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.30 
_reflns.d_resolution_low                               64.54 
_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                                     20931 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.027 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.055 
_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                                    2.30 
_reflns_shell.d_res_low                                     2.42 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.0 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3003 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.860 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.508 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.772 
_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                                 9COW 
_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                            2.30 
_refine.ls_d_res_low                             50.04 
_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                     20903 
_refine.ls_number_reflns_R_free                  1028 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.50 
_refine.ls_percent_reflns_R_free                 4.92 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2621 
_refine.ls_R_factor_R_free                       0.2818 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2612 
_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                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 36.73 
_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                            0.41 
_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                       2.30 
_refine_hist.d_res_low                        50.04 
_refine_hist.number_atoms_solvent             40 
_refine_hist.number_atoms_total               3573 
_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        3441 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         92 
_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' ? 0.003  ? 3668 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.573  ? 4970 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.296 ? 1384 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.040  ? 542  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 621  ? 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' 2.30 2.42  . . 150 2783 99.00  . . . . 0.4027 . . . . . . . . . . . 0.4308 
'X-RAY DIFFRACTION' 2.42 2.57  . . 144 2804 99.00  . . . . 0.3632 . . . . . . . . . . . 0.3836 
'X-RAY DIFFRACTION' 2.57 2.77  . . 166 2771 100.00 . . . . 0.3480 . . . . . . . . . . . 0.3781 
'X-RAY DIFFRACTION' 2.77 3.05  . . 144 2825 100.00 . . . . 0.3348 . . . . . . . . . . . 0.3804 
'X-RAY DIFFRACTION' 3.05 3.49  . . 147 2847 100.00 . . . . 0.2995 . . . . . . . . . . . 0.3672 
'X-RAY DIFFRACTION' 3.49 4.40  . . 132 2868 100.00 . . . . 0.2550 . . . . . . . . . . . 0.2850 
'X-RAY DIFFRACTION' 4.40 50.04 . . 145 2977 99.00  . . . . 0.2307 . . . . . . . . . . . 0.2310 
# 
_struct.entry_id                     9COW 
_struct.title                        'Crystal structure of CYP3A4 bound to an inhibitor' 
_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        9COW 
_struct_keywords.text            'cytochrome P450, CYP3A4, inhibitor, complex, OXIDOREDUCTASE, OXIDOREDUCTASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE/INHIBITOR 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CP3A4_HUMAN 
_struct_ref.pdbx_db_accession          P08684 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQP
VLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNL
RREAETGKPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICV
FPREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYE
LATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYA
LHRDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLG
GLLQPEKPVVLKVESRDGTVSGA
;
_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              9COW 
_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                 483 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P08684 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  503 
_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       503 
# 
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 9COW ?   A ?   ? UNP P08684 LEU 3  deletion         ?   1  
1 9COW ?   A ?   ? UNP P08684 ILE 4  deletion         ?   2  
1 9COW ?   A ?   ? UNP P08684 PRO 5  deletion         ?   3  
1 9COW ?   A ?   ? UNP P08684 ASP 6  deletion         ?   4  
1 9COW ?   A ?   ? UNP P08684 LEU 7  deletion         ?   5  
1 9COW ?   A ?   ? UNP P08684 ALA 8  deletion         ?   6  
1 9COW ?   A ?   ? UNP P08684 MET 9  deletion         ?   7  
1 9COW ?   A ?   ? UNP P08684 GLU 10 deletion         ?   8  
1 9COW ?   A ?   ? UNP P08684 THR 11 deletion         ?   9  
1 9COW ?   A ?   ? UNP P08684 TRP 12 deletion         ?   10 
1 9COW ?   A ?   ? UNP P08684 LEU 13 deletion         ?   11 
1 9COW ?   A ?   ? UNP P08684 LEU 14 deletion         ?   12 
1 9COW ?   A ?   ? UNP P08684 LEU 15 deletion         ?   13 
1 9COW ?   A ?   ? UNP P08684 ALA 16 deletion         ?   14 
1 9COW ?   A ?   ? UNP P08684 VAL 17 deletion         ?   15 
1 9COW ?   A ?   ? UNP P08684 SER 18 deletion         ?   16 
1 9COW ?   A ?   ? UNP P08684 LEU 19 deletion         ?   17 
1 9COW ?   A ?   ? UNP P08684 VAL 20 deletion         ?   18 
1 9COW ?   A ?   ? UNP P08684 LEU 21 deletion         ?   19 
1 9COW ?   A ?   ? UNP P08684 LEU 22 deletion         ?   20 
1 9COW HIS A 484 ? UNP P08684 ?   ?  'expression tag' 504 21 
1 9COW HIS A 485 ? UNP P08684 ?   ?  'expression tag' 505 22 
1 9COW HIS A 486 ? UNP P08684 ?   ?  'expression tag' 506 23 
1 9COW HIS A 487 ? UNP P08684 ?   ?  'expression tag' 507 24 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,E 
1 2 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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000    0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 4_545 x,-y-1,-z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 -100.0900000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 8   ? HIS A 10  ? HIS A 28  HIS A 30  5 ? 3  
HELX_P HELX_P2  AA2 GLY A 11  ? LEU A 16  ? GLY A 31  LEU A 36  1 ? 6  
HELX_P HELX_P3  AA3 ASN A 29  ? HIS A 34  ? ASN A 49  HIS A 54  5 ? 6  
HELX_P HELX_P4  AA4 LYS A 35  ? GLY A 49  ? LYS A 55  GLY A 69  1 ? 15 
HELX_P HELX_P5  AA5 ASP A 66  ? VAL A 75  ? ASP A 86  VAL A 95  1 ? 10 
HELX_P HELX_P6  AA6 VAL A 91  ? ALA A 97  ? VAL A 111 ALA A 117 5 ? 7  
HELX_P HELX_P7  AA7 GLU A 102 ? SER A 114 ? GLU A 122 SER A 134 1 ? 13 
HELX_P HELX_P8  AA8 PRO A 115 ? THR A 118 ? PRO A 135 THR A 138 5 ? 4  
HELX_P HELX_P9  AA9 MET A 125 ? ARG A 141 ? MET A 145 ARG A 161 1 ? 17 
HELX_P HELX_P10 AB1 LEU A 152 ? PHE A 169 ? LEU A 172 PHE A 189 1 ? 18 
HELX_P HELX_P11 AB2 LEU A 201 ? PHE A 206 ? LEU A 221 PHE A 226 1 ? 6  
HELX_P HELX_P12 AB3 LEU A 209 ? GLU A 214 ? LEU A 229 GLU A 234 1 ? 6  
HELX_P HELX_P13 AB4 ASN A 227 ? VAL A 233 ? ASN A 247 VAL A 253 1 ? 7  
HELX_P HELX_P14 AB5 LEU A 252 ? ASP A 257 ? LEU A 272 ASP A 277 1 ? 6  
HELX_P HELX_P15 AB6 SER A 271 ? THR A 303 ? SER A 291 THR A 323 1 ? 33 
HELX_P HELX_P16 AB7 HIS A 304 ? LEU A 319 ? HIS A 324 LEU A 339 1 ? 16 
HELX_P HELX_P17 AB8 PRO A 320 ? ALA A 323 ? PRO A 340 ALA A 343 5 ? 4  
HELX_P HELX_P18 AB9 THR A 326 ? LEU A 331 ? THR A 346 LEU A 351 1 ? 6  
HELX_P HELX_P19 AC1 MET A 333 ? PHE A 347 ? MET A 353 PHE A 367 1 ? 15 
HELX_P HELX_P20 AC2 PRO A 377 ? ARG A 383 ? PRO A 397 ARG A 403 1 ? 7  
HELX_P HELX_P21 AC3 LEU A 395 ? SER A 400 ? LEU A 415 SER A 420 5 ? 6  
HELX_P HELX_P22 AC4 GLY A 424 ? ASN A 442 ? GLY A 444 ASN A 462 1 ? 19 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 422 SG ? ? ? 1_555 B HEM   . FE  ? ? A CYS 442 A HEM   601 1_555 ? ? ? ? ? ? ? 2.374 ? ? 
metalc2 metalc ? ? B HEM .   FE ? ? ? 1_555 D A1A4V . N11 ? ? A HEM 601 A A1A4V 603 1_555 ? ? ? ? ? ? ? 2.192 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 422 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NA  ? B HEM   . ? A HEM   601 ? 1_555 90.5  ? 
2  SG ? A CYS 422 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NB  ? B HEM   . ? A HEM   601 ? 1_555 80.1  ? 
3  NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NB  ? B HEM   . ? A HEM   601 ? 1_555 89.1  ? 
4  SG ? A CYS 422 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NC  ? B HEM   . ? A HEM   601 ? 1_555 87.2  ? 
5  NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NC  ? B HEM   . ? A HEM   601 ? 1_555 177.7 ? 
6  NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NC  ? B HEM   . ? A HEM   601 ? 1_555 90.7  ? 
7  SG ? A CYS 422 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 96.3  ? 
8  NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 90.5  ? 
9  NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 176.4 ? 
10 NC ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 89.4  ? 
11 SG ? A CYS 422 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N11 ? D A1A4V . ? A A1A4V 603 ? 1_555 174.7 ? 
12 NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N11 ? D A1A4V . ? A A1A4V 603 ? 1_555 89.1  ? 
13 NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N11 ? D A1A4V . ? A A1A4V 603 ? 1_555 94.6  ? 
14 NC ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N11 ? D A1A4V . ? A A1A4V 603 ? 1_555 93.2  ? 
15 ND ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N11 ? D A1A4V . ? A A1A4V 603 ? 1_555 89.1  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 89  A . ? GLY 109 A PRO 90  A ? PRO 110 A 1 -1.49 
2 ILE 453 A . ? ILE 473 A PRO 454 A ? PRO 474 A 1 -0.22 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 51  ? ASP A 56  ? VAL A 71  ASP A 76  
AA1 2 GLN A 59  ? ILE A 64  ? GLN A 79  ILE A 84  
AA1 3 VAL A 373 ? ILE A 376 ? VAL A 393 ILE A 396 
AA1 4 LEU A 353 ? VAL A 356 ? LEU A 373 VAL A 376 
AA2 1 VAL A 150 ? THR A 151 ? VAL A 170 THR A 171 
AA2 2 VAL A 470 ? SER A 475 ? VAL A 490 SER A 495 
AA2 3 PHE A 443 ? LYS A 446 ? PHE A 463 LYS A 466 
AA3 1 VAL A 361 ? GLU A 362 ? VAL A 381 GLU A 382 
AA3 2 PHE A 367 ? ILE A 368 ? PHE A 387 ILE A 388 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 54  ? N PHE A 74  O VAL A 61  ? O VAL A 81  
AA1 2 3 N LEU A 62  ? N LEU A 82  O MET A 375 ? O MET A 395 
AA1 3 4 O ILE A 376 ? O ILE A 396 N LEU A 353 ? N LEU A 373 
AA2 1 2 N VAL A 150 ? N VAL A 170 O LEU A 471 ? O LEU A 491 
AA2 2 3 O GLU A 474 ? O GLU A 494 N SER A 444 ? N SER A 464 
AA3 1 2 N VAL A 361 ? N VAL A 381 O ILE A 368 ? O ILE A 388 
# 
_pdbx_entry_details.entry_id                   9COW 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 PHE A 46  ? ? 66.07   -50.21  
2  1 VAL A 95  ? ? -122.55 -60.90  
3  1 VAL A 101 ? ? -127.94 -62.80  
4  1 VAL A 111 ? ? -132.29 -39.27  
5  1 ASP A 123 ? ? 50.42   -114.17 
6  1 GLU A 163 ? ? -111.61 70.83   
7  1 ASN A 197 ? ? -104.05 -161.82 
8  1 LEU A 221 ? ? -152.15 19.87   
9  1 ASN A 247 ? ? -140.02 -62.28  
10 1 MET A 275 ? ? -133.71 -47.35  
11 1 LYS A 288 ? ? -147.04 51.04   
12 1 LEU A 290 ? ? -171.77 110.69  
13 1 MET A 371 ? ? 70.85   -42.59  
14 1 PRO A 429 ? ? -69.09  4.35    
15 1 LEU A 479 ? ? -80.44  45.42   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     740 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   E 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -19.4739 
_pdbx_refine_tls.origin_y         -26.2723 
_pdbx_refine_tls.origin_z         -12.4583 
_pdbx_refine_tls.T[1][1]          0.4909 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0232 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0600 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.5881 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.1197 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.5886 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          3.0656 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -1.3459 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.4125 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          5.5348 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -1.3225 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          4.0049 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0994 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0991 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.2576 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.5131 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.1511 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.4345 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.6376 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.1572 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0276 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 739 ? 6.05 . 
2 1 O ? A HOH 740 ? 6.45 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A ALA 2   ? A ALA 2   
3  1 Y 1 A TYR 23  ? A TYR 3   
4  1 Y 1 A LEU 24  ? A LEU 4   
5  1 Y 1 A TYR 25  ? A TYR 5   
6  1 Y 1 A GLY 26  ? A GLY 6   
7  1 Y 1 A THR 27  ? A THR 7   
8  1 Y 1 A THR 166 ? A THR 146 
9  1 Y 1 A GLY 167 ? A GLY 147 
10 1 Y 1 A LYS 168 ? A LYS 148 
11 1 Y 1 A VAL 204 ? A VAL 184 
12 1 Y 1 A GLU 205 ? A GLU 185 
13 1 Y 1 A ASN 206 ? A ASN 186 
14 1 Y 1 A THR 207 ? A THR 187 
15 1 Y 1 A LYS 208 ? A LYS 188 
16 1 Y 1 A LYS 209 ? A LYS 189 
17 1 Y 1 A LEU 210 ? A LEU 190 
18 1 Y 1 A LEU 211 ? A LEU 191 
19 1 Y 1 A ARG 212 ? A ARG 192 
20 1 Y 1 A PHE 213 ? A PHE 193 
21 1 Y 1 A ASP 214 ? A ASP 194 
22 1 Y 1 A PHE 215 ? A PHE 195 
23 1 Y 1 A LEU 216 ? A LEU 196 
24 1 Y 1 A ASP 217 ? A ASP 197 
25 1 Y 1 A VAL 240 ? A VAL 220 
26 1 Y 1 A PHE 241 ? A PHE 221 
27 1 Y 1 A PRO 242 ? A PRO 222 
28 1 Y 1 A ARG 243 ? A ARG 223 
29 1 Y 1 A GLU 244 ? A GLU 224 
30 1 Y 1 A VAL 245 ? A VAL 225 
31 1 Y 1 A ARG 260 ? A ARG 240 
32 1 Y 1 A LEU 261 ? A LEU 241 
33 1 Y 1 A GLU 262 ? A GLU 242 
34 1 Y 1 A ASP 263 ? A ASP 243 
35 1 Y 1 A THR 264 ? A THR 244 
36 1 Y 1 A GLN 265 ? A GLN 245 
37 1 Y 1 A LYS 266 ? A LYS 246 
38 1 Y 1 A HIS 267 ? A HIS 247 
39 1 Y 1 A ARG 268 ? A ARG 248 
40 1 Y 1 A VAL 269 ? A VAL 249 
41 1 Y 1 A GLN 279 ? A GLN 259 
42 1 Y 1 A ASN 280 ? A ASN 260 
43 1 Y 1 A SER 281 ? A SER 261 
44 1 Y 1 A LYS 282 ? A LYS 262 
45 1 Y 1 A GLU 283 ? A GLU 263 
46 1 Y 1 A THR 284 ? A THR 264 
47 1 Y 1 A GLU 285 ? A GLU 265 
48 1 Y 1 A ASP 497 ? A ASP 477 
49 1 Y 1 A GLY 498 ? A GLY 478 
50 1 Y 1 A THR 499 ? A THR 479 
51 1 Y 1 A VAL 500 ? A VAL 480 
52 1 Y 1 A SER 501 ? A SER 481 
53 1 Y 1 A GLY 502 ? A GLY 482 
54 1 Y 1 A ALA 503 ? A ALA 483 
55 1 Y 1 A HIS 504 ? A HIS 484 
56 1 Y 1 A HIS 505 ? A HIS 485 
57 1 Y 1 A HIS 506 ? A HIS 486 
58 1 Y 1 A HIS 507 ? A HIS 487 
# 
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 
A1A4V C12  C  Y N 1   
A1A4V C14  C  N N 2   
A1A4V C15  C  Y N 3   
A1A4V C16  C  Y N 4   
A1A4V C19  C  Y N 5   
A1A4V C20  C  Y N 6   
A1A4V C22  C  N N 7   
A1A4V C23  C  N S 8   
A1A4V C10  C  Y N 9   
A1A4V C13  C  N R 10  
A1A4V C17  C  Y N 11  
A1A4V C18  C  Y N 12  
A1A4V C02  C  N N 13  
A1A4V C04  C  N N 14  
A1A4V C05  C  N N 15  
A1A4V C06  C  N N 16  
A1A4V C07  C  Y N 17  
A1A4V C08  C  Y N 18  
A1A4V C09  C  Y N 19  
A1A4V C24  C  N N 20  
A1A4V C25  C  Y N 21  
A1A4V C26  C  Y N 22  
A1A4V C27  C  Y N 23  
A1A4V C28  C  Y N 24  
A1A4V C29  C  Y N 25  
A1A4V C30  C  Y N 26  
A1A4V C31  C  Y N 27  
A1A4V C32  C  Y N 28  
A1A4V C33  C  Y N 29  
A1A4V C34  C  Y N 30  
A1A4V C36  C  N N 31  
A1A4V C38  C  Y N 32  
A1A4V C39  C  Y N 33  
A1A4V C41  C  Y N 34  
A1A4V C42  C  Y N 35  
A1A4V C43  C  Y N 36  
A1A4V N03  N  N N 37  
A1A4V N11  N  Y N 38  
A1A4V N35  N  N N 39  
A1A4V N40  N  Y N 40  
A1A4V O01  O  N N 41  
A1A4V O37  O  N N 42  
A1A4V S21  S  N N 43  
A1A4V H1   H  N N 44  
A1A4V H2   H  N N 45  
A1A4V H3   H  N N 46  
A1A4V H4   H  N N 47  
A1A4V H5   H  N N 48  
A1A4V H6   H  N N 49  
A1A4V H7   H  N N 50  
A1A4V H8   H  N N 51  
A1A4V H9   H  N N 52  
A1A4V H10  H  N N 53  
A1A4V H11  H  N N 54  
A1A4V H12  H  N N 55  
A1A4V H13  H  N N 56  
A1A4V H14  H  N N 57  
A1A4V H15  H  N N 58  
A1A4V H16  H  N N 59  
A1A4V H17  H  N N 60  
A1A4V H18  H  N N 61  
A1A4V H19  H  N N 62  
A1A4V H20  H  N N 63  
A1A4V H21  H  N N 64  
A1A4V H22  H  N N 65  
A1A4V H23  H  N N 66  
A1A4V H24  H  N N 67  
A1A4V H25  H  N N 68  
A1A4V H26  H  N N 69  
A1A4V H27  H  N N 70  
A1A4V H28  H  N N 71  
A1A4V H29  H  N N 72  
A1A4V H30  H  N N 73  
A1A4V H31  H  N N 74  
A1A4V H32  H  N N 75  
A1A4V H33  H  N N 76  
A1A4V H34  H  N N 77  
A1A4V H35  H  N N 78  
A1A4V H36  H  N N 79  
ALA   N    N  N N 80  
ALA   CA   C  N S 81  
ALA   C    C  N N 82  
ALA   O    O  N N 83  
ALA   CB   C  N N 84  
ALA   OXT  O  N N 85  
ALA   H    H  N N 86  
ALA   H2   H  N N 87  
ALA   HA   H  N N 88  
ALA   HB1  H  N N 89  
ALA   HB2  H  N N 90  
ALA   HB3  H  N N 91  
ALA   HXT  H  N N 92  
ARG   N    N  N N 93  
ARG   CA   C  N S 94  
ARG   C    C  N N 95  
ARG   O    O  N N 96  
ARG   CB   C  N N 97  
ARG   CG   C  N N 98  
ARG   CD   C  N N 99  
ARG   NE   N  N N 100 
ARG   CZ   C  N N 101 
ARG   NH1  N  N N 102 
ARG   NH2  N  N N 103 
ARG   OXT  O  N N 104 
ARG   H    H  N N 105 
ARG   H2   H  N N 106 
ARG   HA   H  N N 107 
ARG   HB2  H  N N 108 
ARG   HB3  H  N N 109 
ARG   HG2  H  N N 110 
ARG   HG3  H  N N 111 
ARG   HD2  H  N N 112 
ARG   HD3  H  N N 113 
ARG   HE   H  N N 114 
ARG   HH11 H  N N 115 
ARG   HH12 H  N N 116 
ARG   HH21 H  N N 117 
ARG   HH22 H  N N 118 
ARG   HXT  H  N N 119 
ASN   N    N  N N 120 
ASN   CA   C  N S 121 
ASN   C    C  N N 122 
ASN   O    O  N N 123 
ASN   CB   C  N N 124 
ASN   CG   C  N N 125 
ASN   OD1  O  N N 126 
ASN   ND2  N  N N 127 
ASN   OXT  O  N N 128 
ASN   H    H  N N 129 
ASN   H2   H  N N 130 
ASN   HA   H  N N 131 
ASN   HB2  H  N N 132 
ASN   HB3  H  N N 133 
ASN   HD21 H  N N 134 
ASN   HD22 H  N N 135 
ASN   HXT  H  N N 136 
ASP   N    N  N N 137 
ASP   CA   C  N S 138 
ASP   C    C  N N 139 
ASP   O    O  N N 140 
ASP   CB   C  N N 141 
ASP   CG   C  N N 142 
ASP   OD1  O  N N 143 
ASP   OD2  O  N N 144 
ASP   OXT  O  N N 145 
ASP   H    H  N N 146 
ASP   H2   H  N N 147 
ASP   HA   H  N N 148 
ASP   HB2  H  N N 149 
ASP   HB3  H  N N 150 
ASP   HD2  H  N N 151 
ASP   HXT  H  N N 152 
CYS   N    N  N N 153 
CYS   CA   C  N R 154 
CYS   C    C  N N 155 
CYS   O    O  N N 156 
CYS   CB   C  N N 157 
CYS   SG   S  N N 158 
CYS   OXT  O  N N 159 
CYS   H    H  N N 160 
CYS   H2   H  N N 161 
CYS   HA   H  N N 162 
CYS   HB2  H  N N 163 
CYS   HB3  H  N N 164 
CYS   HG   H  N N 165 
CYS   HXT  H  N N 166 
GLN   N    N  N N 167 
GLN   CA   C  N S 168 
GLN   C    C  N N 169 
GLN   O    O  N N 170 
GLN   CB   C  N N 171 
GLN   CG   C  N N 172 
GLN   CD   C  N N 173 
GLN   OE1  O  N N 174 
GLN   NE2  N  N N 175 
GLN   OXT  O  N N 176 
GLN   H    H  N N 177 
GLN   H2   H  N N 178 
GLN   HA   H  N N 179 
GLN   HB2  H  N N 180 
GLN   HB3  H  N N 181 
GLN   HG2  H  N N 182 
GLN   HG3  H  N N 183 
GLN   HE21 H  N N 184 
GLN   HE22 H  N N 185 
GLN   HXT  H  N N 186 
GLU   N    N  N N 187 
GLU   CA   C  N S 188 
GLU   C    C  N N 189 
GLU   O    O  N N 190 
GLU   CB   C  N N 191 
GLU   CG   C  N N 192 
GLU   CD   C  N N 193 
GLU   OE1  O  N N 194 
GLU   OE2  O  N N 195 
GLU   OXT  O  N N 196 
GLU   H    H  N N 197 
GLU   H2   H  N N 198 
GLU   HA   H  N N 199 
GLU   HB2  H  N N 200 
GLU   HB3  H  N N 201 
GLU   HG2  H  N N 202 
GLU   HG3  H  N N 203 
GLU   HE2  H  N N 204 
GLU   HXT  H  N N 205 
GLY   N    N  N N 206 
GLY   CA   C  N N 207 
GLY   C    C  N N 208 
GLY   O    O  N N 209 
GLY   OXT  O  N N 210 
GLY   H    H  N N 211 
GLY   H2   H  N N 212 
GLY   HA2  H  N N 213 
GLY   HA3  H  N N 214 
GLY   HXT  H  N N 215 
GOL   C1   C  N N 216 
GOL   O1   O  N N 217 
GOL   C2   C  N N 218 
GOL   O2   O  N N 219 
GOL   C3   C  N N 220 
GOL   O3   O  N N 221 
GOL   H11  H  N N 222 
GOL   H12  H  N N 223 
GOL   HO1  H  N N 224 
GOL   H2   H  N N 225 
GOL   HO2  H  N N 226 
GOL   H31  H  N N 227 
GOL   H32  H  N N 228 
GOL   HO3  H  N N 229 
HEM   CHA  C  N N 230 
HEM   CHB  C  N N 231 
HEM   CHC  C  N N 232 
HEM   CHD  C  N N 233 
HEM   C1A  C  Y N 234 
HEM   C2A  C  Y N 235 
HEM   C3A  C  Y N 236 
HEM   C4A  C  Y N 237 
HEM   CMA  C  N N 238 
HEM   CAA  C  N N 239 
HEM   CBA  C  N N 240 
HEM   CGA  C  N N 241 
HEM   O1A  O  N N 242 
HEM   O2A  O  N N 243 
HEM   C1B  C  N N 244 
HEM   C2B  C  N N 245 
HEM   C3B  C  N N 246 
HEM   C4B  C  N N 247 
HEM   CMB  C  N N 248 
HEM   CAB  C  N N 249 
HEM   CBB  C  N N 250 
HEM   C1C  C  Y N 251 
HEM   C2C  C  Y N 252 
HEM   C3C  C  Y N 253 
HEM   C4C  C  Y N 254 
HEM   CMC  C  N N 255 
HEM   CAC  C  N N 256 
HEM   CBC  C  N N 257 
HEM   C1D  C  N N 258 
HEM   C2D  C  N N 259 
HEM   C3D  C  N N 260 
HEM   C4D  C  N N 261 
HEM   CMD  C  N N 262 
HEM   CAD  C  N N 263 
HEM   CBD  C  N N 264 
HEM   CGD  C  N N 265 
HEM   O1D  O  N N 266 
HEM   O2D  O  N N 267 
HEM   NA   N  Y N 268 
HEM   NB   N  N N 269 
HEM   NC   N  Y N 270 
HEM   ND   N  N N 271 
HEM   FE   FE N N 272 
HEM   HHB  H  N N 273 
HEM   HHC  H  N N 274 
HEM   HHD  H  N N 275 
HEM   HMA  H  N N 276 
HEM   HMAA H  N N 277 
HEM   HMAB H  N N 278 
HEM   HAA  H  N N 279 
HEM   HAAA H  N N 280 
HEM   HBA  H  N N 281 
HEM   HBAA H  N N 282 
HEM   HMB  H  N N 283 
HEM   HMBA H  N N 284 
HEM   HMBB H  N N 285 
HEM   HAB  H  N N 286 
HEM   HBB  H  N N 287 
HEM   HBBA H  N N 288 
HEM   HMC  H  N N 289 
HEM   HMCA H  N N 290 
HEM   HMCB H  N N 291 
HEM   HAC  H  N N 292 
HEM   HBC  H  N N 293 
HEM   HBCA H  N N 294 
HEM   HMD  H  N N 295 
HEM   HMDA H  N N 296 
HEM   HMDB H  N N 297 
HEM   HAD  H  N N 298 
HEM   HADA H  N N 299 
HEM   HBD  H  N N 300 
HEM   HBDA H  N N 301 
HEM   H2A  H  N N 302 
HEM   H2D  H  N N 303 
HEM   HHA  H  N N 304 
HIS   N    N  N N 305 
HIS   CA   C  N S 306 
HIS   C    C  N N 307 
HIS   O    O  N N 308 
HIS   CB   C  N N 309 
HIS   CG   C  Y N 310 
HIS   ND1  N  Y N 311 
HIS   CD2  C  Y N 312 
HIS   CE1  C  Y N 313 
HIS   NE2  N  Y N 314 
HIS   OXT  O  N N 315 
HIS   H    H  N N 316 
HIS   H2   H  N N 317 
HIS   HA   H  N N 318 
HIS   HB2  H  N N 319 
HIS   HB3  H  N N 320 
HIS   HD1  H  N N 321 
HIS   HD2  H  N N 322 
HIS   HE1  H  N N 323 
HIS   HE2  H  N N 324 
HIS   HXT  H  N N 325 
HOH   O    O  N N 326 
HOH   H1   H  N N 327 
HOH   H2   H  N N 328 
ILE   N    N  N N 329 
ILE   CA   C  N S 330 
ILE   C    C  N N 331 
ILE   O    O  N N 332 
ILE   CB   C  N S 333 
ILE   CG1  C  N N 334 
ILE   CG2  C  N N 335 
ILE   CD1  C  N N 336 
ILE   OXT  O  N N 337 
ILE   H    H  N N 338 
ILE   H2   H  N N 339 
ILE   HA   H  N N 340 
ILE   HB   H  N N 341 
ILE   HG12 H  N N 342 
ILE   HG13 H  N N 343 
ILE   HG21 H  N N 344 
ILE   HG22 H  N N 345 
ILE   HG23 H  N N 346 
ILE   HD11 H  N N 347 
ILE   HD12 H  N N 348 
ILE   HD13 H  N N 349 
ILE   HXT  H  N N 350 
LEU   N    N  N N 351 
LEU   CA   C  N S 352 
LEU   C    C  N N 353 
LEU   O    O  N N 354 
LEU   CB   C  N N 355 
LEU   CG   C  N N 356 
LEU   CD1  C  N N 357 
LEU   CD2  C  N N 358 
LEU   OXT  O  N N 359 
LEU   H    H  N N 360 
LEU   H2   H  N N 361 
LEU   HA   H  N N 362 
LEU   HB2  H  N N 363 
LEU   HB3  H  N N 364 
LEU   HG   H  N N 365 
LEU   HD11 H  N N 366 
LEU   HD12 H  N N 367 
LEU   HD13 H  N N 368 
LEU   HD21 H  N N 369 
LEU   HD22 H  N N 370 
LEU   HD23 H  N N 371 
LEU   HXT  H  N N 372 
LYS   N    N  N N 373 
LYS   CA   C  N S 374 
LYS   C    C  N N 375 
LYS   O    O  N N 376 
LYS   CB   C  N N 377 
LYS   CG   C  N N 378 
LYS   CD   C  N N 379 
LYS   CE   C  N N 380 
LYS   NZ   N  N N 381 
LYS   OXT  O  N N 382 
LYS   H    H  N N 383 
LYS   H2   H  N N 384 
LYS   HA   H  N N 385 
LYS   HB2  H  N N 386 
LYS   HB3  H  N N 387 
LYS   HG2  H  N N 388 
LYS   HG3  H  N N 389 
LYS   HD2  H  N N 390 
LYS   HD3  H  N N 391 
LYS   HE2  H  N N 392 
LYS   HE3  H  N N 393 
LYS   HZ1  H  N N 394 
LYS   HZ2  H  N N 395 
LYS   HZ3  H  N N 396 
LYS   HXT  H  N N 397 
MET   N    N  N N 398 
MET   CA   C  N S 399 
MET   C    C  N N 400 
MET   O    O  N N 401 
MET   CB   C  N N 402 
MET   CG   C  N N 403 
MET   SD   S  N N 404 
MET   CE   C  N N 405 
MET   OXT  O  N N 406 
MET   H    H  N N 407 
MET   H2   H  N N 408 
MET   HA   H  N N 409 
MET   HB2  H  N N 410 
MET   HB3  H  N N 411 
MET   HG2  H  N N 412 
MET   HG3  H  N N 413 
MET   HE1  H  N N 414 
MET   HE2  H  N N 415 
MET   HE3  H  N N 416 
MET   HXT  H  N N 417 
PHE   N    N  N N 418 
PHE   CA   C  N S 419 
PHE   C    C  N N 420 
PHE   O    O  N N 421 
PHE   CB   C  N N 422 
PHE   CG   C  Y N 423 
PHE   CD1  C  Y N 424 
PHE   CD2  C  Y N 425 
PHE   CE1  C  Y N 426 
PHE   CE2  C  Y N 427 
PHE   CZ   C  Y N 428 
PHE   OXT  O  N N 429 
PHE   H    H  N N 430 
PHE   H2   H  N N 431 
PHE   HA   H  N N 432 
PHE   HB2  H  N N 433 
PHE   HB3  H  N N 434 
PHE   HD1  H  N N 435 
PHE   HD2  H  N N 436 
PHE   HE1  H  N N 437 
PHE   HE2  H  N N 438 
PHE   HZ   H  N N 439 
PHE   HXT  H  N N 440 
PRO   N    N  N N 441 
PRO   CA   C  N S 442 
PRO   C    C  N N 443 
PRO   O    O  N N 444 
PRO   CB   C  N N 445 
PRO   CG   C  N N 446 
PRO   CD   C  N N 447 
PRO   OXT  O  N N 448 
PRO   H    H  N N 449 
PRO   HA   H  N N 450 
PRO   HB2  H  N N 451 
PRO   HB3  H  N N 452 
PRO   HG2  H  N N 453 
PRO   HG3  H  N N 454 
PRO   HD2  H  N N 455 
PRO   HD3  H  N N 456 
PRO   HXT  H  N N 457 
SER   N    N  N N 458 
SER   CA   C  N S 459 
SER   C    C  N N 460 
SER   O    O  N N 461 
SER   CB   C  N N 462 
SER   OG   O  N N 463 
SER   OXT  O  N N 464 
SER   H    H  N N 465 
SER   H2   H  N N 466 
SER   HA   H  N N 467 
SER   HB2  H  N N 468 
SER   HB3  H  N N 469 
SER   HG   H  N N 470 
SER   HXT  H  N N 471 
THR   N    N  N N 472 
THR   CA   C  N S 473 
THR   C    C  N N 474 
THR   O    O  N N 475 
THR   CB   C  N R 476 
THR   OG1  O  N N 477 
THR   CG2  C  N N 478 
THR   OXT  O  N N 479 
THR   H    H  N N 480 
THR   H2   H  N N 481 
THR   HA   H  N N 482 
THR   HB   H  N N 483 
THR   HG1  H  N N 484 
THR   HG21 H  N N 485 
THR   HG22 H  N N 486 
THR   HG23 H  N N 487 
THR   HXT  H  N N 488 
TRP   N    N  N N 489 
TRP   CA   C  N S 490 
TRP   C    C  N N 491 
TRP   O    O  N N 492 
TRP   CB   C  N N 493 
TRP   CG   C  Y N 494 
TRP   CD1  C  Y N 495 
TRP   CD2  C  Y N 496 
TRP   NE1  N  Y N 497 
TRP   CE2  C  Y N 498 
TRP   CE3  C  Y N 499 
TRP   CZ2  C  Y N 500 
TRP   CZ3  C  Y N 501 
TRP   CH2  C  Y N 502 
TRP   OXT  O  N N 503 
TRP   H    H  N N 504 
TRP   H2   H  N N 505 
TRP   HA   H  N N 506 
TRP   HB2  H  N N 507 
TRP   HB3  H  N N 508 
TRP   HD1  H  N N 509 
TRP   HE1  H  N N 510 
TRP   HE3  H  N N 511 
TRP   HZ2  H  N N 512 
TRP   HZ3  H  N N 513 
TRP   HH2  H  N N 514 
TRP   HXT  H  N N 515 
TYR   N    N  N N 516 
TYR   CA   C  N S 517 
TYR   C    C  N N 518 
TYR   O    O  N N 519 
TYR   CB   C  N N 520 
TYR   CG   C  Y N 521 
TYR   CD1  C  Y N 522 
TYR   CD2  C  Y N 523 
TYR   CE1  C  Y N 524 
TYR   CE2  C  Y N 525 
TYR   CZ   C  Y N 526 
TYR   OH   O  N N 527 
TYR   OXT  O  N N 528 
TYR   H    H  N N 529 
TYR   H2   H  N N 530 
TYR   HA   H  N N 531 
TYR   HB2  H  N N 532 
TYR   HB3  H  N N 533 
TYR   HD1  H  N N 534 
TYR   HD2  H  N N 535 
TYR   HE1  H  N N 536 
TYR   HE2  H  N N 537 
TYR   HH   H  N N 538 
TYR   HXT  H  N N 539 
VAL   N    N  N N 540 
VAL   CA   C  N S 541 
VAL   C    C  N N 542 
VAL   O    O  N N 543 
VAL   CB   C  N N 544 
VAL   CG1  C  N N 545 
VAL   CG2  C  N N 546 
VAL   OXT  O  N N 547 
VAL   H    H  N N 548 
VAL   H2   H  N N 549 
VAL   HA   H  N N 550 
VAL   HB   H  N N 551 
VAL   HG11 H  N N 552 
VAL   HG12 H  N N 553 
VAL   HG13 H  N N 554 
VAL   HG21 H  N N 555 
VAL   HG22 H  N N 556 
VAL   HG23 H  N N 557 
VAL   HXT  H  N N 558 
# 
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 
A1A4V C29 C28  doub Y N 1   
A1A4V C29 C30  sing Y N 2   
A1A4V C28 C27  sing Y N 3   
A1A4V C30 C31  doub Y N 4   
A1A4V C27 C26  doub Y N 5   
A1A4V C42 C43  doub Y N 6   
A1A4V C42 C41  sing Y N 7   
A1A4V C31 C26  sing Y N 8   
A1A4V C31 C32  sing Y N 9   
A1A4V C43 C38  sing Y N 10  
A1A4V C26 C25  sing Y N 11  
A1A4V C10 C09  doub Y N 12  
A1A4V C10 N11  sing Y N 13  
A1A4V C09 C08  sing Y N 14  
A1A4V C41 N40  doub Y N 15  
A1A4V C32 C33  doub Y N 16  
A1A4V O37 C36  doub N N 17  
A1A4V C38 C36  sing N N 18  
A1A4V C38 C39  doub Y N 19  
A1A4V N40 C39  sing Y N 20  
A1A4V C36 N35  sing N N 21  
A1A4V C25 C24  sing N N 22  
A1A4V C25 C34  doub Y N 23  
A1A4V N11 C12  doub Y N 24  
A1A4V C08 C07  doub Y N 25  
A1A4V C24 C23  sing N N 26  
A1A4V C33 C34  sing Y N 27  
A1A4V N35 C23  sing N N 28  
A1A4V C23 C22  sing N N 29  
A1A4V C12 C07  sing Y N 30  
A1A4V C07 C06  sing N N 31  
A1A4V N03 C04  sing N N 32  
A1A4V N03 C02  sing N N 33  
A1A4V C04 C05  sing N N 34  
A1A4V C22 S21  sing N N 35  
A1A4V C06 C05  sing N N 36  
A1A4V C19 C20  doub Y N 37  
A1A4V C19 C18  sing Y N 38  
A1A4V C20 C15  sing Y N 39  
A1A4V C13 C02  sing N N 40  
A1A4V C13 S21  sing N N 41  
A1A4V C13 C14  sing N N 42  
A1A4V C02 O01  doub N N 43  
A1A4V C14 C15  sing N N 44  
A1A4V C15 C16  doub Y N 45  
A1A4V C18 C17  doub Y N 46  
A1A4V C16 C17  sing Y N 47  
A1A4V C12 H1   sing N N 48  
A1A4V C14 H2   sing N N 49  
A1A4V C14 H3   sing N N 50  
A1A4V C16 H4   sing N N 51  
A1A4V C19 H5   sing N N 52  
A1A4V C20 H6   sing N N 53  
A1A4V C22 H7   sing N N 54  
A1A4V C22 H8   sing N N 55  
A1A4V C23 H9   sing N N 56  
A1A4V C10 H10  sing N N 57  
A1A4V C13 H11  sing N N 58  
A1A4V C17 H12  sing N N 59  
A1A4V C18 H13  sing N N 60  
A1A4V C04 H14  sing N N 61  
A1A4V C04 H15  sing N N 62  
A1A4V C05 H16  sing N N 63  
A1A4V C05 H17  sing N N 64  
A1A4V C06 H18  sing N N 65  
A1A4V C06 H19  sing N N 66  
A1A4V C08 H20  sing N N 67  
A1A4V C09 H21  sing N N 68  
A1A4V C24 H22  sing N N 69  
A1A4V C24 H23  sing N N 70  
A1A4V C27 H24  sing N N 71  
A1A4V C28 H25  sing N N 72  
A1A4V C29 H26  sing N N 73  
A1A4V C30 H27  sing N N 74  
A1A4V C32 H28  sing N N 75  
A1A4V C33 H29  sing N N 76  
A1A4V C34 H30  sing N N 77  
A1A4V C39 H31  sing N N 78  
A1A4V C41 H32  sing N N 79  
A1A4V C42 H33  sing N N 80  
A1A4V C43 H34  sing N N 81  
A1A4V N03 H35  sing N N 82  
A1A4V N35 H36  sing N N 83  
ALA   N   CA   sing N N 84  
ALA   N   H    sing N N 85  
ALA   N   H2   sing N N 86  
ALA   CA  C    sing N N 87  
ALA   CA  CB   sing N N 88  
ALA   CA  HA   sing N N 89  
ALA   C   O    doub N N 90  
ALA   C   OXT  sing N N 91  
ALA   CB  HB1  sing N N 92  
ALA   CB  HB2  sing N N 93  
ALA   CB  HB3  sing N N 94  
ALA   OXT HXT  sing N N 95  
ARG   N   CA   sing N N 96  
ARG   N   H    sing N N 97  
ARG   N   H2   sing N N 98  
ARG   CA  C    sing N N 99  
ARG   CA  CB   sing N N 100 
ARG   CA  HA   sing N N 101 
ARG   C   O    doub N N 102 
ARG   C   OXT  sing N N 103 
ARG   CB  CG   sing N N 104 
ARG   CB  HB2  sing N N 105 
ARG   CB  HB3  sing N N 106 
ARG   CG  CD   sing N N 107 
ARG   CG  HG2  sing N N 108 
ARG   CG  HG3  sing N N 109 
ARG   CD  NE   sing N N 110 
ARG   CD  HD2  sing N N 111 
ARG   CD  HD3  sing N N 112 
ARG   NE  CZ   sing N N 113 
ARG   NE  HE   sing N N 114 
ARG   CZ  NH1  sing N N 115 
ARG   CZ  NH2  doub N N 116 
ARG   NH1 HH11 sing N N 117 
ARG   NH1 HH12 sing N N 118 
ARG   NH2 HH21 sing N N 119 
ARG   NH2 HH22 sing N N 120 
ARG   OXT HXT  sing N N 121 
ASN   N   CA   sing N N 122 
ASN   N   H    sing N N 123 
ASN   N   H2   sing N N 124 
ASN   CA  C    sing N N 125 
ASN   CA  CB   sing N N 126 
ASN   CA  HA   sing N N 127 
ASN   C   O    doub N N 128 
ASN   C   OXT  sing N N 129 
ASN   CB  CG   sing N N 130 
ASN   CB  HB2  sing N N 131 
ASN   CB  HB3  sing N N 132 
ASN   CG  OD1  doub N N 133 
ASN   CG  ND2  sing N N 134 
ASN   ND2 HD21 sing N N 135 
ASN   ND2 HD22 sing N N 136 
ASN   OXT HXT  sing N N 137 
ASP   N   CA   sing N N 138 
ASP   N   H    sing N N 139 
ASP   N   H2   sing N N 140 
ASP   CA  C    sing N N 141 
ASP   CA  CB   sing N N 142 
ASP   CA  HA   sing N N 143 
ASP   C   O    doub N N 144 
ASP   C   OXT  sing N N 145 
ASP   CB  CG   sing N N 146 
ASP   CB  HB2  sing N N 147 
ASP   CB  HB3  sing N N 148 
ASP   CG  OD1  doub N N 149 
ASP   CG  OD2  sing N N 150 
ASP   OD2 HD2  sing N N 151 
ASP   OXT HXT  sing N N 152 
CYS   N   CA   sing N N 153 
CYS   N   H    sing N N 154 
CYS   N   H2   sing N N 155 
CYS   CA  C    sing N N 156 
CYS   CA  CB   sing N N 157 
CYS   CA  HA   sing N N 158 
CYS   C   O    doub N N 159 
CYS   C   OXT  sing N N 160 
CYS   CB  SG   sing N N 161 
CYS   CB  HB2  sing N N 162 
CYS   CB  HB3  sing N N 163 
CYS   SG  HG   sing N N 164 
CYS   OXT HXT  sing N N 165 
GLN   N   CA   sing N N 166 
GLN   N   H    sing N N 167 
GLN   N   H2   sing N N 168 
GLN   CA  C    sing N N 169 
GLN   CA  CB   sing N N 170 
GLN   CA  HA   sing N N 171 
GLN   C   O    doub N N 172 
GLN   C   OXT  sing N N 173 
GLN   CB  CG   sing N N 174 
GLN   CB  HB2  sing N N 175 
GLN   CB  HB3  sing N N 176 
GLN   CG  CD   sing N N 177 
GLN   CG  HG2  sing N N 178 
GLN   CG  HG3  sing N N 179 
GLN   CD  OE1  doub N N 180 
GLN   CD  NE2  sing N N 181 
GLN   NE2 HE21 sing N N 182 
GLN   NE2 HE22 sing N N 183 
GLN   OXT HXT  sing N N 184 
GLU   N   CA   sing N N 185 
GLU   N   H    sing N N 186 
GLU   N   H2   sing N N 187 
GLU   CA  C    sing N N 188 
GLU   CA  CB   sing N N 189 
GLU   CA  HA   sing N N 190 
GLU   C   O    doub N N 191 
GLU   C   OXT  sing N N 192 
GLU   CB  CG   sing N N 193 
GLU   CB  HB2  sing N N 194 
GLU   CB  HB3  sing N N 195 
GLU   CG  CD   sing N N 196 
GLU   CG  HG2  sing N N 197 
GLU   CG  HG3  sing N N 198 
GLU   CD  OE1  doub N N 199 
GLU   CD  OE2  sing N N 200 
GLU   OE2 HE2  sing N N 201 
GLU   OXT HXT  sing N N 202 
GLY   N   CA   sing N N 203 
GLY   N   H    sing N N 204 
GLY   N   H2   sing N N 205 
GLY   CA  C    sing N N 206 
GLY   CA  HA2  sing N N 207 
GLY   CA  HA3  sing N N 208 
GLY   C   O    doub N N 209 
GLY   C   OXT  sing N N 210 
GLY   OXT HXT  sing N N 211 
GOL   C1  O1   sing N N 212 
GOL   C1  C2   sing N N 213 
GOL   C1  H11  sing N N 214 
GOL   C1  H12  sing N N 215 
GOL   O1  HO1  sing N N 216 
GOL   C2  O2   sing N N 217 
GOL   C2  C3   sing N N 218 
GOL   C2  H2   sing N N 219 
GOL   O2  HO2  sing N N 220 
GOL   C3  O3   sing N N 221 
GOL   C3  H31  sing N N 222 
GOL   C3  H32  sing N N 223 
GOL   O3  HO3  sing N N 224 
HEM   CHA C1A  sing N N 225 
HEM   CHA C4D  doub N N 226 
HEM   CHA HHA  sing N N 227 
HEM   CHB C4A  sing N N 228 
HEM   CHB C1B  doub N N 229 
HEM   CHB HHB  sing N N 230 
HEM   CHC C4B  sing N N 231 
HEM   CHC C1C  doub N N 232 
HEM   CHC HHC  sing N N 233 
HEM   CHD C4C  doub N N 234 
HEM   CHD C1D  sing N N 235 
HEM   CHD HHD  sing N N 236 
HEM   C1A C2A  doub Y N 237 
HEM   C1A NA   sing Y N 238 
HEM   C2A C3A  sing Y N 239 
HEM   C2A CAA  sing N N 240 
HEM   C3A C4A  doub Y N 241 
HEM   C3A CMA  sing N N 242 
HEM   C4A NA   sing Y N 243 
HEM   CMA HMA  sing N N 244 
HEM   CMA HMAA sing N N 245 
HEM   CMA HMAB sing N N 246 
HEM   CAA CBA  sing N N 247 
HEM   CAA HAA  sing N N 248 
HEM   CAA HAAA sing N N 249 
HEM   CBA CGA  sing N N 250 
HEM   CBA HBA  sing N N 251 
HEM   CBA HBAA sing N N 252 
HEM   CGA O1A  doub N N 253 
HEM   CGA O2A  sing N N 254 
HEM   C1B C2B  sing N N 255 
HEM   C1B NB   sing N N 256 
HEM   C2B C3B  doub N N 257 
HEM   C2B CMB  sing N N 258 
HEM   C3B C4B  sing N N 259 
HEM   C3B CAB  sing N N 260 
HEM   C4B NB   doub N N 261 
HEM   CMB HMB  sing N N 262 
HEM   CMB HMBA sing N N 263 
HEM   CMB HMBB sing N N 264 
HEM   CAB CBB  doub N N 265 
HEM   CAB HAB  sing N N 266 
HEM   CBB HBB  sing N N 267 
HEM   CBB HBBA sing N N 268 
HEM   C1C C2C  sing Y N 269 
HEM   C1C NC   sing Y N 270 
HEM   C2C C3C  doub Y N 271 
HEM   C2C CMC  sing N N 272 
HEM   C3C C4C  sing Y N 273 
HEM   C3C CAC  sing N N 274 
HEM   C4C NC   sing Y N 275 
HEM   CMC HMC  sing N N 276 
HEM   CMC HMCA sing N N 277 
HEM   CMC HMCB sing N N 278 
HEM   CAC CBC  doub N N 279 
HEM   CAC HAC  sing N N 280 
HEM   CBC HBC  sing N N 281 
HEM   CBC HBCA sing N N 282 
HEM   C1D C2D  sing N N 283 
HEM   C1D ND   doub N N 284 
HEM   C2D C3D  doub N N 285 
HEM   C2D CMD  sing N N 286 
HEM   C3D C4D  sing N N 287 
HEM   C3D CAD  sing N N 288 
HEM   C4D ND   sing N N 289 
HEM   CMD HMD  sing N N 290 
HEM   CMD HMDA sing N N 291 
HEM   CMD HMDB sing N N 292 
HEM   CAD CBD  sing N N 293 
HEM   CAD HAD  sing N N 294 
HEM   CAD HADA sing N N 295 
HEM   CBD CGD  sing N N 296 
HEM   CBD HBD  sing N N 297 
HEM   CBD HBDA sing N N 298 
HEM   CGD O1D  doub N N 299 
HEM   CGD O2D  sing N N 300 
HEM   O2A H2A  sing N N 301 
HEM   O2D H2D  sing N N 302 
HEM   FE  NA   sing N N 303 
HEM   FE  NB   sing N N 304 
HEM   FE  NC   sing N N 305 
HEM   FE  ND   sing N N 306 
HIS   N   CA   sing N N 307 
HIS   N   H    sing N N 308 
HIS   N   H2   sing N N 309 
HIS   CA  C    sing N N 310 
HIS   CA  CB   sing N N 311 
HIS   CA  HA   sing N N 312 
HIS   C   O    doub N N 313 
HIS   C   OXT  sing N N 314 
HIS   CB  CG   sing N N 315 
HIS   CB  HB2  sing N N 316 
HIS   CB  HB3  sing N N 317 
HIS   CG  ND1  sing Y N 318 
HIS   CG  CD2  doub Y N 319 
HIS   ND1 CE1  doub Y N 320 
HIS   ND1 HD1  sing N N 321 
HIS   CD2 NE2  sing Y N 322 
HIS   CD2 HD2  sing N N 323 
HIS   CE1 NE2  sing Y N 324 
HIS   CE1 HE1  sing N N 325 
HIS   NE2 HE2  sing N N 326 
HIS   OXT HXT  sing N N 327 
HOH   O   H1   sing N N 328 
HOH   O   H2   sing N N 329 
ILE   N   CA   sing N N 330 
ILE   N   H    sing N N 331 
ILE   N   H2   sing N N 332 
ILE   CA  C    sing N N 333 
ILE   CA  CB   sing N N 334 
ILE   CA  HA   sing N N 335 
ILE   C   O    doub N N 336 
ILE   C   OXT  sing N N 337 
ILE   CB  CG1  sing N N 338 
ILE   CB  CG2  sing N N 339 
ILE   CB  HB   sing N N 340 
ILE   CG1 CD1  sing N N 341 
ILE   CG1 HG12 sing N N 342 
ILE   CG1 HG13 sing N N 343 
ILE   CG2 HG21 sing N N 344 
ILE   CG2 HG22 sing N N 345 
ILE   CG2 HG23 sing N N 346 
ILE   CD1 HD11 sing N N 347 
ILE   CD1 HD12 sing N N 348 
ILE   CD1 HD13 sing N N 349 
ILE   OXT HXT  sing N N 350 
LEU   N   CA   sing N N 351 
LEU   N   H    sing N N 352 
LEU   N   H2   sing N N 353 
LEU   CA  C    sing N N 354 
LEU   CA  CB   sing N N 355 
LEU   CA  HA   sing N N 356 
LEU   C   O    doub N N 357 
LEU   C   OXT  sing N N 358 
LEU   CB  CG   sing N N 359 
LEU   CB  HB2  sing N N 360 
LEU   CB  HB3  sing N N 361 
LEU   CG  CD1  sing N N 362 
LEU   CG  CD2  sing N N 363 
LEU   CG  HG   sing N N 364 
LEU   CD1 HD11 sing N N 365 
LEU   CD1 HD12 sing N N 366 
LEU   CD1 HD13 sing N N 367 
LEU   CD2 HD21 sing N N 368 
LEU   CD2 HD22 sing N N 369 
LEU   CD2 HD23 sing N N 370 
LEU   OXT HXT  sing N N 371 
LYS   N   CA   sing N N 372 
LYS   N   H    sing N N 373 
LYS   N   H2   sing N N 374 
LYS   CA  C    sing N N 375 
LYS   CA  CB   sing N N 376 
LYS   CA  HA   sing N N 377 
LYS   C   O    doub N N 378 
LYS   C   OXT  sing N N 379 
LYS   CB  CG   sing N N 380 
LYS   CB  HB2  sing N N 381 
LYS   CB  HB3  sing N N 382 
LYS   CG  CD   sing N N 383 
LYS   CG  HG2  sing N N 384 
LYS   CG  HG3  sing N N 385 
LYS   CD  CE   sing N N 386 
LYS   CD  HD2  sing N N 387 
LYS   CD  HD3  sing N N 388 
LYS   CE  NZ   sing N N 389 
LYS   CE  HE2  sing N N 390 
LYS   CE  HE3  sing N N 391 
LYS   NZ  HZ1  sing N N 392 
LYS   NZ  HZ2  sing N N 393 
LYS   NZ  HZ3  sing N N 394 
LYS   OXT HXT  sing N N 395 
MET   N   CA   sing N N 396 
MET   N   H    sing N N 397 
MET   N   H2   sing N N 398 
MET   CA  C    sing N N 399 
MET   CA  CB   sing N N 400 
MET   CA  HA   sing N N 401 
MET   C   O    doub N N 402 
MET   C   OXT  sing N N 403 
MET   CB  CG   sing N N 404 
MET   CB  HB2  sing N N 405 
MET   CB  HB3  sing N N 406 
MET   CG  SD   sing N N 407 
MET   CG  HG2  sing N N 408 
MET   CG  HG3  sing N N 409 
MET   SD  CE   sing N N 410 
MET   CE  HE1  sing N N 411 
MET   CE  HE2  sing N N 412 
MET   CE  HE3  sing N N 413 
MET   OXT HXT  sing N N 414 
PHE   N   CA   sing N N 415 
PHE   N   H    sing N N 416 
PHE   N   H2   sing N N 417 
PHE   CA  C    sing N N 418 
PHE   CA  CB   sing N N 419 
PHE   CA  HA   sing N N 420 
PHE   C   O    doub N N 421 
PHE   C   OXT  sing N N 422 
PHE   CB  CG   sing N N 423 
PHE   CB  HB2  sing N N 424 
PHE   CB  HB3  sing N N 425 
PHE   CG  CD1  doub Y N 426 
PHE   CG  CD2  sing Y N 427 
PHE   CD1 CE1  sing Y N 428 
PHE   CD1 HD1  sing N N 429 
PHE   CD2 CE2  doub Y N 430 
PHE   CD2 HD2  sing N N 431 
PHE   CE1 CZ   doub Y N 432 
PHE   CE1 HE1  sing N N 433 
PHE   CE2 CZ   sing Y N 434 
PHE   CE2 HE2  sing N N 435 
PHE   CZ  HZ   sing N N 436 
PHE   OXT HXT  sing N N 437 
PRO   N   CA   sing N N 438 
PRO   N   CD   sing N N 439 
PRO   N   H    sing N N 440 
PRO   CA  C    sing N N 441 
PRO   CA  CB   sing N N 442 
PRO   CA  HA   sing N N 443 
PRO   C   O    doub N N 444 
PRO   C   OXT  sing N N 445 
PRO   CB  CG   sing N N 446 
PRO   CB  HB2  sing N N 447 
PRO   CB  HB3  sing N N 448 
PRO   CG  CD   sing N N 449 
PRO   CG  HG2  sing N N 450 
PRO   CG  HG3  sing N N 451 
PRO   CD  HD2  sing N N 452 
PRO   CD  HD3  sing N N 453 
PRO   OXT HXT  sing N N 454 
SER   N   CA   sing N N 455 
SER   N   H    sing N N 456 
SER   N   H2   sing N N 457 
SER   CA  C    sing N N 458 
SER   CA  CB   sing N N 459 
SER   CA  HA   sing N N 460 
SER   C   O    doub N N 461 
SER   C   OXT  sing N N 462 
SER   CB  OG   sing N N 463 
SER   CB  HB2  sing N N 464 
SER   CB  HB3  sing N N 465 
SER   OG  HG   sing N N 466 
SER   OXT HXT  sing N N 467 
THR   N   CA   sing N N 468 
THR   N   H    sing N N 469 
THR   N   H2   sing N N 470 
THR   CA  C    sing N N 471 
THR   CA  CB   sing N N 472 
THR   CA  HA   sing N N 473 
THR   C   O    doub N N 474 
THR   C   OXT  sing N N 475 
THR   CB  OG1  sing N N 476 
THR   CB  CG2  sing N N 477 
THR   CB  HB   sing N N 478 
THR   OG1 HG1  sing N N 479 
THR   CG2 HG21 sing N N 480 
THR   CG2 HG22 sing N N 481 
THR   CG2 HG23 sing N N 482 
THR   OXT HXT  sing N N 483 
TRP   N   CA   sing N N 484 
TRP   N   H    sing N N 485 
TRP   N   H2   sing N N 486 
TRP   CA  C    sing N N 487 
TRP   CA  CB   sing N N 488 
TRP   CA  HA   sing N N 489 
TRP   C   O    doub N N 490 
TRP   C   OXT  sing N N 491 
TRP   CB  CG   sing N N 492 
TRP   CB  HB2  sing N N 493 
TRP   CB  HB3  sing N N 494 
TRP   CG  CD1  doub Y N 495 
TRP   CG  CD2  sing Y N 496 
TRP   CD1 NE1  sing Y N 497 
TRP   CD1 HD1  sing N N 498 
TRP   CD2 CE2  doub Y N 499 
TRP   CD2 CE3  sing Y N 500 
TRP   NE1 CE2  sing Y N 501 
TRP   NE1 HE1  sing N N 502 
TRP   CE2 CZ2  sing Y N 503 
TRP   CE3 CZ3  doub Y N 504 
TRP   CE3 HE3  sing N N 505 
TRP   CZ2 CH2  doub Y N 506 
TRP   CZ2 HZ2  sing N N 507 
TRP   CZ3 CH2  sing Y N 508 
TRP   CZ3 HZ3  sing N N 509 
TRP   CH2 HH2  sing N N 510 
TRP   OXT HXT  sing N N 511 
TYR   N   CA   sing N N 512 
TYR   N   H    sing N N 513 
TYR   N   H2   sing N N 514 
TYR   CA  C    sing N N 515 
TYR   CA  CB   sing N N 516 
TYR   CA  HA   sing N N 517 
TYR   C   O    doub N N 518 
TYR   C   OXT  sing N N 519 
TYR   CB  CG   sing N N 520 
TYR   CB  HB2  sing N N 521 
TYR   CB  HB3  sing N N 522 
TYR   CG  CD1  doub Y N 523 
TYR   CG  CD2  sing Y N 524 
TYR   CD1 CE1  sing Y N 525 
TYR   CD1 HD1  sing N N 526 
TYR   CD2 CE2  doub Y N 527 
TYR   CD2 HD2  sing N N 528 
TYR   CE1 CZ   doub Y N 529 
TYR   CE1 HE1  sing N N 530 
TYR   CE2 CZ   sing Y N 531 
TYR   CE2 HE2  sing N N 532 
TYR   CZ  OH   sing N N 533 
TYR   OH  HH   sing N N 534 
TYR   OXT HXT  sing N N 535 
VAL   N   CA   sing N N 536 
VAL   N   H    sing N N 537 
VAL   N   H2   sing N N 538 
VAL   CA  C    sing N N 539 
VAL   CA  CB   sing N N 540 
VAL   CA  HA   sing N N 541 
VAL   C   O    doub N N 542 
VAL   C   OXT  sing N N 543 
VAL   CB  CG1  sing N N 544 
VAL   CB  CG2  sing N N 545 
VAL   CB  HB   sing N N 546 
VAL   CG1 HG11 sing N N 547 
VAL   CG1 HG12 sing N N 548 
VAL   CG1 HG13 sing N N 549 
VAL   CG2 HG21 sing N N 550 
VAL   CG2 HG22 sing N N 551 
VAL   CG2 HG23 sing N N 552 
VAL   OXT HXT  sing N N 553 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of Environmental Health Sciences (NIH/NIEHS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ES025767 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5vcc 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9COW 
_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]   0.013125 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009991 
_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]   0.008233 
_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  
FE 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS   A 1 8   ? -8.608  -58.526 -14.852 1.00 172.93 ? 28  HIS   A N   1 
ATOM   2    C  CA  . HIS   A 1 8   ? -9.601  -58.700 -13.798 1.00 173.49 ? 28  HIS   A CA  1 
ATOM   3    C  C   . HIS   A 1 8   ? -11.001 -58.366 -14.301 1.00 173.79 ? 28  HIS   A C   1 
ATOM   4    O  O   . HIS   A 1 8   ? -11.574 -59.108 -15.096 1.00 176.52 ? 28  HIS   A O   1 
ATOM   5    C  CB  . HIS   A 1 8   ? -9.252  -57.834 -12.587 1.00 173.05 ? 28  HIS   A CB  1 
ATOM   6    C  CG  . HIS   A 1 8   ? -8.089  -58.347 -11.797 1.00 178.59 ? 28  HIS   A CG  1 
ATOM   7    N  ND1 . HIS   A 1 8   ? -7.225  -57.516 -11.118 1.00 181.84 ? 28  HIS   A ND1 1 
ATOM   8    C  CD2 . HIS   A 1 8   ? -7.651  -59.609 -11.573 1.00 178.30 ? 28  HIS   A CD2 1 
ATOM   9    C  CE1 . HIS   A 1 8   ? -6.303  -58.242 -10.513 1.00 181.07 ? 28  HIS   A CE1 1 
ATOM   10   N  NE2 . HIS   A 1 8   ? -6.539  -59.516 -10.772 1.00 180.21 ? 28  HIS   A NE2 1 
ATOM   11   N  N   . SER   A 1 9   ? -11.551 -57.243 -13.838 1.00 143.32 ? 29  SER   A N   1 
ATOM   12   C  CA  . SER   A 1 9   ? -12.851 -56.794 -14.321 1.00 131.91 ? 29  SER   A CA  1 
ATOM   13   C  C   . SER   A 1 9   ? -12.794 -56.239 -15.735 1.00 119.45 ? 29  SER   A C   1 
ATOM   14   O  O   . SER   A 1 9   ? -13.809 -55.725 -16.215 1.00 106.67 ? 29  SER   A O   1 
ATOM   15   C  CB  . SER   A 1 9   ? -13.431 -55.733 -13.384 1.00 123.75 ? 29  SER   A CB  1 
ATOM   16   O  OG  . SER   A 1 9   ? -12.629 -54.565 -13.385 1.00 113.80 ? 29  SER   A OG  1 
ATOM   17   N  N   . HIS   A 1 10  ? -11.646 -56.325 -16.411 1.00 115.28 ? 30  HIS   A N   1 
ATOM   18   C  CA  . HIS   A 1 10  ? -11.535 -55.787 -17.761 1.00 105.84 ? 30  HIS   A CA  1 
ATOM   19   C  C   . HIS   A 1 10  ? -12.347 -56.578 -18.776 1.00 108.32 ? 30  HIS   A C   1 
ATOM   20   O  O   . HIS   A 1 10  ? -12.564 -56.090 -19.890 1.00 108.81 ? 30  HIS   A O   1 
ATOM   21   C  CB  . HIS   A 1 10  ? -10.070 -55.740 -18.191 1.00 103.08 ? 30  HIS   A CB  1 
ATOM   22   C  CG  . HIS   A 1 10  ? -9.321  -54.564 -17.646 1.00 104.35 ? 30  HIS   A CG  1 
ATOM   23   N  ND1 . HIS   A 1 10  ? -8.036  -54.253 -18.036 1.00 96.78  ? 30  HIS   A ND1 1 
ATOM   24   C  CD2 . HIS   A 1 10  ? -9.680  -53.620 -16.745 1.00 92.30  ? 30  HIS   A CD2 1 
ATOM   25   C  CE1 . HIS   A 1 10  ? -7.634  -53.170 -17.395 1.00 92.07  ? 30  HIS   A CE1 1 
ATOM   26   N  NE2 . HIS   A 1 10  ? -8.613  -52.765 -16.605 1.00 89.57  ? 30  HIS   A NE2 1 
ATOM   27   N  N   . GLY   A 1 11  ? -12.795 -57.779 -18.429 1.00 115.07 ? 31  GLY   A N   1 
ATOM   28   C  CA  . GLY   A 1 11  ? -13.661 -58.539 -19.302 1.00 109.73 ? 31  GLY   A CA  1 
ATOM   29   C  C   . GLY   A 1 11  ? -15.137 -58.254 -19.135 1.00 106.57 ? 31  GLY   A C   1 
ATOM   30   O  O   . GLY   A 1 11  ? -15.965 -58.977 -19.699 1.00 110.89 ? 31  GLY   A O   1 
ATOM   31   N  N   . LEU   A 1 12  ? -15.494 -57.212 -18.383 1.00 106.25 ? 32  LEU   A N   1 
ATOM   32   C  CA  . LEU   A 1 12  ? -16.898 -56.951 -18.079 1.00 101.74 ? 32  LEU   A CA  1 
ATOM   33   C  C   . LEU   A 1 12  ? -17.667 -56.529 -19.325 1.00 101.18 ? 32  LEU   A C   1 
ATOM   34   O  O   . LEU   A 1 12  ? -18.639 -57.184 -19.721 1.00 103.68 ? 32  LEU   A O   1 
ATOM   35   C  CB  . LEU   A 1 12  ? -17.007 -55.880 -16.992 1.00 97.77  ? 32  LEU   A CB  1 
ATOM   36   C  CG  . LEU   A 1 12  ? -18.427 -55.544 -16.532 1.00 97.33  ? 32  LEU   A CG  1 
ATOM   37   C  CD1 . LEU   A 1 12  ? -19.032 -56.710 -15.764 1.00 96.81  ? 32  LEU   A CD1 1 
ATOM   38   C  CD2 . LEU   A 1 12  ? -18.439 -54.276 -15.695 1.00 90.70  ? 32  LEU   A CD2 1 
ATOM   39   N  N   . PHE   A 1 13  ? -17.246 -55.431 -19.960 1.00 98.44  ? 33  PHE   A N   1 
ATOM   40   C  CA  . PHE   A 1 13  ? -17.982 -54.923 -21.113 1.00 99.27  ? 33  PHE   A CA  1 
ATOM   41   C  C   . PHE   A 1 13  ? -17.940 -55.896 -22.285 1.00 102.76 ? 33  PHE   A C   1 
ATOM   42   O  O   . PHE   A 1 13  ? -18.840 -55.882 -23.133 1.00 105.83 ? 33  PHE   A O   1 
ATOM   43   C  CB  . PHE   A 1 13  ? -17.436 -53.557 -21.529 1.00 98.13  ? 33  PHE   A CB  1 
ATOM   44   C  CG  . PHE   A 1 13  ? -17.593 -52.498 -20.474 1.00 87.65  ? 33  PHE   A CG  1 
ATOM   45   C  CD1 . PHE   A 1 13  ? -18.851 -52.119 -20.036 1.00 83.74  ? 33  PHE   A CD1 1 
ATOM   46   C  CD2 . PHE   A 1 13  ? -16.484 -51.879 -19.925 1.00 83.91  ? 33  PHE   A CD2 1 
ATOM   47   C  CE1 . PHE   A 1 13  ? -18.999 -51.146 -19.065 1.00 84.79  ? 33  PHE   A CE1 1 
ATOM   48   C  CE2 . PHE   A 1 13  ? -16.624 -50.907 -18.954 1.00 80.51  ? 33  PHE   A CE2 1 
ATOM   49   C  CZ  . PHE   A 1 13  ? -17.883 -50.539 -18.524 1.00 78.89  ? 33  PHE   A CZ  1 
ATOM   50   N  N   . LYS   A 1 14  ? -16.910 -56.744 -22.354 1.00 98.51  ? 34  LYS   A N   1 
ATOM   51   C  CA  . LYS   A 1 14  ? -16.907 -57.809 -23.351 1.00 107.19 ? 34  LYS   A CA  1 
ATOM   52   C  C   . LYS   A 1 14  ? -18.035 -58.801 -23.095 1.00 105.72 ? 34  LYS   A C   1 
ATOM   53   O  O   . LYS   A 1 14  ? -18.703 -59.248 -24.034 1.00 102.71 ? 34  LYS   A O   1 
ATOM   54   C  CB  . LYS   A 1 14  ? -15.557 -58.529 -23.359 1.00 106.53 ? 34  LYS   A CB  1 
ATOM   55   C  CG  . LYS   A 1 14  ? -14.439 -57.780 -24.067 1.00 113.79 ? 34  LYS   A CG  1 
ATOM   56   C  CD  . LYS   A 1 14  ? -13.246 -58.697 -24.303 1.00 110.28 ? 34  LYS   A CD  1 
ATOM   57   C  CE  . LYS   A 1 14  ? -12.189 -58.036 -25.173 1.00 113.75 ? 34  LYS   A CE  1 
ATOM   58   N  NZ  . LYS   A 1 14  ? -11.090 -58.980 -25.525 1.00 117.40 ? 34  LYS   A NZ  1 
ATOM   59   N  N   . LYS   A 1 15  ? -18.264 -59.154 -21.828 1.00 112.03 ? 35  LYS   A N   1 
ATOM   60   C  CA  . LYS   A 1 15  ? -19.315 -60.111 -21.499 1.00 112.51 ? 35  LYS   A CA  1 
ATOM   61   C  C   . LYS   A 1 15  ? -20.706 -59.499 -21.577 1.00 113.71 ? 35  LYS   A C   1 
ATOM   62   O  O   . LYS   A 1 15  ? -21.693 -60.242 -21.601 1.00 117.10 ? 35  LYS   A O   1 
ATOM   63   C  CB  . LYS   A 1 15  ? -19.083 -60.691 -20.102 1.00 117.15 ? 35  LYS   A CB  1 
ATOM   64   C  CG  . LYS   A 1 15  ? -17.778 -61.454 -19.952 1.00 123.49 ? 35  LYS   A CG  1 
ATOM   65   C  CD  . LYS   A 1 15  ? -17.528 -61.844 -18.504 1.00 120.49 ? 35  LYS   A CD  1 
ATOM   66   C  CE  . LYS   A 1 15  ? -16.039 -61.913 -18.201 1.00 119.84 ? 35  LYS   A CE  1 
ATOM   67   N  NZ  . LYS   A 1 15  ? -15.300 -62.729 -19.204 1.00 128.09 ? 35  LYS   A NZ  1 
ATOM   68   N  N   . LEU   A 1 16  ? -20.809 -58.174 -21.616 1.00 112.27 ? 36  LEU   A N   1 
ATOM   69   C  CA  . LEU   A 1 16  ? -22.095 -57.496 -21.699 1.00 109.81 ? 36  LEU   A CA  1 
ATOM   70   C  C   . LEU   A 1 16  ? -22.504 -57.163 -23.127 1.00 111.59 ? 36  LEU   A C   1 
ATOM   71   O  O   . LEU   A 1 16  ? -23.609 -56.650 -23.335 1.00 111.28 ? 36  LEU   A O   1 
ATOM   72   C  CB  . LEU   A 1 16  ? -22.069 -56.209 -20.866 1.00 108.97 ? 36  LEU   A CB  1 
ATOM   73   C  CG  . LEU   A 1 16  ? -21.831 -56.349 -19.362 1.00 110.97 ? 36  LEU   A CG  1 
ATOM   74   C  CD1 . LEU   A 1 16  ? -21.704 -54.978 -18.715 1.00 107.76 ? 36  LEU   A CD1 1 
ATOM   75   C  CD2 . LEU   A 1 16  ? -22.948 -57.149 -18.708 1.00 116.77 ? 36  LEU   A CD2 1 
ATOM   76   N  N   . GLY   A 1 17  ? -21.654 -57.440 -24.112 1.00 108.11 ? 37  GLY   A N   1 
ATOM   77   C  CA  . GLY   A 1 17  ? -21.963 -57.053 -25.475 1.00 107.12 ? 37  GLY   A CA  1 
ATOM   78   C  C   . GLY   A 1 17  ? -21.924 -55.560 -25.705 1.00 97.28  ? 37  GLY   A C   1 
ATOM   79   O  O   . GLY   A 1 17  ? -22.611 -55.058 -26.601 1.00 87.44  ? 37  GLY   A O   1 
ATOM   80   N  N   . ILE   A 1 18  ? -21.138 -54.842 -24.920 1.00 99.27  ? 38  ILE   A N   1 
ATOM   81   C  CA  . ILE   A 1 18  ? -21.048 -53.384 -24.984 1.00 93.32  ? 38  ILE   A CA  1 
ATOM   82   C  C   . ILE   A 1 18  ? -19.692 -53.023 -25.569 1.00 90.66  ? 38  ILE   A C   1 
ATOM   83   O  O   . ILE   A 1 18  ? -18.664 -53.439 -25.028 1.00 86.24  ? 38  ILE   A O   1 
ATOM   84   C  CB  . ILE   A 1 18  ? -21.220 -52.737 -23.598 1.00 96.31  ? 38  ILE   A CB  1 
ATOM   85   C  CG1 . ILE   A 1 18  ? -22.577 -53.114 -23.002 1.00 100.21 ? 38  ILE   A CG1 1 
ATOM   86   C  CG2 . ILE   A 1 18  ? -21.055 -51.229 -23.692 1.00 93.98  ? 38  ILE   A CG2 1 
ATOM   87   C  CD1 . ILE   A 1 18  ? -22.781 -52.627 -21.590 1.00 101.69 ? 38  ILE   A CD1 1 
ATOM   88   N  N   . PRO   A 1 19  ? -19.648 -52.246 -26.646 1.00 93.59  ? 39  PRO   A N   1 
ATOM   89   C  CA  . PRO   A 1 19  ? -18.372 -51.924 -27.284 1.00 94.15  ? 39  PRO   A CA  1 
ATOM   90   C  C   . PRO   A 1 19  ? -17.576 -50.907 -26.477 1.00 90.82  ? 39  PRO   A C   1 
ATOM   91   O  O   . PRO   A 1 19  ? -18.033 -50.354 -25.476 1.00 88.57  ? 39  PRO   A O   1 
ATOM   92   C  CB  . PRO   A 1 19  ? -18.800 -51.344 -28.631 1.00 98.77  ? 39  PRO   A CB  1 
ATOM   93   C  CG  . PRO   A 1 19  ? -20.135 -50.758 -28.367 1.00 94.16  ? 39  PRO   A CG  1 
ATOM   94   C  CD  . PRO   A 1 19  ? -20.789 -51.645 -27.350 1.00 91.02  ? 39  PRO   A CD  1 
ATOM   95   N  N   . GLY   A 1 20  ? -16.364 -50.651 -26.958 1.00 92.03  ? 40  GLY   A N   1 
ATOM   96   C  CA  . GLY   A 1 20  ? -15.483 -49.689 -26.344 1.00 96.16  ? 40  GLY   A CA  1 
ATOM   97   C  C   . GLY   A 1 20  ? -14.034 -49.968 -26.679 1.00 96.74  ? 40  GLY   A C   1 
ATOM   98   O  O   . GLY   A 1 20  ? -13.694 -51.003 -27.262 1.00 95.76  ? 40  GLY   A O   1 
ATOM   99   N  N   . PRO   A 1 21  ? -13.146 -49.043 -26.314 1.00 92.30  ? 41  PRO   A N   1 
ATOM   100  C  CA  . PRO   A 1 21  ? -11.714 -49.255 -26.568 1.00 95.21  ? 41  PRO   A CA  1 
ATOM   101  C  C   . PRO   A 1 21  ? -11.171 -50.388 -25.709 1.00 92.97  ? 41  PRO   A C   1 
ATOM   102  O  O   . PRO   A 1 21  ? -11.413 -50.442 -24.501 1.00 93.07  ? 41  PRO   A O   1 
ATOM   103  C  CB  . PRO   A 1 21  ? -11.084 -47.908 -26.196 1.00 89.62  ? 41  PRO   A CB  1 
ATOM   104  C  CG  . PRO   A 1 21  ? -12.049 -47.295 -25.227 1.00 85.01  ? 41  PRO   A CG  1 
ATOM   105  C  CD  . PRO   A 1 21  ? -13.415 -47.753 -25.657 1.00 86.57  ? 41  PRO   A CD  1 
ATOM   106  N  N   . THR   A 1 22  ? -10.430 -51.292 -26.341 1.00 92.43  ? 42  THR   A N   1 
ATOM   107  C  CA  . THR   A 1 22  ? -9.899  -52.448 -25.633 1.00 91.46  ? 42  THR   A CA  1 
ATOM   108  C  C   . THR   A 1 22  ? -8.906  -51.992 -24.566 1.00 91.05  ? 42  THR   A C   1 
ATOM   109  O  O   . THR   A 1 22  ? -7.961  -51.255 -24.880 1.00 90.10  ? 42  THR   A O   1 
ATOM   110  C  CB  . THR   A 1 22  ? -9.225  -53.413 -26.606 1.00 95.27  ? 42  THR   A CB  1 
ATOM   111  O  OG1 . THR   A 1 22  ? -10.104 -53.666 -27.709 1.00 104.16 ? 42  THR   A OG1 1 
ATOM   112  C  CG2 . THR   A 1 22  ? -8.907  -54.731 -25.914 1.00 89.43  ? 42  THR   A CG2 1 
ATOM   113  N  N   . PRO   A 1 23  ? -9.083  -52.396 -23.312 1.00 91.01  ? 43  PRO   A N   1 
ATOM   114  C  CA  . PRO   A 1 23  ? -8.212  -51.897 -22.246 1.00 90.36  ? 43  PRO   A CA  1 
ATOM   115  C  C   . PRO   A 1 23  ? -6.881  -52.627 -22.189 1.00 94.40  ? 43  PRO   A C   1 
ATOM   116  O  O   . PRO   A 1 23  ? -6.768  -53.807 -22.531 1.00 97.27  ? 43  PRO   A O   1 
ATOM   117  C  CB  . PRO   A 1 23  ? -9.034  -52.162 -20.980 1.00 90.30  ? 43  PRO   A CB  1 
ATOM   118  C  CG  . PRO   A 1 23  ? -9.826  -53.380 -21.322 1.00 90.29  ? 43  PRO   A CG  1 
ATOM   119  C  CD  . PRO   A 1 23  ? -10.159 -53.258 -22.791 1.00 91.74  ? 43  PRO   A CD  1 
ATOM   120  N  N   . LEU   A 1 24  ? -5.864  -51.895 -21.747 1.00 92.93  ? 44  LEU   A N   1 
ATOM   121  C  CA  . LEU   A 1 24  ? -4.557  -52.447 -21.434 1.00 91.80  ? 44  LEU   A CA  1 
ATOM   122  C  C   . LEU   A 1 24  ? -4.528  -52.924 -19.990 1.00 93.68  ? 44  LEU   A C   1 
ATOM   123  O  O   . LEU   A 1 24  ? -5.314  -52.460 -19.159 1.00 94.25  ? 44  LEU   A O   1 
ATOM   124  C  CB  . LEU   A 1 24  ? -3.475  -51.394 -21.664 1.00 91.54  ? 44  LEU   A CB  1 
ATOM   125  C  CG  . LEU   A 1 24  ? -3.274  -50.919 -23.104 1.00 91.93  ? 44  LEU   A CG  1 
ATOM   126  C  CD1 . LEU   A 1 24  ? -2.280  -49.774 -23.150 1.00 93.53  ? 44  LEU   A CD1 1 
ATOM   127  C  CD2 . LEU   A 1 24  ? -2.809  -52.066 -23.988 1.00 96.89  ? 44  LEU   A CD2 1 
ATOM   128  N  N   . PRO   A 1 25  ? -3.644  -53.866 -19.659 1.00 97.52  ? 45  PRO   A N   1 
ATOM   129  C  CA  . PRO   A 1 25  ? -3.576  -54.354 -18.275 1.00 95.01  ? 45  PRO   A CA  1 
ATOM   130  C  C   . PRO   A 1 25  ? -3.282  -53.228 -17.292 1.00 95.03  ? 45  PRO   A C   1 
ATOM   131  O  O   . PRO   A 1 25  ? -2.479  -52.333 -17.567 1.00 95.77  ? 45  PRO   A O   1 
ATOM   132  C  CB  . PRO   A 1 25  ? -2.438  -55.378 -18.318 1.00 99.46  ? 45  PRO   A CB  1 
ATOM   133  C  CG  . PRO   A 1 25  ? -2.399  -55.833 -19.737 1.00 95.08  ? 45  PRO   A CG  1 
ATOM   134  C  CD  . PRO   A 1 25  ? -2.762  -54.631 -20.558 1.00 92.87  ? 45  PRO   A CD  1 
ATOM   135  N  N   . PHE   A 1 26  ? -3.972  -53.271 -16.148 1.00 99.84  ? 46  PHE   A N   1 
ATOM   136  C  CA  . PHE   A 1 26  ? -3.801  -52.330 -15.042 1.00 104.55 ? 46  PHE   A CA  1 
ATOM   137  C  C   . PHE   A 1 26  ? -4.229  -50.915 -15.416 1.00 102.56 ? 46  PHE   A C   1 
ATOM   138  O  O   . PHE   A 1 26  ? -4.996  -50.283 -14.681 1.00 102.37 ? 46  PHE   A O   1 
ATOM   139  C  CB  . PHE   A 1 26  ? -2.356  -52.349 -14.535 1.00 107.74 ? 46  PHE   A CB  1 
ATOM   140  C  CG  . PHE   A 1 26  ? -1.969  -53.635 -13.867 1.00 116.63 ? 46  PHE   A CG  1 
ATOM   141  C  CD1 . PHE   A 1 26  ? -2.457  -53.948 -12.610 1.00 123.19 ? 46  PHE   A CD1 1 
ATOM   142  C  CD2 . PHE   A 1 26  ? -1.117  -54.530 -14.493 1.00 118.28 ? 46  PHE   A CD2 1 
ATOM   143  C  CE1 . PHE   A 1 26  ? -2.106  -55.133 -11.987 1.00 129.08 ? 46  PHE   A CE1 1 
ATOM   144  C  CE2 . PHE   A 1 26  ? -0.759  -55.717 -13.875 1.00 121.61 ? 46  PHE   A CE2 1 
ATOM   145  C  CZ  . PHE   A 1 26  ? -1.255  -56.018 -12.620 1.00 130.49 ? 46  PHE   A CZ  1 
ATOM   146  N  N   . LEU   A 1 27  ? -3.740  -50.402 -16.546 1.00 97.70  ? 47  LEU   A N   1 
ATOM   147  C  CA  . LEU   A 1 27  ? -4.054  -49.032 -16.940 1.00 94.26  ? 47  LEU   A CA  1 
ATOM   148  C  C   . LEU   A 1 27  ? -5.461  -48.894 -17.507 1.00 92.08  ? 47  LEU   A C   1 
ATOM   149  O  O   . LEU   A 1 27  ? -6.060  -47.818 -17.402 1.00 88.70  ? 47  LEU   A O   1 
ATOM   150  C  CB  . LEU   A 1 27  ? -3.038  -48.532 -17.967 1.00 91.34  ? 47  LEU   A CB  1 
ATOM   151  C  CG  . LEU   A 1 27  ? -1.563  -48.604 -17.566 1.00 97.54  ? 47  LEU   A CG  1 
ATOM   152  C  CD1 . LEU   A 1 27  ? -0.689  -47.962 -18.630 1.00 98.20  ? 47  LEU   A CD1 1 
ATOM   153  C  CD2 . LEU   A 1 27  ? -1.346  -47.943 -16.214 1.00 109.44 ? 47  LEU   A CD2 1 
ATOM   154  N  N   . GLY   A 1 28  ? -6.004  -49.948 -18.110 1.00 90.10  ? 48  GLY   A N   1 
ATOM   155  C  CA  . GLY   A 1 28  ? -7.310  -49.843 -18.726 1.00 86.12  ? 48  GLY   A CA  1 
ATOM   156  C  C   . GLY   A 1 28  ? -7.249  -49.020 -19.994 1.00 86.32  ? 48  GLY   A C   1 
ATOM   157  O  O   . GLY   A 1 28  ? -6.533  -49.371 -20.937 1.00 87.40  ? 48  GLY   A O   1 
ATOM   158  N  N   . ASN   A 1 29  ? -7.980  -47.908 -20.025 1.00 83.51  ? 49  ASN   A N   1 
ATOM   159  C  CA  . ASN   A 1 29  ? -7.988  -47.023 -21.182 1.00 82.22  ? 49  ASN   A CA  1 
ATOM   160  C  C   . ASN   A 1 29  ? -7.455  -45.630 -20.864 1.00 82.96  ? 49  ASN   A C   1 
ATOM   161  O  O   . ASN   A 1 29  ? -7.648  -44.713 -21.673 1.00 84.49  ? 49  ASN   A O   1 
ATOM   162  C  CB  . ASN   A 1 29  ? -9.404  -46.916 -21.759 1.00 82.23  ? 49  ASN   A CB  1 
ATOM   163  C  CG  . ASN   A 1 29  ? -10.002 -48.269 -22.097 1.00 83.69  ? 49  ASN   A CG  1 
ATOM   164  O  OD1 . ASN   A 1 29  ? -10.761 -48.840 -21.314 1.00 78.97  ? 49  ASN   A OD1 1 
ATOM   165  N  ND2 . ASN   A 1 29  ? -9.668  -48.784 -23.274 1.00 86.76  ? 49  ASN   A ND2 1 
ATOM   166  N  N   . ILE   A 1 30  ? -6.786  -45.448 -19.718 1.00 84.78  ? 50  ILE   A N   1 
ATOM   167  C  CA  . ILE   A 1 30  ? -6.345  -44.121 -19.290 1.00 87.65  ? 50  ILE   A CA  1 
ATOM   168  C  C   . ILE   A 1 30  ? -5.318  -43.531 -20.241 1.00 88.00  ? 50  ILE   A C   1 
ATOM   169  O  O   . ILE   A 1 30  ? -5.106  -42.313 -20.250 1.00 91.86  ? 50  ILE   A O   1 
ATOM   170  C  CB  . ILE   A 1 30  ? -5.766  -44.174 -17.863 1.00 91.37  ? 50  ILE   A CB  1 
ATOM   171  C  CG1 . ILE   A 1 30  ? -4.499  -45.032 -17.835 1.00 90.31  ? 50  ILE   A CG1 1 
ATOM   172  C  CG2 . ILE   A 1 30  ? -6.810  -44.688 -16.881 1.00 93.17  ? 50  ILE   A CG2 1 
ATOM   173  C  CD1 . ILE   A 1 30  ? -3.484  -44.582 -16.826 1.00 95.76  ? 50  ILE   A CD1 1 
ATOM   174  N  N   . LEU   A 1 31  ? -4.662  -44.372 -21.039 1.00 85.83  ? 51  LEU   A N   1 
ATOM   175  C  CA  . LEU   A 1 31  ? -3.666  -43.870 -21.976 1.00 96.06  ? 51  LEU   A CA  1 
ATOM   176  C  C   . LEU   A 1 31  ? -4.287  -42.978 -23.046 1.00 92.21  ? 51  LEU   A C   1 
ATOM   177  O  O   . LEU   A 1 31  ? -3.622  -42.063 -23.545 1.00 94.52  ? 51  LEU   A O   1 
ATOM   178  C  CB  . LEU   A 1 31  ? -2.912  -45.035 -22.618 1.00 94.06  ? 51  LEU   A CB  1 
ATOM   179  C  CG  . LEU   A 1 31  ? -1.911  -45.786 -21.732 1.00 95.17  ? 51  LEU   A CG  1 
ATOM   180  C  CD1 . LEU   A 1 31  ? -0.881  -46.495 -22.594 1.00 94.12  ? 51  LEU   A CD1 1 
ATOM   181  C  CD2 . LEU   A 1 31  ? -1.230  -44.839 -20.760 1.00 96.08  ? 51  LEU   A CD2 1 
ATOM   182  N  N   . SER   A 1 32  ? -5.553  -43.217 -23.405 1.00 95.32  ? 52  SER   A N   1 
ATOM   183  C  CA  . SER   A 1 32  ? -6.220  -42.426 -24.433 1.00 94.90  ? 52  SER   A CA  1 
ATOM   184  C  C   . SER   A 1 32  ? -6.627  -41.034 -23.961 1.00 93.33  ? 52  SER   A C   1 
ATOM   185  O  O   . SER   A 1 32  ? -7.119  -40.239 -24.770 1.00 92.23  ? 52  SER   A O   1 
ATOM   186  C  CB  . SER   A 1 32  ? -7.531  -43.107 -24.852 1.00 95.58  ? 52  SER   A CB  1 
ATOM   187  O  OG  . SER   A 1 32  ? -7.419  -44.520 -24.907 1.00 94.59  ? 52  SER   A OG  1 
ATOM   188  N  N   . TYR   A 1 33  ? -6.414  -40.720 -22.684 1.00 90.92  ? 53  TYR   A N   1 
ATOM   189  C  CA  . TYR   A 1 33  ? -6.556  -39.374 -22.131 1.00 92.91  ? 53  TYR   A CA  1 
ATOM   190  C  C   . TYR   A 1 33  ? -5.430  -38.413 -22.503 1.00 93.19  ? 53  TYR   A C   1 
ATOM   191  O  O   . TYR   A 1 33  ? -5.416  -37.308 -21.957 1.00 90.28  ? 53  TYR   A O   1 
ATOM   192  C  CB  . TYR   A 1 33  ? -6.709  -39.438 -20.597 1.00 83.99  ? 53  TYR   A CB  1 
ATOM   193  C  CG  . TYR   A 1 33  ? -8.011  -40.053 -20.106 1.00 86.46  ? 53  TYR   A CG  1 
ATOM   194  C  CD1 . TYR   A 1 33  ? -9.159  -40.000 -20.888 1.00 85.34  ? 53  TYR   A CD1 1 
ATOM   195  C  CD2 . TYR   A 1 33  ? -8.094  -40.678 -18.858 1.00 82.31  ? 53  TYR   A CD2 1 
ATOM   196  C  CE1 . TYR   A 1 33  ? -10.325 -40.552 -20.453 1.00 86.23  ? 53  TYR   A CE1 1 
ATOM   197  C  CE2 . TYR   A 1 33  ? -9.271  -41.232 -18.425 1.00 82.03  ? 53  TYR   A CE2 1 
ATOM   198  C  CZ  . TYR   A 1 33  ? -10.370 -41.162 -19.227 1.00 80.12  ? 53  TYR   A CZ  1 
ATOM   199  O  OH  . TYR   A 1 33  ? -11.545 -41.710 -18.803 1.00 75.95  ? 53  TYR   A OH  1 
ATOM   200  N  N   . HIS   A 1 34  ? -4.532  -38.779 -23.419 1.00 94.10  ? 54  HIS   A N   1 
ATOM   201  C  CA  . HIS   A 1 34  ? -3.416  -37.903 -23.748 1.00 100.63 ? 54  HIS   A CA  1 
ATOM   202  C  C   . HIS   A 1 34  ? -3.855  -36.632 -24.453 1.00 99.41  ? 54  HIS   A C   1 
ATOM   203  O  O   . HIS   A 1 34  ? -3.021  -35.739 -24.632 1.00 100.53 ? 54  HIS   A O   1 
ATOM   204  C  CB  . HIS   A 1 34  ? -2.370  -38.610 -24.626 1.00 99.98  ? 54  HIS   A CB  1 
ATOM   205  C  CG  . HIS   A 1 34  ? -2.760  -38.732 -26.068 1.00 103.52 ? 54  HIS   A CG  1 
ATOM   206  N  ND1 . HIS   A 1 34  ? -3.634  -39.695 -26.521 1.00 101.10 ? 54  HIS   A ND1 1 
ATOM   207  C  CD2 . HIS   A 1 34  ? -2.370  -38.032 -27.162 1.00 103.65 ? 54  HIS   A CD2 1 
ATOM   208  C  CE1 . HIS   A 1 34  ? -3.781  -39.573 -27.828 1.00 103.48 ? 54  HIS   A CE1 1 
ATOM   209  N  NE2 . HIS   A 1 34  ? -3.025  -38.572 -28.242 1.00 106.33 ? 54  HIS   A NE2 1 
ATOM   210  N  N   . LYS   A 1 35  ? -5.116  -36.537 -24.886 1.00 100.93 ? 55  LYS   A N   1 
ATOM   211  C  CA  . LYS   A 1 35  ? -5.678  -35.290 -25.399 1.00 99.42  ? 55  LYS   A CA  1 
ATOM   212  C  C   . LYS   A 1 35  ? -6.839  -34.799 -24.545 1.00 96.76  ? 55  LYS   A C   1 
ATOM   213  O  O   . LYS   A 1 35  ? -7.730  -34.112 -25.053 1.00 99.10  ? 55  LYS   A O   1 
ATOM   214  C  CB  . LYS   A 1 35  ? -6.140  -35.441 -26.852 1.00 102.72 ? 55  LYS   A CB  1 
ATOM   215  C  CG  . LYS   A 1 35  ? -5.028  -35.736 -27.847 1.00 107.68 ? 55  LYS   A CG  1 
ATOM   216  C  CD  . LYS   A 1 35  ? -5.449  -35.339 -29.255 1.00 117.69 ? 55  LYS   A CD  1 
ATOM   217  C  CE  . LYS   A 1 35  ? -5.738  -33.844 -29.347 1.00 125.98 ? 55  LYS   A CE  1 
ATOM   218  N  NZ  . LYS   A 1 35  ? -4.549  -33.000 -29.033 1.00 125.36 ? 55  LYS   A NZ  1 
ATOM   219  N  N   . GLY   A 1 36  ? -6.869  -35.170 -23.269 1.00 101.31 ? 56  GLY   A N   1 
ATOM   220  C  CA  . GLY   A 1 36  ? -7.990  -34.837 -22.418 1.00 99.16  ? 56  GLY   A CA  1 
ATOM   221  C  C   . GLY   A 1 36  ? -9.120  -35.837 -22.548 1.00 97.02  ? 56  GLY   A C   1 
ATOM   222  O  O   . GLY   A 1 36  ? -9.314  -36.431 -23.616 1.00 97.53  ? 56  GLY   A O   1 
ATOM   223  N  N   . PHE   A 1 37  ? -9.887  -36.026 -21.474 1.00 86.23  ? 57  PHE   A N   1 
ATOM   224  C  CA  . PHE   A 1 37  ? -10.990 -36.974 -21.543 1.00 85.41  ? 57  PHE   A CA  1 
ATOM   225  C  C   . PHE   A 1 37  ? -12.124 -36.490 -22.440 1.00 82.82  ? 57  PHE   A C   1 
ATOM   226  O  O   . PHE   A 1 37  ? -12.894 -37.324 -22.926 1.00 84.00  ? 57  PHE   A O   1 
ATOM   227  C  CB  . PHE   A 1 37  ? -11.523 -37.295 -20.141 1.00 88.72  ? 57  PHE   A CB  1 
ATOM   228  C  CG  . PHE   A 1 37  ? -12.018 -36.100 -19.378 1.00 86.94  ? 57  PHE   A CG  1 
ATOM   229  C  CD1 . PHE   A 1 37  ? -13.293 -35.596 -19.590 1.00 91.52  ? 57  PHE   A CD1 1 
ATOM   230  C  CD2 . PHE   A 1 37  ? -11.213 -35.494 -18.432 1.00 94.54  ? 57  PHE   A CD2 1 
ATOM   231  C  CE1 . PHE   A 1 37  ? -13.747 -34.500 -18.882 1.00 88.59  ? 57  PHE   A CE1 1 
ATOM   232  C  CE2 . PHE   A 1 37  ? -11.661 -34.398 -17.719 1.00 98.79  ? 57  PHE   A CE2 1 
ATOM   233  C  CZ  . PHE   A 1 37  ? -12.929 -33.901 -17.945 1.00 98.39  ? 57  PHE   A CZ  1 
ATOM   234  N  N   . CYS   A 1 38  ? -12.246 -35.179 -22.678 1.00 82.39  ? 58  CYS   A N   1 
ATOM   235  C  CA  . CYS   A 1 38  ? -13.296 -34.691 -23.570 1.00 81.14  ? 58  CYS   A CA  1 
ATOM   236  C  C   . CYS   A 1 38  ? -13.074 -35.190 -24.992 1.00 79.79  ? 58  CYS   A C   1 
ATOM   237  O  O   . CYS   A 1 38  ? -13.997 -35.703 -25.636 1.00 76.77  ? 58  CYS   A O   1 
ATOM   238  C  CB  . CYS   A 1 38  ? -13.357 -33.162 -23.540 1.00 79.35  ? 58  CYS   A CB  1 
ATOM   239  S  SG  . CYS   A 1 38  ? -13.711 -32.455 -21.907 1.00 78.38  ? 58  CYS   A SG  1 
ATOM   240  N  N   . MET   A 1 39  ? -11.844 -35.049 -25.496 1.00 82.06  ? 59  MET   A N   1 
ATOM   241  C  CA  . MET   A 1 39  ? -11.508 -35.608 -26.801 1.00 82.77  ? 59  MET   A CA  1 
ATOM   242  C  C   . MET   A 1 39  ? -11.750 -37.112 -26.825 1.00 81.77  ? 59  MET   A C   1 
ATOM   243  O  O   . MET   A 1 39  ? -12.242 -37.657 -27.821 1.00 82.24  ? 59  MET   A O   1 
ATOM   244  C  CB  . MET   A 1 39  ? -10.051 -35.291 -27.140 1.00 90.43  ? 59  MET   A CB  1 
ATOM   245  C  CG  . MET   A 1 39  ? -9.602  -35.728 -28.526 1.00 98.43  ? 59  MET   A CG  1 
ATOM   246  S  SD  . MET   A 1 39  ? -10.134 -34.591 -29.821 1.00 111.00 ? 59  MET   A SD  1 
ATOM   247  C  CE  . MET   A 1 39  ? -8.974  -34.984 -31.131 1.00 110.51 ? 59  MET   A CE  1 
ATOM   248  N  N   . PHE   A 1 40  ? -11.422 -37.794 -25.724 1.00 81.09  ? 60  PHE   A N   1 
ATOM   249  C  CA  . PHE   A 1 40  ? -11.697 -39.223 -25.615 1.00 80.26  ? 60  PHE   A CA  1 
ATOM   250  C  C   . PHE   A 1 40  ? -13.195 -39.501 -25.639 1.00 79.26  ? 60  PHE   A C   1 
ATOM   251  O  O   . PHE   A 1 40  ? -13.649 -40.435 -26.311 1.00 78.87  ? 60  PHE   A O   1 
ATOM   252  C  CB  . PHE   A 1 40  ? -11.064 -39.775 -24.338 1.00 84.36  ? 60  PHE   A CB  1 
ATOM   253  C  CG  . PHE   A 1 40  ? -11.360 -41.225 -24.086 1.00 79.34  ? 60  PHE   A CG  1 
ATOM   254  C  CD1 . PHE   A 1 40  ? -10.776 -42.208 -24.862 1.00 82.29  ? 60  PHE   A CD1 1 
ATOM   255  C  CD2 . PHE   A 1 40  ? -12.207 -41.605 -23.058 1.00 78.18  ? 60  PHE   A CD2 1 
ATOM   256  C  CE1 . PHE   A 1 40  ? -11.034 -43.547 -24.626 1.00 85.91  ? 60  PHE   A CE1 1 
ATOM   257  C  CE2 . PHE   A 1 40  ? -12.472 -42.943 -22.817 1.00 81.47  ? 60  PHE   A CE2 1 
ATOM   258  C  CZ  . PHE   A 1 40  ? -11.886 -43.914 -23.603 1.00 82.07  ? 60  PHE   A CZ  1 
ATOM   259  N  N   . ASP   A 1 41  ? -13.981 -38.695 -24.921 1.00 72.38  ? 61  ASP   A N   1 
ATOM   260  C  CA  . ASP   A 1 41  ? -15.423 -38.920 -24.889 1.00 78.53  ? 61  ASP   A CA  1 
ATOM   261  C  C   . ASP   A 1 41  ? -16.054 -38.654 -26.250 1.00 84.87  ? 61  ASP   A C   1 
ATOM   262  O  O   . ASP   A 1 41  ? -16.932 -39.405 -26.694 1.00 85.59  ? 61  ASP   A O   1 
ATOM   263  C  CB  . ASP   A 1 41  ? -16.074 -38.042 -23.819 1.00 76.66  ? 61  ASP   A CB  1 
ATOM   264  C  CG  . ASP   A 1 41  ? -15.682 -38.447 -22.409 1.00 78.54  ? 61  ASP   A CG  1 
ATOM   265  O  OD1 . ASP   A 1 41  ? -14.864 -39.379 -22.256 1.00 78.21  ? 61  ASP   A OD1 1 
ATOM   266  O  OD2 . ASP   A 1 41  ? -16.194 -37.830 -21.450 1.00 73.92  ? 61  ASP   A OD2 1 
ATOM   267  N  N   . MET   A 1 42  ? -15.617 -37.590 -26.930 1.00 80.70  ? 62  MET   A N   1 
ATOM   268  C  CA  A MET   A 1 42  ? -16.183 -37.268 -28.236 0.35 83.27  ? 62  MET   A CA  1 
ATOM   269  C  CA  B MET   A 1 42  ? -16.183 -37.267 -28.236 0.65 84.44  ? 62  MET   A CA  1 
ATOM   270  C  C   . MET   A 1 42  ? -15.822 -38.321 -29.273 1.00 82.76  ? 62  MET   A C   1 
ATOM   271  O  O   . MET   A 1 42  ? -16.676 -38.737 -30.064 1.00 82.77  ? 62  MET   A O   1 
ATOM   272  C  CB  A MET   A 1 42  ? -15.713 -35.887 -28.692 0.35 80.77  ? 62  MET   A CB  1 
ATOM   273  C  CB  B MET   A 1 42  ? -15.713 -35.883 -28.687 0.65 80.66  ? 62  MET   A CB  1 
ATOM   274  C  CG  A MET   A 1 42  ? -16.320 -34.729 -27.914 0.35 78.82  ? 62  MET   A CG  1 
ATOM   275  C  CG  B MET   A 1 42  ? -16.164 -34.750 -27.781 0.65 79.65  ? 62  MET   A CG  1 
ATOM   276  S  SD  A MET   A 1 42  ? -17.177 -33.554 -28.984 0.35 78.48  ? 62  MET   A SD  1 
ATOM   277  S  SD  B MET   A 1 42  ? -15.684 -33.132 -28.407 0.65 71.13  ? 62  MET   A SD  1 
ATOM   278  C  CE  A MET   A 1 42  ? -15.846 -33.058 -30.076 0.35 76.36  ? 62  MET   A CE  1 
ATOM   279  C  CE  B MET   A 1 42  ? -16.625 -33.072 -29.931 0.65 74.89  ? 62  MET   A CE  1 
ATOM   280  N  N   . GLU   A 1 43  ? -14.564 -38.768 -29.287 1.00 82.35  ? 63  GLU   A N   1 
ATOM   281  C  CA  . GLU   A 1 43  ? -14.160 -39.772 -30.266 1.00 86.76  ? 63  GLU   A CA  1 
ATOM   282  C  C   . GLU   A 1 43  ? -14.828 -41.115 -29.992 1.00 87.53  ? 63  GLU   A C   1 
ATOM   283  O  O   . GLU   A 1 43  ? -15.245 -41.808 -30.927 1.00 91.92  ? 63  GLU   A O   1 
ATOM   284  C  CB  . GLU   A 1 43  ? -12.638 -39.913 -30.278 1.00 88.61  ? 63  GLU   A CB  1 
ATOM   285  C  CG  . GLU   A 1 43  ? -11.906 -38.699 -30.833 1.00 96.28  ? 63  GLU   A CG  1 
ATOM   286  C  CD  . GLU   A 1 43  ? -10.505 -39.034 -31.305 1.00 107.79 ? 63  GLU   A CD  1 
ATOM   287  O  OE1 . GLU   A 1 43  ? -10.285 -40.181 -31.749 1.00 114.12 ? 63  GLU   A OE1 1 
ATOM   288  O  OE2 . GLU   A 1 43  ? -9.622  -38.154 -31.231 1.00 110.77 ? 63  GLU   A OE2 1 
ATOM   289  N  N   . CYS   A 1 44  ? -14.938 -41.501 -28.718 1.00 89.64  ? 64  CYS   A N   1 
ATOM   290  C  CA  . CYS   A 1 44  ? -15.678 -42.713 -28.382 1.00 88.98  ? 64  CYS   A CA  1 
ATOM   291  C  C   . CYS   A 1 44  ? -17.154 -42.572 -28.717 1.00 89.46  ? 64  CYS   A C   1 
ATOM   292  O  O   . CYS   A 1 44  ? -17.803 -43.558 -29.087 1.00 87.48  ? 64  CYS   A O   1 
ATOM   293  C  CB  . CYS   A 1 44  ? -15.503 -43.053 -26.902 1.00 82.88  ? 64  CYS   A CB  1 
ATOM   294  S  SG  . CYS   A 1 44  ? -13.867 -43.677 -26.466 1.00 77.60  ? 64  CYS   A SG  1 
ATOM   295  N  N   . HIS   A 1 45  ? -17.698 -41.359 -28.595 1.00 87.32  ? 65  HIS   A N   1 
ATOM   296  C  CA  . HIS   A 1 45  ? -19.095 -41.132 -28.949 1.00 86.84  ? 65  HIS   A CA  1 
ATOM   297  C  C   . HIS   A 1 45  ? -19.330 -41.343 -30.436 1.00 92.11  ? 65  HIS   A C   1 
ATOM   298  O  O   . HIS   A 1 45  ? -20.417 -41.773 -30.838 1.00 93.52  ? 65  HIS   A O   1 
ATOM   299  C  CB  . HIS   A 1 45  ? -19.516 -39.720 -28.538 1.00 90.66  ? 65  HIS   A CB  1 
ATOM   300  C  CG  . HIS   A 1 45  ? -20.968 -39.424 -28.760 1.00 93.16  ? 65  HIS   A CG  1 
ATOM   301  N  ND1 . HIS   A 1 45  ? -21.890 -40.394 -29.094 1.00 95.33  ? 65  HIS   A ND1 1 
ATOM   302  C  CD2 . HIS   A 1 45  ? -21.657 -38.260 -28.690 1.00 91.49  ? 65  HIS   A CD2 1 
ATOM   303  C  CE1 . HIS   A 1 45  ? -23.082 -39.839 -29.223 1.00 93.16  ? 65  HIS   A CE1 1 
ATOM   304  N  NE2 . HIS   A 1 45  ? -22.968 -38.545 -28.983 1.00 90.76  ? 65  HIS   A NE2 1 
ATOM   305  N  N   . LYS   A 1 46  ? -18.323 -41.067 -31.265 1.00 94.60  ? 66  LYS   A N   1 
ATOM   306  C  CA  . LYS   A 1 46  ? -18.469 -41.193 -32.709 1.00 98.24  ? 66  LYS   A CA  1 
ATOM   307  C  C   . LYS   A 1 46  ? -18.169 -42.598 -33.214 1.00 102.23 ? 66  LYS   A C   1 
ATOM   308  O  O   . LYS   A 1 46  ? -18.712 -43.006 -34.247 1.00 103.98 ? 66  LYS   A O   1 
ATOM   309  C  CB  . LYS   A 1 46  ? -17.558 -40.183 -33.417 1.00 100.79 ? 66  LYS   A CB  1 
ATOM   310  C  CG  . LYS   A 1 46  ? -17.826 -40.035 -34.906 1.00 112.33 ? 66  LYS   A CG  1 
ATOM   311  C  CD  . LYS   A 1 46  ? -17.128 -38.812 -35.477 1.00 119.25 ? 66  LYS   A CD  1 
ATOM   312  C  CE  . LYS   A 1 46  ? -17.513 -38.592 -36.931 1.00 131.83 ? 66  LYS   A CE  1 
ATOM   313  N  NZ  . LYS   A 1 46  ? -16.958 -37.318 -37.467 1.00 139.85 ? 66  LYS   A NZ  1 
ATOM   314  N  N   . LYS   A 1 47  ? -17.331 -43.352 -32.505 1.00 104.79 ? 67  LYS   A N   1 
ATOM   315  C  CA  . LYS   A 1 47  ? -16.939 -44.681 -32.959 1.00 110.96 ? 67  LYS   A CA  1 
ATOM   316  C  C   . LYS   A 1 47  ? -17.858 -45.782 -32.447 1.00 108.96 ? 67  LYS   A C   1 
ATOM   317  O  O   . LYS   A 1 47  ? -18.015 -46.807 -33.120 1.00 114.12 ? 67  LYS   A O   1 
ATOM   318  C  CB  . LYS   A 1 47  ? -15.495 -44.973 -32.537 1.00 109.26 ? 67  LYS   A CB  1 
ATOM   319  C  CG  . LYS   A 1 47  ? -14.946 -46.307 -33.026 1.00 113.50 ? 67  LYS   A CG  1 
ATOM   320  C  CD  . LYS   A 1 47  ? -13.480 -46.193 -33.411 1.00 114.56 ? 67  LYS   A CD  1 
ATOM   321  C  CE  . LYS   A 1 47  ? -12.641 -45.659 -32.262 1.00 115.08 ? 67  LYS   A CE  1 
ATOM   322  N  NZ  . LYS   A 1 47  ? -11.235 -45.398 -32.681 1.00 118.03 ? 67  LYS   A NZ  1 
ATOM   323  N  N   . TYR   A 1 48  ? -18.487 -45.594 -31.284 1.00 103.64 ? 68  TYR   A N   1 
ATOM   324  C  CA  . TYR   A 1 48  ? -19.261 -46.655 -30.658 1.00 101.49 ? 68  TYR   A CA  1 
ATOM   325  C  C   . TYR   A 1 48  ? -20.748 -46.360 -30.518 1.00 98.92  ? 68  TYR   A C   1 
ATOM   326  O  O   . TYR   A 1 48  ? -21.517 -47.295 -30.272 1.00 100.54 ? 68  TYR   A O   1 
ATOM   327  C  CB  . TYR   A 1 48  ? -18.686 -46.985 -29.272 1.00 99.30  ? 68  TYR   A CB  1 
ATOM   328  C  CG  . TYR   A 1 48  ? -17.215 -47.330 -29.315 1.00 99.23  ? 68  TYR   A CG  1 
ATOM   329  C  CD1 . TYR   A 1 48  ? -16.777 -48.503 -29.914 1.00 101.20 ? 68  TYR   A CD1 1 
ATOM   330  C  CD2 . TYR   A 1 48  ? -16.264 -46.480 -28.766 1.00 97.73  ? 68  TYR   A CD2 1 
ATOM   331  C  CE1 . TYR   A 1 48  ? -15.435 -48.823 -29.963 1.00 101.46 ? 68  TYR   A CE1 1 
ATOM   332  C  CE2 . TYR   A 1 48  ? -14.917 -46.792 -28.809 1.00 99.30  ? 68  TYR   A CE2 1 
ATOM   333  C  CZ  . TYR   A 1 48  ? -14.509 -47.965 -29.409 1.00 99.41  ? 68  TYR   A CZ  1 
ATOM   334  O  OH  . TYR   A 1 48  ? -13.171 -48.284 -29.457 1.00 96.71  ? 68  TYR   A OH  1 
ATOM   335  N  N   . GLY   A 1 49  ? -21.175 -45.108 -30.660 1.00 97.11  ? 69  GLY   A N   1 
ATOM   336  C  CA  . GLY   A 1 49  ? -22.593 -44.807 -30.673 1.00 98.52  ? 69  GLY   A CA  1 
ATOM   337  C  C   . GLY   A 1 49  ? -23.155 -44.266 -29.374 1.00 94.67  ? 69  GLY   A C   1 
ATOM   338  O  O   . GLY   A 1 49  ? -22.508 -43.471 -28.686 1.00 93.64  ? 69  GLY   A O   1 
ATOM   339  N  N   . LYS   A 1 50  ? -24.370 -44.702 -29.029 1.00 93.76  ? 70  LYS   A N   1 
ATOM   340  C  CA  . LYS   A 1 50  ? -25.084 -44.123 -27.897 1.00 94.13  ? 70  LYS   A CA  1 
ATOM   341  C  C   . LYS   A 1 50  ? -24.566 -44.626 -26.555 1.00 92.30  ? 70  LYS   A C   1 
ATOM   342  O  O   . LYS   A 1 50  ? -24.640 -43.897 -25.560 1.00 92.28  ? 70  LYS   A O   1 
ATOM   343  C  CB  . LYS   A 1 50  ? -26.584 -44.406 -28.024 1.00 94.21  ? 70  LYS   A CB  1 
ATOM   344  C  CG  . LYS   A 1 50  ? -26.942 -45.878 -28.164 1.00 106.41 ? 70  LYS   A CG  1 
ATOM   345  C  CD  . LYS   A 1 50  ? -28.434 -46.060 -28.403 1.00 113.63 ? 70  LYS   A CD  1 
ATOM   346  C  CE  . LYS   A 1 50  ? -29.252 -45.466 -27.268 1.00 109.13 ? 70  LYS   A CE  1 
ATOM   347  N  NZ  . LYS   A 1 50  ? -28.942 -46.113 -25.964 1.00 106.58 ? 70  LYS   A NZ  1 
ATOM   348  N  N   . VAL   A 1 51  ? -24.052 -45.854 -26.498 1.00 91.42  ? 71  VAL   A N   1 
ATOM   349  C  CA  . VAL   A 1 51  ? -23.537 -46.440 -25.266 1.00 87.61  ? 71  VAL   A CA  1 
ATOM   350  C  C   . VAL   A 1 51  ? -22.188 -47.083 -25.556 1.00 86.10  ? 71  VAL   A C   1 
ATOM   351  O  O   . VAL   A 1 51  ? -22.000 -47.704 -26.609 1.00 96.06  ? 71  VAL   A O   1 
ATOM   352  C  CB  . VAL   A 1 51  ? -24.511 -47.482 -24.669 1.00 88.43  ? 71  VAL   A CB  1 
ATOM   353  C  CG1 . VAL   A 1 51  ? -24.034 -47.935 -23.295 1.00 85.72  ? 71  VAL   A CG1 1 
ATOM   354  C  CG2 . VAL   A 1 51  ? -25.926 -46.927 -24.588 1.00 91.78  ? 71  VAL   A CG2 1 
ATOM   355  N  N   . TRP   A 1 52  ? -21.251 -46.936 -24.621 1.00 87.61  ? 72  TRP   A N   1 
ATOM   356  C  CA  . TRP   A 1 52  ? -19.963 -47.611 -24.707 1.00 86.80  ? 72  TRP   A CA  1 
ATOM   357  C  C   . TRP   A 1 52  ? -19.348 -47.666 -23.317 1.00 84.71  ? 72  TRP   A C   1 
ATOM   358  O  O   . TRP   A 1 52  ? -19.719 -46.903 -22.422 1.00 76.04  ? 72  TRP   A O   1 
ATOM   359  C  CB  . TRP   A 1 52  ? -19.017 -46.916 -25.692 1.00 86.67  ? 72  TRP   A CB  1 
ATOM   360  C  CG  . TRP   A 1 52  ? -18.528 -45.575 -25.233 1.00 84.16  ? 72  TRP   A CG  1 
ATOM   361  C  CD1 . TRP   A 1 52  ? -17.378 -45.313 -24.546 1.00 83.10  ? 72  TRP   A CD1 1 
ATOM   362  C  CD2 . TRP   A 1 52  ? -19.170 -44.311 -25.438 1.00 84.80  ? 72  TRP   A CD2 1 
ATOM   363  N  NE1 . TRP   A 1 52  ? -17.267 -43.966 -24.305 1.00 82.27  ? 72  TRP   A NE1 1 
ATOM   364  C  CE2 . TRP   A 1 52  ? -18.352 -43.327 -24.846 1.00 85.11  ? 72  TRP   A CE2 1 
ATOM   365  C  CE3 . TRP   A 1 52  ? -20.355 -43.915 -26.064 1.00 88.07  ? 72  TRP   A CE3 1 
ATOM   366  C  CZ2 . TRP   A 1 52  ? -18.685 -41.975 -24.858 1.00 80.84  ? 72  TRP   A CZ2 1 
ATOM   367  C  CZ3 . TRP   A 1 52  ? -20.683 -42.572 -26.075 1.00 86.28  ? 72  TRP   A CZ3 1 
ATOM   368  C  CH2 . TRP   A 1 52  ? -19.851 -41.618 -25.476 1.00 82.99  ? 72  TRP   A CH2 1 
ATOM   369  N  N   . GLY   A 1 53  ? -18.400 -48.579 -23.151 1.00 79.54  ? 73  GLY   A N   1 
ATOM   370  C  CA  . GLY   A 1 53  ? -17.739 -48.763 -21.876 1.00 77.05  ? 73  GLY   A CA  1 
ATOM   371  C  C   . GLY   A 1 53  ? -16.233 -48.733 -22.019 1.00 77.72  ? 73  GLY   A C   1 
ATOM   372  O  O   . GLY   A 1 53  ? -15.674 -49.105 -23.051 1.00 79.76  ? 73  GLY   A O   1 
ATOM   373  N  N   . PHE   A 1 54  ? -15.577 -48.278 -20.955 1.00 71.49  ? 74  PHE   A N   1 
ATOM   374  C  CA  . PHE   A 1 54  ? -14.124 -48.233 -20.899 1.00 79.09  ? 74  PHE   A CA  1 
ATOM   375  C  C   . PHE   A 1 54  ? -13.700 -48.401 -19.446 1.00 72.99  ? 74  PHE   A C   1 
ATOM   376  O  O   . PHE   A 1 54  ? -14.533 -48.584 -18.554 1.00 74.63  ? 74  PHE   A O   1 
ATOM   377  C  CB  . PHE   A 1 54  ? -13.584 -46.935 -21.508 1.00 78.93  ? 74  PHE   A CB  1 
ATOM   378  C  CG  . PHE   A 1 54  ? -14.007 -45.699 -20.771 1.00 74.41  ? 74  PHE   A CG  1 
ATOM   379  C  CD1 . PHE   A 1 54  ? -15.215 -45.085 -21.055 1.00 71.87  ? 74  PHE   A CD1 1 
ATOM   380  C  CD2 . PHE   A 1 54  ? -13.194 -45.151 -19.795 1.00 74.65  ? 74  PHE   A CD2 1 
ATOM   381  C  CE1 . PHE   A 1 54  ? -15.604 -43.949 -20.375 1.00 69.61  ? 74  PHE   A CE1 1 
ATOM   382  C  CE2 . PHE   A 1 54  ? -13.577 -44.018 -19.112 1.00 73.08  ? 74  PHE   A CE2 1 
ATOM   383  C  CZ  . PHE   A 1 54  ? -14.783 -43.414 -19.403 1.00 71.34  ? 74  PHE   A CZ  1 
ATOM   384  N  N   . TYR   A 1 55  ? -12.393 -48.333 -19.208 1.00 75.10  ? 75  TYR   A N   1 
ATOM   385  C  CA  . TYR   A 1 55  ? -11.832 -48.607 -17.890 1.00 81.04  ? 75  TYR   A CA  1 
ATOM   386  C  C   . TYR   A 1 55  ? -10.857 -47.507 -17.504 1.00 78.26  ? 75  TYR   A C   1 
ATOM   387  O  O   . TYR   A 1 55  ? -9.863  -47.282 -18.202 1.00 77.27  ? 75  TYR   A O   1 
ATOM   388  C  CB  . TYR   A 1 55  ? -11.130 -49.968 -17.866 1.00 83.48  ? 75  TYR   A CB  1 
ATOM   389  C  CG  . TYR   A 1 55  ? -12.035 -51.130 -18.202 1.00 80.31  ? 75  TYR   A CG  1 
ATOM   390  C  CD1 . TYR   A 1 55  ? -12.221 -51.532 -19.518 1.00 85.24  ? 75  TYR   A CD1 1 
ATOM   391  C  CD2 . TYR   A 1 55  ? -12.703 -51.826 -17.204 1.00 86.21  ? 75  TYR   A CD2 1 
ATOM   392  C  CE1 . TYR   A 1 55  ? -13.046 -52.593 -19.830 1.00 91.86  ? 75  TYR   A CE1 1 
ATOM   393  C  CE2 . TYR   A 1 55  ? -13.531 -52.887 -17.506 1.00 88.28  ? 75  TYR   A CE2 1 
ATOM   394  C  CZ  . TYR   A 1 55  ? -13.698 -53.268 -18.821 1.00 91.09  ? 75  TYR   A CZ  1 
ATOM   395  O  OH  . TYR   A 1 55  ? -14.522 -54.326 -19.131 1.00 93.75  ? 75  TYR   A OH  1 
ATOM   396  N  N   . ASP   A 1 56  ? -11.142 -46.827 -16.396 1.00 77.88  ? 76  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 56  ? -10.165 -45.962 -15.739 1.00 79.41  ? 76  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 56  ? -9.358  -46.849 -14.801 1.00 84.67  ? 76  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 56  ? -9.766  -47.108 -13.667 1.00 88.14  ? 76  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 56  ? -10.854 -44.828 -14.990 1.00 80.88  ? 76  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 56  ? -11.603 -43.894 -15.913 1.00 83.81  ? 76  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 56  ? -11.176 -43.745 -17.078 1.00 79.14  ? 76  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 56  ? -12.615 -43.309 -15.477 1.00 83.12  ? 76  ASP   A OD2 1 
ATOM   404  N  N   . GLY   A 1 57  ? -8.213  -47.325 -15.277 1.00 91.06  ? 77  GLY   A N   1 
ATOM   405  C  CA  . GLY   A 1 57  ? -7.508  -48.364 -14.560 1.00 95.61  ? 77  GLY   A CA  1 
ATOM   406  C  C   . GLY   A 1 57  ? -8.262  -49.671 -14.681 1.00 91.40  ? 77  GLY   A C   1 
ATOM   407  O  O   . GLY   A 1 57  ? -8.444  -50.190 -15.786 1.00 91.14  ? 77  GLY   A O   1 
ATOM   408  N  N   . GLN   A 1 58  ? -8.718  -50.212 -13.556 1.00 90.04  ? 78  GLN   A N   1 
ATOM   409  C  CA  . GLN   A 1 58  ? -9.576  -51.388 -13.554 1.00 89.38  ? 78  GLN   A CA  1 
ATOM   410  C  C   . GLN   A 1 58  ? -11.017 -51.042 -13.205 1.00 82.63  ? 78  GLN   A C   1 
ATOM   411  O  O   . GLN   A 1 58  ? -11.825 -51.949 -12.980 1.00 81.30  ? 78  GLN   A O   1 
ATOM   412  C  CB  . GLN   A 1 58  ? -9.034  -52.443 -12.586 1.00 96.48  ? 78  GLN   A CB  1 
ATOM   413  C  CG  . GLN   A 1 58  ? -7.714  -53.059 -13.021 1.00 102.19 ? 78  GLN   A CG  1 
ATOM   414  C  CD  . GLN   A 1 58  ? -7.198  -54.100 -12.046 1.00 123.12 ? 78  GLN   A CD  1 
ATOM   415  O  OE1 . GLN   A 1 58  ? -7.640  -54.168 -10.897 1.00 130.87 ? 78  GLN   A OE1 1 
ATOM   416  N  NE2 . GLN   A 1 58  ? -6.259  -54.920 -12.502 1.00 127.76 ? 78  GLN   A NE2 1 
ATOM   417  N  N   . GLN   A 1 59  ? -11.356 -49.752 -13.152 1.00 84.10  ? 79  GLN   A N   1 
ATOM   418  C  CA  . GLN   A 1 59  ? -12.708 -49.322 -12.822 1.00 74.41  ? 79  GLN   A CA  1 
ATOM   419  C  C   . GLN   A 1 59  ? -13.540 -49.256 -14.095 1.00 75.32  ? 79  GLN   A C   1 
ATOM   420  O  O   . GLN   A 1 59  ? -13.250 -48.423 -14.968 1.00 79.35  ? 79  GLN   A O   1 
ATOM   421  C  CB  . GLN   A 1 59  ? -12.687 -47.964 -12.133 1.00 78.67  ? 79  GLN   A CB  1 
ATOM   422  C  CG  . GLN   A 1 59  ? -14.059 -47.334 -11.972 1.00 79.07  ? 79  GLN   A CG  1 
ATOM   423  C  CD  . GLN   A 1 59  ? -14.971 -48.151 -11.083 1.00 66.80  ? 79  GLN   A CD  1 
ATOM   424  O  OE1 . GLN   A 1 59  ? -14.535 -48.725 -10.085 1.00 79.94  ? 79  GLN   A OE1 1 
ATOM   425  N  NE2 . GLN   A 1 59  ? -16.246 -48.212 -11.444 1.00 66.72  ? 79  GLN   A NE2 1 
ATOM   426  N  N   . PRO   A 1 60  ? -14.565 -50.093 -14.253 1.00 75.20  ? 80  PRO   A N   1 
ATOM   427  C  CA  . PRO   A 1 60  ? -15.399 -50.014 -15.460 1.00 79.20  ? 80  PRO   A CA  1 
ATOM   428  C  C   . PRO   A 1 60  ? -16.301 -48.789 -15.416 1.00 71.02  ? 80  PRO   A C   1 
ATOM   429  O  O   . PRO   A 1 60  ? -16.951 -48.515 -14.405 1.00 67.16  ? 80  PRO   A O   1 
ATOM   430  C  CB  . PRO   A 1 60  ? -16.207 -51.315 -15.417 1.00 74.29  ? 80  PRO   A CB  1 
ATOM   431  C  CG  . PRO   A 1 60  ? -16.274 -51.656 -13.963 1.00 77.93  ? 80  PRO   A CG  1 
ATOM   432  C  CD  . PRO   A 1 60  ? -14.977 -51.190 -13.360 1.00 77.53  ? 80  PRO   A CD  1 
ATOM   433  N  N   . VAL   A 1 61  ? -16.326 -48.048 -16.520 1.00 73.29  ? 81  VAL   A N   1 
ATOM   434  C  CA  . VAL   A 1 61  ? -17.151 -46.854 -16.659 1.00 73.67  ? 81  VAL   A CA  1 
ATOM   435  C  C   . VAL   A 1 61  ? -18.062 -47.043 -17.862 1.00 70.09  ? 81  VAL   A C   1 
ATOM   436  O  O   . VAL   A 1 61  ? -17.586 -47.329 -18.967 1.00 67.05  ? 81  VAL   A O   1 
ATOM   437  C  CB  . VAL   A 1 61  ? -16.295 -45.584 -16.816 1.00 76.47  ? 81  VAL   A CB  1 
ATOM   438  C  CG1 . VAL   A 1 61  ? -17.184 -44.353 -16.858 1.00 66.22  ? 81  VAL   A CG1 1 
ATOM   439  C  CG2 . VAL   A 1 61  ? -15.281 -45.479 -15.689 1.00 71.09  ? 81  VAL   A CG2 1 
ATOM   440  N  N   . LEU   A 1 62  ? -19.366 -46.887 -17.646 1.00 72.46  ? 82  LEU   A N   1 
ATOM   441  C  CA  . LEU   A 1 62  ? -20.360 -47.013 -18.704 1.00 74.18  ? 82  LEU   A CA  1 
ATOM   442  C  C   . LEU   A 1 62  ? -20.819 -45.623 -19.123 1.00 71.52  ? 82  LEU   A C   1 
ATOM   443  O  O   . LEU   A 1 62  ? -21.407 -44.891 -18.320 1.00 73.21  ? 82  LEU   A O   1 
ATOM   444  C  CB  . LEU   A 1 62  ? -21.556 -47.846 -18.244 1.00 78.39  ? 82  LEU   A CB  1 
ATOM   445  C  CG  . LEU   A 1 62  ? -22.606 -48.106 -19.326 1.00 83.09  ? 82  LEU   A CG  1 
ATOM   446  C  CD1 . LEU   A 1 62  ? -22.198 -49.288 -20.193 1.00 83.25  ? 82  LEU   A CD1 1 
ATOM   447  C  CD2 . LEU   A 1 62  ? -23.984 -48.320 -18.719 1.00 91.35  ? 82  LEU   A CD2 1 
ATOM   448  N  N   . ALA   A 1 63  ? -20.556 -45.266 -20.376 1.00 74.73  ? 83  ALA   A N   1 
ATOM   449  C  CA  . ALA   A 1 63  ? -20.959 -43.975 -20.913 1.00 73.87  ? 83  ALA   A CA  1 
ATOM   450  C  C   . ALA   A 1 63  ? -22.306 -44.101 -21.612 1.00 79.52  ? 83  ALA   A C   1 
ATOM   451  O  O   . ALA   A 1 63  ? -22.499 -44.994 -22.443 1.00 80.45  ? 83  ALA   A O   1 
ATOM   452  C  CB  . ALA   A 1 63  ? -19.907 -43.446 -21.885 1.00 71.95  ? 83  ALA   A CB  1 
ATOM   453  N  N   . ILE   A 1 64  ? -23.231 -43.206 -21.276 1.00 79.80  ? 84  ILE   A N   1 
ATOM   454  C  CA  . ILE   A 1 64  ? -24.562 -43.189 -21.869 1.00 82.59  ? 84  ILE   A CA  1 
ATOM   455  C  C   . ILE   A 1 64  ? -24.820 -41.808 -22.455 1.00 84.61  ? 84  ILE   A C   1 
ATOM   456  O  O   . ILE   A 1 64  ? -24.427 -40.790 -21.874 1.00 82.20  ? 84  ILE   A O   1 
ATOM   457  C  CB  . ILE   A 1 64  ? -25.655 -43.563 -20.845 1.00 80.76  ? 84  ILE   A CB  1 
ATOM   458  C  CG1 . ILE   A 1 64  ? -25.652 -42.588 -19.666 1.00 79.98  ? 84  ILE   A CG1 1 
ATOM   459  C  CG2 . ILE   A 1 64  ? -25.457 -44.986 -20.350 1.00 83.69  ? 84  ILE   A CG2 1 
ATOM   460  C  CD1 . ILE   A 1 64  ? -26.825 -42.764 -18.731 1.00 85.30  ? 84  ILE   A CD1 1 
ATOM   461  N  N   . THR   A 1 65  ? -25.468 -41.777 -23.621 1.00 85.22  ? 85  THR   A N   1 
ATOM   462  C  CA  . THR   A 1 65  ? -25.840 -40.528 -24.267 1.00 85.62  ? 85  THR   A CA  1 
ATOM   463  C  C   . THR   A 1 65  ? -27.318 -40.460 -24.627 1.00 88.41  ? 85  THR   A C   1 
ATOM   464  O  O   . THR   A 1 65  ? -27.744 -39.470 -25.232 1.00 91.58  ? 85  THR   A O   1 
ATOM   465  C  CB  . THR   A 1 65  ? -25.005 -40.300 -25.538 1.00 83.64  ? 85  THR   A CB  1 
ATOM   466  O  OG1 . THR   A 1 65  ? -25.321 -41.305 -26.508 1.00 86.87  ? 85  THR   A OG1 1 
ATOM   467  C  CG2 . THR   A 1 65  ? -23.515 -40.352 -25.226 1.00 84.79  ? 85  THR   A CG2 1 
ATOM   468  N  N   . ASP   A 1 66  ? -28.105 -41.473 -24.279 1.00 84.44  ? 86  ASP   A N   1 
ATOM   469  C  CA  . ASP   A 1 66  ? -29.530 -41.468 -24.593 1.00 93.72  ? 86  ASP   A CA  1 
ATOM   470  C  C   . ASP   A 1 66  ? -30.285 -40.645 -23.554 1.00 94.88  ? 86  ASP   A C   1 
ATOM   471  O  O   . ASP   A 1 66  ? -30.090 -40.850 -22.352 1.00 93.17  ? 86  ASP   A O   1 
ATOM   472  C  CB  . ASP   A 1 66  ? -30.071 -42.896 -24.639 1.00 97.73  ? 86  ASP   A CB  1 
ATOM   473  C  CG  . ASP   A 1 66  ? -31.505 -42.965 -25.134 1.00 101.08 ? 86  ASP   A CG  1 
ATOM   474  O  OD1 . ASP   A 1 66  ? -32.415 -42.507 -24.411 1.00 104.10 ? 86  ASP   A OD1 1 
ATOM   475  O  OD2 . ASP   A 1 66  ? -31.720 -43.471 -26.255 1.00 103.93 ? 86  ASP   A OD2 1 
ATOM   476  N  N   . PRO   A 1 67  ? -31.153 -39.720 -23.975 1.00 97.61  ? 87  PRO   A N   1 
ATOM   477  C  CA  . PRO   A 1 67  ? -31.788 -38.822 -22.994 1.00 97.56  ? 87  PRO   A CA  1 
ATOM   478  C  C   . PRO   A 1 67  ? -32.687 -39.539 -22.002 1.00 96.98  ? 87  PRO   A C   1 
ATOM   479  O  O   . PRO   A 1 67  ? -32.652 -39.220 -20.807 1.00 94.01  ? 87  PRO   A O   1 
ATOM   480  C  CB  . PRO   A 1 67  ? -32.580 -37.844 -23.876 1.00 96.95  ? 87  PRO   A CB  1 
ATOM   481  C  CG  . PRO   A 1 67  ? -31.962 -37.956 -25.239 1.00 93.34  ? 87  PRO   A CG  1 
ATOM   482  C  CD  . PRO   A 1 67  ? -31.516 -39.377 -25.359 1.00 97.07  ? 87  PRO   A CD  1 
ATOM   483  N  N   . ASP   A 1 68  ? -33.502 -40.493 -22.461 1.00 102.06 ? 88  ASP   A N   1 
ATOM   484  C  CA  . ASP   A 1 68  ? -34.376 -41.219 -21.543 1.00 100.07 ? 88  ASP   A CA  1 
ATOM   485  C  C   . ASP   A 1 68  ? -33.568 -42.012 -20.524 1.00 98.68  ? 88  ASP   A C   1 
ATOM   486  O  O   . ASP   A 1 68  ? -33.920 -42.056 -19.339 1.00 97.32  ? 88  ASP   A O   1 
ATOM   487  C  CB  . ASP   A 1 68  ? -35.312 -42.144 -22.321 1.00 108.47 ? 88  ASP   A CB  1 
ATOM   488  C  CG  . ASP   A 1 68  ? -36.364 -41.386 -23.105 1.00 108.51 ? 88  ASP   A CG  1 
ATOM   489  O  OD1 . ASP   A 1 68  ? -36.297 -40.140 -23.145 1.00 112.81 ? 88  ASP   A OD1 1 
ATOM   490  O  OD2 . ASP   A 1 68  ? -37.263 -42.038 -23.678 1.00 113.54 ? 88  ASP   A OD2 1 
ATOM   491  N  N   . MET   A 1 69  ? -32.481 -42.648 -20.966 1.00 102.84 ? 89  MET   A N   1 
ATOM   492  C  CA  . MET   A 1 69  ? -31.632 -43.391 -20.041 1.00 102.13 ? 89  MET   A CA  1 
ATOM   493  C  C   . MET   A 1 69  ? -30.925 -42.451 -19.073 1.00 97.23  ? 89  MET   A C   1 
ATOM   494  O  O   . MET   A 1 69  ? -30.793 -42.760 -17.883 1.00 97.11  ? 89  MET   A O   1 
ATOM   495  C  CB  . MET   A 1 69  ? -30.620 -44.228 -20.822 1.00 102.03 ? 89  MET   A CB  1 
ATOM   496  C  CG  . MET   A 1 69  ? -30.037 -45.398 -20.050 1.00 105.14 ? 89  MET   A CG  1 
ATOM   497  S  SD  . MET   A 1 69  ? -28.917 -46.368 -21.076 1.00 107.00 ? 89  MET   A SD  1 
ATOM   498  C  CE  . MET   A 1 69  ? -29.924 -46.593 -22.541 1.00 108.53 ? 89  MET   A CE  1 
ATOM   499  N  N   . ILE   A 1 70  ? -30.466 -41.298 -19.567 1.00 96.02  ? 90  ILE   A N   1 
ATOM   500  C  CA  . ILE   A 1 70  ? -29.848 -40.301 -18.696 1.00 93.90  ? 90  ILE   A CA  1 
ATOM   501  C  C   . ILE   A 1 70  ? -30.851 -39.807 -17.660 1.00 94.31  ? 90  ILE   A C   1 
ATOM   502  O  O   . ILE   A 1 70  ? -30.518 -39.641 -16.480 1.00 89.30  ? 90  ILE   A O   1 
ATOM   503  C  CB  . ILE   A 1 70  ? -29.277 -39.142 -19.534 1.00 90.62  ? 90  ILE   A CB  1 
ATOM   504  C  CG1 . ILE   A 1 70  ? -28.045 -39.603 -20.316 1.00 88.54  ? 90  ILE   A CG1 1 
ATOM   505  C  CG2 . ILE   A 1 70  ? -28.940 -37.946 -18.652 1.00 90.72  ? 90  ILE   A CG2 1 
ATOM   506  C  CD1 . ILE   A 1 70  ? -27.552 -38.591 -21.330 1.00 89.02  ? 90  ILE   A CD1 1 
ATOM   507  N  N   . LYS   A 1 71  ? -32.096 -39.574 -18.083 1.00 89.35  ? 91  LYS   A N   1 
ATOM   508  C  CA  . LYS   A 1 71  ? -33.129 -39.142 -17.146 1.00 93.57  ? 91  LYS   A CA  1 
ATOM   509  C  C   . LYS   A 1 71  ? -33.386 -40.202 -16.083 1.00 94.20  ? 91  LYS   A C   1 
ATOM   510  O  O   . LYS   A 1 71  ? -33.616 -39.876 -14.912 1.00 92.92  ? 91  LYS   A O   1 
ATOM   511  C  CB  . LYS   A 1 71  ? -34.418 -38.817 -17.900 1.00 92.47  ? 91  LYS   A CB  1 
ATOM   512  C  CG  . LYS   A 1 71  ? -35.576 -38.424 -16.999 1.00 97.50  ? 91  LYS   A CG  1 
ATOM   513  C  CD  . LYS   A 1 71  ? -36.878 -38.349 -17.775 1.00 99.24  ? 91  LYS   A CD  1 
ATOM   514  C  CE  . LYS   A 1 71  ? -37.251 -39.707 -18.343 1.00 102.28 ? 91  LYS   A CE  1 
ATOM   515  N  NZ  . LYS   A 1 71  ? -38.558 -39.671 -19.052 1.00 110.58 ? 91  LYS   A NZ  1 
ATOM   516  N  N   . THR   A 1 72  ? -33.353 -41.478 -16.472 1.00 95.43  ? 92  THR   A N   1 
ATOM   517  C  CA  . THR   A 1 72  ? -33.539 -42.553 -15.504 1.00 97.59  ? 92  THR   A CA  1 
ATOM   518  C  C   . THR   A 1 72  ? -32.423 -42.560 -14.466 1.00 94.76  ? 92  THR   A C   1 
ATOM   519  O  O   . THR   A 1 72  ? -32.675 -42.763 -13.272 1.00 93.35  ? 92  THR   A O   1 
ATOM   520  C  CB  . THR   A 1 72  ? -33.614 -43.899 -16.227 1.00 100.87 ? 92  THR   A CB  1 
ATOM   521  O  OG1 . THR   A 1 72  ? -34.820 -43.965 -16.998 1.00 103.21 ? 92  THR   A OG1 1 
ATOM   522  C  CG2 . THR   A 1 72  ? -33.593 -45.046 -15.232 1.00 104.22 ? 92  THR   A CG2 1 
ATOM   523  N  N   . VAL   A 1 73  ? -31.185 -42.322 -14.900 1.00 91.27  ? 93  VAL   A N   1 
ATOM   524  C  CA  . VAL   A 1 73  ? -30.054 -42.351 -13.977 1.00 92.35  ? 93  VAL   A CA  1 
ATOM   525  C  C   . VAL   A 1 73  ? -30.103 -41.154 -13.032 1.00 91.66  ? 93  VAL   A C   1 
ATOM   526  O  O   . VAL   A 1 73  ? -30.038 -41.306 -11.807 1.00 90.57  ? 93  VAL   A O   1 
ATOM   527  C  CB  . VAL   A 1 73  ? -28.729 -42.399 -14.759 1.00 92.13  ? 93  VAL   A CB  1 
ATOM   528  C  CG1 . VAL   A 1 73  ? -27.545 -42.307 -13.807 1.00 87.23  ? 93  VAL   A CG1 1 
ATOM   529  C  CG2 . VAL   A 1 73  ? -28.648 -43.673 -15.591 1.00 88.56  ? 93  VAL   A CG2 1 
ATOM   530  N  N   . LEU   A 1 74  ? -30.224 -39.947 -13.586 1.00 91.36  ? 94  LEU   A N   1 
ATOM   531  C  CA  . LEU   A 1 74  ? -30.125 -38.739 -12.776 1.00 87.01  ? 94  LEU   A CA  1 
ATOM   532  C  C   . LEU   A 1 74  ? -31.382 -38.473 -11.957 1.00 87.51  ? 94  LEU   A C   1 
ATOM   533  O  O   . LEU   A 1 74  ? -31.297 -37.847 -10.895 1.00 85.07  ? 94  LEU   A O   1 
ATOM   534  C  CB  . LEU   A 1 74  ? -29.828 -37.526 -13.661 1.00 89.24  ? 94  LEU   A CB  1 
ATOM   535  C  CG  . LEU   A 1 74  ? -28.384 -37.265 -14.098 1.00 85.09  ? 94  LEU   A CG  1 
ATOM   536  C  CD1 . LEU   A 1 74  ? -27.904 -38.306 -15.094 1.00 85.11  ? 94  LEU   A CD1 1 
ATOM   537  C  CD2 . LEU   A 1 74  ? -28.244 -35.863 -14.680 1.00 84.09  ? 94  LEU   A CD2 1 
ATOM   538  N  N   . VAL   A 1 75  ? -32.545 -38.939 -12.411 1.00 88.76  ? 95  VAL   A N   1 
ATOM   539  C  CA  . VAL   A 1 75  ? -33.804 -38.549 -11.783 1.00 92.00  ? 95  VAL   A CA  1 
ATOM   540  C  C   . VAL   A 1 75  ? -34.584 -39.764 -11.298 1.00 94.21  ? 95  VAL   A C   1 
ATOM   541  O  O   . VAL   A 1 75  ? -34.863 -39.894 -10.101 1.00 92.67  ? 95  VAL   A O   1 
ATOM   542  C  CB  . VAL   A 1 75  ? -34.664 -37.709 -12.746 1.00 89.81  ? 95  VAL   A CB  1 
ATOM   543  C  CG1 . VAL   A 1 75  ? -35.983 -37.330 -12.088 1.00 85.34  ? 95  VAL   A CG1 1 
ATOM   544  C  CG2 . VAL   A 1 75  ? -33.905 -36.466 -13.192 1.00 89.59  ? 95  VAL   A CG2 1 
ATOM   545  N  N   . LYS   A 1 76  ? -34.953 -40.656 -12.223 1.00 94.77  ? 96  LYS   A N   1 
ATOM   546  C  CA  . LYS   A 1 76  ? -35.904 -41.717 -11.896 1.00 100.14 ? 96  LYS   A CA  1 
ATOM   547  C  C   . LYS   A 1 76  ? -35.352 -42.677 -10.848 1.00 100.59 ? 96  LYS   A C   1 
ATOM   548  O  O   . LYS   A 1 76  ? -36.072 -43.080 -9.927  1.00 94.88  ? 96  LYS   A O   1 
ATOM   549  C  CB  . LYS   A 1 76  ? -36.301 -42.479 -13.162 1.00 101.74 ? 96  LYS   A CB  1 
ATOM   550  C  CG  . LYS   A 1 76  ? -37.398 -41.808 -13.973 1.00 107.52 ? 96  LYS   A CG  1 
ATOM   551  C  CD  . LYS   A 1 76  ? -37.685 -42.573 -15.256 1.00 107.66 ? 96  LYS   A CD  1 
ATOM   552  C  CE  . LYS   A 1 76  ? -38.871 -41.978 -15.998 1.00 114.32 ? 96  LYS   A CE  1 
ATOM   553  N  NZ  . LYS   A 1 76  ? -39.061 -42.603 -17.336 1.00 119.21 ? 96  LYS   A NZ  1 
ATOM   554  N  N   . GLU   A 1 77  ? -34.083 -43.057 -10.968 1.00 98.83  ? 97  GLU   A N   1 
ATOM   555  C  CA  . GLU   A 1 77  ? -33.476 -44.048 -10.086 1.00 101.35 ? 97  GLU   A CA  1 
ATOM   556  C  C   . GLU   A 1 77  ? -32.324 -43.450 -9.284  1.00 99.61  ? 97  GLU   A C   1 
ATOM   557  O  O   . GLU   A 1 77  ? -31.292 -44.089 -9.072  1.00 106.64 ? 97  GLU   A O   1 
ATOM   558  C  CB  . GLU   A 1 77  ? -33.002 -45.262 -10.883 1.00 105.90 ? 97  GLU   A CB  1 
ATOM   559  C  CG  . GLU   A 1 77  ? -34.084 -45.909 -11.737 1.00 106.56 ? 97  GLU   A CG  1 
ATOM   560  C  CD  . GLU   A 1 77  ? -35.205 -46.511 -10.912 1.00 112.22 ? 97  GLU   A CD  1 
ATOM   561  O  OE1 . GLU   A 1 77  ? -34.943 -46.936 -9.767  1.00 120.57 ? 97  GLU   A OE1 1 
ATOM   562  O  OE2 . GLU   A 1 77  ? -36.351 -46.558 -11.409 1.00 112.22 ? 97  GLU   A OE2 1 
ATOM   563  N  N   . CYS   A 1 78  ? -32.495 -42.213 -8.813  1.00 98.65  ? 98  CYS   A N   1 
ATOM   564  C  CA  . CYS   A 1 78  ? -31.440 -41.556 -8.047  1.00 101.33 ? 98  CYS   A CA  1 
ATOM   565  C  C   . CYS   A 1 78  ? -31.361 -42.097 -6.624  1.00 102.42 ? 98  CYS   A C   1 
ATOM   566  O  O   . CYS   A 1 78  ? -30.296 -42.540 -6.180  1.00 95.59  ? 98  CYS   A O   1 
ATOM   567  C  CB  . CYS   A 1 78  ? -31.663 -40.043 -8.027  1.00 101.71 ? 98  CYS   A CB  1 
ATOM   568  S  SG  . CYS   A 1 78  ? -30.502 -39.144 -6.970  1.00 81.35  ? 98  CYS   A SG  1 
ATOM   569  N  N   . TYR   A 1 79  ? -32.479 -42.067 -5.895  1.00 108.10 ? 99  TYR   A N   1 
ATOM   570  C  CA  . TYR   A 1 79  ? -32.455 -42.450 -4.486  1.00 109.11 ? 99  TYR   A CA  1 
ATOM   571  C  C   . TYR   A 1 79  ? -32.152 -43.933 -4.307  1.00 108.61 ? 99  TYR   A C   1 
ATOM   572  O  O   . TYR   A 1 79  ? -31.435 -44.317 -3.376  1.00 106.19 ? 99  TYR   A O   1 
ATOM   573  C  CB  . TYR   A 1 79  ? -33.787 -42.101 -3.822  1.00 109.93 ? 99  TYR   A CB  1 
ATOM   574  C  CG  . TYR   A 1 79  ? -33.994 -40.622 -3.587  1.00 116.75 ? 99  TYR   A CG  1 
ATOM   575  C  CD1 . TYR   A 1 79  ? -32.913 -39.767 -3.423  1.00 113.81 ? 99  TYR   A CD1 1 
ATOM   576  C  CD2 . TYR   A 1 79  ? -35.272 -40.081 -3.526  1.00 119.03 ? 99  TYR   A CD2 1 
ATOM   577  C  CE1 . TYR   A 1 79  ? -33.098 -38.414 -3.205  1.00 117.45 ? 99  TYR   A CE1 1 
ATOM   578  C  CE2 . TYR   A 1 79  ? -35.468 -38.729 -3.308  1.00 116.53 ? 99  TYR   A CE2 1 
ATOM   579  C  CZ  . TYR   A 1 79  ? -34.377 -37.900 -3.149  1.00 118.61 ? 99  TYR   A CZ  1 
ATOM   580  O  OH  . TYR   A 1 79  ? -34.562 -36.554 -2.932  1.00 124.12 ? 99  TYR   A OH  1 
ATOM   581  N  N   . SER   A 1 80  ? -32.683 -44.779 -5.186  1.00 103.22 ? 100 SER   A N   1 
ATOM   582  C  CA  . SER   A 1 80  ? -32.582 -46.220 -4.996  1.00 106.91 ? 100 SER   A CA  1 
ATOM   583  C  C   . SER   A 1 80  ? -31.303 -46.817 -5.564  1.00 102.82 ? 100 SER   A C   1 
ATOM   584  O  O   . SER   A 1 80  ? -30.821 -47.830 -5.044  1.00 103.75 ? 100 SER   A O   1 
ATOM   585  C  CB  . SER   A 1 80  ? -33.790 -46.921 -5.627  1.00 108.01 ? 100 SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 80  ? -33.860 -46.661 -7.017  1.00 114.90 ? 100 SER   A OG  1 
ATOM   587  N  N   . VAL   A 1 81  ? -30.738 -46.226 -6.615  1.00 102.08 ? 101 VAL   A N   1 
ATOM   588  C  CA  . VAL   A 1 81  ? -29.604 -46.841 -7.297  1.00 99.70  ? 101 VAL   A CA  1 
ATOM   589  C  C   . VAL   A 1 81  ? -28.446 -45.861 -7.430  1.00 94.72  ? 101 VAL   A C   1 
ATOM   590  O  O   . VAL   A 1 81  ? -27.360 -46.090 -6.886  1.00 93.86  ? 101 VAL   A O   1 
ATOM   591  C  CB  . VAL   A 1 81  ? -30.021 -47.378 -8.678  1.00 100.12 ? 101 VAL   A CB  1 
ATOM   592  C  CG1 . VAL   A 1 81  ? -28.817 -47.958 -9.403  1.00 96.03  ? 101 VAL   A CG1 1 
ATOM   593  C  CG2 . VAL   A 1 81  ? -31.115 -48.421 -8.529  1.00 102.64 ? 101 VAL   A CG2 1 
ATOM   594  N  N   . PHE   A 1 82  ? -28.663 -44.771 -8.156  1.00 93.89  ? 102 PHE   A N   1 
ATOM   595  C  CA  . PHE   A 1 82  ? -27.583 -43.848 -8.509  1.00 91.92  ? 102 PHE   A CA  1 
ATOM   596  C  C   . PHE   A 1 82  ? -27.546 -42.662 -7.547  1.00 94.04  ? 102 PHE   A C   1 
ATOM   597  O  O   . PHE   A 1 82  ? -27.719 -41.504 -7.925  1.00 91.33  ? 102 PHE   A O   1 
ATOM   598  C  CB  . PHE   A 1 82  ? -27.743 -43.390 -9.955  1.00 95.50  ? 102 PHE   A CB  1 
ATOM   599  C  CG  . PHE   A 1 82  ? -27.968 -44.515 -10.925 1.00 90.24  ? 102 PHE   A CG  1 
ATOM   600  C  CD1 . PHE   A 1 82  ? -26.912 -45.302 -11.353 1.00 89.43  ? 102 PHE   A CD1 1 
ATOM   601  C  CD2 . PHE   A 1 82  ? -29.237 -44.784 -11.410 1.00 92.60  ? 102 PHE   A CD2 1 
ATOM   602  C  CE1 . PHE   A 1 82  ? -27.118 -46.339 -12.246 1.00 89.41  ? 102 PHE   A CE1 1 
ATOM   603  C  CE2 . PHE   A 1 82  ? -29.450 -45.819 -12.304 1.00 96.21  ? 102 PHE   A CE2 1 
ATOM   604  C  CZ  . PHE   A 1 82  ? -28.388 -46.597 -12.722 1.00 94.32  ? 102 PHE   A CZ  1 
ATOM   605  N  N   . THR   A 1 83  ? -27.299 -42.974 -6.274  1.00 89.63  ? 103 THR   A N   1 
ATOM   606  C  CA  . THR   A 1 83  ? -27.305 -41.955 -5.234  1.00 93.68  ? 103 THR   A CA  1 
ATOM   607  C  C   . THR   A 1 83  ? -25.971 -41.235 -5.103  1.00 88.56  ? 103 THR   A C   1 
ATOM   608  O  O   . THR   A 1 83  ? -25.937 -40.105 -4.607  1.00 80.22  ? 103 THR   A O   1 
ATOM   609  C  CB  . THR   A 1 83  ? -27.679 -42.583 -3.888  1.00 88.68  ? 103 THR   A CB  1 
ATOM   610  O  OG1 . THR   A 1 83  ? -28.780 -43.481 -4.070  1.00 97.08  ? 103 THR   A OG1 1 
ATOM   611  C  CG2 . THR   A 1 83  ? -28.078 -41.512 -2.881  1.00 96.56  ? 103 THR   A CG2 1 
ATOM   612  N  N   . ASN   A 1 84  ? -24.877 -41.849 -5.544  1.00 84.05  ? 104 ASN   A N   1 
ATOM   613  C  CA  . ASN   A 1 84  ? -23.548 -41.340 -5.254  1.00 81.78  ? 104 ASN   A CA  1 
ATOM   614  C  C   . ASN   A 1 84  ? -22.720 -41.232 -6.526  1.00 76.80  ? 104 ASN   A C   1 
ATOM   615  O  O   . ASN   A 1 84  ? -22.976 -41.909 -7.526  1.00 76.22  ? 104 ASN   A O   1 
ATOM   616  C  CB  . ASN   A 1 84  ? -22.830 -42.234 -4.237  1.00 81.56  ? 104 ASN   A CB  1 
ATOM   617  C  CG  . ASN   A 1 84  ? -23.617 -42.396 -2.954  1.00 90.06  ? 104 ASN   A CG  1 
ATOM   618  O  OD1 . ASN   A 1 84  ? -24.189 -41.435 -2.441  1.00 92.28  ? 104 ASN   A OD1 1 
ATOM   619  N  ND2 . ASN   A 1 84  ? -23.666 -43.618 -2.438  1.00 92.60  ? 104 ASN   A ND2 1 
ATOM   620  N  N   . ARG   A 1 85  ? -21.718 -40.363 -6.465  1.00 80.02  ? 105 ARG   A N   1 
ATOM   621  C  CA  . ARG   A 1 85  ? -20.733 -40.190 -7.515  1.00 81.95  ? 105 ARG   A CA  1 
ATOM   622  C  C   . ARG   A 1 85  ? -19.487 -41.008 -7.173  1.00 77.03  ? 105 ARG   A C   1 
ATOM   623  O  O   . ARG   A 1 85  ? -19.460 -41.762 -6.195  1.00 80.85  ? 105 ARG   A O   1 
ATOM   624  C  CB  . ARG   A 1 85  ? -20.411 -38.703 -7.688  1.00 73.79  ? 105 ARG   A CB  1 
ATOM   625  C  CG  . ARG   A 1 85  ? -21.623 -37.813 -7.897  1.00 74.92  ? 105 ARG   A CG  1 
ATOM   626  C  CD  . ARG   A 1 85  ? -21.196 -36.384 -8.226  1.00 75.17  ? 105 ARG   A CD  1 
ATOM   627  N  NE  . ARG   A 1 85  ? -22.330 -35.474 -8.339  1.00 73.10  ? 105 ARG   A NE  1 
ATOM   628  C  CZ  . ARG   A 1 85  ? -22.752 -34.681 -7.363  1.00 77.70  ? 105 ARG   A CZ  1 
ATOM   629  N  NH1 . ARG   A 1 85  ? -22.146 -34.649 -6.188  1.00 77.47  ? 105 ARG   A NH1 1 
ATOM   630  N  NH2 . ARG   A 1 85  ? -23.811 -33.903 -7.571  1.00 77.22  ? 105 ARG   A NH2 1 
ATOM   631  N  N   . ARG   A 1 86  ? -18.443 -40.859 -7.980  1.00 73.14  ? 106 ARG   A N   1 
ATOM   632  C  CA  . ARG   A 1 86  ? -17.201 -41.581 -7.738  1.00 78.81  ? 106 ARG   A CA  1 
ATOM   633  C  C   . ARG   A 1 86  ? -16.619 -41.169 -6.387  1.00 82.29  ? 106 ARG   A C   1 
ATOM   634  O  O   . ARG   A 1 86  ? -16.503 -39.967 -6.110  1.00 86.58  ? 106 ARG   A O   1 
ATOM   635  C  CB  . ARG   A 1 86  ? -16.198 -41.300 -8.855  1.00 80.38  ? 106 ARG   A CB  1 
ATOM   636  C  CG  . ARG   A 1 86  ? -15.445 -42.522 -9.363  1.00 74.40  ? 106 ARG   A CG  1 
ATOM   637  C  CD  . ARG   A 1 86  ? -14.375 -42.126 -10.375 1.00 74.62  ? 106 ARG   A CD  1 
ATOM   638  N  NE  . ARG   A 1 86  ? -14.899 -41.962 -11.726 1.00 76.30  ? 106 ARG   A NE  1 
ATOM   639  C  CZ  . ARG   A 1 86  ? -14.448 -42.619 -12.787 1.00 75.32  ? 106 ARG   A CZ  1 
ATOM   640  N  NH1 . ARG   A 1 86  ? -13.444 -43.476 -12.693 1.00 73.44  ? 106 ARG   A NH1 1 
ATOM   641  N  NH2 . ARG   A 1 86  ? -15.009 -42.401 -13.973 1.00 77.90  ? 106 ARG   A NH2 1 
ATOM   642  N  N   . PRO   A 1 87  ? -16.254 -42.119 -5.525  1.00 82.72  ? 107 PRO   A N   1 
ATOM   643  C  CA  . PRO   A 1 87  ? -15.740 -41.761 -4.192  1.00 88.57  ? 107 PRO   A CA  1 
ATOM   644  C  C   . PRO   A 1 87  ? -14.391 -41.063 -4.287  1.00 92.08  ? 107 PRO   A C   1 
ATOM   645  O  O   . PRO   A 1 87  ? -13.400 -41.650 -4.729  1.00 91.95  ? 107 PRO   A O   1 
ATOM   646  C  CB  . PRO   A 1 87  ? -15.631 -43.115 -3.479  1.00 89.33  ? 107 PRO   A CB  1 
ATOM   647  C  CG  . PRO   A 1 87  ? -15.501 -44.114 -4.578  1.00 86.47  ? 107 PRO   A CG  1 
ATOM   648  C  CD  . PRO   A 1 87  ? -16.314 -43.576 -5.725  1.00 84.34  ? 107 PRO   A CD  1 
ATOM   649  N  N   . PHE   A 1 88  ? -14.355 -39.806 -3.855  1.00 97.37  ? 108 PHE   A N   1 
ATOM   650  C  CA  . PHE   A 1 88  ? -13.137 -39.012 -3.874  1.00 98.37  ? 108 PHE   A CA  1 
ATOM   651  C  C   . PHE   A 1 88  ? -12.391 -39.144 -2.552  1.00 103.79 ? 108 PHE   A C   1 
ATOM   652  O  O   . PHE   A 1 88  ? -12.994 -39.270 -1.483  1.00 102.78 ? 108 PHE   A O   1 
ATOM   653  C  CB  . PHE   A 1 88  ? -13.456 -37.540 -4.151  1.00 98.95  ? 108 PHE   A CB  1 
ATOM   654  C  CG  . PHE   A 1 88  ? -12.244 -36.652 -4.196  1.00 105.85 ? 108 PHE   A CG  1 
ATOM   655  C  CD1 . PHE   A 1 88  ? -11.490 -36.543 -5.354  1.00 109.03 ? 108 PHE   A CD1 1 
ATOM   656  C  CD2 . PHE   A 1 88  ? -11.862 -35.920 -3.083  1.00 106.36 ? 108 PHE   A CD2 1 
ATOM   657  C  CE1 . PHE   A 1 88  ? -10.375 -35.726 -5.398  1.00 110.30 ? 108 PHE   A CE1 1 
ATOM   658  C  CE2 . PHE   A 1 88  ? -10.748 -35.102 -3.121  1.00 104.26 ? 108 PHE   A CE2 1 
ATOM   659  C  CZ  . PHE   A 1 88  ? -10.004 -35.005 -4.280  1.00 109.44 ? 108 PHE   A CZ  1 
ATOM   660  N  N   . GLY   A 1 89  ? -11.063 -39.112 -2.639  1.00 120.96 ? 109 GLY   A N   1 
ATOM   661  C  CA  . GLY   A 1 89  ? -10.216 -39.214 -1.476  1.00 126.28 ? 109 GLY   A CA  1 
ATOM   662  C  C   . GLY   A 1 89  ? -8.747  -39.192 -1.842  1.00 126.36 ? 109 GLY   A C   1 
ATOM   663  O  O   . GLY   A 1 89  ? -8.377  -39.206 -3.020  1.00 129.99 ? 109 GLY   A O   1 
ATOM   664  N  N   . PRO   A 1 90  ? -7.870  -39.151 -0.830  1.00 119.07 ? 110 PRO   A N   1 
ATOM   665  C  CA  . PRO   A 1 90  ? -8.153  -39.094 0.612   1.00 123.96 ? 110 PRO   A CA  1 
ATOM   666  C  C   . PRO   A 1 90  ? -8.533  -37.688 1.060   1.00 125.49 ? 110 PRO   A C   1 
ATOM   667  O  O   . PRO   A 1 90  ? -8.030  -36.707 0.519   1.00 124.03 ? 110 PRO   A O   1 
ATOM   668  C  CB  . PRO   A 1 90  ? -6.832  -39.554 1.231   1.00 125.86 ? 110 PRO   A CB  1 
ATOM   669  C  CG  . PRO   A 1 90  ? -5.802  -39.036 0.270   1.00 123.82 ? 110 PRO   A CG  1 
ATOM   670  C  CD  . PRO   A 1 90  ? -6.421  -39.209 -1.094  1.00 117.14 ? 110 PRO   A CD  1 
ATOM   671  N  N   . VAL   A 1 91  ? -9.413  -37.552 2.050   1.00 132.11 ? 111 VAL   A N   1 
ATOM   672  C  CA  . VAL   A 1 91  ? -9.910  -36.241 2.449   1.00 135.64 ? 111 VAL   A CA  1 
ATOM   673  C  C   . VAL   A 1 91  ? -9.845  -36.079 3.962   1.00 136.12 ? 111 VAL   A C   1 
ATOM   674  O  O   . VAL   A 1 91  ? -9.513  -35.003 4.467   1.00 138.45 ? 111 VAL   A O   1 
ATOM   675  C  CB  . VAL   A 1 91  ? -11.345 -36.019 1.939   1.00 132.79 ? 111 VAL   A CB  1 
ATOM   676  C  CG1 . VAL   A 1 91  ? -11.336 -35.674 0.461   1.00 131.70 ? 111 VAL   A CG1 1 
ATOM   677  C  CG2 . VAL   A 1 91  ? -12.191 -37.255 2.191   1.00 130.40 ? 111 VAL   A CG2 1 
ATOM   678  N  N   . GLY   A 1 92  ? -10.161 -37.134 4.695   1.00 128.27 ? 112 GLY   A N   1 
ATOM   679  C  CA  . GLY   A 1 92  ? -10.231 -37.050 6.143   1.00 129.69 ? 112 GLY   A CA  1 
ATOM   680  C  C   . GLY   A 1 92  ? -11.595 -36.567 6.581   1.00 126.09 ? 112 GLY   A C   1 
ATOM   681  O  O   . GLY   A 1 92  ? -12.606 -37.173 6.239   1.00 123.29 ? 112 GLY   A O   1 
ATOM   682  N  N   . PHE   A 1 93  ? -11.620 -35.465 7.341   1.00 124.20 ? 113 PHE   A N   1 
ATOM   683  C  CA  . PHE   A 1 93  ? -12.888 -34.900 7.792   1.00 121.97 ? 113 PHE   A CA  1 
ATOM   684  C  C   . PHE   A 1 93  ? -13.716 -34.363 6.632   1.00 117.78 ? 113 PHE   A C   1 
ATOM   685  O  O   . PHE   A 1 93  ? -14.941 -34.272 6.747   1.00 112.23 ? 113 PHE   A O   1 
ATOM   686  C  CB  . PHE   A 1 93  ? -12.637 -33.789 8.822   1.00 125.25 ? 113 PHE   A CB  1 
ATOM   687  C  CG  . PHE   A 1 93  ? -12.298 -32.462 8.209   1.00 126.04 ? 113 PHE   A CG  1 
ATOM   688  C  CD1 . PHE   A 1 93  ? -11.013 -32.192 7.776   1.00 128.18 ? 113 PHE   A CD1 1 
ATOM   689  C  CD2 . PHE   A 1 93  ? -13.269 -31.485 8.060   1.00 126.18 ? 113 PHE   A CD2 1 
ATOM   690  C  CE1 . PHE   A 1 93  ? -10.700 -30.976 7.203   1.00 130.12 ? 113 PHE   A CE1 1 
ATOM   691  C  CE2 . PHE   A 1 93  ? -12.966 -30.268 7.487   1.00 126.52 ? 113 PHE   A CE2 1 
ATOM   692  C  CZ  . PHE   A 1 93  ? -11.679 -30.011 7.058   1.00 128.87 ? 113 PHE   A CZ  1 
ATOM   693  N  N   . MET   A 1 94  ? -13.076 -34.016 5.515   1.00 117.37 ? 114 MET   A N   1 
ATOM   694  C  CA  . MET   A 1 94  ? -13.810 -33.546 4.349   1.00 114.88 ? 114 MET   A CA  1 
ATOM   695  C  C   . MET   A 1 94  ? -14.712 -34.610 3.740   1.00 110.20 ? 114 MET   A C   1 
ATOM   696  O  O   . MET   A 1 94  ? -15.458 -34.296 2.807   1.00 106.27 ? 114 MET   A O   1 
ATOM   697  C  CB  . MET   A 1 94  ? -12.839 -33.011 3.294   1.00 118.49 ? 114 MET   A CB  1 
ATOM   698  C  CG  . MET   A 1 94  ? -12.294 -31.603 3.576   1.00 120.15 ? 114 MET   A CG  1 
ATOM   699  S  SD  . MET   A 1 94  ? -13.641 -30.409 3.543   1.00 116.55 ? 114 MET   A SD  1 
ATOM   700  C  CE  . MET   A 1 94  ? -14.188 -30.580 1.847   1.00 105.32 ? 114 MET   A CE  1 
ATOM   701  N  N   . LYS   A 1 95  ? -14.692 -35.840 4.253   1.00 112.92 ? 115 LYS   A N   1 
ATOM   702  C  CA  . LYS   A 1 95  ? -15.623 -36.840 3.752   1.00 108.30 ? 115 LYS   A CA  1 
ATOM   703  C  C   . LYS   A 1 95  ? -17.059 -36.470 4.068   1.00 102.26 ? 115 LYS   A C   1 
ATOM   704  O  O   . LYS   A 1 95  ? -17.976 -36.963 3.403   1.00 99.98  ? 115 LYS   A O   1 
ATOM   705  C  CB  . LYS   A 1 95  ? -15.322 -38.214 4.349   1.00 109.88 ? 115 LYS   A CB  1 
ATOM   706  C  CG  . LYS   A 1 95  ? -15.556 -38.279 5.850   1.00 111.46 ? 115 LYS   A CG  1 
ATOM   707  C  CD  . LYS   A 1 95  ? -15.029 -39.572 6.469   1.00 114.40 ? 115 LYS   A CD  1 
ATOM   708  C  CE  . LYS   A 1 95  ? -15.322 -39.619 7.970   1.00 112.78 ? 115 LYS   A CE  1 
ATOM   709  N  NZ  . LYS   A 1 95  ? -14.729 -40.824 8.617   1.00 103.86 ? 115 LYS   A NZ  1 
ATOM   710  N  N   . SER   A 1 96  ? -17.269 -35.619 5.069   1.00 103.49 ? 116 SER   A N   1 
ATOM   711  C  CA  . SER   A 1 96  ? -18.600 -35.216 5.493   1.00 104.66 ? 116 SER   A CA  1 
ATOM   712  C  C   . SER   A 1 96  ? -19.093 -33.973 4.764   1.00 100.58 ? 116 SER   A C   1 
ATOM   713  O  O   . SER   A 1 96  ? -20.138 -33.425 5.131   1.00 96.66  ? 116 SER   A O   1 
ATOM   714  C  CB  . SER   A 1 96  ? -18.626 -34.982 7.007   1.00 107.41 ? 116 SER   A CB  1 
ATOM   715  O  OG  . SER   A 1 96  ? -17.692 -33.988 7.386   1.00 111.98 ? 116 SER   A OG  1 
ATOM   716  N  N   . ALA   A 1 97  ? -18.356 -33.504 3.761   1.00 97.72  ? 117 ALA   A N   1 
ATOM   717  C  CA  . ALA   A 1 97  ? -18.841 -32.418 2.921   1.00 95.45  ? 117 ALA   A CA  1 
ATOM   718  C  C   . ALA   A 1 97  ? -19.972 -32.918 2.031   1.00 93.07  ? 117 ALA   A C   1 
ATOM   719  O  O   . ALA   A 1 97  ? -19.945 -34.054 1.548   1.00 97.10  ? 117 ALA   A O   1 
ATOM   720  C  CB  . ALA   A 1 97  ? -17.704 -31.852 2.073   1.00 92.56  ? 117 ALA   A CB  1 
ATOM   721  N  N   . ILE   A 1 98  ? -20.971 -32.058 1.810   1.00 90.21  ? 118 ILE   A N   1 
ATOM   722  C  CA  . ILE   A 1 98  ? -22.192 -32.488 1.128   1.00 90.79  ? 118 ILE   A CA  1 
ATOM   723  C  C   . ILE   A 1 98  ? -21.884 -32.974 -0.283  1.00 89.78  ? 118 ILE   A C   1 
ATOM   724  O  O   . ILE   A 1 98  ? -22.441 -33.978 -0.745  1.00 87.88  ? 118 ILE   A O   1 
ATOM   725  C  CB  . ILE   A 1 98  ? -23.236 -31.355 1.121   1.00 95.44  ? 118 ILE   A CB  1 
ATOM   726  C  CG1 . ILE   A 1 98  ? -24.463 -31.767 0.303   1.00 90.65  ? 118 ILE   A CG1 1 
ATOM   727  C  CG2 . ILE   A 1 98  ? -22.637 -30.060 0.585   1.00 87.88  ? 118 ILE   A CG2 1 
ATOM   728  C  CD1 . ILE   A 1 98  ? -25.473 -30.657 0.109   1.00 93.94  ? 118 ILE   A CD1 1 
ATOM   729  N  N   . SER   A 1 99  ? -20.987 -32.284 -0.986  1.00 86.91  ? 119 SER   A N   1 
ATOM   730  C  CA  . SER   A 1 99  ? -20.623 -32.685 -2.339  1.00 83.39  ? 119 SER   A CA  1 
ATOM   731  C  C   . SER   A 1 99  ? -19.789 -33.959 -2.375  1.00 86.29  ? 119 SER   A C   1 
ATOM   732  O  O   . SER   A 1 99  ? -19.471 -34.435 -3.470  1.00 86.55  ? 119 SER   A O   1 
ATOM   733  C  CB  . SER   A 1 99  ? -19.870 -31.547 -3.030  1.00 83.19  ? 119 SER   A CB  1 
ATOM   734  O  OG  . SER   A 1 99  ? -18.728 -31.166 -2.281  1.00 80.86  ? 119 SER   A OG  1 
ATOM   735  N  N   . ILE   A 1 100 ? -19.434 -34.516 -1.219  1.00 88.94  ? 120 ILE   A N   1 
ATOM   736  C  CA  . ILE   A 1 100 ? -18.632 -35.731 -1.160  1.00 89.67  ? 120 ILE   A CA  1 
ATOM   737  C  C   . ILE   A 1 100 ? -19.315 -36.858 -0.393  1.00 92.52  ? 120 ILE   A C   1 
ATOM   738  O  O   . ILE   A 1 100 ? -19.007 -38.035 -0.649  1.00 92.50  ? 120 ILE   A O   1 
ATOM   739  C  CB  . ILE   A 1 100 ? -17.240 -35.443 -0.554  1.00 90.13  ? 120 ILE   A CB  1 
ATOM   740  C  CG1 . ILE   A 1 100 ? -16.689 -34.111 -1.072  1.00 89.06  ? 120 ILE   A CG1 1 
ATOM   741  C  CG2 . ILE   A 1 100 ? -16.266 -36.567 -0.877  1.00 93.67  ? 120 ILE   A CG2 1 
ATOM   742  C  CD1 . ILE   A 1 100 ? -15.387 -33.686 -0.416  1.00 92.01  ? 120 ILE   A CD1 1 
ATOM   743  N  N   . ALA   A 1 101 ? -20.233 -36.558 0.526   1.00 95.88  ? 121 ALA   A N   1 
ATOM   744  C  CA  . ALA   A 1 101 ? -20.879 -37.580 1.338   1.00 94.84  ? 121 ALA   A CA  1 
ATOM   745  C  C   . ALA   A 1 101 ? -21.755 -38.488 0.474   1.00 92.25  ? 121 ALA   A C   1 
ATOM   746  O  O   . ALA   A 1 101 ? -22.025 -38.212 -0.698  1.00 88.06  ? 121 ALA   A O   1 
ATOM   747  C  CB  . ALA   A 1 101 ? -21.713 -36.936 2.444   1.00 98.18  ? 121 ALA   A CB  1 
ATOM   748  N  N   . GLU   A 1 102 ? -22.213 -39.586 1.077   1.00 94.35  ? 122 GLU   A N   1 
ATOM   749  C  CA  . GLU   A 1 102 ? -22.918 -40.628 0.347   1.00 93.47  ? 122 GLU   A CA  1 
ATOM   750  C  C   . GLU   A 1 102 ? -24.220 -41.002 1.042   1.00 96.37  ? 122 GLU   A C   1 
ATOM   751  O  O   . GLU   A 1 102 ? -24.312 -40.996 2.273   1.00 93.35  ? 122 GLU   A O   1 
ATOM   752  C  CB  . GLU   A 1 102 ? -22.049 -41.885 0.190   1.00 87.30  ? 122 GLU   A CB  1 
ATOM   753  C  CG  . GLU   A 1 102 ? -20.731 -41.650 -0.529  1.00 93.46  ? 122 GLU   A CG  1 
ATOM   754  C  CD  . GLU   A 1 102 ? -20.100 -42.941 -1.010  1.00 92.57  ? 122 GLU   A CD  1 
ATOM   755  O  OE1 . GLU   A 1 102 ? -20.672 -44.017 -0.738  1.00 95.67  ? 122 GLU   A OE1 1 
ATOM   756  O  OE2 . GLU   A 1 102 ? -19.037 -42.880 -1.665  1.00 88.40  ? 122 GLU   A OE2 1 
ATOM   757  N  N   . ASP   A 1 103 ? -25.225 -41.324 0.224   1.00 90.83  ? 123 ASP   A N   1 
ATOM   758  C  CA  . ASP   A 1 103 ? -26.477 -41.936 0.663   1.00 97.07  ? 123 ASP   A CA  1 
ATOM   759  C  C   . ASP   A 1 103 ? -27.136 -41.207 1.829   1.00 102.67 ? 123 ASP   A C   1 
ATOM   760  O  O   . ASP   A 1 103 ? -27.576 -40.062 1.685   1.00 104.63 ? 123 ASP   A O   1 
ATOM   761  C  CB  . ASP   A 1 103 ? -26.235 -43.401 1.035   1.00 102.88 ? 123 ASP   A CB  1 
ATOM   762  C  CG  . ASP   A 1 103 ? -26.039 -44.285 -0.182  1.00 99.24  ? 123 ASP   A CG  1 
ATOM   763  O  OD1 . ASP   A 1 103 ? -26.954 -44.339 -1.032  1.00 100.88 ? 123 ASP   A OD1 1 
ATOM   764  O  OD2 . ASP   A 1 103 ? -24.968 -44.918 -0.296  1.00 101.91 ? 123 ASP   A OD2 1 
ATOM   765  N  N   . GLU   A 1 104 ? -27.208 -41.871 2.986   1.00 108.31 ? 124 GLU   A N   1 
ATOM   766  C  CA  . GLU   A 1 104 ? -27.970 -41.332 4.108   1.00 108.18 ? 124 GLU   A CA  1 
ATOM   767  C  C   . GLU   A 1 104 ? -27.336 -40.064 4.665   1.00 107.41 ? 124 GLU   A C   1 
ATOM   768  O  O   . GLU   A 1 104 ? -28.049 -39.130 5.051   1.00 103.33 ? 124 GLU   A O   1 
ATOM   769  C  CB  . GLU   A 1 104 ? -28.110 -42.389 5.202   1.00 111.18 ? 124 GLU   A CB  1 
ATOM   770  C  CG  . GLU   A 1 104 ? -29.034 -43.535 4.829   1.00 115.15 ? 124 GLU   A CG  1 
ATOM   771  C  CD  . GLU   A 1 104 ? -30.463 -43.077 4.610   1.00 118.81 ? 124 GLU   A CD  1 
ATOM   772  O  OE1 . GLU   A 1 104 ? -30.940 -42.223 5.386   1.00 118.61 ? 124 GLU   A OE1 1 
ATOM   773  O  OE2 . GLU   A 1 104 ? -31.105 -43.566 3.657   1.00 124.83 ? 124 GLU   A OE2 1 
ATOM   774  N  N   . GLU   A 1 105 ? -26.004 -40.008 4.720   1.00 102.34 ? 125 GLU   A N   1 
ATOM   775  C  CA  . GLU   A 1 105 ? -25.360 -38.805 5.236   1.00 103.33 ? 125 GLU   A CA  1 
ATOM   776  C  C   . GLU   A 1 105 ? -25.542 -37.634 4.279   1.00 104.66 ? 125 GLU   A C   1 
ATOM   777  O  O   . GLU   A 1 105 ? -25.781 -36.502 4.716   1.00 103.24 ? 125 GLU   A O   1 
ATOM   778  C  CB  . GLU   A 1 105 ? -23.876 -39.058 5.501   1.00 102.54 ? 125 GLU   A CB  1 
ATOM   779  C  CG  . GLU   A 1 105 ? -23.278 -38.097 6.521   1.00 106.79 ? 125 GLU   A CG  1 
ATOM   780  C  CD  . GLU   A 1 105 ? -21.764 -38.145 6.562   1.00 108.75 ? 125 GLU   A CD  1 
ATOM   781  O  OE1 . GLU   A 1 105 ? -21.147 -38.374 5.501   1.00 109.78 ? 125 GLU   A OE1 1 
ATOM   782  O  OE2 . GLU   A 1 105 ? -21.191 -37.952 7.655   1.00 113.88 ? 125 GLU   A OE2 1 
ATOM   783  N  N   . TRP   A 1 106 ? -25.440 -37.882 2.970   1.00 101.35 ? 126 TRP   A N   1 
ATOM   784  C  CA  . TRP   A 1 106 ? -25.716 -36.821 2.008   1.00 103.33 ? 126 TRP   A CA  1 
ATOM   785  C  C   . TRP   A 1 106 ? -27.185 -36.421 2.034   1.00 105.15 ? 126 TRP   A C   1 
ATOM   786  O  O   . TRP   A 1 106 ? -27.510 -35.229 1.974   1.00 101.64 ? 126 TRP   A O   1 
ATOM   787  C  CB  . TRP   A 1 106 ? -25.320 -37.247 0.595   1.00 96.99  ? 126 TRP   A CB  1 
ATOM   788  C  CG  . TRP   A 1 106 ? -26.019 -36.412 -0.434  1.00 98.71  ? 126 TRP   A CG  1 
ATOM   789  C  CD1 . TRP   A 1 106 ? -25.638 -35.184 -0.891  1.00 95.82  ? 126 TRP   A CD1 1 
ATOM   790  C  CD2 . TRP   A 1 106 ? -27.245 -36.727 -1.105  1.00 99.76  ? 126 TRP   A CD2 1 
ATOM   791  N  NE1 . TRP   A 1 106 ? -26.544 -34.720 -1.813  1.00 95.00  ? 126 TRP   A NE1 1 
ATOM   792  C  CE2 . TRP   A 1 106 ? -27.541 -35.648 -1.962  1.00 96.12  ? 126 TRP   A CE2 1 
ATOM   793  C  CE3 . TRP   A 1 106 ? -28.120 -37.818 -1.067  1.00 99.91  ? 126 TRP   A CE3 1 
ATOM   794  C  CZ2 . TRP   A 1 106 ? -28.674 -35.629 -2.772  1.00 90.44  ? 126 TRP   A CZ2 1 
ATOM   795  C  CZ3 . TRP   A 1 106 ? -29.241 -37.798 -1.875  1.00 100.51 ? 126 TRP   A CZ3 1 
ATOM   796  C  CH2 . TRP   A 1 106 ? -29.507 -36.712 -2.719  1.00 100.00 ? 126 TRP   A CH2 1 
ATOM   797  N  N   . LYS   A 1 107 ? -28.087 -37.408 2.103   1.00 120.01 ? 127 LYS   A N   1 
ATOM   798  C  CA  . LYS   A 1 107 ? -29.518 -37.121 2.145   1.00 120.78 ? 127 LYS   A CA  1 
ATOM   799  C  C   . LYS   A 1 107 ? -29.853 -36.162 3.277   1.00 123.97 ? 127 LYS   A C   1 
ATOM   800  O  O   . LYS   A 1 107 ? -30.725 -35.296 3.136   1.00 128.51 ? 127 LYS   A O   1 
ATOM   801  C  CB  . LYS   A 1 107 ? -30.305 -38.423 2.305   1.00 124.16 ? 127 LYS   A CB  1 
ATOM   802  C  CG  . LYS   A 1 107 ? -31.396 -38.641 1.271   1.00 125.86 ? 127 LYS   A CG  1 
ATOM   803  C  CD  . LYS   A 1 107 ? -31.144 -39.923 0.495   1.00 129.93 ? 127 LYS   A CD  1 
ATOM   804  C  CE  . LYS   A 1 107 ? -30.893 -41.093 1.436   1.00 127.52 ? 127 LYS   A CE  1 
ATOM   805  N  NZ  . LYS   A 1 107 ? -30.352 -42.284 0.724   1.00 125.26 ? 127 LYS   A NZ  1 
ATOM   806  N  N   . ARG   A 1 108 ? -29.164 -36.303 4.409   1.00 117.29 ? 128 ARG   A N   1 
ATOM   807  C  CA  . ARG   A 1 108 ? -29.348 -35.377 5.519   1.00 114.85 ? 128 ARG   A CA  1 
ATOM   808  C  C   . ARG   A 1 108 ? -28.706 -34.029 5.216   1.00 110.37 ? 128 ARG   A C   1 
ATOM   809  O  O   . ARG   A 1 108 ? -29.314 -32.976 5.441   1.00 107.31 ? 128 ARG   A O   1 
ATOM   810  C  CB  . ARG   A 1 108 ? -28.757 -35.979 6.791   1.00 118.41 ? 128 ARG   A CB  1 
ATOM   811  C  CG  . ARG   A 1 108 ? -29.644 -35.871 8.009   1.00 126.94 ? 128 ARG   A CG  1 
ATOM   812  C  CD  . ARG   A 1 108 ? -29.102 -36.728 9.137   1.00 140.50 ? 128 ARG   A CD  1 
ATOM   813  N  NE  . ARG   A 1 108 ? -28.945 -38.123 8.740   1.00 138.68 ? 128 ARG   A NE  1 
ATOM   814  C  CZ  . ARG   A 1 108 ? -27.780 -38.710 8.502   1.00 132.69 ? 128 ARG   A CZ  1 
ATOM   815  N  NH1 . ARG   A 1 108 ? -26.637 -38.055 8.629   1.00 127.22 ? 128 ARG   A NH1 1 
ATOM   816  N  NH2 . ARG   A 1 108 ? -27.760 -39.987 8.131   1.00 128.81 ? 128 ARG   A NH2 1 
ATOM   817  N  N   . LEU   A 1 109 ? -27.471 -34.045 4.707   1.00 109.76 ? 129 LEU   A N   1 
ATOM   818  C  CA  . LEU   A 1 109 ? -26.779 -32.798 4.397   1.00 109.72 ? 129 LEU   A CA  1 
ATOM   819  C  C   . LEU   A 1 109 ? -27.529 -31.998 3.340   1.00 109.67 ? 129 LEU   A C   1 
ATOM   820  O  O   . LEU   A 1 109 ? -27.535 -30.762 3.375   1.00 109.87 ? 129 LEU   A O   1 
ATOM   821  C  CB  . LEU   A 1 109 ? -25.352 -33.090 3.934   1.00 101.78 ? 129 LEU   A CB  1 
ATOM   822  C  CG  . LEU   A 1 109 ? -24.389 -33.620 4.995   1.00 98.95  ? 129 LEU   A CG  1 
ATOM   823  C  CD1 . LEU   A 1 109 ? -23.146 -34.173 4.331   1.00 99.55  ? 129 LEU   A CD1 1 
ATOM   824  C  CD2 . LEU   A 1 109 ? -24.025 -32.528 5.990   1.00 104.73 ? 129 LEU   A CD2 1 
ATOM   825  N  N   . ARG   A 1 110 ? -28.167 -32.685 2.391   1.00 102.63 ? 130 ARG   A N   1 
ATOM   826  C  CA  . ARG   A 1 110 ? -28.971 -31.988 1.393   1.00 101.09 ? 130 ARG   A CA  1 
ATOM   827  C  C   . ARG   A 1 110 ? -30.167 -31.304 2.043   1.00 103.75 ? 130 ARG   A C   1 
ATOM   828  O  O   . ARG   A 1 110 ? -30.416 -30.114 1.818   1.00 102.44 ? 130 ARG   A O   1 
ATOM   829  C  CB  . ARG   A 1 110 ? -29.433 -32.968 0.315   1.00 99.96  ? 130 ARG   A CB  1 
ATOM   830  C  CG  . ARG   A 1 110 ? -30.103 -32.302 -0.875  1.00 94.69  ? 130 ARG   A CG  1 
ATOM   831  C  CD  . ARG   A 1 110 ? -29.075 -31.727 -1.834  1.00 92.40  ? 130 ARG   A CD  1 
ATOM   832  N  NE  . ARG   A 1 110 ? -29.699 -31.019 -2.945  1.00 91.35  ? 130 ARG   A NE  1 
ATOM   833  C  CZ  . ARG   A 1 110 ? -29.077 -30.690 -4.069  1.00 87.52  ? 130 ARG   A CZ  1 
ATOM   834  N  NH1 . ARG   A 1 110 ? -27.810 -31.012 -4.277  1.00 85.87  ? 130 ARG   A NH1 1 
ATOM   835  N  NH2 . ARG   A 1 110 ? -29.743 -30.027 -5.009  1.00 84.67  ? 130 ARG   A NH2 1 
ATOM   836  N  N   . SER   A 1 111 ? -30.917 -32.044 2.863   1.00 104.22 ? 131 SER   A N   1 
ATOM   837  C  CA  . SER   A 1 111 ? -32.062 -31.460 3.552   1.00 105.30 ? 131 SER   A CA  1 
ATOM   838  C  C   . SER   A 1 111 ? -31.631 -30.392 4.547   1.00 105.92 ? 131 SER   A C   1 
ATOM   839  O  O   . SER   A 1 111 ? -32.385 -29.448 4.813   1.00 107.29 ? 131 SER   A O   1 
ATOM   840  C  CB  . SER   A 1 111 ? -32.861 -32.556 4.259   1.00 106.47 ? 131 SER   A CB  1 
ATOM   841  O  OG  . SER   A 1 111 ? -34.044 -32.036 4.838   1.00 113.06 ? 131 SER   A OG  1 
ATOM   842  N  N   . LEU   A 1 112 ? -30.424 -30.521 5.102   1.00 105.29 ? 132 LEU   A N   1 
ATOM   843  C  CA  . LEU   A 1 112 ? -29.940 -29.528 6.055   1.00 108.87 ? 132 LEU   A CA  1 
ATOM   844  C  C   . LEU   A 1 112 ? -29.586 -28.219 5.359   1.00 109.72 ? 132 LEU   A C   1 
ATOM   845  O  O   . LEU   A 1 112 ? -29.851 -27.135 5.892   1.00 109.99 ? 132 LEU   A O   1 
ATOM   846  C  CB  . LEU   A 1 112 ? -28.728 -30.073 6.809   1.00 110.45 ? 132 LEU   A CB  1 
ATOM   847  C  CG  . LEU   A 1 112 ? -28.272 -29.314 8.059   1.00 113.59 ? 132 LEU   A CG  1 
ATOM   848  C  CD1 . LEU   A 1 112 ? -28.926 -29.889 9.309   1.00 122.81 ? 132 LEU   A CD1 1 
ATOM   849  C  CD2 . LEU   A 1 112 ? -26.756 -29.329 8.181   1.00 119.48 ? 132 LEU   A CD2 1 
ATOM   850  N  N   . LEU   A 1 113 ? -28.992 -28.297 4.168   1.00 109.15 ? 133 LEU   A N   1 
ATOM   851  C  CA  . LEU   A 1 113 ? -28.493 -27.122 3.464   1.00 109.84 ? 133 LEU   A CA  1 
ATOM   852  C  C   . LEU   A 1 113 ? -29.385 -26.673 2.315   1.00 109.73 ? 133 LEU   A C   1 
ATOM   853  O  O   . LEU   A 1 113 ? -29.037 -25.709 1.625   1.00 111.16 ? 133 LEU   A O   1 
ATOM   854  C  CB  . LEU   A 1 113 ? -27.076 -27.380 2.938   1.00 108.29 ? 133 LEU   A CB  1 
ATOM   855  C  CG  . LEU   A 1 113 ? -25.948 -27.218 3.959   1.00 112.98 ? 133 LEU   A CG  1 
ATOM   856  C  CD1 . LEU   A 1 113 ? -26.286 -26.087 4.915   1.00 119.42 ? 133 LEU   A CD1 1 
ATOM   857  C  CD2 . LEU   A 1 113 ? -25.677 -28.509 4.716   1.00 113.84 ? 133 LEU   A CD2 1 
ATOM   858  N  N   . SER   A 1 114 ? -30.517 -27.339 2.090   1.00 111.35 ? 134 SER   A N   1 
ATOM   859  C  CA  . SER   A 1 114 ? -31.425 -26.914 1.025   1.00 114.31 ? 134 SER   A CA  1 
ATOM   860  C  C   . SER   A 1 114 ? -31.941 -25.489 1.199   1.00 121.38 ? 134 SER   A C   1 
ATOM   861  O  O   . SER   A 1 114 ? -31.905 -24.724 0.219   1.00 121.24 ? 134 SER   A O   1 
ATOM   862  C  CB  . SER   A 1 114 ? -32.585 -27.909 0.905   1.00 106.48 ? 134 SER   A CB  1 
ATOM   863  O  OG  . SER   A 1 114 ? -32.244 -28.993 0.057   1.00 110.26 ? 134 SER   A OG  1 
ATOM   864  N  N   . PRO   A 1 115 ? -32.424 -25.053 2.385   1.00 121.06 ? 135 PRO   A N   1 
ATOM   865  C  CA  . PRO   A 1 115 ? -33.054 -23.725 2.460   1.00 120.45 ? 135 PRO   A CA  1 
ATOM   866  C  C   . PRO   A 1 115 ? -32.137 -22.530 2.242   1.00 127.98 ? 135 PRO   A C   1 
ATOM   867  O  O   . PRO   A 1 115 ? -32.599 -21.385 2.278   1.00 133.85 ? 135 PRO   A O   1 
ATOM   868  C  CB  . PRO   A 1 115 ? -33.793 -23.770 3.802   1.00 122.61 ? 135 PRO   A CB  1 
ATOM   869  C  CG  . PRO   A 1 115 ? -32.979 -24.684 4.627   1.00 118.72 ? 135 PRO   A CG  1 
ATOM   870  C  CD  . PRO   A 1 115 ? -32.499 -25.751 3.683   1.00 118.12 ? 135 PRO   A CD  1 
ATOM   871  N  N   . THR   A 1 116 ? -30.847 -22.769 2.009   1.00 129.32 ? 136 THR   A N   1 
ATOM   872  C  CA  . THR   A 1 116 ? -29.919 -21.677 1.748   1.00 133.68 ? 136 THR   A CA  1 
ATOM   873  C  C   . THR   A 1 116 ? -30.104 -20.856 0.479   1.00 133.07 ? 136 THR   A C   1 
ATOM   874  O  O   . THR   A 1 116 ? -29.710 -19.684 0.453   1.00 134.47 ? 136 THR   A O   1 
ATOM   875  C  CB  . THR   A 1 116 ? -28.490 -22.232 1.792   1.00 136.51 ? 136 THR   A CB  1 
ATOM   876  O  OG1 . THR   A 1 116 ? -28.412 -23.272 2.774   1.00 134.32 ? 136 THR   A OG1 1 
ATOM   877  C  CG2 . THR   A 1 116 ? -27.501 -21.133 2.161   1.00 135.94 ? 136 THR   A CG2 1 
ATOM   878  N  N   . PHE   A 1 117 ? -30.701 -21.431 -0.562  1.00 131.81 ? 137 PHE   A N   1 
ATOM   879  C  CA  . PHE   A 1 117 ? -30.925 -20.745 -1.830  1.00 131.79 ? 137 PHE   A CA  1 
ATOM   880  C  C   . PHE   A 1 117 ? -32.360 -20.946 -2.302  1.00 132.18 ? 137 PHE   A C   1 
ATOM   881  O  O   . PHE   A 1 117 ? -32.615 -21.380 -3.428  1.00 128.30 ? 137 PHE   A O   1 
ATOM   882  C  CB  . PHE   A 1 117 ? -29.946 -21.225 -2.898  1.00 124.59 ? 137 PHE   A CB  1 
ATOM   883  C  CG  . PHE   A 1 117 ? -28.510 -21.190 -2.466  1.00 121.14 ? 137 PHE   A CG  1 
ATOM   884  C  CD1 . PHE   A 1 117 ? -27.907 -19.994 -2.113  1.00 121.90 ? 137 PHE   A CD1 1 
ATOM   885  C  CD2 . PHE   A 1 117 ? -27.759 -22.352 -2.424  1.00 116.03 ? 137 PHE   A CD2 1 
ATOM   886  C  CE1 . PHE   A 1 117 ? -26.583 -19.959 -1.719  1.00 118.16 ? 137 PHE   A CE1 1 
ATOM   887  C  CE2 . PHE   A 1 117 ? -26.434 -22.324 -2.032  1.00 114.35 ? 137 PHE   A CE2 1 
ATOM   888  C  CZ  . PHE   A 1 117 ? -25.846 -21.125 -1.679  1.00 116.99 ? 137 PHE   A CZ  1 
ATOM   889  N  N   . THR   A 1 118 ? -33.323 -20.622 -1.446  1.00 142.64 ? 138 THR   A N   1 
ATOM   890  C  CA  . THR   A 1 118 ? -34.729 -20.714 -1.819  1.00 144.67 ? 138 THR   A CA  1 
ATOM   891  C  C   . THR   A 1 118 ? -35.082 -19.552 -2.746  1.00 144.85 ? 138 THR   A C   1 
ATOM   892  O  O   . THR   A 1 118 ? -34.219 -18.810 -3.224  1.00 142.79 ? 138 THR   A O   1 
ATOM   893  C  CB  . THR   A 1 118 ? -35.623 -20.724 -0.583  1.00 144.49 ? 138 THR   A CB  1 
ATOM   894  O  OG1 . THR   A 1 118 ? -35.746 -19.392 -0.068  1.00 141.74 ? 138 THR   A OG1 1 
ATOM   895  C  CG2 . THR   A 1 118 ? -35.039 -21.617 0.486   1.00 145.92 ? 138 THR   A CG2 1 
ATOM   896  N  N   . SER   A 1 119 ? -36.379 -19.386 -3.012  1.00 156.91 ? 139 SER   A N   1 
ATOM   897  C  CA  . SER   A 1 119 ? -36.830 -18.278 -3.846  1.00 158.86 ? 139 SER   A CA  1 
ATOM   898  C  C   . SER   A 1 119 ? -36.531 -16.942 -3.177  1.00 161.94 ? 139 SER   A C   1 
ATOM   899  O  O   . SER   A 1 119 ? -35.848 -16.082 -3.746  1.00 160.92 ? 139 SER   A O   1 
ATOM   900  C  CB  . SER   A 1 119 ? -38.327 -18.415 -4.137  1.00 156.09 ? 139 SER   A CB  1 
ATOM   901  O  OG  . SER   A 1 119 ? -38.643 -19.704 -4.633  1.00 150.04 ? 139 SER   A OG  1 
ATOM   902  N  N   . GLY   A 1 120 ? -37.030 -16.758 -1.949  1.00 151.76 ? 140 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 120 ? -36.797 -15.523 -1.223  1.00 148.29 ? 140 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 120 ? -35.462 -15.436 -0.510  1.00 146.71 ? 140 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 120 ? -35.048 -14.333 -0.139  1.00 143.23 ? 140 GLY   A O   1 
ATOM   906  N  N   . LYS   A 1 121 ? -34.780 -16.570 -0.303  1.00 142.44 ? 141 LYS   A N   1 
ATOM   907  C  CA  . LYS   A 1 121 ? -33.466 -16.530 0.335   1.00 141.73 ? 141 LYS   A CA  1 
ATOM   908  C  C   . LYS   A 1 121 ? -32.460 -15.759 -0.507  1.00 137.47 ? 141 LYS   A C   1 
ATOM   909  O  O   . LYS   A 1 121 ? -31.548 -15.124 0.036   1.00 134.13 ? 141 LYS   A O   1 
ATOM   910  C  CB  . LYS   A 1 121 ? -32.959 -17.950 0.597   1.00 137.83 ? 141 LYS   A CB  1 
ATOM   911  C  CG  . LYS   A 1 121 ? -32.950 -18.352 2.066   1.00 137.45 ? 141 LYS   A CG  1 
ATOM   912  C  CD  . LYS   A 1 121 ? -34.328 -18.208 2.692   1.00 139.62 ? 141 LYS   A CD  1 
ATOM   913  C  CE  . LYS   A 1 121 ? -34.274 -18.408 4.199   1.00 140.02 ? 141 LYS   A CE  1 
ATOM   914  N  NZ  . LYS   A 1 121 ? -33.827 -19.780 4.567   1.00 133.87 ? 141 LYS   A NZ  1 
ATOM   915  N  N   . LEU   A 1 122 ? -32.606 -15.805 -1.830  1.00 140.63 ? 142 LEU   A N   1 
ATOM   916  C  CA  . LEU   A 1 122 ? -31.737 -15.039 -2.711  1.00 140.03 ? 142 LEU   A CA  1 
ATOM   917  C  C   . LEU   A 1 122 ? -32.187 -13.593 -2.850  1.00 136.83 ? 142 LEU   A C   1 
ATOM   918  O  O   . LEU   A 1 122 ? -31.385 -12.743 -3.253  1.00 135.91 ? 142 LEU   A O   1 
ATOM   919  C  CB  . LEU   A 1 122 ? -31.683 -15.697 -4.092  1.00 139.30 ? 142 LEU   A CB  1 
ATOM   920  C  CG  . LEU   A 1 122 ? -31.427 -17.207 -4.118  1.00 134.00 ? 142 LEU   A CG  1 
ATOM   921  C  CD1 . LEU   A 1 122 ? -31.627 -17.770 -5.516  1.00 123.68 ? 142 LEU   A CD1 1 
ATOM   922  C  CD2 . LEU   A 1 122 ? -30.035 -17.533 -3.605  1.00 129.09 ? 142 LEU   A CD2 1 
ATOM   923  N  N   . LYS   A 1 123 ? -33.447 -13.297 -2.523  1.00 140.86 ? 143 LYS   A N   1 
ATOM   924  C  CA  . LYS   A 1 123 ? -33.962 -11.944 -2.697  1.00 145.09 ? 143 LYS   A CA  1 
ATOM   925  C  C   . LYS   A 1 123 ? -33.346 -10.947 -1.726  1.00 142.33 ? 143 LYS   A C   1 
ATOM   926  O  O   . LYS   A 1 123 ? -33.019 -9.815  -2.100  1.00 143.34 ? 143 LYS   A O   1 
ATOM   927  C  CB  . LYS   A 1 123 ? -35.475 -11.933 -2.476  1.00 142.81 ? 143 LYS   A CB  1 
ATOM   928  C  CG  . LYS   A 1 123 ? -36.267 -11.136 -3.506  1.00 143.08 ? 143 LYS   A CG  1 
ATOM   929  C  CD  . LYS   A 1 123 ? -36.174 -9.638  -3.254  1.00 142.29 ? 143 LYS   A CD  1 
ATOM   930  C  CE  . LYS   A 1 123 ? -36.885 -8.848  -4.342  1.00 140.59 ? 143 LYS   A CE  1 
ATOM   931  N  NZ  . LYS   A 1 123 ? -38.264 -9.356  -4.584  1.00 139.48 ? 143 LYS   A NZ  1 
ATOM   932  N  N   . GLU   A 1 124 ? -33.154 -11.360 -0.477  1.00 135.75 ? 144 GLU   A N   1 
ATOM   933  C  CA  . GLU   A 1 124 ? -32.415 -10.573 0.509   1.00 137.51 ? 144 GLU   A CA  1 
ATOM   934  C  C   . GLU   A 1 124 ? -30.912 -10.815 0.469   1.00 137.49 ? 144 GLU   A C   1 
ATOM   935  O  O   . GLU   A 1 124 ? -30.239 -10.722 1.498   1.00 138.85 ? 144 GLU   A O   1 
ATOM   936  C  CB  . GLU   A 1 124 ? -32.991 -10.835 1.898   1.00 137.21 ? 144 GLU   A CB  1 
ATOM   937  C  CG  . GLU   A 1 124 ? -34.385 -10.255 2.111   1.00 141.62 ? 144 GLU   A CG  1 
ATOM   938  C  CD  . GLU   A 1 124 ? -34.432 -8.756  1.879   1.00 142.09 ? 144 GLU   A CD  1 
ATOM   939  O  OE1 . GLU   A 1 124 ? -34.480 -8.326  0.706   1.00 138.58 ? 144 GLU   A OE1 1 
ATOM   940  O  OE2 . GLU   A 1 124 ? -34.399 -8.006  2.875   1.00 151.30 ? 144 GLU   A OE2 1 
ATOM   941  N  N   . MET   A 1 125 ? -30.372 -11.164 -0.695  1.00 137.54 ? 145 MET   A N   1 
ATOM   942  C  CA  . MET   A 1 125 ? -28.935 -11.196 -0.926  1.00 135.73 ? 145 MET   A CA  1 
ATOM   943  C  C   . MET   A 1 125 ? -28.441 -10.065 -1.811  1.00 134.26 ? 145 MET   A C   1 
ATOM   944  O  O   . MET   A 1 125 ? -27.348 -9.538  -1.574  1.00 131.70 ? 145 MET   A O   1 
ATOM   945  C  CB  . MET   A 1 125 ? -28.525 -12.528 -1.566  1.00 134.09 ? 145 MET   A CB  1 
ATOM   946  C  CG  . MET   A 1 125 ? -28.708 -13.747 -0.697  1.00 133.79 ? 145 MET   A CG  1 
ATOM   947  S  SD  . MET   A 1 125 ? -28.121 -15.248 -1.506  1.00 140.25 ? 145 MET   A SD  1 
ATOM   948  C  CE  . MET   A 1 125 ? -28.486 -16.463 -0.243  1.00 133.33 ? 145 MET   A CE  1 
ATOM   949  N  N   . VAL   A 1 126 ? -29.230 -9.685  -2.816  1.00 141.73 ? 146 VAL   A N   1 
ATOM   950  C  CA  . VAL   A 1 126 ? -28.918 -8.643  -3.801  1.00 141.59 ? 146 VAL   A CA  1 
ATOM   951  C  C   . VAL   A 1 126 ? -28.511 -7.324  -3.147  1.00 145.77 ? 146 VAL   A C   1 
ATOM   952  O  O   . VAL   A 1 126 ? -27.564 -6.677  -3.624  1.00 148.88 ? 146 VAL   A O   1 
ATOM   953  C  CB  . VAL   A 1 126 ? -30.107 -8.401  -4.750  1.00 142.09 ? 146 VAL   A CB  1 
ATOM   954  C  CG1 . VAL   A 1 126 ? -29.803 -7.274  -5.718  1.00 139.93 ? 146 VAL   A CG1 1 
ATOM   955  C  CG2 . VAL   A 1 126 ? -30.498 -9.682  -5.467  1.00 138.99 ? 146 VAL   A CG2 1 
ATOM   956  N  N   . PRO   A 1 127 ? -29.210 -6.846  -2.107  1.00 147.80 ? 147 PRO   A N   1 
ATOM   957  C  CA  . PRO   A 1 127 ? -28.725 -5.636  -1.416  1.00 148.73 ? 147 PRO   A CA  1 
ATOM   958  C  C   . PRO   A 1 127 ? -27.306 -5.774  -0.892  1.00 150.33 ? 147 PRO   A C   1 
ATOM   959  O  O   . PRO   A 1 127 ? -26.572 -4.779  -0.835  1.00 148.68 ? 147 PRO   A O   1 
ATOM   960  C  CB  . PRO   A 1 127 ? -29.739 -5.458  -0.274  1.00 153.76 ? 147 PRO   A CB  1 
ATOM   961  C  CG  . PRO   A 1 127 ? -30.981 -6.077  -0.808  1.00 153.09 ? 147 PRO   A CG  1 
ATOM   962  C  CD  . PRO   A 1 127 ? -30.540 -7.251  -1.605  1.00 147.20 ? 147 PRO   A CD  1 
ATOM   963  N  N   . ILE   A 1 128 ? -26.887 -6.984  -0.525  1.00 143.49 ? 148 ILE   A N   1 
ATOM   964  C  CA  . ILE   A 1 128 ? -25.512 -7.174  -0.079  1.00 138.85 ? 148 ILE   A CA  1 
ATOM   965  C  C   . ILE   A 1 128 ? -24.589 -7.397  -1.269  1.00 138.06 ? 148 ILE   A C   1 
ATOM   966  O  O   . ILE   A 1 128 ? -23.465 -6.886  -1.297  1.00 137.63 ? 148 ILE   A O   1 
ATOM   967  C  CB  . ILE   A 1 128 ? -25.426 -8.330  0.935   1.00 131.94 ? 148 ILE   A CB  1 
ATOM   968  C  CG1 . ILE   A 1 128 ? -26.181 -7.976  2.219   1.00 129.86 ? 148 ILE   A CG1 1 
ATOM   969  C  CG2 . ILE   A 1 128 ? -23.968 -8.652  1.257   1.00 126.37 ? 148 ILE   A CG2 1 
ATOM   970  C  CD1 . ILE   A 1 128 ? -26.038 -9.009  3.319   1.00 122.94 ? 148 ILE   A CD1 1 
ATOM   971  N  N   . ILE   A 1 129 ? -25.051 -8.146  -2.274  1.00 134.90 ? 149 ILE   A N   1 
ATOM   972  C  CA  . ILE   A 1 129 ? -24.229 -8.417  -3.452  1.00 135.24 ? 149 ILE   A CA  1 
ATOM   973  C  C   . ILE   A 1 129 ? -23.986 -7.136  -4.245  1.00 136.60 ? 149 ILE   A C   1 
ATOM   974  O  O   . ILE   A 1 129 ? -22.905 -6.938  -4.817  1.00 134.47 ? 149 ILE   A O   1 
ATOM   975  C  CB  . ILE   A 1 129 ? -24.892 -9.504  -4.321  1.00 129.69 ? 149 ILE   A CB  1 
ATOM   976  C  CG1 . ILE   A 1 129 ? -25.204 -10.756 -3.498  1.00 129.52 ? 149 ILE   A CG1 1 
ATOM   977  C  CG2 . ILE   A 1 129 ? -23.995 -9.879  -5.486  1.00 125.34 ? 149 ILE   A CG2 1 
ATOM   978  C  CD1 . ILE   A 1 129 ? -26.079 -11.762 -4.231  1.00 128.31 ? 149 ILE   A CD1 1 
ATOM   979  N  N   . ALA   A 1 130 ? -24.980 -6.242  -4.282  1.00 137.69 ? 150 ALA   A N   1 
ATOM   980  C  CA  . ALA   A 1 130 ? -24.882 -5.046  -5.116  1.00 140.45 ? 150 ALA   A CA  1 
ATOM   981  C  C   . ALA   A 1 130 ? -23.736 -4.146  -4.673  1.00 145.15 ? 150 ALA   A C   1 
ATOM   982  O  O   . ALA   A 1 130 ? -23.084 -3.504  -5.507  1.00 147.39 ? 150 ALA   A O   1 
ATOM   983  C  CB  . ALA   A 1 130 ? -26.203 -4.276  -5.088  1.00 137.51 ? 150 ALA   A CB  1 
ATOM   984  N  N   . GLN   A 1 131 ? -23.479 -4.087  -3.361  1.00 147.45 ? 151 GLN   A N   1 
ATOM   985  C  CA  . GLN   A 1 131 ? -22.399 -3.247  -2.848  1.00 143.82 ? 151 GLN   A CA  1 
ATOM   986  C  C   . GLN   A 1 131 ? -21.046 -3.702  -3.381  1.00 147.39 ? 151 GLN   A C   1 
ATOM   987  O  O   . GLN   A 1 131 ? -20.199 -2.875  -3.741  1.00 154.34 ? 151 GLN   A O   1 
ATOM   988  C  CB  . GLN   A 1 131 ? -22.401 -3.257  -1.317  1.00 142.99 ? 151 GLN   A CB  1 
ATOM   989  C  CG  . GLN   A 1 131 ? -23.767 -3.018  -0.692  1.00 147.13 ? 151 GLN   A CG  1 
ATOM   990  C  CD  . GLN   A 1 131 ? -23.688 -2.327  0.659   1.00 155.39 ? 151 GLN   A CD  1 
ATOM   991  O  OE1 . GLN   A 1 131 ? -24.156 -1.201  0.810   1.00 155.01 ? 151 GLN   A OE1 1 
ATOM   992  N  NE2 . GLN   A 1 131 ? -23.104 -3.000  1.647   1.00 156.46 ? 151 GLN   A NE2 1 
ATOM   993  N  N   . TYR   A 1 132 ? -20.827 -5.015  -3.450  1.00 140.30 ? 152 TYR   A N   1 
ATOM   994  C  CA  . TYR   A 1 132 ? -19.562 -5.517  -3.975  1.00 140.88 ? 152 TYR   A CA  1 
ATOM   995  C  C   . TYR   A 1 132 ? -19.439 -5.279  -5.471  1.00 144.74 ? 152 TYR   A C   1 
ATOM   996  O  O   . TYR   A 1 132 ? -18.320 -5.277  -6.006  1.00 144.16 ? 152 TYR   A O   1 
ATOM   997  C  CB  . TYR   A 1 132 ? -19.415 -7.003  -3.667  1.00 133.32 ? 152 TYR   A CB  1 
ATOM   998  C  CG  . TYR   A 1 132 ? -19.298 -7.288  -2.192  1.00 133.49 ? 152 TYR   A CG  1 
ATOM   999  C  CD1 . TYR   A 1 132 ? -18.070 -7.226  -1.550  1.00 139.35 ? 152 TYR   A CD1 1 
ATOM   1000 C  CD2 . TYR   A 1 132 ? -20.417 -7.608  -1.437  1.00 133.87 ? 152 TYR   A CD2 1 
ATOM   1001 C  CE1 . TYR   A 1 132 ? -17.954 -7.484  -0.198  1.00 145.24 ? 152 TYR   A CE1 1 
ATOM   1002 C  CE2 . TYR   A 1 132 ? -20.314 -7.866  -0.084  1.00 133.14 ? 152 TYR   A CE2 1 
ATOM   1003 C  CZ  . TYR   A 1 132 ? -19.079 -7.801  0.530   1.00 142.64 ? 152 TYR   A CZ  1 
ATOM   1004 O  OH  . TYR   A 1 132 ? -18.967 -8.058  1.877   1.00 150.19 ? 152 TYR   A OH  1 
ATOM   1005 N  N   . GLY   A 1 133 ? -20.570 -5.108  -6.161  1.00 163.34 ? 153 GLY   A N   1 
ATOM   1006 C  CA  . GLY   A 1 133 ? -20.512 -4.758  -7.569  1.00 158.40 ? 153 GLY   A CA  1 
ATOM   1007 C  C   . GLY   A 1 133 ? -19.763 -3.458  -7.802  1.00 172.37 ? 153 GLY   A C   1 
ATOM   1008 O  O   . GLY   A 1 133 ? -18.880 -3.380  -8.660  1.00 173.31 ? 153 GLY   A O   1 
ATOM   1009 N  N   . ASP   A 1 134 ? -20.105 -2.417  -7.032  1.00 187.30 ? 154 ASP   A N   1 
ATOM   1010 C  CA  . ASP   A 1 134 ? -19.424 -1.129  -7.157  1.00 184.81 ? 154 ASP   A CA  1 
ATOM   1011 C  C   . ASP   A 1 134 ? -17.931 -1.275  -6.909  1.00 182.94 ? 154 ASP   A C   1 
ATOM   1012 O  O   . ASP   A 1 134 ? -17.112 -0.674  -7.613  1.00 184.34 ? 154 ASP   A O   1 
ATOM   1013 C  CB  . ASP   A 1 134 ? -20.024 -0.124  -6.176  1.00 184.06 ? 154 ASP   A CB  1 
ATOM   1014 C  CG  . ASP   A 1 134 ? -19.001 0.850   -5.648  1.00 187.92 ? 154 ASP   A CG  1 
ATOM   1015 O  OD1 . ASP   A 1 134 ? -18.646 1.815   -6.364  1.00 185.68 ? 154 ASP   A OD1 1 
ATOM   1016 O  OD2 . ASP   A 1 134 ? -18.515 0.632   -4.518  1.00 187.81 ? 154 ASP   A OD2 1 
ATOM   1017 N  N   . VAL   A 1 135 ? -17.562 -2.072  -5.900  1.00 162.39 ? 155 VAL   A N   1 
ATOM   1018 C  CA  . VAL   A 1 135 ? -16.152 -2.317  -5.597  1.00 159.75 ? 155 VAL   A CA  1 
ATOM   1019 C  C   . VAL   A 1 135 ? -15.446 -2.863  -6.822  1.00 158.22 ? 155 VAL   A C   1 
ATOM   1020 O  O   . VAL   A 1 135 ? -14.277 -2.550  -7.081  1.00 158.03 ? 155 VAL   A O   1 
ATOM   1021 C  CB  . VAL   A 1 135 ? -16.019 -3.282  -4.404  1.00 158.38 ? 155 VAL   A CB  1 
ATOM   1022 C  CG1 . VAL   A 1 135 ? -14.557 -3.394  -3.958  1.00 159.51 ? 155 VAL   A CG1 1 
ATOM   1023 C  CG2 . VAL   A 1 135 ? -16.911 -2.845  -3.264  1.00 160.37 ? 155 VAL   A CG2 1 
ATOM   1024 N  N   . LEU   A 1 136 ? -16.149 -3.693  -7.591  1.00 154.99 ? 156 LEU   A N   1 
ATOM   1025 C  CA  . LEU   A 1 136 ? -15.594 -4.208  -8.834  1.00 153.59 ? 156 LEU   A CA  1 
ATOM   1026 C  C   . LEU   A 1 136 ? -15.448 -3.097  -9.868  1.00 161.54 ? 156 LEU   A C   1 
ATOM   1027 O  O   . LEU   A 1 136 ? -14.387 -2.947  -10.485 1.00 159.87 ? 156 LEU   A O   1 
ATOM   1028 C  CB  . LEU   A 1 136 ? -16.473 -5.341  -9.369  1.00 142.62 ? 156 LEU   A CB  1 
ATOM   1029 C  CG  . LEU   A 1 136 ? -15.769 -6.381  -10.245 1.00 132.59 ? 156 LEU   A CG  1 
ATOM   1030 C  CD1 . LEU   A 1 136 ? -14.568 -6.932  -9.501  1.00 131.39 ? 156 LEU   A CD1 1 
ATOM   1031 C  CD2 . LEU   A 1 136 ? -16.726 -7.499  -10.646 1.00 124.76 ? 156 LEU   A CD2 1 
ATOM   1032 N  N   . VAL   A 1 137 ? -16.495 -2.287  -10.055 1.00 157.73 ? 157 VAL   A N   1 
ATOM   1033 C  CA  . VAL   A 1 137 ? -16.424 -1.233  -11.067 1.00 159.88 ? 157 VAL   A CA  1 
ATOM   1034 C  C   . VAL   A 1 137 ? -15.386 -0.183  -10.680 1.00 162.21 ? 157 VAL   A C   1 
ATOM   1035 O  O   . VAL   A 1 137 ? -14.812 0.484   -11.550 1.00 165.95 ? 157 VAL   A O   1 
ATOM   1036 C  CB  . VAL   A 1 137 ? -17.816 -0.604  -11.311 1.00 160.13 ? 157 VAL   A CB  1 
ATOM   1037 C  CG1 . VAL   A 1 137 ? -18.925 -1.653  -11.192 1.00 156.19 ? 157 VAL   A CG1 1 
ATOM   1038 C  CG2 . VAL   A 1 137 ? -18.065 0.577   -10.379 1.00 168.85 ? 157 VAL   A CG2 1 
ATOM   1039 N  N   . ARG   A 1 138 ? -15.115 -0.030  -9.380  1.00 164.30 ? 158 ARG   A N   1 
ATOM   1040 C  CA  . ARG   A 1 138 ? -14.057 0.875   -8.939  1.00 164.04 ? 158 ARG   A CA  1 
ATOM   1041 C  C   . ARG   A 1 138 ? -12.690 0.326   -9.327  1.00 160.95 ? 158 ARG   A C   1 
ATOM   1042 O  O   . ARG   A 1 138 ? -11.897 1.004   -9.990  1.00 162.78 ? 158 ARG   A O   1 
ATOM   1043 C  CB  . ARG   A 1 138 ? -14.157 1.103   -7.424  1.00 166.80 ? 158 ARG   A CB  1 
ATOM   1044 C  CG  . ARG   A 1 138 ? -12.829 1.383   -6.713  1.00 167.08 ? 158 ARG   A CG  1 
ATOM   1045 C  CD  . ARG   A 1 138 ? -12.187 2.698   -7.137  1.00 166.61 ? 158 ARG   A CD  1 
ATOM   1046 N  NE  . ARG   A 1 138 ? -10.730 2.614   -7.127  1.00 166.47 ? 158 ARG   A NE  1 
ATOM   1047 C  CZ  . ARG   A 1 138 ? -9.919  3.648   -7.302  1.00 174.33 ? 158 ARG   A CZ  1 
ATOM   1048 N  NH1 . ARG   A 1 138 ? -10.388 4.874   -7.468  1.00 174.82 ? 158 ARG   A NH1 1 
ATOM   1049 N  NH2 . ARG   A 1 138 ? -8.604  3.448   -7.310  1.00 176.71 ? 158 ARG   A NH2 1 
ATOM   1050 N  N   . ASN   A 1 139 ? -12.404 -0.913  -8.928  1.00 162.14 ? 159 ASN   A N   1 
ATOM   1051 C  CA  . ASN   A 1 139 ? -11.175 -1.575  -9.345  1.00 160.98 ? 159 ASN   A CA  1 
ATOM   1052 C  C   . ASN   A 1 139 ? -11.138 -1.823  -10.848 1.00 157.69 ? 159 ASN   A C   1 
ATOM   1053 O  O   . ASN   A 1 139 ? -10.054 -2.032  -11.404 1.00 158.42 ? 159 ASN   A O   1 
ATOM   1054 C  CB  . ASN   A 1 139 ? -11.014 -2.892  -8.581  1.00 157.81 ? 159 ASN   A CB  1 
ATOM   1055 C  CG  . ASN   A 1 139 ? -10.826 -2.680  -7.086  1.00 163.48 ? 159 ASN   A CG  1 
ATOM   1056 O  OD1 . ASN   A 1 139 ? -9.718  -2.808  -6.567  1.00 167.43 ? 159 ASN   A OD1 1 
ATOM   1057 N  ND2 . ASN   A 1 139 ? -11.910 -2.351  -6.389  1.00 162.68 ? 159 ASN   A ND2 1 
ATOM   1058 N  N   . LEU   A 1 140 ? -12.292 -1.809  -11.518 1.00 160.64 ? 160 LEU   A N   1 
ATOM   1059 C  CA  . LEU   A 1 140 ? -12.304 -1.920  -12.973 1.00 159.18 ? 160 LEU   A CA  1 
ATOM   1060 C  C   . LEU   A 1 140 ? -12.023 -0.582  -13.645 1.00 164.23 ? 160 LEU   A C   1 
ATOM   1061 O  O   . LEU   A 1 140 ? -11.407 -0.542  -14.716 1.00 163.27 ? 160 LEU   A O   1 
ATOM   1062 C  CB  . LEU   A 1 140 ? -13.647 -2.464  -13.458 1.00 154.23 ? 160 LEU   A CB  1 
ATOM   1063 C  CG  . LEU   A 1 140 ? -13.712 -3.907  -13.960 1.00 142.90 ? 160 LEU   A CG  1 
ATOM   1064 C  CD1 . LEU   A 1 140 ? -12.394 -4.626  -13.731 1.00 140.80 ? 160 LEU   A CD1 1 
ATOM   1065 C  CD2 . LEU   A 1 140 ? -14.851 -4.637  -13.277 1.00 136.59 ? 160 LEU   A CD2 1 
ATOM   1066 N  N   . ARG   A 1 141 ? -12.465 0.521   -13.034 1.00 157.99 ? 161 ARG   A N   1 
ATOM   1067 C  CA  . ARG   A 1 141 ? -12.377 1.823   -13.688 1.00 162.38 ? 161 ARG   A CA  1 
ATOM   1068 C  C   . ARG   A 1 141 ? -10.935 2.268   -13.884 1.00 172.63 ? 161 ARG   A C   1 
ATOM   1069 O  O   . ARG   A 1 141 ? -10.687 3.227   -14.626 1.00 182.66 ? 161 ARG   A O   1 
ATOM   1070 C  CB  . ARG   A 1 141 ? -13.145 2.873   -12.879 1.00 163.42 ? 161 ARG   A CB  1 
ATOM   1071 C  CG  . ARG   A 1 141 ? -13.468 4.142   -13.653 1.00 163.94 ? 161 ARG   A CG  1 
ATOM   1072 C  CD  . ARG   A 1 141 ? -14.534 3.878   -14.700 1.00 156.30 ? 161 ARG   A CD  1 
ATOM   1073 N  NE  . ARG   A 1 141 ? -15.849 3.687   -14.099 1.00 154.67 ? 161 ARG   A NE  1 
ATOM   1074 C  CZ  . ARG   A 1 141 ? -16.931 3.309   -14.765 1.00 152.05 ? 161 ARG   A CZ  1 
ATOM   1075 N  NH1 . ARG   A 1 141 ? -16.886 3.040   -16.060 1.00 152.43 ? 161 ARG   A NH1 1 
ATOM   1076 N  NH2 . ARG   A 1 141 ? -18.086 3.198   -14.116 1.00 152.31 ? 161 ARG   A NH2 1 
ATOM   1077 N  N   . ARG   A 1 142 ? -10.002 1.537   -13.269 1.00 174.13 ? 162 ARG   A N   1 
ATOM   1078 C  CA  . ARG   A 1 142 ? -8.565  1.836   -13.482 1.00 182.39 ? 162 ARG   A CA  1 
ATOM   1079 C  C   . ARG   A 1 142 ? -8.325  1.982   -14.985 1.00 191.28 ? 162 ARG   A C   1 
ATOM   1080 O  O   . ARG   A 1 142 ? -8.814  1.122   -15.743 1.00 188.73 ? 162 ARG   A O   1 
ATOM   1081 C  CB  . ARG   A 1 142 ? -7.703  0.714   -12.905 1.00 176.92 ? 162 ARG   A CB  1 
ATOM   1082 C  CG  . ARG   A 1 142 ? -7.956  0.429   -11.433 1.00 173.68 ? 162 ARG   A CG  1 
ATOM   1083 C  CD  . ARG   A 1 142 ? -7.286  -0.868  -11.025 1.00 173.32 ? 162 ARG   A CD  1 
ATOM   1084 N  NE  . ARG   A 1 142 ? -7.326  -1.834  -12.114 1.00 170.46 ? 162 ARG   A NE  1 
ATOM   1085 C  CZ  . ARG   A 1 142 ? -6.362  -2.704  -12.385 1.00 171.38 ? 162 ARG   A CZ  1 
ATOM   1086 N  NH1 . ARG   A 1 142 ? -5.272  -2.740  -11.639 1.00 171.44 ? 162 ARG   A NH1 1 
ATOM   1087 N  NH2 . ARG   A 1 142 ? -6.493  -3.539  -13.400 1.00 172.86 ? 162 ARG   A NH2 1 
ATOM   1088 N  N   . GLU   A 1 143 ? -7.587  3.019   -15.393 1.00 206.16 ? 163 GLU   A N   1 
ATOM   1089 C  CA  . GLU   A 1 143 ? -7.389  3.286   -16.843 1.00 212.13 ? 163 GLU   A CA  1 
ATOM   1090 C  C   . GLU   A 1 143 ? -5.936  3.033   -17.247 1.00 212.99 ? 163 GLU   A C   1 
ATOM   1091 O  O   . GLU   A 1 143 ? -5.227  4.013   -17.526 1.00 213.36 ? 163 GLU   A O   1 
ATOM   1092 C  CB  . GLU   A 1 143 ? -7.805  4.720   -17.171 1.00 212.10 ? 163 GLU   A CB  1 
ATOM   1093 C  CG  . GLU   A 1 143 ? -9.052  4.792   -18.031 1.00 208.64 ? 163 GLU   A CG  1 
ATOM   1094 C  CD  . GLU   A 1 143 ? -10.288 4.164   -17.411 1.00 206.98 ? 163 GLU   A CD  1 
ATOM   1095 O  OE1 . GLU   A 1 143 ? -10.453 2.932   -17.530 1.00 212.29 ? 163 GLU   A OE1 1 
ATOM   1096 O  OE2 . GLU   A 1 143 ? -11.085 4.909   -16.811 1.00 200.32 ? 163 GLU   A OE2 1 
ATOM   1097 N  N   . ALA   A 1 144 ? -5.512  1.770   -17.275 1.00 221.98 ? 164 ALA   A N   1 
ATOM   1098 C  CA  . ALA   A 1 144 ? -4.157  1.462   -17.785 1.00 220.45 ? 164 ALA   A CA  1 
ATOM   1099 C  C   . ALA   A 1 144 ? -4.265  1.352   -19.306 1.00 243.44 ? 164 ALA   A C   1 
ATOM   1100 O  O   . ALA   A 1 144 ? -4.039  0.247   -19.838 1.00 228.62 ? 164 ALA   A O   1 
ATOM   1101 C  CB  . ALA   A 1 144 ? -3.640  0.191   -17.163 1.00 199.06 ? 164 ALA   A CB  1 
ATOM   1102 N  N   . GLU   A 1 145 ? -4.616  2.453   -19.975 1.00 288.74 ? 165 GLU   A N   1 
ATOM   1103 C  CA  . GLU   A 1 145 ? -4.835  2.425   -21.446 1.00 289.01 ? 165 GLU   A CA  1 
ATOM   1104 C  C   . GLU   A 1 145 ? -3.511  2.578   -22.195 1.00 292.04 ? 165 GLU   A C   1 
ATOM   1105 O  O   . GLU   A 1 145 ? -3.276  3.666   -22.752 1.00 294.28 ? 165 GLU   A O   1 
ATOM   1106 C  CB  . GLU   A 1 145 ? -5.787  3.549   -21.855 1.00 287.42 ? 165 GLU   A CB  1 
ATOM   1107 C  CG  . GLU   A 1 145 ? -6.542  4.153   -20.686 1.00 296.29 ? 165 GLU   A CG  1 
ATOM   1108 C  CD  . GLU   A 1 145 ? -5.941  5.439   -20.147 1.00 291.38 ? 165 GLU   A CD  1 
ATOM   1109 O  OE1 . GLU   A 1 145 ? -4.704  5.501   -20.014 1.00 290.48 ? 165 GLU   A OE1 1 
ATOM   1110 O  OE2 . GLU   A 1 145 ? -6.713  6.373   -19.857 1.00 293.23 ? 165 GLU   A OE2 1 
ATOM   1111 N  N   . PRO   A 1 149 ? -4.024  -5.401  -21.700 1.00 171.73 ? 169 PRO   A N   1 
ATOM   1112 C  CA  . PRO   A 1 149 ? -5.348  -5.935  -21.370 1.00 166.15 ? 169 PRO   A CA  1 
ATOM   1113 C  C   . PRO   A 1 149 ? -5.542  -6.073  -19.854 1.00 163.88 ? 169 PRO   A C   1 
ATOM   1114 O  O   . PRO   A 1 149 ? -4.847  -5.403  -19.114 1.00 161.09 ? 169 PRO   A O   1 
ATOM   1115 C  CB  . PRO   A 1 149 ? -5.317  -7.325  -22.013 1.00 163.52 ? 169 PRO   A CB  1 
ATOM   1116 C  CG  . PRO   A 1 149 ? -3.890  -7.778  -21.816 1.00 166.44 ? 169 PRO   A CG  1 
ATOM   1117 C  CD  . PRO   A 1 149 ? -3.066  -6.512  -21.685 1.00 171.85 ? 169 PRO   A CD  1 
ATOM   1118 N  N   . VAL   A 1 150 ? -6.472  -6.934  -19.435 1.00 145.60 ? 170 VAL   A N   1 
ATOM   1119 C  CA  . VAL   A 1 150 ? -6.746  -7.140  -17.981 1.00 140.96 ? 170 VAL   A CA  1 
ATOM   1120 C  C   . VAL   A 1 150 ? -6.960  -8.637  -17.747 1.00 131.84 ? 170 VAL   A C   1 
ATOM   1121 O  O   . VAL   A 1 150 ? -7.721  -9.245  -18.524 1.00 131.99 ? 170 VAL   A O   1 
ATOM   1122 C  CB  . VAL   A 1 150 ? -7.968  -6.321  -17.525 1.00 137.31 ? 170 VAL   A CB  1 
ATOM   1123 C  CG1 . VAL   A 1 150 ? -8.768  -7.040  -16.449 1.00 137.13 ? 170 VAL   A CG1 1 
ATOM   1124 C  CG2 . VAL   A 1 150 ? -7.573  -4.928  -17.062 1.00 146.88 ? 170 VAL   A CG2 1 
ATOM   1125 N  N   . THR   A 1 151 ? -6.322  -9.210  -16.721 1.00 124.98 ? 171 THR   A N   1 
ATOM   1126 C  CA  . THR   A 1 151 ? -6.590  -10.642 -16.433 1.00 118.69 ? 171 THR   A CA  1 
ATOM   1127 C  C   . THR   A 1 151 ? -7.999  -10.751 -15.866 1.00 114.58 ? 171 THR   A C   1 
ATOM   1128 O  O   . THR   A 1 151 ? -8.180  -10.422 -14.687 1.00 119.16 ? 171 THR   A O   1 
ATOM   1129 C  CB  . THR   A 1 151 ? -5.559  -11.212 -15.460 1.00 120.98 ? 171 THR   A CB  1 
ATOM   1130 O  OG1 . THR   A 1 151 ? -5.622  -10.436 -14.264 1.00 125.46 ? 171 THR   A OG1 1 
ATOM   1131 C  CG2 . THR   A 1 151 ? -4.155  -11.184 -16.020 1.00 122.46 ? 171 THR   A CG2 1 
ATOM   1132 N  N   . LEU   A 1 152 ? -8.949  -11.216 -16.670 1.00 117.85 ? 172 LEU   A N   1 
ATOM   1133 C  CA  . LEU   A 1 152 ? -10.339 -11.218 -16.218 1.00 114.12 ? 172 LEU   A CA  1 
ATOM   1134 C  C   . LEU   A 1 152 ? -10.555 -12.092 -14.987 1.00 114.16 ? 172 LEU   A C   1 
ATOM   1135 O  O   . LEU   A 1 152 ? -11.474 -11.832 -14.202 1.00 114.30 ? 172 LEU   A O   1 
ATOM   1136 C  CB  . LEU   A 1 152 ? -11.259 -11.680 -17.350 1.00 111.60 ? 172 LEU   A CB  1 
ATOM   1137 C  CG  . LEU   A 1 152 ? -11.861 -10.619 -18.275 1.00 108.05 ? 172 LEU   A CG  1 
ATOM   1138 C  CD1 . LEU   A 1 152 ? -12.742 -9.657  -17.494 1.00 110.50 ? 172 LEU   A CD1 1 
ATOM   1139 C  CD2 . LEU   A 1 152 ? -10.777 -9.864  -19.018 1.00 116.61 ? 172 LEU   A CD2 1 
ATOM   1140 N  N   . LYS   A 1 153 ? -9.736  -13.129 -14.801 1.00 111.72 ? 173 LYS   A N   1 
ATOM   1141 C  CA  . LYS   A 1 153 ? -9.993  -14.081 -13.722 1.00 111.15 ? 173 LYS   A CA  1 
ATOM   1142 C  C   . LYS   A 1 153 ? -9.770  -13.444 -12.354 1.00 114.07 ? 173 LYS   A C   1 
ATOM   1143 O  O   . LYS   A 1 153 ? -10.604 -13.589 -11.451 1.00 113.47 ? 173 LYS   A O   1 
ATOM   1144 C  CB  . LYS   A 1 153 ? -9.114  -15.322 -13.892 1.00 106.91 ? 173 LYS   A CB  1 
ATOM   1145 C  CG  . LYS   A 1 153 ? -9.815  -16.650 -13.587 1.00 103.48 ? 173 LYS   A CG  1 
ATOM   1146 C  CD  . LYS   A 1 153 ? -10.454 -16.655 -12.204 1.00 102.20 ? 173 LYS   A CD  1 
ATOM   1147 C  CE  . LYS   A 1 153 ? -10.491 -18.049 -11.595 1.00 103.40 ? 173 LYS   A CE  1 
ATOM   1148 N  NZ  . LYS   A 1 153 ? -11.612 -18.879 -12.116 1.00 100.54 ? 173 LYS   A NZ  1 
ATOM   1149 N  N   . ASP   A 1 154 ? -8.650  -12.739 -12.177 1.00 112.82 ? 174 ASP   A N   1 
ATOM   1150 C  CA  . ASP   A 1 154 ? -8.325  -12.183 -10.865 1.00 118.70 ? 174 ASP   A CA  1 
ATOM   1151 C  C   . ASP   A 1 154 ? -9.372  -11.172 -10.413 1.00 117.59 ? 174 ASP   A C   1 
ATOM   1152 O  O   . ASP   A 1 154 ? -9.800  -11.183 -9.253  1.00 120.27 ? 174 ASP   A O   1 
ATOM   1153 C  CB  . ASP   A 1 154 ? -6.935  -11.545 -10.890 1.00 126.43 ? 174 ASP   A CB  1 
ATOM   1154 C  CG  . ASP   A 1 154 ? -5.845  -12.502 -10.448 1.00 133.78 ? 174 ASP   A CG  1 
ATOM   1155 O  OD1 . ASP   A 1 154 ? -6.149  -13.694 -10.229 1.00 130.95 ? 174 ASP   A OD1 1 
ATOM   1156 O  OD2 . ASP   A 1 154 ? -4.684  -12.062 -10.313 1.00 138.89 ? 174 ASP   A OD2 1 
ATOM   1157 N  N   . VAL   A 1 155 ? -9.797  -10.286 -11.318 1.00 118.59 ? 175 VAL   A N   1 
ATOM   1158 C  CA  . VAL   A 1 155 ? -10.808 -9.294  -10.962 1.00 116.81 ? 175 VAL   A CA  1 
ATOM   1159 C  C   . VAL   A 1 155 ? -12.126 -9.977  -10.619 1.00 115.21 ? 175 VAL   A C   1 
ATOM   1160 O  O   . VAL   A 1 155 ? -12.786 -9.627  -9.632  1.00 113.08 ? 175 VAL   A O   1 
ATOM   1161 C  CB  . VAL   A 1 155 ? -10.969 -8.261  -12.095 1.00 118.74 ? 175 VAL   A CB  1 
ATOM   1162 C  CG1 . VAL   A 1 155 ? -10.445 -8.816  -13.401 1.00 116.81 ? 175 VAL   A CG1 1 
ATOM   1163 C  CG2 . VAL   A 1 155 ? -12.423 -7.847  -12.247 1.00 117.92 ? 175 VAL   A CG2 1 
ATOM   1164 N  N   . PHE   A 1 156 ? -12.524 -10.971 -11.416 1.00 110.29 ? 176 PHE   A N   1 
ATOM   1165 C  CA  . PHE   A 1 156 ? -13.743 -11.714 -11.112 1.00 109.54 ? 176 PHE   A CA  1 
ATOM   1166 C  C   . PHE   A 1 156 ? -13.573 -12.565 -9.860  1.00 106.89 ? 176 PHE   A C   1 
ATOM   1167 O  O   . PHE   A 1 156 ? -14.511 -12.705 -9.066  1.00 105.47 ? 176 PHE   A O   1 
ATOM   1168 C  CB  . PHE   A 1 156 ? -14.139 -12.584 -12.303 1.00 106.87 ? 176 PHE   A CB  1 
ATOM   1169 C  CG  . PHE   A 1 156 ? -14.730 -11.813 -13.447 1.00 105.24 ? 176 PHE   A CG  1 
ATOM   1170 C  CD1 . PHE   A 1 156 ? -15.404 -10.624 -13.221 1.00 104.47 ? 176 PHE   A CD1 1 
ATOM   1171 C  CD2 . PHE   A 1 156 ? -14.612 -12.275 -14.746 1.00 102.12 ? 176 PHE   A CD2 1 
ATOM   1172 C  CE1 . PHE   A 1 156 ? -15.951 -9.912  -14.271 1.00 100.68 ? 176 PHE   A CE1 1 
ATOM   1173 C  CE2 . PHE   A 1 156 ? -15.159 -11.569 -15.799 1.00 101.30 ? 176 PHE   A CE2 1 
ATOM   1174 C  CZ  . PHE   A 1 156 ? -15.827 -10.384 -15.561 1.00 102.00 ? 176 PHE   A CZ  1 
ATOM   1175 N  N   . GLY   A 1 157 ? -12.386 -13.142 -9.668  1.00 116.12 ? 177 GLY   A N   1 
ATOM   1176 C  CA  . GLY   A 1 157 ? -12.147 -13.935 -8.474  1.00 119.65 ? 177 GLY   A CA  1 
ATOM   1177 C  C   . GLY   A 1 157 ? -12.173 -13.100 -7.208  1.00 121.04 ? 177 GLY   A C   1 
ATOM   1178 O  O   . GLY   A 1 157 ? -12.663 -13.549 -6.167  1.00 125.00 ? 177 GLY   A O   1 
ATOM   1179 N  N   . ALA   A 1 158 ? -11.640 -11.878 -7.278  1.00 121.90 ? 178 ALA   A N   1 
ATOM   1180 C  CA  . ALA   A 1 158 ? -11.737 -10.959 -6.151  1.00 120.88 ? 178 ALA   A CA  1 
ATOM   1181 C  C   . ALA   A 1 158 ? -13.190 -10.696 -5.783  1.00 119.00 ? 178 ALA   A C   1 
ATOM   1182 O  O   . ALA   A 1 158 ? -13.551 -10.692 -4.601  1.00 117.99 ? 178 ALA   A O   1 
ATOM   1183 C  CB  . ALA   A 1 158 ? -11.024 -9.650  -6.487  1.00 127.71 ? 178 ALA   A CB  1 
ATOM   1184 N  N   . TYR   A 1 159 ? -14.042 -10.490 -6.789  1.00 116.88 ? 179 TYR   A N   1 
ATOM   1185 C  CA  . TYR   A 1 159 ? -15.456 -10.235 -6.537  1.00 114.24 ? 179 TYR   A CA  1 
ATOM   1186 C  C   . TYR   A 1 159 ? -16.157 -11.478 -6.001  1.00 113.45 ? 179 TYR   A C   1 
ATOM   1187 O  O   . TYR   A 1 159 ? -16.842 -11.421 -4.973  1.00 116.29 ? 179 TYR   A O   1 
ATOM   1188 C  CB  . TYR   A 1 159 ? -16.122 -9.744  -7.823  1.00 112.52 ? 179 TYR   A CB  1 
ATOM   1189 C  CG  . TYR   A 1 159 ? -17.633 -9.816  -7.831  1.00 111.28 ? 179 TYR   A CG  1 
ATOM   1190 C  CD1 . TYR   A 1 159 ? -18.401 -8.777  -7.322  1.00 116.34 ? 179 TYR   A CD1 1 
ATOM   1191 C  CD2 . TYR   A 1 159 ? -18.291 -10.915 -8.369  1.00 111.76 ? 179 TYR   A CD2 1 
ATOM   1192 C  CE1 . TYR   A 1 159 ? -19.782 -8.838  -7.336  1.00 115.72 ? 179 TYR   A CE1 1 
ATOM   1193 C  CE2 . TYR   A 1 159 ? -19.669 -10.985 -8.386  1.00 111.51 ? 179 TYR   A CE2 1 
ATOM   1194 C  CZ  . TYR   A 1 159 ? -20.410 -9.945  -7.869  1.00 110.30 ? 179 TYR   A CZ  1 
ATOM   1195 O  OH  . TYR   A 1 159 ? -21.783 -10.012 -7.887  1.00 111.39 ? 179 TYR   A OH  1 
ATOM   1196 N  N   . SER   A 1 160 ? -15.991 -12.615 -6.685  1.00 115.41 ? 180 SER   A N   1 
ATOM   1197 C  CA  . SER   A 1 160 ? -16.733 -13.820 -6.324  1.00 116.56 ? 180 SER   A CA  1 
ATOM   1198 C  C   . SER   A 1 160 ? -16.357 -14.328 -4.938  1.00 117.06 ? 180 SER   A C   1 
ATOM   1199 O  O   . SER   A 1 160 ? -17.188 -14.937 -4.254  1.00 111.02 ? 180 SER   A O   1 
ATOM   1200 C  CB  . SER   A 1 160 ? -16.502 -14.910 -7.370  1.00 111.00 ? 180 SER   A CB  1 
ATOM   1201 O  OG  . SER   A 1 160 ? -16.926 -14.478 -8.652  1.00 107.29 ? 180 SER   A OG  1 
ATOM   1202 N  N   . MET   A 1 161 ? -15.114 -14.103 -4.510  1.00 110.77 ? 181 MET   A N   1 
ATOM   1203 C  CA  . MET   A 1 161 ? -14.748 -14.418 -3.134  1.00 112.93 ? 181 MET   A CA  1 
ATOM   1204 C  C   . MET   A 1 161 ? -15.417 -13.458 -2.159  1.00 114.51 ? 181 MET   A C   1 
ATOM   1205 O  O   . MET   A 1 161 ? -15.868 -13.869 -1.083  1.00 113.59 ? 181 MET   A O   1 
ATOM   1206 C  CB  . MET   A 1 161 ? -13.228 -14.382 -2.977  1.00 118.11 ? 181 MET   A CB  1 
ATOM   1207 C  CG  . MET   A 1 161 ? -12.748 -14.084 -1.566  1.00 129.63 ? 181 MET   A CG  1 
ATOM   1208 S  SD  . MET   A 1 161 ? -10.951 -14.020 -1.449  1.00 152.45 ? 181 MET   A SD  1 
ATOM   1209 C  CE  . MET   A 1 161 ? -10.743 -12.965 -0.018  1.00 159.79 ? 181 MET   A CE  1 
ATOM   1210 N  N   . ASP   A 1 162 ? -15.506 -12.177 -2.527  1.00 125.83 ? 182 ASP   A N   1 
ATOM   1211 C  CA  . ASP   A 1 162 ? -16.115 -11.188 -1.645  1.00 127.82 ? 182 ASP   A CA  1 
ATOM   1212 C  C   . ASP   A 1 162 ? -17.604 -11.438 -1.448  1.00 125.35 ? 182 ASP   A C   1 
ATOM   1213 O  O   . ASP   A 1 162 ? -18.161 -11.049 -0.414  1.00 128.71 ? 182 ASP   A O   1 
ATOM   1214 C  CB  . ASP   A 1 162 ? -15.898 -9.780  -2.196  1.00 133.25 ? 182 ASP   A CB  1 
ATOM   1215 C  CG  . ASP   A 1 162 ? -14.435 -9.451  -2.408  1.00 140.57 ? 182 ASP   A CG  1 
ATOM   1216 O  OD1 . ASP   A 1 162 ? -13.577 -10.051 -1.725  1.00 143.21 ? 182 ASP   A OD1 1 
ATOM   1217 O  OD2 . ASP   A 1 162 ? -14.142 -8.597  -3.270  1.00 149.67 ? 182 ASP   A OD2 1 
ATOM   1218 N  N   . VAL   A 1 163 ? -18.266 -12.072 -2.412  1.00 118.73 ? 183 VAL   A N   1 
ATOM   1219 C  CA  . VAL   A 1 163 ? -19.714 -12.241 -2.326  1.00 116.52 ? 183 VAL   A CA  1 
ATOM   1220 C  C   . VAL   A 1 163 ? -20.090 -13.530 -1.604  1.00 114.92 ? 183 VAL   A C   1 
ATOM   1221 O  O   . VAL   A 1 163 ? -21.074 -13.559 -0.861  1.00 114.52 ? 183 VAL   A O   1 
ATOM   1222 C  CB  . VAL   A 1 163 ? -20.353 -12.169 -3.731  1.00 109.33 ? 183 VAL   A CB  1 
ATOM   1223 C  CG1 . VAL   A 1 163 ? -20.008 -10.849 -4.403  1.00 110.64 ? 183 VAL   A CG1 1 
ATOM   1224 C  CG2 . VAL   A 1 163 ? -19.923 -13.341 -4.597  1.00 109.69 ? 183 VAL   A CG2 1 
ATOM   1225 N  N   . ILE   A 1 164 ? -19.325 -14.608 -1.787  1.00 112.67 ? 184 ILE   A N   1 
ATOM   1226 C  CA  . ILE   A 1 164 ? -19.691 -15.864 -1.141  1.00 111.61 ? 184 ILE   A CA  1 
ATOM   1227 C  C   . ILE   A 1 164 ? -19.224 -15.883 0.311   1.00 113.06 ? 184 ILE   A C   1 
ATOM   1228 O  O   . ILE   A 1 164 ? -19.855 -16.522 1.161   1.00 117.20 ? 184 ILE   A O   1 
ATOM   1229 C  CB  . ILE   A 1 164 ? -19.148 -17.063 -1.940  1.00 106.30 ? 184 ILE   A CB  1 
ATOM   1230 C  CG1 . ILE   A 1 164 ? -20.253 -18.102 -2.156  1.00 104.26 ? 184 ILE   A CG1 1 
ATOM   1231 C  CG2 . ILE   A 1 164 ? -17.951 -17.700 -1.247  1.00 105.00 ? 184 ILE   A CG2 1 
ATOM   1232 C  CD1 . ILE   A 1 164 ? -20.716 -18.794 -0.896  1.00 101.09 ? 184 ILE   A CD1 1 
ATOM   1233 N  N   . THR   A 1 165 ? -18.136 -15.180 0.627   1.00 118.02 ? 185 THR   A N   1 
ATOM   1234 C  CA  . THR   A 1 165 ? -17.727 -15.027 2.016   1.00 124.16 ? 185 THR   A CA  1 
ATOM   1235 C  C   . THR   A 1 165 ? -18.640 -14.085 2.787   1.00 127.74 ? 185 THR   A C   1 
ATOM   1236 O  O   . THR   A 1 165 ? -18.572 -14.054 4.020   1.00 133.50 ? 185 THR   A O   1 
ATOM   1237 C  CB  . THR   A 1 165 ? -16.285 -14.524 2.090   1.00 125.14 ? 185 THR   A CB  1 
ATOM   1238 O  OG1 . THR   A 1 165 ? -16.126 -13.406 1.207   1.00 129.81 ? 185 THR   A OG1 1 
ATOM   1239 C  CG2 . THR   A 1 165 ? -15.312 -15.625 1.689   1.00 124.74 ? 185 THR   A CG2 1 
ATOM   1240 N  N   . SER   A 1 166 ? -19.489 -13.327 2.093   1.00 125.37 ? 186 SER   A N   1 
ATOM   1241 C  CA  . SER   A 1 166 ? -20.425 -12.399 2.715   1.00 132.41 ? 186 SER   A CA  1 
ATOM   1242 C  C   . SER   A 1 166 ? -21.834 -12.965 2.830   1.00 130.37 ? 186 SER   A C   1 
ATOM   1243 O  O   . SER   A 1 166 ? -22.487 -12.778 3.861   1.00 130.45 ? 186 SER   A O   1 
ATOM   1244 C  CB  . SER   A 1 166 ? -20.468 -11.087 1.924   1.00 135.54 ? 186 SER   A CB  1 
ATOM   1245 O  OG  . SER   A 1 166 ? -19.163 -10.575 1.719   1.00 143.27 ? 186 SER   A OG  1 
ATOM   1246 N  N   . THR   A 1 167 ? -22.267 -13.700 1.801   1.00 120.37 ? 187 THR   A N   1 
ATOM   1247 C  CA  . THR   A 1 167 ? -23.609 -14.340 1.833   1.00 122.31 ? 187 THR   A CA  1 
ATOM   1248 C  C   . THR   A 1 167 ? -23.590 -15.518 2.815   1.00 127.01 ? 187 THR   A C   1 
ATOM   1249 O  O   . THR   A 1 167 ? -24.658 -15.830 3.376   1.00 128.80 ? 187 THR   A O   1 
ATOM   1250 C  CB  . THR   A 1 167 ? -24.042 -14.789 0.432   1.00 121.66 ? 187 THR   A CB  1 
ATOM   1251 O  OG1 . THR   A 1 167 ? -25.386 -15.263 0.518   1.00 131.98 ? 187 THR   A OG1 1 
ATOM   1252 C  CG2 . THR   A 1 167 ? -23.155 -15.871 -0.143  1.00 110.95 ? 187 THR   A CG2 1 
ATOM   1253 N  N   . SER   A 1 168 ? -22.424 -16.142 3.009   1.00 137.57 ? 188 SER   A N   1 
ATOM   1254 C  CA  . SER   A 1 168 ? -22.314 -17.309 3.923   1.00 138.96 ? 188 SER   A CA  1 
ATOM   1255 C  C   . SER   A 1 168 ? -21.942 -16.832 5.330   1.00 142.37 ? 188 SER   A C   1 
ATOM   1256 O  O   . SER   A 1 168 ? -22.503 -17.374 6.301   1.00 147.74 ? 188 SER   A O   1 
ATOM   1257 C  CB  . SER   A 1 168 ? -21.317 -18.310 3.404   1.00 136.69 ? 188 SER   A CB  1 
ATOM   1258 O  OG  . SER   A 1 168 ? -21.942 -19.246 2.540   1.00 126.68 ? 188 SER   A OG  1 
ATOM   1259 N  N   . PHE   A 1 169 ? -21.027 -15.863 5.427   1.00 139.05 ? 189 PHE   A N   1 
ATOM   1260 C  CA  . PHE   A 1 169 ? -20.581 -15.338 6.745   1.00 142.27 ? 189 PHE   A CA  1 
ATOM   1261 C  C   . PHE   A 1 169 ? -20.403 -13.820 6.638   1.00 147.67 ? 189 PHE   A C   1 
ATOM   1262 O  O   . PHE   A 1 169 ? -20.586 -13.279 5.545   1.00 148.56 ? 189 PHE   A O   1 
ATOM   1263 C  CB  . PHE   A 1 169 ? -19.286 -16.029 7.179   1.00 139.95 ? 189 PHE   A CB  1 
ATOM   1264 C  CG  . PHE   A 1 169 ? -18.989 -17.313 6.447   1.00 144.33 ? 189 PHE   A CG  1 
ATOM   1265 C  CD1 . PHE   A 1 169 ? -18.270 -17.305 5.263   1.00 135.03 ? 189 PHE   A CD1 1 
ATOM   1266 C  CD2 . PHE   A 1 169 ? -19.442 -18.528 6.935   1.00 150.24 ? 189 PHE   A CD2 1 
ATOM   1267 C  CE1 . PHE   A 1 169 ? -18.005 -18.486 4.587   1.00 135.47 ? 189 PHE   A CE1 1 
ATOM   1268 C  CE2 . PHE   A 1 169 ? -19.177 -19.708 6.258   1.00 145.92 ? 189 PHE   A CE2 1 
ATOM   1269 C  CZ  . PHE   A 1 169 ? -18.458 -19.685 5.087   1.00 137.61 ? 189 PHE   A CZ  1 
ATOM   1270 N  N   . GLY   A 1 170 ? -20.062 -13.153 7.742   1.00 146.45 ? 190 GLY   A N   1 
ATOM   1271 C  CA  . GLY   A 1 170 ? -19.943 -11.682 7.715   1.00 144.38 ? 190 GLY   A CA  1 
ATOM   1272 C  C   . GLY   A 1 170 ? -18.510 -11.236 7.483   1.00 151.71 ? 190 GLY   A C   1 
ATOM   1273 O  O   . GLY   A 1 170 ? -17.737 -11.231 8.461   1.00 156.31 ? 190 GLY   A O   1 
ATOM   1274 N  N   . VAL   A 1 171 ? -18.166 -10.866 6.243   1.00 162.62 ? 191 VAL   A N   1 
ATOM   1275 C  CA  . VAL   A 1 171 ? -16.793 -10.346 5.960   1.00 168.94 ? 191 VAL   A CA  1 
ATOM   1276 C  C   . VAL   A 1 171 ? -16.905 -9.635  4.605   1.00 167.87 ? 191 VAL   A C   1 
ATOM   1277 O  O   . VAL   A 1 171 ? -17.607 -10.161 3.718   1.00 168.16 ? 191 VAL   A O   1 
ATOM   1278 C  CB  . VAL   A 1 171 ? -15.727 -11.448 6.130   1.00 168.78 ? 191 VAL   A CB  1 
ATOM   1279 C  CG1 . VAL   A 1 171 ? -16.108 -12.730 5.407   1.00 160.67 ? 191 VAL   A CG1 1 
ATOM   1280 C  CG2 . VAL   A 1 171 ? -14.350 -10.972 5.696   1.00 170.27 ? 191 VAL   A CG2 1 
ATOM   1281 N  N   . ASN   A 1 172 ? -16.244 -8.482  4.458   1.00 182.77 ? 192 ASN   A N   1 
ATOM   1282 C  CA  . ASN   A 1 172 ? -16.029 -7.841  3.132   1.00 182.61 ? 192 ASN   A CA  1 
ATOM   1283 C  C   . ASN   A 1 172 ? -14.518 -7.814  2.893   1.00 183.71 ? 192 ASN   A C   1 
ATOM   1284 O  O   . ASN   A 1 172 ? -13.778 -7.808  3.896   1.00 185.98 ? 192 ASN   A O   1 
ATOM   1285 C  CB  . ASN   A 1 172 ? -16.637 -6.439  3.064   1.00 186.25 ? 192 ASN   A CB  1 
ATOM   1286 C  CG  . ASN   A 1 172 ? -15.825 -5.485  2.213   1.00 188.61 ? 192 ASN   A CG  1 
ATOM   1287 O  OD1 . ASN   A 1 172 ? -15.808 -5.598  0.989   1.00 186.74 ? 192 ASN   A OD1 1 
ATOM   1288 N  ND2 . ASN   A 1 172 ? -15.141 -4.551  2.852   1.00 193.25 ? 192 ASN   A ND2 1 
ATOM   1289 N  N   . ILE   A 1 173 ? -14.066 -7.797  1.635   1.00 177.65 ? 193 ILE   A N   1 
ATOM   1290 C  CA  . ILE   A 1 173 ? -12.593 -7.896  1.408   1.00 178.70 ? 193 ILE   A CA  1 
ATOM   1291 C  C   . ILE   A 1 173 ? -12.483 -7.099  0.105   1.00 179.63 ? 193 ILE   A C   1 
ATOM   1292 O  O   . ILE   A 1 173 ? -12.861 -7.659  -0.940  1.00 174.89 ? 193 ILE   A O   1 
ATOM   1293 C  CB  . ILE   A 1 173 ? -12.165 -9.379  1.392   1.00 176.34 ? 193 ILE   A CB  1 
ATOM   1294 C  CG1 . ILE   A 1 173 ? -13.345 -10.310 1.098   1.00 167.42 ? 193 ILE   A CG1 1 
ATOM   1295 C  CG2 . ILE   A 1 173 ? -11.459 -9.753  2.685   1.00 180.10 ? 193 ILE   A CG2 1 
ATOM   1296 C  CD1 . ILE   A 1 173 ? -13.707 -11.236 2.234   1.00 160.88 ? 193 ILE   A CD1 1 
ATOM   1297 N  N   . ASP   A 1 174 ? -11.969 -5.863  0.150   1.00 179.63 ? 194 ASP   A N   1 
ATOM   1298 C  CA  . ASP   A 1 174 ? -11.435 -5.184  -1.027  1.00 175.41 ? 194 ASP   A CA  1 
ATOM   1299 C  C   . ASP   A 1 174 ? -10.141 -5.934  -1.316  1.00 179.28 ? 194 ASP   A C   1 
ATOM   1300 O  O   . ASP   A 1 174 ? -9.124  -5.720  -0.652  1.00 181.70 ? 194 ASP   A O   1 
ATOM   1301 C  CB  . ASP   A 1 174 ? -11.214 -3.703  -0.717  1.00 171.34 ? 194 ASP   A CB  1 
ATOM   1302 C  CG  . ASP   A 1 174 ? -10.486 -2.973  -1.829  1.00 171.11 ? 194 ASP   A CG  1 
ATOM   1303 O  OD1 . ASP   A 1 174 ? -11.115 -2.700  -2.871  1.00 168.36 ? 194 ASP   A OD1 1 
ATOM   1304 O  OD2 . ASP   A 1 174 ? -9.285  -2.675  -1.661  1.00 172.91 ? 194 ASP   A OD2 1 
ATOM   1305 N  N   . SER   A 1 175 ? -10.176 -6.814  -2.316  1.00 180.44 ? 195 SER   A N   1 
ATOM   1306 C  CA  . SER   A 1 175 ? -9.048  -7.654  -2.700  1.00 179.94 ? 195 SER   A CA  1 
ATOM   1307 C  C   . SER   A 1 175 ? -8.029  -6.917  -3.591  1.00 181.35 ? 195 SER   A C   1 
ATOM   1308 O  O   . SER   A 1 175 ? -7.178  -7.572  -4.204  1.00 182.58 ? 195 SER   A O   1 
ATOM   1309 C  CB  . SER   A 1 175 ? -9.551  -8.930  -3.388  1.00 171.28 ? 195 SER   A CB  1 
ATOM   1310 O  OG  . SER   A 1 175 ? -10.374 -9.735  -2.559  1.00 166.14 ? 195 SER   A OG  1 
ATOM   1311 N  N   . LEU   A 1 176 ? -8.090  -5.585  -3.641  1.00 184.86 ? 196 LEU   A N   1 
ATOM   1312 C  CA  . LEU   A 1 176 ? -6.972  -4.824  -4.179  1.00 185.84 ? 196 LEU   A CA  1 
ATOM   1313 C  C   . LEU   A 1 176 ? -5.691  -5.125  -3.422  1.00 193.06 ? 196 LEU   A C   1 
ATOM   1314 O  O   . LEU   A 1 176 ? -4.596  -5.034  -3.990  1.00 193.22 ? 196 LEU   A O   1 
ATOM   1315 C  CB  . LEU   A 1 176 ? -7.268  -3.324  -4.138  1.00 181.42 ? 196 LEU   A CB  1 
ATOM   1316 C  CG  . LEU   A 1 176 ? -6.157  -2.302  -4.363  1.00 181.30 ? 196 LEU   A CG  1 
ATOM   1317 C  CD1 . LEU   A 1 176 ? -5.600  -2.402  -5.770  1.00 178.86 ? 196 LEU   A CD1 1 
ATOM   1318 C  CD2 . LEU   A 1 176 ? -6.663  -0.888  -4.094  1.00 175.13 ? 196 LEU   A CD2 1 
ATOM   1319 N  N   . ASN   A 1 177 ? -5.808  -5.490  -2.146  1.00 199.84 ? 197 ASN   A N   1 
ATOM   1320 C  CA  . ASN   A 1 177 ? -4.653  -5.847  -1.335  1.00 204.51 ? 197 ASN   A CA  1 
ATOM   1321 C  C   . ASN   A 1 177 ? -4.788  -7.364  -1.303  1.00 203.70 ? 197 ASN   A C   1 
ATOM   1322 O  O   . ASN   A 1 177 ? -5.441  -7.955  -2.170  1.00 200.32 ? 197 ASN   A O   1 
ATOM   1323 C  CB  . ASN   A 1 177 ? -4.874  -5.450  0.128   1.00 205.18 ? 197 ASN   A CB  1 
ATOM   1324 C  CG  . ASN   A 1 177 ? -4.922  -3.948  0.327   1.00 205.64 ? 197 ASN   A CG  1 
ATOM   1325 O  OD1 . ASN   A 1 177 ? -5.140  -3.187  -0.618  1.00 202.59 ? 197 ASN   A OD1 1 
ATOM   1326 N  ND2 . ASN   A 1 177 ? -4.715  -3.513  1.563   1.00 211.35 ? 197 ASN   A ND2 1 
ATOM   1327 N  N   . ASN   A 1 178 ? -4.107  -7.985  -0.337  1.00 206.74 ? 198 ASN   A N   1 
ATOM   1328 C  CA  . ASN   A 1 178 ? -4.038  -9.469  -0.320  1.00 210.07 ? 198 ASN   A CA  1 
ATOM   1329 C  C   . ASN   A 1 178 ? -5.209  -10.082 0.442   1.00 209.70 ? 198 ASN   A C   1 
ATOM   1330 O  O   . ASN   A 1 178 ? -5.531  -9.584  1.538   1.00 211.21 ? 198 ASN   A O   1 
ATOM   1331 C  CB  . ASN   A 1 178 ? -2.708  -9.943  0.270   1.00 211.24 ? 198 ASN   A CB  1 
ATOM   1332 C  CG  . ASN   A 1 178 ? -2.150  -8.965  1.282   1.00 211.50 ? 198 ASN   A CG  1 
ATOM   1333 O  OD1 . ASN   A 1 178 ? -1.503  -7.986  0.915   1.00 211.68 ? 198 ASN   A OD1 1 
ATOM   1334 N  ND2 . ASN   A 1 178 ? -2.408  -9.212  2.555   1.00 211.64 ? 198 ASN   A ND2 1 
ATOM   1335 N  N   . PRO   A 1 179 ? -5.857  -11.133 -0.104  1.00 197.50 ? 199 PRO   A N   1 
ATOM   1336 C  CA  . PRO   A 1 179 ? -6.914  -11.841 0.605   1.00 185.55 ? 199 PRO   A CA  1 
ATOM   1337 C  C   . PRO   A 1 179 ? -6.252  -13.029 1.312   1.00 180.49 ? 199 PRO   A C   1 
ATOM   1338 O  O   . PRO   A 1 179 ? -5.038  -13.085 1.337   1.00 183.42 ? 199 PRO   A O   1 
ATOM   1339 C  CB  . PRO   A 1 179 ? -7.685  -12.522 -0.530  1.00 181.50 ? 199 PRO   A CB  1 
ATOM   1340 C  CG  . PRO   A 1 179 ? -7.076  -11.996 -1.814  1.00 187.01 ? 199 PRO   A CG  1 
ATOM   1341 C  CD  . PRO   A 1 179 ? -5.651  -11.650 -1.449  1.00 193.74 ? 199 PRO   A CD  1 
ATOM   1342 N  N   . GLN   A 1 180 ? -7.053  -13.946 1.859   1.00 174.25 ? 200 GLN   A N   1 
ATOM   1343 C  CA  . GLN   A 1 180 ? -6.499  -15.073 2.653   1.00 164.66 ? 200 GLN   A CA  1 
ATOM   1344 C  C   . GLN   A 1 180 ? -6.893  -16.374 1.963   1.00 163.02 ? 200 GLN   A C   1 
ATOM   1345 O  O   . GLN   A 1 180 ? -6.286  -17.411 2.268   1.00 160.49 ? 200 GLN   A O   1 
ATOM   1346 C  CB  . GLN   A 1 180 ? -7.048  -15.045 4.078   1.00 155.21 ? 200 GLN   A CB  1 
ATOM   1347 C  CG  . GLN   A 1 180 ? -7.951  -13.855 4.365   1.00 149.87 ? 200 GLN   A CG  1 
ATOM   1348 C  CD  . GLN   A 1 180 ? -7.613  -13.191 5.678   1.00 141.67 ? 200 GLN   A CD  1 
ATOM   1349 O  OE1 . GLN   A 1 180 ? -8.483  -12.683 6.383   1.00 142.16 ? 200 GLN   A OE1 1 
ATOM   1350 N  NE2 . GLN   A 1 180 ? -6.335  -13.193 6.020   1.00 138.62 ? 200 GLN   A NE2 1 
ATOM   1351 N  N   . ASP   A 1 181 ? -7.876  -16.300 1.067   1.00 159.57 ? 201 ASP   A N   1 
ATOM   1352 C  CA  . ASP   A 1 181 ? -8.342  -17.504 0.329   1.00 161.31 ? 201 ASP   A CA  1 
ATOM   1353 C  C   . ASP   A 1 181 ? -7.198  -18.042 -0.533  1.00 161.93 ? 201 ASP   A C   1 
ATOM   1354 O  O   . ASP   A 1 181 ? -6.824  -17.372 -1.513  1.00 161.39 ? 201 ASP   A O   1 
ATOM   1355 C  CB  . ASP   A 1 181 ? -9.595  -17.191 -0.489  1.00 159.33 ? 201 ASP   A CB  1 
ATOM   1356 C  CG  . ASP   A 1 181 ? -10.770 -16.767 0.374   1.00 157.94 ? 201 ASP   A CG  1 
ATOM   1357 O  OD1 . ASP   A 1 181 ? -10.526 -16.253 1.485   1.00 155.62 ? 201 ASP   A OD1 1 
ATOM   1358 O  OD2 . ASP   A 1 181 ? -11.919 -16.952 -0.072  1.00 154.50 ? 201 ASP   A OD2 1 
ATOM   1359 N  N   . PRO   A 1 182 ? -6.635  -19.222 -0.208  1.00 162.37 ? 202 PRO   A N   1 
ATOM   1360 C  CA  . PRO   A 1 182 ? -5.512  -19.774 -0.946  1.00 163.39 ? 202 PRO   A CA  1 
ATOM   1361 C  C   . PRO   A 1 182 ? -5.913  -20.879 -1.932  1.00 163.08 ? 202 PRO   A C   1 
ATOM   1362 O  O   . PRO   A 1 182 ? -5.040  -21.363 -2.628  1.00 164.45 ? 202 PRO   A O   1 
ATOM   1363 C  CB  . PRO   A 1 182 ? -4.748  -20.413 0.213   1.00 169.74 ? 202 PRO   A CB  1 
ATOM   1364 C  CG  . PRO   A 1 182 ? -5.840  -21.006 1.078   1.00 167.64 ? 202 PRO   A CG  1 
ATOM   1365 C  CD  . PRO   A 1 182 ? -7.026  -20.077 0.914   1.00 163.90 ? 202 PRO   A CD  1 
ATOM   1366 N  N   . PHE   A 1 183 ? -7.199  -21.247 -1.972  1.00 157.35 ? 203 PHE   A N   1 
ATOM   1367 C  CA  . PHE   A 1 183 ? -7.671  -22.330 -2.876  1.00 149.78 ? 203 PHE   A CA  1 
ATOM   1368 C  C   . PHE   A 1 183 ? -6.570  -23.382 -3.042  1.00 146.31 ? 203 PHE   A C   1 
ATOM   1369 O  O   . PHE   A 1 183 ? -6.079  -23.514 -4.179  1.00 142.12 ? 203 PHE   A O   1 
ATOM   1370 C  CB  . PHE   A 1 183 ? -8.087  -21.771 -4.239  1.00 142.68 ? 203 PHE   A CB  1 
ATOM   1371 C  CG  . PHE   A 1 183 ? -7.370  -20.521 -4.680  1.00 141.74 ? 203 PHE   A CG  1 
ATOM   1372 C  CD1 . PHE   A 1 183 ? -7.814  -19.270 -4.283  1.00 142.73 ? 203 PHE   A CD1 1 
ATOM   1373 C  CD2 . PHE   A 1 183 ? -6.258  -20.595 -5.501  1.00 140.43 ? 203 PHE   A CD2 1 
ATOM   1374 C  CE1 . PHE   A 1 183 ? -7.156  -18.122 -4.692  1.00 140.62 ? 203 PHE   A CE1 1 
ATOM   1375 C  CE2 . PHE   A 1 183 ? -5.600  -19.446 -5.910  1.00 141.99 ? 203 PHE   A CE2 1 
ATOM   1376 C  CZ  . PHE   A 1 183 ? -6.050  -18.212 -5.505  1.00 140.99 ? 203 PHE   A CZ  1 
ATOM   1377 N  N   . PRO   A 1 198 ? -2.610  -28.859 -8.793  1.00 157.13 ? 218 PRO   A N   1 
ATOM   1378 C  CA  . PRO   A 1 198 ? -3.351  -30.116 -8.969  1.00 155.63 ? 218 PRO   A CA  1 
ATOM   1379 C  C   . PRO   A 1 198 ? -2.499  -31.234 -9.588  1.00 163.63 ? 218 PRO   A C   1 
ATOM   1380 O  O   . PRO   A 1 198 ? -1.650  -31.767 -8.896  1.00 161.71 ? 218 PRO   A O   1 
ATOM   1381 C  CB  . PRO   A 1 198 ? -4.444  -29.714 -9.961  1.00 150.63 ? 218 PRO   A CB  1 
ATOM   1382 C  CG  . PRO   A 1 198 ? -4.785  -28.304 -9.553  1.00 144.64 ? 218 PRO   A CG  1 
ATOM   1383 C  CD  . PRO   A 1 198 ? -3.468  -27.710 -9.100  1.00 149.39 ? 218 PRO   A CD  1 
ATOM   1384 N  N   . PHE   A 1 199 ? -2.754  -31.574 -10.854 1.00 167.97 ? 219 PHE   A N   1 
ATOM   1385 C  CA  . PHE   A 1 199 ? -1.957  -32.607 -11.570 1.00 169.20 ? 219 PHE   A CA  1 
ATOM   1386 C  C   . PHE   A 1 199 ? -1.622  -33.794 -10.661 1.00 165.16 ? 219 PHE   A C   1 
ATOM   1387 O  O   . PHE   A 1 199 ? -0.439  -34.171 -10.598 1.00 164.80 ? 219 PHE   A O   1 
ATOM   1388 C  CB  . PHE   A 1 199 ? -0.677  -31.997 -12.148 1.00 173.78 ? 219 PHE   A CB  1 
ATOM   1389 C  CG  . PHE   A 1 199 ? 0.072   -31.069 -11.225 1.00 173.80 ? 219 PHE   A CG  1 
ATOM   1390 C  CD1 . PHE   A 1 199 ? 1.045   -31.553 -10.367 1.00 171.66 ? 219 PHE   A CD1 1 
ATOM   1391 C  CD2 . PHE   A 1 199 ? -0.195  -29.709 -11.216 1.00 170.30 ? 219 PHE   A CD2 1 
ATOM   1392 C  CE1 . PHE   A 1 199 ? 1.731   -30.701 -9.517  1.00 174.30 ? 219 PHE   A CE1 1 
ATOM   1393 C  CE2 . PHE   A 1 199 ? 0.490   -28.858 -10.365 1.00 170.98 ? 219 PHE   A CE2 1 
ATOM   1394 C  CZ  . PHE   A 1 199 ? 1.453   -29.355 -9.518  1.00 174.25 ? 219 PHE   A CZ  1 
ATOM   1395 N  N   . PHE   A 1 200 ? -2.646  -34.408 -10.058 1.00 163.93 ? 220 PHE   A N   1 
ATOM   1396 C  CA  . PHE   A 1 200 ? -2.440  -35.641 -9.253  1.00 160.21 ? 220 PHE   A CA  1 
ATOM   1397 C  C   . PHE   A 1 200 ? -3.716  -36.486 -9.331  1.00 155.98 ? 220 PHE   A C   1 
ATOM   1398 O  O   . PHE   A 1 200 ? -4.739  -36.069 -8.754  1.00 154.61 ? 220 PHE   A O   1 
ATOM   1399 C  CB  . PHE   A 1 200 ? -2.107  -35.324 -7.795  1.00 161.17 ? 220 PHE   A CB  1 
ATOM   1400 C  CG  . PHE   A 1 200 ? -2.404  -36.466 -6.857  1.00 158.95 ? 220 PHE   A CG  1 
ATOM   1401 C  CD1 . PHE   A 1 200 ? -1.836  -37.714 -7.059  1.00 156.70 ? 220 PHE   A CD1 1 
ATOM   1402 C  CD2 . PHE   A 1 200 ? -3.272  -36.305 -5.789  1.00 156.20 ? 220 PHE   A CD2 1 
ATOM   1403 C  CE1 . PHE   A 1 200 ? -2.117  -38.770 -6.208  1.00 157.05 ? 220 PHE   A CE1 1 
ATOM   1404 C  CE2 . PHE   A 1 200 ? -3.551  -37.361 -4.937  1.00 152.10 ? 220 PHE   A CE2 1 
ATOM   1405 C  CZ  . PHE   A 1 200 ? -2.973  -38.591 -5.147  1.00 155.30 ? 220 PHE   A CZ  1 
ATOM   1406 N  N   . LEU   A 1 201 ? -3.660  -37.630 -10.021 1.00 162.05 ? 221 LEU   A N   1 
ATOM   1407 C  CA  . LEU   A 1 201 ? -4.877  -38.469 -10.199 1.00 155.67 ? 221 LEU   A CA  1 
ATOM   1408 C  C   . LEU   A 1 201 ? -4.481  -39.939 -10.370 1.00 156.80 ? 221 LEU   A C   1 
ATOM   1409 O  O   . LEU   A 1 201 ? -5.308  -40.712 -10.891 1.00 162.82 ? 221 LEU   A O   1 
ATOM   1410 C  CB  . LEU   A 1 201 ? -5.650  -37.968 -11.423 1.00 143.17 ? 221 LEU   A CB  1 
ATOM   1411 C  CG  . LEU   A 1 201 ? -7.121  -37.640 -11.176 1.00 135.74 ? 221 LEU   A CG  1 
ATOM   1412 C  CD1 . LEU   A 1 201 ? -7.688  -38.501 -10.057 1.00 136.82 ? 221 LEU   A CD1 1 
ATOM   1413 C  CD2 . LEU   A 1 201 ? -7.298  -36.165 -10.853 1.00 132.67 ? 221 LEU   A CD2 1 
ATOM   1414 N  N   . SER   A 1 202 ? -3.270  -40.309 -9.945  1.00 155.29 ? 222 SER   A N   1 
ATOM   1415 C  CA  . SER   A 1 202 ? -2.835  -41.729 -10.016 1.00 156.61 ? 222 SER   A CA  1 
ATOM   1416 C  C   . SER   A 1 202 ? -3.960  -42.629 -9.498  1.00 164.87 ? 222 SER   A C   1 
ATOM   1417 O  O   . SER   A 1 202 ? -4.149  -43.725 -10.057 1.00 164.53 ? 222 SER   A O   1 
ATOM   1418 C  CB  . SER   A 1 202 ? -1.572  -41.939 -9.231  1.00 158.14 ? 222 SER   A CB  1 
ATOM   1419 O  OG  . SER   A 1 202 ? -1.781  -41.632 -7.860  1.00 156.49 ? 222 SER   A OG  1 
ATOM   1420 N  N   . ILE   A 1 203 ? -4.670  -42.175 -8.462  1.00 147.81 ? 223 ILE   A N   1 
ATOM   1421 C  CA  . ILE   A 1 203 ? -5.791  -42.969 -7.879  1.00 149.62 ? 223 ILE   A CA  1 
ATOM   1422 C  C   . ILE   A 1 203 ? -6.715  -43.439 -9.005  1.00 148.14 ? 223 ILE   A C   1 
ATOM   1423 O  O   . ILE   A 1 203 ? -7.114  -44.611 -8.980  1.00 151.73 ? 223 ILE   A O   1 
ATOM   1424 C  CB  . ILE   A 1 203 ? -6.552  -42.137 -6.828  1.00 147.96 ? 223 ILE   A CB  1 
ATOM   1425 C  CG1 . ILE   A 1 203 ? -6.856  -40.725 -7.335  1.00 143.69 ? 223 ILE   A CG1 1 
ATOM   1426 C  CG2 . ILE   A 1 203 ? -5.794  -42.114 -5.511  1.00 149.17 ? 223 ILE   A CG2 1 
ATOM   1427 C  CD1 . ILE   A 1 203 ? -5.872  -39.676 -6.870  1.00 140.89 ? 223 ILE   A CD1 1 
ATOM   1428 N  N   . THR   A 1 204 ? -7.049  -42.564 -9.957  1.00 144.74 ? 224 THR   A N   1 
ATOM   1429 C  CA  . THR   A 1 204 ? -8.007  -42.976 -10.984 1.00 136.85 ? 224 THR   A CA  1 
ATOM   1430 C  C   . THR   A 1 204 ? -7.567  -44.282 -11.629 1.00 134.90 ? 224 THR   A C   1 
ATOM   1431 O  O   . THR   A 1 204 ? -8.395  -45.131 -11.983 1.00 126.96 ? 224 THR   A O   1 
ATOM   1432 C  CB  . THR   A 1 204 ? -8.158  -41.874 -12.037 1.00 128.17 ? 224 THR   A CB  1 
ATOM   1433 O  OG1 . THR   A 1 204 ? -9.217  -40.988 -11.658 1.00 122.57 ? 224 THR   A OG1 1 
ATOM   1434 C  CG2 . THR   A 1 204 ? -8.457  -42.452 -13.413 1.00 117.94 ? 224 THR   A CG2 1 
ATOM   1435 N  N   . VAL   A 1 205 ? -6.258  -44.467 -11.760 1.00 137.88 ? 225 VAL   A N   1 
ATOM   1436 C  CA  . VAL   A 1 205 ? -5.727  -45.753 -12.182 1.00 140.74 ? 225 VAL   A CA  1 
ATOM   1437 C  C   . VAL   A 1 205 ? -5.729  -46.741 -11.021 1.00 147.16 ? 225 VAL   A C   1 
ATOM   1438 O  O   . VAL   A 1 205 ? -6.162  -47.889 -11.165 1.00 145.68 ? 225 VAL   A O   1 
ATOM   1439 C  CB  . VAL   A 1 205 ? -4.316  -45.572 -12.772 1.00 140.18 ? 225 VAL   A CB  1 
ATOM   1440 C  CG1 . VAL   A 1 205 ? -4.067  -46.612 -13.855 1.00 128.03 ? 225 VAL   A CG1 1 
ATOM   1441 C  CG2 . VAL   A 1 205 ? -4.145  -44.154 -13.312 1.00 137.52 ? 225 VAL   A CG2 1 
ATOM   1442 N  N   . PHE   A 1 206 ? -5.256  -46.309 -9.854  1.00 161.38 ? 226 PHE   A N   1 
ATOM   1443 C  CA  . PHE   A 1 206 ? -5.002  -47.194 -8.719  1.00 161.98 ? 226 PHE   A CA  1 
ATOM   1444 C  C   . PHE   A 1 206 ? -5.645  -46.590 -7.476  1.00 166.38 ? 226 PHE   A C   1 
ATOM   1445 O  O   . PHE   A 1 206 ? -4.972  -45.972 -6.644  1.00 166.62 ? 226 PHE   A O   1 
ATOM   1446 C  CB  . PHE   A 1 206 ? -3.496  -47.402 -8.533  1.00 159.67 ? 226 PHE   A CB  1 
ATOM   1447 C  CG  . PHE   A 1 206 ? -2.776  -47.783 -9.798  1.00 165.18 ? 226 PHE   A CG  1 
ATOM   1448 C  CD1 . PHE   A 1 206 ? -3.089  -48.961 -10.455 1.00 172.71 ? 226 PHE   A CD1 1 
ATOM   1449 C  CD2 . PHE   A 1 206 ? -1.805  -46.959 -10.344 1.00 166.05 ? 226 PHE   A CD2 1 
ATOM   1450 C  CE1 . PHE   A 1 206 ? -2.446  -49.316 -11.627 1.00 169.29 ? 226 PHE   A CE1 1 
ATOM   1451 C  CE2 . PHE   A 1 206 ? -1.154  -47.310 -11.520 1.00 171.92 ? 226 PHE   A CE2 1 
ATOM   1452 C  CZ  . PHE   A 1 206 ? -1.477  -48.490 -12.161 1.00 170.70 ? 226 PHE   A CZ  1 
ATOM   1453 N  N   . PRO   A 1 207 ? -6.961  -46.738 -7.321  1.00 166.79 ? 227 PRO   A N   1 
ATOM   1454 C  CA  . PRO   A 1 207 ? -7.636  -46.027 -6.224  1.00 166.44 ? 227 PRO   A CA  1 
ATOM   1455 C  C   . PRO   A 1 207 ? -7.637  -46.814 -4.929  1.00 164.51 ? 227 PRO   A C   1 
ATOM   1456 O  O   . PRO   A 1 207 ? -8.072  -46.311 -3.887  1.00 164.09 ? 227 PRO   A O   1 
ATOM   1457 C  CB  . PRO   A 1 207 ? -9.064  -45.837 -6.754  1.00 162.18 ? 227 PRO   A CB  1 
ATOM   1458 C  CG  . PRO   A 1 207 ? -9.274  -47.020 -7.649  1.00 165.45 ? 227 PRO   A CG  1 
ATOM   1459 C  CD  . PRO   A 1 207 ? -7.922  -47.479 -8.165  1.00 170.33 ? 227 PRO   A CD  1 
ATOM   1460 N  N   . PHE   A 1 208 ? -7.211  -48.076 -5.011  1.00 151.00 ? 228 PHE   A N   1 
ATOM   1461 C  CA  . PHE   A 1 208 ? -7.250  -49.022 -3.899  1.00 145.96 ? 228 PHE   A CA  1 
ATOM   1462 C  C   . PHE   A 1 208 ? -6.303  -48.551 -2.805  1.00 140.72 ? 228 PHE   A C   1 
ATOM   1463 O  O   . PHE   A 1 208 ? -6.280  -49.073 -1.680  1.00 136.68 ? 228 PHE   A O   1 
ATOM   1464 C  CB  . PHE   A 1 208 ? -6.857  -50.422 -4.400  1.00 144.32 ? 228 PHE   A CB  1 
ATOM   1465 C  CG  . PHE   A 1 208 ? -5.542  -50.460 -5.123  1.00 146.52 ? 228 PHE   A CG  1 
ATOM   1466 C  CD1 . PHE   A 1 208 ? -4.367  -50.652 -4.426  1.00 143.71 ? 228 PHE   A CD1 1 
ATOM   1467 C  CD2 . PHE   A 1 208 ? -5.483  -50.312 -6.499  1.00 147.48 ? 228 PHE   A CD2 1 
ATOM   1468 C  CE1 . PHE   A 1 208 ? -3.154  -50.703 -5.075  1.00 144.51 ? 228 PHE   A CE1 1 
ATOM   1469 C  CE2 . PHE   A 1 208 ? -4.263  -50.361 -7.160  1.00 148.77 ? 228 PHE   A CE2 1 
ATOM   1470 C  CZ  . PHE   A 1 208 ? -3.097  -50.554 -6.443  1.00 146.75 ? 228 PHE   A CZ  1 
ATOM   1471 N  N   . LEU   A 1 209 ? -5.494  -47.567 -3.174  1.00 143.77 ? 229 LEU   A N   1 
ATOM   1472 C  CA  . LEU   A 1 209 ? -4.586  -46.873 -2.282  1.00 142.15 ? 229 LEU   A CA  1 
ATOM   1473 C  C   . LEU   A 1 209 ? -5.249  -45.726 -1.524  1.00 143.50 ? 229 LEU   A C   1 
ATOM   1474 O  O   . LEU   A 1 209 ? -4.609  -45.139 -0.645  1.00 140.78 ? 229 LEU   A O   1 
ATOM   1475 C  CB  . LEU   A 1 209 ? -3.386  -46.346 -3.080  1.00 142.71 ? 229 LEU   A CB  1 
ATOM   1476 C  CG  . LEU   A 1 209 ? -2.577  -47.416 -3.816  1.00 143.52 ? 229 LEU   A CG  1 
ATOM   1477 C  CD1 . LEU   A 1 209 ? -1.630  -46.782 -4.808  1.00 144.24 ? 229 LEU   A CD1 1 
ATOM   1478 C  CD2 . LEU   A 1 209 ? -1.809  -48.287 -2.841  1.00 143.36 ? 229 LEU   A CD2 1 
ATOM   1479 N  N   . ILE   A 1 210 ? -6.505  -45.387 -1.833  1.00 134.04 ? 230 ILE   A N   1 
ATOM   1480 C  CA  . ILE   A 1 210 ? -7.213  -44.379 -1.039  1.00 132.66 ? 230 ILE   A CA  1 
ATOM   1481 C  C   . ILE   A 1 210 ? -7.408  -44.828 0.408   1.00 136.00 ? 230 ILE   A C   1 
ATOM   1482 O  O   . ILE   A 1 210 ? -7.100  -44.039 1.317   1.00 137.53 ? 230 ILE   A O   1 
ATOM   1483 C  CB  . ILE   A 1 210 ? -8.533  -43.986 -1.724  1.00 128.70 ? 230 ILE   A CB  1 
ATOM   1484 C  CG1 . ILE   A 1 210 ? -8.256  -43.115 -2.951  1.00 126.88 ? 230 ILE   A CG1 1 
ATOM   1485 C  CG2 . ILE   A 1 210 ? -9.445  -43.247 -0.745  1.00 121.72 ? 230 ILE   A CG2 1 
ATOM   1486 C  CD1 . ILE   A 1 210 ? -9.502  -42.616 -3.653  1.00 123.26 ? 230 ILE   A CD1 1 
ATOM   1487 N  N   . PRO   A 1 211 ? -7.899  -46.039 0.697   1.00 136.92 ? 231 PRO   A N   1 
ATOM   1488 C  CA  . PRO   A 1 211 ? -7.978  -46.464 2.106   1.00 136.23 ? 231 PRO   A CA  1 
ATOM   1489 C  C   . PRO   A 1 211 ? -6.627  -46.521 2.801   1.00 137.50 ? 231 PRO   A C   1 
ATOM   1490 O  O   . PRO   A 1 211 ? -6.582  -46.473 4.037   1.00 136.42 ? 231 PRO   A O   1 
ATOM   1491 C  CB  . PRO   A 1 211 ? -8.628  -47.852 2.021   1.00 132.65 ? 231 PRO   A CB  1 
ATOM   1492 C  CG  . PRO   A 1 211 ? -9.366  -47.845 0.735   1.00 129.81 ? 231 PRO   A CG  1 
ATOM   1493 C  CD  . PRO   A 1 211 ? -8.513  -47.042 -0.195  1.00 134.01 ? 231 PRO   A CD  1 
ATOM   1494 N  N   . ILE   A 1 212 ? -5.526  -46.625 2.051   1.00 145.05 ? 232 ILE   A N   1 
ATOM   1495 C  CA  . ILE   A 1 212 ? -4.201  -46.495 2.654   1.00 145.49 ? 232 ILE   A CA  1 
ATOM   1496 C  C   . ILE   A 1 212 ? -4.021  -45.098 3.228   1.00 147.41 ? 232 ILE   A C   1 
ATOM   1497 O  O   . ILE   A 1 212 ? -3.565  -44.923 4.364   1.00 148.75 ? 232 ILE   A O   1 
ATOM   1498 C  CB  . ILE   A 1 212 ? -3.102  -46.817 1.625   1.00 149.60 ? 232 ILE   A CB  1 
ATOM   1499 C  CG1 . ILE   A 1 212 ? -2.850  -48.321 1.548   1.00 151.05 ? 232 ILE   A CG1 1 
ATOM   1500 C  CG2 . ILE   A 1 212 ? -1.812  -46.064 1.955   1.00 152.35 ? 232 ILE   A CG2 1 
ATOM   1501 C  CD1 . ILE   A 1 212 ? -1.471  -48.664 1.053   1.00 154.97 ? 232 ILE   A CD1 1 
ATOM   1502 N  N   . LEU   A 1 213 ? -4.380  -44.082 2.447   1.00 148.75 ? 233 LEU   A N   1 
ATOM   1503 C  CA  . LEU   A 1 213 ? -4.164  -42.704 2.857   1.00 146.53 ? 233 LEU   A CA  1 
ATOM   1504 C  C   . LEU   A 1 213 ? -5.217  -42.214 3.842   1.00 147.90 ? 233 LEU   A C   1 
ATOM   1505 O  O   . LEU   A 1 213 ? -4.958  -41.253 4.576   1.00 150.38 ? 233 LEU   A O   1 
ATOM   1506 C  CB  . LEU   A 1 213 ? -4.126  -41.809 1.620   1.00 140.95 ? 233 LEU   A CB  1 
ATOM   1507 C  CG  . LEU   A 1 213 ? -3.224  -42.332 0.497   1.00 137.31 ? 233 LEU   A CG  1 
ATOM   1508 C  CD1 . LEU   A 1 213 ? -3.343  -41.470 -0.748  1.00 131.58 ? 233 LEU   A CD1 1 
ATOM   1509 C  CD2 . LEU   A 1 213 ? -1.779  -42.409 0.960   1.00 140.87 ? 233 LEU   A CD2 1 
ATOM   1510 N  N   . GLU   A 1 214 ? -6.391  -42.850 3.878   1.00 134.38 ? 234 GLU   A N   1 
ATOM   1511 C  CA  . GLU   A 1 214 ? -7.379  -42.547 4.907   1.00 134.18 ? 234 GLU   A CA  1 
ATOM   1512 C  C   . GLU   A 1 214 ? -6.899  -42.932 6.300   1.00 139.76 ? 234 GLU   A C   1 
ATOM   1513 O  O   . GLU   A 1 214 ? -7.477  -42.465 7.288   1.00 145.84 ? 234 GLU   A O   1 
ATOM   1514 C  CB  . GLU   A 1 214 ? -8.702  -43.256 4.601   1.00 133.22 ? 234 GLU   A CB  1 
ATOM   1515 C  CG  . GLU   A 1 214 ? -9.329  -42.889 3.260   1.00 131.44 ? 234 GLU   A CG  1 
ATOM   1516 C  CD  . GLU   A 1 214 ? -10.064 -41.560 3.285   1.00 128.18 ? 234 GLU   A CD  1 
ATOM   1517 O  OE1 . GLU   A 1 214 ? -10.150 -40.940 4.366   1.00 129.54 ? 234 GLU   A OE1 1 
ATOM   1518 O  OE2 . GLU   A 1 214 ? -10.562 -41.135 2.220   1.00 123.61 ? 234 GLU   A OE2 1 
ATOM   1519 N  N   . VAL   A 1 215 ? -5.872  -43.774 6.400   1.00 150.67 ? 235 VAL   A N   1 
ATOM   1520 C  CA  . VAL   A 1 215 ? -5.223  -44.071 7.673   1.00 153.89 ? 235 VAL   A CA  1 
ATOM   1521 C  C   . VAL   A 1 215 ? -3.796  -43.554 7.729   1.00 158.90 ? 235 VAL   A C   1 
ATOM   1522 O  O   . VAL   A 1 215 ? -3.206  -43.529 8.822   1.00 159.49 ? 235 VAL   A O   1 
ATOM   1523 C  CB  . VAL   A 1 215 ? -5.244  -45.582 7.984   1.00 147.12 ? 235 VAL   A CB  1 
ATOM   1524 C  CG1 . VAL   A 1 215 ? -6.634  -46.154 7.760   1.00 143.17 ? 235 VAL   A CG1 1 
ATOM   1525 C  CG2 . VAL   A 1 215 ? -4.215  -46.301 7.140   1.00 146.94 ? 235 VAL   A CG2 1 
ATOM   1526 N  N   . LEU   A 1 216 ? -3.218  -43.151 6.596   1.00 166.78 ? 236 LEU   A N   1 
ATOM   1527 C  CA  . LEU   A 1 216 ? -1.915  -42.500 6.558   1.00 168.72 ? 236 LEU   A CA  1 
ATOM   1528 C  C   . LEU   A 1 216 ? -1.991  -41.024 6.930   1.00 172.63 ? 236 LEU   A C   1 
ATOM   1529 O  O   . LEU   A 1 216 ? -0.992  -40.310 6.787   1.00 176.87 ? 236 LEU   A O   1 
ATOM   1530 C  CB  . LEU   A 1 216 ? -1.290  -42.657 5.167   1.00 169.26 ? 236 LEU   A CB  1 
ATOM   1531 C  CG  . LEU   A 1 216 ? 0.106   -43.279 5.056   1.00 171.73 ? 236 LEU   A CG  1 
ATOM   1532 C  CD1 . LEU   A 1 216 ? 0.449   -43.561 3.601   1.00 166.08 ? 236 LEU   A CD1 1 
ATOM   1533 C  CD2 . LEU   A 1 216 ? 1.160   -42.383 5.686   1.00 165.26 ? 236 LEU   A CD2 1 
ATOM   1534 N  N   . ASN   A 1 217 ? -3.154  -40.560 7.394   1.00 165.52 ? 237 ASN   A N   1 
ATOM   1535 C  CA  . ASN   A 1 217 ? -3.379  -39.171 7.797   1.00 168.64 ? 237 ASN   A CA  1 
ATOM   1536 C  C   . ASN   A 1 217 ? -3.177  -38.111 6.709   1.00 167.87 ? 237 ASN   A C   1 
ATOM   1537 O  O   . ASN   A 1 217 ? -2.350  -37.203 6.816   1.00 167.55 ? 237 ASN   A O   1 
ATOM   1538 C  CB  . ASN   A 1 217 ? -2.554  -38.822 9.041   1.00 171.88 ? 237 ASN   A CB  1 
ATOM   1539 C  CG  . ASN   A 1 217 ? -3.041  -39.540 10.285  1.00 172.90 ? 237 ASN   A CG  1 
ATOM   1540 O  OD1 . ASN   A 1 217 ? -3.907  -39.042 11.004  1.00 176.62 ? 237 ASN   A OD1 1 
ATOM   1541 N  ND2 . ASN   A 1 217 ? -2.484  -40.718 10.546  1.00 169.15 ? 237 ASN   A ND2 1 
ATOM   1542 N  N   . ILE   A 1 218 ? -3.966  -38.260 5.648   1.00 156.25 ? 238 ILE   A N   1 
ATOM   1543 C  CA  . ILE   A 1 218 ? -3.870  -37.424 4.457   1.00 149.57 ? 238 ILE   A CA  1 
ATOM   1544 C  C   . ILE   A 1 218 ? -5.182  -36.671 4.293   1.00 141.87 ? 238 ILE   A C   1 
ATOM   1545 O  O   . ILE   A 1 218 ? -6.261  -37.261 4.417   1.00 137.12 ? 238 ILE   A O   1 
ATOM   1546 C  CB  . ILE   A 1 218 ? -3.563  -38.251 3.194   1.00 145.11 ? 238 ILE   A CB  1 
ATOM   1547 C  CG1 . ILE   A 1 218 ? -2.416  -39.231 3.455   1.00 145.81 ? 238 ILE   A CG1 1 
ATOM   1548 C  CG2 . ILE   A 1 218 ? -3.210  -37.333 2.035   1.00 140.29 ? 238 ILE   A CG2 1 
ATOM   1549 C  CD1 . ILE   A 1 218 ? -1.085  -38.564 3.715   1.00 152.95 ? 238 ILE   A CD1 1 
ATOM   1550 N  N   . CYS   A 1 219 ? -5.089  -35.373 4.018   1.00 142.35 ? 239 CYS   A N   1 
ATOM   1551 C  CA  . CYS   A 1 219 ? -6.270  -34.547 3.797   1.00 137.64 ? 239 CYS   A CA  1 
ATOM   1552 C  C   . CYS   A 1 219 ? -6.330  -34.059 2.353   1.00 130.29 ? 239 CYS   A C   1 
ATOM   1553 O  O   . CYS   A 1 219 ? -5.936  -32.932 2.051   1.00 126.13 ? 239 CYS   A O   1 
ATOM   1554 C  CB  . CYS   A 1 219 ? -6.283  -33.354 4.757   1.00 141.06 ? 239 CYS   A CB  1 
ATOM   1555 S  SG  . CYS   A 1 219 ? -6.462  -33.795 6.502   1.00 150.66 ? 239 CYS   A SG  1 
ATOM   1556 N  N   . THR   A 1 226 ? -6.934  -29.362 4.462   1.00 164.33 ? 246 THR   A N   1 
ATOM   1557 C  CA  . THR   A 1 226 ? -6.848  -27.932 4.858   1.00 170.66 ? 246 THR   A CA  1 
ATOM   1558 C  C   . THR   A 1 226 ? -6.406  -27.823 6.317   1.00 179.29 ? 246 THR   A C   1 
ATOM   1559 O  O   . THR   A 1 226 ? -6.642  -28.783 7.071   1.00 181.73 ? 246 THR   A O   1 
ATOM   1560 C  CB  . THR   A 1 226 ? -8.195  -27.221 4.690   1.00 167.63 ? 246 THR   A CB  1 
ATOM   1561 O  OG1 . THR   A 1 226 ? -8.102  -25.939 5.313   1.00 171.02 ? 246 THR   A OG1 1 
ATOM   1562 C  CG2 . THR   A 1 226 ? -9.340  -27.998 5.300   1.00 165.90 ? 246 THR   A CG2 1 
ATOM   1563 N  N   . ASN   A 1 227 ? -5.793  -26.698 6.693   1.00 179.28 ? 247 ASN   A N   1 
ATOM   1564 C  CA  . ASN   A 1 227 ? -5.407  -26.477 8.111   1.00 182.33 ? 247 ASN   A CA  1 
ATOM   1565 C  C   . ASN   A 1 227 ? -5.689  -25.015 8.461   1.00 184.49 ? 247 ASN   A C   1 
ATOM   1566 O  O   . ASN   A 1 227 ? -6.526  -24.773 9.350   1.00 184.08 ? 247 ASN   A O   1 
ATOM   1567 C  CB  . ASN   A 1 227 ? -3.953  -26.862 8.388   1.00 183.69 ? 247 ASN   A CB  1 
ATOM   1568 C  CG  . ASN   A 1 227 ? -3.683  -27.061 9.864   1.00 183.70 ? 247 ASN   A CG  1 
ATOM   1569 O  OD1 . ASN   A 1 227 ? -4.606  -27.044 10.676  1.00 187.37 ? 247 ASN   A OD1 1 
ATOM   1570 N  ND2 . ASN   A 1 227 ? -2.424  -27.250 10.221  1.00 186.12 ? 247 ASN   A ND2 1 
ATOM   1571 N  N   . PHE   A 1 228 ? -5.016  -24.081 7.784   1.00 177.51 ? 248 PHE   A N   1 
ATOM   1572 C  CA  . PHE   A 1 228 ? -5.327  -22.648 8.014   1.00 171.32 ? 248 PHE   A CA  1 
ATOM   1573 C  C   . PHE   A 1 228 ? -6.849  -22.494 8.000   1.00 171.99 ? 248 PHE   A C   1 
ATOM   1574 O  O   . PHE   A 1 228 ? -7.416  -22.016 9.000   1.00 175.16 ? 248 PHE   A O   1 
ATOM   1575 C  CB  . PHE   A 1 228 ? -4.674  -21.764 6.948   1.00 165.65 ? 248 PHE   A CB  1 
ATOM   1576 C  CG  . PHE   A 1 228 ? -5.598  -20.740 6.338   1.00 162.07 ? 248 PHE   A CG  1 
ATOM   1577 C  CD1 . PHE   A 1 228 ? -6.040  -19.654 7.076   1.00 162.03 ? 248 PHE   A CD1 1 
ATOM   1578 C  CD2 . PHE   A 1 228 ? -6.039  -20.872 5.032   1.00 161.48 ? 248 PHE   A CD2 1 
ATOM   1579 C  CE1 . PHE   A 1 228 ? -6.900  -18.720 6.520   1.00 159.09 ? 248 PHE   A CE1 1 
ATOM   1580 C  CE2 . PHE   A 1 228 ? -6.896  -19.936 4.476   1.00 159.55 ? 248 PHE   A CE2 1 
ATOM   1581 C  CZ  . PHE   A 1 228 ? -7.325  -18.864 5.221   1.00 158.07 ? 248 PHE   A CZ  1 
ATOM   1582 N  N   . LEU   A 1 229 ? -7.485  -22.907 6.900   1.00 173.33 ? 249 LEU   A N   1 
ATOM   1583 C  CA  . LEU   A 1 229 ? -8.929  -22.762 6.796   1.00 171.89 ? 249 LEU   A CA  1 
ATOM   1584 C  C   . LEU   A 1 229 ? -9.682  -23.814 7.597   1.00 176.56 ? 249 LEU   A C   1 
ATOM   1585 O  O   . LEU   A 1 229 ? -10.866 -23.614 7.894   1.00 175.14 ? 249 LEU   A O   1 
ATOM   1586 C  CB  . LEU   A 1 229 ? -9.377  -22.828 5.334   1.00 164.76 ? 249 LEU   A CB  1 
ATOM   1587 C  CG  . LEU   A 1 229 ? -9.982  -21.560 4.725   1.00 161.23 ? 249 LEU   A CG  1 
ATOM   1588 C  CD1 . LEU   A 1 229 ? -11.180 -21.914 3.855   1.00 149.07 ? 249 LEU   A CD1 1 
ATOM   1589 C  CD2 . LEU   A 1 229 ? -10.368 -20.536 5.788   1.00 163.28 ? 249 LEU   A CD2 1 
ATOM   1590 N  N   . ARG   A 1 230 ? -9.031  -24.920 7.963   1.00 181.02 ? 250 ARG   A N   1 
ATOM   1591 C  CA  . ARG   A 1 230 ? -9.719  -25.952 8.730   1.00 181.97 ? 250 ARG   A CA  1 
ATOM   1592 C  C   . ARG   A 1 230 ? -10.117 -25.474 10.119  1.00 185.92 ? 250 ARG   A C   1 
ATOM   1593 O  O   . ARG   A 1 230 ? -10.932 -26.135 10.774  1.00 188.79 ? 250 ARG   A O   1 
ATOM   1594 C  CB  . ARG   A 1 230 ? -8.846  -27.207 8.841   1.00 185.04 ? 250 ARG   A CB  1 
ATOM   1595 C  CG  . ARG   A 1 230 ? -8.032  -27.265 10.114  1.00 187.37 ? 250 ARG   A CG  1 
ATOM   1596 C  CD  . ARG   A 1 230 ? -8.149  -28.608 10.814  1.00 188.76 ? 250 ARG   A CD  1 
ATOM   1597 N  NE  . ARG   A 1 230 ? -7.942  -29.727 9.903   1.00 188.43 ? 250 ARG   A NE  1 
ATOM   1598 C  CZ  . ARG   A 1 230 ? -6.753  -30.179 9.527   1.00 186.63 ? 250 ARG   A CZ  1 
ATOM   1599 N  NH1 . ARG   A 1 230 ? -5.633  -29.621 9.955   1.00 189.93 ? 250 ARG   A NH1 1 
ATOM   1600 N  NH2 . ARG   A 1 230 ? -6.688  -31.213 8.693   1.00 179.66 ? 250 ARG   A NH2 1 
ATOM   1601 N  N   . LYS   A 1 231 ? -9.584  -24.342 10.575  1.00 192.73 ? 251 LYS   A N   1 
ATOM   1602 C  CA  . LYS   A 1 231 ? -10.024 -23.776 11.842  1.00 196.20 ? 251 LYS   A CA  1 
ATOM   1603 C  C   . LYS   A 1 231 ? -10.370 -22.294 11.724  1.00 196.29 ? 251 LYS   A C   1 
ATOM   1604 O  O   . LYS   A 1 231 ? -11.143 -21.778 12.537  1.00 199.48 ? 251 LYS   A O   1 
ATOM   1605 C  CB  . LYS   A 1 231 ? -8.966  -23.989 12.928  1.00 201.48 ? 251 LYS   A CB  1 
ATOM   1606 C  CG  . LYS   A 1 231 ? -7.555  -24.221 12.415  1.00 199.83 ? 251 LYS   A CG  1 
ATOM   1607 C  CD  . LYS   A 1 231 ? -6.958  -25.472 13.047  1.00 194.18 ? 251 LYS   A CD  1 
ATOM   1608 C  CE  . LYS   A 1 231 ? -7.211  -25.512 14.544  1.00 195.32 ? 251 LYS   A CE  1 
ATOM   1609 N  NZ  . LYS   A 1 231 ? -6.591  -24.359 15.243  1.00 194.34 ? 251 LYS   A NZ  1 
ATOM   1610 N  N   . SER   A 1 232 ? -9.800  -21.598 10.733  1.00 192.90 ? 252 SER   A N   1 
ATOM   1611 C  CA  . SER   A 1 232 ? -10.183 -20.210 10.478  1.00 186.47 ? 252 SER   A CA  1 
ATOM   1612 C  C   . SER   A 1 232 ? -11.685 -20.085 10.272  1.00 190.00 ? 252 SER   A C   1 
ATOM   1613 O  O   . SER   A 1 232 ? -12.310 -19.117 10.724  1.00 186.81 ? 252 SER   A O   1 
ATOM   1614 C  CB  . SER   A 1 232 ? -9.443  -19.675 9.253   1.00 174.89 ? 252 SER   A CB  1 
ATOM   1615 O  OG  . SER   A 1 232 ? -10.021 -18.464 8.796   1.00 163.38 ? 252 SER   A OG  1 
ATOM   1616 N  N   . VAL   A 1 233 ? -12.275 -21.046 9.563   1.00 183.42 ? 253 VAL   A N   1 
ATOM   1617 C  CA  . VAL   A 1 233 ? -13.728 -21.127 9.475   1.00 179.82 ? 253 VAL   A CA  1 
ATOM   1618 C  C   . VAL   A 1 233 ? -14.311 -21.528 10.823  1.00 179.63 ? 253 VAL   A C   1 
ATOM   1619 O  O   . VAL   A 1 233 ? -15.272 -20.922 11.312  1.00 182.17 ? 253 VAL   A O   1 
ATOM   1620 C  CB  . VAL   A 1 233 ? -14.145 -22.114 8.371   1.00 168.47 ? 253 VAL   A CB  1 
ATOM   1621 C  CG1 . VAL   A 1 233 ? -15.653 -22.299 8.373   1.00 161.46 ? 253 VAL   A CG1 1 
ATOM   1622 C  CG2 . VAL   A 1 233 ? -13.652 -21.637 7.011   1.00 165.50 ? 253 VAL   A CG2 1 
ATOM   1623 N  N   . LYS   A 1 234 ? -13.717 -22.546 11.451  1.00 179.63 ? 254 LYS   A N   1 
ATOM   1624 C  CA  . LYS   A 1 234 ? -14.209 -23.118 12.702  1.00 183.83 ? 254 LYS   A CA  1 
ATOM   1625 C  C   . LYS   A 1 234 ? -14.392 -22.058 13.778  1.00 184.92 ? 254 LYS   A C   1 
ATOM   1626 O  O   . LYS   A 1 234 ? -15.274 -22.188 14.639  1.00 184.24 ? 254 LYS   A O   1 
ATOM   1627 C  CB  . LYS   A 1 234 ? -13.252 -24.212 13.203  1.00 184.95 ? 254 LYS   A CB  1 
ATOM   1628 C  CG  . LYS   A 1 234 ? -12.764 -24.017 14.643  1.00 185.51 ? 254 LYS   A CG  1 
ATOM   1629 C  CD  . LYS   A 1 234 ? -11.690 -25.019 15.056  1.00 182.87 ? 254 LYS   A CD  1 
ATOM   1630 C  CE  . LYS   A 1 234 ? -10.963 -24.528 16.304  1.00 177.18 ? 254 LYS   A CE  1 
ATOM   1631 N  NZ  . LYS   A 1 234 ? -11.927 -24.167 17.381  1.00 173.51 ? 254 LYS   A NZ  1 
ATOM   1632 N  N   . ARG   A 1 235 ? -13.546 -21.018 13.719  1.00 184.88 ? 255 ARG   A N   1 
ATOM   1633 C  CA  . ARG   A 1 235 ? -13.575 -19.928 14.690  1.00 190.48 ? 255 ARG   A CA  1 
ATOM   1634 C  C   . ARG   A 1 235 ? -14.947 -19.281 14.748  1.00 195.84 ? 255 ARG   A C   1 
ATOM   1635 O  O   . ARG   A 1 235 ? -15.426 -18.909 15.824  1.00 199.12 ? 255 ARG   A O   1 
ATOM   1636 C  CB  . ARG   A 1 235 ? -12.519 -18.878 14.333  1.00 195.66 ? 255 ARG   A CB  1 
ATOM   1637 C  CG  . ARG   A 1 235 ? -11.079 -19.337 14.511  1.00 201.09 ? 255 ARG   A CG  1 
ATOM   1638 C  CD  . ARG   A 1 235 ? -10.114 -18.223 14.158  1.00 206.17 ? 255 ARG   A CD  1 
ATOM   1639 N  NE  . ARG   A 1 235 ? -8.724  -18.631 14.314  1.00 212.47 ? 255 ARG   A NE  1 
ATOM   1640 C  CZ  . ARG   A 1 235 ? -8.060  -18.594 15.461  1.00 218.35 ? 255 ARG   A CZ  1 
ATOM   1641 N  NH1 . ARG   A 1 235 ? -8.637  -18.191 16.581  1.00 218.70 ? 255 ARG   A NH1 1 
ATOM   1642 N  NH2 . ARG   A 1 235 ? -6.785  -18.972 15.485  1.00 220.85 ? 255 ARG   A NH2 1 
ATOM   1643 N  N   . MET   A 1 236 ? -15.596 -19.163 13.595  1.00 183.56 ? 256 MET   A N   1 
ATOM   1644 C  CA  . MET   A 1 236 ? -16.888 -18.511 13.447  1.00 178.28 ? 256 MET   A CA  1 
ATOM   1645 C  C   . MET   A 1 236 ? -17.799 -19.029 14.545  1.00 176.22 ? 256 MET   A C   1 
ATOM   1646 O  O   . MET   A 1 236 ? -18.144 -20.214 14.593  1.00 176.32 ? 256 MET   A O   1 
ATOM   1647 C  CB  . MET   A 1 236 ? -17.432 -18.732 12.035  1.00 178.48 ? 256 MET   A CB  1 
ATOM   1648 C  CG  . MET   A 1 236 ? -17.012 -17.665 11.039  1.00 175.03 ? 256 MET   A CG  1 
ATOM   1649 S  SD  . MET   A 1 236 ? -16.011 -18.314 9.689   1.00 191.85 ? 256 MET   A SD  1 
ATOM   1650 C  CE  . MET   A 1 236 ? -15.730 -16.830 8.728   1.00 165.79 ? 256 MET   A CE  1 
ATOM   1651 N  N   . LYS   A 1 237 ? -18.174 -18.133 15.436  1.00 178.57 ? 257 LYS   A N   1 
ATOM   1652 C  CA  . LYS   A 1 237 ? -19.128 -18.398 16.494  1.00 177.19 ? 257 LYS   A CA  1 
ATOM   1653 C  C   . LYS   A 1 237 ? -20.353 -17.500 16.433  1.00 181.31 ? 257 LYS   A C   1 
ATOM   1654 O  O   . LYS   A 1 237 ? -21.473 -17.992 16.612  1.00 181.44 ? 257 LYS   A O   1 
ATOM   1655 C  CB  . LYS   A 1 237 ? -18.424 -18.263 17.863  1.00 173.86 ? 257 LYS   A CB  1 
ATOM   1656 C  CG  . LYS   A 1 237 ? -17.858 -16.873 18.211  1.00 171.14 ? 257 LYS   A CG  1 
ATOM   1657 C  CD  . LYS   A 1 237 ? -16.368 -16.675 17.871  1.00 167.68 ? 257 LYS   A CD  1 
ATOM   1658 C  CE  . LYS   A 1 237 ? -16.168 -15.999 16.515  1.00 171.36 ? 257 LYS   A CE  1 
ATOM   1659 N  NZ  . LYS   A 1 237 ? -17.280 -15.062 16.201  1.00 174.88 ? 257 LYS   A NZ  1 
ATOM   1660 N  N   . GLU   A 1 238 ? -20.170 -16.206 16.145  1.00 182.37 ? 258 GLU   A N   1 
ATOM   1661 C  CA  . GLU   A 1 238 ? -21.257 -15.232 16.004  1.00 180.85 ? 258 GLU   A CA  1 
ATOM   1662 C  C   . GLU   A 1 238 ? -22.248 -15.326 17.161  1.00 183.35 ? 258 GLU   A C   1 
ATOM   1663 O  O   . GLU   A 1 238 ? -23.461 -15.426 16.970  1.00 186.57 ? 258 GLU   A O   1 
ATOM   1664 C  CB  . GLU   A 1 238 ? -21.964 -15.393 14.657  1.00 184.21 ? 258 GLU   A CB  1 
ATOM   1665 C  CG  . GLU   A 1 238 ? -21.045 -15.189 13.462  1.00 189.14 ? 258 GLU   A CG  1 
ATOM   1666 C  CD  . GLU   A 1 238 ? -20.470 -13.792 13.417  1.00 198.79 ? 258 GLU   A CD  1 
ATOM   1667 O  OE1 . GLU   A 1 238 ? -21.186 -12.842 13.802  1.00 199.22 ? 258 GLU   A OE1 1 
ATOM   1668 O  OE2 . GLU   A 1 238 ? -19.301 -13.644 13.006  1.00 206.83 ? 258 GLU   A OE2 1 
ATOM   1669 N  N   . SER   A 1 239 ? -21.711 -15.295 18.376  1.00 177.93 ? 259 SER   A N   1 
ATOM   1670 C  CA  . SER   A 1 239 ? -22.523 -15.353 19.586  1.00 176.77 ? 259 SER   A CA  1 
ATOM   1671 C  C   . SER   A 1 239 ? -21.760 -14.801 20.792  1.00 168.30 ? 259 SER   A C   1 
ATOM   1672 O  O   . SER   A 1 239 ? -20.538 -14.652 20.754  1.00 168.60 ? 259 SER   A O   1 
ATOM   1673 C  CB  . SER   A 1 239 ? -22.969 -16.789 19.863  1.00 178.40 ? 259 SER   A CB  1 
ATOM   1674 O  OG  . SER   A 1 239 ? -23.854 -17.256 18.859  1.00 180.38 ? 259 SER   A OG  1 
ATOM   1675 N  N   . ASP   A 1 250 ? -28.632 -16.724 6.114   1.00 135.40 ? 270 ASP   A N   1 
ATOM   1676 C  CA  . ASP   A 1 250 ? -27.267 -16.839 6.613   1.00 144.23 ? 270 ASP   A CA  1 
ATOM   1677 C  C   . ASP   A 1 250 ? -26.836 -18.303 6.654   1.00 149.18 ? 270 ASP   A C   1 
ATOM   1678 O  O   . ASP   A 1 250 ? -27.356 -19.091 7.442   1.00 153.06 ? 270 ASP   A O   1 
ATOM   1679 C  CB  . ASP   A 1 250 ? -27.149 -16.207 8.001   1.00 151.11 ? 270 ASP   A CB  1 
ATOM   1680 C  CG  . ASP   A 1 250 ? -25.711 -15.928 8.396   1.00 151.28 ? 270 ASP   A CG  1 
ATOM   1681 O  OD1 . ASP   A 1 250 ? -24.799 -16.269 7.614   1.00 148.17 ? 270 ASP   A OD1 1 
ATOM   1682 O  OD2 . ASP   A 1 250 ? -25.493 -15.359 9.487   1.00 152.20 ? 270 ASP   A OD2 1 
ATOM   1683 N  N   . PHE   A 1 251 ? -25.880 -18.658 5.793   1.00 140.15 ? 271 PHE   A N   1 
ATOM   1684 C  CA  . PHE   A 1 251 ? -25.419 -20.041 5.716   1.00 137.72 ? 271 PHE   A CA  1 
ATOM   1685 C  C   . PHE   A 1 251 ? -24.715 -20.466 6.999   1.00 146.48 ? 271 PHE   A C   1 
ATOM   1686 O  O   . PHE   A 1 251 ? -24.915 -21.587 7.482   1.00 152.80 ? 271 PHE   A O   1 
ATOM   1687 C  CB  . PHE   A 1 251 ? -24.497 -20.209 4.507   1.00 132.93 ? 271 PHE   A CB  1 
ATOM   1688 C  CG  . PHE   A 1 251 ? -23.807 -21.542 4.440   1.00 128.30 ? 271 PHE   A CG  1 
ATOM   1689 C  CD1 . PHE   A 1 251 ? -24.463 -22.654 3.937   1.00 129.61 ? 271 PHE   A CD1 1 
ATOM   1690 C  CD2 . PHE   A 1 251 ? -22.493 -21.679 4.858   1.00 127.71 ? 271 PHE   A CD2 1 
ATOM   1691 C  CE1 . PHE   A 1 251 ? -23.825 -23.878 3.867   1.00 121.14 ? 271 PHE   A CE1 1 
ATOM   1692 C  CE2 . PHE   A 1 251 ? -21.852 -22.900 4.789   1.00 124.18 ? 271 PHE   A CE2 1 
ATOM   1693 C  CZ  . PHE   A 1 251 ? -22.520 -24.000 4.291   1.00 120.21 ? 271 PHE   A CZ  1 
ATOM   1694 N  N   . LEU   A 1 252 ? -23.885 -19.587 7.563   1.00 146.69 ? 272 LEU   A N   1 
ATOM   1695 C  CA  . LEU   A 1 252 ? -23.180 -19.918 8.797   1.00 151.33 ? 272 LEU   A CA  1 
ATOM   1696 C  C   . LEU   A 1 252 ? -24.140 -20.016 9.975   1.00 158.63 ? 272 LEU   A C   1 
ATOM   1697 O  O   . LEU   A 1 252 ? -24.058 -20.956 10.775  1.00 163.98 ? 272 LEU   A O   1 
ATOM   1698 C  CB  . LEU   A 1 252 ? -22.099 -18.875 9.076   1.00 153.07 ? 272 LEU   A CB  1 
ATOM   1699 C  CG  . LEU   A 1 252 ? -21.409 -18.950 10.438  1.00 161.87 ? 272 LEU   A CG  1 
ATOM   1700 C  CD1 . LEU   A 1 252 ? -20.469 -20.139 10.497  1.00 161.94 ? 272 LEU   A CD1 1 
ATOM   1701 C  CD2 . LEU   A 1 252 ? -20.671 -17.655 10.729  1.00 164.25 ? 272 LEU   A CD2 1 
ATOM   1702 N  N   . GLN   A 1 253 ? -25.059 -19.055 10.097  1.00 163.70 ? 273 GLN   A N   1 
ATOM   1703 C  CA  . GLN   A 1 253 ? -25.987 -19.058 11.224  1.00 170.73 ? 273 GLN   A CA  1 
ATOM   1704 C  C   . GLN   A 1 253 ? -27.128 -20.063 11.137  1.00 174.05 ? 273 GLN   A C   1 
ATOM   1705 O  O   . GLN   A 1 253 ? -27.603 -20.566 12.162  1.00 174.60 ? 273 GLN   A O   1 
ATOM   1706 C  CB  . GLN   A 1 253 ? -26.719 -17.718 11.303  1.00 166.71 ? 273 GLN   A CB  1 
ATOM   1707 C  CG  . GLN   A 1 253 ? -27.760 -17.638 12.408  1.00 169.84 ? 273 GLN   A CG  1 
ATOM   1708 C  CD  . GLN   A 1 253 ? -29.165 -17.913 11.908  1.00 172.00 ? 273 GLN   A CD  1 
ATOM   1709 O  OE1 . GLN   A 1 253 ? -29.696 -17.174 11.078  1.00 172.93 ? 273 GLN   A OE1 1 
ATOM   1710 N  NE2 . GLN   A 1 253 ? -29.774 -18.984 12.406  1.00 176.75 ? 273 GLN   A NE2 1 
ATOM   1711 N  N   . LEU   A 1 254 ? -27.481 -20.446 9.908   1.00 168.73 ? 274 LEU   A N   1 
ATOM   1712 C  CA  . LEU   A 1 254 ? -28.477 -21.533 9.704   1.00 172.28 ? 274 LEU   A CA  1 
ATOM   1713 C  C   . LEU   A 1 254 ? -27.821 -22.908 9.824   1.00 171.57 ? 274 LEU   A C   1 
ATOM   1714 O  O   . LEU   A 1 254 ? -28.397 -23.880 9.305   1.00 168.45 ? 274 LEU   A O   1 
ATOM   1715 C  CB  . LEU   A 1 254 ? -29.184 -21.328 8.364   1.00 171.22 ? 274 LEU   A CB  1 
ATOM   1716 C  CG  . LEU   A 1 254 ? -30.036 -20.064 8.282   1.00 172.82 ? 274 LEU   A CG  1 
ATOM   1717 C  CD1 . LEU   A 1 254 ? -30.582 -19.862 6.877   1.00 166.27 ? 274 LEU   A CD1 1 
ATOM   1718 C  CD2 . LEU   A 1 254 ? -31.164 -20.104 9.301   1.00 177.11 ? 274 LEU   A CD2 1 
ATOM   1719 N  N   . MET   A 1 255 ? -26.668 -22.978 10.486  1.00 173.50 ? 275 MET   A N   1 
ATOM   1720 C  CA  . MET   A 1 255 ? -25.955 -24.270 10.638  1.00 176.20 ? 275 MET   A CA  1 
ATOM   1721 C  C   . MET   A 1 255 ? -25.523 -24.412 12.097  1.00 182.61 ? 275 MET   A C   1 
ATOM   1722 O  O   . MET   A 1 255 ? -25.766 -25.484 12.676  1.00 179.38 ? 275 MET   A O   1 
ATOM   1723 C  CB  . MET   A 1 255 ? -24.723 -24.318 9.735   1.00 170.47 ? 275 MET   A CB  1 
ATOM   1724 C  CG  . MET   A 1 255 ? -24.601 -25.600 8.937   1.00 163.94 ? 275 MET   A CG  1 
ATOM   1725 S  SD  . MET   A 1 255 ? -23.919 -25.324 7.282   1.00 163.59 ? 275 MET   A SD  1 
ATOM   1726 C  CE  . MET   A 1 255 ? -22.187 -25.081 7.672   1.00 150.57 ? 275 MET   A CE  1 
ATOM   1727 N  N   . ILE   A 1 256 ? -24.924 -23.363 12.672  1.00 177.61 ? 276 ILE   A N   1 
ATOM   1728 C  CA  . ILE   A 1 256 ? -24.562 -23.401 14.121  1.00 177.50 ? 276 ILE   A CA  1 
ATOM   1729 C  C   . ILE   A 1 256 ? -25.830 -23.750 14.898  1.00 181.75 ? 276 ILE   A C   1 
ATOM   1730 O  O   . ILE   A 1 256 ? -25.705 -24.213 16.044  1.00 181.54 ? 276 ILE   A O   1 
ATOM   1731 C  CB  . ILE   A 1 256 ? -23.939 -22.074 14.596  1.00 173.19 ? 276 ILE   A CB  1 
ATOM   1732 C  CG1 . ILE   A 1 256 ? -24.582 -20.862 13.921  1.00 170.09 ? 276 ILE   A CG1 1 
ATOM   1733 C  CG2 . ILE   A 1 256 ? -22.431 -22.091 14.400  1.00 168.13 ? 276 ILE   A CG2 1 
ATOM   1734 C  CD1 . ILE   A 1 256 ? -23.642 -19.694 13.755  1.00 163.70 ? 276 ILE   A CD1 1 
ATOM   1735 N  N   . ASP   A 1 257 ? -27.001 -23.545 14.291  1.00 190.75 ? 277 ASP   A N   1 
ATOM   1736 C  CA  . ASP   A 1 257 ? -28.269 -23.963 14.940  1.00 193.71 ? 277 ASP   A CA  1 
ATOM   1737 C  C   . ASP   A 1 257 ? -28.096 -25.401 15.432  1.00 190.58 ? 277 ASP   A C   1 
ATOM   1738 O  O   . ASP   A 1 257 ? -28.788 -25.776 16.396  1.00 188.38 ? 277 ASP   A O   1 
ATOM   1739 C  CB  . ASP   A 1 257 ? -29.450 -23.813 13.980  1.00 195.55 ? 277 ASP   A CB  1 
ATOM   1740 C  CG  . ASP   A 1 257 ? -29.586 -22.411 13.414  1.00 191.45 ? 277 ASP   A CG  1 
ATOM   1741 O  OD1 . ASP   A 1 257 ? -29.083 -21.471 14.057  1.00 187.62 ? 277 ASP   A OD1 1 
ATOM   1742 O  OD2 . ASP   A 1 257 ? -30.196 -22.272 12.337  1.00 191.04 ? 277 ASP   A OD2 1 
ATOM   1743 N  N   . SER   A 1 258 ? -27.213 -26.170 14.788  1.00 182.11 ? 278 SER   A N   1 
ATOM   1744 C  CA  . SER   A 1 258 ? -26.921 -27.559 15.227  1.00 176.07 ? 278 SER   A CA  1 
ATOM   1745 C  C   . SER   A 1 258 ? -27.254 -27.722 16.713  1.00 172.43 ? 278 SER   A C   1 
ATOM   1746 O  O   . SER   A 1 258 ? -26.378 -27.381 17.531  1.00 170.10 ? 278 SER   A O   1 
ATOM   1747 C  CB  . SER   A 1 258 ? -25.481 -27.902 14.954  1.00 174.04 ? 278 SER   A CB  1 
ATOM   1748 O  OG  . SER   A 1 258 ? -24.660 -26.750 15.060  1.00 174.16 ? 278 SER   A OG  1 
ATOM   1749 N  N   . SER   A 1 266 ? -31.134 -35.929 17.826  1.00 174.20 ? 286 SER   A N   1 
ATOM   1750 C  CA  . SER   A 1 266 ? -32.357 -36.008 17.037  1.00 176.22 ? 286 SER   A CA  1 
ATOM   1751 C  C   . SER   A 1 266 ? -32.056 -36.475 15.620  1.00 181.01 ? 286 SER   A C   1 
ATOM   1752 O  O   . SER   A 1 266 ? -32.900 -36.353 14.730  1.00 184.59 ? 286 SER   A O   1 
ATOM   1753 C  CB  . SER   A 1 266 ? -33.057 -34.654 16.989  1.00 175.26 ? 286 SER   A CB  1 
ATOM   1754 O  OG  . SER   A 1 266 ? -32.452 -33.815 16.021  1.00 180.36 ? 286 SER   A OG  1 
ATOM   1755 N  N   . HIS   A 1 267 ? -30.842 -36.998 15.421  1.00 184.50 ? 287 HIS   A N   1 
ATOM   1756 C  CA  . HIS   A 1 267 ? -30.358 -37.453 14.118  1.00 190.06 ? 287 HIS   A CA  1 
ATOM   1757 C  C   . HIS   A 1 267 ? -30.286 -36.304 13.113  1.00 190.67 ? 287 HIS   A C   1 
ATOM   1758 O  O   . HIS   A 1 267 ? -30.429 -36.510 11.908  1.00 183.61 ? 287 HIS   A O   1 
ATOM   1759 C  CB  . HIS   A 1 267 ? -31.222 -38.603 13.578  1.00 183.32 ? 287 HIS   A CB  1 
ATOM   1760 C  CG  . HIS   A 1 267 ? -30.649 -39.302 12.381  1.00 177.39 ? 287 HIS   A CG  1 
ATOM   1761 N  ND1 . HIS   A 1 267 ? -29.313 -39.621 12.263  1.00 173.64 ? 287 HIS   A ND1 1 
ATOM   1762 C  CD2 . HIS   A 1 267 ? -31.244 -39.759 11.253  1.00 173.66 ? 287 HIS   A CD2 1 
ATOM   1763 C  CE1 . HIS   A 1 267 ? -29.109 -40.236 11.111  1.00 167.67 ? 287 HIS   A CE1 1 
ATOM   1764 N  NE2 . HIS   A 1 267 ? -30.265 -40.332 10.479  1.00 171.52 ? 287 HIS   A NE2 1 
ATOM   1765 N  N   . LYS   A 1 268 ? -30.057 -35.086 13.598  1.00 193.91 ? 288 LYS   A N   1 
ATOM   1766 C  CA  . LYS   A 1 268 ? -29.976 -33.912 12.732  1.00 196.12 ? 288 LYS   A CA  1 
ATOM   1767 C  C   . LYS   A 1 268 ? -28.975 -32.911 13.307  1.00 200.67 ? 288 LYS   A C   1 
ATOM   1768 O  O   . LYS   A 1 268 ? -29.269 -31.724 13.472  1.00 197.35 ? 288 LYS   A O   1 
ATOM   1769 C  CB  . LYS   A 1 268 ? -31.353 -33.270 12.549  1.00 192.69 ? 288 LYS   A CB  1 
ATOM   1770 C  CG  . LYS   A 1 268 ? -32.334 -34.062 11.693  1.00 187.10 ? 288 LYS   A CG  1 
ATOM   1771 C  CD  . LYS   A 1 268 ? -33.703 -33.399 11.669  1.00 188.51 ? 288 LYS   A CD  1 
ATOM   1772 C  CE  . LYS   A 1 268 ? -34.701 -34.231 10.884  1.00 187.60 ? 288 LYS   A CE  1 
ATOM   1773 N  NZ  . LYS   A 1 268 ? -36.050 -33.602 10.841  1.00 186.11 ? 288 LYS   A NZ  1 
ATOM   1774 N  N   . ALA   A 1 269 ? -27.772 -33.387 13.622  1.00 209.87 ? 289 ALA   A N   1 
ATOM   1775 C  CA  . ALA   A 1 269 ? -26.756 -32.557 14.242  1.00 204.37 ? 289 ALA   A CA  1 
ATOM   1776 C  C   . ALA   A 1 269 ? -25.753 -32.082 13.198  1.00 200.68 ? 289 ALA   A C   1 
ATOM   1777 O  O   . ALA   A 1 269 ? -25.965 -32.221 11.988  1.00 204.58 ? 289 ALA   A O   1 
ATOM   1778 C  CB  . ALA   A 1 269 ? -26.065 -33.324 15.371  1.00 201.28 ? 289 ALA   A CB  1 
ATOM   1779 N  N   . LEU   A 1 270 ? -24.643 -31.516 13.679  1.00 178.10 ? 290 LEU   A N   1 
ATOM   1780 C  CA  . LEU   A 1 270 ? -23.574 -31.008 12.827  1.00 164.19 ? 290 LEU   A CA  1 
ATOM   1781 C  C   . LEU   A 1 270 ? -22.369 -30.613 13.672  1.00 158.76 ? 290 LEU   A C   1 
ATOM   1782 O  O   . LEU   A 1 270 ? -22.429 -29.643 14.436  1.00 156.72 ? 290 LEU   A O   1 
ATOM   1783 C  CB  . LEU   A 1 270 ? -24.062 -29.820 11.991  1.00 157.91 ? 290 LEU   A CB  1 
ATOM   1784 C  CG  . LEU   A 1 270 ? -22.974 -29.066 11.231  1.00 151.83 ? 290 LEU   A CG  1 
ATOM   1785 C  CD1 . LEU   A 1 270 ? -23.325 -28.983 9.758   1.00 150.29 ? 290 LEU   A CD1 1 
ATOM   1786 C  CD2 . LEU   A 1 270 ? -22.807 -27.687 11.835  1.00 153.97 ? 290 LEU   A CD2 1 
ATOM   1787 N  N   . SER   A 1 271 ? -21.278 -31.370 13.558  1.00 155.71 ? 291 SER   A N   1 
ATOM   1788 C  CA  . SER   A 1 271 ? -20.070 -31.045 14.296  1.00 154.78 ? 291 SER   A CA  1 
ATOM   1789 C  C   . SER   A 1 271 ? -19.450 -29.762 13.753  1.00 158.52 ? 291 SER   A C   1 
ATOM   1790 O  O   . SER   A 1 271 ? -19.848 -29.227 12.712  1.00 150.75 ? 291 SER   A O   1 
ATOM   1791 C  CB  . SER   A 1 271 ? -19.057 -32.193 14.227  1.00 150.89 ? 291 SER   A CB  1 
ATOM   1792 O  OG  . SER   A 1 271 ? -18.232 -32.101 13.075  1.00 151.14 ? 291 SER   A OG  1 
ATOM   1793 N  N   . ASP   A 1 272 ? -18.463 -29.261 14.493  1.00 174.34 ? 292 ASP   A N   1 
ATOM   1794 C  CA  . ASP   A 1 272 ? -17.694 -28.115 14.026  1.00 173.95 ? 292 ASP   A CA  1 
ATOM   1795 C  C   . ASP   A 1 272 ? -17.012 -28.418 12.700  1.00 163.50 ? 292 ASP   A C   1 
ATOM   1796 O  O   . ASP   A 1 272 ? -17.018 -27.590 11.781  1.00 165.16 ? 292 ASP   A O   1 
ATOM   1797 C  CB  . ASP   A 1 272 ? -16.659 -27.721 15.074  1.00 171.22 ? 292 ASP   A CB  1 
ATOM   1798 C  CG  . ASP   A 1 272 ? -15.593 -26.820 14.507  1.00 176.29 ? 292 ASP   A CG  1 
ATOM   1799 O  OD1 . ASP   A 1 272 ? -15.959 -25.799 13.883  1.00 183.47 ? 292 ASP   A OD1 1 
ATOM   1800 O  OD2 . ASP   A 1 272 ? -14.398 -27.137 14.662  1.00 169.04 ? 292 ASP   A OD2 1 
ATOM   1801 N  N   . LEU   A 1 273 ? -16.407 -29.605 12.584  1.00 153.23 ? 293 LEU   A N   1 
ATOM   1802 C  CA  . LEU   A 1 273 ? -15.768 -29.987 11.328  1.00 145.96 ? 293 LEU   A CA  1 
ATOM   1803 C  C   . LEU   A 1 273 ? -16.787 -30.078 10.203  1.00 142.90 ? 293 LEU   A C   1 
ATOM   1804 O  O   . LEU   A 1 273 ? -16.502 -29.690 9.062   1.00 142.21 ? 293 LEU   A O   1 
ATOM   1805 C  CB  . LEU   A 1 273 ? -15.032 -31.317 11.488  1.00 146.37 ? 293 LEU   A CB  1 
ATOM   1806 C  CG  . LEU   A 1 273 ? -13.716 -31.269 12.260  1.00 145.70 ? 293 LEU   A CG  1 
ATOM   1807 C  CD1 . LEU   A 1 273 ? -13.101 -32.655 12.309  1.00 145.70 ? 293 LEU   A CD1 1 
ATOM   1808 C  CD2 . LEU   A 1 273 ? -12.773 -30.278 11.602  1.00 146.88 ? 293 LEU   A CD2 1 
ATOM   1809 N  N   . GLU   A 1 274 ? -17.987 -30.584 10.513  1.00 143.11 ? 294 GLU   A N   1 
ATOM   1810 C  CA  . GLU   A 1 274 ? -19.065 -30.633 9.530   1.00 137.66 ? 294 GLU   A CA  1 
ATOM   1811 C  C   . GLU   A 1 274 ? -19.415 -29.232 9.046   1.00 133.05 ? 294 GLU   A C   1 
ATOM   1812 O  O   . GLU   A 1 274 ? -19.521 -28.985 7.838   1.00 127.20 ? 294 GLU   A O   1 
ATOM   1813 C  CB  . GLU   A 1 274 ? -20.301 -31.322 10.122  1.00 139.21 ? 294 GLU   A CB  1 
ATOM   1814 C  CG  . GLU   A 1 274 ? -20.131 -32.810 10.454  1.00 140.81 ? 294 GLU   A CG  1 
ATOM   1815 C  CD  . GLU   A 1 274 ? -21.448 -33.569 10.412  1.00 142.45 ? 294 GLU   A CD  1 
ATOM   1816 O  OE1 . GLU   A 1 274 ? -22.511 -32.916 10.316  1.00 149.55 ? 294 GLU   A OE1 1 
ATOM   1817 O  OE2 . GLU   A 1 274 ? -21.419 -34.819 10.466  1.00 138.19 ? 294 GLU   A OE2 1 
ATOM   1818 N  N   . LEU   A 1 275 ? -19.593 -28.299 9.988   1.00 138.48 ? 295 LEU   A N   1 
ATOM   1819 C  CA  . LEU   A 1 275 ? -19.754 -26.889 9.647   1.00 135.92 ? 295 LEU   A CA  1 
ATOM   1820 C  C   . LEU   A 1 275 ? -18.671 -26.449 8.673   1.00 128.99 ? 295 LEU   A C   1 
ATOM   1821 O  O   . LEU   A 1 275 ? -18.959 -25.884 7.614   1.00 126.06 ? 295 LEU   A O   1 
ATOM   1822 C  CB  . LEU   A 1 275 ? -19.709 -26.029 10.921  1.00 141.46 ? 295 LEU   A CB  1 
ATOM   1823 C  CG  . LEU   A 1 275 ? -20.133 -24.545 11.041  1.00 141.19 ? 295 LEU   A CG  1 
ATOM   1824 C  CD1 . LEU   A 1 275 ? -19.495 -23.592 10.015  1.00 139.19 ? 295 LEU   A CD1 1 
ATOM   1825 C  CD2 . LEU   A 1 275 ? -21.650 -24.393 11.056  1.00 153.61 ? 295 LEU   A CD2 1 
ATOM   1826 N  N   . VAL   A 1 276 ? -17.408 -26.715 9.015   1.00 131.01 ? 296 VAL   A N   1 
ATOM   1827 C  CA  . VAL   A 1 276 ? -16.304 -26.266 8.172   1.00 129.58 ? 296 VAL   A CA  1 
ATOM   1828 C  C   . VAL   A 1 276 ? -16.330 -26.991 6.831   1.00 127.69 ? 296 VAL   A C   1 
ATOM   1829 O  O   . VAL   A 1 276 ? -16.154 -26.379 5.771   1.00 122.53 ? 296 VAL   A O   1 
ATOM   1830 C  CB  . VAL   A 1 276 ? -14.960 -26.458 8.897   1.00 137.77 ? 296 VAL   A CB  1 
ATOM   1831 C  CG1 . VAL   A 1 276 ? -13.829 -25.952 8.025   1.00 142.66 ? 296 VAL   A CG1 1 
ATOM   1832 C  CG2 . VAL   A 1 276 ? -14.967 -25.730 10.237  1.00 154.19 ? 296 VAL   A CG2 1 
ATOM   1833 N  N   . ALA   A 1 277 ? -16.573 -28.307 6.861   1.00 133.19 ? 297 ALA   A N   1 
ATOM   1834 C  CA  . ALA   A 1 277 ? -16.576 -29.115 5.644   1.00 124.41 ? 297 ALA   A CA  1 
ATOM   1835 C  C   . ALA   A 1 277 ? -17.601 -28.622 4.631   1.00 121.46 ? 297 ALA   A C   1 
ATOM   1836 O  O   . ALA   A 1 277 ? -17.348 -28.671 3.422   1.00 116.85 ? 297 ALA   A O   1 
ATOM   1837 C  CB  . ALA   A 1 277 ? -16.842 -30.579 5.988   1.00 119.26 ? 297 ALA   A CB  1 
ATOM   1838 N  N   . GLN   A 1 278 ? -18.758 -28.150 5.096   1.00 112.44 ? 298 GLN   A N   1 
ATOM   1839 C  CA  . GLN   A 1 278 ? -19.710 -27.542 4.173   1.00 108.54 ? 298 GLN   A CA  1 
ATOM   1840 C  C   . GLN   A 1 278 ? -19.246 -26.155 3.752   1.00 111.85 ? 298 GLN   A C   1 
ATOM   1841 O  O   . GLN   A 1 278 ? -19.439 -25.750 2.600   1.00 109.67 ? 298 GLN   A O   1 
ATOM   1842 C  CB  . GLN   A 1 278 ? -21.098 -27.464 4.807   1.00 109.48 ? 298 GLN   A CB  1 
ATOM   1843 C  CG  . GLN   A 1 278 ? -21.502 -28.686 5.608   1.00 115.38 ? 298 GLN   A CG  1 
ATOM   1844 C  CD  . GLN   A 1 278 ? -21.283 -29.982 4.863   1.00 106.18 ? 298 GLN   A CD  1 
ATOM   1845 O  OE1 . GLN   A 1 278 ? -21.652 -30.110 3.697   1.00 102.22 ? 298 GLN   A OE1 1 
ATOM   1846 N  NE2 . GLN   A 1 278 ? -20.675 -30.955 5.533   1.00 109.63 ? 298 GLN   A NE2 1 
ATOM   1847 N  N   . SER   A 1 279 ? -18.623 -25.417 4.674   1.00 110.07 ? 299 SER   A N   1 
ATOM   1848 C  CA  . SER   A 1 279 ? -18.153 -24.073 4.357   1.00 109.71 ? 299 SER   A CA  1 
ATOM   1849 C  C   . SER   A 1 279 ? -17.055 -24.109 3.303   1.00 104.39 ? 299 SER   A C   1 
ATOM   1850 O  O   . SER   A 1 279 ? -16.979 -23.223 2.444   1.00 96.08  ? 299 SER   A O   1 
ATOM   1851 C  CB  . SER   A 1 279 ? -17.653 -23.380 5.624   1.00 115.79 ? 299 SER   A CB  1 
ATOM   1852 O  OG  . SER   A 1 279 ? -18.570 -23.532 6.695   1.00 118.29 ? 299 SER   A OG  1 
ATOM   1853 N  N   . ILE   A 1 280 ? -16.194 -25.128 3.353   1.00 102.43 ? 300 ILE   A N   1 
ATOM   1854 C  CA  . ILE   A 1 280 ? -15.111 -25.238 2.381   1.00 104.45 ? 300 ILE   A CA  1 
ATOM   1855 C  C   . ILE   A 1 280 ? -15.674 -25.424 0.978   1.00 102.95 ? 300 ILE   A C   1 
ATOM   1856 O  O   . ILE   A 1 280 ? -15.163 -24.855 0.004   1.00 101.47 ? 300 ILE   A O   1 
ATOM   1857 C  CB  . ILE   A 1 280 ? -14.161 -26.385 2.776   1.00 107.05 ? 300 ILE   A CB  1 
ATOM   1858 C  CG1 . ILE   A 1 280 ? -13.486 -26.074 4.113   1.00 106.07 ? 300 ILE   A CG1 1 
ATOM   1859 C  CG2 . ILE   A 1 280 ? -13.119 -26.623 1.692   1.00 108.28 ? 300 ILE   A CG2 1 
ATOM   1860 C  CD1 . ILE   A 1 280 ? -12.595 -27.182 4.625   1.00 117.02 ? 300 ILE   A CD1 1 
ATOM   1861 N  N   . ILE   A 1 281 ? -16.747 -26.208 0.856   1.00 105.95 ? 301 ILE   A N   1 
ATOM   1862 C  CA  . ILE   A 1 281 ? -17.361 -26.439 -0.448  1.00 99.46  ? 301 ILE   A CA  1 
ATOM   1863 C  C   . ILE   A 1 281 ? -18.015 -25.162 -0.962  1.00 95.30  ? 301 ILE   A C   1 
ATOM   1864 O  O   . ILE   A 1 281 ? -17.806 -24.756 -2.111  1.00 92.74  ? 301 ILE   A O   1 
ATOM   1865 C  CB  . ILE   A 1 281 ? -18.374 -27.595 -0.365  1.00 96.20  ? 301 ILE   A CB  1 
ATOM   1866 C  CG1 . ILE   A 1 281 ? -17.682 -28.874 0.105   1.00 94.68  ? 301 ILE   A CG1 1 
ATOM   1867 C  CG2 . ILE   A 1 281 ? -19.064 -27.805 -1.705  1.00 92.01  ? 301 ILE   A CG2 1 
ATOM   1868 C  CD1 . ILE   A 1 281 ? -16.499 -29.281 -0.745  1.00 91.86  ? 301 ILE   A CD1 1 
ATOM   1869 N  N   . PHE   A 1 282 ? -18.815 -24.509 -0.114  1.00 97.15  ? 302 PHE   A N   1 
ATOM   1870 C  CA  . PHE   A 1 282 ? -19.548 -23.322 -0.544  1.00 97.40  ? 302 PHE   A CA  1 
ATOM   1871 C  C   . PHE   A 1 282 ? -18.602 -22.193 -0.936  1.00 95.25  ? 302 PHE   A C   1 
ATOM   1872 O  O   . PHE   A 1 282 ? -18.872 -21.450 -1.887  1.00 86.72  ? 302 PHE   A O   1 
ATOM   1873 C  CB  . PHE   A 1 282 ? -20.502 -22.867 0.562   1.00 103.22 ? 302 PHE   A CB  1 
ATOM   1874 C  CG  . PHE   A 1 282 ? -21.816 -23.599 0.573   1.00 104.68 ? 302 PHE   A CG  1 
ATOM   1875 C  CD1 . PHE   A 1 282 ? -21.857 -24.977 0.707   1.00 103.75 ? 302 PHE   A CD1 1 
ATOM   1876 C  CD2 . PHE   A 1 282 ? -23.011 -22.906 0.464   1.00 106.86 ? 302 PHE   A CD2 1 
ATOM   1877 C  CE1 . PHE   A 1 282 ? -23.063 -25.651 0.720   1.00 108.70 ? 302 PHE   A CE1 1 
ATOM   1878 C  CE2 . PHE   A 1 282 ? -24.222 -23.576 0.475   1.00 109.74 ? 302 PHE   A CE2 1 
ATOM   1879 C  CZ  . PHE   A 1 282 ? -24.247 -24.950 0.604   1.00 108.79 ? 302 PHE   A CZ  1 
ATOM   1880 N  N   . ILE   A 1 283 ? -17.485 -22.051 -0.219  1.00 96.28  ? 303 ILE   A N   1 
ATOM   1881 C  CA  . ILE   A 1 283 ? -16.529 -20.995 -0.533  1.00 94.06  ? 303 ILE   A CA  1 
ATOM   1882 C  C   . ILE   A 1 283 ? -15.855 -21.268 -1.872  1.00 91.27  ? 303 ILE   A C   1 
ATOM   1883 O  O   . ILE   A 1 283 ? -15.776 -20.387 -2.737  1.00 97.33  ? 303 ILE   A O   1 
ATOM   1884 C  CB  . ILE   A 1 283 ? -15.496 -20.850 0.599   1.00 96.74  ? 303 ILE   A CB  1 
ATOM   1885 C  CG1 . ILE   A 1 283 ? -16.144 -20.231 1.839   1.00 99.51  ? 303 ILE   A CG1 1 
ATOM   1886 C  CG2 . ILE   A 1 283 ? -14.314 -20.009 0.142   1.00 97.34  ? 303 ILE   A CG2 1 
ATOM   1887 C  CD1 . ILE   A 1 283 ? -15.213 -20.136 3.027   1.00 105.45 ? 303 ILE   A CD1 1 
ATOM   1888 N  N   . PHE   A 1 284 ? -15.360 -22.493 -2.063  1.00 93.80  ? 304 PHE   A N   1 
ATOM   1889 C  CA  . PHE   A 1 284 ? -14.683 -22.833 -3.311  1.00 91.96  ? 304 PHE   A CA  1 
ATOM   1890 C  C   . PHE   A 1 284 ? -15.629 -22.714 -4.501  1.00 91.17  ? 304 PHE   A C   1 
ATOM   1891 O  O   . PHE   A 1 284 ? -15.274 -22.144 -5.539  1.00 88.14  ? 304 PHE   A O   1 
ATOM   1892 C  CB  . PHE   A 1 284 ? -14.098 -24.244 -3.225  1.00 91.37  ? 304 PHE   A CB  1 
ATOM   1893 C  CG  . PHE   A 1 284 ? -13.356 -24.669 -4.462  1.00 90.57  ? 304 PHE   A CG  1 
ATOM   1894 C  CD1 . PHE   A 1 284 ? -12.009 -24.385 -4.609  1.00 92.18  ? 304 PHE   A CD1 1 
ATOM   1895 C  CD2 . PHE   A 1 284 ? -14.006 -25.353 -5.478  1.00 88.70  ? 304 PHE   A CD2 1 
ATOM   1896 C  CE1 . PHE   A 1 284 ? -11.323 -24.773 -5.744  1.00 93.13  ? 304 PHE   A CE1 1 
ATOM   1897 C  CE2 . PHE   A 1 284 ? -13.326 -25.741 -6.618  1.00 86.06  ? 304 PHE   A CE2 1 
ATOM   1898 C  CZ  . PHE   A 1 284 ? -11.983 -25.452 -6.749  1.00 90.15  ? 304 PHE   A CZ  1 
ATOM   1899 N  N   . ALA   A 1 285 ? -16.844 -23.250 -4.365  1.00 88.64  ? 305 ALA   A N   1 
ATOM   1900 C  CA  . ALA   A 1 285 ? -17.809 -23.199 -5.459  1.00 90.70  ? 305 ALA   A CA  1 
ATOM   1901 C  C   . ALA   A 1 285 ? -18.219 -21.769 -5.779  1.00 93.22  ? 305 ALA   A C   1 
ATOM   1902 O  O   . ALA   A 1 285 ? -18.344 -21.399 -6.952  1.00 94.40  ? 305 ALA   A O   1 
ATOM   1903 C  CB  . ALA   A 1 285 ? -19.034 -24.037 -5.107  1.00 88.60  ? 305 ALA   A CB  1 
ATOM   1904 N  N   . GLY   A 1 286 ? -18.438 -20.952 -4.747  1.00 94.91  ? 306 GLY   A N   1 
ATOM   1905 C  CA  . GLY   A 1 286 ? -18.830 -19.573 -4.970  1.00 97.98  ? 306 GLY   A CA  1 
ATOM   1906 C  C   . GLY   A 1 286 ? -17.723 -18.711 -5.533  1.00 96.11  ? 306 GLY   A C   1 
ATOM   1907 O  O   . GLY   A 1 286 ? -17.994 -17.706 -6.195  1.00 100.20 ? 306 GLY   A O   1 
ATOM   1908 N  N   . TYR   A 1 287 ? -16.470 -19.084 -5.290  1.00 92.28  ? 307 TYR   A N   1 
ATOM   1909 C  CA  . TYR   A 1 287 ? -15.347 -18.329 -5.822  1.00 97.29  ? 307 TYR   A CA  1 
ATOM   1910 C  C   . TYR   A 1 287 ? -14.950 -18.802 -7.215  1.00 96.21  ? 307 TYR   A C   1 
ATOM   1911 O  O   . TYR   A 1 287 ? -14.877 -17.999 -8.150  1.00 96.79  ? 307 TYR   A O   1 
ATOM   1912 C  CB  . TYR   A 1 287 ? -14.151 -18.433 -4.872  1.00 97.91  ? 307 TYR   A CB  1 
ATOM   1913 C  CG  . TYR   A 1 287 ? -12.833 -18.128 -5.545  1.00 106.50 ? 307 TYR   A CG  1 
ATOM   1914 C  CD1 . TYR   A 1 287 ? -12.448 -16.818 -5.793  1.00 106.30 ? 307 TYR   A CD1 1 
ATOM   1915 C  CD2 . TYR   A 1 287 ? -11.977 -19.150 -5.941  1.00 104.09 ? 307 TYR   A CD2 1 
ATOM   1916 C  CE1 . TYR   A 1 287 ? -11.249 -16.536 -6.410  1.00 110.53 ? 307 TYR   A CE1 1 
ATOM   1917 C  CE2 . TYR   A 1 287 ? -10.779 -18.874 -6.561  1.00 106.75 ? 307 TYR   A CE2 1 
ATOM   1918 C  CZ  . TYR   A 1 287 ? -10.419 -17.566 -6.793  1.00 109.38 ? 307 TYR   A CZ  1 
ATOM   1919 O  OH  . TYR   A 1 287 ? -9.220  -17.284 -7.410  1.00 116.96 ? 307 TYR   A OH  1 
ATOM   1920 N  N   . GLU   A 1 288 ? -14.696 -20.101 -7.365  1.00 97.11  ? 308 GLU   A N   1 
ATOM   1921 C  CA  . GLU   A 1 288 ? -14.118 -20.608 -8.603  1.00 98.32  ? 308 GLU   A CA  1 
ATOM   1922 C  C   . GLU   A 1 288 ? -15.144 -20.672 -9.726  1.00 97.81  ? 308 GLU   A C   1 
ATOM   1923 O  O   . GLU   A 1 288 ? -14.921 -20.118 -10.807 1.00 97.15  ? 308 GLU   A O   1 
ATOM   1924 C  CB  . GLU   A 1 288 ? -13.499 -21.986 -8.366  1.00 96.86  ? 308 GLU   A CB  1 
ATOM   1925 C  CG  . GLU   A 1 288 ? -11.985 -21.963 -8.243  1.00 102.32 ? 308 GLU   A CG  1 
ATOM   1926 C  CD  . GLU   A 1 288 ? -11.301 -21.552 -9.534  1.00 102.59 ? 308 GLU   A CD  1 
ATOM   1927 O  OE1 . GLU   A 1 288 ? -11.906 -21.724 -10.613 1.00 96.98  ? 308 GLU   A OE1 1 
ATOM   1928 O  OE2 . GLU   A 1 288 ? -10.157 -21.055 -9.469  1.00 103.64 ? 308 GLU   A OE2 1 
ATOM   1929 N  N   . THR   A 1 289 ? -16.270 -21.350 -9.490  1.00 94.90  ? 309 THR   A N   1 
ATOM   1930 C  CA  . THR   A 1 289 ? -17.260 -21.544 -10.547 1.00 93.72  ? 309 THR   A CA  1 
ATOM   1931 C  C   . THR   A 1 289 ? -17.762 -20.212 -11.084 1.00 92.10  ? 309 THR   A C   1 
ATOM   1932 O  O   . THR   A 1 289 ? -17.871 -20.019 -12.300 1.00 86.28  ? 309 THR   A O   1 
ATOM   1933 C  CB  . THR   A 1 289 ? -18.427 -22.381 -10.026 1.00 87.52  ? 309 THR   A CB  1 
ATOM   1934 O  OG1 . THR   A 1 289 ? -19.110 -21.661 -8.994  1.00 90.82  ? 309 THR   A OG1 1 
ATOM   1935 C  CG2 . THR   A 1 289 ? -17.922 -23.697 -9.470  1.00 84.54  ? 309 THR   A CG2 1 
ATOM   1936 N  N   . THR   A 1 290 ? -18.076 -19.278 -10.186 1.00 91.97  ? 310 THR   A N   1 
ATOM   1937 C  CA  . THR   A 1 290 ? -18.545 -17.966 -10.611 1.00 95.31  ? 310 THR   A CA  1 
ATOM   1938 C  C   . THR   A 1 290 ? -17.492 -17.264 -11.461 1.00 92.77  ? 310 THR   A C   1 
ATOM   1939 O  O   . THR   A 1 290 ? -17.739 -16.921 -12.622 1.00 87.12  ? 310 THR   A O   1 
ATOM   1940 C  CB  . THR   A 1 290 ? -18.909 -17.120 -9.390  1.00 94.99  ? 310 THR   A CB  1 
ATOM   1941 O  OG1 . THR   A 1 290 ? -19.784 -17.866 -8.535  1.00 93.98  ? 310 THR   A OG1 1 
ATOM   1942 C  CG2 . THR   A 1 290 ? -19.604 -15.841 -9.820  1.00 94.99  ? 310 THR   A CG2 1 
ATOM   1943 N  N   . SER   A 1 291 ? -16.294 -17.072 -10.901 1.00 93.89  ? 311 SER   A N   1 
ATOM   1944 C  CA  . SER   A 1 291 ? -15.258 -16.312 -11.594 1.00 96.31  ? 311 SER   A CA  1 
ATOM   1945 C  C   . SER   A 1 291 ? -14.834 -16.989 -12.892 1.00 91.09  ? 311 SER   A C   1 
ATOM   1946 O  O   . SER   A 1 291 ? -14.581 -16.313 -13.896 1.00 91.67  ? 311 SER   A O   1 
ATOM   1947 C  CB  . SER   A 1 291 ? -14.050 -16.119 -10.678 1.00 97.02  ? 311 SER   A CB  1 
ATOM   1948 O  OG  . SER   A 1 291 ? -13.499 -17.368 -10.295 1.00 96.34  ? 311 SER   A OG  1 
ATOM   1949 N  N   . SER   A 1 292 ? -14.747 -18.321 -12.893 1.00 90.29  ? 312 SER   A N   1 
ATOM   1950 C  CA  . SER   A 1 292 ? -14.304 -19.035 -14.088 1.00 90.05  ? 312 SER   A CA  1 
ATOM   1951 C  C   . SER   A 1 292 ? -15.288 -18.850 -15.237 1.00 87.26  ? 312 SER   A C   1 
ATOM   1952 O  O   . SER   A 1 292 ? -14.889 -18.557 -16.369 1.00 89.11  ? 312 SER   A O   1 
ATOM   1953 C  CB  . SER   A 1 292 ? -14.112 -20.519 -13.776 1.00 90.39  ? 312 SER   A CB  1 
ATOM   1954 O  OG  . SER   A 1 292 ? -13.722 -21.239 -14.932 1.00 92.56  ? 312 SER   A OG  1 
ATOM   1955 N  N   . VAL   A 1 293 ? -16.583 -19.007 -14.961 1.00 87.61  ? 313 VAL   A N   1 
ATOM   1956 C  CA  . VAL   A 1 293 ? -17.584 -18.841 -16.009 1.00 88.20  ? 313 VAL   A CA  1 
ATOM   1957 C  C   . VAL   A 1 293 ? -17.680 -17.380 -16.432 1.00 91.16  ? 313 VAL   A C   1 
ATOM   1958 O  O   . VAL   A 1 293 ? -17.844 -17.077 -17.620 1.00 87.44  ? 313 VAL   A O   1 
ATOM   1959 C  CB  . VAL   A 1 293 ? -18.943 -19.393 -15.540 1.00 84.37  ? 313 VAL   A CB  1 
ATOM   1960 C  CG1 . VAL   A 1 293 ? -20.008 -19.151 -16.598 1.00 82.88  ? 313 VAL   A CG1 1 
ATOM   1961 C  CG2 . VAL   A 1 293 ? -18.830 -20.878 -15.241 1.00 89.72  ? 313 VAL   A CG2 1 
ATOM   1962 N  N   . LEU   A 1 294 ? -17.577 -16.451 -15.474 1.00 91.18  ? 314 LEU   A N   1 
ATOM   1963 C  CA  . LEU   A 1 294 ? -17.602 -15.030 -15.814 1.00 92.40  ? 314 LEU   A CA  1 
ATOM   1964 C  C   . LEU   A 1 294 ? -16.505 -14.683 -16.812 1.00 93.13  ? 314 LEU   A C   1 
ATOM   1965 O  O   . LEU   A 1 294 ? -16.741 -13.944 -17.776 1.00 88.65  ? 314 LEU   A O   1 
ATOM   1966 C  CB  . LEU   A 1 294 ? -17.456 -14.178 -14.551 1.00 94.80  ? 314 LEU   A CB  1 
ATOM   1967 C  CG  . LEU   A 1 294 ? -18.583 -14.138 -13.516 1.00 94.17  ? 314 LEU   A CG  1 
ATOM   1968 C  CD1 . LEU   A 1 294 ? -18.190 -13.250 -12.343 1.00 100.02 ? 314 LEU   A CD1 1 
ATOM   1969 C  CD2 . LEU   A 1 294 ? -19.882 -13.669 -14.133 1.00 93.21  ? 314 LEU   A CD2 1 
ATOM   1970 N  N   . SER   A 1 295 ? -15.300 -15.218 -16.605 1.00 89.38  ? 315 SER   A N   1 
ATOM   1971 C  CA  . SER   A 1 295 ? -14.206 -14.955 -17.535 1.00 88.76  ? 315 SER   A CA  1 
ATOM   1972 C  C   . SER   A 1 295 ? -14.464 -15.605 -18.889 1.00 89.69  ? 315 SER   A C   1 
ATOM   1973 O  O   . SER   A 1 295 ? -14.126 -15.033 -19.932 1.00 87.31  ? 315 SER   A O   1 
ATOM   1974 C  CB  . SER   A 1 295 ? -12.885 -15.445 -16.942 1.00 91.48  ? 315 SER   A CB  1 
ATOM   1975 O  OG  . SER   A 1 295 ? -12.911 -16.845 -16.725 1.00 94.84  ? 315 SER   A OG  1 
ATOM   1976 N  N   . PHE   A 1 296 ? -15.060 -16.802 -18.894 1.00 88.22  ? 316 PHE   A N   1 
ATOM   1977 C  CA  . PHE   A 1 296 ? -15.420 -17.439 -20.157 1.00 86.95  ? 316 PHE   A CA  1 
ATOM   1978 C  C   . PHE   A 1 296 ? -16.486 -16.639 -20.893 1.00 82.97  ? 316 PHE   A C   1 
ATOM   1979 O  O   . PHE   A 1 296 ? -16.444 -16.525 -22.123 1.00 79.82  ? 316 PHE   A O   1 
ATOM   1980 C  CB  . PHE   A 1 296 ? -15.902 -18.871 -19.917 1.00 85.92  ? 316 PHE   A CB  1 
ATOM   1981 C  CG  . PHE   A 1 296 ? -14.794 -19.878 -19.824 1.00 87.08  ? 316 PHE   A CG  1 
ATOM   1982 C  CD1 . PHE   A 1 296 ? -13.982 -20.133 -20.917 1.00 83.58  ? 316 PHE   A CD1 1 
ATOM   1983 C  CD2 . PHE   A 1 296 ? -14.574 -20.583 -18.653 1.00 88.69  ? 316 PHE   A CD2 1 
ATOM   1984 C  CE1 . PHE   A 1 296 ? -12.963 -21.063 -20.839 1.00 85.44  ? 316 PHE   A CE1 1 
ATOM   1985 C  CE2 . PHE   A 1 296 ? -13.556 -21.515 -18.569 1.00 87.63  ? 316 PHE   A CE2 1 
ATOM   1986 C  CZ  . PHE   A 1 296 ? -12.751 -21.756 -19.663 1.00 88.70  ? 316 PHE   A CZ  1 
ATOM   1987 N  N   . ILE   A 1 297 ? -17.450 -16.080 -20.157 1.00 78.34  ? 317 ILE   A N   1 
ATOM   1988 C  CA  . ILE   A 1 297 ? -18.482 -15.257 -20.782 1.00 86.79  ? 317 ILE   A CA  1 
ATOM   1989 C  C   . ILE   A 1 297 ? -17.858 -14.021 -21.417 1.00 85.56  ? 317 ILE   A C   1 
ATOM   1990 O  O   . ILE   A 1 297 ? -18.191 -13.645 -22.547 1.00 86.58  ? 317 ILE   A O   1 
ATOM   1991 C  CB  . ILE   A 1 297 ? -19.562 -14.878 -19.752 1.00 85.97  ? 317 ILE   A CB  1 
ATOM   1992 C  CG1 . ILE   A 1 297 ? -20.322 -16.119 -19.283 1.00 83.83  ? 317 ILE   A CG1 1 
ATOM   1993 C  CG2 . ILE   A 1 297 ? -20.515 -13.842 -20.334 1.00 89.20  ? 317 ILE   A CG2 1 
ATOM   1994 C  CD1 . ILE   A 1 297 ? -21.192 -15.877 -18.068 1.00 89.45  ? 317 ILE   A CD1 1 
ATOM   1995 N  N   . MET   A 1 298 ? -16.935 -13.375 -20.699 1.00 87.79  ? 318 MET   A N   1 
ATOM   1996 C  CA  . MET   A 1 298 ? -16.301 -12.165 -21.211 1.00 92.54  ? 318 MET   A CA  1 
ATOM   1997 C  C   . MET   A 1 298 ? -15.444 -12.449 -22.437 1.00 95.09  ? 318 MET   A C   1 
ATOM   1998 O  O   . MET   A 1 298 ? -15.344 -11.599 -23.329 1.00 93.09  ? 318 MET   A O   1 
ATOM   1999 C  CB  . MET   A 1 298 ? -15.467 -11.504 -20.113 1.00 90.64  ? 318 MET   A CB  1 
ATOM   2000 C  CG  . MET   A 1 298 ? -16.314 -10.821 -19.054 1.00 93.01  ? 318 MET   A CG  1 
ATOM   2001 S  SD  . MET   A 1 298 ? -17.394 -9.578  -19.787 1.00 115.57 ? 318 MET   A SD  1 
ATOM   2002 C  CE  . MET   A 1 298 ? -18.891 -9.835  -18.843 1.00 102.21 ? 318 MET   A CE  1 
ATOM   2003 N  N   . TYR   A 1 299 ? -14.824 -13.631 -22.504 1.00 92.94  ? 319 TYR   A N   1 
ATOM   2004 C  CA  . TYR   A 1 299 ? -14.049 -13.985 -23.689 1.00 95.48  ? 319 TYR   A CA  1 
ATOM   2005 C  C   . TYR   A 1 299 ? -14.939 -14.044 -24.923 1.00 92.93  ? 319 TYR   A C   1 
ATOM   2006 O  O   . TYR   A 1 299 ? -14.582 -13.526 -25.988 1.00 92.06  ? 319 TYR   A O   1 
ATOM   2007 C  CB  . TYR   A 1 299 ? -13.335 -15.321 -23.484 1.00 93.78  ? 319 TYR   A CB  1 
ATOM   2008 C  CG  . TYR   A 1 299 ? -12.714 -15.856 -24.755 1.00 95.42  ? 319 TYR   A CG  1 
ATOM   2009 C  CD1 . TYR   A 1 299 ? -11.485 -15.388 -25.200 1.00 98.38  ? 319 TYR   A CD1 1 
ATOM   2010 C  CD2 . TYR   A 1 299 ? -13.364 -16.820 -25.517 1.00 93.58  ? 319 TYR   A CD2 1 
ATOM   2011 C  CE1 . TYR   A 1 299 ? -10.917 -15.869 -26.365 1.00 101.29 ? 319 TYR   A CE1 1 
ATOM   2012 C  CE2 . TYR   A 1 299 ? -12.805 -17.305 -26.682 1.00 97.25  ? 319 TYR   A CE2 1 
ATOM   2013 C  CZ  . TYR   A 1 299 ? -11.584 -16.824 -27.102 1.00 101.75 ? 319 TYR   A CZ  1 
ATOM   2014 O  OH  . TYR   A 1 299 ? -11.021 -17.309 -28.260 1.00 110.13 ? 319 TYR   A OH  1 
ATOM   2015 N  N   . GLU   A 1 300 ? -16.111 -14.670 -24.797 1.00 90.73  ? 320 GLU   A N   1 
ATOM   2016 C  CA  . GLU   A 1 300 ? -17.023 -14.756 -25.932 1.00 91.66  ? 320 GLU   A CA  1 
ATOM   2017 C  C   . GLU   A 1 300 ? -17.632 -13.401 -26.269 1.00 90.48  ? 320 GLU   A C   1 
ATOM   2018 O  O   . GLU   A 1 300 ? -17.938 -13.137 -27.437 1.00 91.69  ? 320 GLU   A O   1 
ATOM   2019 C  CB  . GLU   A 1 300 ? -18.122 -15.782 -25.649 1.00 88.67  ? 320 GLU   A CB  1 
ATOM   2020 C  CG  . GLU   A 1 300 ? -17.604 -17.196 -25.426 1.00 88.85  ? 320 GLU   A CG  1 
ATOM   2021 C  CD  . GLU   A 1 300 ? -16.952 -17.788 -26.663 1.00 90.08  ? 320 GLU   A CD  1 
ATOM   2022 O  OE1 . GLU   A 1 300 ? -17.250 -17.319 -27.782 1.00 81.92  ? 320 GLU   A OE1 1 
ATOM   2023 O  OE2 . GLU   A 1 300 ? -16.140 -18.725 -26.517 1.00 92.50  ? 320 GLU   A OE2 1 
ATOM   2024 N  N   . LEU   A 1 301 ? -17.813 -12.533 -25.272 1.00 89.88  ? 321 LEU   A N   1 
ATOM   2025 C  CA  . LEU   A 1 301 ? -18.335 -11.199 -25.549 1.00 97.10  ? 321 LEU   A CA  1 
ATOM   2026 C  C   . LEU   A 1 301 ? -17.304 -10.343 -26.274 1.00 93.47  ? 321 LEU   A C   1 
ATOM   2027 O  O   . LEU   A 1 301 ? -17.656 -9.550  -27.154 1.00 96.42  ? 321 LEU   A O   1 
ATOM   2028 C  CB  . LEU   A 1 301 ? -18.778 -10.525 -24.251 1.00 97.56  ? 321 LEU   A CB  1 
ATOM   2029 C  CG  . LEU   A 1 301 ? -19.971 -11.155 -23.531 1.00 94.29  ? 321 LEU   A CG  1 
ATOM   2030 C  CD1 . LEU   A 1 301 ? -20.293 -10.390 -22.258 1.00 99.25  ? 321 LEU   A CD1 1 
ATOM   2031 C  CD2 . LEU   A 1 301 ? -21.183 -11.216 -24.447 1.00 90.78  ? 321 LEU   A CD2 1 
ATOM   2032 N  N   . ALA   A 1 302 ? -16.026 -10.493 -25.922 1.00 97.76  ? 322 ALA   A N   1 
ATOM   2033 C  CA  . ALA   A 1 302 ? -14.984 -9.726  -26.597 1.00 97.97  ? 322 ALA   A CA  1 
ATOM   2034 C  C   . ALA   A 1 302 ? -14.791 -10.199 -28.033 1.00 95.55  ? 322 ALA   A C   1 
ATOM   2035 O  O   . ALA   A 1 302 ? -14.591 -9.381  -28.939 1.00 105.17 ? 322 ALA   A O   1 
ATOM   2036 C  CB  . ALA   A 1 302 ? -13.673 -9.821  -25.820 1.00 104.04 ? 322 ALA   A CB  1 
ATOM   2037 N  N   . THR   A 1 303 ? -14.847 -11.510 -28.261 1.00 93.08  ? 323 THR   A N   1 
ATOM   2038 C  CA  . THR   A 1 303 ? -14.673 -12.065 -29.598 1.00 93.93  ? 323 THR   A CA  1 
ATOM   2039 C  C   . THR   A 1 303 ? -15.945 -12.013 -30.434 1.00 92.35  ? 323 THR   A C   1 
ATOM   2040 O  O   . THR   A 1 303 ? -15.912 -12.403 -31.607 1.00 93.90  ? 323 THR   A O   1 
ATOM   2041 C  CB  . THR   A 1 303 ? -14.175 -13.510 -29.512 1.00 99.33  ? 323 THR   A CB  1 
ATOM   2042 O  OG1 . THR   A 1 303 ? -15.076 -14.284 -28.711 1.00 93.17  ? 323 THR   A OG1 1 
ATOM   2043 C  CG2 . THR   A 1 303 ? -12.784 -13.558 -28.893 1.00 101.16 ? 323 THR   A CG2 1 
ATOM   2044 N  N   . HIS   A 1 304 ? -17.055 -11.546 -29.864 1.00 88.48  ? 324 HIS   A N   1 
ATOM   2045 C  CA  . HIS   A 1 304 ? -18.318 -11.375 -30.580 1.00 95.64  ? 324 HIS   A CA  1 
ATOM   2046 C  C   . HIS   A 1 304 ? -18.888 -10.013 -30.208 1.00 99.23  ? 324 HIS   A C   1 
ATOM   2047 O  O   . HIS   A 1 304 ? -19.762 -9.908  -29.336 1.00 95.21  ? 324 HIS   A O   1 
ATOM   2048 C  CB  . HIS   A 1 304 ? -19.303 -12.498 -30.255 1.00 91.10  ? 324 HIS   A CB  1 
ATOM   2049 C  CG  . HIS   A 1 304 ? -18.798 -13.861 -30.610 1.00 93.22  ? 324 HIS   A CG  1 
ATOM   2050 N  ND1 . HIS   A 1 304 ? -17.896 -14.548 -29.827 1.00 92.02  ? 324 HIS   A ND1 1 
ATOM   2051 C  CD2 . HIS   A 1 304 ? -19.067 -14.662 -31.667 1.00 95.07  ? 324 HIS   A CD2 1 
ATOM   2052 C  CE1 . HIS   A 1 304 ? -17.634 -15.717 -30.386 1.00 94.36  ? 324 HIS   A CE1 1 
ATOM   2053 N  NE2 . HIS   A 1 304 ? -18.332 -15.810 -31.503 1.00 95.73  ? 324 HIS   A NE2 1 
ATOM   2054 N  N   . PRO   A 1 305 ? -18.410 -8.944  -30.850 1.00 91.09  ? 325 PRO   A N   1 
ATOM   2055 C  CA  . PRO   A 1 305 ? -18.896 -7.597  -30.500 1.00 98.23  ? 325 PRO   A CA  1 
ATOM   2056 C  C   . PRO   A 1 305 ? -20.387 -7.412  -30.708 1.00 96.84  ? 325 PRO   A C   1 
ATOM   2057 O  O   . PRO   A 1 305 ? -21.011 -6.657  -29.955 1.00 97.58  ? 325 PRO   A O   1 
ATOM   2058 C  CB  . PRO   A 1 305 ? -18.081 -6.684  -31.427 1.00 92.02  ? 325 PRO   A CB  1 
ATOM   2059 C  CG  . PRO   A 1 305 ? -16.844 -7.477  -31.738 1.00 96.40  ? 325 PRO   A CG  1 
ATOM   2060 C  CD  . PRO   A 1 305 ? -17.290 -8.903  -31.806 1.00 102.49 ? 325 PRO   A CD  1 
ATOM   2061 N  N   . ASP   A 1 306 ? -20.980 -8.078  -31.704 1.00 99.11  ? 326 ASP   A N   1 
ATOM   2062 C  CA  . ASP   A 1 306 ? -22.415 -7.940  -31.928 1.00 90.76  ? 326 ASP   A CA  1 
ATOM   2063 C  C   . ASP   A 1 306 ? -23.212 -8.490  -30.751 1.00 100.14 ? 326 ASP   A C   1 
ATOM   2064 O  O   . ASP   A 1 306 ? -24.239 -7.919  -30.365 1.00 103.31 ? 326 ASP   A O   1 
ATOM   2065 C  CB  . ASP   A 1 306 ? -22.815 -8.638  -33.228 1.00 96.74  ? 326 ASP   A CB  1 
ATOM   2066 C  CG  . ASP   A 1 306 ? -22.435 -10.110 -33.249 1.00 102.84 ? 326 ASP   A CG  1 
ATOM   2067 O  OD1 . ASP   A 1 306 ? -21.703 -10.558 -32.341 1.00 93.64  ? 326 ASP   A OD1 1 
ATOM   2068 O  OD2 . ASP   A 1 306 ? -22.874 -10.821 -34.179 1.00 108.71 ? 326 ASP   A OD2 1 
ATOM   2069 N  N   . VAL   A 1 307 ? -22.753 -9.598  -30.166 1.00 93.29  ? 327 VAL   A N   1 
ATOM   2070 C  CA  . VAL   A 1 307 ? -23.436 -10.161 -29.006 1.00 95.05  ? 327 VAL   A CA  1 
ATOM   2071 C  C   . VAL   A 1 307 ? -23.201 -9.293  -27.777 1.00 89.44  ? 327 VAL   A C   1 
ATOM   2072 O  O   . VAL   A 1 307 ? -24.126 -9.028  -27.000 1.00 95.32  ? 327 VAL   A O   1 
ATOM   2073 C  CB  . VAL   A 1 307 ? -22.983 -11.614 -28.775 1.00 92.42  ? 327 VAL   A CB  1 
ATOM   2074 C  CG1 . VAL   A 1 307 ? -23.537 -12.144 -27.461 1.00 93.47  ? 327 VAL   A CG1 1 
ATOM   2075 C  CG2 . VAL   A 1 307 ? -23.421 -12.495 -29.934 1.00 85.75  ? 327 VAL   A CG2 1 
ATOM   2076 N  N   . GLN   A 1 308 ? -21.963 -8.831  -27.584 1.00 92.21  ? 328 GLN   A N   1 
ATOM   2077 C  CA  . GLN   A 1 308 ? -21.666 -7.948  -26.460 1.00 97.81  ? 328 GLN   A CA  1 
ATOM   2078 C  C   . GLN   A 1 308 ? -22.420 -6.629  -26.578 1.00 101.60 ? 328 GLN   A C   1 
ATOM   2079 O  O   . GLN   A 1 308 ? -22.857 -6.063  -25.569 1.00 94.51  ? 328 GLN   A O   1 
ATOM   2080 C  CB  . GLN   A 1 308 ? -20.160 -7.701  -26.377 1.00 98.56  ? 328 GLN   A CB  1 
ATOM   2081 C  CG  . GLN   A 1 308 ? -19.735 -6.798  -25.230 1.00 102.19 ? 328 GLN   A CG  1 
ATOM   2082 C  CD  . GLN   A 1 308 ? -18.249 -6.491  -25.246 1.00 105.68 ? 328 GLN   A CD  1 
ATOM   2083 O  OE1 . GLN   A 1 308 ? -17.742 -5.769  -24.387 1.00 119.77 ? 328 GLN   A OE1 1 
ATOM   2084 N  NE2 . GLN   A 1 308 ? -17.542 -7.040  -26.227 1.00 102.46 ? 328 GLN   A NE2 1 
ATOM   2085 N  N   . GLN   A 1 309 ? -22.581 -6.122  -27.802 1.00 94.18  ? 329 GLN   A N   1 
ATOM   2086 C  CA  . GLN   A 1 309 ? -23.311 -4.875  -28.002 1.00 104.00 ? 329 GLN   A CA  1 
ATOM   2087 C  C   . GLN   A 1 309 ? -24.812 -5.069  -27.833 1.00 107.70 ? 329 GLN   A C   1 
ATOM   2088 O  O   . GLN   A 1 309 ? -25.475 -4.251  -27.185 1.00 100.24 ? 329 GLN   A O   1 
ATOM   2089 C  CB  . GLN   A 1 309 ? -22.999 -4.295  -29.383 1.00 99.53  ? 329 GLN   A CB  1 
ATOM   2090 C  CG  . GLN   A 1 309 ? -24.192 -3.646  -30.064 1.00 107.02 ? 329 GLN   A CG  1 
ATOM   2091 C  CD  . GLN   A 1 309 ? -23.838 -2.353  -30.755 1.00 102.63 ? 329 GLN   A CD  1 
ATOM   2092 O  OE1 . GLN   A 1 309 ? -22.673 -1.960  -30.808 1.00 103.70 ? 329 GLN   A OE1 1 
ATOM   2093 N  NE2 . GLN   A 1 309 ? -24.848 -1.675  -31.285 1.00 108.25 ? 329 GLN   A NE2 1 
ATOM   2094 N  N   . LYS   A 1 310 ? -25.366 -6.141  -28.409 1.00 104.24 ? 330 LYS   A N   1 
ATOM   2095 C  CA  . LYS   A 1 310 ? -26.793 -6.398  -28.254 1.00 105.55 ? 330 LYS   A CA  1 
ATOM   2096 C  C   . LYS   A 1 310 ? -27.148 -6.668  -26.800 1.00 102.52 ? 330 LYS   A C   1 
ATOM   2097 O  O   . LYS   A 1 310 ? -28.247 -6.320  -26.353 1.00 106.29 ? 330 LYS   A O   1 
ATOM   2098 C  CB  . LYS   A 1 310 ? -27.221 -7.573  -29.134 1.00 110.24 ? 330 LYS   A CB  1 
ATOM   2099 C  CG  . LYS   A 1 310 ? -28.726 -7.792  -29.174 1.00 109.56 ? 330 LYS   A CG  1 
ATOM   2100 C  CD  . LYS   A 1 310 ? -29.088 -9.061  -29.927 1.00 110.38 ? 330 LYS   A CD  1 
ATOM   2101 C  CE  . LYS   A 1 310 ? -30.592 -9.282  -29.928 1.00 115.21 ? 330 LYS   A CE  1 
ATOM   2102 N  NZ  . LYS   A 1 310 ? -30.966 -10.583 -30.550 1.00 121.53 ? 330 LYS   A NZ  1 
ATOM   2103 N  N   . LEU   A 1 311 ? -26.231 -7.277  -26.046 1.00 102.93 ? 331 LEU   A N   1 
ATOM   2104 C  CA  . LEU   A 1 311 ? -26.474 -7.489  -24.625 1.00 103.80 ? 331 LEU   A CA  1 
ATOM   2105 C  C   . LEU   A 1 311 ? -26.419 -6.175  -23.856 1.00 103.34 ? 331 LEU   A C   1 
ATOM   2106 O  O   . LEU   A 1 311 ? -27.261 -5.925  -22.987 1.00 104.34 ? 331 LEU   A O   1 
ATOM   2107 C  CB  . LEU   A 1 311 ? -25.464 -8.488  -24.062 1.00 96.89  ? 331 LEU   A CB  1 
ATOM   2108 C  CG  . LEU   A 1 311 ? -25.641 -8.824  -22.582 1.00 95.48  ? 331 LEU   A CG  1 
ATOM   2109 C  CD1 . LEU   A 1 311 ? -27.076 -9.238  -22.307 1.00 94.47  ? 331 LEU   A CD1 1 
ATOM   2110 C  CD2 . LEU   A 1 311 ? -24.675 -9.917  -22.160 1.00 97.27  ? 331 LEU   A CD2 1 
ATOM   2111 N  N   . GLN   A 1 312 ? -25.441 -5.319  -24.167 1.00 103.59 ? 332 GLN   A N   1 
ATOM   2112 C  CA  . GLN   A 1 312 ? -25.355 -4.025  -23.495 1.00 105.86 ? 332 GLN   A CA  1 
ATOM   2113 C  C   . GLN   A 1 312 ? -26.578 -3.163  -23.780 1.00 107.08 ? 332 GLN   A C   1 
ATOM   2114 O  O   . GLN   A 1 312 ? -26.978 -2.357  -22.932 1.00 107.32 ? 332 GLN   A O   1 
ATOM   2115 C  CB  . GLN   A 1 312 ? -24.075 -3.299  -23.910 1.00 99.09  ? 332 GLN   A CB  1 
ATOM   2116 C  CG  . GLN   A 1 312 ? -22.833 -3.767  -23.160 1.00 108.83 ? 332 GLN   A CG  1 
ATOM   2117 C  CD  . GLN   A 1 312 ? -21.553 -3.205  -23.744 1.00 106.37 ? 332 GLN   A CD  1 
ATOM   2118 O  OE1 . GLN   A 1 312 ? -21.545 -2.675  -24.855 1.00 107.02 ? 332 GLN   A OE1 1 
ATOM   2119 N  NE2 . GLN   A 1 312 ? -20.459 -3.319  -22.998 1.00 111.07 ? 332 GLN   A NE2 1 
ATOM   2120 N  N   . GLU   A 1 313 ? -27.185 -3.316  -24.961 1.00 102.98 ? 333 GLU   A N   1 
ATOM   2121 C  CA  . GLU   A 1 313 ? -28.453 -2.644  -25.227 1.00 110.11 ? 333 GLU   A CA  1 
ATOM   2122 C  C   . GLU   A 1 313 ? -29.552 -3.175  -24.317 1.00 112.99 ? 333 GLU   A C   1 
ATOM   2123 O  O   . GLU   A 1 313 ? -30.411 -2.413  -23.856 1.00 112.24 ? 333 GLU   A O   1 
ATOM   2124 C  CB  . GLU   A 1 313 ? -28.851 -2.824  -26.692 1.00 103.50 ? 333 GLU   A CB  1 
ATOM   2125 C  CG  . GLU   A 1 313 ? -27.924 -2.160  -27.693 1.00 111.82 ? 333 GLU   A CG  1 
ATOM   2126 C  CD  . GLU   A 1 313 ? -28.288 -2.498  -29.126 1.00 110.86 ? 333 GLU   A CD  1 
ATOM   2127 O  OE1 . GLU   A 1 313 ? -28.979 -3.517  -29.341 1.00 110.00 ? 333 GLU   A OE1 1 
ATOM   2128 O  OE2 . GLU   A 1 313 ? -27.887 -1.744  -30.037 1.00 108.65 ? 333 GLU   A OE2 1 
ATOM   2129 N  N   . GLU   A 1 314 ? -29.540 -4.484  -24.052 1.00 111.58 ? 334 GLU   A N   1 
ATOM   2130 C  CA  . GLU   A 1 314 ? -30.559 -5.088  -23.198 1.00 109.15 ? 334 GLU   A CA  1 
ATOM   2131 C  C   . GLU   A 1 314 ? -30.498 -4.529  -21.783 1.00 113.65 ? 334 GLU   A C   1 
ATOM   2132 O  O   . GLU   A 1 314 ? -31.537 -4.308  -21.149 1.00 118.33 ? 334 GLU   A O   1 
ATOM   2133 C  CB  . GLU   A 1 314 ? -30.388 -6.608  -23.187 1.00 114.04 ? 334 GLU   A CB  1 
ATOM   2134 C  CG  . GLU   A 1 314 ? -31.220 -7.337  -22.144 1.00 113.28 ? 334 GLU   A CG  1 
ATOM   2135 C  CD  . GLU   A 1 314 ? -32.316 -8.183  -22.759 1.00 112.35 ? 334 GLU   A CD  1 
ATOM   2136 O  OE1 . GLU   A 1 314 ? -33.074 -7.657  -23.601 1.00 115.19 ? 334 GLU   A OE1 1 
ATOM   2137 O  OE2 . GLU   A 1 314 ? -32.413 -9.378  -22.408 1.00 108.22 ? 334 GLU   A OE2 1 
ATOM   2138 N  N   . ILE   A 1 315 ? -29.289 -4.287  -21.271 1.00 109.70 ? 335 ILE   A N   1 
ATOM   2139 C  CA  . ILE   A 1 315 ? -29.163 -3.788  -19.906 1.00 112.38 ? 335 ILE   A CA  1 
ATOM   2140 C  C   . ILE   A 1 315 ? -29.575 -2.326  -19.823 1.00 121.91 ? 335 ILE   A C   1 
ATOM   2141 O  O   . ILE   A 1 315 ? -30.105 -1.880  -18.797 1.00 126.41 ? 335 ILE   A O   1 
ATOM   2142 C  CB  . ILE   A 1 315 ? -27.729 -3.989  -19.386 1.00 113.53 ? 335 ILE   A CB  1 
ATOM   2143 C  CG1 . ILE   A 1 315 ? -27.133 -5.284  -19.936 1.00 118.39 ? 335 ILE   A CG1 1 
ATOM   2144 C  CG2 . ILE   A 1 315 ? -27.731 -4.022  -17.874 1.00 118.50 ? 335 ILE   A CG2 1 
ATOM   2145 C  CD1 . ILE   A 1 315 ? -25.815 -5.672  -19.305 1.00 112.27 ? 335 ILE   A CD1 1 
ATOM   2146 N  N   . ASP   A 1 316 ? -29.335 -1.553  -20.883 1.00 112.74 ? 336 ASP   A N   1 
ATOM   2147 C  CA  . ASP   A 1 316 ? -29.708 -0.144  -20.858 1.00 122.72 ? 336 ASP   A CA  1 
ATOM   2148 C  C   . ASP   A 1 316 ? -31.221 0.033   -20.846 1.00 122.71 ? 336 ASP   A C   1 
ATOM   2149 O  O   . ASP   A 1 316 ? -31.735 0.935   -20.173 1.00 130.44 ? 336 ASP   A O   1 
ATOM   2150 C  CB  . ASP   A 1 316 ? -29.098 0.590   -22.053 1.00 116.63 ? 336 ASP   A CB  1 
ATOM   2151 C  CG  . ASP   A 1 316 ? -27.600 0.750   -21.936 1.00 112.66 ? 336 ASP   A CG  1 
ATOM   2152 O  OD1 . ASP   A 1 316 ? -27.095 0.793   -20.794 1.00 120.02 ? 336 ASP   A OD1 1 
ATOM   2153 O  OD2 . ASP   A 1 316 ? -26.926 0.839   -22.984 1.00 110.72 ? 336 ASP   A OD2 1 
ATOM   2154 N  N   . ALA   A 1 317 ? -31.952 -0.810  -21.583 1.00 127.69 ? 337 ALA   A N   1 
ATOM   2155 C  CA  . ALA   A 1 317 ? -33.398 -0.633  -21.676 1.00 128.80 ? 337 ALA   A CA  1 
ATOM   2156 C  C   . ALA   A 1 317 ? -34.090 -1.052  -20.382 1.00 131.84 ? 337 ALA   A C   1 
ATOM   2157 O  O   . ALA   A 1 317 ? -34.756 -0.243  -19.727 1.00 134.24 ? 337 ALA   A O   1 
ATOM   2158 C  CB  . ALA   A 1 317 ? -33.950 -1.418  -22.867 1.00 128.90 ? 337 ALA   A CB  1 
ATOM   2159 N  N   . VAL   A 1 318 ? -33.933 -2.319  -19.995 1.00 131.22 ? 338 VAL   A N   1 
ATOM   2160 C  CA  . VAL   A 1 318 ? -34.602 -2.833  -18.802 1.00 135.12 ? 338 VAL   A CA  1 
ATOM   2161 C  C   . VAL   A 1 318 ? -34.174 -2.048  -17.568 1.00 132.62 ? 338 VAL   A C   1 
ATOM   2162 O  O   . VAL   A 1 318 ? -34.997 -1.730  -16.702 1.00 133.62 ? 338 VAL   A O   1 
ATOM   2163 C  CB  . VAL   A 1 318 ? -34.329 -4.343  -18.647 1.00 134.53 ? 338 VAL   A CB  1 
ATOM   2164 C  CG1 . VAL   A 1 318 ? -34.404 -4.766  -17.181 1.00 135.42 ? 338 VAL   A CG1 1 
ATOM   2165 C  CG2 . VAL   A 1 318 ? -35.324 -5.140  -19.476 1.00 137.95 ? 338 VAL   A CG2 1 
ATOM   2166 N  N   . LEU   A 1 319 ? -32.887 -1.721  -17.469 1.00 128.50 ? 339 LEU   A N   1 
ATOM   2167 C  CA  . LEU   A 1 319 ? -32.384 -0.897  -16.377 1.00 131.66 ? 339 LEU   A CA  1 
ATOM   2168 C  C   . LEU   A 1 319 ? -31.965 0.462   -16.925 1.00 138.53 ? 339 LEU   A C   1 
ATOM   2169 O  O   . LEU   A 1 319 ? -30.787 0.668   -17.245 1.00 138.90 ? 339 LEU   A O   1 
ATOM   2170 C  CB  . LEU   A 1 319 ? -31.212 -1.584  -15.676 1.00 131.62 ? 339 LEU   A CB  1 
ATOM   2171 C  CG  . LEU   A 1 319 ? -31.534 -2.886  -14.939 1.00 132.73 ? 339 LEU   A CG  1 
ATOM   2172 C  CD1 . LEU   A 1 319 ? -30.636 -4.016  -15.414 1.00 122.49 ? 339 LEU   A CD1 1 
ATOM   2173 C  CD2 . LEU   A 1 319 ? -31.396 -2.689  -13.439 1.00 129.65 ? 339 LEU   A CD2 1 
ATOM   2174 N  N   . PRO   A 1 320 ? -32.895 1.407   -17.053 1.00 135.21 ? 340 PRO   A N   1 
ATOM   2175 C  CA  . PRO   A 1 320 ? -32.548 2.705   -17.637 1.00 141.03 ? 340 PRO   A CA  1 
ATOM   2176 C  C   . PRO   A 1 320 ? -31.735 3.555   -16.675 1.00 142.41 ? 340 PRO   A C   1 
ATOM   2177 O  O   . PRO   A 1 320 ? -31.856 3.441   -15.453 1.00 151.65 ? 340 PRO   A O   1 
ATOM   2178 C  CB  . PRO   A 1 320 ? -33.913 3.338   -17.921 1.00 134.41 ? 340 PRO   A CB  1 
ATOM   2179 C  CG  . PRO   A 1 320 ? -34.805 2.747   -16.883 1.00 139.23 ? 340 PRO   A CG  1 
ATOM   2180 C  CD  . PRO   A 1 320 ? -34.312 1.340   -16.657 1.00 136.04 ? 340 PRO   A CD  1 
ATOM   2181 N  N   . ASN   A 1 321 ? -30.894 4.415   -17.253 1.00 142.29 ? 341 ASN   A N   1 
ATOM   2182 C  CA  . ASN   A 1 321 ? -30.038 5.326   -16.492 1.00 151.32 ? 341 ASN   A CA  1 
ATOM   2183 C  C   . ASN   A 1 321 ? -29.111 4.569   -15.544 1.00 143.06 ? 341 ASN   A C   1 
ATOM   2184 O  O   . ASN   A 1 321 ? -28.737 5.083   -14.487 1.00 140.81 ? 341 ASN   A O   1 
ATOM   2185 C  CB  . ASN   A 1 321 ? -30.870 6.354   -15.719 1.00 147.10 ? 341 ASN   A CB  1 
ATOM   2186 C  CG  . ASN   A 1 321 ? -32.064 6.853   -16.510 1.00 141.57 ? 341 ASN   A CG  1 
ATOM   2187 O  OD1 . ASN   A 1 321 ? -32.026 6.919   -17.739 1.00 146.48 ? 341 ASN   A OD1 1 
ATOM   2188 N  ND2 . ASN   A 1 321 ? -33.135 7.202   -15.807 1.00 141.38 ? 341 ASN   A ND2 1 
ATOM   2189 N  N   . LYS   A 1 322 ? -28.735 3.348   -15.926 1.00 144.90 ? 342 LYS   A N   1 
ATOM   2190 C  CA  . LYS   A 1 322 ? -27.934 2.458   -15.085 1.00 143.76 ? 342 LYS   A CA  1 
ATOM   2191 C  C   . LYS   A 1 322 ? -28.548 2.319   -13.694 1.00 149.36 ? 342 LYS   A C   1 
ATOM   2192 O  O   . LYS   A 1 322 ? -27.894 2.525   -12.669 1.00 153.73 ? 342 LYS   A O   1 
ATOM   2193 C  CB  . LYS   A 1 322 ? -26.480 2.929   -15.008 1.00 145.81 ? 342 LYS   A CB  1 
ATOM   2194 C  CG  . LYS   A 1 322 ? -25.629 2.441   -16.169 1.00 145.93 ? 342 LYS   A CG  1 
ATOM   2195 C  CD  . LYS   A 1 322 ? -24.143 2.636   -15.917 1.00 144.39 ? 342 LYS   A CD  1 
ATOM   2196 C  CE  . LYS   A 1 322 ? -23.627 3.901   -16.581 1.00 142.45 ? 342 LYS   A CE  1 
ATOM   2197 N  NZ  . LYS   A 1 322 ? -22.185 3.778   -16.941 1.00 141.32 ? 342 LYS   A NZ  1 
ATOM   2198 N  N   . ALA   A 1 323 ? -29.833 1.971   -13.671 1.00 150.15 ? 343 ALA   A N   1 
ATOM   2199 C  CA  . ALA   A 1 323 ? -30.535 1.770   -12.415 1.00 150.62 ? 343 ALA   A CA  1 
ATOM   2200 C  C   . ALA   A 1 323 ? -29.900 0.614   -11.642 1.00 147.21 ? 343 ALA   A C   1 
ATOM   2201 O  O   . ALA   A 1 323 ? -29.348 -0.312  -12.243 1.00 142.82 ? 343 ALA   A O   1 
ATOM   2202 C  CB  . ALA   A 1 323 ? -32.014 1.487   -12.672 1.00 144.92 ? 343 ALA   A CB  1 
ATOM   2203 N  N   . PRO   A 1 324 ? -29.947 0.651   -10.312 1.00 137.03 ? 344 PRO   A N   1 
ATOM   2204 C  CA  . PRO   A 1 324 ? -29.324 -0.413  -9.514  1.00 136.51 ? 344 PRO   A CA  1 
ATOM   2205 C  C   . PRO   A 1 324 ? -29.944 -1.764  -9.820  1.00 134.70 ? 344 PRO   A C   1 
ATOM   2206 O  O   . PRO   A 1 324 ? -31.176 -1.896  -9.868  1.00 133.83 ? 344 PRO   A O   1 
ATOM   2207 C  CB  . PRO   A 1 324 ? -29.609 0.016   -8.067  1.00 137.48 ? 344 PRO   A CB  1 
ATOM   2208 C  CG  . PRO   A 1 324 ? -29.805 1.488   -8.143  1.00 140.17 ? 344 PRO   A CG  1 
ATOM   2209 C  CD  . PRO   A 1 324 ? -30.473 1.737   -9.466  1.00 139.65 ? 344 PRO   A CD  1 
ATOM   2210 N  N   . PRO   A 1 325 ? -29.123 -2.790  -10.042 1.00 136.81 ? 345 PRO   A N   1 
ATOM   2211 C  CA  . PRO   A 1 325 ? -29.661 -4.126  -10.346 1.00 137.04 ? 345 PRO   A CA  1 
ATOM   2212 C  C   . PRO   A 1 325 ? -30.395 -4.699  -9.143  1.00 141.12 ? 345 PRO   A C   1 
ATOM   2213 O  O   . PRO   A 1 325 ? -29.814 -4.870  -8.069  1.00 145.60 ? 345 PRO   A O   1 
ATOM   2214 C  CB  . PRO   A 1 325 ? -28.410 -4.945  -10.690 1.00 136.32 ? 345 PRO   A CB  1 
ATOM   2215 C  CG  . PRO   A 1 325 ? -27.349 -3.932  -11.000 1.00 139.81 ? 345 PRO   A CG  1 
ATOM   2216 C  CD  . PRO   A 1 325 ? -27.654 -2.755  -10.129 1.00 139.73 ? 345 PRO   A CD  1 
ATOM   2217 N  N   . THR   A 1 326 ? -31.679 -4.990  -9.327  1.00 140.59 ? 346 THR   A N   1 
ATOM   2218 C  CA  . THR   A 1 326 ? -32.500 -5.594  -8.293  1.00 142.31 ? 346 THR   A CA  1 
ATOM   2219 C  C   . THR   A 1 326 ? -32.651 -7.090  -8.562  1.00 143.60 ? 346 THR   A C   1 
ATOM   2220 O  O   . THR   A 1 326 ? -32.107 -7.637  -9.524  1.00 143.64 ? 346 THR   A O   1 
ATOM   2221 C  CB  . THR   A 1 326 ? -33.865 -4.908  -8.218  1.00 133.05 ? 346 THR   A CB  1 
ATOM   2222 O  OG1 . THR   A 1 326 ? -34.544 -5.049  -9.472  1.00 134.63 ? 346 THR   A OG1 1 
ATOM   2223 C  CG2 . THR   A 1 326 ? -33.702 -3.428  -7.898  1.00 137.96 ? 346 THR   A CG2 1 
ATOM   2224 N  N   . TYR   A 1 327 ? -33.409 -7.761  -7.692  1.00 152.23 ? 347 TYR   A N   1 
ATOM   2225 C  CA  . TYR   A 1 327 ? -33.604 -9.199  -7.846  1.00 156.38 ? 347 TYR   A CA  1 
ATOM   2226 C  C   . TYR   A 1 327 ? -34.530 -9.520  -9.011  1.00 152.56 ? 347 TYR   A C   1 
ATOM   2227 O  O   . TYR   A 1 327 ? -34.427 -10.601 -9.601  1.00 153.86 ? 347 TYR   A O   1 
ATOM   2228 C  CB  . TYR   A 1 327 ? -34.151 -9.794  -6.548  1.00 159.16 ? 347 TYR   A CB  1 
ATOM   2229 C  CG  . TYR   A 1 327 ? -34.323 -11.297 -6.577  1.00 155.86 ? 347 TYR   A CG  1 
ATOM   2230 C  CD1 . TYR   A 1 327 ? -33.256 -12.143 -6.305  1.00 153.89 ? 347 TYR   A CD1 1 
ATOM   2231 C  CD2 . TYR   A 1 327 ? -35.555 -11.870 -6.868  1.00 151.83 ? 347 TYR   A CD2 1 
ATOM   2232 C  CE1 . TYR   A 1 327 ? -33.409 -13.517 -6.328  1.00 156.46 ? 347 TYR   A CE1 1 
ATOM   2233 C  CE2 . TYR   A 1 327 ? -35.718 -13.242 -6.891  1.00 154.79 ? 347 TYR   A CE2 1 
ATOM   2234 C  CZ  . TYR   A 1 327 ? -34.642 -14.061 -6.621  1.00 160.81 ? 347 TYR   A CZ  1 
ATOM   2235 O  OH  . TYR   A 1 327 ? -34.799 -15.428 -6.645  1.00 163.08 ? 347 TYR   A OH  1 
ATOM   2236 N  N   . ASP   A 1 328 ? -35.429 -8.600  -9.364  1.00 141.28 ? 348 ASP   A N   1 
ATOM   2237 C  CA  . ASP   A 1 328 ? -36.405 -8.853  -10.417 1.00 139.12 ? 348 ASP   A CA  1 
ATOM   2238 C  C   . ASP   A 1 328 ? -35.965 -8.354  -11.788 1.00 138.77 ? 348 ASP   A C   1 
ATOM   2239 O  O   . ASP   A 1 328 ? -36.497 -8.826  -12.801 1.00 138.97 ? 348 ASP   A O   1 
ATOM   2240 C  CB  . ASP   A 1 328 ? -37.751 -8.219  -10.049 1.00 140.87 ? 348 ASP   A CB  1 
ATOM   2241 C  CG  . ASP   A 1 328 ? -38.469 -8.979  -8.948  1.00 142.72 ? 348 ASP   A CG  1 
ATOM   2242 O  OD1 . ASP   A 1 328 ? -38.017 -8.917  -7.785  1.00 143.18 ? 348 ASP   A OD1 1 
ATOM   2243 O  OD2 . ASP   A 1 328 ? -39.483 -9.645  -9.248  1.00 145.45 ? 348 ASP   A OD2 1 
ATOM   2244 N  N   . THR   A 1 329 ? -35.014 -7.416  -11.852 1.00 135.34 ? 349 THR   A N   1 
ATOM   2245 C  CA  . THR   A 1 329 ? -34.505 -6.969  -13.145 1.00 136.48 ? 349 THR   A CA  1 
ATOM   2246 C  C   . THR   A 1 329 ? -33.603 -8.014  -13.788 1.00 133.93 ? 349 THR   A C   1 
ATOM   2247 O  O   . THR   A 1 329 ? -33.556 -8.112  -15.020 1.00 133.11 ? 349 THR   A O   1 
ATOM   2248 C  CB  . THR   A 1 329 ? -33.751 -5.644  -13.000 1.00 134.40 ? 349 THR   A CB  1 
ATOM   2249 O  OG1 . THR   A 1 329 ? -33.291 -5.499  -11.650 1.00 132.28 ? 349 THR   A OG1 1 
ATOM   2250 C  CG2 . THR   A 1 329 ? -34.655 -4.469  -13.359 1.00 134.17 ? 349 THR   A CG2 1 
ATOM   2251 N  N   . VAL   A 1 330 ? -32.887 -8.795  -12.976 1.00 129.54 ? 350 VAL   A N   1 
ATOM   2252 C  CA  . VAL   A 1 330 ? -32.051 -9.866  -13.513 1.00 129.15 ? 350 VAL   A CA  1 
ATOM   2253 C  C   . VAL   A 1 330 ? -32.913 -10.940 -14.158 1.00 131.39 ? 350 VAL   A C   1 
ATOM   2254 O  O   . VAL   A 1 330 ? -32.598 -11.446 -15.242 1.00 127.18 ? 350 VAL   A O   1 
ATOM   2255 C  CB  . VAL   A 1 330 ? -31.163 -10.457 -12.403 1.00 124.76 ? 350 VAL   A CB  1 
ATOM   2256 C  CG1 . VAL   A 1 330 ? -30.462 -11.711 -12.896 1.00 116.35 ? 350 VAL   A CG1 1 
ATOM   2257 C  CG2 . VAL   A 1 330 ? -30.159 -9.429  -11.915 1.00 120.30 ? 350 VAL   A CG2 1 
ATOM   2258 N  N   . LEU   A 1 331 ? -34.025 -11.288 -13.511 1.00 134.56 ? 351 LEU   A N   1 
ATOM   2259 C  CA  . LEU   A 1 331 ? -34.852 -12.418 -13.914 1.00 137.06 ? 351 LEU   A CA  1 
ATOM   2260 C  C   . LEU   A 1 331 ? -35.643 -12.173 -15.193 1.00 140.16 ? 351 LEU   A C   1 
ATOM   2261 O  O   . LEU   A 1 331 ? -36.366 -13.078 -15.624 1.00 138.72 ? 351 LEU   A O   1 
ATOM   2262 C  CB  . LEU   A 1 331 ? -35.813 -12.784 -12.781 1.00 137.62 ? 351 LEU   A CB  1 
ATOM   2263 C  CG  . LEU   A 1 331 ? -35.167 -13.177 -11.452 1.00 138.50 ? 351 LEU   A CG  1 
ATOM   2264 C  CD1 . LEU   A 1 331 ? -36.231 -13.374 -10.386 1.00 142.91 ? 351 LEU   A CD1 1 
ATOM   2265 C  CD2 . LEU   A 1 331 ? -34.325 -14.433 -11.612 1.00 129.14 ? 351 LEU   A CD2 1 
ATOM   2266 N  N   . GLN   A 1 332 ? -35.538 -10.995 -15.812 1.00 157.32 ? 352 GLN   A N   1 
ATOM   2267 C  CA  . GLN   A 1 332 ? -36.278 -10.711 -17.033 1.00 155.98 ? 352 GLN   A CA  1 
ATOM   2268 C  C   . GLN   A 1 332 ? -35.399 -10.396 -18.234 1.00 156.03 ? 352 GLN   A C   1 
ATOM   2269 O  O   . GLN   A 1 332 ? -35.898 -10.437 -19.363 1.00 156.91 ? 352 GLN   A O   1 
ATOM   2270 C  CB  . GLN   A 1 332 ? -37.253 -9.543  -16.815 1.00 153.41 ? 352 GLN   A CB  1 
ATOM   2271 C  CG  . GLN   A 1 332 ? -36.583 -8.217  -16.514 1.00 157.34 ? 352 GLN   A CG  1 
ATOM   2272 C  CD  . GLN   A 1 332 ? -37.587 -7.113  -16.259 1.00 165.62 ? 352 GLN   A CD  1 
ATOM   2273 O  OE1 . GLN   A 1 332 ? -37.246 -5.931  -16.266 1.00 173.76 ? 352 GLN   A OE1 1 
ATOM   2274 N  NE2 . GLN   A 1 332 ? -38.837 -7.496  -16.029 1.00 167.36 ? 352 GLN   A NE2 1 
ATOM   2275 N  N   . MET   A 1 333 ? -34.119 -10.089 -18.031 1.00 130.91 ? 353 MET   A N   1 
ATOM   2276 C  CA  . MET   A 1 333 ? -33.215 -9.854  -19.148 1.00 119.79 ? 353 MET   A CA  1 
ATOM   2277 C  C   . MET   A 1 333 ? -33.102 -11.212 -19.829 1.00 117.46 ? 353 MET   A C   1 
ATOM   2278 O  O   . MET   A 1 333 ? -32.406 -12.108 -19.342 1.00 112.65 ? 353 MET   A O   1 
ATOM   2279 C  CB  . MET   A 1 333 ? -31.895 -9.267  -18.650 1.00 116.57 ? 353 MET   A CB  1 
ATOM   2280 C  CG  . MET   A 1 333 ? -32.053 -7.888  -18.029 1.00 123.69 ? 353 MET   A CG  1 
ATOM   2281 S  SD  . MET   A 1 333 ? -30.481 -7.191  -17.510 1.00 122.90 ? 353 MET   A SD  1 
ATOM   2282 C  CE  . MET   A 1 333 ? -29.455 -7.674  -18.892 1.00 114.39 ? 353 MET   A CE  1 
ATOM   2283 N  N   . GLU   A 1 334 ? -33.788 -11.361 -20.964 1.00 115.61 ? 354 GLU   A N   1 
ATOM   2284 C  CA  . GLU   A 1 334 ? -33.836 -12.663 -21.623 1.00 110.30 ? 354 GLU   A CA  1 
ATOM   2285 C  C   . GLU   A 1 334 ? -32.546 -12.956 -22.380 1.00 104.16 ? 354 GLU   A C   1 
ATOM   2286 O  O   . GLU   A 1 334 ? -31.989 -14.056 -22.271 1.00 105.14 ? 354 GLU   A O   1 
ATOM   2287 C  CB  . GLU   A 1 334 ? -35.043 -12.723 -22.560 1.00 109.60 ? 354 GLU   A CB  1 
ATOM   2288 C  CG  . GLU   A 1 334 ? -35.400 -14.122 -23.022 1.00 111.98 ? 354 GLU   A CG  1 
ATOM   2289 C  CD  . GLU   A 1 334 ? -36.455 -14.121 -24.109 1.00 116.38 ? 354 GLU   A CD  1 
ATOM   2290 O  OE1 . GLU   A 1 334 ? -37.033 -13.047 -24.376 1.00 115.21 ? 354 GLU   A OE1 1 
ATOM   2291 O  OE2 . GLU   A 1 334 ? -36.701 -15.193 -24.700 1.00 118.76 ? 354 GLU   A OE2 1 
ATOM   2292 N  N   . TYR   A 1 335 ? -32.055 -11.987 -23.160 1.00 102.57 ? 355 TYR   A N   1 
ATOM   2293 C  CA  . TYR   A 1 335 ? -30.830 -12.208 -23.923 1.00 101.75 ? 355 TYR   A CA  1 
ATOM   2294 C  C   . TYR   A 1 335 ? -29.641 -12.457 -23.006 1.00 95.33  ? 355 TYR   A C   1 
ATOM   2295 O  O   . TYR   A 1 335 ? -28.734 -13.222 -23.357 1.00 90.70  ? 355 TYR   A O   1 
ATOM   2296 C  CB  . TYR   A 1 335 ? -30.557 -11.021 -24.849 1.00 98.15  ? 355 TYR   A CB  1 
ATOM   2297 C  CG  . TYR   A 1 335 ? -29.512 -11.303 -25.908 1.00 97.23  ? 355 TYR   A CG  1 
ATOM   2298 C  CD1 . TYR   A 1 335 ? -29.837 -12.010 -27.058 1.00 99.17  ? 355 TYR   A CD1 1 
ATOM   2299 C  CD2 . TYR   A 1 335 ? -28.205 -10.856 -25.761 1.00 92.95  ? 355 TYR   A CD2 1 
ATOM   2300 C  CE1 . TYR   A 1 335 ? -28.889 -12.270 -28.029 1.00 100.77 ? 355 TYR   A CE1 1 
ATOM   2301 C  CE2 . TYR   A 1 335 ? -27.248 -11.112 -26.729 1.00 95.32  ? 355 TYR   A CE2 1 
ATOM   2302 C  CZ  . TYR   A 1 335 ? -27.597 -11.819 -27.861 1.00 96.60  ? 355 TYR   A CZ  1 
ATOM   2303 O  OH  . TYR   A 1 335 ? -26.655 -12.080 -28.830 1.00 90.21  ? 355 TYR   A OH  1 
ATOM   2304 N  N   . LEU   A 1 336 ? -29.628 -11.823 -21.830 1.00 97.97  ? 356 LEU   A N   1 
ATOM   2305 C  CA  . LEU   A 1 336 ? -28.595 -12.124 -20.845 1.00 97.96  ? 356 LEU   A CA  1 
ATOM   2306 C  C   . LEU   A 1 336 ? -28.635 -13.592 -20.453 1.00 96.88  ? 356 LEU   A C   1 
ATOM   2307 O  O   . LEU   A 1 336 ? -27.591 -14.248 -20.355 1.00 90.38  ? 356 LEU   A O   1 
ATOM   2308 C  CB  . LEU   A 1 336 ? -28.766 -11.239 -19.611 1.00 100.22 ? 356 LEU   A CB  1 
ATOM   2309 C  CG  . LEU   A 1 336 ? -27.840 -11.550 -18.428 1.00 94.18  ? 356 LEU   A CG  1 
ATOM   2310 C  CD1 . LEU   A 1 336 ? -26.385 -11.350 -18.809 1.00 92.73  ? 356 LEU   A CD1 1 
ATOM   2311 C  CD2 . LEU   A 1 336 ? -28.199 -10.711 -17.209 1.00 101.71 ? 356 LEU   A CD2 1 
ATOM   2312 N  N   . ASP   A 1 337 ? -29.839 -14.130 -20.249 1.00 98.42  ? 357 ASP   A N   1 
ATOM   2313 C  CA  . ASP   A 1 337 ? -29.971 -15.540 -19.903 1.00 91.58  ? 357 ASP   A CA  1 
ATOM   2314 C  C   . ASP   A 1 337 ? -29.446 -16.433 -21.020 1.00 90.17  ? 357 ASP   A C   1 
ATOM   2315 O  O   . ASP   A 1 337 ? -28.818 -17.465 -20.757 1.00 88.22  ? 357 ASP   A O   1 
ATOM   2316 C  CB  . ASP   A 1 337 ? -31.431 -15.867 -19.589 1.00 94.46  ? 357 ASP   A CB  1 
ATOM   2317 C  CG  . ASP   A 1 337 ? -31.648 -17.338 -19.295 1.00 90.05  ? 357 ASP   A CG  1 
ATOM   2318 O  OD1 . ASP   A 1 337 ? -31.182 -17.810 -18.238 1.00 85.09  ? 357 ASP   A OD1 1 
ATOM   2319 O  OD2 . ASP   A 1 337 ? -32.289 -18.020 -20.120 1.00 86.69  ? 357 ASP   A OD2 1 
ATOM   2320 N  N   . MET   A 1 338 ? -29.686 -16.047 -22.277 1.00 89.12  ? 358 MET   A N   1 
ATOM   2321 C  CA  . MET   A 1 338 ? -29.194 -16.838 -23.400 1.00 90.67  ? 358 MET   A CA  1 
ATOM   2322 C  C   . MET   A 1 338 ? -27.673 -16.824 -23.460 1.00 90.29  ? 358 MET   A C   1 
ATOM   2323 O  O   . MET   A 1 338 ? -27.048 -17.828 -23.823 1.00 89.05  ? 358 MET   A O   1 
ATOM   2324 C  CB  . MET   A 1 338 ? -29.772 -16.313 -24.715 1.00 86.32  ? 358 MET   A CB  1 
ATOM   2325 C  CG  . MET   A 1 338 ? -31.269 -16.062 -24.711 1.00 94.21  ? 358 MET   A CG  1 
ATOM   2326 S  SD  . MET   A 1 338 ? -31.813 -15.387 -26.293 1.00 96.23  ? 358 MET   A SD  1 
ATOM   2327 C  CE  . MET   A 1 338 ? -33.479 -14.872 -25.900 1.00 107.26 ? 358 MET   A CE  1 
ATOM   2328 N  N   . VAL   A 1 339 ? -27.058 -15.691 -23.112 1.00 87.30  ? 359 VAL   A N   1 
ATOM   2329 C  CA  . VAL   A 1 339 ? -25.609 -15.565 -23.229 1.00 87.57  ? 359 VAL   A CA  1 
ATOM   2330 C  C   . VAL   A 1 339 ? -24.907 -16.448 -22.205 1.00 79.54  ? 359 VAL   A C   1 
ATOM   2331 O  O   . VAL   A 1 339 ? -23.930 -17.135 -22.528 1.00 77.09  ? 359 VAL   A O   1 
ATOM   2332 C  CB  . VAL   A 1 339 ? -25.191 -14.089 -23.099 1.00 86.60  ? 359 VAL   A CB  1 
ATOM   2333 C  CG1 . VAL   A 1 339 ? -23.682 -13.971 -22.969 1.00 84.82  ? 359 VAL   A CG1 1 
ATOM   2334 C  CG2 . VAL   A 1 339 ? -25.681 -13.297 -24.300 1.00 93.39  ? 359 VAL   A CG2 1 
ATOM   2335 N  N   . VAL   A 1 340 ? -25.388 -16.453 -20.959 1.00 82.79  ? 360 VAL   A N   1 
ATOM   2336 C  CA  . VAL   A 1 340 ? -24.770 -17.319 -19.958 1.00 85.41  ? 360 VAL   A CA  1 
ATOM   2337 C  C   . VAL   A 1 340 ? -25.104 -18.779 -20.236 1.00 80.74  ? 360 VAL   A C   1 
ATOM   2338 O  O   . VAL   A 1 340 ? -24.334 -19.677 -19.874 1.00 77.90  ? 360 VAL   A O   1 
ATOM   2339 C  CB  . VAL   A 1 340 ? -25.187 -16.903 -18.532 1.00 90.26  ? 360 VAL   A CB  1 
ATOM   2340 C  CG1 . VAL   A 1 340 ? -25.414 -15.406 -18.454 1.00 84.79  ? 360 VAL   A CG1 1 
ATOM   2341 C  CG2 . VAL   A 1 340 ? -26.422 -17.669 -18.066 1.00 85.29  ? 360 VAL   A CG2 1 
ATOM   2342 N  N   . ASN   A 1 341 ? -26.237 -19.046 -20.890 1.00 78.84  ? 361 ASN   A N   1 
ATOM   2343 C  CA  . ASN   A 1 341 ? -26.601 -20.423 -21.205 1.00 80.73  ? 361 ASN   A CA  1 
ATOM   2344 C  C   . ASN   A 1 341 ? -25.729 -20.976 -22.324 1.00 79.61  ? 361 ASN   A C   1 
ATOM   2345 O  O   . ASN   A 1 341 ? -25.227 -22.103 -22.235 1.00 75.83  ? 361 ASN   A O   1 
ATOM   2346 C  CB  . ASN   A 1 341 ? -28.080 -20.506 -21.585 1.00 82.34  ? 361 ASN   A CB  1 
ATOM   2347 C  CG  . ASN   A 1 341 ? -28.987 -20.631 -20.377 1.00 86.90  ? 361 ASN   A CG  1 
ATOM   2348 O  OD1 . ASN   A 1 341 ? -28.558 -20.435 -19.240 1.00 88.02  ? 361 ASN   A OD1 1 
ATOM   2349 N  ND2 . ASN   A 1 341 ? -30.250 -20.961 -20.619 1.00 91.83  ? 361 ASN   A ND2 1 
ATOM   2350 N  N   . GLU   A 1 342 ? -25.536 -20.194 -23.388 1.00 72.63  ? 362 GLU   A N   1 
ATOM   2351 C  CA  . GLU   A 1 342 ? -24.708 -20.649 -24.498 1.00 77.15  ? 362 GLU   A CA  1 
ATOM   2352 C  C   . GLU   A 1 342 ? -23.250 -20.808 -24.085 1.00 76.06  ? 362 GLU   A C   1 
ATOM   2353 O  O   . GLU   A 1 342 ? -22.556 -21.694 -24.598 1.00 75.12  ? 362 GLU   A O   1 
ATOM   2354 C  CB  . GLU   A 1 342 ? -24.834 -19.682 -25.678 1.00 83.43  ? 362 GLU   A CB  1 
ATOM   2355 C  CG  . GLU   A 1 342 ? -23.877 -19.942 -26.840 1.00 83.49  ? 362 GLU   A CG  1 
ATOM   2356 C  CD  . GLU   A 1 342 ? -24.259 -21.144 -27.694 1.00 85.08  ? 362 GLU   A CD  1 
ATOM   2357 O  OE1 . GLU   A 1 342 ? -24.966 -22.050 -27.202 1.00 83.02  ? 362 GLU   A OE1 1 
ATOM   2358 O  OE2 . GLU   A 1 342 ? -23.848 -21.181 -28.872 1.00 85.51  ? 362 GLU   A OE2 1 
ATOM   2359 N  N   . THR   A 1 343 ? -22.771 -19.972 -23.161 1.00 70.85  ? 363 THR   A N   1 
ATOM   2360 C  CA  . THR   A 1 343 ? -21.406 -20.129 -22.670 1.00 74.10  ? 363 THR   A CA  1 
ATOM   2361 C  C   . THR   A 1 343 ? -21.261 -21.406 -21.851 1.00 77.79  ? 363 THR   A C   1 
ATOM   2362 O  O   . THR   A 1 343 ? -20.229 -22.084 -21.923 1.00 70.06  ? 363 THR   A O   1 
ATOM   2363 C  CB  . THR   A 1 343 ? -20.997 -18.909 -21.843 1.00 75.65  ? 363 THR   A CB  1 
ATOM   2364 O  OG1 . THR   A 1 343 ? -21.167 -17.720 -22.626 1.00 77.03  ? 363 THR   A OG1 1 
ATOM   2365 C  CG2 . THR   A 1 343 ? -19.540 -19.018 -21.415 1.00 72.85  ? 363 THR   A CG2 1 
ATOM   2366 N  N   . LEU   A 1 344 ? -22.287 -21.753 -21.070 1.00 72.07  ? 364 LEU   A N   1 
ATOM   2367 C  CA  . LEU   A 1 344 ? -22.258 -22.995 -20.307 1.00 80.64  ? 364 LEU   A CA  1 
ATOM   2368 C  C   . LEU   A 1 344 ? -22.308 -24.223 -21.205 1.00 78.47  ? 364 LEU   A C   1 
ATOM   2369 O  O   . LEU   A 1 344 ? -21.855 -25.296 -20.791 1.00 66.88  ? 364 LEU   A O   1 
ATOM   2370 C  CB  . LEU   A 1 344 ? -23.417 -23.028 -19.310 1.00 73.80  ? 364 LEU   A CB  1 
ATOM   2371 C  CG  . LEU   A 1 344 ? -23.268 -22.132 -18.079 1.00 76.70  ? 364 LEU   A CG  1 
ATOM   2372 C  CD1 . LEU   A 1 344 ? -24.561 -22.100 -17.281 1.00 79.74  ? 364 LEU   A CD1 1 
ATOM   2373 C  CD2 . LEU   A 1 344 ? -22.112 -22.606 -17.213 1.00 71.10  ? 364 LEU   A CD2 1 
ATOM   2374 N  N   . ARG   A 1 345 ? -22.848 -24.093 -22.419 1.00 77.47  ? 365 ARG   A N   1 
ATOM   2375 C  CA  . ARG   A 1 345 ? -22.826 -25.206 -23.362 1.00 78.21  ? 365 ARG   A CA  1 
ATOM   2376 C  C   . ARG   A 1 345 ? -21.410 -25.469 -23.858 1.00 80.37  ? 365 ARG   A C   1 
ATOM   2377 O  O   . ARG   A 1 345 ? -20.927 -26.606 -23.817 1.00 76.35  ? 365 ARG   A O   1 
ATOM   2378 C  CB  . ARG   A 1 345 ? -23.764 -24.918 -24.536 1.00 76.54  ? 365 ARG   A CB  1 
ATOM   2379 C  CG  . ARG   A 1 345 ? -23.892 -26.069 -25.524 1.00 76.42  ? 365 ARG   A CG  1 
ATOM   2380 C  CD  . ARG   A 1 345 ? -24.692 -25.666 -26.753 1.00 79.45  ? 365 ARG   A CD  1 
ATOM   2381 N  NE  . ARG   A 1 345 ? -24.007 -24.645 -27.537 1.00 82.63  ? 365 ARG   A NE  1 
ATOM   2382 C  CZ  . ARG   A 1 345 ? -23.124 -24.901 -28.492 1.00 85.60  ? 365 ARG   A CZ  1 
ATOM   2383 N  NH1 . ARG   A 1 345 ? -22.790 -26.141 -28.810 1.00 88.56  ? 365 ARG   A NH1 1 
ATOM   2384 N  NH2 . ARG   A 1 345 ? -22.560 -23.888 -29.143 1.00 85.88  ? 365 ARG   A NH2 1 
ATOM   2385 N  N   . LEU   A 1 346 ? -20.724 -24.424 -24.323 1.00 75.62  ? 366 LEU   A N   1 
ATOM   2386 C  CA  . LEU   A 1 346 ? -19.384 -24.595 -24.870 1.00 80.28  ? 366 LEU   A CA  1 
ATOM   2387 C  C   . LEU   A 1 346 ? -18.342 -24.828 -23.784 1.00 75.11  ? 366 LEU   A C   1 
ATOM   2388 O  O   . LEU   A 1 346 ? -17.317 -25.468 -24.045 1.00 75.82  ? 366 LEU   A O   1 
ATOM   2389 C  CB  . LEU   A 1 346 ? -19.004 -23.376 -25.711 1.00 76.61  ? 366 LEU   A CB  1 
ATOM   2390 C  CG  . LEU   A 1 346 ? -19.784 -23.192 -27.014 1.00 82.45  ? 366 LEU   A CG  1 
ATOM   2391 C  CD1 . LEU   A 1 346 ? -19.745 -21.740 -27.457 1.00 85.03  ? 366 LEU   A CD1 1 
ATOM   2392 C  CD2 . LEU   A 1 346 ? -19.224 -24.098 -28.101 1.00 87.99  ? 366 LEU   A CD2 1 
ATOM   2393 N  N   . PHE   A 1 347 ? -18.580 -24.331 -22.571 1.00 74.90  ? 367 PHE   A N   1 
ATOM   2394 C  CA  . PHE   A 1 347 ? -17.634 -24.454 -21.463 1.00 76.18  ? 367 PHE   A CA  1 
ATOM   2395 C  C   . PHE   A 1 347 ? -18.360 -24.981 -20.233 1.00 73.71  ? 367 PHE   A C   1 
ATOM   2396 O  O   . PHE   A 1 347 ? -18.657 -24.224 -19.299 1.00 70.34  ? 367 PHE   A O   1 
ATOM   2397 C  CB  . PHE   A 1 347 ? -16.956 -23.115 -21.166 1.00 77.62  ? 367 PHE   A CB  1 
ATOM   2398 C  CG  . PHE   A 1 347 ? -16.314 -22.483 -22.368 1.00 77.95  ? 367 PHE   A CG  1 
ATOM   2399 C  CD1 . PHE   A 1 347 ? -15.153 -23.011 -22.907 1.00 78.87  ? 367 PHE   A CD1 1 
ATOM   2400 C  CD2 . PHE   A 1 347 ? -16.870 -21.358 -22.956 1.00 78.47  ? 367 PHE   A CD2 1 
ATOM   2401 C  CE1 . PHE   A 1 347 ? -14.560 -22.433 -24.013 1.00 83.62  ? 367 PHE   A CE1 1 
ATOM   2402 C  CE2 . PHE   A 1 347 ? -16.281 -20.774 -24.061 1.00 82.30  ? 367 PHE   A CE2 1 
ATOM   2403 C  CZ  . PHE   A 1 347 ? -15.124 -21.312 -24.590 1.00 83.30  ? 367 PHE   A CZ  1 
ATOM   2404 N  N   . PRO   A 1 348 ? -18.659 -26.279 -20.194 1.00 75.02  ? 368 PRO   A N   1 
ATOM   2405 C  CA  . PRO   A 1 348 ? -19.267 -26.855 -18.991 1.00 73.52  ? 368 PRO   A CA  1 
ATOM   2406 C  C   . PRO   A 1 348 ? -18.235 -27.041 -17.891 1.00 76.94  ? 368 PRO   A C   1 
ATOM   2407 O  O   . PRO   A 1 348 ? -17.095 -27.444 -18.138 1.00 78.51  ? 368 PRO   A O   1 
ATOM   2408 C  CB  . PRO   A 1 348 ? -19.809 -28.203 -19.481 1.00 73.87  ? 368 PRO   A CB  1 
ATOM   2409 C  CG  . PRO   A 1 348 ? -18.883 -28.577 -20.593 1.00 78.70  ? 368 PRO   A CG  1 
ATOM   2410 C  CD  . PRO   A 1 348 ? -18.478 -27.283 -21.259 1.00 71.41  ? 368 PRO   A CD  1 
ATOM   2411 N  N   . ILE   A 1 349 ? -18.644 -26.727 -16.660 1.00 79.01  ? 369 ILE   A N   1 
ATOM   2412 C  CA  . ILE   A 1 349 ? -17.757 -26.918 -15.519 1.00 80.30  ? 369 ILE   A CA  1 
ATOM   2413 C  C   . ILE   A 1 349 ? -17.594 -28.402 -15.215 1.00 78.98  ? 369 ILE   A C   1 
ATOM   2414 O  O   . ILE   A 1 349 ? -16.534 -28.835 -14.742 1.00 72.39  ? 369 ILE   A O   1 
ATOM   2415 C  CB  . ILE   A 1 349 ? -18.285 -26.123 -14.308 1.00 81.65  ? 369 ILE   A CB  1 
ATOM   2416 C  CG1 . ILE   A 1 349 ? -17.461 -24.849 -14.108 1.00 83.60  ? 369 ILE   A CG1 1 
ATOM   2417 C  CG2 . ILE   A 1 349 ? -18.302 -26.970 -13.036 1.00 80.13  ? 369 ILE   A CG2 1 
ATOM   2418 C  CD1 . ILE   A 1 349 ? -18.137 -23.823 -13.245 1.00 86.06  ? 369 ILE   A CD1 1 
ATOM   2419 N  N   . ALA   A 1 350 ? -18.620 -29.205 -15.501 1.00 82.78  ? 370 ALA   A N   1 
ATOM   2420 C  CA  . ALA   A 1 350 ? -18.557 -30.638 -15.238 1.00 79.12  ? 370 ALA   A CA  1 
ATOM   2421 C  C   . ALA   A 1 350 ? -17.743 -31.366 -16.304 1.00 79.66  ? 370 ALA   A C   1 
ATOM   2422 O  O   . ALA   A 1 350 ? -16.776 -32.066 -15.988 1.00 85.18  ? 370 ALA   A O   1 
ATOM   2423 C  CB  . ALA   A 1 350 ? -19.972 -31.218 -15.158 1.00 78.72  ? 370 ALA   A CB  1 
ATOM   2424 N  N   . MET   A 1 351 ? -18.140 -31.219 -17.574 1.00 74.25  ? 371 MET   A N   1 
ATOM   2425 C  CA  . MET   A 1 351 ? -17.610 -31.974 -18.711 1.00 77.14  ? 371 MET   A CA  1 
ATOM   2426 C  C   . MET   A 1 351 ? -18.090 -33.420 -18.625 1.00 75.31  ? 371 MET   A C   1 
ATOM   2427 O  O   . MET   A 1 351 ? -18.481 -34.011 -19.637 1.00 68.34  ? 371 MET   A O   1 
ATOM   2428 C  CB  . MET   A 1 351 ? -16.091 -31.819 -18.825 1.00 76.99  ? 371 MET   A CB  1 
ATOM   2429 C  CG  . MET   A 1 351 ? -15.634 -30.443 -19.278 1.00 80.03  ? 371 MET   A CG  1 
ATOM   2430 S  SD  . MET   A 1 351 ? -13.864 -30.235 -19.033 1.00 90.59  ? 371 MET   A SD  1 
ATOM   2431 C  CE  . MET   A 1 351 ? -13.763 -30.531 -17.272 1.00 95.83  ? 371 MET   A CE  1 
ATOM   2432 N  N   . ARG   A 1 352 ? -18.062 -33.999 -17.427 1.00 69.79  ? 372 ARG   A N   1 
ATOM   2433 C  CA  . ARG   A 1 352 ? -18.596 -35.330 -17.175 1.00 75.85  ? 372 ARG   A CA  1 
ATOM   2434 C  C   . ARG   A 1 352 ? -19.522 -35.331 -15.971 1.00 71.19  ? 372 ARG   A C   1 
ATOM   2435 O  O   . ARG   A 1 352 ? -19.164 -34.809 -14.911 1.00 71.18  ? 372 ARG   A O   1 
ATOM   2436 C  CB  . ARG   A 1 352 ? -17.425 -36.292 -16.932 1.00 73.32  ? 372 ARG   A CB  1 
ATOM   2437 C  CG  . ARG   A 1 352 ? -16.653 -36.700 -18.176 1.00 74.41  ? 372 ARG   A CG  1 
ATOM   2438 C  CD  . ARG   A 1 352 ? -15.491 -37.607 -17.802 1.00 78.43  ? 372 ARG   A CD  1 
ATOM   2439 N  NE  . ARG   A 1 352 ? -15.017 -38.394 -18.934 1.00 74.85  ? 372 ARG   A NE  1 
ATOM   2440 C  CZ  . ARG   A 1 352 ? -14.107 -39.355 -18.848 1.00 77.51  ? 372 ARG   A CZ  1 
ATOM   2441 N  NH1 . ARG   A 1 352 ? -13.544 -39.673 -17.694 1.00 81.48  ? 372 ARG   A NH1 1 
ATOM   2442 N  NH2 . ARG   A 1 352 ? -13.755 -40.016 -19.947 1.00 77.11  ? 372 ARG   A NH2 1 
ATOM   2443 N  N   . LEU   A 1 353 ? -20.712 -35.899 -16.139 1.00 65.43  ? 373 LEU   A N   1 
ATOM   2444 C  CA  . LEU   A 1 353 ? -21.580 -36.241 -15.023 1.00 71.63  ? 373 LEU   A CA  1 
ATOM   2445 C  C   . LEU   A 1 353 ? -21.468 -37.737 -14.757 1.00 70.87  ? 373 LEU   A C   1 
ATOM   2446 O  O   . LEU   A 1 353 ? -21.410 -38.538 -15.693 1.00 64.73  ? 373 LEU   A O   1 
ATOM   2447 C  CB  . LEU   A 1 353 ? -23.033 -35.864 -15.313 1.00 69.03  ? 373 LEU   A CB  1 
ATOM   2448 C  CG  . LEU   A 1 353 ? -23.360 -34.403 -15.625 1.00 74.23  ? 373 LEU   A CG  1 
ATOM   2449 C  CD1 . LEU   A 1 353 ? -24.840 -34.264 -15.941 1.00 75.70  ? 373 LEU   A CD1 1 
ATOM   2450 C  CD2 . LEU   A 1 353 ? -22.970 -33.496 -14.469 1.00 72.98  ? 373 LEU   A CD2 1 
ATOM   2451 N  N   . GLU   A 1 354 ? -21.430 -38.113 -13.481 1.00 64.75  ? 374 GLU   A N   1 
ATOM   2452 C  CA  . GLU   A 1 354 ? -21.205 -39.506 -13.126 1.00 76.42  ? 374 GLU   A CA  1 
ATOM   2453 C  C   . GLU   A 1 354 ? -22.043 -39.897 -11.920 1.00 74.19  ? 374 GLU   A C   1 
ATOM   2454 O  O   . GLU   A 1 354 ? -22.303 -39.085 -11.028 1.00 74.16  ? 374 GLU   A O   1 
ATOM   2455 C  CB  . GLU   A 1 354 ? -19.719 -39.777 -12.840 1.00 69.23  ? 374 GLU   A CB  1 
ATOM   2456 C  CG  . GLU   A 1 354 ? -18.843 -39.809 -14.083 1.00 71.42  ? 374 GLU   A CG  1 
ATOM   2457 C  CD  . GLU   A 1 354 ? -17.383 -40.048 -13.760 1.00 69.69  ? 374 GLU   A CD  1 
ATOM   2458 O  OE1 . GLU   A 1 354 ? -17.054 -40.224 -12.567 1.00 71.26  ? 374 GLU   A OE1 1 
ATOM   2459 O  OE2 . GLU   A 1 354 ? -16.563 -40.060 -14.700 1.00 70.76  ? 374 GLU   A OE2 1 
ATOM   2460 N  N   . ARG   A 1 355 ? -22.468 -41.161 -11.913 1.00 72.29  ? 375 ARG   A N   1 
ATOM   2461 C  CA  . ARG   A 1 355 ? -23.182 -41.772 -10.803 1.00 78.00  ? 375 ARG   A CA  1 
ATOM   2462 C  C   . ARG   A 1 355 ? -22.686 -43.201 -10.637 1.00 74.51  ? 375 ARG   A C   1 
ATOM   2463 O  O   . ARG   A 1 355 ? -22.516 -43.921 -11.624 1.00 61.24  ? 375 ARG   A O   1 
ATOM   2464 C  CB  . ARG   A 1 355 ? -24.699 -41.776 -11.031 1.00 73.49  ? 375 ARG   A CB  1 
ATOM   2465 C  CG  . ARG   A 1 355 ? -25.351 -40.403 -11.065 1.00 75.35  ? 375 ARG   A CG  1 
ATOM   2466 C  CD  . ARG   A 1 355 ? -25.290 -39.722 -9.709  1.00 71.41  ? 375 ARG   A CD  1 
ATOM   2467 N  NE  . ARG   A 1 355 ? -26.134 -38.534 -9.674  1.00 78.08  ? 375 ARG   A NE  1 
ATOM   2468 C  CZ  . ARG   A 1 355 ? -25.771 -37.344 -10.130 1.00 74.24  ? 375 ARG   A CZ  1 
ATOM   2469 N  NH1 . ARG   A 1 355 ? -24.574 -37.142 -10.657 1.00 64.58  ? 375 ARG   A NH1 1 
ATOM   2470 N  NH2 . ARG   A 1 355 ? -26.630 -36.331 -10.058 1.00 71.68  ? 375 ARG   A NH2 1 
ATOM   2471 N  N   . VAL   A 1 356 ? -22.459 -43.614 -9.395  1.00 78.57  ? 376 VAL   A N   1 
ATOM   2472 C  CA  . VAL   A 1 356 ? -22.016 -44.973 -9.098  1.00 80.56  ? 376 VAL   A CA  1 
ATOM   2473 C  C   . VAL   A 1 356 ? -23.240 -45.869 -8.958  1.00 73.32  ? 376 VAL   A C   1 
ATOM   2474 O  O   . VAL   A 1 356 ? -24.146 -45.582 -8.168  1.00 74.38  ? 376 VAL   A O   1 
ATOM   2475 C  CB  . VAL   A 1 356 ? -21.148 -45.020 -7.832  1.00 80.59  ? 376 VAL   A CB  1 
ATOM   2476 C  CG1 . VAL   A 1 356 ? -20.909 -46.462 -7.418  1.00 76.38  ? 376 VAL   A CG1 1 
ATOM   2477 C  CG2 . VAL   A 1 356 ? -19.822 -44.320 -8.084  1.00 76.67  ? 376 VAL   A CG2 1 
ATOM   2478 N  N   . CYS   A 1 357 ? -23.270 -46.948 -9.734  1.00 83.84  ? 377 CYS   A N   1 
ATOM   2479 C  CA  . CYS   A 1 357 ? -24.351 -47.920 -9.637  1.00 86.09  ? 377 CYS   A CA  1 
ATOM   2480 C  C   . CYS   A 1 357 ? -24.212 -48.698 -8.334  1.00 84.91  ? 377 CYS   A C   1 
ATOM   2481 O  O   . CYS   A 1 357 ? -23.193 -49.358 -8.102  1.00 93.74  ? 377 CYS   A O   1 
ATOM   2482 C  CB  . CYS   A 1 357 ? -24.324 -48.858 -10.842 1.00 83.60  ? 377 CYS   A CB  1 
ATOM   2483 S  SG  . CYS   A 1 357 ? -25.662 -50.061 -10.892 1.00 96.69  ? 377 CYS   A SG  1 
ATOM   2484 N  N   . LYS   A 1 358 ? -25.227 -48.608 -7.476  1.00 86.99  ? 378 LYS   A N   1 
ATOM   2485 C  CA  . LYS   A 1 358 ? -25.140 -49.210 -6.153  1.00 97.37  ? 378 LYS   A CA  1 
ATOM   2486 C  C   . LYS   A 1 358 ? -25.705 -50.621 -6.105  1.00 95.61  ? 378 LYS   A C   1 
ATOM   2487 O  O   . LYS   A 1 358 ? -25.307 -51.409 -5.239  1.00 95.95  ? 378 LYS   A O   1 
ATOM   2488 C  CB  . LYS   A 1 358 ? -25.862 -48.331 -5.129  1.00 97.63  ? 378 LYS   A CB  1 
ATOM   2489 C  CG  . LYS   A 1 358 ? -24.937 -47.785 -4.051  1.00 95.02  ? 378 LYS   A CG  1 
ATOM   2490 C  CD  . LYS   A 1 358 ? -23.714 -47.102 -4.657  1.00 94.87  ? 378 LYS   A CD  1 
ATOM   2491 C  CE  . LYS   A 1 358 ? -22.778 -46.594 -3.571  1.00 98.44  ? 378 LYS   A CE  1 
ATOM   2492 N  NZ  . LYS   A 1 358 ? -21.615 -45.868 -4.152  1.00 83.92  ? 378 LYS   A NZ  1 
ATOM   2493 N  N   . LYS   A 1 359 ? -26.631 -50.955 -7.001  1.00 97.12  ? 379 LYS   A N   1 
ATOM   2494 C  CA  . LYS   A 1 359 ? -27.177 -52.302 -7.069  1.00 103.50 ? 379 LYS   A CA  1 
ATOM   2495 C  C   . LYS   A 1 359 ? -27.603 -52.582 -8.501  1.00 106.75 ? 379 LYS   A C   1 
ATOM   2496 O  O   . LYS   A 1 359 ? -27.777 -51.665 -9.305  1.00 103.89 ? 379 LYS   A O   1 
ATOM   2497 C  CB  . LYS   A 1 359 ? -28.351 -52.492 -6.098  1.00 107.85 ? 379 LYS   A CB  1 
ATOM   2498 C  CG  . LYS   A 1 359 ? -29.512 -51.543 -6.317  1.00 105.88 ? 379 LYS   A CG  1 
ATOM   2499 C  CD  . LYS   A 1 359 ? -30.568 -51.717 -5.240  1.00 107.37 ? 379 LYS   A CD  1 
ATOM   2500 C  CE  . LYS   A 1 359 ? -29.999 -51.427 -3.857  1.00 109.70 ? 379 LYS   A CE  1 
ATOM   2501 N  NZ  . LYS   A 1 359 ? -31.022 -51.595 -2.786  1.00 116.33 ? 379 LYS   A NZ  1 
ATOM   2502 N  N   . ASP   A 1 360 ? -27.758 -53.869 -8.809  1.00 109.58 ? 380 ASP   A N   1 
ATOM   2503 C  CA  . ASP   A 1 360 ? -28.071 -54.292 -10.168 1.00 113.12 ? 380 ASP   A CA  1 
ATOM   2504 C  C   . ASP   A 1 360 ? -29.371 -53.660 -10.651 1.00 115.89 ? 380 ASP   A C   1 
ATOM   2505 O  O   . ASP   A 1 360 ? -30.370 -53.624 -9.928  1.00 119.82 ? 380 ASP   A O   1 
ATOM   2506 C  CB  . ASP   A 1 360 ? -28.176 -55.814 -10.227 1.00 118.62 ? 380 ASP   A CB  1 
ATOM   2507 C  CG  . ASP   A 1 360 ? -27.109 -56.503 -9.397  1.00 116.65 ? 380 ASP   A CG  1 
ATOM   2508 O  OD1 . ASP   A 1 360 ? -27.136 -56.365 -8.154  1.00 103.86 ? 380 ASP   A OD1 1 
ATOM   2509 O  OD2 . ASP   A 1 360 ? -26.241 -57.182 -9.985  1.00 120.68 ? 380 ASP   A OD2 1 
ATOM   2510 N  N   . VAL   A 1 361 ? -29.354 -53.149 -11.884 1.00 120.34 ? 381 VAL   A N   1 
ATOM   2511 C  CA  . VAL   A 1 361 ? -30.510 -52.482 -12.470 1.00 120.46 ? 381 VAL   A CA  1 
ATOM   2512 C  C   . VAL   A 1 361 ? -30.671 -52.909 -13.920 1.00 121.13 ? 381 VAL   A C   1 
ATOM   2513 O  O   . VAL   A 1 361 ? -29.725 -53.352 -14.575 1.00 120.82 ? 381 VAL   A O   1 
ATOM   2514 C  CB  . VAL   A 1 361 ? -30.406 -50.942 -12.403 1.00 116.29 ? 381 VAL   A CB  1 
ATOM   2515 C  CG1 . VAL   A 1 361 ? -31.433 -50.387 -11.438 1.00 117.29 ? 381 VAL   A CG1 1 
ATOM   2516 C  CG2 . VAL   A 1 361 ? -29.000 -50.510 -12.023 1.00 111.55 ? 381 VAL   A CG2 1 
ATOM   2517 N  N   . GLU   A 1 362 ? -31.898 -52.764 -14.415 1.00 125.71 ? 382 GLU   A N   1 
ATOM   2518 C  CA  . GLU   A 1 362 ? -32.205 -52.848 -15.839 1.00 133.22 ? 382 GLU   A CA  1 
ATOM   2519 C  C   . GLU   A 1 362 ? -32.974 -51.587 -16.209 1.00 135.00 ? 382 GLU   A C   1 
ATOM   2520 O  O   . GLU   A 1 362 ? -34.139 -51.432 -15.829 1.00 140.11 ? 382 GLU   A O   1 
ATOM   2521 C  CB  . GLU   A 1 362 ? -33.008 -54.105 -16.170 1.00 134.55 ? 382 GLU   A CB  1 
ATOM   2522 C  CG  . GLU   A 1 362 ? -33.419 -54.201 -17.633 1.00 135.53 ? 382 GLU   A CG  1 
ATOM   2523 C  CD  . GLU   A 1 362 ? -33.841 -55.599 -18.029 1.00 138.06 ? 382 GLU   A CD  1 
ATOM   2524 O  OE1 . GLU   A 1 362 ? -33.425 -56.559 -17.347 1.00 134.41 ? 382 GLU   A OE1 1 
ATOM   2525 O  OE2 . GLU   A 1 362 ? -34.588 -55.737 -19.021 1.00 137.71 ? 382 GLU   A OE2 1 
ATOM   2526 N  N   . ILE   A 1 363 ? -32.322 -50.682 -16.935 1.00 130.64 ? 383 ILE   A N   1 
ATOM   2527 C  CA  . ILE   A 1 363 ? -32.893 -49.387 -17.282 1.00 131.06 ? 383 ILE   A CA  1 
ATOM   2528 C  C   . ILE   A 1 363 ? -32.951 -49.270 -18.798 1.00 130.16 ? 383 ILE   A C   1 
ATOM   2529 O  O   . ILE   A 1 363 ? -31.952 -49.512 -19.485 1.00 132.65 ? 383 ILE   A O   1 
ATOM   2530 C  CB  . ILE   A 1 363 ? -32.094 -48.227 -16.658 1.00 131.51 ? 383 ILE   A CB  1 
ATOM   2531 C  CG1 . ILE   A 1 363 ? -30.637 -48.237 -17.120 1.00 125.91 ? 383 ILE   A CG1 1 
ATOM   2532 C  CG2 . ILE   A 1 363 ? -32.141 -48.316 -15.141 1.00 129.09 ? 383 ILE   A CG2 1 
ATOM   2533 C  CD1 . ILE   A 1 363 ? -29.845 -47.039 -16.649 1.00 122.66 ? 383 ILE   A CD1 1 
ATOM   2534 N  N   . ASN   A 1 364 ? -34.132 -48.921 -19.314 1.00 131.31 ? 384 ASN   A N   1 
ATOM   2535 C  CA  . ASN   A 1 364 ? -34.358 -48.761 -20.752 1.00 130.16 ? 384 ASN   A CA  1 
ATOM   2536 C  C   . ASN   A 1 364 ? -33.908 -49.995 -21.529 1.00 133.44 ? 384 ASN   A C   1 
ATOM   2537 O  O   . ASN   A 1 364 ? -33.371 -49.900 -22.635 1.00 133.25 ? 384 ASN   A O   1 
ATOM   2538 C  CB  . ASN   A 1 364 ? -33.671 -47.500 -21.279 1.00 123.23 ? 384 ASN   A CB  1 
ATOM   2539 C  CG  . ASN   A 1 364 ? -34.311 -46.227 -20.759 1.00 119.82 ? 384 ASN   A CG  1 
ATOM   2540 O  OD1 . ASN   A 1 364 ? -33.922 -45.705 -19.714 1.00 112.02 ? 384 ASN   A OD1 1 
ATOM   2541 N  ND2 . ASN   A 1 364 ? -35.299 -45.720 -21.488 1.00 120.09 ? 384 ASN   A ND2 1 
ATOM   2542 N  N   . GLY   A 1 365 ? -34.127 -51.167 -20.941 1.00 137.61 ? 385 GLY   A N   1 
ATOM   2543 C  CA  . GLY   A 1 365 ? -33.773 -52.415 -21.594 1.00 134.13 ? 385 GLY   A CA  1 
ATOM   2544 C  C   . GLY   A 1 365 ? -32.288 -52.705 -21.638 1.00 137.57 ? 385 GLY   A C   1 
ATOM   2545 O  O   . GLY   A 1 365 ? -31.775 -53.132 -22.681 1.00 140.67 ? 385 GLY   A O   1 
ATOM   2546 N  N   . MET   A 1 366 ? -31.581 -52.486 -20.530 1.00 134.68 ? 386 MET   A N   1 
ATOM   2547 C  CA  . MET   A 1 366 ? -30.151 -52.760 -20.469 1.00 131.02 ? 386 MET   A CA  1 
ATOM   2548 C  C   . MET   A 1 366 ? -29.760 -52.995 -19.019 1.00 127.37 ? 386 MET   A C   1 
ATOM   2549 O  O   . MET   A 1 366 ? -30.106 -52.193 -18.146 1.00 125.56 ? 386 MET   A O   1 
ATOM   2550 C  CB  . MET   A 1 366 ? -29.337 -51.603 -21.056 1.00 126.49 ? 386 MET   A CB  1 
ATOM   2551 C  CG  . MET   A 1 366 ? -27.846 -51.884 -21.142 1.00 122.36 ? 386 MET   A CG  1 
ATOM   2552 S  SD  . MET   A 1 366 ? -26.861 -50.381 -21.263 1.00 111.07 ? 386 MET   A SD  1 
ATOM   2553 C  CE  . MET   A 1 366 ? -27.687 -49.542 -22.611 1.00 105.12 ? 386 MET   A CE  1 
ATOM   2554 N  N   . PHE   A 1 367 ? -29.034 -54.082 -18.769 1.00 124.63 ? 387 PHE   A N   1 
ATOM   2555 C  CA  . PHE   A 1 367 ? -28.627 -54.447 -17.419 1.00 122.37 ? 387 PHE   A CA  1 
ATOM   2556 C  C   . PHE   A 1 367 ? -27.297 -53.798 -17.060 1.00 119.49 ? 387 PHE   A C   1 
ATOM   2557 O  O   . PHE   A 1 367 ? -26.378 -53.735 -17.882 1.00 122.06 ? 387 PHE   A O   1 
ATOM   2558 C  CB  . PHE   A 1 367 ? -28.519 -55.967 -17.283 1.00 120.60 ? 387 PHE   A CB  1 
ATOM   2559 C  CG  . PHE   A 1 367 ? -27.957 -56.418 -15.965 1.00 121.64 ? 387 PHE   A CG  1 
ATOM   2560 C  CD1 . PHE   A 1 367 ? -28.738 -56.404 -14.822 1.00 126.29 ? 387 PHE   A CD1 1 
ATOM   2561 C  CD2 . PHE   A 1 367 ? -26.647 -56.861 -15.870 1.00 120.66 ? 387 PHE   A CD2 1 
ATOM   2562 C  CE1 . PHE   A 1 367 ? -28.224 -56.819 -13.608 1.00 124.88 ? 387 PHE   A CE1 1 
ATOM   2563 C  CE2 . PHE   A 1 367 ? -26.128 -57.278 -14.659 1.00 117.92 ? 387 PHE   A CE2 1 
ATOM   2564 C  CZ  . PHE   A 1 367 ? -26.917 -57.257 -13.527 1.00 118.80 ? 387 PHE   A CZ  1 
ATOM   2565 N  N   . ILE   A 1 368 ? -27.202 -53.320 -15.823 1.00 115.48 ? 388 ILE   A N   1 
ATOM   2566 C  CA  . ILE   A 1 368 ? -25.986 -52.689 -15.313 1.00 112.92 ? 388 ILE   A CA  1 
ATOM   2567 C  C   . ILE   A 1 368 ? -25.622 -53.325 -13.976 1.00 112.35 ? 388 ILE   A C   1 
ATOM   2568 O  O   . ILE   A 1 368 ? -26.448 -53.339 -13.052 1.00 113.28 ? 388 ILE   A O   1 
ATOM   2569 C  CB  . ILE   A 1 368 ? -26.161 -51.169 -15.166 1.00 111.76 ? 388 ILE   A CB  1 
ATOM   2570 C  CG1 . ILE   A 1 368 ? -26.472 -50.530 -16.521 1.00 114.60 ? 388 ILE   A CG1 1 
ATOM   2571 C  CG2 . ILE   A 1 368 ? -24.913 -50.546 -14.555 1.00 104.48 ? 388 ILE   A CG2 1 
ATOM   2572 C  CD1 . ILE   A 1 368 ? -26.752 -49.047 -16.446 1.00 110.02 ? 388 ILE   A CD1 1 
ATOM   2573 N  N   . PRO   A 1 369 ? -24.414 -53.856 -13.825 1.00 105.64 ? 389 PRO   A N   1 
ATOM   2574 C  CA  . PRO   A 1 369 ? -24.022 -54.478 -12.557 1.00 102.70 ? 389 PRO   A CA  1 
ATOM   2575 C  C   . PRO   A 1 369 ? -23.677 -53.432 -11.502 1.00 99.04  ? 389 PRO   A C   1 
ATOM   2576 O  O   . PRO   A 1 369 ? -23.482 -52.249 -11.785 1.00 97.09  ? 389 PRO   A O   1 
ATOM   2577 C  CB  . PRO   A 1 369 ? -22.784 -55.308 -12.931 1.00 102.58 ? 389 PRO   A CB  1 
ATOM   2578 C  CG  . PRO   A 1 369 ? -22.752 -55.331 -14.444 1.00 102.56 ? 389 PRO   A CG  1 
ATOM   2579 C  CD  . PRO   A 1 369 ? -23.400 -54.056 -14.870 1.00 104.40 ? 389 PRO   A CD  1 
ATOM   2580 N  N   . LYS   A 1 370 ? -23.602 -53.902 -10.259 1.00 98.61  ? 390 LYS   A N   1 
ATOM   2581 C  CA  . LYS   A 1 370 ? -23.200 -53.052 -9.148  1.00 93.36  ? 390 LYS   A CA  1 
ATOM   2582 C  C   . LYS   A 1 370 ? -21.729 -52.668 -9.279  1.00 91.68  ? 390 LYS   A C   1 
ATOM   2583 O  O   . LYS   A 1 370 ? -20.902 -53.448 -9.757  1.00 89.38  ? 390 LYS   A O   1 
ATOM   2584 C  CB  . LYS   A 1 370 ? -23.457 -53.769 -7.814  1.00 98.30  ? 390 LYS   A CB  1 
ATOM   2585 C  CG  . LYS   A 1 370 ? -22.442 -53.487 -6.701  1.00 98.69  ? 390 LYS   A CG  1 
ATOM   2586 C  CD  . LYS   A 1 370 ? -21.338 -54.543 -6.658  1.00 98.81  ? 390 LYS   A CD  1 
ATOM   2587 C  CE  . LYS   A 1 370 ? -20.102 -54.022 -5.944  1.00 97.07  ? 390 LYS   A CE  1 
ATOM   2588 N  NZ  . LYS   A 1 370 ? -18.933 -54.928 -6.120  1.00 98.35  ? 390 LYS   A NZ  1 
ATOM   2589 N  N   . GLY   A 1 371 ? -21.409 -51.445 -8.859  1.00 89.76  ? 391 GLY   A N   1 
ATOM   2590 C  CA  . GLY   A 1 371 ? -20.040 -50.979 -8.846  1.00 87.09  ? 391 GLY   A CA  1 
ATOM   2591 C  C   . GLY   A 1 371 ? -19.566 -50.322 -10.122 1.00 77.76  ? 391 GLY   A C   1 
ATOM   2592 O  O   . GLY   A 1 371 ? -18.434 -49.822 -10.158 1.00 76.76  ? 391 GLY   A O   1 
ATOM   2593 N  N   . VAL   A 1 372 ? -20.383 -50.311 -11.167 1.00 75.51  ? 392 VAL   A N   1 
ATOM   2594 C  CA  . VAL   A 1 372 ? -20.032 -49.632 -12.407 1.00 76.97  ? 392 VAL   A CA  1 
ATOM   2595 C  C   . VAL   A 1 372 ? -20.362 -48.153 -12.273 1.00 76.23  ? 392 VAL   A C   1 
ATOM   2596 O  O   . VAL   A 1 372 ? -21.420 -47.780 -11.752 1.00 75.35  ? 392 VAL   A O   1 
ATOM   2597 C  CB  . VAL   A 1 372 ? -20.772 -50.266 -13.599 1.00 82.54  ? 392 VAL   A CB  1 
ATOM   2598 C  CG1 . VAL   A 1 372 ? -20.506 -49.482 -14.878 1.00 75.88  ? 392 VAL   A CG1 1 
ATOM   2599 C  CG2 . VAL   A 1 372 ? -20.359 -51.720 -13.766 1.00 84.53  ? 392 VAL   A CG2 1 
ATOM   2600 N  N   . VAL   A 1 373 ? -19.449 -47.303 -12.730 1.00 78.07  ? 393 VAL   A N   1 
ATOM   2601 C  CA  . VAL   A 1 373 ? -19.684 -45.866 -12.779 1.00 71.79  ? 393 VAL   A CA  1 
ATOM   2602 C  C   . VAL   A 1 373 ? -20.364 -45.541 -14.102 1.00 70.39  ? 393 VAL   A C   1 
ATOM   2603 O  O   . VAL   A 1 373 ? -19.820 -45.825 -15.175 1.00 71.03  ? 393 VAL   A O   1 
ATOM   2604 C  CB  . VAL   A 1 373 ? -18.374 -45.079 -12.622 1.00 74.16  ? 393 VAL   A CB  1 
ATOM   2605 C  CG1 . VAL   A 1 373 ? -18.610 -43.598 -12.895 1.00 66.65  ? 393 VAL   A CG1 1 
ATOM   2606 C  CG2 . VAL   A 1 373 ? -17.799 -45.279 -11.229 1.00 66.12  ? 393 VAL   A CG2 1 
ATOM   2607 N  N   . VAL   A 1 374 ? -21.556 -44.958 -14.028 1.00 71.31  ? 394 VAL   A N   1 
ATOM   2608 C  CA  . VAL   A 1 374 ? -22.281 -44.517 -15.213 1.00 71.40  ? 394 VAL   A CA  1 
ATOM   2609 C  C   . VAL   A 1 374 ? -21.923 -43.059 -15.466 1.00 72.99  ? 394 VAL   A C   1 
ATOM   2610 O  O   . VAL   A 1 374 ? -22.136 -42.200 -14.605 1.00 69.50  ? 394 VAL   A O   1 
ATOM   2611 C  CB  . VAL   A 1 374 ? -23.796 -44.695 -15.043 1.00 73.37  ? 394 VAL   A CB  1 
ATOM   2612 C  CG1 . VAL   A 1 374 ? -24.523 -44.209 -16.284 1.00 74.98  ? 394 VAL   A CG1 1 
ATOM   2613 C  CG2 . VAL   A 1 374 ? -24.128 -46.153 -14.760 1.00 81.57  ? 394 VAL   A CG2 1 
ATOM   2614 N  N   . MET   A 1 375 ? -21.380 -42.781 -16.647 1.00 70.22  ? 395 MET   A N   1 
ATOM   2615 C  CA  A MET   A 1 375 ? -20.909 -41.450 -16.998 0.60 70.26  ? 395 MET   A CA  1 
ATOM   2616 C  CA  B MET   A 1 375 ? -20.902 -41.453 -17.005 0.40 77.66  ? 395 MET   A CA  1 
ATOM   2617 C  C   . MET   A 1 375 ? -21.759 -40.861 -18.115 1.00 74.17  ? 395 MET   A C   1 
ATOM   2618 O  O   . MET   A 1 375 ? -22.108 -41.551 -19.079 1.00 72.04  ? 395 MET   A O   1 
ATOM   2619 C  CB  A MET   A 1 375 ? -19.435 -41.487 -17.418 0.60 71.95  ? 395 MET   A CB  1 
ATOM   2620 C  CB  B MET   A 1 375 ? -19.441 -41.502 -17.459 0.40 69.53  ? 395 MET   A CB  1 
ATOM   2621 C  CG  A MET   A 1 375 ? -18.841 -40.130 -17.768 0.60 72.26  ? 395 MET   A CG  1 
ATOM   2622 C  CG  B MET   A 1 375 ? -18.854 -40.147 -17.813 0.40 77.99  ? 395 MET   A CG  1 
ATOM   2623 S  SD  A MET   A 1 375 ? -18.864 -39.784 -19.537 0.60 54.20  ? 395 MET   A SD  1 
ATOM   2624 S  SD  B MET   A 1 375 ? -17.424 -40.274 -18.903 0.40 76.65  ? 395 MET   A SD  1 
ATOM   2625 C  CE  A MET   A 1 375 ? -17.711 -41.015 -20.136 0.60 71.52  ? 395 MET   A CE  1 
ATOM   2626 C  CE  B MET   A 1 375 ? -18.217 -40.584 -20.477 0.40 72.58  ? 395 MET   A CE  1 
ATOM   2627 N  N   . ILE   A 1 376 ? -22.090 -39.581 -17.979 1.00 72.53  ? 396 ILE   A N   1 
ATOM   2628 C  CA  . ILE   A 1 376 ? -22.811 -38.820 -18.991 1.00 73.81  ? 396 ILE   A CA  1 
ATOM   2629 C  C   . ILE   A 1 376 ? -21.849 -37.771 -19.540 1.00 67.09  ? 396 ILE   A C   1 
ATOM   2630 O  O   . ILE   A 1 376 ? -21.537 -36.792 -18.843 1.00 69.88  ? 396 ILE   A O   1 
ATOM   2631 C  CB  . ILE   A 1 376 ? -24.083 -38.169 -18.428 1.00 73.46  ? 396 ILE   A CB  1 
ATOM   2632 C  CG1 . ILE   A 1 376 ? -25.129 -39.229 -18.069 1.00 78.41  ? 396 ILE   A CG1 1 
ATOM   2633 C  CG2 . ILE   A 1 376 ? -24.665 -37.184 -19.432 1.00 70.28  ? 396 ILE   A CG2 1 
ATOM   2634 C  CD1 . ILE   A 1 376 ? -24.983 -39.813 -16.678 1.00 76.52  ? 396 ILE   A CD1 1 
ATOM   2635 N  N   . PRO   A 1 377 ? -21.337 -37.932 -20.762 1.00 62.23  ? 397 PRO   A N   1 
ATOM   2636 C  CA  . PRO   A 1 377 ? -20.342 -36.985 -21.309 1.00 71.05  ? 397 PRO   A CA  1 
ATOM   2637 C  C   . PRO   A 1 377 ? -20.969 -35.658 -21.730 1.00 69.19  ? 397 PRO   A C   1 
ATOM   2638 O  O   . PRO   A 1 377 ? -21.294 -35.412 -22.892 1.00 66.42  ? 397 PRO   A O   1 
ATOM   2639 C  CB  . PRO   A 1 377 ? -19.768 -37.756 -22.499 1.00 68.66  ? 397 PRO   A CB  1 
ATOM   2640 C  CG  . PRO   A 1 377 ? -20.904 -38.609 -22.960 1.00 65.62  ? 397 PRO   A CG  1 
ATOM   2641 C  CD  . PRO   A 1 377 ? -21.664 -39.005 -21.718 1.00 69.74  ? 397 PRO   A CD  1 
ATOM   2642 N  N   . SER   A 1 378 ? -21.137 -34.772 -20.745 1.00 64.42  ? 398 SER   A N   1 
ATOM   2643 C  CA  . SER   A 1 378 ? -21.804 -33.496 -20.987 1.00 73.09  ? 398 SER   A CA  1 
ATOM   2644 C  C   . SER   A 1 378 ? -21.081 -32.689 -22.058 1.00 68.01  ? 398 SER   A C   1 
ATOM   2645 O  O   . SER   A 1 378 ? -21.714 -32.131 -22.962 1.00 71.75  ? 398 SER   A O   1 
ATOM   2646 C  CB  . SER   A 1 378 ? -21.897 -32.700 -19.684 1.00 72.42  ? 398 SER   A CB  1 
ATOM   2647 O  OG  . SER   A 1 378 ? -22.530 -33.458 -18.669 1.00 69.91  ? 398 SER   A OG  1 
ATOM   2648 N  N   . TYR   A 1 379 ? -19.751 -32.620 -21.976 1.00 67.94  ? 399 TYR   A N   1 
ATOM   2649 C  CA  . TYR   A 1 379 ? -18.985 -31.879 -22.974 1.00 70.81  ? 399 TYR   A CA  1 
ATOM   2650 C  C   . TYR   A 1 379 ? -19.197 -32.461 -24.366 1.00 75.99  ? 399 TYR   A C   1 
ATOM   2651 O  O   . TYR   A 1 379 ? -19.401 -31.721 -25.336 1.00 71.81  ? 399 TYR   A O   1 
ATOM   2652 C  CB  . TYR   A 1 379 ? -17.501 -31.882 -22.606 1.00 70.96  ? 399 TYR   A CB  1 
ATOM   2653 C  CG  . TYR   A 1 379 ? -16.649 -30.989 -23.483 1.00 76.08  ? 399 TYR   A CG  1 
ATOM   2654 C  CD1 . TYR   A 1 379 ? -16.117 -31.458 -24.678 1.00 78.46  ? 399 TYR   A CD1 1 
ATOM   2655 C  CD2 . TYR   A 1 379 ? -16.376 -29.678 -23.116 1.00 80.27  ? 399 TYR   A CD2 1 
ATOM   2656 C  CE1 . TYR   A 1 379 ? -15.339 -30.648 -25.481 1.00 83.98  ? 399 TYR   A CE1 1 
ATOM   2657 C  CE2 . TYR   A 1 379 ? -15.599 -28.859 -23.914 1.00 82.75  ? 399 TYR   A CE2 1 
ATOM   2658 C  CZ  . TYR   A 1 379 ? -15.083 -29.350 -25.095 1.00 82.97  ? 399 TYR   A CZ  1 
ATOM   2659 O  OH  . TYR   A 1 379 ? -14.309 -28.542 -25.895 1.00 84.16  ? 399 TYR   A OH  1 
ATOM   2660 N  N   . ALA   A 1 380 ? -19.156 -33.790 -24.484 1.00 76.64  ? 400 ALA   A N   1 
ATOM   2661 C  CA  . ALA   A 1 380 ? -19.368 -34.418 -25.784 1.00 74.42  ? 400 ALA   A CA  1 
ATOM   2662 C  C   . ALA   A 1 380 ? -20.790 -34.192 -26.279 1.00 74.05  ? 400 ALA   A C   1 
ATOM   2663 O  O   . ALA   A 1 380 ? -21.016 -34.004 -27.480 1.00 79.01  ? 400 ALA   A O   1 
ATOM   2664 C  CB  . ALA   A 1 380 ? -19.056 -35.912 -25.702 1.00 74.23  ? 400 ALA   A CB  1 
ATOM   2665 N  N   . LEU   A 1 381 ? -21.762 -34.198 -25.365 1.00 69.24  ? 401 LEU   A N   1 
ATOM   2666 C  CA  . LEU   A 1 381 ? -23.152 -33.959 -25.739 1.00 77.31  ? 401 LEU   A CA  1 
ATOM   2667 C  C   . LEU   A 1 381 ? -23.407 -32.490 -26.053 1.00 79.42  ? 401 LEU   A C   1 
ATOM   2668 O  O   . LEU   A 1 381 ? -24.216 -32.173 -26.933 1.00 83.25  ? 401 LEU   A O   1 
ATOM   2669 C  CB  . LEU   A 1 381 ? -24.082 -34.435 -24.623 1.00 76.58  ? 401 LEU   A CB  1 
ATOM   2670 C  CG  . LEU   A 1 381 ? -24.050 -35.937 -24.345 1.00 77.87  ? 401 LEU   A CG  1 
ATOM   2671 C  CD1 . LEU   A 1 381 ? -24.943 -36.299 -23.167 1.00 74.10  ? 401 LEU   A CD1 1 
ATOM   2672 C  CD2 . LEU   A 1 381 ? -24.458 -36.704 -25.592 1.00 82.14  ? 401 LEU   A CD2 1 
ATOM   2673 N  N   . HIS   A 1 382 ? -22.731 -31.581 -25.346 1.00 73.20  ? 402 HIS   A N   1 
ATOM   2674 C  CA  . HIS   A 1 382 ? -22.890 -30.160 -25.636 1.00 82.13  ? 402 HIS   A CA  1 
ATOM   2675 C  C   . HIS   A 1 382 ? -22.292 -29.794 -26.988 1.00 83.59  ? 402 HIS   A C   1 
ATOM   2676 O  O   . HIS   A 1 382 ? -22.736 -28.827 -27.619 1.00 78.83  ? 402 HIS   A O   1 
ATOM   2677 C  CB  . HIS   A 1 382 ? -22.248 -29.316 -24.536 1.00 76.82  ? 402 HIS   A CB  1 
ATOM   2678 C  CG  . HIS   A 1 382 ? -22.953 -29.392 -23.217 1.00 72.96  ? 402 HIS   A CG  1 
ATOM   2679 N  ND1 . HIS   A 1 382 ? -22.584 -28.623 -22.135 1.00 71.00  ? 402 HIS   A ND1 1 
ATOM   2680 C  CD2 . HIS   A 1 382 ? -24.001 -30.143 -22.804 1.00 76.34  ? 402 HIS   A CD2 1 
ATOM   2681 C  CE1 . HIS   A 1 382 ? -23.374 -28.897 -21.112 1.00 73.02  ? 402 HIS   A CE1 1 
ATOM   2682 N  NE2 . HIS   A 1 382 ? -24.242 -29.817 -21.492 1.00 69.23  ? 402 HIS   A NE2 1 
ATOM   2683 N  N   . ARG   A 1 383 ? -21.291 -30.547 -27.447 1.00 81.13  ? 403 ARG   A N   1 
ATOM   2684 C  CA  . ARG   A 1 383 ? -20.644 -30.312 -28.730 1.00 83.95  ? 403 ARG   A CA  1 
ATOM   2685 C  C   . ARG   A 1 383 ? -21.106 -31.294 -29.801 1.00 89.84  ? 403 ARG   A C   1 
ATOM   2686 O  O   . ARG   A 1 383 ? -20.405 -31.486 -30.800 1.00 89.71  ? 403 ARG   A O   1 
ATOM   2687 C  CB  . ARG   A 1 383 ? -19.123 -30.389 -28.577 1.00 78.95  ? 403 ARG   A CB  1 
ATOM   2688 C  CG  . ARG   A 1 383 ? -18.539 -29.474 -27.511 1.00 82.95  ? 403 ARG   A CG  1 
ATOM   2689 C  CD  . ARG   A 1 383 ? -18.669 -28.009 -27.892 1.00 85.98  ? 403 ARG   A CD  1 
ATOM   2690 N  NE  . ARG   A 1 383 ? -17.928 -27.145 -26.980 1.00 84.63  ? 403 ARG   A NE  1 
ATOM   2691 C  CZ  . ARG   A 1 383 ? -16.677 -26.750 -27.173 1.00 85.47  ? 403 ARG   A CZ  1 
ATOM   2692 N  NH1 . ARG   A 1 383 ? -15.993 -27.117 -28.244 1.00 87.38  ? 403 ARG   A NH1 1 
ATOM   2693 N  NH2 . ARG   A 1 383 ? -16.097 -25.966 -26.268 1.00 81.10  ? 403 ARG   A NH2 1 
ATOM   2694 N  N   . ASP   A 1 384 ? -22.264 -31.920 -29.614 1.00 92.31  ? 404 ASP   A N   1 
ATOM   2695 C  CA  . ASP   A 1 384 ? -22.717 -32.966 -30.524 1.00 96.58  ? 404 ASP   A CA  1 
ATOM   2696 C  C   . ASP   A 1 384 ? -23.396 -32.348 -31.740 1.00 101.38 ? 404 ASP   A C   1 
ATOM   2697 O  O   . ASP   A 1 384 ? -24.407 -31.654 -31.585 1.00 104.35 ? 404 ASP   A O   1 
ATOM   2698 C  CB  . ASP   A 1 384 ? -23.676 -33.911 -29.807 1.00 97.19  ? 404 ASP   A CB  1 
ATOM   2699 C  CG  . ASP   A 1 384 ? -23.884 -35.217 -30.554 1.00 104.14 ? 404 ASP   A CG  1 
ATOM   2700 O  OD1 . ASP   A 1 384 ? -23.360 -35.358 -31.679 1.00 105.17 ? 404 ASP   A OD1 1 
ATOM   2701 O  OD2 . ASP   A 1 384 ? -24.569 -36.107 -30.006 1.00 102.82 ? 404 ASP   A OD2 1 
ATOM   2702 N  N   . PRO   A 1 385 ? -22.883 -32.568 -32.955 1.00 107.89 ? 405 PRO   A N   1 
ATOM   2703 C  CA  . PRO   A 1 385 ? -23.558 -32.030 -34.148 1.00 110.27 ? 405 PRO   A CA  1 
ATOM   2704 C  C   . PRO   A 1 385 ? -24.939 -32.622 -34.395 1.00 115.32 ? 405 PRO   A C   1 
ATOM   2705 O  O   . PRO   A 1 385 ? -25.680 -32.081 -35.226 1.00 120.94 ? 405 PRO   A O   1 
ATOM   2706 C  CB  . PRO   A 1 385 ? -22.593 -32.382 -35.290 1.00 110.11 ? 405 PRO   A CB  1 
ATOM   2707 C  CG  . PRO   A 1 385 ? -21.265 -32.590 -34.621 1.00 111.06 ? 405 PRO   A CG  1 
ATOM   2708 C  CD  . PRO   A 1 385 ? -21.587 -33.186 -33.285 1.00 106.98 ? 405 PRO   A CD  1 
ATOM   2709 N  N   . LYS   A 1 386 ? -25.305 -33.711 -33.716 1.00 114.71 ? 406 LYS   A N   1 
ATOM   2710 C  CA  . LYS   A 1 386 ? -26.638 -34.282 -33.865 1.00 122.75 ? 406 LYS   A CA  1 
ATOM   2711 C  C   . LYS   A 1 386 ? -27.703 -33.496 -33.112 1.00 122.14 ? 406 LYS   A C   1 
ATOM   2712 O  O   . LYS   A 1 386 ? -28.885 -33.594 -33.458 1.00 132.34 ? 406 LYS   A O   1 
ATOM   2713 C  CB  . LYS   A 1 386 ? -26.645 -35.739 -33.395 1.00 125.51 ? 406 LYS   A CB  1 
ATOM   2714 C  CG  . LYS   A 1 386 ? -26.129 -36.736 -34.421 1.00 139.59 ? 406 LYS   A CG  1 
ATOM   2715 C  CD  . LYS   A 1 386 ? -27.181 -37.037 -35.479 1.00 150.67 ? 406 LYS   A CD  1 
ATOM   2716 C  CE  . LYS   A 1 386 ? -26.711 -38.122 -36.437 1.00 153.32 ? 406 LYS   A CE  1 
ATOM   2717 N  NZ  . LYS   A 1 386 ? -27.799 -38.551 -37.360 1.00 152.37 ? 406 LYS   A NZ  1 
ATOM   2718 N  N   . TYR   A 1 387 ? -27.318 -32.726 -32.093 1.00 113.98 ? 407 TYR   A N   1 
ATOM   2719 C  CA  . TYR   A 1 387 ? -28.259 -31.910 -31.339 1.00 112.86 ? 407 TYR   A CA  1 
ATOM   2720 C  C   . TYR   A 1 387 ? -28.030 -30.415 -31.502 1.00 110.43 ? 407 TYR   A C   1 
ATOM   2721 O  O   . TYR   A 1 387 ? -28.909 -29.628 -31.131 1.00 111.43 ? 407 TYR   A O   1 
ATOM   2722 C  CB  . TYR   A 1 387 ? -28.203 -32.270 -29.846 1.00 107.78 ? 407 TYR   A CB  1 
ATOM   2723 C  CG  . TYR   A 1 387 ? -28.619 -33.693 -29.538 1.00 111.46 ? 407 TYR   A CG  1 
ATOM   2724 C  CD1 . TYR   A 1 387 ? -29.941 -34.096 -29.678 1.00 113.36 ? 407 TYR   A CD1 1 
ATOM   2725 C  CD2 . TYR   A 1 387 ? -27.693 -34.630 -29.098 1.00 116.11 ? 407 TYR   A CD2 1 
ATOM   2726 C  CE1 . TYR   A 1 387 ? -30.328 -35.394 -29.397 1.00 113.17 ? 407 TYR   A CE1 1 
ATOM   2727 C  CE2 . TYR   A 1 387 ? -28.070 -35.930 -28.812 1.00 116.38 ? 407 TYR   A CE2 1 
ATOM   2728 C  CZ  . TYR   A 1 387 ? -29.388 -36.306 -28.964 1.00 117.88 ? 407 TYR   A CZ  1 
ATOM   2729 O  OH  . TYR   A 1 387 ? -29.769 -37.598 -28.682 1.00 121.27 ? 407 TYR   A OH  1 
ATOM   2730 N  N   . TRP   A 1 388 ? -26.884 -30.001 -32.040 1.00 108.29 ? 408 TRP   A N   1 
ATOM   2731 C  CA  . TRP   A 1 388 ? -26.594 -28.591 -32.269 1.00 107.61 ? 408 TRP   A CA  1 
ATOM   2732 C  C   . TRP   A 1 388 ? -25.995 -28.430 -33.657 1.00 110.31 ? 408 TRP   A C   1 
ATOM   2733 O  O   . TRP   A 1 388 ? -25.070 -29.160 -34.022 1.00 110.78 ? 408 TRP   A O   1 
ATOM   2734 C  CB  . TRP   A 1 388 ? -25.621 -28.038 -31.217 1.00 103.81 ? 408 TRP   A CB  1 
ATOM   2735 C  CG  . TRP   A 1 388 ? -25.818 -28.580 -29.830 1.00 101.07 ? 408 TRP   A CG  1 
ATOM   2736 C  CD1 . TRP   A 1 388 ? -25.211 -29.675 -29.287 1.00 98.41  ? 408 TRP   A CD1 1 
ATOM   2737 C  CD2 . TRP   A 1 388 ? -26.669 -28.046 -28.807 1.00 95.72  ? 408 TRP   A CD2 1 
ATOM   2738 N  NE1 . TRP   A 1 388 ? -25.634 -29.859 -27.993 1.00 91.37  ? 408 TRP   A NE1 1 
ATOM   2739 C  CE2 . TRP   A 1 388 ? -26.530 -28.873 -27.674 1.00 87.31  ? 408 TRP   A CE2 1 
ATOM   2740 C  CE3 . TRP   A 1 388 ? -27.538 -26.953 -28.740 1.00 92.60  ? 408 TRP   A CE3 1 
ATOM   2741 C  CZ2 . TRP   A 1 388 ? -27.225 -28.641 -26.490 1.00 82.08  ? 408 TRP   A CZ2 1 
ATOM   2742 C  CZ3 . TRP   A 1 388 ? -28.227 -26.724 -27.563 1.00 92.06  ? 408 TRP   A CZ3 1 
ATOM   2743 C  CH2 . TRP   A 1 388 ? -28.066 -27.564 -26.454 1.00 87.15  ? 408 TRP   A CH2 1 
ATOM   2744 N  N   . THR   A 1 389 ? -26.519 -27.477 -34.425 1.00 110.20 ? 409 THR   A N   1 
ATOM   2745 C  CA  . THR   A 1 389 ? -25.952 -27.157 -35.729 1.00 116.63 ? 409 THR   A CA  1 
ATOM   2746 C  C   . THR   A 1 389 ? -24.751 -26.236 -35.555 1.00 114.56 ? 409 THR   A C   1 
ATOM   2747 O  O   . THR   A 1 389 ? -24.834 -25.223 -34.852 1.00 111.29 ? 409 THR   A O   1 
ATOM   2748 C  CB  . THR   A 1 389 ? -27.002 -26.500 -36.625 1.00 117.75 ? 409 THR   A CB  1 
ATOM   2749 O  OG1 . THR   A 1 389 ? -27.445 -25.275 -36.029 1.00 118.17 ? 409 THR   A OG1 1 
ATOM   2750 C  CG2 . THR   A 1 389 ? -28.202 -27.426 -36.812 1.00 118.65 ? 409 THR   A CG2 1 
ATOM   2751 N  N   . GLU   A 1 390 ? -23.639 -26.585 -36.211 1.00 109.69 ? 410 GLU   A N   1 
ATOM   2752 C  CA  . GLU   A 1 390 ? -22.362 -25.906 -36.019 1.00 106.76 ? 410 GLU   A CA  1 
ATOM   2753 C  C   . GLU   A 1 390 ? -22.075 -25.796 -34.525 1.00 101.46 ? 410 GLU   A C   1 
ATOM   2754 O  O   . GLU   A 1 390 ? -22.036 -24.687 -33.977 1.00 95.79  ? 410 GLU   A O   1 
ATOM   2755 C  CB  . GLU   A 1 390 ? -22.369 -24.527 -36.684 1.00 108.13 ? 410 GLU   A CB  1 
ATOM   2756 C  CG  . GLU   A 1 390 ? -22.312 -24.580 -38.206 1.00 113.25 ? 410 GLU   A CG  1 
ATOM   2757 C  CD  . GLU   A 1 390 ? -22.444 -23.212 -38.854 1.00 120.42 ? 410 GLU   A CD  1 
ATOM   2758 O  OE1 . GLU   A 1 390 ? -23.189 -22.362 -38.320 1.00 120.60 ? 410 GLU   A OE1 1 
ATOM   2759 O  OE2 . GLU   A 1 390 ? -21.800 -22.985 -39.901 1.00 124.77 ? 410 GLU   A OE2 1 
ATOM   2760 N  N   . PRO   A 1 391 ? -21.864 -26.924 -33.838 1.00 100.63 ? 411 PRO   A N   1 
ATOM   2761 C  CA  . PRO   A 1 391 ? -21.830 -26.893 -32.367 1.00 100.37 ? 411 PRO   A CA  1 
ATOM   2762 C  C   . PRO   A 1 391 ? -20.615 -26.191 -31.792 1.00 94.57  ? 411 PRO   A C   1 
ATOM   2763 O  O   . PRO   A 1 391 ? -20.652 -25.793 -30.621 1.00 91.36  ? 411 PRO   A O   1 
ATOM   2764 C  CB  . PRO   A 1 391 ? -21.842 -28.379 -31.988 1.00 99.63  ? 411 PRO   A CB  1 
ATOM   2765 C  CG  . PRO   A 1 391 ? -21.185 -29.051 -33.150 1.00 105.58 ? 411 PRO   A CG  1 
ATOM   2766 C  CD  . PRO   A 1 391 ? -21.588 -28.269 -34.371 1.00 102.61 ? 411 PRO   A CD  1 
ATOM   2767 N  N   . GLU   A 1 392 ? -19.542 -26.027 -32.563 1.00 96.59  ? 412 GLU   A N   1 
ATOM   2768 C  CA  . GLU   A 1 392 ? -18.364 -25.333 -32.063 1.00 94.78  ? 412 GLU   A CA  1 
ATOM   2769 C  C   . GLU   A 1 392 ? -18.521 -23.819 -32.075 1.00 91.99  ? 412 GLU   A C   1 
ATOM   2770 O  O   . GLU   A 1 392 ? -17.625 -23.117 -31.595 1.00 88.71  ? 412 GLU   A O   1 
ATOM   2771 C  CB  . GLU   A 1 392 ? -17.134 -25.731 -32.882 1.00 94.47  ? 412 GLU   A CB  1 
ATOM   2772 C  CG  . GLU   A 1 392 ? -15.902 -26.043 -32.046 1.00 97.15  ? 412 GLU   A CG  1 
ATOM   2773 C  CD  . GLU   A 1 392 ? -15.956 -27.419 -31.405 1.00 101.41 ? 412 GLU   A CD  1 
ATOM   2774 O  OE1 . GLU   A 1 392 ? -16.954 -28.141 -31.613 1.00 98.54  ? 412 GLU   A OE1 1 
ATOM   2775 O  OE2 . GLU   A 1 392 ? -14.993 -27.782 -30.696 1.00 99.41  ? 412 GLU   A OE2 1 
ATOM   2776 N  N   . LYS   A 1 393 ? -19.629 -23.304 -32.600 1.00 94.46  ? 413 LYS   A N   1 
ATOM   2777 C  CA  . LYS   A 1 393 ? -19.839 -21.870 -32.717 1.00 98.14  ? 413 LYS   A CA  1 
ATOM   2778 C  C   . LYS   A 1 393 ? -20.594 -21.331 -31.509 1.00 95.13  ? 413 LYS   A C   1 
ATOM   2779 O  O   . LYS   A 1 393 ? -21.450 -22.006 -30.930 1.00 93.75  ? 413 LYS   A O   1 
ATOM   2780 C  CB  . LYS   A 1 393 ? -20.611 -21.536 -33.995 1.00 101.28 ? 413 LYS   A CB  1 
ATOM   2781 C  CG  . LYS   A 1 393 ? -19.810 -21.690 -35.278 1.00 103.97 ? 413 LYS   A CG  1 
ATOM   2782 C  CD  . LYS   A 1 393 ? -20.565 -21.099 -36.462 1.00 110.06 ? 413 LYS   A CD  1 
ATOM   2783 C  CE  . LYS   A 1 393 ? -19.687 -20.998 -37.703 1.00 112.39 ? 413 LYS   A CE  1 
ATOM   2784 N  NZ  . LYS   A 1 393 ? -20.415 -20.377 -38.848 1.00 108.17 ? 413 LYS   A NZ  1 
ATOM   2785 N  N   . PHE   A 1 394 ? -20.263 -20.099 -31.133 1.00 92.33  ? 414 PHE   A N   1 
ATOM   2786 C  CA  . PHE   A 1 394 ? -20.945 -19.390 -30.054 1.00 89.26  ? 414 PHE   A CA  1 
ATOM   2787 C  C   . PHE   A 1 394 ? -22.162 -18.683 -30.640 1.00 89.48  ? 414 PHE   A C   1 
ATOM   2788 O  O   . PHE   A 1 394 ? -22.028 -17.666 -31.328 1.00 93.00  ? 414 PHE   A O   1 
ATOM   2789 C  CB  . PHE   A 1 394 ? -19.990 -18.407 -29.378 1.00 90.94  ? 414 PHE   A CB  1 
ATOM   2790 C  CG  . PHE   A 1 394 ? -20.669 -17.402 -28.489 1.00 90.54  ? 414 PHE   A CG  1 
ATOM   2791 C  CD1 . PHE   A 1 394 ? -21.106 -17.756 -27.224 1.00 82.19  ? 414 PHE   A CD1 1 
ATOM   2792 C  CD2 . PHE   A 1 394 ? -20.852 -16.096 -28.917 1.00 91.76  ? 414 PHE   A CD2 1 
ATOM   2793 C  CE1 . PHE   A 1 394 ? -21.727 -16.829 -26.408 1.00 80.86  ? 414 PHE   A CE1 1 
ATOM   2794 C  CE2 . PHE   A 1 394 ? -21.471 -15.167 -28.106 1.00 88.29  ? 414 PHE   A CE2 1 
ATOM   2795 C  CZ  . PHE   A 1 394 ? -21.909 -15.533 -26.850 1.00 90.28  ? 414 PHE   A CZ  1 
ATOM   2796 N  N   . LEU   A 1 395 ? -23.350 -19.229 -30.378 1.00 91.30  ? 415 LEU   A N   1 
ATOM   2797 C  CA  . LEU   A 1 395 ? -24.597 -18.688 -30.916 1.00 90.95  ? 415 LEU   A CA  1 
ATOM   2798 C  C   . LEU   A 1 395 ? -25.654 -18.702 -29.822 1.00 93.78  ? 415 LEU   A C   1 
ATOM   2799 O  O   . LEU   A 1 395 ? -26.347 -19.707 -29.617 1.00 97.05  ? 415 LEU   A O   1 
ATOM   2800 C  CB  . LEU   A 1 395 ? -25.065 -19.479 -32.139 1.00 89.99  ? 415 LEU   A CB  1 
ATOM   2801 C  CG  . LEU   A 1 395 ? -24.260 -19.298 -33.428 1.00 95.64  ? 415 LEU   A CG  1 
ATOM   2802 C  CD1 . LEU   A 1 395 ? -24.637 -20.359 -34.449 1.00 99.32  ? 415 LEU   A CD1 1 
ATOM   2803 C  CD2 . LEU   A 1 395 ? -24.477 -17.905 -33.999 1.00 91.37  ? 415 LEU   A CD2 1 
ATOM   2804 N  N   . PRO   A 1 396 ? -25.809 -17.592 -29.094 1.00 95.21  ? 416 PRO   A N   1 
ATOM   2805 C  CA  . PRO   A 1 396 ? -26.803 -17.555 -28.009 1.00 94.16  ? 416 PRO   A CA  1 
ATOM   2806 C  C   . PRO   A 1 396 ? -28.244 -17.642 -28.486 1.00 96.55  ? 416 PRO   A C   1 
ATOM   2807 O  O   . PRO   A 1 396 ? -29.142 -17.808 -27.650 1.00 90.39  ? 416 PRO   A O   1 
ATOM   2808 C  CB  . PRO   A 1 396 ? -26.525 -16.211 -27.323 1.00 92.67  ? 416 PRO   A CB  1 
ATOM   2809 C  CG  . PRO   A 1 396 ? -25.875 -15.376 -28.375 1.00 96.03  ? 416 PRO   A CG  1 
ATOM   2810 C  CD  . PRO   A 1 396 ? -25.061 -16.327 -29.207 1.00 91.33  ? 416 PRO   A CD  1 
ATOM   2811 N  N   . GLU   A 1 397 ? -28.498 -17.546 -29.793 1.00 104.06 ? 417 GLU   A N   1 
ATOM   2812 C  CA  . GLU   A 1 397 ? -29.855 -17.707 -30.297 1.00 105.31 ? 417 GLU   A CA  1 
ATOM   2813 C  C   . GLU   A 1 397 ? -30.375 -19.129 -30.145 1.00 104.20 ? 417 GLU   A C   1 
ATOM   2814 O  O   . GLU   A 1 397 ? -31.586 -19.339 -30.276 1.00 105.77 ? 417 GLU   A O   1 
ATOM   2815 C  CB  . GLU   A 1 397 ? -29.931 -17.275 -31.761 1.00 107.18 ? 417 GLU   A CB  1 
ATOM   2816 C  CG  . GLU   A 1 397 ? -30.312 -15.811 -31.946 1.00 120.06 ? 417 GLU   A CG  1 
ATOM   2817 C  CD  . GLU   A 1 397 ? -31.704 -15.503 -31.427 1.00 126.25 ? 417 GLU   A CD  1 
ATOM   2818 O  OE1 . GLU   A 1 397 ? -32.672 -16.133 -31.904 1.00 127.62 ? 417 GLU   A OE1 1 
ATOM   2819 O  OE2 . GLU   A 1 397 ? -31.828 -14.645 -30.528 1.00 123.35 ? 417 GLU   A OE2 1 
ATOM   2820 N  N   . ARG   A 1 398 ? -29.504 -20.102 -29.861 1.00 98.99  ? 418 ARG   A N   1 
ATOM   2821 C  CA  . ARG   A 1 398 ? -29.989 -21.447 -29.569 1.00 102.69 ? 418 ARG   A CA  1 
ATOM   2822 C  C   . ARG   A 1 398 ? -30.950 -21.443 -28.390 1.00 106.04 ? 418 ARG   A C   1 
ATOM   2823 O  O   . ARG   A 1 398 ? -31.845 -22.293 -28.315 1.00 110.01 ? 418 ARG   A O   1 
ATOM   2824 C  CB  . ARG   A 1 398 ? -28.827 -22.395 -29.269 1.00 98.02  ? 418 ARG   A CB  1 
ATOM   2825 C  CG  . ARG   A 1 398 ? -27.759 -22.498 -30.341 1.00 95.75  ? 418 ARG   A CG  1 
ATOM   2826 C  CD  . ARG   A 1 398 ? -26.706 -23.516 -29.917 1.00 84.37  ? 418 ARG   A CD  1 
ATOM   2827 N  NE  . ARG   A 1 398 ? -25.510 -23.468 -30.748 1.00 89.48  ? 418 ARG   A NE  1 
ATOM   2828 C  CZ  . ARG   A 1 398 ? -25.342 -24.165 -31.864 1.00 98.79  ? 418 ARG   A CZ  1 
ATOM   2829 N  NH1 . ARG   A 1 398 ? -26.293 -24.956 -32.334 1.00 99.93  ? 418 ARG   A NH1 1 
ATOM   2830 N  NH2 . ARG   A 1 398 ? -24.191 -24.068 -32.522 1.00 98.14  ? 418 ARG   A NH2 1 
ATOM   2831 N  N   . PHE   A 1 399 ? -30.779 -20.501 -27.462 1.00 98.23  ? 419 PHE   A N   1 
ATOM   2832 C  CA  . PHE   A 1 399 ? -31.605 -20.413 -26.265 1.00 99.96  ? 419 PHE   A CA  1 
ATOM   2833 C  C   . PHE   A 1 399 ? -32.640 -19.298 -26.356 1.00 105.66 ? 419 PHE   A C   1 
ATOM   2834 O  O   . PHE   A 1 399 ? -33.078 -18.772 -25.327 1.00 107.08 ? 419 PHE   A O   1 
ATOM   2835 C  CB  . PHE   A 1 399 ? -30.727 -20.224 -25.029 1.00 95.13  ? 419 PHE   A CB  1 
ATOM   2836 C  CG  . PHE   A 1 399 ? -29.843 -21.402 -24.729 1.00 92.67  ? 419 PHE   A CG  1 
ATOM   2837 C  CD1 . PHE   A 1 399 ? -28.630 -21.560 -25.380 1.00 89.42  ? 419 PHE   A CD1 1 
ATOM   2838 C  CD2 . PHE   A 1 399 ? -30.227 -22.355 -23.800 1.00 91.13  ? 419 PHE   A CD2 1 
ATOM   2839 C  CE1 . PHE   A 1 399 ? -27.816 -22.645 -25.111 1.00 83.16  ? 419 PHE   A CE1 1 
ATOM   2840 C  CE2 . PHE   A 1 399 ? -29.416 -23.443 -23.525 1.00 87.04  ? 419 PHE   A CE2 1 
ATOM   2841 C  CZ  . PHE   A 1 399 ? -28.209 -23.588 -24.182 1.00 86.39  ? 419 PHE   A CZ  1 
ATOM   2842 N  N   . SER   A 1 400 ? -33.043 -18.927 -27.568 1.00 110.03 ? 420 SER   A N   1 
ATOM   2843 C  CA  . SER   A 1 400 ? -34.074 -17.915 -27.738 1.00 116.56 ? 420 SER   A CA  1 
ATOM   2844 C  C   . SER   A 1 400 ? -35.436 -18.484 -27.344 1.00 124.02 ? 420 SER   A C   1 
ATOM   2845 O  O   . SER   A 1 400 ? -35.575 -19.659 -26.995 1.00 125.80 ? 420 SER   A O   1 
ATOM   2846 C  CB  . SER   A 1 400 ? -34.091 -17.405 -29.177 1.00 124.20 ? 420 SER   A CB  1 
ATOM   2847 O  OG  . SER   A 1 400 ? -34.434 -18.441 -30.080 1.00 132.04 ? 420 SER   A OG  1 
ATOM   2848 N  N   . LYS   A 1 401 ? -36.459 -17.628 -27.410 1.00 124.63 ? 421 LYS   A N   1 
ATOM   2849 C  CA  . LYS   A 1 401 ? -37.806 -18.041 -27.024 1.00 129.23 ? 421 LYS   A CA  1 
ATOM   2850 C  C   . LYS   A 1 401 ? -38.286 -19.230 -27.850 1.00 134.82 ? 421 LYS   A C   1 
ATOM   2851 O  O   . LYS   A 1 401 ? -38.833 -20.195 -27.304 1.00 131.97 ? 421 LYS   A O   1 
ATOM   2852 C  CB  . LYS   A 1 401 ? -38.774 -16.868 -27.171 1.00 126.13 ? 421 LYS   A CB  1 
ATOM   2853 C  CG  . LYS   A 1 401 ? -40.233 -17.283 -27.144 1.00 127.10 ? 421 LYS   A CG  1 
ATOM   2854 C  CD  . LYS   A 1 401 ? -41.105 -16.311 -27.912 1.00 127.20 ? 421 LYS   A CD  1 
ATOM   2855 C  CE  . LYS   A 1 401 ? -42.494 -16.886 -28.118 1.00 129.36 ? 421 LYS   A CE  1 
ATOM   2856 N  NZ  . LYS   A 1 401 ? -42.449 -18.185 -28.849 1.00 131.53 ? 421 LYS   A NZ  1 
ATOM   2857 N  N   . LYS   A 1 402 ? -38.082 -19.185 -29.167 1.00 146.18 ? 422 LYS   A N   1 
ATOM   2858 C  CA  . LYS   A 1 402 ? -38.560 -20.254 -30.035 1.00 143.18 ? 422 LYS   A CA  1 
ATOM   2859 C  C   . LYS   A 1 402 ? -37.613 -21.449 -30.065 1.00 146.09 ? 422 LYS   A C   1 
ATOM   2860 O  O   . LYS   A 1 402 ? -38.072 -22.591 -30.184 1.00 151.42 ? 422 LYS   A O   1 
ATOM   2861 C  CB  . LYS   A 1 402 ? -38.781 -19.719 -31.452 1.00 146.08 ? 422 LYS   A CB  1 
ATOM   2862 C  CG  . LYS   A 1 402 ? -37.518 -19.205 -32.124 1.00 145.49 ? 422 LYS   A CG  1 
ATOM   2863 C  CD  . LYS   A 1 402 ? -37.686 -17.776 -32.608 1.00 153.42 ? 422 LYS   A CD  1 
ATOM   2864 C  CE  . LYS   A 1 402 ? -36.441 -17.293 -33.331 1.00 154.35 ? 422 LYS   A CE  1 
ATOM   2865 N  NZ  . LYS   A 1 402 ? -35.224 -17.392 -32.480 1.00 151.77 ? 422 LYS   A NZ  1 
ATOM   2866 N  N   . ASN   A 1 403 ? -36.306 -21.219 -29.947 1.00 134.73 ? 423 ASN   A N   1 
ATOM   2867 C  CA  . ASN   A 1 403 ? -35.345 -22.309 -30.038 1.00 128.72 ? 423 ASN   A CA  1 
ATOM   2868 C  C   . ASN   A 1 403 ? -35.111 -23.009 -28.707 1.00 125.99 ? 423 ASN   A C   1 
ATOM   2869 O  O   . ASN   A 1 403 ? -34.386 -24.010 -28.674 1.00 126.76 ? 423 ASN   A O   1 
ATOM   2870 C  CB  . ASN   A 1 403 ? -34.014 -21.794 -30.592 1.00 125.28 ? 423 ASN   A CB  1 
ATOM   2871 C  CG  . ASN   A 1 403 ? -34.177 -21.043 -31.904 1.00 127.97 ? 423 ASN   A CG  1 
ATOM   2872 O  OD1 . ASN   A 1 403 ? -33.487 -20.060 -32.155 1.00 119.72 ? 423 ASN   A OD1 1 
ATOM   2873 N  ND2 . ASN   A 1 403 ? -35.103 -21.498 -32.742 1.00 140.06 ? 423 ASN   A ND2 1 
ATOM   2874 N  N   . LYS   A 1 404 ? -35.698 -22.508 -27.619 1.00 130.33 ? 424 LYS   A N   1 
ATOM   2875 C  CA  . LYS   A 1 404 ? -35.578 -23.156 -26.317 1.00 127.69 ? 424 LYS   A CA  1 
ATOM   2876 C  C   . LYS   A 1 404 ? -36.244 -24.529 -26.287 1.00 131.55 ? 424 LYS   A C   1 
ATOM   2877 O  O   . LYS   A 1 404 ? -35.825 -25.392 -25.507 1.00 130.63 ? 424 LYS   A O   1 
ATOM   2878 C  CB  . LYS   A 1 404 ? -36.169 -22.233 -25.242 1.00 127.52 ? 424 LYS   A CB  1 
ATOM   2879 C  CG  . LYS   A 1 404 ? -36.522 -22.885 -23.918 1.00 130.54 ? 424 LYS   A CG  1 
ATOM   2880 C  CD  . LYS   A 1 404 ? -38.030 -23.004 -23.763 1.00 132.84 ? 424 LYS   A CD  1 
ATOM   2881 C  CE  . LYS   A 1 404 ? -38.409 -23.727 -22.482 1.00 130.44 ? 424 LYS   A CE  1 
ATOM   2882 N  NZ  . LYS   A 1 404 ? -39.886 -23.870 -22.350 1.00 124.68 ? 424 LYS   A NZ  1 
ATOM   2883 N  N   . ASP   A 1 405 ? -37.250 -24.760 -27.133 1.00 133.96 ? 425 ASP   A N   1 
ATOM   2884 C  CA  . ASP   A 1 405 ? -37.981 -26.022 -27.101 1.00 135.23 ? 425 ASP   A CA  1 
ATOM   2885 C  C   . ASP   A 1 405 ? -37.207 -27.167 -27.744 1.00 135.62 ? 425 ASP   A C   1 
ATOM   2886 O  O   . ASP   A 1 405 ? -37.371 -28.322 -27.336 1.00 134.55 ? 425 ASP   A O   1 
ATOM   2887 C  CB  . ASP   A 1 405 ? -39.337 -25.860 -27.790 1.00 138.59 ? 425 ASP   A CB  1 
ATOM   2888 C  CG  . ASP   A 1 405 ? -40.245 -24.889 -27.064 1.00 146.49 ? 425 ASP   A CG  1 
ATOM   2889 O  OD1 . ASP   A 1 405 ? -39.913 -24.503 -25.924 1.00 142.69 ? 425 ASP   A OD1 1 
ATOM   2890 O  OD2 . ASP   A 1 405 ? -41.290 -24.508 -27.633 1.00 150.72 ? 425 ASP   A OD2 1 
ATOM   2891 N  N   . ASN   A 1 406 ? -36.365 -26.878 -28.738 1.00 130.30 ? 426 ASN   A N   1 
ATOM   2892 C  CA  . ASN   A 1 406 ? -35.632 -27.932 -29.431 1.00 127.89 ? 426 ASN   A CA  1 
ATOM   2893 C  C   . ASN   A 1 406 ? -34.517 -28.536 -28.586 1.00 126.28 ? 426 ASN   A C   1 
ATOM   2894 O  O   . ASN   A 1 406 ? -33.908 -29.523 -29.014 1.00 126.08 ? 426 ASN   A O   1 
ATOM   2895 C  CB  . ASN   A 1 406 ? -35.049 -27.393 -30.739 1.00 130.23 ? 426 ASN   A CB  1 
ATOM   2896 C  CG  . ASN   A 1 406 ? -36.112 -26.833 -31.665 1.00 134.23 ? 426 ASN   A CG  1 
ATOM   2897 O  OD1 . ASN   A 1 406 ? -36.413 -25.639 -31.633 1.00 135.80 ? 426 ASN   A OD1 1 
ATOM   2898 N  ND2 . ASN   A 1 406 ? -36.688 -27.694 -32.496 1.00 134.52 ? 426 ASN   A ND2 1 
ATOM   2899 N  N   . ILE   A 1 407 ? -34.238 -27.981 -27.412 1.00 121.30 ? 427 ILE   A N   1 
ATOM   2900 C  CA  . ILE   A 1 407 ? -33.152 -28.452 -26.562 1.00 114.61 ? 427 ILE   A CA  1 
ATOM   2901 C  C   . ILE   A 1 407 ? -33.700 -29.475 -25.578 1.00 109.90 ? 427 ILE   A C   1 
ATOM   2902 O  O   . ILE   A 1 407 ? -34.682 -29.211 -24.873 1.00 110.96 ? 427 ILE   A O   1 
ATOM   2903 C  CB  . ILE   A 1 407 ? -32.485 -27.281 -25.823 1.00 110.61 ? 427 ILE   A CB  1 
ATOM   2904 C  CG1 . ILE   A 1 407 ? -32.017 -26.219 -26.820 1.00 109.95 ? 427 ILE   A CG1 1 
ATOM   2905 C  CG2 . ILE   A 1 407 ? -31.319 -27.776 -24.981 1.00 102.53 ? 427 ILE   A CG2 1 
ATOM   2906 C  CD1 . ILE   A 1 407 ? -31.454 -24.977 -26.167 1.00 102.78 ? 427 ILE   A CD1 1 
ATOM   2907 N  N   . ASP   A 1 408 ? -33.072 -30.641 -25.530 1.00 104.61 ? 428 ASP   A N   1 
ATOM   2908 C  CA  . ASP   A 1 408 ? -33.471 -31.661 -24.569 1.00 98.25  ? 428 ASP   A CA  1 
ATOM   2909 C  C   . ASP   A 1 408 ? -32.807 -31.375 -23.225 1.00 91.41  ? 428 ASP   A C   1 
ATOM   2910 O  O   . ASP   A 1 408 ? -31.584 -31.213 -23.169 1.00 88.35  ? 428 ASP   A O   1 
ATOM   2911 C  CB  . ASP   A 1 408 ? -33.088 -33.051 -25.079 1.00 97.86  ? 428 ASP   A CB  1 
ATOM   2912 C  CG  . ASP   A 1 408 ? -33.741 -34.175 -24.287 1.00 95.11  ? 428 ASP   A CG  1 
ATOM   2913 O  OD1 . ASP   A 1 408 ? -33.604 -34.200 -23.046 1.00 91.04  ? 428 ASP   A OD1 1 
ATOM   2914 O  OD2 . ASP   A 1 408 ? -34.391 -35.042 -24.910 1.00 94.39  ? 428 ASP   A OD2 1 
ATOM   2915 N  N   . PRO   A 1 409 ? -33.572 -31.296 -22.131 1.00 92.37  ? 429 PRO   A N   1 
ATOM   2916 C  CA  . PRO   A 1 409 ? -32.972 -30.977 -20.827 1.00 85.19  ? 429 PRO   A CA  1 
ATOM   2917 C  C   . PRO   A 1 409 ? -32.085 -32.074 -20.265 1.00 86.80  ? 429 PRO   A C   1 
ATOM   2918 O  O   . PRO   A 1 409 ? -31.609 -31.937 -19.133 1.00 86.03  ? 429 PRO   A O   1 
ATOM   2919 C  CB  . PRO   A 1 409 ? -34.197 -30.749 -19.929 1.00 90.01  ? 429 PRO   A CB  1 
ATOM   2920 C  CG  . PRO   A 1 409 ? -35.272 -31.562 -20.559 1.00 94.32  ? 429 PRO   A CG  1 
ATOM   2921 C  CD  . PRO   A 1 409 ? -35.032 -31.471 -22.041 1.00 92.32  ? 429 PRO   A CD  1 
ATOM   2922 N  N   . TYR   A 1 410 ? -31.855 -33.157 -21.006 1.00 84.86  ? 430 TYR   A N   1 
ATOM   2923 C  CA  . TYR   A 1 410 ? -30.940 -34.208 -20.582 1.00 86.69  ? 430 TYR   A CA  1 
ATOM   2924 C  C   . TYR   A 1 410 ? -29.771 -34.368 -21.544 1.00 89.66  ? 430 TYR   A C   1 
ATOM   2925 O  O   . TYR   A 1 410 ? -28.977 -35.305 -21.395 1.00 87.08  ? 430 TYR   A O   1 
ATOM   2926 C  CB  . TYR   A 1 410 ? -31.698 -35.526 -20.411 1.00 87.71  ? 430 TYR   A CB  1 
ATOM   2927 C  CG  . TYR   A 1 410 ? -32.810 -35.409 -19.396 1.00 88.95  ? 430 TYR   A CG  1 
ATOM   2928 C  CD1 . TYR   A 1 410 ? -32.535 -35.406 -18.034 1.00 88.63  ? 430 TYR   A CD1 1 
ATOM   2929 C  CD2 . TYR   A 1 410 ? -34.133 -35.277 -19.797 1.00 91.99  ? 430 TYR   A CD2 1 
ATOM   2930 C  CE1 . TYR   A 1 410 ? -33.546 -35.288 -17.101 1.00 88.62  ? 430 TYR   A CE1 1 
ATOM   2931 C  CE2 . TYR   A 1 410 ? -35.151 -35.159 -18.871 1.00 91.59  ? 430 TYR   A CE2 1 
ATOM   2932 C  CZ  . TYR   A 1 410 ? -34.851 -35.163 -17.525 1.00 89.36  ? 430 TYR   A CZ  1 
ATOM   2933 O  OH  . TYR   A 1 410 ? -35.862 -35.047 -16.600 1.00 97.24  ? 430 TYR   A OH  1 
ATOM   2934 N  N   . ILE   A 1 411 ? -29.654 -33.482 -22.529 1.00 85.95  ? 431 ILE   A N   1 
ATOM   2935 C  CA  . ILE   A 1 411 ? -28.443 -33.350 -23.325 1.00 88.31  ? 431 ILE   A CA  1 
ATOM   2936 C  C   . ILE   A 1 411 ? -27.631 -32.136 -22.892 1.00 83.35  ? 431 ILE   A C   1 
ATOM   2937 O  O   . ILE   A 1 411 ? -26.406 -32.206 -22.793 1.00 78.74  ? 431 ILE   A O   1 
ATOM   2938 C  CB  . ILE   A 1 411 ? -28.797 -33.278 -24.826 1.00 85.13  ? 431 ILE   A CB  1 
ATOM   2939 C  CG1 . ILE   A 1 411 ? -29.661 -34.475 -25.227 1.00 93.76  ? 431 ILE   A CG1 1 
ATOM   2940 C  CG2 . ILE   A 1 411 ? -27.535 -33.223 -25.672 1.00 88.30  ? 431 ILE   A CG2 1 
ATOM   2941 C  CD1 . ILE   A 1 411 ? -29.006 -35.814 -24.971 1.00 95.43  ? 431 ILE   A CD1 1 
ATOM   2942 N  N   . TYR   A 1 412 ? -28.311 -31.025 -22.620 1.00 84.24  ? 432 TYR   A N   1 
ATOM   2943 C  CA  . TYR   A 1 412 ? -27.696 -29.816 -22.078 1.00 77.66  ? 432 TYR   A CA  1 
ATOM   2944 C  C   . TYR   A 1 412 ? -27.960 -29.801 -20.576 1.00 74.33  ? 432 TYR   A C   1 
ATOM   2945 O  O   . TYR   A 1 412 ? -29.058 -29.458 -20.131 1.00 75.04  ? 432 TYR   A O   1 
ATOM   2946 C  CB  . TYR   A 1 412 ? -28.255 -28.574 -22.766 1.00 81.19  ? 432 TYR   A CB  1 
ATOM   2947 C  CG  . TYR   A 1 412 ? -27.810 -27.266 -22.153 1.00 76.09  ? 432 TYR   A CG  1 
ATOM   2948 C  CD1 . TYR   A 1 412 ? -26.531 -26.773 -22.376 1.00 74.38  ? 432 TYR   A CD1 1 
ATOM   2949 C  CD2 . TYR   A 1 412 ? -28.672 -26.520 -21.360 1.00 75.41  ? 432 TYR   A CD2 1 
ATOM   2950 C  CE1 . TYR   A 1 412 ? -26.121 -25.576 -21.820 1.00 74.47  ? 432 TYR   A CE1 1 
ATOM   2951 C  CE2 . TYR   A 1 412 ? -28.271 -25.321 -20.800 1.00 77.28  ? 432 TYR   A CE2 1 
ATOM   2952 C  CZ  . TYR   A 1 412 ? -26.995 -24.855 -21.034 1.00 72.97  ? 432 TYR   A CZ  1 
ATOM   2953 O  OH  . TYR   A 1 412 ? -26.591 -23.664 -20.478 1.00 81.82  ? 432 TYR   A OH  1 
ATOM   2954 N  N   . THR   A 1 413 ? -26.952 -30.187 -19.796 1.00 74.62  ? 433 THR   A N   1 
ATOM   2955 C  CA  . THR   A 1 413 ? -27.065 -30.276 -18.338 1.00 73.58  ? 433 THR   A CA  1 
ATOM   2956 C  C   . THR   A 1 413 ? -25.841 -29.632 -17.699 1.00 72.58  ? 433 THR   A C   1 
ATOM   2957 O  O   . THR   A 1 413 ? -24.972 -30.317 -17.147 1.00 77.06  ? 433 THR   A O   1 
ATOM   2958 C  CB  . THR   A 1 413 ? -27.215 -31.732 -17.890 1.00 77.51  ? 433 THR   A CB  1 
ATOM   2959 O  OG1 . THR   A 1 413 ? -26.233 -32.541 -18.553 1.00 81.07  ? 433 THR   A OG1 1 
ATOM   2960 C  CG2 . THR   A 1 413 ? -28.603 -32.257 -18.218 1.00 74.12  ? 433 THR   A CG2 1 
ATOM   2961 N  N   . PRO   A 1 414 ? -25.745 -28.300 -17.749 1.00 73.83  ? 434 PRO   A N   1 
ATOM   2962 C  CA  . PRO   A 1 414 ? -24.577 -27.638 -17.147 1.00 74.96  ? 434 PRO   A CA  1 
ATOM   2963 C  C   . PRO   A 1 414 ? -24.572 -27.700 -15.632 1.00 69.19  ? 434 PRO   A C   1 
ATOM   2964 O  O   . PRO   A 1 414 ? -23.494 -27.674 -15.023 1.00 66.78  ? 434 PRO   A O   1 
ATOM   2965 C  CB  . PRO   A 1 414 ? -24.696 -26.194 -17.653 1.00 71.00  ? 434 PRO   A CB  1 
ATOM   2966 C  CG  . PRO   A 1 414 ? -26.161 -26.004 -17.865 1.00 66.35  ? 434 PRO   A CG  1 
ATOM   2967 C  CD  . PRO   A 1 414 ? -26.686 -27.333 -18.340 1.00 71.47  ? 434 PRO   A CD  1 
ATOM   2968 N  N   . PHE   A 1 415 ? -25.746 -27.775 -15.005 1.00 69.86  ? 435 PHE   A N   1 
ATOM   2969 C  CA  . PHE   A 1 415 ? -25.869 -27.928 -13.562 1.00 73.86  ? 435 PHE   A CA  1 
ATOM   2970 C  C   . PHE   A 1 415 ? -26.335 -29.327 -13.173 1.00 76.09  ? 435 PHE   A C   1 
ATOM   2971 O  O   . PHE   A 1 415 ? -26.719 -29.554 -12.020 1.00 72.58  ? 435 PHE   A O   1 
ATOM   2972 C  CB  . PHE   A 1 415 ? -26.824 -26.874 -12.997 1.00 72.39  ? 435 PHE   A CB  1 
ATOM   2973 C  CG  . PHE   A 1 415 ? -26.330 -25.458 -13.145 1.00 79.59  ? 435 PHE   A CG  1 
ATOM   2974 C  CD1 . PHE   A 1 415 ? -25.561 -24.871 -12.153 1.00 79.55  ? 435 PHE   A CD1 1 
ATOM   2975 C  CD2 . PHE   A 1 415 ? -26.642 -24.711 -14.271 1.00 71.85  ? 435 PHE   A CD2 1 
ATOM   2976 C  CE1 . PHE   A 1 415 ? -25.109 -23.571 -12.282 1.00 83.27  ? 435 PHE   A CE1 1 
ATOM   2977 C  CE2 . PHE   A 1 415 ? -26.192 -23.411 -14.405 1.00 80.55  ? 435 PHE   A CE2 1 
ATOM   2978 C  CZ  . PHE   A 1 415 ? -25.424 -22.841 -13.409 1.00 75.70  ? 435 PHE   A CZ  1 
ATOM   2979 N  N   . GLY   A 1 416 ? -26.302 -30.273 -14.109 1.00 76.74  ? 436 GLY   A N   1 
ATOM   2980 C  CA  . GLY   A 1 416 ? -26.838 -31.558 -13.735 1.00 76.46  ? 436 GLY   A CA  1 
ATOM   2981 C  C   . GLY   A 1 416 ? -28.352 -31.478 -13.612 1.00 80.07  ? 436 GLY   A C   1 
ATOM   2982 O  O   . GLY   A 1 416 ? -28.995 -30.510 -14.023 1.00 81.62  ? 436 GLY   A O   1 
ATOM   2983 N  N   . SER   A 1 417 ? -28.923 -32.534 -13.042 1.00 79.65  ? 437 SER   A N   1 
ATOM   2984 C  CA  . SER   A 1 417 ? -30.348 -32.559 -12.743 1.00 78.90  ? 437 SER   A CA  1 
ATOM   2985 C  C   . SER   A 1 417 ? -30.594 -33.645 -11.707 1.00 81.46  ? 437 SER   A C   1 
ATOM   2986 O  O   . SER   A 1 417 ? -29.713 -34.452 -11.402 1.00 75.66  ? 437 SER   A O   1 
ATOM   2987 C  CB  . SER   A 1 417 ? -31.190 -32.788 -14.003 1.00 82.14  ? 437 SER   A CB  1 
ATOM   2988 O  OG  . SER   A 1 417 ? -30.930 -34.059 -14.567 1.00 85.45  ? 437 SER   A OG  1 
ATOM   2989 N  N   . GLY   A 1 418 ? -31.806 -33.650 -11.161 1.00 83.73  ? 438 GLY   A N   1 
ATOM   2990 C  CA  . GLY   A 1 418 ? -32.176 -34.622 -10.163 1.00 85.13  ? 438 GLY   A CA  1 
ATOM   2991 C  C   . GLY   A 1 418 ? -31.856 -34.154 -8.759  1.00 84.67  ? 438 GLY   A C   1 
ATOM   2992 O  O   . GLY   A 1 418 ? -31.484 -32.998 -8.533  1.00 82.47  ? 438 GLY   A O   1 
ATOM   2993 N  N   . PRO   A 1 419 ? -32.004 -35.050 -7.782  1.00 87.08  ? 439 PRO   A N   1 
ATOM   2994 C  CA  . PRO   A 1 419 ? -31.754 -34.661 -6.385  1.00 85.00  ? 439 PRO   A CA  1 
ATOM   2995 C  C   . PRO   A 1 419 ? -30.311 -34.279 -6.093  1.00 85.80  ? 439 PRO   A C   1 
ATOM   2996 O  O   . PRO   A 1 419 ? -30.064 -33.601 -5.088  1.00 83.23  ? 439 PRO   A O   1 
ATOM   2997 C  CB  . PRO   A 1 419 ? -32.176 -35.909 -5.596  1.00 97.00  ? 439 PRO   A CB  1 
ATOM   2998 C  CG  . PRO   A 1 419 ? -33.129 -36.624 -6.499  1.00 94.07  ? 439 PRO   A CG  1 
ATOM   2999 C  CD  . PRO   A 1 419 ? -32.604 -36.391 -7.885  1.00 90.50  ? 439 PRO   A CD  1 
ATOM   3000 N  N   . ARG   A 1 420 ? -29.351 -34.689 -6.924  1.00 80.93  ? 440 ARG   A N   1 
ATOM   3001 C  CA  . ARG   A 1 420 ? -27.947 -34.341 -6.729  1.00 86.06  ? 440 ARG   A CA  1 
ATOM   3002 C  C   . ARG   A 1 420 ? -27.468 -33.285 -7.720  1.00 79.43  ? 440 ARG   A C   1 
ATOM   3003 O  O   . ARG   A 1 420 ? -26.281 -33.236 -8.053  1.00 80.63  ? 440 ARG   A O   1 
ATOM   3004 C  CB  . ARG   A 1 420 ? -27.053 -35.578 -6.821  1.00 81.84  ? 440 ARG   A CB  1 
ATOM   3005 C  CG  . ARG   A 1 420 ? -27.090 -36.464 -5.593  1.00 85.74  ? 440 ARG   A CG  1 
ATOM   3006 C  CD  . ARG   A 1 420 ? -25.746 -37.121 -5.315  1.00 84.17  ? 440 ARG   A CD  1 
ATOM   3007 N  NE  . ARG   A 1 420 ? -24.859 -36.287 -4.511  1.00 86.14  ? 440 ARG   A NE  1 
ATOM   3008 C  CZ  . ARG   A 1 420 ? -23.963 -36.760 -3.655  1.00 86.19  ? 440 ARG   A CZ  1 
ATOM   3009 N  NH1 . ARG   A 1 420 ? -23.832 -38.059 -3.439  1.00 85.26  ? 440 ARG   A NH1 1 
ATOM   3010 N  NH2 . ARG   A 1 420 ? -23.186 -35.908 -2.991  1.00 81.14  ? 440 ARG   A NH2 1 
ATOM   3011 N  N   . ASN   A 1 421 ? -28.370 -32.431 -8.197  1.00 84.65  ? 441 ASN   A N   1 
ATOM   3012 C  CA  . ASN   A 1 421 ? -27.965 -31.353 -9.086  1.00 79.66  ? 441 ASN   A CA  1 
ATOM   3013 C  C   . ASN   A 1 421 ? -27.209 -30.286 -8.294  1.00 80.16  ? 441 ASN   A C   1 
ATOM   3014 O  O   . ASN   A 1 421 ? -27.016 -30.390 -7.079  1.00 78.32  ? 441 ASN   A O   1 
ATOM   3015 C  CB  . ASN   A 1 421 ? -29.182 -30.759 -9.793  1.00 79.75  ? 441 ASN   A CB  1 
ATOM   3016 C  CG  . ASN   A 1 421 ? -30.000 -29.853 -8.892  1.00 80.66  ? 441 ASN   A CG  1 
ATOM   3017 O  OD1 . ASN   A 1 421 ? -30.141 -30.104 -7.696  1.00 86.13  ? 441 ASN   A OD1 1 
ATOM   3018 N  ND2 . ASN   A 1 421 ? -30.545 -28.787 -9.468  1.00 85.67  ? 441 ASN   A ND2 1 
ATOM   3019 N  N   . CYS   A 1 422 ? -26.773 -29.241 -8.995  1.00 84.38  ? 442 CYS   A N   1 
ATOM   3020 C  CA  . CYS   A 1 422 ? -26.060 -28.143 -8.349  1.00 85.72  ? 442 CYS   A CA  1 
ATOM   3021 C  C   . CYS   A 1 422 ? -27.003 -27.420 -7.396  1.00 84.87  ? 442 CYS   A C   1 
ATOM   3022 O  O   . CYS   A 1 422 ? -27.965 -26.778 -7.830  1.00 80.05  ? 442 CYS   A O   1 
ATOM   3023 C  CB  . CYS   A 1 422 ? -25.499 -27.185 -9.395  1.00 83.36  ? 442 CYS   A CB  1 
ATOM   3024 S  SG  . CYS   A 1 422 ? -24.567 -25.805 -8.695  1.00 71.13  ? 442 CYS   A SG  1 
ATOM   3025 N  N   . ILE   A 1 423 ? -26.731 -27.522 -6.093  1.00 81.07  ? 443 ILE   A N   1 
ATOM   3026 C  CA  . ILE   A 1 423 ? -27.608 -26.910 -5.103  1.00 84.24  ? 443 ILE   A CA  1 
ATOM   3027 C  C   . ILE   A 1 423 ? -27.500 -25.390 -5.117  1.00 89.97  ? 443 ILE   A C   1 
ATOM   3028 O  O   . ILE   A 1 423 ? -28.434 -24.701 -4.689  1.00 91.54  ? 443 ILE   A O   1 
ATOM   3029 C  CB  . ILE   A 1 423 ? -27.304 -27.476 -3.701  1.00 79.43  ? 443 ILE   A CB  1 
ATOM   3030 C  CG1 . ILE   A 1 423 ? -28.440 -27.160 -2.726  1.00 90.98  ? 443 ILE   A CG1 1 
ATOM   3031 C  CG2 . ILE   A 1 423 ? -25.986 -26.934 -3.174  1.00 83.60  ? 443 ILE   A CG2 1 
ATOM   3032 C  CD1 . ILE   A 1 423 ? -28.179 -27.644 -1.314  1.00 96.48  ? 443 ILE   A CD1 1 
ATOM   3033 N  N   . GLY   A 1 424 ? -26.391 -24.844 -5.610  1.00 84.99  ? 444 GLY   A N   1 
ATOM   3034 C  CA  . GLY   A 1 424 ? -26.224 -23.407 -5.675  1.00 92.29  ? 444 GLY   A CA  1 
ATOM   3035 C  C   . GLY   A 1 424 ? -26.405 -22.877 -7.080  1.00 92.05  ? 444 GLY   A C   1 
ATOM   3036 O  O   . GLY   A 1 424 ? -25.818 -21.855 -7.450  1.00 96.91  ? 444 GLY   A O   1 
ATOM   3037 N  N   . MET   A 1 425 ? -27.223 -23.574 -7.872  1.00 86.78  ? 445 MET   A N   1 
ATOM   3038 C  CA  . MET   A 1 425 ? -27.426 -23.185 -9.264  1.00 85.48  ? 445 MET   A CA  1 
ATOM   3039 C  C   . MET   A 1 425 ? -28.017 -21.785 -9.366  1.00 90.74  ? 445 MET   A C   1 
ATOM   3040 O  O   . MET   A 1 425 ? -27.495 -20.929 -10.089 1.00 86.84  ? 445 MET   A O   1 
ATOM   3041 C  CB  . MET   A 1 425 ? -28.331 -24.198 -9.962  1.00 80.83  ? 445 MET   A CB  1 
ATOM   3042 C  CG  . MET   A 1 425 ? -28.898 -23.698 -11.278 1.00 79.85  ? 445 MET   A CG  1 
ATOM   3043 S  SD  . MET   A 1 425 ? -30.210 -24.754 -11.914 1.00 85.78  ? 445 MET   A SD  1 
ATOM   3044 C  CE  . MET   A 1 425 ? -31.359 -24.729 -10.540 1.00 92.53  ? 445 MET   A CE  1 
ATOM   3045 N  N   . ARG   A 1 426 ? -29.108 -21.532 -8.641  1.00 95.57  ? 446 ARG   A N   1 
ATOM   3046 C  CA  A ARG   A 1 426 ? -29.769 -20.235 -8.739  0.66 94.78  ? 446 ARG   A CA  1 
ATOM   3047 C  CA  B ARG   A 1 426 ? -29.768 -20.235 -8.740  0.34 101.74 ? 446 ARG   A CA  1 
ATOM   3048 C  C   . ARG   A 1 426 ? -28.949 -19.132 -8.084  1.00 96.61  ? 446 ARG   A C   1 
ATOM   3049 O  O   . ARG   A 1 426 ? -29.024 -17.973 -8.508  1.00 94.81  ? 446 ARG   A O   1 
ATOM   3050 C  CB  A ARG   A 1 426 ? -31.165 -20.309 -8.122  0.66 99.37  ? 446 ARG   A CB  1 
ATOM   3051 C  CB  B ARG   A 1 426 ? -31.166 -20.319 -8.129  0.34 100.83 ? 446 ARG   A CB  1 
ATOM   3052 C  CG  A ARG   A 1 426 ? -32.082 -21.304 -8.812  0.66 100.03 ? 446 ARG   A CG  1 
ATOM   3053 C  CG  B ARG   A 1 426 ? -32.066 -21.297 -8.864  0.34 101.48 ? 446 ARG   A CG  1 
ATOM   3054 C  CD  A ARG   A 1 426 ? -33.533 -21.090 -8.419  0.66 103.03 ? 446 ARG   A CD  1 
ATOM   3055 C  CD  B ARG   A 1 426 ? -33.449 -21.388 -8.249  0.34 103.27 ? 446 ARG   A CD  1 
ATOM   3056 N  NE  A ARG   A 1 426 ? -33.775 -21.370 -7.009  0.66 108.92 ? 446 ARG   A NE  1 
ATOM   3057 N  NE  B ARG   A 1 426 ? -34.300 -22.302 -9.002  0.34 102.81 ? 446 ARG   A NE  1 
ATOM   3058 C  CZ  A ARG   A 1 426 ? -34.949 -21.223 -6.412  0.66 115.84 ? 446 ARG   A CZ  1 
ATOM   3059 C  CZ  B ARG   A 1 426 ? -35.549 -22.605 -8.679  0.34 105.17 ? 446 ARG   A CZ  1 
ATOM   3060 N  NH1 A ARG   A 1 426 ? -36.008 -20.781 -7.069  0.66 113.86 ? 446 ARG   A NH1 1 
ATOM   3061 N  NH1 B ARG   A 1 426 ? -36.132 -22.088 -7.610  0.34 109.07 ? 446 ARG   A NH1 1 
ATOM   3062 N  NH2 A ARG   A 1 426 ? -35.064 -21.528 -5.123  0.66 121.45 ? 446 ARG   A NH2 1 
ATOM   3063 N  NH2 B ARG   A 1 426 ? -36.231 -23.450 -9.448  0.34 105.83 ? 446 ARG   A NH2 1 
ATOM   3064 N  N   . PHE   A 1 427 ? -28.164 -19.463 -7.056  1.00 95.62  ? 447 PHE   A N   1 
ATOM   3065 C  CA  . PHE   A 1 427 ? -27.254 -18.469 -6.498  1.00 98.25  ? 447 PHE   A CA  1 
ATOM   3066 C  C   . PHE   A 1 427 ? -26.141 -18.146 -7.483  1.00 98.78  ? 447 PHE   A C   1 
ATOM   3067 O  O   . PHE   A 1 427 ? -25.748 -16.983 -7.627  1.00 98.54  ? 447 PHE   A O   1 
ATOM   3068 C  CB  . PHE   A 1 427 ? -26.669 -18.957 -5.174  1.00 100.31 ? 447 PHE   A CB  1 
ATOM   3069 C  CG  . PHE   A 1 427 ? -25.486 -18.154 -4.704  1.00 102.03 ? 447 PHE   A CG  1 
ATOM   3070 C  CD1 . PHE   A 1 427 ? -25.650 -16.858 -4.244  1.00 107.57 ? 447 PHE   A CD1 1 
ATOM   3071 C  CD2 . PHE   A 1 427 ? -24.211 -18.696 -4.725  1.00 103.11 ? 447 PHE   A CD2 1 
ATOM   3072 C  CE1 . PHE   A 1 427 ? -24.564 -16.117 -3.815  1.00 111.39 ? 447 PHE   A CE1 1 
ATOM   3073 C  CE2 . PHE   A 1 427 ? -23.122 -17.961 -4.297  1.00 102.48 ? 447 PHE   A CE2 1 
ATOM   3074 C  CZ  . PHE   A 1 427 ? -23.299 -16.669 -3.841  1.00 109.96 ? 447 PHE   A CZ  1 
ATOM   3075 N  N   . ALA   A 1 428 ? -25.629 -19.164 -8.179  1.00 95.76  ? 448 ALA   A N   1 
ATOM   3076 C  CA  . ALA   A 1 428 ? -24.581 -18.934 -9.168  1.00 98.17  ? 448 ALA   A CA  1 
ATOM   3077 C  C   . ALA   A 1 428 ? -25.109 -18.149 -10.362 1.00 94.18  ? 448 ALA   A C   1 
ATOM   3078 O  O   . ALA   A 1 428 ? -24.432 -17.244 -10.863 1.00 90.15  ? 448 ALA   A O   1 
ATOM   3079 C  CB  . ALA   A 1 428 ? -23.987 -20.266 -9.622  1.00 93.99  ? 448 ALA   A CB  1 
ATOM   3080 N  N   . LEU   A 1 429 ? -26.313 -18.482 -10.834 1.00 94.77  ? 449 LEU   A N   1 
ATOM   3081 C  CA  . LEU   A 1 429 ? -26.890 -17.750 -11.957 1.00 93.68  ? 449 LEU   A CA  1 
ATOM   3082 C  C   . LEU   A 1 429 ? -27.161 -16.297 -11.588 1.00 98.43  ? 449 LEU   A C   1 
ATOM   3083 O  O   . LEU   A 1 429 ? -26.908 -15.389 -12.388 1.00 90.77  ? 449 LEU   A O   1 
ATOM   3084 C  CB  . LEU   A 1 429 ? -28.176 -18.431 -12.428 1.00 91.26  ? 449 LEU   A CB  1 
ATOM   3085 C  CG  . LEU   A 1 429 ? -28.029 -19.797 -13.101 1.00 86.88  ? 449 LEU   A CG  1 
ATOM   3086 C  CD1 . LEU   A 1 429 ? -29.375 -20.293 -13.605 1.00 85.00  ? 449 LEU   A CD1 1 
ATOM   3087 C  CD2 . LEU   A 1 429 ? -27.019 -19.727 -14.235 1.00 83.49  ? 449 LEU   A CD2 1 
ATOM   3088 N  N   . MET   A 1 430 ? -27.673 -16.057 -10.380 1.00 99.38  ? 450 MET   A N   1 
ATOM   3089 C  CA  . MET   A 1 430 ? -27.948 -14.690 -9.952  1.00 99.73  ? 450 MET   A CA  1 
ATOM   3090 C  C   . MET   A 1 430 ? -26.657 -13.924 -9.692  1.00 101.62 ? 450 MET   A C   1 
ATOM   3091 O  O   . MET   A 1 430 ? -26.514 -12.770 -10.111 1.00 100.93 ? 450 MET   A O   1 
ATOM   3092 C  CB  . MET   A 1 430 ? -28.830 -14.700 -8.703  1.00 104.43 ? 450 MET   A CB  1 
ATOM   3093 C  CG  . MET   A 1 430 ? -29.091 -13.323 -8.118  1.00 108.28 ? 450 MET   A CG  1 
ATOM   3094 S  SD  . MET   A 1 430 ? -29.907 -12.224 -9.290  1.00 122.99 ? 450 MET   A SD  1 
ATOM   3095 C  CE  . MET   A 1 430 ? -31.413 -13.137 -9.614  1.00 124.30 ? 450 MET   A CE  1 
ATOM   3096 N  N   . ASN   A 1 431 ? -25.704 -14.553 -8.998  1.00 99.95  ? 451 ASN   A N   1 
ATOM   3097 C  CA  . ASN   A 1 431 ? -24.452 -13.874 -8.675  1.00 100.51 ? 451 ASN   A CA  1 
ATOM   3098 C  C   . ASN   A 1 431 ? -23.674 -13.518 -9.936  1.00 106.39 ? 451 ASN   A C   1 
ATOM   3099 O  O   . ASN   A 1 431 ? -23.034 -12.462 -10.002 1.00 103.69 ? 451 ASN   A O   1 
ATOM   3100 C  CB  . ASN   A 1 431 ? -23.609 -14.747 -7.744  1.00 102.93 ? 451 ASN   A CB  1 
ATOM   3101 C  CG  . ASN   A 1 431 ? -22.334 -14.064 -7.293  1.00 106.00 ? 451 ASN   A CG  1 
ATOM   3102 O  OD1 . ASN   A 1 431 ? -21.251 -14.647 -7.344  1.00 102.56 ? 451 ASN   A OD1 1 
ATOM   3103 N  ND2 . ASN   A 1 431 ? -22.455 -12.818 -6.850  1.00 106.62 ? 451 ASN   A ND2 1 
ATOM   3104 N  N   . MET   A 1 432 ? -23.724 -14.383 -10.951 1.00 93.76  ? 452 MET   A N   1 
ATOM   3105 C  CA  . MET   A 1 432 ? -23.046 -14.082 -12.208 1.00 97.63  ? 452 MET   A CA  1 
ATOM   3106 C  C   . MET   A 1 432 ? -23.783 -12.996 -12.983 1.00 99.14  ? 452 MET   A C   1 
ATOM   3107 O  O   . MET   A 1 432 ? -23.168 -12.035 -13.458 1.00 95.11  ? 452 MET   A O   1 
ATOM   3108 C  CB  . MET   A 1 432 ? -22.912 -15.346 -13.057 1.00 93.89  ? 452 MET   A CB  1 
ATOM   3109 C  CG  . MET   A 1 432 ? -21.917 -16.358 -12.519 1.00 92.07  ? 452 MET   A CG  1 
ATOM   3110 S  SD  . MET   A 1 432 ? -21.506 -17.626 -13.729 1.00 73.92  ? 452 MET   A SD  1 
ATOM   3111 C  CE  . MET   A 1 432 ? -23.138 -18.184 -14.211 1.00 77.25  ? 452 MET   A CE  1 
ATOM   3112 N  N   . LYS   A 1 433 ? -25.104 -13.134 -13.120 1.00 101.32 ? 453 LYS   A N   1 
ATOM   3113 C  CA  . LYS   A 1 433 ? -25.873 -12.164 -13.893 1.00 99.83  ? 453 LYS   A CA  1 
ATOM   3114 C  C   . LYS   A 1 433 ? -25.852 -10.787 -13.240 1.00 106.51 ? 453 LYS   A C   1 
ATOM   3115 O  O   . LYS   A 1 433 ? -25.820 -9.767  -13.938 1.00 104.53 ? 453 LYS   A O   1 
ATOM   3116 C  CB  . LYS   A 1 433 ? -27.307 -12.656 -14.076 1.00 96.12  ? 453 LYS   A CB  1 
ATOM   3117 C  CG  . LYS   A 1 433 ? -27.456 -13.773 -15.096 1.00 95.12  ? 453 LYS   A CG  1 
ATOM   3118 C  CD  . LYS   A 1 433 ? -28.885 -14.288 -15.145 1.00 96.73  ? 453 LYS   A CD  1 
ATOM   3119 C  CE  . LYS   A 1 433 ? -29.044 -15.372 -16.198 1.00 96.38  ? 453 LYS   A CE  1 
ATOM   3120 N  NZ  . LYS   A 1 433 ? -30.415 -15.951 -16.188 1.00 97.16  ? 453 LYS   A NZ  1 
ATOM   3121 N  N   . LEU   A 1 434 ? -25.871 -10.734 -11.905 1.00 106.25 ? 454 LEU   A N   1 
ATOM   3122 C  CA  . LEU   A 1 434 ? -25.696 -9.456  -11.222 1.00 107.78 ? 454 LEU   A CA  1 
ATOM   3123 C  C   . LEU   A 1 434 ? -24.336 -8.846  -11.531 1.00 110.31 ? 454 LEU   A C   1 
ATOM   3124 O  O   . LEU   A 1 434 ? -24.190 -7.619  -11.529 1.00 117.06 ? 454 LEU   A O   1 
ATOM   3125 C  CB  . LEU   A 1 434 ? -25.865 -9.630  -9.711  1.00 111.13 ? 454 LEU   A CB  1 
ATOM   3126 C  CG  . LEU   A 1 434 ? -27.288 -9.650  -9.151  1.00 116.73 ? 454 LEU   A CG  1 
ATOM   3127 C  CD1 . LEU   A 1 434 ? -27.284 -10.084 -7.695  1.00 118.54 ? 454 LEU   A CD1 1 
ATOM   3128 C  CD2 . LEU   A 1 434 ? -27.933 -8.282  -9.293  1.00 120.07 ? 454 LEU   A CD2 1 
ATOM   3129 N  N   . ALA   A 1 435 ? -23.333 -9.684  -11.801 1.00 107.30 ? 455 ALA   A N   1 
ATOM   3130 C  CA  . ALA   A 1 435 ? -22.013 -9.182  -12.160 1.00 109.26 ? 455 ALA   A CA  1 
ATOM   3131 C  C   . ALA   A 1 435 ? -21.963 -8.749  -13.620 1.00 112.37 ? 455 ALA   A C   1 
ATOM   3132 O  O   . ALA   A 1 435 ? -21.443 -7.674  -13.937 1.00 114.58 ? 455 ALA   A O   1 
ATOM   3133 C  CB  . ALA   A 1 435 ? -20.951 -10.246 -11.876 1.00 108.15 ? 455 ALA   A CB  1 
ATOM   3134 N  N   . LEU   A 1 436 ? -22.508 -9.572  -14.523 1.00 108.08 ? 456 LEU   A N   1 
ATOM   3135 C  CA  . LEU   A 1 436 ? -22.509 -9.238  -15.944 1.00 106.81 ? 456 LEU   A CA  1 
ATOM   3136 C  C   . LEU   A 1 436 ? -23.275 -7.956  -16.239 1.00 108.59 ? 456 LEU   A C   1 
ATOM   3137 O  O   . LEU   A 1 436 ? -23.010 -7.309  -17.258 1.00 108.16 ? 456 LEU   A O   1 
ATOM   3138 C  CB  . LEU   A 1 436 ? -23.113 -10.383 -16.759 1.00 102.27 ? 456 LEU   A CB  1 
ATOM   3139 C  CG  . LEU   A 1 436 ? -22.544 -11.789 -16.570 1.00 102.73 ? 456 LEU   A CG  1 
ATOM   3140 C  CD1 . LEU   A 1 436 ? -23.291 -12.779 -17.438 1.00 95.95  ? 456 LEU   A CD1 1 
ATOM   3141 C  CD2 . LEU   A 1 436 ? -21.068 -11.817 -16.891 1.00 102.90 ? 456 LEU   A CD2 1 
ATOM   3142 N  N   . ILE   A 1 437 ? -24.217 -7.579  -15.376 1.00 112.41 ? 457 ILE   A N   1 
ATOM   3143 C  CA  . ILE   A 1 437 ? -25.071 -6.428  -15.647 1.00 124.85 ? 457 ILE   A CA  1 
ATOM   3144 C  C   . ILE   A 1 437 ? -24.331 -5.124  -15.374 1.00 129.84 ? 457 ILE   A C   1 
ATOM   3145 O  O   . ILE   A 1 437 ? -24.292 -4.227  -16.225 1.00 131.00 ? 457 ILE   A O   1 
ATOM   3146 C  CB  . ILE   A 1 437 ? -26.368 -6.535  -14.823 1.00 119.39 ? 457 ILE   A CB  1 
ATOM   3147 C  CG1 . ILE   A 1 437 ? -27.355 -7.476  -15.517 1.00 114.16 ? 457 ILE   A CG1 1 
ATOM   3148 C  CG2 . ILE   A 1 437 ? -26.986 -5.163  -14.590 1.00 125.12 ? 457 ILE   A CG2 1 
ATOM   3149 C  CD1 . ILE   A 1 437 ? -28.538 -7.845  -14.664 1.00 114.25 ? 457 ILE   A CD1 1 
ATOM   3150 N  N   . ARG   A 1 438 ? -23.728 -4.998  -14.190 1.00 130.16 ? 458 ARG   A N   1 
ATOM   3151 C  CA  . ARG   A 1 438 ? -23.063 -3.748  -13.835 1.00 137.04 ? 458 ARG   A CA  1 
ATOM   3152 C  C   . ARG   A 1 438 ? -21.744 -3.570  -14.577 1.00 135.15 ? 458 ARG   A C   1 
ATOM   3153 O  O   . ARG   A 1 438 ? -21.369 -2.438  -14.902 1.00 139.34 ? 458 ARG   A O   1 
ATOM   3154 C  CB  . ARG   A 1 438 ? -22.836 -3.685  -12.324 1.00 137.96 ? 458 ARG   A CB  1 
ATOM   3155 C  CG  . ARG   A 1 438 ? -23.862 -2.851  -11.573 1.00 137.95 ? 458 ARG   A CG  1 
ATOM   3156 C  CD  . ARG   A 1 438 ? -23.783 -1.387  -11.985 1.00 141.75 ? 458 ARG   A CD  1 
ATOM   3157 N  NE  . ARG   A 1 438 ? -24.499 -0.513  -11.063 1.00 146.01 ? 458 ARG   A NE  1 
ATOM   3158 C  CZ  . ARG   A 1 438 ? -25.720 -0.039  -11.269 1.00 143.97 ? 458 ARG   A CZ  1 
ATOM   3159 N  NH1 . ARG   A 1 438 ? -26.400 -0.332  -12.365 1.00 141.88 ? 458 ARG   A NH1 1 
ATOM   3160 N  NH2 . ARG   A 1 438 ? -26.272 0.750   -10.352 1.00 140.11 ? 458 ARG   A NH2 1 
ATOM   3161 N  N   . VAL   A 1 439 ? -21.030 -4.664  -14.858 1.00 119.28 ? 459 VAL   A N   1 
ATOM   3162 C  CA  . VAL   A 1 439 ? -19.736 -4.536  -15.521 1.00 119.33 ? 459 VAL   A CA  1 
ATOM   3163 C  C   . VAL   A 1 439 ? -19.913 -4.159  -16.987 1.00 122.98 ? 459 VAL   A C   1 
ATOM   3164 O  O   . VAL   A 1 439 ? -19.031 -3.527  -17.583 1.00 125.80 ? 459 VAL   A O   1 
ATOM   3165 C  CB  . VAL   A 1 439 ? -18.916 -5.831  -15.361 1.00 120.17 ? 459 VAL   A CB  1 
ATOM   3166 C  CG1 . VAL   A 1 439 ? -19.440 -6.929  -16.277 1.00 117.19 ? 459 VAL   A CG1 1 
ATOM   3167 C  CG2 . VAL   A 1 439 ? -17.446 -5.562  -15.628 1.00 122.81 ? 459 VAL   A CG2 1 
ATOM   3168 N  N   . LEU   A 1 440 ? -21.044 -4.524  -17.592 1.00 128.00 ? 460 LEU   A N   1 
ATOM   3169 C  CA  . LEU   A 1 440 ? -21.326 -4.144  -18.969 1.00 124.39 ? 460 LEU   A CA  1 
ATOM   3170 C  C   . LEU   A 1 440 ? -22.099 -2.839  -19.072 1.00 123.82 ? 460 LEU   A C   1 
ATOM   3171 O  O   . LEU   A 1 440 ? -22.106 -2.222  -20.144 1.00 125.96 ? 460 LEU   A O   1 
ATOM   3172 C  CB  . LEU   A 1 440 ? -22.101 -5.257  -19.682 1.00 118.91 ? 460 LEU   A CB  1 
ATOM   3173 C  CG  . LEU   A 1 440 ? -21.296 -6.521  -19.993 1.00 115.69 ? 460 LEU   A CG  1 
ATOM   3174 C  CD1 . LEU   A 1 440 ? -22.183 -7.601  -20.594 1.00 109.78 ? 460 LEU   A CD1 1 
ATOM   3175 C  CD2 . LEU   A 1 440 ? -20.136 -6.198  -20.922 1.00 116.19 ? 460 LEU   A CD2 1 
ATOM   3176 N  N   . GLN   A 1 441 ? -22.747 -2.404  -17.989 1.00 127.71 ? 461 GLN   A N   1 
ATOM   3177 C  CA  . GLN   A 1 441 ? -23.378 -1.091  -17.973 1.00 129.77 ? 461 GLN   A CA  1 
ATOM   3178 C  C   . GLN   A 1 441 ? -22.358 0.037   -18.035 1.00 134.09 ? 461 GLN   A C   1 
ATOM   3179 O  O   . GLN   A 1 441 ? -22.719 1.163   -18.392 1.00 137.50 ? 461 GLN   A O   1 
ATOM   3180 C  CB  . GLN   A 1 441 ? -24.243 -0.932  -16.721 1.00 133.17 ? 461 GLN   A CB  1 
ATOM   3181 C  CG  . GLN   A 1 441 ? -25.712 -1.262  -16.924 1.00 132.05 ? 461 GLN   A CG  1 
ATOM   3182 C  CD  . GLN   A 1 441 ? -26.529 -1.096  -15.655 1.00 134.77 ? 461 GLN   A CD  1 
ATOM   3183 O  OE1 . GLN   A 1 441 ? -25.992 -1.124  -14.549 1.00 136.89 ? 461 GLN   A OE1 1 
ATOM   3184 N  NE2 . GLN   A 1 441 ? -27.836 -0.915  -15.812 1.00 132.68 ? 461 GLN   A NE2 1 
ATOM   3185 N  N   . ASN   A 1 442 ? -21.100 -0.239  -17.702 1.00 129.05 ? 462 ASN   A N   1 
ATOM   3186 C  CA  . ASN   A 1 442 ? -20.066 0.782   -17.642 1.00 137.51 ? 462 ASN   A CA  1 
ATOM   3187 C  C   . ASN   A 1 442 ? -18.904 0.550   -18.594 1.00 134.91 ? 462 ASN   A C   1 
ATOM   3188 O  O   . ASN   A 1 442 ? -18.329 1.525   -19.084 1.00 137.51 ? 462 ASN   A O   1 
ATOM   3189 C  CB  . ASN   A 1 442 ? -19.512 0.896   -16.211 1.00 136.46 ? 462 ASN   A CB  1 
ATOM   3190 C  CG  . ASN   A 1 442 ? -20.535 1.433   -15.230 1.00 140.69 ? 462 ASN   A CG  1 
ATOM   3191 O  OD1 . ASN   A 1 442 ? -20.674 2.644   -15.072 1.00 142.57 ? 462 ASN   A OD1 1 
ATOM   3192 N  ND2 . ASN   A 1 442 ? -21.254 0.533   -14.562 1.00 137.86 ? 462 ASN   A ND2 1 
ATOM   3193 N  N   . PHE   A 1 443 ? -18.546 -0.699  -18.879 1.00 131.20 ? 463 PHE   A N   1 
ATOM   3194 C  CA  . PHE   A 1 443 ? -17.332 -1.005  -19.617 1.00 130.23 ? 463 PHE   A CA  1 
ATOM   3195 C  C   . PHE   A 1 443 ? -17.638 -1.802  -20.879 1.00 123.45 ? 463 PHE   A C   1 
ATOM   3196 O  O   . PHE   A 1 443 ? -18.674 -2.465  -20.995 1.00 121.85 ? 463 PHE   A O   1 
ATOM   3197 C  CB  . PHE   A 1 443 ? -16.342 -1.795  -18.750 1.00 135.10 ? 463 PHE   A CB  1 
ATOM   3198 C  CG  . PHE   A 1 443 ? -16.020 -1.136  -17.440 1.00 138.88 ? 463 PHE   A CG  1 
ATOM   3199 C  CD1 . PHE   A 1 443 ? -14.964 -0.244  -17.337 1.00 143.07 ? 463 PHE   A CD1 1 
ATOM   3200 C  CD2 . PHE   A 1 443 ? -16.771 -1.410  -16.310 1.00 139.03 ? 463 PHE   A CD2 1 
ATOM   3201 C  CE1 . PHE   A 1 443 ? -14.668 0.363   -16.130 1.00 148.95 ? 463 PHE   A CE1 1 
ATOM   3202 C  CE2 . PHE   A 1 443 ? -16.480 -0.808  -15.103 1.00 142.20 ? 463 PHE   A CE2 1 
ATOM   3203 C  CZ  . PHE   A 1 443 ? -15.428 0.080   -15.012 1.00 149.64 ? 463 PHE   A CZ  1 
ATOM   3204 N  N   . SER   A 1 444 ? -16.709 -1.720  -21.829 1.00 130.32 ? 464 SER   A N   1 
ATOM   3205 C  CA  . SER   A 1 444 ? -16.672 -2.587  -22.995 1.00 124.94 ? 464 SER   A CA  1 
ATOM   3206 C  C   . SER   A 1 444 ? -15.372 -3.378  -22.981 1.00 126.78 ? 464 SER   A C   1 
ATOM   3207 O  O   . SER   A 1 444 ? -14.339 -2.898  -22.503 1.00 132.28 ? 464 SER   A O   1 
ATOM   3208 C  CB  . SER   A 1 444 ? -16.788 -1.793  -24.302 1.00 118.34 ? 464 SER   A CB  1 
ATOM   3209 O  OG  . SER   A 1 444 ? -18.142 -1.656  -24.703 1.00 119.94 ? 464 SER   A OG  1 
ATOM   3210 N  N   . PHE   A 1 445 ? -15.428 -4.596  -23.507 1.00 119.62 ? 465 PHE   A N   1 
ATOM   3211 C  CA  . PHE   A 1 445 ? -14.305 -5.520  -23.456 1.00 121.32 ? 465 PHE   A CA  1 
ATOM   3212 C  C   . PHE   A 1 445 ? -13.890 -5.903  -24.868 1.00 119.14 ? 465 PHE   A C   1 
ATOM   3213 O  O   . PHE   A 1 445 ? -14.738 -6.126  -25.739 1.00 115.20 ? 465 PHE   A O   1 
ATOM   3214 C  CB  . PHE   A 1 445 ? -14.662 -6.754  -22.624 1.00 117.18 ? 465 PHE   A CB  1 
ATOM   3215 C  CG  . PHE   A 1 445 ? -14.955 -6.437  -21.184 1.00 119.33 ? 465 PHE   A CG  1 
ATOM   3216 C  CD1 . PHE   A 1 445 ? -16.206 -5.979  -20.800 1.00 118.63 ? 465 PHE   A CD1 1 
ATOM   3217 C  CD2 . PHE   A 1 445 ? -13.974 -6.577  -20.217 1.00 118.11 ? 465 PHE   A CD2 1 
ATOM   3218 C  CE1 . PHE   A 1 445 ? -16.474 -5.675  -19.479 1.00 120.76 ? 465 PHE   A CE1 1 
ATOM   3219 C  CE2 . PHE   A 1 445 ? -14.237 -6.276  -18.895 1.00 118.76 ? 465 PHE   A CE2 1 
ATOM   3220 C  CZ  . PHE   A 1 445 ? -15.488 -5.825  -18.526 1.00 118.86 ? 465 PHE   A CZ  1 
ATOM   3221 N  N   . LYS   A 1 446 ? -12.579 -5.980  -25.085 1.00 115.83 ? 466 LYS   A N   1 
ATOM   3222 C  CA  . LYS   A 1 446 ? -11.998 -6.007  -26.418 1.00 120.81 ? 466 LYS   A CA  1 
ATOM   3223 C  C   . LYS   A 1 446 ? -10.753 -6.880  -26.399 1.00 120.57 ? 466 LYS   A C   1 
ATOM   3224 O  O   . LYS   A 1 446 ? -10.043 -6.916  -25.386 1.00 121.94 ? 466 LYS   A O   1 
ATOM   3225 C  CB  . LYS   A 1 446 ? -11.662 -4.577  -26.878 1.00 125.95 ? 466 LYS   A CB  1 
ATOM   3226 C  CG  . LYS   A 1 446 ? -10.664 -4.445  -28.013 1.00 128.70 ? 466 LYS   A CG  1 
ATOM   3227 C  CD  . LYS   A 1 446 ? -10.578 -2.996  -28.471 1.00 135.55 ? 466 LYS   A CD  1 
ATOM   3228 C  CE  . LYS   A 1 446 ? -9.388  -2.762  -29.383 1.00 143.23 ? 466 LYS   A CE  1 
ATOM   3229 N  NZ  . LYS   A 1 446 ? -8.097  -2.895  -28.652 1.00 145.39 ? 466 LYS   A NZ  1 
ATOM   3230 N  N   . PRO   A 1 447 ? -10.473 -7.606  -27.482 1.00 121.48 ? 467 PRO   A N   1 
ATOM   3231 C  CA  . PRO   A 1 447 ? -9.261  -8.436  -27.530 1.00 125.03 ? 467 PRO   A CA  1 
ATOM   3232 C  C   . PRO   A 1 447 ? -7.994  -7.604  -27.391 1.00 133.78 ? 467 PRO   A C   1 
ATOM   3233 O  O   . PRO   A 1 447 ? -8.007  -6.371  -27.396 1.00 139.05 ? 467 PRO   A O   1 
ATOM   3234 C  CB  . PRO   A 1 447 ? -9.341  -9.104  -28.907 1.00 124.68 ? 467 PRO   A CB  1 
ATOM   3235 C  CG  . PRO   A 1 447 ? -10.791 -9.097  -29.243 1.00 119.06 ? 467 PRO   A CG  1 
ATOM   3236 C  CD  . PRO   A 1 447 ? -11.343 -7.834  -28.649 1.00 121.07 ? 467 PRO   A CD  1 
ATOM   3237 N  N   . CYS   A 1 448 ? -6.872  -8.310  -27.273 1.00 142.65 ? 468 CYS   A N   1 
ATOM   3238 C  CA  . CYS   A 1 448 ? -5.580  -7.672  -27.076 1.00 145.30 ? 468 CYS   A CA  1 
ATOM   3239 C  C   . CYS   A 1 448 ? -4.492  -8.556  -27.668 1.00 147.15 ? 468 CYS   A C   1 
ATOM   3240 O  O   . CYS   A 1 448 ? -4.738  -9.694  -28.078 1.00 145.97 ? 468 CYS   A O   1 
ATOM   3241 C  CB  . CYS   A 1 448 ? -5.312  -7.405  -25.591 1.00 146.40 ? 468 CYS   A CB  1 
ATOM   3242 S  SG  . CYS   A 1 448 ? -3.595  -6.997  -25.204 1.00 167.75 ? 468 CYS   A SG  1 
ATOM   3243 N  N   . LYS   A 1 449 ? -3.273  -8.012  -27.713 1.00 149.27 ? 469 LYS   A N   1 
ATOM   3244 C  CA  . LYS   A 1 449 ? -2.133  -8.800  -28.166 1.00 150.49 ? 469 LYS   A CA  1 
ATOM   3245 C  C   . LYS   A 1 449 ? -1.791  -9.905  -27.175 1.00 149.64 ? 469 LYS   A C   1 
ATOM   3246 O  O   . LYS   A 1 449 ? -1.244  -10.942 -27.569 1.00 148.00 ? 469 LYS   A O   1 
ATOM   3247 C  CB  . LYS   A 1 449 ? -0.923  -7.893  -28.395 1.00 148.09 ? 469 LYS   A CB  1 
ATOM   3248 C  CG  . LYS   A 1 449 ? -0.547  -7.043  -27.193 1.00 152.00 ? 469 LYS   A CG  1 
ATOM   3249 C  CD  . LYS   A 1 449 ? 0.721   -6.245  -27.452 1.00 153.29 ? 469 LYS   A CD  1 
ATOM   3250 C  CE  . LYS   A 1 449 ? 1.089   -5.395  -26.248 1.00 163.96 ? 469 LYS   A CE  1 
ATOM   3251 N  NZ  . LYS   A 1 449 ? 2.371   -4.665  -26.449 1.00 171.55 ? 469 LYS   A NZ  1 
ATOM   3252 N  N   . GLU   A 1 450 ? -2.107  -9.707  -25.895 1.00 148.48 ? 470 GLU   A N   1 
ATOM   3253 C  CA  . GLU   A 1 450 ? -1.895  -10.712 -24.865 1.00 146.98 ? 470 GLU   A CA  1 
ATOM   3254 C  C   . GLU   A 1 450 ? -3.101  -11.629 -24.686 1.00 140.74 ? 470 GLU   A C   1 
ATOM   3255 O  O   . GLU   A 1 450 ? -3.273  -12.209 -23.608 1.00 140.13 ? 470 GLU   A O   1 
ATOM   3256 C  CB  . GLU   A 1 450 ? -1.549  -10.041 -23.534 1.00 152.55 ? 470 GLU   A CB  1 
ATOM   3257 C  CG  . GLU   A 1 450 ? -0.343  -9.116  -23.588 1.00 162.63 ? 470 GLU   A CG  1 
ATOM   3258 C  CD  . GLU   A 1 450 ? 0.018   -8.554  -22.226 1.00 168.15 ? 470 GLU   A CD  1 
ATOM   3259 O  OE1 . GLU   A 1 450 ? -0.427  -9.128  -21.209 1.00 164.90 ? 470 GLU   A OE1 1 
ATOM   3260 O  OE2 . GLU   A 1 450 ? 0.742   -7.538  -22.171 1.00 169.82 ? 470 GLU   A OE2 1 
ATOM   3261 N  N   . THR   A 1 451 ? -3.936  -11.767 -25.712 1.00 137.69 ? 471 THR   A N   1 
ATOM   3262 C  CA  . THR   A 1 451 ? -5.141  -12.583 -25.652 1.00 135.00 ? 471 THR   A CA  1 
ATOM   3263 C  C   . THR   A 1 451 ? -4.966  -13.812 -26.534 1.00 130.01 ? 471 THR   A C   1 
ATOM   3264 O  O   . THR   A 1 451 ? -4.502  -13.702 -27.674 1.00 126.76 ? 471 THR   A O   1 
ATOM   3265 C  CB  . THR   A 1 451 ? -6.368  -11.785 -26.100 1.00 131.77 ? 471 THR   A CB  1 
ATOM   3266 O  OG1 . THR   A 1 451 ? -6.485  -10.597 -25.307 1.00 134.37 ? 471 THR   A OG1 1 
ATOM   3267 C  CG2 . THR   A 1 451 ? -7.632  -12.616 -25.948 1.00 123.47 ? 471 THR   A CG2 1 
ATOM   3268 N  N   . GLN   A 1 452 ? -5.337  -14.976 -26.004 1.00 129.92 ? 472 GLN   A N   1 
ATOM   3269 C  CA  . GLN   A 1 452 ? -5.278  -16.221 -26.762 1.00 122.33 ? 472 GLN   A CA  1 
ATOM   3270 C  C   . GLN   A 1 452 ? -6.543  -16.348 -27.602 1.00 121.87 ? 472 GLN   A C   1 
ATOM   3271 O  O   . GLN   A 1 452 ? -7.641  -16.536 -27.065 1.00 118.71 ? 472 GLN   A O   1 
ATOM   3272 C  CB  . GLN   A 1 452 ? -5.118  -17.418 -25.829 1.00 118.69 ? 472 GLN   A CB  1 
ATOM   3273 C  CG  . GLN   A 1 452 ? -5.187  -18.759 -26.546 1.00 117.83 ? 472 GLN   A CG  1 
ATOM   3274 C  CD  . GLN   A 1 452 ? -4.969  -19.940 -25.620 1.00 121.16 ? 472 GLN   A CD  1 
ATOM   3275 O  OE1 . GLN   A 1 452 ? -5.831  -20.277 -24.808 1.00 114.92 ? 472 GLN   A OE1 1 
ATOM   3276 N  NE2 . GLN   A 1 452 ? -3.812  -20.579 -25.742 1.00 124.46 ? 472 GLN   A NE2 1 
ATOM   3277 N  N   . ILE   A 1 453 ? -6.392  -16.233 -28.922 1.00 115.70 ? 473 ILE   A N   1 
ATOM   3278 C  CA  . ILE   A 1 453 ? -7.494  -16.378 -29.859 1.00 116.07 ? 473 ILE   A CA  1 
ATOM   3279 C  C   . ILE   A 1 453 ? -7.041  -17.322 -30.967 1.00 117.81 ? 473 ILE   A C   1 
ATOM   3280 O  O   . ILE   A 1 453 ? -6.079  -17.020 -31.678 1.00 122.33 ? 473 ILE   A O   1 
ATOM   3281 C  CB  . ILE   A 1 453 ? -7.947  -15.035 -30.458 1.00 117.86 ? 473 ILE   A CB  1 
ATOM   3282 C  CG1 . ILE   A 1 453 ? -8.271  -14.030 -29.350 1.00 118.32 ? 473 ILE   A CG1 1 
ATOM   3283 C  CG2 . ILE   A 1 453 ? -9.150  -15.239 -31.370 1.00 123.60 ? 473 ILE   A CG2 1 
ATOM   3284 C  CD1 . ILE   A 1 453 ? -8.812  -12.715 -29.866 1.00 115.28 ? 473 ILE   A CD1 1 
ATOM   3285 N  N   . PRO   A 1 454 ? -7.696  -18.471 -31.159 1.00 114.91 ? 474 PRO   A N   1 
ATOM   3286 C  CA  . PRO   A 1 454 ? -8.851  -18.973 -30.403 1.00 115.56 ? 474 PRO   A CA  1 
ATOM   3287 C  C   . PRO   A 1 454 ? -8.446  -19.523 -29.039 1.00 113.02 ? 474 PRO   A C   1 
ATOM   3288 O  O   . PRO   A 1 454 ? -7.388  -20.131 -28.904 1.00 114.87 ? 474 PRO   A O   1 
ATOM   3289 C  CB  . PRO   A 1 454 ? -9.406  -20.064 -31.326 1.00 114.22 ? 474 PRO   A CB  1 
ATOM   3290 C  CG  . PRO   A 1 454 ? -8.185  -20.601 -32.016 1.00 117.52 ? 474 PRO   A CG  1 
ATOM   3291 C  CD  . PRO   A 1 454 ? -7.308  -19.394 -32.242 1.00 119.20 ? 474 PRO   A CD  1 
ATOM   3292 N  N   . LEU   A 1 455 ? -9.266  -19.311 -28.011 1.00 113.82 ? 475 LEU   A N   1 
ATOM   3293 C  CA  . LEU   A 1 455 ? -8.952  -19.825 -26.684 1.00 112.29 ? 475 LEU   A CA  1 
ATOM   3294 C  C   . LEU   A 1 455 ? -8.951  -21.347 -26.695 1.00 111.37 ? 475 LEU   A C   1 
ATOM   3295 O  O   . LEU   A 1 455 ? -9.874  -21.978 -27.219 1.00 110.64 ? 475 LEU   A O   1 
ATOM   3296 C  CB  . LEU   A 1 455 ? -9.962  -19.307 -25.661 1.00 108.70 ? 475 LEU   A CB  1 
ATOM   3297 C  CG  . LEU   A 1 455 ? -9.706  -19.628 -24.187 1.00 105.84 ? 475 LEU   A CG  1 
ATOM   3298 C  CD1 . LEU   A 1 455 ? -8.492  -18.867 -23.680 1.00 107.60 ? 475 LEU   A CD1 1 
ATOM   3299 C  CD2 . LEU   A 1 455 ? -10.931 -19.316 -23.341 1.00 99.67  ? 475 LEU   A CD2 1 
ATOM   3300 N  N   . LYS   A 1 456 ? -7.911  -21.936 -26.116 1.00 109.08 ? 476 LYS   A N   1 
ATOM   3301 C  CA  . LYS   A 1 456 ? -7.783  -23.381 -26.018 1.00 112.04 ? 476 LYS   A CA  1 
ATOM   3302 C  C   . LYS   A 1 456 ? -7.904  -23.811 -24.563 1.00 108.07 ? 476 LYS   A C   1 
ATOM   3303 O  O   . LYS   A 1 456 ? -7.316  -23.190 -23.671 1.00 110.24 ? 476 LYS   A O   1 
ATOM   3304 C  CB  . LYS   A 1 456 ? -6.448  -23.859 -26.597 1.00 114.87 ? 476 LYS   A CB  1 
ATOM   3305 C  CG  . LYS   A 1 456 ? -6.331  -25.371 -26.692 1.00 116.30 ? 476 LYS   A CG  1 
ATOM   3306 C  CD  . LYS   A 1 456 ? -7.407  -25.944 -27.600 1.00 114.86 ? 476 LYS   A CD  1 
ATOM   3307 C  CE  . LYS   A 1 456 ? -8.136  -27.104 -26.939 1.00 114.69 ? 476 LYS   A CE  1 
ATOM   3308 N  NZ  . LYS   A 1 456 ? -9.525  -26.736 -26.544 1.00 106.85 ? 476 LYS   A NZ  1 
ATOM   3309 N  N   . LEU   A 1 457 ? -8.711  -24.844 -24.315 1.00 112.78 ? 477 LEU   A N   1 
ATOM   3310 C  CA  . LEU   A 1 457 ? -8.954  -25.282 -22.915 1.00 110.15 ? 477 LEU   A CA  1 
ATOM   3311 C  C   . LEU   A 1 457 ? -7.873  -26.278 -22.492 1.00 114.23 ? 477 LEU   A C   1 
ATOM   3312 O  O   . LEU   A 1 457 ? -7.403  -27.042 -23.358 1.00 116.39 ? 477 LEU   A O   1 
ATOM   3313 C  CB  . LEU   A 1 457 ? -10.343 -25.921 -22.834 1.00 103.82 ? 477 LEU   A CB  1 
ATOM   3314 C  CG  . LEU   A 1 457 ? -11.482 -24.965 -22.486 1.00 98.72  ? 477 LEU   A CG  1 
ATOM   3315 C  CD1 . LEU   A 1 457 ? -12.832 -25.619 -22.738 1.00 93.49  ? 477 LEU   A CD1 1 
ATOM   3316 C  CD2 . LEU   A 1 457 ? -11.375 -24.506 -21.041 1.00 96.49  ? 477 LEU   A CD2 1 
ATOM   3317 N  N   . SER   A 1 458 ? -7.497  -26.263 -21.210 1.00 111.30 ? 478 SER   A N   1 
ATOM   3318 C  CA  . SER   A 1 458 ? -6.513  -27.251 -20.700 1.00 112.33 ? 478 SER   A CA  1 
ATOM   3319 C  C   . SER   A 1 458 ? -7.032  -28.624 -21.136 1.00 113.77 ? 478 SER   A C   1 
ATOM   3320 O  O   . SER   A 1 458 ? -8.172  -28.965 -20.765 1.00 110.47 ? 478 SER   A O   1 
ATOM   3321 C  CB  . SER   A 1 458 ? -6.329  -27.103 -19.214 1.00 108.75 ? 478 SER   A CB  1 
ATOM   3322 O  OG  . SER   A 1 458 ? -7.586  -27.057 -18.553 1.00 107.58 ? 478 SER   A OG  1 
ATOM   3323 N  N   . LEU   A 1 459 ? -6.238  -29.363 -21.915 1.00 120.10 ? 479 LEU   A N   1 
ATOM   3324 C  CA  . LEU   A 1 459 ? -6.638  -30.728 -22.349 1.00 112.53 ? 479 LEU   A CA  1 
ATOM   3325 C  C   . LEU   A 1 459 ? -6.355  -31.717 -21.215 1.00 109.10 ? 479 LEU   A C   1 
ATOM   3326 O  O   . LEU   A 1 459 ? -5.790  -32.791 -21.497 1.00 106.13 ? 479 LEU   A O   1 
ATOM   3327 C  CB  . LEU   A 1 459 ? -5.864  -31.097 -23.618 1.00 111.76 ? 479 LEU   A CB  1 
ATOM   3328 C  CG  . LEU   A 1 459 ? -6.185  -30.240 -24.841 1.00 114.05 ? 479 LEU   A CG  1 
ATOM   3329 C  CD1 . LEU   A 1 459 ? -5.263  -30.588 -25.999 1.00 115.50 ? 479 LEU   A CD1 1 
ATOM   3330 C  CD2 . LEU   A 1 459 ? -7.640  -30.408 -25.252 1.00 115.54 ? 479 LEU   A CD2 1 
ATOM   3331 N  N   . GLY   A 1 460 ? -6.729  -31.358 -19.983 1.00 108.76 ? 480 GLY   A N   1 
ATOM   3332 C  CA  . GLY   A 1 460 ? -6.521  -32.251 -18.827 1.00 105.32 ? 480 GLY   A CA  1 
ATOM   3333 C  C   . GLY   A 1 460 ? -7.843  -32.700 -18.232 1.00 108.36 ? 480 GLY   A C   1 
ATOM   3334 O  O   . GLY   A 1 460 ? -8.470  -33.611 -18.810 1.00 107.78 ? 480 GLY   A O   1 
ATOM   3335 N  N   . GLY   A 1 461 ? -8.259  -32.077 -17.125 1.00 106.05 ? 481 GLY   A N   1 
ATOM   3336 C  CA  . GLY   A 1 461 ? -9.521  -32.455 -16.460 1.00 107.97 ? 481 GLY   A CA  1 
ATOM   3337 C  C   . GLY   A 1 461 ? -10.139 -31.290 -15.711 1.00 113.45 ? 481 GLY   A C   1 
ATOM   3338 O  O   . GLY   A 1 461 ? -10.569 -31.495 -14.560 1.00 110.26 ? 481 GLY   A O   1 
ATOM   3339 N  N   . LEU   A 1 462 ? -10.183 -30.109 -16.335 1.00 117.27 ? 482 LEU   A N   1 
ATOM   3340 C  CA  . LEU   A 1 462 ? -10.706 -28.899 -15.645 1.00 117.33 ? 482 LEU   A CA  1 
ATOM   3341 C  C   . LEU   A 1 462 ? -11.176 -27.879 -16.684 1.00 113.87 ? 482 LEU   A C   1 
ATOM   3342 O  O   . LEU   A 1 462 ? -10.462 -27.699 -17.691 1.00 112.66 ? 482 LEU   A O   1 
ATOM   3343 C  CB  . LEU   A 1 462 ? -9.589  -28.309 -14.778 1.00 114.61 ? 482 LEU   A CB  1 
ATOM   3344 C  CG  . LEU   A 1 462 ? -8.172  -28.743 -15.151 1.00 114.39 ? 482 LEU   A CG  1 
ATOM   3345 C  CD1 . LEU   A 1 462 ? -7.273  -27.540 -15.381 1.00 113.07 ? 482 LEU   A CD1 1 
ATOM   3346 C  CD2 . LEU   A 1 462 ? -7.583  -29.652 -14.083 1.00 123.07 ? 482 LEU   A CD2 1 
ATOM   3347 N  N   . LEU   A 1 463 ? -12.332 -27.247 -16.451 1.00 105.70 ? 483 LEU   A N   1 
ATOM   3348 C  CA  . LEU   A 1 463 ? -12.798 -26.175 -17.371 1.00 101.61 ? 483 LEU   A CA  1 
ATOM   3349 C  C   . LEU   A 1 463 ? -11.871 -25.007 -17.031 1.00 100.54 ? 483 LEU   A C   1 
ATOM   3350 O  O   . LEU   A 1 463 ? -12.347 -24.005 -16.460 1.00 101.70 ? 483 LEU   A O   1 
ATOM   3351 C  CB  . LEU   A 1 463 ? -14.260 -25.832 -17.073 1.00 94.65  ? 483 LEU   A CB  1 
ATOM   3352 C  CG  . LEU   A 1 463 ? -14.888 -24.846 -18.056 1.00 89.74  ? 483 LEU   A CG  1 
ATOM   3353 C  CD1 . LEU   A 1 463 ? -15.061 -25.483 -19.425 1.00 85.35  ? 483 LEU   A CD1 1 
ATOM   3354 C  CD2 . LEU   A 1 463 ? -16.203 -24.301 -17.527 1.00 77.81  ? 483 LEU   A CD2 1 
ATOM   3355 N  N   . GLN   A 1 464 ? -10.584 -25.151 -17.342 1.00 103.77 ? 484 GLN   A N   1 
ATOM   3356 C  CA  . GLN   A 1 464 ? -9.644  -24.052 -17.184 1.00 98.66  ? 484 GLN   A CA  1 
ATOM   3357 C  C   . GLN   A 1 464 ? -9.023  -23.772 -18.543 1.00 100.35 ? 484 GLN   A C   1 
ATOM   3358 O  O   . GLN   A 1 464 ? -8.740  -24.719 -19.291 1.00 103.57 ? 484 GLN   A O   1 
ATOM   3359 C  CB  . GLN   A 1 464 ? -8.542  -24.370 -16.165 1.00 103.10 ? 484 GLN   A CB  1 
ATOM   3360 C  CG  . GLN   A 1 464 ? -9.016  -24.488 -14.721 1.00 106.22 ? 484 GLN   A CG  1 
ATOM   3361 C  CD  . GLN   A 1 464 ? -8.741  -23.237 -13.906 1.00 112.65 ? 484 GLN   A CD  1 
ATOM   3362 O  OE1 . GLN   A 1 464 ? -7.835  -22.464 -14.219 1.00 114.58 ? 484 GLN   A OE1 1 
ATOM   3363 N  NE2 . GLN   A 1 464 ? -9.524  -23.033 -12.852 1.00 110.22 ? 484 GLN   A NE2 1 
ATOM   3364 N  N   . PRO   A 1 465 ? -8.811  -22.508 -18.897 1.00 108.06 ? 485 PRO   A N   1 
ATOM   3365 C  CA  . PRO   A 1 465 ? -8.131  -22.202 -20.160 1.00 111.84 ? 485 PRO   A CA  1 
ATOM   3366 C  C   . PRO   A 1 465 ? -6.641  -22.493 -20.065 1.00 112.31 ? 485 PRO   A C   1 
ATOM   3367 O  O   . PRO   A 1 465 ? -6.054  -22.539 -18.982 1.00 110.49 ? 485 PRO   A O   1 
ATOM   3368 C  CB  . PRO   A 1 465 ? -8.390  -20.702 -20.358 1.00 106.69 ? 485 PRO   A CB  1 
ATOM   3369 C  CG  . PRO   A 1 465 ? -9.462  -20.339 -19.362 1.00 105.67 ? 485 PRO   A CG  1 
ATOM   3370 C  CD  . PRO   A 1 465 ? -9.293  -21.292 -18.224 1.00 105.04 ? 485 PRO   A CD  1 
ATOM   3371 N  N   . GLU   A 1 466 ? -6.028  -22.700 -21.233 1.00 110.94 ? 486 GLU   A N   1 
ATOM   3372 C  CA  . GLU   A 1 466 ? -4.577  -22.856 -21.281 1.00 114.60 ? 486 GLU   A CA  1 
ATOM   3373 C  C   . GLU   A 1 466 ? -3.882  -21.566 -20.863 1.00 118.59 ? 486 GLU   A C   1 
ATOM   3374 O  O   . GLU   A 1 466 ? -3.004  -21.573 -19.993 1.00 120.44 ? 486 GLU   A O   1 
ATOM   3375 C  CB  . GLU   A 1 466 ? -4.132  -23.278 -22.682 1.00 125.12 ? 486 GLU   A CB  1 
ATOM   3376 C  CG  . GLU   A 1 466 ? -4.402  -24.736 -23.018 1.00 127.58 ? 486 GLU   A CG  1 
ATOM   3377 C  CD  . GLU   A 1 466 ? -3.715  -25.174 -24.299 1.00 127.91 ? 486 GLU   A CD  1 
ATOM   3378 O  OE1 . GLU   A 1 466 ? -3.005  -24.346 -24.908 1.00 134.22 ? 486 GLU   A OE1 1 
ATOM   3379 O  OE2 . GLU   A 1 466 ? -3.883  -26.346 -24.696 1.00 125.64 ? 486 GLU   A OE2 1 
ATOM   3380 N  N   . LYS   A 1 467 ? -4.263  -20.451 -21.476 1.00 117.88 ? 487 LYS   A N   1 
ATOM   3381 C  CA  . LYS   A 1 467 ? -3.804  -19.127 -21.104 1.00 117.05 ? 487 LYS   A CA  1 
ATOM   3382 C  C   . LYS   A 1 467 ? -4.958  -18.324 -20.513 1.00 116.15 ? 487 LYS   A C   1 
ATOM   3383 O  O   . LYS   A 1 467 ? -6.106  -18.473 -20.944 1.00 117.77 ? 487 LYS   A O   1 
ATOM   3384 C  CB  . LYS   A 1 467 ? -3.228  -18.375 -22.310 1.00 118.41 ? 487 LYS   A CB  1 
ATOM   3385 C  CG  . LYS   A 1 467 ? -2.083  -19.097 -23.003 1.00 119.69 ? 487 LYS   A CG  1 
ATOM   3386 C  CD  . LYS   A 1 467 ? -1.705  -18.409 -24.305 1.00 124.55 ? 487 LYS   A CD  1 
ATOM   3387 C  CE  . LYS   A 1 467 ? -0.669  -19.213 -25.075 1.00 124.93 ? 487 LYS   A CE  1 
ATOM   3388 N  NZ  . LYS   A 1 467 ? -0.420  -18.647 -26.430 1.00 122.83 ? 487 LYS   A NZ  1 
ATOM   3389 N  N   . PRO   A 1 468 ? -4.693  -17.477 -19.520 1.00 114.60 ? 488 PRO   A N   1 
ATOM   3390 C  CA  . PRO   A 1 468 ? -5.777  -16.704 -18.904 1.00 113.70 ? 488 PRO   A CA  1 
ATOM   3391 C  C   . PRO   A 1 468 ? -6.447  -15.777 -19.908 1.00 114.40 ? 488 PRO   A C   1 
ATOM   3392 O  O   . PRO   A 1 468 ? -5.869  -15.389 -20.926 1.00 114.08 ? 488 PRO   A O   1 
ATOM   3393 C  CB  . PRO   A 1 468 ? -5.067  -15.908 -17.801 1.00 115.18 ? 488 PRO   A CB  1 
ATOM   3394 C  CG  . PRO   A 1 468 ? -3.807  -16.668 -17.533 1.00 118.09 ? 488 PRO   A CG  1 
ATOM   3395 C  CD  . PRO   A 1 468 ? -3.401  -17.242 -18.856 1.00 117.17 ? 488 PRO   A CD  1 
ATOM   3396 N  N   . VAL   A 1 469 ? -7.696  -15.432 -19.612 1.00 112.13 ? 489 VAL   A N   1 
ATOM   3397 C  CA  . VAL   A 1 469 ? -8.453  -14.499 -20.439 1.00 112.59 ? 489 VAL   A CA  1 
ATOM   3398 C  C   . VAL   A 1 469 ? -8.001  -13.086 -20.085 1.00 115.89 ? 489 VAL   A C   1 
ATOM   3399 O  O   . VAL   A 1 469 ? -8.359  -12.554 -19.031 1.00 118.00 ? 489 VAL   A O   1 
ATOM   3400 C  CB  . VAL   A 1 469 ? -9.963  -14.668 -20.244 1.00 105.81 ? 489 VAL   A CB  1 
ATOM   3401 C  CG1 . VAL   A 1 469 ? -10.719 -13.562 -20.965 1.00 103.83 ? 489 VAL   A CG1 1 
ATOM   3402 C  CG2 . VAL   A 1 469 ? -10.413 -16.030 -20.750 1.00 102.18 ? 489 VAL   A CG2 1 
ATOM   3403 N  N   . VAL   A 1 470 ? -7.204  -12.479 -20.960 1.00 117.20 ? 490 VAL   A N   1 
ATOM   3404 C  CA  . VAL   A 1 470 ? -6.685  -11.129 -20.763 1.00 125.05 ? 490 VAL   A CA  1 
ATOM   3405 C  C   . VAL   A 1 470 ? -7.268  -10.268 -21.877 1.00 127.93 ? 490 VAL   A C   1 
ATOM   3406 O  O   . VAL   A 1 470 ? -6.821  -10.338 -23.028 1.00 131.40 ? 490 VAL   A O   1 
ATOM   3407 C  CB  . VAL   A 1 470 ? -5.153  -11.087 -20.770 1.00 127.00 ? 490 VAL   A CB  1 
ATOM   3408 C  CG1 . VAL   A 1 470 ? -4.646  -10.204 -19.648 1.00 132.38 ? 490 VAL   A CG1 1 
ATOM   3409 C  CG2 . VAL   A 1 470 ? -4.578  -12.489 -20.643 1.00 124.30 ? 490 VAL   A CG2 1 
ATOM   3410 N  N   . LEU   A 1 471 ? -8.268  -9.457  -21.545 1.00 121.85 ? 491 LEU   A N   1 
ATOM   3411 C  CA  . LEU   A 1 471 ? -8.973  -8.638  -22.517 1.00 123.49 ? 491 LEU   A CA  1 
ATOM   3412 C  C   . LEU   A 1 471 ? -8.723  -7.160  -22.252 1.00 129.17 ? 491 LEU   A C   1 
ATOM   3413 O  O   . LEU   A 1 471 ? -8.553  -6.733  -21.107 1.00 132.17 ? 491 LEU   A O   1 
ATOM   3414 C  CB  . LEU   A 1 471 ? -10.477 -8.912  -22.479 1.00 115.23 ? 491 LEU   A CB  1 
ATOM   3415 C  CG  . LEU   A 1 471 ? -10.915 -10.362 -22.689 1.00 113.43 ? 491 LEU   A CG  1 
ATOM   3416 C  CD1 . LEU   A 1 471 ? -12.407 -10.509 -22.447 1.00 103.94 ? 491 LEU   A CD1 1 
ATOM   3417 C  CD2 . LEU   A 1 471 ? -10.542 -10.846 -24.081 1.00 116.52 ? 491 LEU   A CD2 1 
ATOM   3418 N  N   . LYS   A 1 472 ? -8.704  -6.383  -23.329 1.00 135.04 ? 492 LYS   A N   1 
ATOM   3419 C  CA  . LYS   A 1 472 ? -8.579  -4.935  -23.235 1.00 138.05 ? 492 LYS   A CA  1 
ATOM   3420 C  C   . LYS   A 1 472 ? -9.920  -4.339  -22.823 1.00 135.86 ? 492 LYS   A C   1 
ATOM   3421 O  O   . LYS   A 1 472 ? -10.903 -4.433  -23.566 1.00 135.99 ? 492 LYS   A O   1 
ATOM   3422 C  CB  . LYS   A 1 472 ? -8.118  -4.361  -24.572 1.00 143.99 ? 492 LYS   A CB  1 
ATOM   3423 C  CG  . LYS   A 1 472 ? -8.119  -2.850  -24.645 1.00 154.18 ? 492 LYS   A CG  1 
ATOM   3424 C  CD  . LYS   A 1 472 ? -6.771  -2.337  -25.118 1.00 168.33 ? 492 LYS   A CD  1 
ATOM   3425 C  CE  . LYS   A 1 472 ? -6.901  -1.000  -25.828 1.00 182.74 ? 492 LYS   A CE  1 
ATOM   3426 N  NZ  . LYS   A 1 472 ? -5.588  -0.552  -26.369 1.00 195.89 ? 492 LYS   A NZ  1 
ATOM   3427 N  N   . VAL   A 1 473 ? -9.961  -3.729  -21.644 1.00 132.79 ? 493 VAL   A N   1 
ATOM   3428 C  CA  . VAL   A 1 473 ? -11.188 -3.146  -21.115 1.00 134.28 ? 493 VAL   A CA  1 
ATOM   3429 C  C   . VAL   A 1 473 ? -11.238 -1.673  -21.495 1.00 145.30 ? 493 VAL   A C   1 
ATOM   3430 O  O   . VAL   A 1 473 ? -10.271 -0.931  -21.281 1.00 156.30 ? 493 VAL   A O   1 
ATOM   3431 C  CB  . VAL   A 1 473 ? -11.270 -3.325  -19.591 1.00 134.11 ? 493 VAL   A CB  1 
ATOM   3432 C  CG1 . VAL   A 1 473 ? -12.630 -2.880  -19.078 1.00 130.62 ? 493 VAL   A CG1 1 
ATOM   3433 C  CG2 . VAL   A 1 473 ? -10.992 -4.773  -19.210 1.00 132.98 ? 493 VAL   A CG2 1 
ATOM   3434 N  N   . GLU   A 1 474 ? -12.362 -1.249  -22.065 1.00 140.10 ? 494 GLU   A N   1 
ATOM   3435 C  CA  . GLU   A 1 474 ? -12.578 0.138   -22.442 1.00 144.11 ? 494 GLU   A CA  1 
ATOM   3436 C  C   . GLU   A 1 474 ? -13.807 0.668   -21.717 1.00 144.75 ? 494 GLU   A C   1 
ATOM   3437 O  O   . GLU   A 1 474 ? -14.683 -0.094  -21.299 1.00 140.00 ? 494 GLU   A O   1 
ATOM   3438 C  CB  . GLU   A 1 474 ? -12.741 0.279   -23.962 1.00 147.07 ? 494 GLU   A CB  1 
ATOM   3439 C  CG  . GLU   A 1 474 ? -11.828 -0.646  -24.755 1.00 148.06 ? 494 GLU   A CG  1 
ATOM   3440 C  CD  . GLU   A 1 474 ? -11.190 0.031   -25.951 1.00 150.58 ? 494 GLU   A CD  1 
ATOM   3441 O  OE1 . GLU   A 1 474 ? -11.761 1.021   -26.455 1.00 151.51 ? 494 GLU   A OE1 1 
ATOM   3442 O  OE2 . GLU   A 1 474 ? -10.111 -0.426  -26.383 1.00 154.87 ? 494 GLU   A OE2 1 
ATOM   3443 N  N   . SER   A 1 475 ? -13.865 1.986   -21.561 1.00 145.31 ? 495 SER   A N   1 
ATOM   3444 C  CA  . SER   A 1 475 ? -14.911 2.628   -20.779 1.00 144.10 ? 495 SER   A CA  1 
ATOM   3445 C  C   . SER   A 1 475 ? -15.736 3.563   -21.656 1.00 143.50 ? 495 SER   A C   1 
ATOM   3446 O  O   . SER   A 1 475 ? -15.396 3.843   -22.808 1.00 139.64 ? 495 SER   A O   1 
ATOM   3447 C  CB  . SER   A 1 475 ? -14.316 3.397   -19.593 1.00 144.69 ? 495 SER   A CB  1 
ATOM   3448 O  OG  . SER   A 1 475 ? -15.330 4.044   -18.846 1.00 143.79 ? 495 SER   A OG  1 
ATOM   3449 N  N   . ARG   A 1 476 ? -16.837 4.046   -21.087 1.00 140.70 ? 496 ARG   A N   1 
ATOM   3450 C  CA  . ARG   A 1 476 ? -17.728 4.966   -21.785 1.00 146.34 ? 496 ARG   A CA  1 
ATOM   3451 C  C   . ARG   A 1 476 ? -17.866 6.281   -21.025 1.00 142.42 ? 496 ARG   A C   1 
ATOM   3452 O  O   . ARG   A 1 476 ? -16.912 6.760   -20.411 1.00 144.64 ? 496 ARG   A O   1 
ATOM   3453 C  CB  . ARG   A 1 476 ? -19.105 4.329   -21.987 1.00 140.44 ? 496 ARG   A CB  1 
ATOM   3454 C  CG  . ARG   A 1 476 ? -19.824 3.984   -20.692 1.00 136.32 ? 496 ARG   A CG  1 
ATOM   3455 C  CD  . ARG   A 1 476 ? -21.150 3.288   -20.958 1.00 133.60 ? 496 ARG   A CD  1 
ATOM   3456 N  NE  . ARG   A 1 476 ? -20.972 2.019   -21.653 1.00 134.06 ? 496 ARG   A NE  1 
ATOM   3457 C  CZ  . ARG   A 1 476 ? -21.964 1.209   -21.999 1.00 128.56 ? 496 ARG   A CZ  1 
ATOM   3458 N  NH1 . ARG   A 1 476 ? -23.225 1.504   -21.728 1.00 126.34 ? 496 ARG   A NH1 1 
ATOM   3459 N  NH2 . ARG   A 1 476 ? -21.683 0.074   -22.634 1.00 125.59 ? 496 ARG   A NH2 1 
HETATM 3460 C  CHA . HEM   B 2 .   ? -23.017 -29.775 -7.703  1.00 76.17  ? 601 HEM   A CHA 1 
HETATM 3461 C  CHB . HEM   B 2 .   ? -22.139 -27.063 -11.639 1.00 78.16  ? 601 HEM   A CHB 1 
HETATM 3462 C  CHC . HEM   B 2 .   ? -21.870 -23.124 -8.823  1.00 81.44  ? 601 HEM   A CHC 1 
HETATM 3463 C  CHD . HEM   B 2 .   ? -22.516 -25.860 -4.865  1.00 80.81  ? 601 HEM   A CHD 1 
HETATM 3464 C  C1A . HEM   B 2 .   ? -22.806 -29.394 -9.013  1.00 77.49  ? 601 HEM   A C1A 1 
HETATM 3465 C  C2A . HEM   B 2 .   ? -22.815 -30.265 -10.172 1.00 79.26  ? 601 HEM   A C2A 1 
HETATM 3466 C  C3A . HEM   B 2 .   ? -22.573 -29.518 -11.256 1.00 72.05  ? 601 HEM   A C3A 1 
HETATM 3467 C  C4A . HEM   B 2 .   ? -22.403 -28.145 -10.826 1.00 78.13  ? 601 HEM   A C4A 1 
HETATM 3468 C  CMA . HEM   B 2 .   ? -22.486 -30.018 -12.715 1.00 65.44  ? 601 HEM   A CMA 1 
HETATM 3469 C  CAA . HEM   B 2 .   ? -23.059 -31.789 -10.151 1.00 70.40  ? 601 HEM   A CAA 1 
HETATM 3470 C  CBA . HEM   B 2 .   ? -24.508 -32.071 -10.532 1.00 73.49  ? 601 HEM   A CBA 1 
HETATM 3471 C  CGA . HEM   B 2 .   ? -24.682 -33.542 -10.802 1.00 71.68  ? 601 HEM   A CGA 1 
HETATM 3472 O  O1A . HEM   B 2 .   ? -25.805 -33.952 -11.193 1.00 71.46  ? 601 HEM   A O1A 1 
HETATM 3473 O  O2A . HEM   B 2 .   ? -23.695 -34.303 -10.630 1.00 67.27  ? 601 HEM   A O2A 1 
HETATM 3474 C  C1B . HEM   B 2 .   ? -22.036 -25.751 -11.227 1.00 80.98  ? 601 HEM   A C1B 1 
HETATM 3475 C  C2B . HEM   B 2 .   ? -21.915 -24.592 -12.091 1.00 79.55  ? 601 HEM   A C2B 1 
HETATM 3476 C  C3B . HEM   B 2 .   ? -21.838 -23.497 -11.311 1.00 85.02  ? 601 HEM   A C3B 1 
HETATM 3477 C  C4B . HEM   B 2 .   ? -21.912 -23.941 -9.932  1.00 78.76  ? 601 HEM   A C4B 1 
HETATM 3478 C  CMB . HEM   B 2 .   ? -21.884 -24.680 -13.634 1.00 72.22  ? 601 HEM   A CMB 1 
HETATM 3479 C  CAB . HEM   B 2 .   ? -21.702 -21.998 -11.698 1.00 79.62  ? 601 HEM   A CAB 1 
HETATM 3480 C  CBB . HEM   B 2 .   ? -21.684 -21.518 -12.947 1.00 79.35  ? 601 HEM   A CBB 1 
HETATM 3481 C  C1C . HEM   B 2 .   ? -22.051 -23.507 -7.512  1.00 81.52  ? 601 HEM   A C1C 1 
HETATM 3482 C  C2C . HEM   B 2 .   ? -22.129 -22.619 -6.373  1.00 92.19  ? 601 HEM   A C2C 1 
HETATM 3483 C  C3C . HEM   B 2 .   ? -22.307 -23.354 -5.273  1.00 83.82  ? 601 HEM   A C3C 1 
HETATM 3484 C  C4C . HEM   B 2 .   ? -22.351 -24.754 -5.675  1.00 84.13  ? 601 HEM   A C4C 1 
HETATM 3485 C  CMC . HEM   B 2 .   ? -22.021 -21.079 -6.420  1.00 81.85  ? 601 HEM   A CMC 1 
HETATM 3486 C  CAC . HEM   B 2 .   ? -22.435 -22.754 -3.853  1.00 87.89  ? 601 HEM   A CAC 1 
HETATM 3487 C  CBC . HEM   B 2 .   ? -22.557 -23.509 -2.758  1.00 94.36  ? 601 HEM   A CBC 1 
HETATM 3488 C  C1D . HEM   B 2 .   ? -22.659 -27.166 -5.283  1.00 79.37  ? 601 HEM   A C1D 1 
HETATM 3489 C  C2D . HEM   B 2 .   ? -22.736 -28.335 -4.430  1.00 77.95  ? 601 HEM   A C2D 1 
HETATM 3490 C  C3D . HEM   B 2 .   ? -22.871 -29.409 -5.212  1.00 81.52  ? 601 HEM   A C3D 1 
HETATM 3491 C  C4D . HEM   B 2 .   ? -22.890 -28.968 -6.591  1.00 72.73  ? 601 HEM   A C4D 1 
HETATM 3492 C  CMD . HEM   B 2 .   ? -22.666 -28.336 -2.886  1.00 74.90  ? 601 HEM   A CMD 1 
HETATM 3493 C  CAD . HEM   B 2 .   ? -22.996 -30.871 -4.734  1.00 69.42  ? 601 HEM   A CAD 1 
HETATM 3494 C  CBD . HEM   B 2 .   ? -24.456 -31.144 -4.391  1.00 77.68  ? 601 HEM   A CBD 1 
HETATM 3495 C  CGD . HEM   B 2 .   ? -24.601 -32.528 -3.815  1.00 84.01  ? 601 HEM   A CGD 1 
HETATM 3496 O  O1D . HEM   B 2 .   ? -25.717 -32.862 -3.340  1.00 84.46  ? 601 HEM   A O1D 1 
HETATM 3497 O  O2D . HEM   B 2 .   ? -23.603 -33.294 -3.827  1.00 80.29  ? 601 HEM   A O2D 1 
HETATM 3498 N  NA  . HEM   B 2 .   ? -22.553 -28.108 -9.452  1.00 82.66  ? 601 HEM   A NA  1 
HETATM 3499 N  NB  . HEM   B 2 .   ? -22.031 -25.316 -9.918  1.00 88.33  ? 601 HEM   A NB  1 
HETATM 3500 N  NC  . HEM   B 2 .   ? -22.190 -24.801 -7.048  1.00 88.23  ? 601 HEM   A NC  1 
HETATM 3501 N  ND  . HEM   B 2 .   ? -22.758 -27.592 -6.595  1.00 85.39  ? 601 HEM   A ND  1 
HETATM 3502 FE FE  . HEM   B 2 .   ? -22.331 -26.463 -8.246  1.00 70.67  ? 601 HEM   A FE  1 
HETATM 3503 C  C1  . GOL   C 3 .   ? -16.682 -19.128 -34.304 1.00 100.64 ? 602 GOL   A C1  1 
HETATM 3504 O  O1  . GOL   C 3 .   ? -16.199 -19.752 -33.172 1.00 107.04 ? 602 GOL   A O1  1 
HETATM 3505 C  C2  . GOL   C 3 .   ? -17.606 -17.999 -33.817 1.00 101.75 ? 602 GOL   A C2  1 
HETATM 3506 O  O2  . GOL   C 3 .   ? -17.790 -18.015 -32.435 1.00 96.76  ? 602 GOL   A O2  1 
HETATM 3507 C  C3  . GOL   C 3 .   ? -18.908 -18.260 -34.595 1.00 103.54 ? 602 GOL   A C3  1 
HETATM 3508 O  O3  . GOL   C 3 .   ? -19.952 -18.025 -33.721 1.00 103.34 ? 602 GOL   A O3  1 
HETATM 3509 C  C12 . A1A4V D 4 .   ? -19.578 -27.025 -6.822  1.00 83.19  ? 603 A1A4V A C12 1 
HETATM 3510 C  C14 . A1A4V D 4 .   ? -13.330 -32.080 -3.911  1.00 91.70  ? 603 A1A4V A C14 1 
HETATM 3511 C  C15 . A1A4V D 4 .   ? -12.911 -30.602 -3.860  1.00 86.65  ? 603 A1A4V A C15 1 
HETATM 3512 C  C16 . A1A4V D 4 .   ? -13.085 -29.801 -2.706  1.00 88.70  ? 603 A1A4V A C16 1 
HETATM 3513 C  C19 . A1A4V D 4 .   ? -12.031 -28.629 -5.000  1.00 95.79  ? 603 A1A4V A C19 1 
HETATM 3514 C  C20 . A1A4V D 4 .   ? -12.388 -29.976 -4.998  1.00 91.34  ? 603 A1A4V A C20 1 
HETATM 3515 C  C22 . A1A4V D 4 .   ? -16.798 -34.629 -5.443  1.00 93.28  ? 603 A1A4V A C22 1 
HETATM 3516 C  C23 . A1A4V D 4 .   ? -16.509 -34.545 -7.005  1.00 85.12  ? 603 A1A4V A C23 1 
HETATM 3517 C  C10 . A1A4V D 4 .   ? -19.468 -27.015 -9.127  1.00 76.72  ? 603 A1A4V A C10 1 
HETATM 3518 C  C13 . A1A4V D 4 .   ? -14.628 -32.395 -4.782  1.00 88.06  ? 603 A1A4V A C13 1 
HETATM 3519 C  C17 . A1A4V D 4 .   ? -12.727 -28.443 -2.700  1.00 94.02  ? 603 A1A4V A C17 1 
HETATM 3520 C  C18 . A1A4V D 4 .   ? -12.196 -27.849 -3.853  1.00 92.97  ? 603 A1A4V A C18 1 
HETATM 3521 C  C02 . A1A4V D 4 .   ? -15.817 -31.428 -4.558  1.00 78.15  ? 603 A1A4V A C02 1 
HETATM 3522 C  C04 . A1A4V D 4 .   ? -17.498 -29.746 -5.563  1.00 78.52  ? 603 A1A4V A C04 1 
HETATM 3523 C  C05 . A1A4V D 4 .   ? -17.178 -28.530 -4.667  1.00 87.07  ? 603 A1A4V A C05 1 
HETATM 3524 C  C06 . A1A4V D 4 .   ? -17.502 -27.164 -5.301  1.00 80.05  ? 603 A1A4V A C06 1 
HETATM 3525 C  C07 . A1A4V D 4 .   ? -18.173 -27.133 -6.674  1.00 78.99  ? 603 A1A4V A C07 1 
HETATM 3526 C  C08 . A1A4V D 4 .   ? -17.435 -27.166 -7.867  1.00 79.89  ? 603 A1A4V A C08 1 
HETATM 3527 C  C09 . A1A4V D 4 .   ? -18.073 -27.117 -9.102  1.00 76.57  ? 603 A1A4V A C09 1 
HETATM 3528 C  C24 . A1A4V D 4 .   ? -17.856 -34.517 -7.841  1.00 78.57  ? 603 A1A4V A C24 1 
HETATM 3529 C  C25 . A1A4V D 4 .   ? -18.450 -33.128 -8.129  1.00 76.04  ? 603 A1A4V A C25 1 
HETATM 3530 C  C26 . A1A4V D 4 .   ? -17.989 -32.360 -9.262  1.00 76.57  ? 603 A1A4V A C26 1 
HETATM 3531 C  C27 . A1A4V D 4 .   ? -16.990 -32.822 -10.156 1.00 74.59  ? 603 A1A4V A C27 1 
HETATM 3532 C  C28 . A1A4V D 4 .   ? -16.546 -32.106 -11.235 1.00 79.32  ? 603 A1A4V A C28 1 
HETATM 3533 C  C29 . A1A4V D 4 .   ? -17.096 -30.815 -11.510 1.00 79.13  ? 603 A1A4V A C29 1 
HETATM 3534 C  C30 . A1A4V D 4 .   ? -18.061 -30.332 -10.673 1.00 80.17  ? 603 A1A4V A C30 1 
HETATM 3535 C  C31 . A1A4V D 4 .   ? -18.530 -31.071 -9.548  1.00 79.29  ? 603 A1A4V A C31 1 
HETATM 3536 C  C32 . A1A4V D 4 .   ? -19.533 -30.560 -8.685  1.00 79.83  ? 603 A1A4V A C32 1 
HETATM 3537 C  C33 . A1A4V D 4 .   ? -19.974 -31.274 -7.610  1.00 80.87  ? 603 A1A4V A C33 1 
HETATM 3538 C  C34 . A1A4V D 4 .   ? -19.426 -32.577 -7.325  1.00 80.23  ? 603 A1A4V A C34 1 
HETATM 3539 C  C36 . A1A4V D 4 .   ? -14.438 -35.568 -8.171  1.00 93.58  ? 603 A1A4V A C36 1 
HETATM 3540 C  C38 . A1A4V D 4 .   ? -13.566 -36.779 -8.494  1.00 94.59  ? 603 A1A4V A C38 1 
HETATM 3541 C  C39 . A1A4V D 4 .   ? -13.791 -38.047 -7.939  1.00 91.32  ? 603 A1A4V A C39 1 
HETATM 3542 C  C41 . A1A4V D 4 .   ? -12.004 -39.048 -9.039  1.00 93.24  ? 603 A1A4V A C41 1 
HETATM 3543 C  C42 . A1A4V D 4 .   ? -11.682 -37.832 -9.656  1.00 96.48  ? 603 A1A4V A C42 1 
HETATM 3544 C  C43 . A1A4V D 4 .   ? -12.466 -36.702 -9.380  1.00 95.71  ? 603 A1A4V A C43 1 
HETATM 3545 N  N03 . A1A4V D 4 .   ? -16.373 -30.673 -5.661  1.00 83.09  ? 603 A1A4V A N03 1 
HETATM 3546 N  N11 . A1A4V D 4 .   ? -20.213 -26.970 -8.000  1.00 79.71  ? 603 A1A4V A N11 1 
HETATM 3547 N  N35 . A1A4V D 4 .   ? -15.609 -35.672 -7.379  1.00 89.97  ? 603 A1A4V A N35 1 
HETATM 3548 N  N40 . A1A4V D 4 .   ? -13.052 -39.154 -8.185  1.00 93.38  ? 603 A1A4V A N40 1 
HETATM 3549 O  O01 . A1A4V D 4 .   ? -16.260 -31.319 -3.429  1.00 79.02  ? 603 A1A4V A O01 1 
HETATM 3550 O  O37 . A1A4V D 4 .   ? -14.139 -34.469 -8.595  1.00 90.12  ? 603 A1A4V A O37 1 
HETATM 3551 S  S21 . A1A4V D 4 .   ? -15.335 -34.114 -4.406  1.00 83.77  ? 603 A1A4V A S21 1 
HETATM 3552 O  O   . HOH   E 5 .   ? -15.489 -33.390 -14.715 1.00 80.25  ? 701 HOH   A O   1 
HETATM 3553 O  O   . HOH   E 5 .   ? -20.347 -36.358 -4.645  1.00 93.00  ? 702 HOH   A O   1 
HETATM 3554 O  O   . HOH   E 5 .   ? -33.430 -15.261 -34.033 1.00 137.57 ? 703 HOH   A O   1 
HETATM 3555 O  O   . HOH   E 5 .   ? -5.316  -50.862 -12.311 1.00 123.50 ? 704 HOH   A O   1 
HETATM 3556 O  O   . HOH   E 5 .   ? -29.112 -36.534 -9.940  1.00 78.56  ? 705 HOH   A O   1 
HETATM 3557 O  O   . HOH   E 5 .   ? -24.794 -20.526 -38.912 1.00 137.04 ? 706 HOH   A O   1 
HETATM 3558 O  O   . HOH   E 5 .   ? -8.580  -43.830 9.094   1.00 154.45 ? 707 HOH   A O   1 
HETATM 3559 O  O   . HOH   E 5 .   ? -38.681 -21.295 -2.652  1.00 152.60 ? 708 HOH   A O   1 
HETATM 3560 O  O   . HOH   E 5 .   ? -28.482 -26.019 -33.169 1.00 106.85 ? 709 HOH   A O   1 
HETATM 3561 O  O   . HOH   E 5 .   ? -17.177 -35.475 -21.849 1.00 68.34  ? 710 HOH   A O   1 
HETATM 3562 O  O   . HOH   E 5 .   ? -14.578 -38.428 -14.395 1.00 77.38  ? 711 HOH   A O   1 
HETATM 3563 O  O   . HOH   E 5 .   ? -5.000  -55.489 -15.262 1.00 107.71 ? 712 HOH   A O   1 
HETATM 3564 O  O   . HOH   E 5 .   ? -4.337  -2.777  -19.141 1.00 198.33 ? 713 HOH   A O   1 
HETATM 3565 O  O   . HOH   E 5 .   ? -17.752 -38.857 -10.363 1.00 74.83  ? 714 HOH   A O   1 
HETATM 3566 O  O   . HOH   E 5 .   ? -17.949 -21.974 16.646  1.00 162.49 ? 715 HOH   A O   1 
HETATM 3567 O  O   . HOH   E 5 .   ? -24.043 -18.866 0.819   1.00 117.61 ? 716 HOH   A O   1 
HETATM 3568 O  O   . HOH   E 5 .   ? -22.250 -30.150 -17.578 1.00 82.42  ? 717 HOH   A O   1 
HETATM 3569 O  O   . HOH   E 5 .   ? -30.617 -26.342 -7.186  1.00 99.34  ? 718 HOH   A O   1 
HETATM 3570 O  O   . HOH   E 5 .   ? -9.421  -31.532 -20.586 1.00 103.58 ? 719 HOH   A O   1 
HETATM 3571 O  O   . HOH   E 5 .   ? -15.423 -41.972 -23.498 1.00 77.48  ? 720 HOH   A O   1 
HETATM 3572 O  O   . HOH   E 5 .   ? -16.861 -46.559 -35.713 1.00 117.90 ? 721 HOH   A O   1 
HETATM 3573 O  O   . HOH   E 5 .   ? -21.221 -35.111 -11.792 1.00 64.74  ? 722 HOH   A O   1 
HETATM 3574 O  O   . HOH   E 5 .   ? -12.355 -26.101 -26.968 1.00 98.62  ? 723 HOH   A O   1 
HETATM 3575 O  O   . HOH   E 5 .   ? -27.777 -46.406 -3.022  1.00 98.61  ? 724 HOH   A O   1 
HETATM 3576 O  O   . HOH   E 5 .   ? -10.471 -32.823 -22.061 1.00 92.89  ? 725 HOH   A O   1 
HETATM 3577 O  O   . HOH   E 5 .   ? -20.884 -17.360 -37.922 1.00 118.04 ? 726 HOH   A O   1 
HETATM 3578 O  O   . HOH   E 5 .   ? -35.477 -40.509 -6.829  1.00 106.81 ? 727 HOH   A O   1 
HETATM 3579 O  O   . HOH   E 5 .   ? -14.404 -6.279  -6.252  1.00 141.23 ? 728 HOH   A O   1 
HETATM 3580 O  O   . HOH   E 5 .   ? -29.605 -25.368 -31.202 1.00 91.49  ? 729 HOH   A O   1 
HETATM 3581 O  O   . HOH   E 5 .   ? -13.623 -23.821 -27.650 1.00 89.65  ? 730 HOH   A O   1 
HETATM 3582 O  O   . HOH   E 5 .   ? -41.642 -11.426 -11.469 1.00 133.77 ? 731 HOH   A O   1 
HETATM 3583 O  O   . HOH   E 5 .   ? -17.357 -53.977 -11.385 1.00 91.40  ? 732 HOH   A O   1 
HETATM 3584 O  O   . HOH   E 5 .   ? -18.422 -36.295 -11.244 1.00 71.71  ? 733 HOH   A O   1 
HETATM 3585 O  O   . HOH   E 5 .   ? -22.285 -15.845 -36.819 1.00 106.24 ? 734 HOH   A O   1 
HETATM 3586 O  O   . HOH   E 5 .   ? -14.764 -35.653 -13.879 1.00 81.19  ? 735 HOH   A O   1 
HETATM 3587 O  O   . HOH   E 5 .   ? -7.433  -35.709 -14.326 1.00 105.43 ? 736 HOH   A O   1 
HETATM 3588 O  O   . HOH   E 5 .   ? -5.121  -35.254 -15.235 1.00 101.72 ? 737 HOH   A O   1 
HETATM 3589 O  O   . HOH   E 5 .   ? -18.412 -51.641 -31.864 1.00 104.29 ? 738 HOH   A O   1 
HETATM 3590 O  O   . HOH   E 5 .   ? -24.613 -15.844 -37.063 1.00 115.34 ? 739 HOH   A O   1 
HETATM 3591 O  O   . HOH   E 5 .   ? -0.000  -50.045 -9.626  0.50 147.88 ? 740 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . HIS   A 8   ? 2.2946 2.0355 2.2404 0.4304  -0.0059 -0.0217 28  HIS   A N   
2    C  CA  . HIS   A 8   ? 2.3074 2.0122 2.2724 0.3985  -0.0102 -0.0014 28  HIS   A CA  
3    C  C   . HIS   A 8   ? 2.3143 1.9965 2.2923 0.3558  -0.0209 -0.0116 28  HIS   A C   
4    O  O   . HIS   A 8   ? 2.3750 1.9937 2.3382 0.3524  -0.0347 -0.0330 28  HIS   A O   
5    C  CB  . HIS   A 8   ? 2.2734 2.0412 2.2604 0.3901  -0.0008 0.0278  28  HIS   A CB  
6    C  CG  . HIS   A 8   ? 2.3429 2.1203 2.3226 0.4274  0.0037  0.0440  28  HIS   A CG  
7    N  ND1 . HIS   A 8   ? 2.3548 2.2065 2.3478 0.4342  0.0076  0.0610  28  HIS   A ND1 
8    C  CD2 . HIS   A 8   ? 2.3641 2.0846 2.3258 0.4602  0.0022  0.0463  28  HIS   A CD2 
9    C  CE1 . HIS   A 8   ? 2.3497 2.1948 2.3354 0.4700  0.0070  0.0736  28  HIS   A CE1 
10   N  NE2 . HIS   A 8   ? 2.3719 2.1375 2.3379 0.4878  0.0053  0.0656  28  HIS   A NE2 
11   N  N   . SER   A 9   ? 1.9024 1.6352 1.9080 0.3239  -0.0163 0.0033  29  SER   A N   
12   C  CA  . SER   A 9   ? 1.7540 1.4785 1.7796 0.2852  -0.0261 -0.0039 29  SER   A CA  
13   C  C   . SER   A 9   ? 1.5936 1.3417 1.6031 0.2865  -0.0352 -0.0309 29  SER   A C   
14   O  O   . SER   A 9   ? 1.4254 1.1761 1.4514 0.2564  -0.0459 -0.0370 29  SER   A O   
15   C  CB  . SER   A 9   ? 1.6247 1.3951 1.6820 0.2560  -0.0156 0.0207  29  SER   A CB  
16   O  OG  . SER   A 9   ? 1.4749 1.3197 1.5293 0.2631  -0.0073 0.0234  29  SER   A OG  
17   N  N   . HIS   A 10  ? 1.5450 1.3118 1.5234 0.3220  -0.0303 -0.0453 30  HIS   A N   
18   C  CA  . HIS   A 10  ? 1.4259 1.2144 1.3810 0.3267  -0.0349 -0.0685 30  HIS   A CA  
19   C  C   . HIS   A 10  ? 1.4908 1.2052 1.4197 0.3215  -0.0574 -0.0965 30  HIS   A C   
20   O  O   . HIS   A 10  ? 1.5010 1.2251 1.4081 0.3182  -0.0663 -0.1154 30  HIS   A O   
21   C  CB  . HIS   A 10  ? 1.3859 1.2144 1.3165 0.3688  -0.0189 -0.0736 30  HIS   A CB  
22   C  CG  . HIS   A 10  ? 1.3633 1.2808 1.3208 0.3663  -0.0029 -0.0519 30  HIS   A CG  
23   N  ND1 . HIS   A 10  ? 1.2509 1.2242 1.2021 0.3968  0.0127  -0.0512 30  HIS   A ND1 
24   C  CD2 . HIS   A 10  ? 1.1858 1.1440 1.1772 0.3364  -0.0007 -0.0303 30  HIS   A CD2 
25   C  CE1 . HIS   A 10  ? 1.1569 1.2010 1.1404 0.3824  0.0205  -0.0301 30  HIS   A CE1 
26   N  NE2 . HIS   A 10  ? 1.1224 1.1551 1.1257 0.3469  0.0120  -0.0187 30  HIS   A NE2 
27   N  N   . GLY   A 11  ? 1.6020 1.2398 1.5303 0.3203  -0.0686 -0.0994 31  GLY   A N   
28   C  CA  . GLY   A 11  ? 1.5664 1.1278 1.4749 0.3089  -0.0958 -0.1258 31  GLY   A CA  
29   C  C   . GLY   A 11  ? 1.5143 1.0667 1.4682 0.2595  -0.1142 -0.1183 31  GLY   A C   
30   O  O   . GLY   A 11  ? 1.5928 1.0783 1.5423 0.2437  -0.1415 -0.1369 31  GLY   A O   
31   N  N   . LEU   A 12  ? 1.4735 1.0912 1.4724 0.2350  -0.1008 -0.0919 32  LEU   A N   
32   C  CA  . LEU   A 12  ? 1.3998 1.0150 1.4510 0.1910  -0.1128 -0.0796 32  LEU   A CA  
33   C  C   . LEU   A 12  ? 1.3943 1.0091 1.4408 0.1732  -0.1403 -0.1027 32  LEU   A C   
34   O  O   . LEU   A 12  ? 1.4388 1.0000 1.5008 0.1507  -0.1682 -0.1142 32  LEU   A O   
35   C  CB  . LEU   A 12  ? 1.3133 0.9972 1.4043 0.1761  -0.0887 -0.0474 32  LEU   A CB  
36   C  CG  . LEU   A 12  ? 1.2858 0.9759 1.4364 0.1349  -0.0929 -0.0294 32  LEU   A CG  
37   C  CD1 . LEU   A 12  ? 1.2903 0.9192 1.4690 0.1215  -0.0934 -0.0146 32  LEU   A CD1 
38   C  CD2 . LEU   A 12  ? 1.1706 0.9306 1.3451 0.1268  -0.0688 -0.0043 32  LEU   A CD2 
39   N  N   . PHE   A 13  ? 1.3470 1.0203 1.3728 0.1822  -0.1347 -0.1085 33  PHE   A N   
40   C  CA  . PHE   A 13  ? 1.3591 1.0356 1.3770 0.1666  -0.1609 -0.1270 33  PHE   A CA  
41   C  C   . PHE   A 13  ? 1.4463 1.0502 1.4080 0.1821  -0.1894 -0.1632 33  PHE   A C   
42   O  O   . PHE   A 13  ? 1.4937 1.0739 1.4534 0.1628  -0.2227 -0.1804 33  PHE   A O   
43   C  CB  . PHE   A 13  ? 1.3258 1.0756 1.3273 0.1758  -0.1457 -0.1228 33  PHE   A CB  
44   C  CG  . PHE   A 13  ? 1.1550 0.9689 1.2066 0.1582  -0.1231 -0.0912 33  PHE   A CG  
45   C  CD1 . PHE   A 13  ? 1.0833 0.9068 1.1918 0.1238  -0.1313 -0.0760 33  PHE   A CD1 
46   C  CD2 . PHE   A 13  ? 1.0940 0.9578 1.1365 0.1768  -0.0943 -0.0770 33  PHE   A CD2 
47   C  CE1 . PHE   A 13  ? 1.0665 0.9421 1.2129 0.1115  -0.1087 -0.0489 33  PHE   A CE1 
48   C  CE2 . PHE   A 13  ? 1.0218 0.9354 1.1019 0.1612  -0.0766 -0.0512 33  PHE   A CE2 
49   C  CZ  . PHE   A 13  ? 0.9844 0.9010 1.1121 0.1301  -0.0825 -0.0380 33  PHE   A CZ  
50   N  N   . LYS   A 14  ? 1.4211 0.9871 1.3347 0.2186  -0.1786 -0.1759 34  LYS   A N   
51   C  CA  . LYS   A 14  ? 1.5785 1.0603 1.4341 0.2354  -0.2053 -0.2118 34  LYS   A CA  
52   C  C   . LYS   A 14  ? 1.5727 0.9808 1.4634 0.2031  -0.2366 -0.2157 34  LYS   A C   
53   O  O   . LYS   A 14  ? 1.5617 0.9126 1.4281 0.1920  -0.2750 -0.2438 34  LYS   A O   
54   C  CB  . LYS   A 14  ? 1.5961 1.0532 1.3985 0.2847  -0.1828 -0.2215 34  LYS   A CB  
55   C  CG  . LYS   A 14  ? 1.6857 1.1983 1.4396 0.3212  -0.1591 -0.2278 34  LYS   A CG  
56   C  CD  . LYS   A 14  ? 1.6724 1.1469 1.3709 0.3729  -0.1424 -0.2433 34  LYS   A CD  
57   C  CE  . LYS   A 14  ? 1.7155 1.2416 1.3649 0.4103  -0.1181 -0.2507 34  LYS   A CE  
58   N  NZ  . LYS   A 14  ? 1.7937 1.2796 1.3875 0.4649  -0.1013 -0.2681 34  LYS   A NZ  
59   N  N   . LYS   A 15  ? 1.6339 1.0412 1.5816 0.1868  -0.2215 -0.1868 35  LYS   A N   
60   C  CA  . LYS   A 15  ? 1.6483 0.9883 1.6381 0.1539  -0.2465 -0.1845 35  LYS   A CA  
61   C  C   . LYS   A 15  ? 1.6312 1.0016 1.6876 0.1059  -0.2688 -0.1742 35  LYS   A C   
62   O  O   . LYS   A 15  ? 1.6794 0.9960 1.7740 0.0743  -0.2980 -0.1770 35  LYS   A O   
63   C  CB  . LYS   A 15  ? 1.6991 1.0277 1.7242 0.1545  -0.2190 -0.1529 35  LYS   A CB  
64   C  CG  . LYS   A 15  ? 1.8109 1.1027 1.7785 0.2022  -0.2008 -0.1608 35  LYS   A CG  
65   C  CD  . LYS   A 15  ? 1.7617 1.0537 1.7627 0.2039  -0.1730 -0.1247 35  LYS   A CD  
66   C  CE  . LYS   A 15  ? 1.7615 1.0736 1.7183 0.2542  -0.1455 -0.1220 35  LYS   A CE  
67   N  NZ  . LYS   A 15  ? 1.9094 1.1596 1.7977 0.2938  -0.1572 -0.1580 35  LYS   A NZ  
68   N  N   . LEU   A 16  ? 1.5787 1.0334 1.6538 0.0998  -0.2563 -0.1613 36  LEU   A N   
69   C  CA  . LEU   A 16  ? 1.5134 1.0049 1.6539 0.0593  -0.2751 -0.1498 36  LEU   A CA  
70   C  C   . LEU   A 16  ? 1.5498 1.0338 1.6561 0.0559  -0.3152 -0.1806 36  LEU   A C   
71   O  O   . LEU   A 16  ? 1.5187 1.0304 1.6790 0.0237  -0.3380 -0.1736 36  LEU   A O   
72   C  CB  . LEU   A 16  ? 1.4589 1.0413 1.6403 0.0545  -0.2395 -0.1166 36  LEU   A CB  
73   C  CG  . LEU   A 16  ? 1.4673 1.0646 1.6845 0.0544  -0.2009 -0.0824 36  LEU   A CG  
74   C  CD1 . LEU   A 16  ? 1.3917 1.0724 1.6304 0.0543  -0.1700 -0.0574 36  LEU   A CD1 
75   C  CD2 . LEU   A 16  ? 1.5300 1.0904 1.8161 0.0199  -0.2092 -0.0641 36  LEU   A CD2 
76   N  N   . GLY   A 17  ? 1.5477 0.9952 1.5648 0.0902  -0.3240 -0.2133 37  GLY   A N   
77   C  CA  . GLY   A 17  ? 1.5531 0.9933 1.5237 0.0917  -0.3595 -0.2415 37  GLY   A CA  
78   C  C   . GLY   A 17  ? 1.3979 0.9247 1.3736 0.0930  -0.3446 -0.2269 37  GLY   A C   
79   O  O   . GLY   A 17  ? 1.2730 0.8075 1.2418 0.0804  -0.3774 -0.2385 37  GLY   A O   
80   N  N   . ILE   A 18  ? 1.3987 0.9878 1.3853 0.1077  -0.2984 -0.2017 38  ILE   A N   
81   C  CA  . ILE   A 18  ? 1.2933 0.9628 1.2896 0.1073  -0.2803 -0.1842 38  ILE   A CA  
82   C  C   . ILE   A 18  ? 1.2801 0.9662 1.1985 0.1480  -0.2560 -0.1948 38  ILE   A C   
83   O  O   . ILE   A 18  ? 1.2304 0.9144 1.1317 0.1724  -0.2266 -0.1909 38  ILE   A O   
84   C  CB  . ILE   A 18  ? 1.2868 1.0151 1.3575 0.0902  -0.2471 -0.1461 38  ILE   A CB  
85   C  CG1 . ILE   A 18  ? 1.3130 1.0289 1.4656 0.0516  -0.2651 -0.1317 38  ILE   A CG1 
86   C  CG2 . ILE   A 18  ? 1.2317 1.0338 1.3054 0.0918  -0.2293 -0.1305 38  ILE   A CG2 
87   C  CD1 . ILE   A 18  ? 1.2945 1.0571 1.5122 0.0383  -0.2296 -0.0949 38  ILE   A CD1 
88   N  N   . PRO   A 19  ? 1.3257 1.0314 1.1991 0.1567  -0.2662 -0.2054 39  PRO   A N   
89   C  CA  . PRO   A 19  ? 1.3515 1.0737 1.1519 0.1955  -0.2406 -0.2134 39  PRO   A CA  
90   C  C   . PRO   A 19  ? 1.2731 1.0733 1.1044 0.2001  -0.1969 -0.1826 39  PRO   A C   
91   O  O   . PRO   A 19  ? 1.2090 1.0480 1.1083 0.1751  -0.1873 -0.1571 39  PRO   A O   
92   C  CB  . PRO   A 19  ? 1.4287 1.1463 1.1779 0.1970  -0.2678 -0.2295 39  PRO   A CB  
93   C  CG  . PRO   A 19  ? 1.3391 1.0799 1.1585 0.1569  -0.2936 -0.2147 39  PRO   A CG  
94   C  CD  . PRO   A 19  ? 1.2853 0.9989 1.1740 0.1322  -0.3022 -0.2086 39  PRO   A CD  
95   N  N   . GLY   A 20  ? 1.2987 1.1207 1.0772 0.2334  -0.1705 -0.1855 40  GLY   A N   
96   C  CA  . GLY   A 20  ? 1.3188 1.2133 1.1216 0.2386  -0.1326 -0.1587 40  GLY   A CA  
97   C  C   . GLY   A 20  ? 1.3383 1.2436 1.0936 0.2792  -0.1031 -0.1638 40  GLY   A C   
98   O  O   . GLY   A 20  ? 1.3612 1.2133 1.0641 0.3067  -0.1085 -0.1883 40  GLY   A O   
99   N  N   . PRO   A 21  ? 1.2524 1.2270 1.0275 0.2842  -0.0714 -0.1404 41  PRO   A N   
100  C  CA  . PRO   A 21  ? 1.2914 1.2899 1.0363 0.3223  -0.0402 -0.1402 41  PRO   A CA  
101  C  C   . PRO   A 21  ? 1.2652 1.2407 1.0264 0.3398  -0.0326 -0.1425 41  PRO   A C   
102  O  O   . PRO   A 21  ? 1.2455 1.2297 1.0609 0.3200  -0.0339 -0.1268 41  PRO   A O   
103  C  CB  . PRO   A 21  ? 1.1809 1.2617 0.9627 0.3118  -0.0145 -0.1104 41  PRO   A CB  
104  C  CG  . PRO   A 21  ? 1.0994 1.1912 0.9394 0.2716  -0.0286 -0.0947 41  PRO   A CG  
105  C  CD  . PRO   A 21  ? 1.1426 1.1758 0.9708 0.2551  -0.0634 -0.1131 41  PRO   A CD  
106  N  N   . THR   A 22  ? 1.2863 1.2296 0.9959 0.3798  -0.0236 -0.1615 42  THR   A N   
107  C  CA  . THR   A 22  ? 1.2812 1.1944 0.9994 0.4019  -0.0176 -0.1651 42  THR   A CA  
108  C  C   . THR   A 22  ? 1.2331 1.2198 1.0067 0.4056  0.0094  -0.1353 42  THR   A C   
109  O  O   . THR   A 22  ? 1.1985 1.2505 0.9744 0.4201  0.0349  -0.1223 42  THR   A O   
110  C  CB  . THR   A 22  ? 1.3689 1.2349 1.0160 0.4498  -0.0099 -0.1917 42  THR   A CB  
111  O  OG1 . THR   A 22  ? 1.5236 1.3239 1.1099 0.4460  -0.0379 -0.2207 42  THR   A OG1 
112  C  CG2 . THR   A 22  ? 1.3101 1.1255 0.9622 0.4713  -0.0108 -0.1985 42  THR   A CG2 
113  N  N   . PRO   A 23  ? 1.2205 1.1986 1.0387 0.3923  0.0039  -0.1226 43  PRO   A N   
114  C  CA  . PRO   A 23  ? 1.1732 1.2190 1.0411 0.3926  0.0231  -0.0946 43  PRO   A CA  
115  C  C   . PRO   A 23  ? 1.2219 1.2819 1.0828 0.4381  0.0433  -0.0937 43  PRO   A C   
116  O  O   . PRO   A 23  ? 1.2906 1.2901 1.1151 0.4681  0.0406  -0.1130 43  PRO   A O   
117  C  CB  . PRO   A 23  ? 1.1691 1.1872 1.0747 0.3639  0.0077  -0.0833 43  PRO   A CB  
118  C  CG  . PRO   A 23  ? 1.2086 1.1374 1.0845 0.3674  -0.0123 -0.1062 43  PRO   A CG  
119  C  CD  . PRO   A 23  ? 1.2508 1.1573 1.0775 0.3727  -0.0215 -0.1310 43  PRO   A CD  
120  N  N   . LEU   A 24  ? 1.1637 1.3046 1.0625 0.4431  0.0626  -0.0706 44  LEU   A N   
121  C  CA  . LEU   A 24  ? 1.1340 1.3068 1.0473 0.4826  0.0808  -0.0619 44  LEU   A CA  
122  C  C   . LEU   A 24  ? 1.1492 1.3124 1.0980 0.4769  0.0700  -0.0468 44  LEU   A C   
123  O  O   . LEU   A 24  ? 1.1507 1.3084 1.1218 0.4393  0.0555  -0.0363 44  LEU   A O   
124  C  CB  . LEU   A 24  ? 1.0875 1.3577 1.0329 0.4873  0.1040  -0.0419 44  LEU   A CB  
125  C  CG  . LEU   A 24  ? 1.0989 1.3869 1.0073 0.5000  0.1225  -0.0511 44  LEU   A CG  
126  C  CD1 . LEU   A 24  ? 1.0706 1.4584 1.0247 0.4951  0.1449  -0.0247 44  LEU   A CD1 
127  C  CD2 . LEU   A 24  ? 1.1937 1.4387 1.0490 0.5518  0.1364  -0.0731 44  LEU   A CD2 
128  N  N   . PRO   A 25  ? 1.1984 1.3569 1.1500 0.5163  0.0777  -0.0444 45  PRO   A N   
129  C  CA  . PRO   A 25  ? 1.1616 1.3079 1.1407 0.5142  0.0667  -0.0279 45  PRO   A CA  
130  C  C   . PRO   A 25  ? 1.1208 1.3407 1.1490 0.4858  0.0639  -0.0013 45  PRO   A C   
131  O  O   . PRO   A 25  ? 1.0950 1.3934 1.1503 0.4860  0.0757  0.0094  45  PRO   A O   
132  C  CB  . PRO   A 25  ? 1.2191 1.3653 1.1946 0.5685  0.0790  -0.0283 45  PRO   A CB  
133  C  CG  . PRO   A 25  ? 1.1914 1.3035 1.1176 0.5971  0.0914  -0.0551 45  PRO   A CG  
134  C  CD  . PRO   A 25  ? 1.1513 1.3038 1.0733 0.5681  0.0965  -0.0581 45  PRO   A CD  
135  N  N   . PHE   A 26  ? 1.1888 1.3787 1.2258 0.4604  0.0483  0.0094  46  PHE   A N   
136  C  CA  . PHE   A 26  ? 1.2201 1.4607 1.2915 0.4347  0.0417  0.0322  46  PHE   A CA  
137  C  C   . PHE   A 26  ? 1.1768 1.4595 1.2605 0.3976  0.0428  0.0337  46  PHE   A C   
138  O  O   . PHE   A 26  ? 1.1744 1.4504 1.2646 0.3644  0.0335  0.0421  46  PHE   A O   
139  C  CB  . PHE   A 26  ? 1.2279 1.5339 1.3317 0.4626  0.0448  0.0493  46  PHE   A CB  
140  C  CG  . PHE   A 26  ? 1.3564 1.6229 1.4521 0.4972  0.0400  0.0542  46  PHE   A CG  
141  C  CD1 . PHE   A 26  ? 1.4553 1.6812 1.5442 0.4852  0.0257  0.0669  46  PHE   A CD1 
142  C  CD2 . PHE   A 26  ? 1.3784 1.6457 1.4700 0.5443  0.0518  0.0472  46  PHE   A CD2 
143  C  CE1 . PHE   A 26  ? 1.5469 1.7323 1.6254 0.5178  0.0212  0.0741  46  PHE   A CE1 
144  C  CE2 . PHE   A 26  ? 1.4368 1.6635 1.5202 0.5785  0.0469  0.0527  46  PHE   A CE2 
145  C  CZ  . PHE   A 26  ? 1.5653 1.7504 1.6424 0.5643  0.0306  0.0669  46  PHE   A CZ  
146  N  N   . LEU   A 27  ? 1.1013 1.4252 1.1856 0.4048  0.0560  0.0270  47  LEU   A N   
147  C  CA  . LEU   A 27  ? 1.0414 1.4038 1.1363 0.3715  0.0579  0.0307  47  LEU   A CA  
148  C  C   . LEU   A 27  ? 1.0420 1.3493 1.1074 0.3473  0.0510  0.0153  47  LEU   A C   
149  O  O   . LEU   A 27  ? 0.9911 1.3128 1.0663 0.3141  0.0466  0.0211  47  LEU   A O   
150  C  CB  . LEU   A 27  ? 0.9792 1.4060 1.0853 0.3879  0.0771  0.0333  47  LEU   A CB  
151  C  CG  . LEU   A 27  ? 1.0206 1.5167 1.1687 0.4127  0.0854  0.0507  47  LEU   A CG  
152  C  CD1 . LEU   A 27  ? 1.0006 1.5648 1.1659 0.4229  0.1087  0.0570  47  LEU   A CD1 
153  C  CD2 . LEU   A 27  ? 1.1481 1.6763 1.3338 0.3872  0.0679  0.0699  47  LEU   A CD2 
154  N  N   . GLY   A 28  ? 1.0496 1.2933 1.0807 0.3632  0.0478  -0.0042 48  GLY   A N   
155  C  CA  . GLY   A 28  ? 1.0226 1.2185 1.0309 0.3403  0.0369  -0.0190 48  GLY   A CA  
156  C  C   . GLY   A 28  ? 1.0213 1.2463 1.0123 0.3378  0.0444  -0.0261 48  GLY   A C   
157  O  O   . GLY   A 28  ? 1.0410 1.2737 1.0063 0.3685  0.0572  -0.0359 48  GLY   A O   
158  N  N   . ASN   A 29  ? 0.9767 1.2173 0.9791 0.3040  0.0386  -0.0196 49  ASN   A N   
159  C  CA  . ASN   A 29  ? 0.9577 1.2240 0.9424 0.2993  0.0449  -0.0224 49  ASN   A CA  
160  C  C   . ASN   A 29  ? 0.9334 1.2673 0.9515 0.2798  0.0550  -0.0001 49  ASN   A C   
161  O  O   . ASN   A 29  ? 0.9502 1.3021 0.9579 0.2680  0.0588  0.0023  49  ASN   A O   
162  C  CB  . ASN   A 29  ? 0.9809 1.1992 0.9444 0.2781  0.0259  -0.0360 49  ASN   A CB  
163  C  CG  . ASN   A 29  ? 1.0335 1.1797 0.9665 0.2917  0.0106  -0.0591 49  ASN   A CG  
164  O  OD1 . ASN   A 29  ? 0.9806 1.0879 0.9320 0.2777  -0.0030 -0.0595 49  ASN   A OD1 
165  N  ND2 . ASN   A 29  ? 1.0959 1.2207 0.9799 0.3191  0.0132  -0.0782 49  ASN   A ND2 
166  N  N   . ILE   A 30  ? 0.9327 1.3006 0.9880 0.2759  0.0574  0.0163  50  ILE   A N   
167  C  CA  . ILE   A 30  ? 0.9396 1.3630 1.0277 0.2527  0.0611  0.0360  50  ILE   A CA  
168  C  C   . ILE   A 30  ? 0.9233 1.4036 1.0166 0.2631  0.0803  0.0445  50  ILE   A C   
169  O  O   . ILE   A 30  ? 0.9521 1.4715 1.0667 0.2401  0.0837  0.0596  50  ILE   A O   
170  C  CB  . ILE   A 30  ? 0.9692 1.4126 1.0900 0.2495  0.0550  0.0494  50  ILE   A CB  
171  C  CG1 . ILE   A 30  ? 0.9418 1.4151 1.0746 0.2842  0.0641  0.0523  50  ILE   A CG1 
172  C  CG2 . ILE   A 30  ? 1.0135 1.4003 1.1262 0.2388  0.0408  0.0451  50  ILE   A CG2 
173  C  CD1 . ILE   A 30  ? 0.9787 1.5063 1.1535 0.2796  0.0597  0.0713  50  ILE   A CD1 
174  N  N   . LEU   A 31  ? 0.9011 1.3852 0.9750 0.2985  0.0948  0.0363  51  LEU   A N   
175  C  CA  . LEU   A 31  ? 1.0100 1.5509 1.0888 0.3121  0.1191  0.0471  51  LEU   A CA  
176  C  C   . LEU   A 31  ? 0.9741 1.5073 1.0222 0.2962  0.1234  0.0465  51  LEU   A C   
177  O  O   . LEU   A 31  ? 0.9805 1.5661 1.0446 0.2902  0.1412  0.0645  51  LEU   A O   
178  C  CB  . LEU   A 31  ? 0.9926 1.5317 1.0494 0.3591  0.1368  0.0368  51  LEU   A CB  
179  C  CG  . LEU   A 31  ? 0.9840 1.5524 1.0796 0.3825  0.1393  0.0445  51  LEU   A CG  
180  C  CD1 . LEU   A 31  ? 0.9659 1.5596 1.0506 0.4300  0.1673  0.0424  51  LEU   A CD1 
181  C  CD2 . LEU   A 31  ? 0.9516 1.5871 1.1120 0.3567  0.1345  0.0701  51  LEU   A CD2 
182  N  N   . SER   A 32  ? 1.0483 1.5179 1.0554 0.2885  0.1063  0.0281  52  SER   A N   
183  C  CA  . SER   A 32  ? 1.0581 1.5157 1.0320 0.2759  0.1057  0.0270  52  SER   A CA  
184  C  C   . SER   A 32  ? 1.0180 1.5029 1.0254 0.2380  0.1012  0.0470  52  SER   A C   
185  O  O   . SER   A 32  ? 1.0090 1.4989 0.9965 0.2285  0.1061  0.0540  52  SER   A O   
186  C  CB  . SER   A 32  ? 1.1060 1.4902 1.0354 0.2764  0.0825  0.0021  52  SER   A CB  
187  O  OG  . SER   A 32  ? 1.1148 1.4596 1.0198 0.3056  0.0795  -0.0182 52  SER   A OG  
188  N  N   . TYR   A 33  ? 0.9680 1.4663 1.0202 0.2182  0.0919  0.0563  53  TYR   A N   
189  C  CA  . TYR   A 33  ? 0.9760 1.4956 1.0585 0.1842  0.0872  0.0737  53  TYR   A CA  
190  C  C   . TYR   A 33  ? 0.9501 1.5319 1.0587 0.1780  0.1062  0.0962  53  TYR   A C   
191  O  O   . TYR   A 33  ? 0.8981 1.4963 1.0357 0.1491  0.1005  0.1107  53  TYR   A O   
192  C  CB  . TYR   A 33  ? 0.8553 1.3669 0.9692 0.1692  0.0721  0.0754  53  TYR   A CB  
193  C  CG  . TYR   A 33  ? 0.9117 1.3638 1.0095 0.1653  0.0552  0.0603  53  TYR   A CG  
194  C  CD1 . TYR   A 33  ? 0.9191 1.3337 0.9898 0.1607  0.0477  0.0500  53  TYR   A CD1 
195  C  CD2 . TYR   A 33  ? 0.8601 1.2953 0.9722 0.1658  0.0465  0.0586  53  TYR   A CD2 
196  C  CE1 . TYR   A 33  ? 0.9470 1.3148 1.0145 0.1550  0.0329  0.0393  53  TYR   A CE1 
197  C  CE2 . TYR   A 33  ? 0.8766 1.2609 0.9793 0.1612  0.0353  0.0489  53  TYR   A CE2 
198  C  CZ  . TYR   A 33  ? 0.8684 1.2222 0.9536 0.1548  0.0289  0.0397  53  TYR   A CZ  
199  O  OH  . TYR   A 33  ? 0.8299 1.1393 0.9165 0.1480  0.0178  0.0326  53  TYR   A OH  
200  N  N   . HIS   A 34  ? 0.9543 1.5680 1.0531 0.2038  0.1291  0.1001  54  HIS   A N   
201  C  CA  . HIS   A 34  ? 1.0039 1.6828 1.1368 0.1967  0.1503  0.1257  54  HIS   A CA  
202  C  C   . HIS   A 34  ? 0.9945 1.6699 1.1129 0.1728  0.1544  0.1392  54  HIS   A C   
203  O  O   . HIS   A 34  ? 0.9808 1.7061 1.1329 0.1588  0.1702  0.1638  54  HIS   A O   
204  C  CB  . HIS   A 34  ? 0.9853 1.7022 1.1112 0.2344  0.1801  0.1290  54  HIS   A CB  
205  C  CG  . HIS   A 34  ? 1.0611 1.7508 1.1212 0.2548  0.1959  0.1215  54  HIS   A CG  
206  N  ND1 . HIS   A 34  ? 1.0725 1.6973 1.0715 0.2762  0.1839  0.0931  54  HIS   A ND1 
207  C  CD2 . HIS   A 34  ? 1.0597 1.7762 1.1023 0.2579  0.2219  0.1392  54  HIS   A CD2 
208  C  CE1 . HIS   A 34  ? 1.1264 1.7371 1.0683 0.2922  0.1987  0.0913  54  HIS   A CE1 
209  N  NE2 . HIS   A 34  ? 1.1367 1.8022 1.1014 0.2828  0.2239  0.1199  54  HIS   A NE2 
210  N  N   . LYS   A 35  ? 1.0479 1.6669 1.1201 0.1683  0.1404  0.1256  55  LYS   A N   
211  C  CA  . LYS   A 35  ? 1.0367 1.6448 1.0959 0.1449  0.1389  0.1388  55  LYS   A CA  
212  C  C   . LYS   A 35  ? 1.0147 1.5808 1.0811 0.1190  0.1118  0.1317  55  LYS   A C   
213  O  O   . LYS   A 35  ? 1.0623 1.5992 1.1040 0.1083  0.1041  0.1337  55  LYS   A O   
214  C  CB  . LYS   A 35  ? 1.1085 1.6910 1.1033 0.1651  0.1473  0.1331  55  LYS   A CB  
215  C  CG  . LYS   A 35  ? 1.1641 1.7859 1.1414 0.1929  0.1807  0.1435  55  LYS   A CG  
216  C  CD  . LYS   A 35  ? 1.3203 1.9193 1.2320 0.2034  0.1902  0.1476  55  LYS   A CD  
217  C  CE  . LYS   A 35  ? 1.4196 2.0226 1.3445 0.1706  0.1886  0.1726  55  LYS   A CE  
218  N  NZ  . LYS   A 35  ? 1.3710 2.0363 1.3558 0.1519  0.2124  0.2042  55  LYS   A NZ  
219  N  N   . GLY   A 36  ? 1.0636 1.6252 1.1605 0.1118  0.0981  0.1243  56  GLY   A N   
220  C  CA  . GLY   A 36  ? 1.0489 1.5694 1.1492 0.0928  0.0770  0.1170  56  GLY   A CA  
221  C  C   . GLY   A 36  ? 1.0468 1.5205 1.1191 0.1069  0.0637  0.0954  56  GLY   A C   
222  O  O   . GLY   A 36  ? 1.0692 1.5303 1.1061 0.1261  0.0661  0.0856  56  GLY   A O   
223  N  N   . PHE   A 37  ? 0.9149 1.3603 1.0013 0.0971  0.0493  0.0880  57  PHE   A N   
224  C  CA  . PHE   A 37  ? 0.9239 1.3271 0.9943 0.1063  0.0363  0.0704  57  PHE   A CA  
225  C  C   . PHE   A 37  ? 0.9062 1.2844 0.9563 0.1007  0.0260  0.0681  57  PHE   A C   
226  O  O   . PHE   A 37  ? 0.9369 1.2854 0.9694 0.1105  0.0136  0.0529  57  PHE   A O   
227  C  CB  . PHE   A 37  ? 0.9652 1.3472 1.0584 0.0977  0.0280  0.0675  57  PHE   A CB  
228  C  CG  . PHE   A 37  ? 0.9389 1.3159 1.0484 0.0753  0.0254  0.0783  57  PHE   A CG  
229  C  CD1 . PHE   A 37  ? 1.0060 1.3569 1.1144 0.0661  0.0177  0.0779  57  PHE   A CD1 
230  C  CD2 . PHE   A 37  ? 1.0234 1.4196 1.1489 0.0648  0.0290  0.0881  57  PHE   A CD2 
231  C  CE1 . PHE   A 37  ? 0.9679 1.3100 1.0881 0.0498  0.0177  0.0871  57  PHE   A CE1 
232  C  CE2 . PHE   A 37  ? 1.0796 1.4620 1.2118 0.0463  0.0260  0.0952  57  PHE   A CE2 
233  C  CZ  . PHE   A 37  ? 1.0854 1.4395 1.2135 0.0403  0.0223  0.0946  57  PHE   A CZ  
234  N  N   . CYS   A 38  ? 0.8969 1.2841 0.9494 0.0851  0.0284  0.0829  58  CYS   A N   
235  C  CA  . CYS   A 38  ? 0.8951 1.2602 0.9278 0.0825  0.0169  0.0829  58  CYS   A CA  
236  C  C   . CYS   A 38  ? 0.8934 1.2570 0.8814 0.1021  0.0175  0.0758  58  CYS   A C   
237  O  O   . CYS   A 38  ? 0.8723 1.2067 0.8380 0.1094  -0.0007 0.0624  58  CYS   A O   
238  C  CB  . CYS   A 38  ? 0.8673 1.2392 0.9086 0.0643  0.0209  0.1022  58  CYS   A CB  
239  S  SG  . CYS   A 38  ? 0.8455 1.2073 0.9254 0.0441  0.0193  0.1078  58  CYS   A SG  
240  N  N   . MET   A 39  ? 0.9161 1.3112 0.8905 0.1112  0.0382  0.0851  59  MET   A N   
241  C  CA  . MET   A 39  ? 0.9428 1.3352 0.8668 0.1354  0.0444  0.0779  59  MET   A CA  
242  C  C   . MET   A 39  ? 0.9453 1.3098 0.8518 0.1552  0.0331  0.0518  59  MET   A C   
243  O  O   . MET   A 39  ? 0.9773 1.3111 0.8363 0.1707  0.0207  0.0364  59  MET   A O   
244  C  CB  . MET   A 39  ? 1.0244 1.4629 0.9485 0.1433  0.0748  0.0949  59  MET   A CB  
245  C  CG  . MET   A 39  ? 1.1453 1.5836 1.0110 0.1718  0.0891  0.0913  59  MET   A CG  
246  S  SD  . MET   A 39  ? 1.3256 1.7499 1.1419 0.1681  0.0884  0.1073  59  MET   A SD  
247  C  CE  . MET   A 39  ? 1.3315 1.7771 1.0902 0.2026  0.1228  0.1128  59  MET   A CE  
248  N  N   . PHE   A 40  ? 0.9233 1.2931 0.8647 0.1548  0.0350  0.0465  60  PHE   A N   
249  C  CA  . PHE   A 40  ? 0.9277 1.2645 0.8572 0.1712  0.0235  0.0235  60  PHE   A CA  
250  C  C   . PHE   A 40  ? 0.9301 1.2222 0.8591 0.1598  -0.0056 0.0104  60  PHE   A C   
251  O  O   . PHE   A 40  ? 0.9486 1.2036 0.8445 0.1732  -0.0218 -0.0099 60  PHE   A O   
252  C  CB  . PHE   A 40  ? 0.9617 1.3131 0.9306 0.1715  0.0314  0.0254  60  PHE   A CB  
253  C  CG  . PHE   A 40  ? 0.9137 1.2263 0.8745 0.1864  0.0202  0.0050  60  PHE   A CG  
254  C  CD1 . PHE   A 40  ? 0.9685 1.2679 0.8904 0.2164  0.0261  -0.0102 60  PHE   A CD1 
255  C  CD2 . PHE   A 40  ? 0.8977 1.1842 0.8885 0.1715  0.0059  0.0022  60  PHE   A CD2 
256  C  CE1 . PHE   A 40  ? 1.0317 1.2877 0.9447 0.2298  0.0148  -0.0291 60  PHE   A CE1 
257  C  CE2 . PHE   A 40  ? 0.9542 1.2015 0.9398 0.1830  -0.0038 -0.0138 60  PHE   A CE2 
258  C  CZ  . PHE   A 40  ? 0.9806 1.2103 0.9273 0.2115  -0.0010 -0.0301 60  PHE   A CZ  
259  N  N   . ASP   A 41  ? 0.8297 1.1241 0.7964 0.1356  -0.0133 0.0219  61  ASP   A N   
260  C  CA  . ASP   A 41  ? 0.9144 1.1757 0.8938 0.1244  -0.0390 0.0134  61  ASP   A CA  
261  C  C   . ASP   A 41  ? 1.0134 1.2581 0.9534 0.1289  -0.0576 0.0075  61  ASP   A C   
262  O  O   . ASP   A 41  ? 1.0368 1.2480 0.9670 0.1306  -0.0836 -0.0093 61  ASP   A O   
263  C  CB  . ASP   A 41  ? 0.8715 1.1421 0.8990 0.1021  -0.0378 0.0290  61  ASP   A CB  
264  C  CG  . ASP   A 41  ? 0.8830 1.1588 0.9424 0.0983  -0.0253 0.0323  61  ASP   A CG  
265  O  OD1 . ASP   A 41  ? 0.8823 1.1580 0.9313 0.1124  -0.0184 0.0243  61  ASP   A OD1 
266  O  OD2 . ASP   A 41  ? 0.8133 1.0910 0.9045 0.0834  -0.0223 0.0432  61  ASP   A OD2 
267  N  N   . MET   A 42  ? 0.9614 1.2274 0.8776 0.1303  -0.0464 0.0220  62  MET   A N   
268  C  CA  A MET   A 42  ? 1.0146 1.2636 0.8855 0.1367  -0.0642 0.0191  62  MET   A CA  
269  C  CA  B MET   A 42  ? 1.0296 1.2786 0.9004 0.1367  -0.0641 0.0191  62  MET   A CA  
270  C  C   . MET   A 42  ? 1.0376 1.2611 0.8459 0.1619  -0.0702 -0.0026 62  MET   A C   
271  O  O   . MET   A 42  ? 1.0598 1.2485 0.8366 0.1664  -0.1006 -0.0186 62  MET   A O   
272  C  CB  A MET   A 42  ? 0.9792 1.2539 0.8359 0.1331  -0.0469 0.0432  62  MET   A CB  
273  C  CB  B MET   A 42  ? 0.9777 1.2525 0.8346 0.1331  -0.0468 0.0433  62  MET   A CB  
274  C  CG  A MET   A 42  ? 0.9347 1.2200 0.8400 0.1103  -0.0480 0.0620  62  MET   A CG  
275  C  CG  B MET   A 42  ? 0.9429 1.2316 0.8517 0.1099  -0.0443 0.0626  62  MET   A CG  
276  S  SD  A MET   A 42  ? 0.9432 1.2173 0.8213 0.1082  -0.0651 0.0765  62  MET   A SD  
277  S  SD  B MET   A 42  ? 0.8353 1.1427 0.7246 0.1042  -0.0276 0.0913  62  MET   A SD  
278  C  CE  A MET   A 42  ? 0.9309 1.2218 0.7484 0.1225  -0.0376 0.0911  62  MET   A CE  
279  C  CE  B MET   A 42  ? 0.9118 1.1901 0.7436 0.1176  -0.0551 0.0867  62  MET   A CE  
280  N  N   . GLU   A 43  ? 1.0335 1.2727 0.8227 0.1800  -0.0430 -0.0041 63  GLU   A N   
281  C  CA  . GLU   A 43  ? 1.1206 1.3317 0.8440 0.2091  -0.0444 -0.0257 63  GLU   A CA  
282  C  C   . GLU   A 43  ? 1.1446 1.3096 0.8716 0.2113  -0.0714 -0.0532 63  GLU   A C   
283  O  O   . GLU   A 43  ? 1.2337 1.3539 0.9051 0.2256  -0.0948 -0.0761 63  GLU   A O   
284  C  CB  . GLU   A 43  ? 1.1365 1.3816 0.8486 0.2302  -0.0051 -0.0179 63  GLU   A CB  
285  C  CG  . GLU   A 43  ? 1.2242 1.5107 0.9232 0.2306  0.0226  0.0091  63  GLU   A CG  
286  C  CD  . GLU   A 43  ? 1.3700 1.6843 1.0411 0.2596  0.0594  0.0134  63  GLU   A CD  
287  O  OE1 . GLU   A 43  ? 1.4747 1.7596 1.1017 0.2884  0.0591  -0.0100 63  GLU   A OE1 
288  O  OE2 . GLU   A 43  ? 1.3828 1.7476 1.0784 0.2539  0.0891  0.0406  63  GLU   A OE2 
289  N  N   . CYS   A 44  ? 1.1489 1.3198 0.9375 0.1969  -0.0697 -0.0510 64  CYS   A N   
290  C  CA  . CYS   A 44  ? 1.1514 1.2771 0.9522 0.1938  -0.0953 -0.0723 64  CYS   A CA  
291  C  C   . CYS   A 44  ? 1.1622 1.2620 0.9750 0.1740  -0.1337 -0.0782 64  CYS   A C   
292  O  O   . CYS   A 44  ? 1.1580 1.2108 0.9553 0.1753  -0.1636 -0.1009 64  CYS   A O   
293  C  CB  . CYS   A 44  ? 1.0489 1.1880 0.9120 0.1823  -0.0823 -0.0633 64  CYS   A CB  
294  S  SG  . CYS   A 44  ? 0.9786 1.1379 0.8321 0.2091  -0.0482 -0.0623 64  CYS   A SG  
295  N  N   . HIS   A 45  ? 1.1152 1.2442 0.9582 0.1559  -0.1350 -0.0578 65  HIS   A N   
296  C  CA  . HIS   A 45  ? 1.1086 1.2215 0.9696 0.1393  -0.1714 -0.0601 65  HIS   A CA  
297  C  C   . HIS   A 45  ? 1.2108 1.2907 0.9983 0.1546  -0.1994 -0.0783 65  HIS   A C   
298  O  O   . HIS   A 45  ? 1.2370 1.2869 1.0295 0.1454  -0.2401 -0.0921 65  HIS   A O   
299  C  CB  . HIS   A 45  ? 1.1303 1.2808 1.0336 0.1225  -0.1631 -0.0332 65  HIS   A CB  
300  C  CG  . HIS   A 45  ? 1.1534 1.2965 1.0898 0.1068  -0.1979 -0.0313 65  HIS   A CG  
301  N  ND1 . HIS   A 45  ? 1.1892 1.2993 1.1338 0.1013  -0.2356 -0.0506 65  HIS   A ND1 
302  C  CD2 . HIS   A 45  ? 1.1142 1.2799 1.0822 0.0957  -0.2017 -0.0114 65  HIS   A CD2 
303  C  CE1 . HIS   A 45  ? 1.1451 1.2643 1.1302 0.0870  -0.2616 -0.0414 65  HIS   A CE1 
304  N  NE2 . HIS   A 45  ? 1.0993 1.2516 1.0977 0.0854  -0.2405 -0.0176 65  HIS   A NE2 
305  N  N   . LYS   A 46  ? 1.2638 1.3484 0.9823 0.1782  -0.1788 -0.0780 66  LYS   A N   
306  C  CA  . LYS   A 46  ? 1.3494 1.3999 0.9834 0.1970  -0.2016 -0.0939 66  LYS   A CA  
307  C  C   . LYS   A 46  ? 1.4368 1.4348 1.0129 0.2188  -0.2136 -0.1271 66  LYS   A C   
308  O  O   . LYS   A 46  ? 1.4947 1.4467 1.0093 0.2281  -0.2496 -0.1490 66  LYS   A O   
309  C  CB  . LYS   A 46  ? 1.3896 1.4681 0.9717 0.2139  -0.1699 -0.0746 66  LYS   A CB  
310  C  CG  . LYS   A 46  ? 1.5772 1.6231 1.0679 0.2325  -0.1925 -0.0841 66  LYS   A CG  
311  C  CD  . LYS   A 46  ? 1.6657 1.7443 1.1208 0.2420  -0.1603 -0.0557 66  LYS   A CD  
312  C  CE  . LYS   A 46  ? 1.8684 1.9118 1.2287 0.2604  -0.1849 -0.0619 66  LYS   A CE  
313  N  NZ  . LYS   A 46  ? 1.9702 2.0433 1.3002 0.2666  -0.1543 -0.0290 66  LYS   A NZ  
314  N  N   . LYS   A 47  ? 1.4633 1.4632 1.0550 0.2283  -0.1868 -0.1322 67  LYS   A N   
315  C  CA  . LYS   A 47  ? 1.5787 1.5250 1.1123 0.2535  -0.1937 -0.1633 67  LYS   A CA  
316  C  C   . LYS   A 47  ? 1.5561 1.4558 1.1280 0.2356  -0.2303 -0.1837 67  LYS   A C   
317  O  O   . LYS   A 47  ? 1.6615 1.4981 1.1763 0.2500  -0.2567 -0.2148 67  LYS   A O   
318  C  CB  . LYS   A 47  ? 1.5505 1.5219 1.0789 0.2779  -0.1455 -0.1573 67  LYS   A CB  
319  C  CG  . LYS   A 47  ? 1.6444 1.5605 1.1076 0.3113  -0.1456 -0.1883 67  LYS   A CG  
320  C  CD  . LYS   A 47  ? 1.6626 1.6087 1.0816 0.3483  -0.0971 -0.1806 67  LYS   A CD  
321  C  CE  . LYS   A 47  ? 1.6190 1.6366 1.1170 0.3389  -0.0583 -0.1498 67  LYS   A CE  
322  N  NZ  . LYS   A 47  ? 1.6523 1.7118 1.1205 0.3712  -0.0113 -0.1369 67  LYS   A NZ  
323  N  N   . TYR   A 48  ? 1.4490 1.3749 1.1139 0.2047  -0.2325 -0.1666 68  TYR   A N   
324  C  CA  . TYR   A 48  ? 1.4192 1.3064 1.1304 0.1865  -0.2589 -0.1798 68  TYR   A CA  
325  C  C   . TYR   A 48  ? 1.3653 1.2549 1.1384 0.1524  -0.2973 -0.1737 68  TYR   A C   
326  O  O   . TYR   A 48  ? 1.3877 1.2387 1.1935 0.1358  -0.3270 -0.1869 68  TYR   A O   
327  C  CB  . TYR   A 48  ? 1.3647 1.2741 1.1341 0.1827  -0.2250 -0.1649 68  TYR   A CB  
328  C  CG  . TYR   A 48  ? 1.3781 1.2918 1.1005 0.2166  -0.1884 -0.1687 68  TYR   A CG  
329  C  CD1 . TYR   A 48  ? 1.4433 1.2991 1.1029 0.2437  -0.1957 -0.1975 68  TYR   A CD1 
330  C  CD2 . TYR   A 48  ? 1.3318 1.3070 1.0745 0.2223  -0.1476 -0.1435 68  TYR   A CD2 
331  C  CE1 . TYR   A 48  ? 1.4563 1.3205 1.0781 0.2784  -0.1599 -0.1994 68  TYR   A CE1 
332  C  CE2 . TYR   A 48  ? 1.3584 1.3458 1.0689 0.2532  -0.1149 -0.1445 68  TYR   A CE2 
333  C  CZ  . TYR   A 48  ? 1.3971 1.3314 1.0488 0.2827  -0.1195 -0.1717 68  TYR   A CZ  
334  O  OH  . TYR   A 48  ? 1.3665 1.3170 0.9911 0.3170  -0.0848 -0.1712 68  TYR   A OH  
335  N  N   . GLY   A 49  ? 1.3206 1.2543 1.1149 0.1416  -0.2973 -0.1527 69  GLY   A N   
336  C  CA  . GLY   A 49  ? 1.3177 1.2566 1.1690 0.1142  -0.3354 -0.1468 69  GLY   A CA  
337  C  C   . GLY   A 49  ? 1.2202 1.2046 1.1722 0.0893  -0.3175 -0.1183 69  GLY   A C   
338  O  O   . GLY   A 49  ? 1.1885 1.2137 1.1558 0.0928  -0.2772 -0.0969 69  GLY   A O   
339  N  N   . LYS   A 50  ? 1.1881 1.1647 1.2096 0.0640  -0.3475 -0.1178 70  LYS   A N   
340  C  CA  . LYS   A 50  ? 1.1467 1.1670 1.2630 0.0424  -0.3314 -0.0895 70  LYS   A CA  
341  C  C   . LYS   A 50  ? 1.1106 1.1344 1.2620 0.0397  -0.2931 -0.0795 70  LYS   A C   
342  O  O   . LYS   A 50  ? 1.0812 1.1438 1.2811 0.0328  -0.2629 -0.0548 70  LYS   A O   
343  C  CB  . LYS   A 50  ? 1.1254 1.1429 1.3112 0.0170  -0.3748 -0.0889 70  LYS   A CB  
344  C  CG  . LYS   A 50  ? 1.2954 1.2597 1.4879 0.0054  -0.4071 -0.1119 70  LYS   A CG  
345  C  CD  . LYS   A 50  ? 1.3605 1.3287 1.6281 -0.0225 -0.4550 -0.1097 70  LYS   A CD  
346  C  CE  . LYS   A 50  ? 1.2485 1.2726 1.6253 -0.0417 -0.4313 -0.0750 70  LYS   A CE  
347  N  NZ  . LYS   A 50  ? 1.2049 1.2243 1.6204 -0.0483 -0.3917 -0.0633 70  LYS   A NZ  
348  N  N   . VAL   A 51  ? 1.1233 1.1032 1.2470 0.0466  -0.2945 -0.0982 71  VAL   A N   
349  C  CA  . VAL   A 51  ? 1.0673 1.0442 1.2175 0.0465  -0.2617 -0.0888 71  VAL   A CA  
350  C  C   . VAL   A 51  ? 1.0825 1.0310 1.1580 0.0746  -0.2465 -0.1069 71  VAL   A C   
351  O  O   . VAL   A 51  ? 1.2427 1.1490 1.2583 0.0880  -0.2709 -0.1333 71  VAL   A O   
352  C  CB  . VAL   A 51  ? 1.0653 1.0138 1.2810 0.0226  -0.2792 -0.0877 71  VAL   A CB  
353  C  CG1 . VAL   A 51  ? 1.0217 0.9707 1.2647 0.0232  -0.2416 -0.0716 71  VAL   A CG1 
354  C  CG2 . VAL   A 51  ? 1.0713 1.0502 1.3656 -0.0037 -0.2989 -0.0712 71  VAL   A CG2 
355  N  N   . TRP   A 52  ? 1.0932 1.0643 1.1712 0.0852  -0.2070 -0.0927 72  TRP   A N   
356  C  CA  . TRP   A 52  ? 1.1081 1.0592 1.1308 0.1129  -0.1894 -0.1055 72  TRP   A CA  
357  C  C   . TRP   A 52  ? 1.0638 1.0361 1.1188 0.1144  -0.1550 -0.0856 72  TRP   A C   
358  O  O   . TRP   A 52  ? 0.9260 0.9340 1.0291 0.0984  -0.1401 -0.0626 72  TRP   A O   
359  C  CB  . TRP   A 52  ? 1.1214 1.0935 1.0783 0.1370  -0.1788 -0.1119 72  TRP   A CB  
360  C  CG  . TRP   A 52  ? 1.0634 1.0966 1.0378 0.1348  -0.1494 -0.0869 72  TRP   A CG  
361  C  CD1 . TRP   A 52  ? 1.0394 1.1043 1.0136 0.1470  -0.1157 -0.0741 72  TRP   A CD1 
362  C  CD2 . TRP   A 52  ? 1.0536 1.1201 1.0483 0.1194  -0.1541 -0.0719 72  TRP   A CD2 
363  N  NE1 . TRP   A 52  ? 1.0070 1.1195 0.9993 0.1374  -0.1003 -0.0534 72  TRP   A NE1 
364  C  CE2 . TRP   A 52  ? 1.0395 1.1518 1.0426 0.1218  -0.1218 -0.0516 72  TRP   A CE2 
365  C  CE3 . TRP   A 52  ? 1.0922 1.1536 1.1005 0.1042  -0.1846 -0.0733 72  TRP   A CE3 
366  C  CZ2 . TRP   A 52  ? 0.9684 1.1144 0.9888 0.1099  -0.1173 -0.0336 72  TRP   A CZ2 
367  C  CZ3 . TRP   A 52  ? 1.0504 1.1500 1.0777 0.0951  -0.1789 -0.0540 72  TRP   A CZ3 
368  C  CH2 . TRP   A 52  ? 0.9946 1.1328 1.0257 0.0981  -0.1446 -0.0348 72  TRP   A CH2 
369  N  N   . GLY   A 53  ? 1.0171 0.9643 1.0409 0.1364  -0.1434 -0.0952 73  GLY   A N   
370  C  CA  . GLY   A 53  ? 0.9730 0.9349 1.0196 0.1416  -0.1153 -0.0778 73  GLY   A CA  
371  C  C   . GLY   A 53  ? 0.9887 0.9714 0.9930 0.1727  -0.0926 -0.0804 73  GLY   A C   
372  O  O   . GLY   A 53  ? 1.0375 1.0026 0.9902 0.1957  -0.0972 -0.1000 73  GLY   A O   
373  N  N   . PHE   A 54  ? 0.8893 0.9105 0.9164 0.1741  -0.0681 -0.0596 74  PHE   A N   
374  C  CA  . PHE   A 54  ? 0.9835 1.0343 0.9871 0.2011  -0.0467 -0.0571 74  PHE   A CA  
375  C  C   . PHE   A 54  ? 0.8924 0.9553 0.9257 0.2007  -0.0317 -0.0381 74  PHE   A C   
376  O  O   . PHE   A 54  ? 0.9092 0.9530 0.9733 0.1817  -0.0350 -0.0276 74  PHE   A O   
377  C  CB  . PHE   A 54  ? 0.9671 1.0725 0.9595 0.2018  -0.0356 -0.0503 74  PHE   A CB  
378  C  CG  . PHE   A 54  ? 0.8848 1.0274 0.9149 0.1758  -0.0300 -0.0294 74  PHE   A CG  
379  C  CD1 . PHE   A 54  ? 0.8496 0.9863 0.8950 0.1530  -0.0444 -0.0280 74  PHE   A CD1 
380  C  CD2 . PHE   A 54  ? 0.8685 1.0500 0.9178 0.1757  -0.0122 -0.0116 74  PHE   A CD2 
381  C  CE1 . PHE   A 54  ? 0.8008 0.9668 0.8775 0.1331  -0.0374 -0.0097 74  PHE   A CE1 
382  C  CE2 . PHE   A 54  ? 0.8315 1.0380 0.9073 0.1536  -0.0081 0.0047  74  PHE   A CE2 
383  C  CZ  . PHE   A 54  ? 0.8084 1.0057 0.8966 0.1336  -0.0188 0.0056  74  PHE   A CZ  
384  N  N   . TYR   A 55  ? 0.9109 1.0075 0.9352 0.2226  -0.0149 -0.0320 75  TYR   A N   
385  C  CA  . TYR   A 55  ? 0.9766 1.0822 1.0203 0.2280  -0.0047 -0.0157 75  TYR   A CA  
386  C  C   . TYR   A 55  ? 0.9155 1.0864 0.9715 0.2282  0.0087  -0.0001 75  TYR   A C   
387  O  O   . TYR   A 55  ? 0.8950 1.1013 0.9395 0.2460  0.0174  -0.0030 75  TYR   A O   
388  C  CB  . TYR   A 55  ? 1.0251 1.0972 1.0496 0.2592  -0.0033 -0.0244 75  TYR   A CB  
389  C  CG  . TYR   A 55  ? 1.0137 1.0123 1.0254 0.2578  -0.0191 -0.0405 75  TYR   A CG  
390  C  CD1 . TYR   A 55  ? 1.0979 1.0655 1.0753 0.2679  -0.0306 -0.0653 75  TYR   A CD1 
391  C  CD2 . TYR   A 55  ? 1.0954 1.0528 1.1274 0.2457  -0.0232 -0.0305 75  TYR   A CD2 
392  C  CE1 . TYR   A 55  ? 1.2095 1.1053 1.1756 0.2638  -0.0501 -0.0818 75  TYR   A CE1 
393  C  CE2 . TYR   A 55  ? 1.1461 1.0352 1.1731 0.2404  -0.0391 -0.0435 75  TYR   A CE2 
394  C  CZ  . TYR   A 55  ? 1.2027 1.0604 1.1980 0.2484  -0.0547 -0.0703 75  TYR   A CZ  
395  O  OH  . TYR   A 55  ? 1.2621 1.0473 1.2527 0.2405  -0.0755 -0.0852 75  TYR   A OH  
396  N  N   . ASP   A 56  ? 0.8984 1.0836 0.9773 0.2084  0.0107  0.0167  76  ASP   A N   
397  C  CA  . ASP   A 56  ? 0.8964 1.1333 0.9876 0.2077  0.0183  0.0315  76  ASP   A CA  
398  C  C   . ASP   A 56  ? 0.9644 1.1965 1.0562 0.2286  0.0197  0.0386  76  ASP   A C   
399  O  O   . ASP   A 56  ? 1.0158 1.2227 1.1104 0.2223  0.0177  0.0486  76  ASP   A O   
400  C  CB  . ASP   A 56  ? 0.9075 1.1525 1.0129 0.1796  0.0178  0.0434  76  ASP   A CB  
401  C  CG  . ASP   A 56  ? 0.9419 1.1939 1.0486 0.1616  0.0158  0.0387  76  ASP   A CG  
402  O  OD1 . ASP   A 56  ? 0.8804 1.1509 0.9756 0.1698  0.0168  0.0308  76  ASP   A OD1 
403  O  OD2 . ASP   A 56  ? 0.9340 1.1728 1.0515 0.1415  0.0143  0.0443  76  ASP   A OD2 
404  N  N   . GLY   A 57  ? 1.0386 1.2946 1.1267 0.2561  0.0244  0.0350  77  GLY   A N   
405  C  CA  . GLY   A 57  ? 1.1004 1.3448 1.1875 0.2817  0.0239  0.0400  77  GLY   A CA  
406  C  C   . GLY   A 57  ? 1.0773 1.2504 1.1451 0.2916  0.0199  0.0289  77  GLY   A C   
407  O  O   . GLY   A 57  ? 1.0882 1.2368 1.1379 0.3027  0.0196  0.0109  77  GLY   A O   
408  N  N   . GLN   A 58  ? 1.0724 1.2079 1.1410 0.2871  0.0162  0.0397  78  GLN   A N   
409  C  CA  . GLN   A 58  ? 1.0917 1.1554 1.1488 0.2888  0.0119  0.0331  78  GLN   A CA  
410  C  C   . GLN   A 58  ? 1.0116 1.0475 1.0804 0.2544  0.0096  0.0381  78  GLN   A C   
411  O  O   . GLN   A 58  ? 1.0136 0.9925 1.0830 0.2493  0.0065  0.0386  78  GLN   A O   
412  C  CB  . GLN   A 58  ? 1.1937 1.2285 1.2436 0.3126  0.0123  0.0451  78  GLN   A CB  
413  C  CG  . GLN   A 58  ? 1.2628 1.3154 1.3045 0.3524  0.0145  0.0390  78  GLN   A CG  
414  C  CD  . GLN   A 58  ? 1.5404 1.5625 1.5751 0.3781  0.0129  0.0527  78  GLN   A CD  
415  O  OE1 . GLN   A 58  ? 1.6462 1.6460 1.6802 0.3657  0.0111  0.0706  78  GLN   A OE1 
416  N  NE2 . GLN   A 58  ? 1.6029 1.6222 1.6292 0.4168  0.0151  0.0454  78  GLN   A NE2 
417  N  N   . GLN   A 59  ? 1.0129 1.0879 1.0946 0.2313  0.0120  0.0432  79  GLN   A N   
418  C  CA  . GLN   A 59  ? 0.8909 0.9476 0.9886 0.2019  0.0127  0.0495  79  GLN   A CA  
419  C  C   . GLN   A 59  ? 0.9044 0.9494 1.0079 0.1892  0.0031  0.0322  79  GLN   A C   
420  O  O   . GLN   A 59  ? 0.9451 1.0263 1.0437 0.1878  0.0011  0.0234  79  GLN   A O   
421  C  CB  . GLN   A 59  ? 0.9290 1.0266 1.0335 0.1865  0.0191  0.0624  79  GLN   A CB  
422  C  CG  . GLN   A 59  ? 0.9313 1.0186 1.0544 0.1597  0.0227  0.0679  79  GLN   A CG  
423  C  CD  . GLN   A 59  ? 0.7880 0.8295 0.9205 0.1538  0.0298  0.0811  79  GLN   A CD  
424  O  OE1 . GLN   A 59  ? 0.9653 0.9892 1.0829 0.1664  0.0359  0.0936  79  GLN   A OE1 
425  N  NE2 . GLN   A 59  ? 0.7839 0.8074 0.9436 0.1346  0.0287  0.0805  79  GLN   A NE2 
426  N  N   . PRO   A 60  ? 0.9160 0.9113 1.0300 0.1790  -0.0046 0.0279  80  PRO   A N   
427  C  CA  . PRO   A 60  ? 0.9688 0.9524 1.0882 0.1655  -0.0199 0.0107  80  PRO   A CA  
428  C  C   . PRO   A 60  ? 0.8458 0.8607 0.9920 0.1396  -0.0185 0.0196  80  PRO   A C   
429  O  O   . PRO   A 60  ? 0.7884 0.8038 0.9597 0.1251  -0.0078 0.0381  80  PRO   A O   
430  C  CB  . PRO   A 60  ? 0.9242 0.8441 1.0546 0.1592  -0.0307 0.0069  80  PRO   A CB  
431  C  CG  . PRO   A 60  ? 0.9698 0.8769 1.1144 0.1574  -0.0147 0.0315  80  PRO   A CG  
432  C  CD  . PRO   A 60  ? 0.9598 0.9051 1.0811 0.1791  -0.0016 0.0395  80  PRO   A CD  
433  N  N   . VAL   A 61  ? 0.8694 0.9086 1.0068 0.1368  -0.0275 0.0072  81  VAL   A N   
434  C  CA  . VAL   A 61  ? 0.8573 0.9245 1.0174 0.1158  -0.0284 0.0142  81  VAL   A CA  
435  C  C   . VAL   A 61  ? 0.8166 0.8650 0.9815 0.1058  -0.0518 -0.0015 81  VAL   A C   
436  O  O   . VAL   A 61  ? 0.7928 0.8324 0.9225 0.1195  -0.0639 -0.0206 81  VAL   A O   
437  C  CB  . VAL   A 61  ? 0.8818 0.9982 1.0257 0.1206  -0.0187 0.0181  81  VAL   A CB  
438  C  CG1 . VAL   A 61  ? 0.7373 0.8750 0.9036 0.1006  -0.0188 0.0268  81  VAL   A CG1 
439  C  CG2 . VAL   A 61  ? 0.8100 0.9438 0.9473 0.1309  -0.0025 0.0307  81  VAL   A CG2 
440  N  N   . LEU   A 62  ? 0.8342 0.8771 1.0417 0.0833  -0.0585 0.0071  82  LEU   A N   
441  C  CA  . LEU   A 62  ? 0.8562 0.8848 1.0776 0.0703  -0.0860 -0.0056 82  LEU   A CA  
442  C  C   . LEU   A 62  ? 0.8054 0.8742 1.0380 0.0612  -0.0879 0.0008  82  LEU   A C   
443  O  O   . LEU   A 62  ? 0.8068 0.8981 1.0766 0.0495  -0.0735 0.0201  82  LEU   A O   
444  C  CB  . LEU   A 62  ? 0.9023 0.9007 1.1754 0.0500  -0.0953 0.0016  82  LEU   A CB  
445  C  CG  . LEU   A 62  ? 0.9606 0.9421 1.2543 0.0340  -0.1310 -0.0124 82  LEU   A CG  
446  C  CD1 . LEU   A 62  ? 0.9943 0.9233 1.2453 0.0448  -0.1554 -0.0397 82  LEU   A CD1 
447  C  CD2 . LEU   A 62  ? 1.0398 1.0209 1.4100 0.0073  -0.1340 0.0059  82  LEU   A CD2 
448  N  N   . ALA   A 63  ? 0.8562 0.9304 1.0529 0.0688  -0.1042 -0.0146 83  ALA   A N   
449  C  CA  . ALA   A 63  ? 0.8330 0.9397 1.0341 0.0623  -0.1085 -0.0084 83  ALA   A CA  
450  C  C   . ALA   A 63  ? 0.8979 0.9931 1.1303 0.0465  -0.1401 -0.0134 83  ALA   A C   
451  O  O   . ALA   A 63  ? 0.9273 0.9884 1.1410 0.0477  -0.1674 -0.0332 83  ALA   A O   
452  C  CB  . ALA   A 63  ? 0.8235 0.9442 0.9662 0.0800  -0.1066 -0.0179 83  ALA   A CB  
453  N  N   . ILE   A 64  ? 0.8767 0.9989 1.1565 0.0326  -0.1378 0.0040  84  ILE   A N   
454  C  CA  . ILE   A 64  ? 0.8976 1.0201 1.2202 0.0171  -0.1683 0.0037  84  ILE   A CA  
455  C  C   . ILE   A 64  ? 0.9144 1.0685 1.2320 0.0193  -0.1725 0.0117  84  ILE   A C   
456  O  O   . ILE   A 64  ? 0.8766 1.0553 1.1911 0.0240  -0.1451 0.0266  84  ILE   A O   
457  C  CB  . ILE   A 64  ? 0.8466 0.9731 1.2488 -0.0014 -0.1613 0.0215  84  ILE   A CB  
458  C  CG1 . ILE   A 64  ? 0.8187 0.9760 1.2442 0.0004  -0.1231 0.0457  84  ILE   A CG1 
459  C  CG2 . ILE   A 64  ? 0.8952 0.9835 1.3012 -0.0049 -0.1599 0.0152  84  ILE   A CG2 
460  C  CD1 . ILE   A 64  ? 0.8566 1.0243 1.3600 -0.0145 -0.1111 0.0669  84  ILE   A CD1 
461  N  N   . THR   A 65  ? 0.9256 1.0742 1.2383 0.0162  -0.2095 0.0014  85  THR   A N   
462  C  CA  . THR   A 65  ? 0.9235 1.0976 1.2323 0.0189  -0.2185 0.0104  85  THR   A CA  
463  C  C   . THR   A 65  ? 0.9342 1.1193 1.3057 0.0044  -0.2520 0.0160  85  THR   A C   
464  O  O   . THR   A 65  ? 0.9681 1.1725 1.3392 0.0080  -0.2649 0.0241  85  THR   A O   
465  C  CB  . THR   A 65  ? 0.9307 1.0919 1.1553 0.0355  -0.2311 -0.0051 85  THR   A CB  
466  O  OG1 . THR   A 65  ? 0.9915 1.1182 1.1910 0.0353  -0.2705 -0.0285 85  THR   A OG1 
467  C  CG2 . THR   A 65  ? 0.9634 1.1224 1.1357 0.0502  -0.1974 -0.0083 85  THR   A CG2 
468  N  N   . ASP   A 66  ? 0.8684 1.0428 1.2972 -0.0120 -0.2672 0.0140  86  ASP   A N   
469  C  CA  . ASP   A 66  ? 0.9559 1.1472 1.4579 -0.0283 -0.3012 0.0213  86  ASP   A CA  
470  C  C   . ASP   A 66  ? 0.9301 1.1644 1.5105 -0.0329 -0.2715 0.0515  86  ASP   A C   
471  O  O   . ASP   A 66  ? 0.8996 1.1366 1.5039 -0.0348 -0.2331 0.0636  86  ASP   A O   
472  C  CB  . ASP   A 66  ? 1.0042 1.1663 1.5428 -0.0471 -0.3299 0.0086  86  ASP   A CB  
473  C  CG  . ASP   A 66  ? 1.0146 1.1953 1.6309 -0.0665 -0.3742 0.0138  86  ASP   A CG  
474  O  OD1 . ASP   A 66  ? 1.0089 1.2320 1.7144 -0.0762 -0.3593 0.0404  86  ASP   A OD1 
475  O  OD2 . ASP   A 66  ? 1.0694 1.2224 1.6569 -0.0708 -0.4248 -0.0087 86  ASP   A OD2 
476  N  N   . PRO   A 67  ? 0.9416 1.2076 1.5597 -0.0322 -0.2878 0.0644  87  PRO   A N   
477  C  CA  . PRO   A 67  ? 0.9063 1.2107 1.5897 -0.0300 -0.2541 0.0928  87  PRO   A CA  
478  C  C   . PRO   A 67  ? 0.8624 1.1825 1.6397 -0.0465 -0.2402 0.1088  87  PRO   A C   
479  O  O   . PRO   A 67  ? 0.8137 1.1455 1.6128 -0.0414 -0.1941 0.1268  87  PRO   A O   
480  C  CB  . PRO   A 67  ? 0.8829 1.2139 1.5869 -0.0243 -0.2840 0.1009  87  PRO   A CB  
481  C  CG  . PRO   A 67  ? 0.8751 1.1774 1.4939 -0.0182 -0.3216 0.0774  87  PRO   A CG  
482  C  CD  . PRO   A 67  ? 0.9432 1.2087 1.5365 -0.0289 -0.3355 0.0543  87  PRO   A CD  
483  N  N   . ASP   A 68  ? 0.9089 1.2277 1.7414 -0.0664 -0.2790 0.1037  88  ASP   A N   
484  C  CA  . ASP   A 68  ? 0.8458 1.1810 1.7752 -0.0850 -0.2647 0.1225  88  ASP   A CA  
485  C  C   . ASP   A 68  ? 0.8493 1.1522 1.7480 -0.0858 -0.2260 0.1213  88  ASP   A C   
486  O  O   . ASP   A 68  ? 0.8097 1.1286 1.7594 -0.0879 -0.1849 0.1450  88  ASP   A O   
487  C  CB  . ASP   A 68  ? 0.9316 1.2661 1.9235 -0.1102 -0.3202 0.1150  88  ASP   A CB  
488  C  CG  . ASP   A 68  ? 0.8986 1.2764 1.9479 -0.1111 -0.3576 0.1242  88  ASP   A CG  
489  O  OD1 . ASP   A 68  ? 0.9514 1.3536 1.9812 -0.0898 -0.3408 0.1345  88  ASP   A OD1 
490  O  OD2 . ASP   A 68  ? 0.9493 1.3234 2.0413 -0.1301 -0.3975 0.1198  88  ASP   A OD2 
491  N  N   . MET   A 69  ? 0.9456 1.2026 1.7592 -0.0816 -0.2376 0.0951  89  MET   A N   
492  C  CA  . MET   A 69  ? 0.9585 1.1840 1.7381 -0.0788 -0.2037 0.0939  89  MET   A CA  
493  C  C   . MET   A 69  ? 0.9045 1.1429 1.6471 -0.0590 -0.1532 0.1071  89  MET   A C   
494  O  O   . MET   A 69  ? 0.9005 1.1336 1.6554 -0.0584 -0.1155 0.1220  89  MET   A O   
495  C  CB  . MET   A 69  ? 1.0013 1.1770 1.6985 -0.0742 -0.2285 0.0624  89  MET   A CB  
496  C  CG  . MET   A 69  ? 1.0586 1.1952 1.7412 -0.0769 -0.2091 0.0600  89  MET   A CG  
497  S  SD  . MET   A 69  ? 1.1336 1.2108 1.7211 -0.0663 -0.2394 0.0218  89  MET   A SD  
498  C  CE  . MET   A 69  ? 1.1482 1.2174 1.7582 -0.0829 -0.3050 0.0030  89  MET   A CE  
499  N  N   . ILE   A 70  ? 0.9008 1.1524 1.5952 -0.0431 -0.1534 0.1022  90  ILE   A N   
500  C  CA  . ILE   A 70  ? 0.8817 1.1428 1.5431 -0.0268 -0.1110 0.1136  90  ILE   A CA  
501  C  C   . ILE   A 70  ? 0.8536 1.1433 1.5863 -0.0275 -0.0800 0.1414  90  ILE   A C   
502  O  O   . ILE   A 70  ? 0.7964 1.0807 1.5160 -0.0194 -0.0393 0.1530  90  ILE   A O   
503  C  CB  . ILE   A 70  ? 0.8570 1.1249 1.4612 -0.0132 -0.1211 0.1050  90  ILE   A CB  
504  C  CG1 . ILE   A 70  ? 0.8669 1.1069 1.3905 -0.0072 -0.1366 0.0808  90  ILE   A CG1 
505  C  CG2 . ILE   A 70  ? 0.8605 1.1392 1.4474 -0.0001 -0.0826 0.1193  90  ILE   A CG2 
506  C  CD1 . ILE   A 70  ? 0.8888 1.1347 1.3588 0.0039  -0.1495 0.0742  90  ILE   A CD1 
507  N  N   . LYS   A 71  ? 0.7551 1.0760 1.5636 -0.0355 -0.0988 0.1529  91  LYS   A N   
508  C  CA  . LYS   A 71  ? 0.7724 1.1255 1.6573 -0.0336 -0.0668 0.1814  91  LYS   A CA  
509  C  C   . LYS   A 71  ? 0.7697 1.1143 1.6951 -0.0446 -0.0394 0.1956  91  LYS   A C   
510  O  O   . LYS   A 71  ? 0.7454 1.0984 1.6870 -0.0348 0.0064  0.2166  91  LYS   A O   
511  C  CB  . LYS   A 71  ? 0.7171 1.1107 1.6857 -0.0406 -0.0974 0.1918  91  LYS   A CB  
512  C  CG  . LYS   A 71  ? 0.7365 1.1708 1.7971 -0.0369 -0.0634 0.2236  91  LYS   A CG  
513  C  CD  . LYS   A 71  ? 0.7244 1.1890 1.8571 -0.0460 -0.0975 0.2309  91  LYS   A CD  
514  C  CE  . LYS   A 71  ? 0.7532 1.2081 1.9248 -0.0746 -0.1381 0.2218  91  LYS   A CE  
515  N  NZ  . LYS   A 71  ? 0.8311 1.3086 2.0620 -0.0838 -0.1712 0.2278  91  LYS   A NZ  
516  N  N   . THR   A 72  ? 0.7886 1.1115 1.7257 -0.0638 -0.0665 0.1848  92  THR   A N   
517  C  CA  . THR   A 72  ? 0.8095 1.1174 1.7810 -0.0755 -0.0417 0.1996  92  THR   A CA  
518  C  C   . THR   A 72  ? 0.8104 1.0871 1.7032 -0.0588 -0.0012 0.1992  92  THR   A C   
519  O  O   . THR   A 72  ? 0.7856 1.0618 1.6995 -0.0561 0.0403  0.2221  92  THR   A O   
520  C  CB  . THR   A 72  ? 0.8547 1.1345 1.8433 -0.0989 -0.0838 0.1841  92  THR   A CB  
521  O  OG1 . THR   A 72  ? 0.8443 1.1558 1.9214 -0.1181 -0.1214 0.1892  92  THR   A OG1 
522  C  CG2 . THR   A 72  ? 0.8997 1.1523 1.9080 -0.1097 -0.0574 0.1986  92  THR   A CG2 
523  N  N   . VAL   A 73  ? 0.8045 1.0567 1.6065 -0.0466 -0.0126 0.1749  93  VAL   A N   
524  C  CA  . VAL   A 73  ? 0.8514 1.0767 1.5808 -0.0316 0.0185  0.1732  93  VAL   A CA  
525  C  C   . VAL   A 73  ? 0.8417 1.0832 1.5578 -0.0144 0.0579  0.1890  93  VAL   A C   
526  O  O   . VAL   A 73  ? 0.8350 1.0647 1.5417 -0.0072 0.0953  0.2050  93  VAL   A O   
527  C  CB  . VAL   A 73  ? 0.8838 1.0864 1.5306 -0.0234 -0.0050 0.1448  93  VAL   A CB  
528  C  CG1 . VAL   A 73  ? 0.8508 1.0338 1.4297 -0.0077 0.0238  0.1444  93  VAL   A CG1 
529  C  CG2 . VAL   A 73  ? 0.8464 1.0224 1.4959 -0.0361 -0.0402 0.1274  93  VAL   A CG2 
530  N  N   . LEU   A 74  ? 0.8328 1.0960 1.5426 -0.0063 0.0496  0.1848  94  LEU   A N   
531  C  CA  . LEU   A 74  ? 0.7852 1.0530 1.4679 0.0118  0.0830  0.1945  94  LEU   A CA  
532  C  C   . LEU   A 74  ? 0.7611 1.0515 1.5125 0.0159  0.1160  0.2220  94  LEU   A C   
533  O  O   . LEU   A 74  ? 0.7429 1.0240 1.4655 0.0326  0.1540  0.2324  94  LEU   A O   
534  C  CB  . LEU   A 74  ? 0.8202 1.0980 1.4726 0.0192  0.0636  0.1823  94  LEU   A CB  
535  C  CG  . LEU   A 74  ? 0.8023 1.0596 1.3710 0.0234  0.0499  0.1610  94  LEU   A CG  
536  C  CD1 . LEU   A 74  ? 0.8093 1.0582 1.3661 0.0126  0.0160  0.1432  94  LEU   A CD1 
537  C  CD2 . LEU   A 74  ? 0.7948 1.0608 1.3394 0.0317  0.0427  0.1578  94  LEU   A CD2 
538  N  N   . VAL   A 75  ? 0.7371 1.0569 1.5786 0.0018  0.1024  0.2342  95  VAL   A N   
539  C  CA  . VAL   A 75  ? 0.7411 1.0940 1.6603 0.0077  0.1336  0.2626  95  VAL   A CA  
540  C  C   . VAL   A 75  ? 0.7406 1.1029 1.7361 -0.0096 0.1464  0.2840  95  VAL   A C   
541  O  O   . VAL   A 75  ? 0.7228 1.0779 1.7204 -0.0003 0.1922  0.3051  95  VAL   A O   
542  C  CB  . VAL   A 75  ? 0.6811 1.0739 1.6574 0.0091  0.1083  0.2649  95  VAL   A CB  
543  C  CG1 . VAL   A 75  ? 0.5980 1.0121 1.6324 0.0184  0.1386  0.2905  95  VAL   A CG1 
544  C  CG2 . VAL   A 75  ? 0.7084 1.0872 1.6085 0.0260  0.0989  0.2475  95  VAL   A CG2 
545  N  N   . LYS   A 76  ? 0.7269 1.0979 1.7760 -0.0346 0.1042  0.2777  96  LYS   A N   
546  C  CA  . LYS   A 76  ? 0.7686 1.1443 1.8921 -0.0537 0.1089  0.2973  96  LYS   A CA  
547  C  C   . LYS   A 76  ? 0.7934 1.1358 1.8926 -0.0568 0.1422  0.3083  96  LYS   A C   
548  O  O   . LYS   A 76  ? 0.7141 1.0522 1.8386 -0.0552 0.1750  0.3322  96  LYS   A O   
549  C  CB  . LYS   A 76  ? 0.7693 1.1516 1.9447 -0.0811 0.0501  0.2835  96  LYS   A CB  
550  C  CG  . LYS   A 76  ? 0.8155 1.2315 2.0383 -0.0812 0.0220  0.2848  96  LYS   A CG  
551  C  CD  . LYS   A 76  ? 0.8060 1.2206 2.0640 -0.1073 -0.0411 0.2671  96  LYS   A CD  
552  C  CE  . LYS   A 76  ? 0.8623 1.3108 2.1705 -0.1076 -0.0684 0.2719  96  LYS   A CE  
553  N  NZ  . LYS   A 76  ? 0.9212 1.3627 2.2456 -0.1299 -0.1350 0.2505  96  LYS   A NZ  
554  N  N   . GLU   A 77  ? 0.8146 1.1140 1.8265 -0.0542 0.1289  0.2847  97  GLU   A N   
555  C  CA  . GLU   A 77  ? 0.8739 1.1310 1.8460 -0.0551 0.1515  0.2910  97  GLU   A CA  
556  C  C   . GLU   A 77  ? 0.8965 1.1259 1.7621 -0.0284 0.1786  0.2831  97  GLU   A C   
557  O  O   . GLU   A 77  ? 1.0209 1.2106 1.8202 -0.0252 0.1739  0.2709  97  GLU   A O   
558  C  CB  . GLU   A 77  ? 0.9460 1.1690 1.9086 -0.0748 0.1083  0.2703  97  GLU   A CB  
559  C  CG  . GLU   A 77  ? 0.9147 1.1571 1.9770 -0.1045 0.0723  0.2738  97  GLU   A CG  
560  C  CD  . GLU   A 77  ? 0.9481 1.2082 2.1075 -0.1210 0.1036  0.3123  97  GLU   A CD  
561  O  OE1 . GLU   A 77  ? 1.0704 1.3061 2.2047 -0.1134 0.1467  0.3321  97  GLU   A OE1 
562  O  OE2 . GLU   A 77  ? 0.9136 1.2026 2.1477 -0.1348 0.0820  0.3185  97  GLU   A OE2 
563  N  N   . CYS   A 78  ? 0.8836 1.1319 1.7328 -0.0082 0.2059  0.2899  98  CYS   A N   
564  C  CA  . CYS   A 78  ? 0.9603 1.1805 1.7093 0.0153  0.2270  0.2810  98  CYS   A CA  
565  C  C   . CYS   A 78  ? 0.9925 1.1852 1.7137 0.0252  0.2714  0.3033  98  CYS   A C   
566  O  O   . CYS   A 78  ? 0.9430 1.0986 1.5902 0.0317  0.2704  0.2941  98  CYS   A O   
567  C  CB  . CYS   A 78  ? 0.9628 1.2029 1.6987 0.0334  0.2389  0.2791  98  CYS   A CB  
568  S  SG  . CYS   A 78  ? 0.7573 0.9590 1.3749 0.0599  0.2641  0.2694  98  CYS   A SG  
569  N  N   . TYR   A 79  ? 1.0385 1.2503 1.8186 0.0284  0.3117  0.3346  99  TYR   A N   
570  C  CA  . TYR   A 79  ? 1.0723 1.2565 1.8169 0.0423  0.3601  0.3589  99  TYR   A CA  
571  C  C   . TYR   A 79  ? 1.0750 1.2291 1.8226 0.0260  0.3539  0.3670  99  TYR   A C   
572  O  O   . TYR   A 79  ? 1.0824 1.1962 1.7562 0.0392  0.3735  0.3723  99  TYR   A O   
573  C  CB  . TYR   A 79  ? 1.0633 1.2639 1.8497 0.0541  0.3922  0.3815  99  TYR   A CB  
574  C  CG  . TYR   A 79  ? 1.1583 1.3665 1.9110 0.0796  0.4076  0.3750  99  TYR   A CG  
575  C  CD1 . TYR   A 79  ? 1.1566 1.3442 1.8237 0.0957  0.4096  0.3566  99  TYR   A CD1 
576  C  CD2 . TYR   A 79  ? 1.1606 1.3943 1.9677 0.0875  0.4200  0.3883  99  TYR   A CD2 
577  C  CE1 . TYR   A 79  ? 1.2136 1.4006 1.8482 0.1184  0.4227  0.3500  99  TYR   A CE1 
578  C  CE2 . TYR   A 79  ? 1.1395 1.3738 1.9145 0.1119  0.4349  0.3832  99  TYR   A CE2 
579  C  CZ  . TYR   A 79  ? 1.2036 1.4119 1.8912 0.1269  0.4358  0.3633  99  TYR   A CZ  
580  O  OH  . TYR   A 79  ? 1.2866 1.4888 1.9406 0.1508  0.4499  0.3574  99  TYR   A OH  
581  N  N   . SER   A 80  ? 0.9746 1.1437 1.8038 -0.0020 0.3245  0.3678  100 SER   A N   
582  C  CA  . SER   A 80  ? 1.0272 1.1639 1.8711 -0.0190 0.3212  0.3792  100 SER   A CA  
583  C  C   . SER   A 80  ? 1.0117 1.1086 1.7863 -0.0206 0.2800  0.3476  100 SER   A C   
584  O  O   . SER   A 80  ? 1.0477 1.1028 1.7915 -0.0210 0.2863  0.3556  100 SER   A O   
585  C  CB  . SER   A 80  ? 0.9943 1.1570 1.9526 -0.0483 0.3037  0.3916  100 SER   A CB  
586  O  OG  . SER   A 80  ? 1.0596 1.2476 2.0585 -0.0651 0.2542  0.3668  100 SER   A OG  
587  N  N   . VAL   A 81  ? 1.0069 1.1155 1.7562 -0.0195 0.2400  0.3140  101 VAL   A N   
588  C  CA  . VAL   A 81  ? 1.0054 1.0823 1.7006 -0.0206 0.2016  0.2848  101 VAL   A CA  
589  C  C   . VAL   A 81  ? 0.9700 1.0484 1.5804 0.0005  0.1923  0.2599  101 VAL   A C   
590  O  O   . VAL   A 81  ? 0.9931 1.0425 1.5308 0.0156  0.1965  0.2541  101 VAL   A O   
591  C  CB  . VAL   A 81  ? 0.9891 1.0733 1.7419 -0.0447 0.1550  0.2671  101 VAL   A CB  
592  C  CG1 . VAL   A 81  ? 0.9701 1.0198 1.6589 -0.0401 0.1195  0.2357  101 VAL   A CG1 
593  C  CG2 . VAL   A 81  ? 0.9931 1.0723 1.8344 -0.0700 0.1598  0.2919  101 VAL   A CG2 
594  N  N   . PHE   A 82  ? 0.9443 1.0566 1.5665 0.0012  0.1782  0.2468  102 PHE   A N   
595  C  CA  . PHE   A 82  ? 0.9418 1.0570 1.4939 0.0156  0.1634  0.2226  102 PHE   A CA  
596  C  C   . PHE   A 82  ? 0.9789 1.1002 1.4942 0.0338  0.1960  0.2321  102 PHE   A C   
597  O  O   . PHE   A 82  ? 0.9369 1.0805 1.4528 0.0382  0.1925  0.2251  102 PHE   A O   
598  C  CB  . PHE   A 82  ? 0.9705 1.1108 1.5473 0.0060  0.1259  0.2019  102 PHE   A CB  
599  C  CG  . PHE   A 82  ? 0.8951 1.0251 1.5083 -0.0119 0.0921  0.1913  102 PHE   A CG  
600  C  CD1 . PHE   A 82  ? 0.9113 1.0115 1.4751 -0.0085 0.0708  0.1712  102 PHE   A CD1 
601  C  CD2 . PHE   A 82  ? 0.8908 1.0397 1.5880 -0.0311 0.0802  0.2009  102 PHE   A CD2 
602  C  CE1 . PHE   A 82  ? 0.9092 0.9905 1.4977 -0.0227 0.0389  0.1585  102 PHE   A CE1 
603  C  CE2 . PHE   A 82  ? 0.9323 1.0647 1.6586 -0.0491 0.0441  0.1885  102 PHE   A CE2 
604  C  CZ  . PHE   A 82  ? 0.9407 1.0351 1.6079 -0.0443 0.0237  0.1661  102 PHE   A CZ  
605  N  N   . THR   A 83  ? 0.9446 1.0396 1.4212 0.0459  0.2271  0.2481  103 THR   A N   
606  C  CA  . THR   A 83  ? 1.0125 1.1025 1.4447 0.0651  0.2595  0.2569  103 THR   A CA  
607  C  C   . THR   A 83  ? 0.9806 1.0564 1.3279 0.0777  0.2448  0.2353  103 THR   A C   
608  O  O   . THR   A 83  ? 0.8879 0.9612 1.1991 0.0904  0.2590  0.2336  103 THR   A O   
609  C  CB  . THR   A 83  ? 0.9612 1.0259 1.3822 0.0744  0.3006  0.2853  103 THR   A CB  
610  O  OG1 . THR   A 83  ? 1.0347 1.1120 1.5419 0.0575  0.3104  0.3069  103 THR   A OG1 
611  C  CG2 . THR   A 83  ? 1.0734 1.1342 1.4611 0.0951  0.3392  0.2971  103 THR   A CG2 
612  N  N   . ASN   A 84  ? 0.9366 1.0030 1.2541 0.0747  0.2166  0.2190  104 ASN   A N   
613  C  CA  . ASN   A 84  ? 0.9360 0.9914 1.1797 0.0860  0.2044  0.2034  104 ASN   A CA  
614  C  C   . ASN   A 84  ? 0.8659 0.9412 1.1108 0.0781  0.1677  0.1797  104 ASN   A C   
615  O  O   . ASN   A 84  ? 0.8413 0.9268 1.1279 0.0671  0.1498  0.1738  104 ASN   A O   
616  C  CB  . ASN   A 84  ? 0.9603 0.9835 1.1552 0.0973  0.2125  0.2121  104 ASN   A CB  
617  C  CG  . ASN   A 84  ? 1.0791 1.0787 1.2639 0.1073  0.2523  0.2383  104 ASN   A CG  
618  O  OD1 . ASN   A 84  ? 1.1106 1.1108 1.2850 0.1150  0.2751  0.2442  104 ASN   A OD1 
619  N  ND2 . ASN   A 84  ? 1.1190 1.0946 1.3048 0.1088  0.2630  0.2552  104 ASN   A ND2 
620  N  N   . ARG   A 85  ? 0.9217 1.0005 1.1181 0.0840  0.1569  0.1667  105 ARG   A N   
621  C  CA  . ARG   A 85  ? 0.9421 1.0408 1.1309 0.0795  0.1277  0.1475  105 ARG   A CA  
622  C  C   . ARG   A 85  ? 0.8951 0.9842 1.0476 0.0884  0.1172  0.1433  105 ARG   A C   
623  O  O   . ARG   A 85  ? 0.9579 1.0221 1.0920 0.0971  0.1299  0.1552  105 ARG   A O   
624  C  CB  . ARG   A 85  ? 0.8416 0.9528 1.0092 0.0781  0.1227  0.1391  105 ARG   A CB  
625  C  CG  . ARG   A 85  ? 0.8434 0.9606 1.0425 0.0743  0.1349  0.1450  105 ARG   A CG  
626  C  CD  . ARG   A 85  ? 0.8519 0.9760 1.0284 0.0723  0.1259  0.1356  105 ARG   A CD  
627  N  NE  . ARG   A 85  ? 0.8164 0.9422 1.0188 0.0731  0.1386  0.1422  105 ARG   A NE  
628  C  CZ  . ARG   A 85  ? 0.8899 0.9935 1.0689 0.0834  0.1608  0.1485  105 ARG   A CZ  
629  N  NH1 . ARG   A 85  ? 0.9150 0.9901 1.0385 0.0923  0.1704  0.1481  105 ARG   A NH1 
630  N  NH2 . ARG   A 85  ? 0.8723 0.9804 1.0815 0.0871  0.1727  0.1551  105 ARG   A NH2 
631  N  N   . ARG   A 86  ? 0.8420 0.9520 0.9849 0.0878  0.0952  0.1283  106 ARG   A N   
632  C  CA  . ARG   A 86  ? 0.9234 1.0321 1.0390 0.0987  0.0843  0.1247  106 ARG   A CA  
633  C  C   . ARG   A 86  ? 0.9875 1.0823 1.0570 0.1075  0.0900  0.1318  106 ARG   A C   
634  O  O   . ARG   A 86  ? 1.0465 1.1461 1.0971 0.1031  0.0896  0.1288  106 ARG   A O   
635  C  CB  . ARG   A 86  ? 0.9317 1.0729 1.0494 0.0976  0.0643  0.1098  106 ARG   A CB  
636  C  CG  . ARG   A 86  ? 0.8549 0.9976 0.9742 0.1089  0.0537  0.1036  106 ARG   A CG  
637  C  CD  . ARG   A 86  ? 0.8458 1.0252 0.9642 0.1110  0.0400  0.0917  106 ARG   A CD  
638  N  NE  . ARG   A 86  ? 0.8573 1.0465 0.9951 0.1035  0.0347  0.0818  106 ARG   A NE  
639  C  CZ  . ARG   A 86  ? 0.8423 1.0388 0.9808 0.1123  0.0262  0.0706  106 ARG   A CZ  
640  N  NH1 . ARG   A 86  ? 0.8216 1.0202 0.9485 0.1299  0.0239  0.0681  106 ARG   A NH1 
641  N  NH2 . ARG   A 86  ? 0.8706 1.0710 1.0183 0.1057  0.0197  0.0618  106 ARG   A NH2 
642  N  N   . PRO   A 87  ? 1.0081 1.0806 1.0543 0.1203  0.0934  0.1409  107 PRO   A N   
643  C  CA  . PRO   A 87  ? 1.1057 1.1598 1.0996 0.1303  0.0958  0.1478  107 PRO   A CA  
644  C  C   . PRO   A 87  ? 1.1476 1.2287 1.1222 0.1301  0.0711  0.1362  107 PRO   A C   
645  O  O   . PRO   A 87  ? 1.1354 1.2386 1.1196 0.1362  0.0546  0.1317  107 PRO   A O   
646  C  CB  . PRO   A 87  ? 1.1299 1.1557 1.1086 0.1450  0.1020  0.1615  107 PRO   A CB  
647  C  CG  . PRO   A 87  ? 1.0763 1.1137 1.0953 0.1441  0.0925  0.1553  107 PRO   A CG  
648  C  CD  . PRO   A 87  ? 1.0283 1.0855 1.0909 0.1270  0.0935  0.1455  107 PRO   A CD  
649  N  N   . PHE   A 88  ? 1.2239 1.3022 1.1734 0.1235  0.0691  0.1320  108 PHE   A N   
650  C  CA  . PHE   A 88  ? 1.2333 1.3354 1.1691 0.1182  0.0442  0.1225  108 PHE   A CA  
651  C  C   . PHE   A 88  ? 1.3263 1.4076 1.2096 0.1302  0.0323  0.1269  108 PHE   A C   
652  O  O   . PHE   A 88  ? 1.3419 1.3810 1.1824 0.1403  0.0473  0.1353  108 PHE   A O   
653  C  CB  . PHE   A 88  ? 1.2402 1.3440 1.1756 0.1026  0.0440  0.1145  108 PHE   A CB  
654  C  CG  . PHE   A 88  ? 1.3226 1.4491 1.2502 0.0921  0.0177  0.1062  108 PHE   A CG  
655  C  CD1 . PHE   A 88  ? 1.3332 1.5067 1.3026 0.0823  0.0050  0.1020  108 PHE   A CD1 
656  C  CD2 . PHE   A 88  ? 1.3546 1.4540 1.2325 0.0915  0.0056  0.1032  108 PHE   A CD2 
657  C  CE1 . PHE   A 88  ? 1.3400 1.5388 1.3119 0.0699  -0.0176 0.0979  108 PHE   A CE1 
658  C  CE2 . PHE   A 88  ? 1.3211 1.4414 1.1988 0.0777  -0.0223 0.0962  108 PHE   A CE2 
659  C  CZ  . PHE   A 88  ? 1.3518 1.5248 1.2817 0.0657  -0.0331 0.0950  108 PHE   A CZ  
660  N  N   . GLY   A 89  ? 1.5320 1.6448 1.4192 0.1299  0.0051  0.1224  109 GLY   A N   
661  C  CA  . GLY   A 89  ? 1.6188 1.7187 1.4606 0.1405  -0.0147 0.1257  109 GLY   A CA  
662  C  C   . GLY   A 89  ? 1.5937 1.7444 1.4631 0.1379  -0.0457 0.1220  109 GLY   A C   
663  O  O   . GLY   A 89  ? 1.6071 1.8026 1.5293 0.1305  -0.0467 0.1183  109 GLY   A O   
664  N  N   . PRO   A 90  ? 1.5146 1.6607 1.3487 0.1448  -0.0717 0.1241  110 PRO   A N   
665  C  CA  . PRO   A 90  ? 1.6201 1.7106 1.3791 0.1560  -0.0745 0.1279  110 PRO   A CA  
666  C  C   . PRO   A 90  ? 1.6631 1.7223 1.3825 0.1402  -0.0781 0.1165  110 PRO   A C   
667  O  O   . PRO   A 90  ? 1.6262 1.7132 1.3733 0.1191  -0.0958 0.1061  110 PRO   A O   
668  C  CB  . PRO   A 90  ? 1.6406 1.7521 1.3895 0.1679  -0.1101 0.1326  110 PRO   A CB  
669  C  CG  . PRO   A 90  ? 1.5703 1.7492 1.3852 0.1505  -0.1322 0.1258  110 PRO   A CG  
670  C  CD  . PRO   A 90  ? 1.4599 1.6616 1.3294 0.1438  -0.1027 0.1239  110 PRO   A CD  
671  N  N   . VAL   A 91  ? 1.7893 1.7879 1.4424 0.1510  -0.0599 0.1189  111 VAL   A N   
672  C  CA  . VAL   A 91  ? 1.8610 1.8211 1.4716 0.1406  -0.0578 0.1068  111 VAL   A CA  
673  C  C   . VAL   A 91  ? 1.9191 1.8195 1.4333 0.1566  -0.0681 0.1059  111 VAL   A C   
674  O  O   . VAL   A 91  ? 1.9723 1.8461 1.4419 0.1474  -0.0918 0.0912  111 VAL   A O   
675  C  CB  . VAL   A 91  ? 1.8244 1.7680 1.4531 0.1393  -0.0153 0.1091  111 VAL   A CB  
676  C  CG1 . VAL   A 91  ? 1.7674 1.7614 1.4752 0.1191  -0.0148 0.1039  111 VAL   A CG1 
677  C  CG2 . VAL   A 91  ? 1.7998 1.7273 1.4275 0.1587  0.0182  0.1269  111 VAL   A CG2 
678  N  N   . GLY   A 92  ? 1.8409 1.7150 1.3178 0.1806  -0.0513 0.1216  112 GLY   A N   
679  C  CA  . GLY   A 92  ? 1.9140 1.7250 1.2887 0.2002  -0.0549 0.1233  112 GLY   A CA  
680  C  C   . GLY   A 92  ? 1.9019 1.6586 1.2303 0.2095  -0.0108 0.1247  112 GLY   A C   
681  O  O   . GLY   A 92  ? 1.8542 1.6137 1.2164 0.2157  0.0317  0.1397  112 GLY   A O   
682  N  N   . PHE   A 93  ? 1.9199 1.6267 1.1723 0.2109  -0.0216 0.1090  113 PHE   A N   
683  C  CA  . PHE   A 93  ? 1.9255 1.5791 1.1297 0.2239  0.0221  0.1092  113 PHE   A CA  
684  C  C   . PHE   A 93  ? 1.8353 1.5196 1.1201 0.2074  0.0485  0.1062  113 PHE   A C   
685  O  O   . PHE   A 93  ? 1.7745 1.4357 1.0542 0.2198  0.0945  0.1150  113 PHE   A O   
686  C  CB  . PHE   A 93  ? 2.0244 1.6115 1.1229 0.2304  0.0003  0.0889  113 PHE   A CB  
687  C  CG  . PHE   A 93  ? 2.0241 1.6175 1.1474 0.2042  -0.0269 0.0645  113 PHE   A CG  
688  C  CD1 . PHE   A 93  ? 2.0252 1.6584 1.1866 0.1787  -0.0812 0.0528  113 PHE   A CD1 
689  C  CD2 . PHE   A 93  ? 2.0406 1.6008 1.1529 0.2055  0.0032  0.0556  113 PHE   A CD2 
690  C  CE1 . PHE   A 93  ? 2.0398 1.6770 1.2271 0.1522  -0.1046 0.0336  113 PHE   A CE1 
691  C  CE2 . PHE   A 93  ? 2.0378 1.5980 1.1716 0.1815  -0.0214 0.0351  113 PHE   A CE2 
692  C  CZ  . PHE   A 93  ? 2.0427 1.6401 1.2135 0.1533  -0.0753 0.0245  113 PHE   A CZ  
693  N  N   . MET   A 94  ? 1.7872 1.5248 1.1474 0.1809  0.0211  0.0959  114 MET   A N   
694  C  CA  . MET   A 94  ? 1.7209 1.4886 1.1556 0.1660  0.0424  0.0944  114 MET   A CA  
695  C  C   . MET   A 94  ? 1.6304 1.4281 1.1286 0.1719  0.0797  0.1142  114 MET   A C   
696  O  O   . MET   A 94  ? 1.5530 1.3738 1.1111 0.1620  0.0982  0.1147  114 MET   A O   
697  C  CB  . MET   A 94  ? 1.7293 1.5473 1.2255 0.1376  0.0053  0.0821  114 MET   A CB  
698  C  CG  . MET   A 94  ? 1.7742 1.5616 1.2294 0.1230  -0.0255 0.0615  114 MET   A CG  
699  S  SD  . MET   A 94  ? 1.7530 1.4903 1.1849 0.1281  0.0099  0.0542  114 MET   A SD  
700  C  CE  . MET   A 94  ? 1.5502 1.3548 1.0965 0.1122  0.0294  0.0642  114 MET   A CE  
701  N  N   . LYS   A 95  ? 1.6701 1.4644 1.1558 0.1873  0.0897  0.1311  115 LYS   A N   
702  C  CA  . LYS   A 95  ? 1.5858 1.3995 1.1297 0.1909  0.1246  0.1501  115 LYS   A CA  
703  C  C   . LYS   A 95  ? 1.5216 1.3065 1.0572 0.2013  0.1709  0.1595  115 LYS   A C   
704  O  O   . LYS   A 95  ? 1.4622 1.2714 1.0654 0.1970  0.1973  0.1721  115 LYS   A O   
705  C  CB  . LYS   A 95  ? 1.6148 1.4202 1.1400 0.2062  0.1269  0.1683  115 LYS   A CB  
706  C  CG  . LYS   A 95  ? 1.6876 1.4321 1.1153 0.2309  0.1438  0.1789  115 LYS   A CG  
707  C  CD  . LYS   A 95  ? 1.7373 1.4711 1.1382 0.2465  0.1378  0.1970  115 LYS   A CD  
708  C  CE  . LYS   A 95  ? 1.7740 1.4427 1.0686 0.2732  0.1576  0.2099  115 LYS   A CE  
709  N  NZ  . LYS   A 95  ? 1.6773 1.3312 0.9377 0.2900  0.1478  0.2288  115 LYS   A NZ  
710  N  N   . SER   A 96  ? 1.5813 1.3147 1.0360 0.2159  0.1803  0.1534  116 SER   A N   
711  C  CA  . SER   A 96  ? 1.6110 1.3149 1.0507 0.2317  0.2283  0.1632  116 SER   A CA  
712  C  C   . SER   A 96  ? 1.5451 1.2578 1.0185 0.2213  0.2307  0.1484  116 SER   A C   
713  O  O   . SER   A 96  ? 1.5094 1.1961 0.9669 0.2371  0.2682  0.1536  116 SER   A O   
714  C  CB  . SER   A 96  ? 1.7075 1.3431 1.0305 0.2592  0.2424  0.1650  116 SER   A CB  
715  O  OG  . SER   A 96  ? 1.7988 1.4030 1.0529 0.2561  0.2022  0.1388  116 SER   A OG  
716  N  N   . ALA   A 97  ? 1.4826 1.2301 1.0003 0.1972  0.1932  0.1319  117 ALA   A N   
717  C  CA  . ALA   A 97  ? 1.4364 1.1954 0.9947 0.1862  0.1953  0.1216  117 ALA   A CA  
718  C  C   . ALA   A 97  ? 1.3624 1.1632 1.0106 0.1832  0.2247  0.1382  117 ALA   A C   
719  O  O   . ALA   A 97  ? 1.3841 1.2210 1.0845 0.1760  0.2237  0.1500  117 ALA   A O   
720  C  CB  . ALA   A 97  ? 1.3827 1.1692 0.9649 0.1604  0.1489  0.1036  117 ALA   A CB  
721  N  N   . ILE   A 98  ? 1.3226 1.1161 0.9888 0.1893  0.2486  0.1387  118 ILE   A N   
722  C  CA  . ILE   A 98  ? 1.2895 1.1203 1.0397 0.1892  0.2778  0.1566  118 ILE   A CA  
723  C  C   . ILE   A 98  ? 1.2310 1.1180 1.0622 0.1643  0.2503  0.1545  118 ILE   A C   
724  O  O   . ILE   A 98  ? 1.1757 1.0944 1.0689 0.1596  0.2608  0.1691  118 ILE   A O   
725  C  CB  . ILE   A 98  ? 1.3517 1.1668 1.1076 0.2026  0.3044  0.1567  118 ILE   A CB  
726  C  CG1 . ILE   A 98  ? 1.2419 1.1049 1.0974 0.1998  0.3273  0.1755  118 ILE   A CG1 
727  C  CG2 . ILE   A 98  ? 1.2662 1.0686 1.0042 0.1914  0.2736  0.1343  118 ILE   A CG2 
728  C  CD1 . ILE   A 98  ? 1.2781 1.1364 1.1547 0.2131  0.3494  0.1770  118 ILE   A CD1 
729  N  N   . SER   A 99  ? 1.1918 1.0890 1.0214 0.1479  0.2149  0.1366  119 SER   A N   
730  C  CA  . SER   A 99  ? 1.1088 1.0558 1.0039 0.1274  0.1905  0.1340  119 SER   A CA  
731  C  C   . SER   A 99  ? 1.1375 1.1034 1.0377 0.1222  0.1744  0.1362  119 SER   A C   
732  O  O   . SER   A 99  ? 1.1119 1.1158 1.0607 0.1088  0.1566  0.1336  119 SER   A O   
733  C  CB  . SER   A 99  ? 1.1067 1.0581 0.9958 0.1125  0.1618  0.1179  119 SER   A CB  
734  O  OG  . SER   A 99  ? 1.1073 1.0319 0.9330 0.1104  0.1407  0.1060  119 SER   A OG  
735  N  N   . ILE   A 100 ? 1.1983 1.1357 1.0455 0.1349  0.1806  0.1411  120 ILE   A N   
736  C  CA  . ILE   A 100 ? 1.2028 1.1532 1.0509 0.1340  0.1658  0.1447  120 ILE   A CA  
737  C  C   . ILE   A 100 ? 1.2465 1.1786 1.0902 0.1482  0.1946  0.1648  120 ILE   A C   
738  O  O   . ILE   A 100 ? 1.2333 1.1797 1.1016 0.1461  0.1877  0.1714  120 ILE   A O   
739  C  CB  . ILE   A 100 ? 1.2327 1.1702 1.0217 0.1342  0.1355  0.1329  120 ILE   A CB  
740  C  CG1 . ILE   A 100 ? 1.2176 1.1622 1.0041 0.1193  0.1121  0.1158  120 ILE   A CG1 
741  C  CG2 . ILE   A 100 ? 1.2618 1.2274 1.0699 0.1317  0.1139  0.1346  120 ILE   A CG2 
742  C  CD1 . ILE   A 100 ? 1.2771 1.2082 1.0106 0.1161  0.0798  0.1044  120 ILE   A CD1 
743  N  N   . ALA   A 101 ? 1.3099 1.2094 1.1236 0.1634  0.2288  0.1762  121 ALA   A N   
744  C  CA  . ALA   A 101 ? 1.3056 1.1858 1.1121 0.1770  0.2608  0.1995  121 ALA   A CA  
745  C  C   . ALA   A 101 ? 1.2315 1.1449 1.1285 0.1653  0.2732  0.2137  121 ALA   A C   
746  O  O   . ALA   A 101 ? 1.1461 1.0944 1.1054 0.1498  0.2600  0.2051  121 ALA   A O   
747  C  CB  . ALA   A 101 ? 1.3781 1.2187 1.1335 0.1979  0.2995  0.2092  121 ALA   A CB  
748  N  N   . GLU   A 102 ? 1.2615 1.1604 1.1631 0.1723  0.2977  0.2366  122 GLU   A N   
749  C  CA  . GLU   A 102 ? 1.2147 1.1379 1.1990 0.1585  0.3038  0.2502  122 GLU   A CA  
750  C  C   . GLU   A 102 ? 1.2465 1.1591 1.2560 0.1657  0.3513  0.2801  122 GLU   A C   
751  O  O   . GLU   A 102 ? 1.2408 1.1180 1.1882 0.1854  0.3805  0.2952  122 GLU   A O   
752  C  CB  . GLU   A 102 ? 1.1393 1.0573 1.1205 0.1549  0.2811  0.2504  122 GLU   A CB  
753  C  CG  . GLU   A 102 ? 1.2164 1.1521 1.1823 0.1493  0.2376  0.2244  122 GLU   A CG  
754  C  CD  . GLU   A 102 ? 1.1976 1.1363 1.1834 0.1459  0.2175  0.2242  122 GLU   A CD  
755  O  OE1 . GLU   A 102 ? 1.2358 1.1563 1.2429 0.1464  0.2352  0.2438  122 GLU   A OE1 
756  O  OE2 . GLU   A 102 ? 1.1398 1.0978 1.1214 0.1433  0.1856  0.2055  122 GLU   A OE2 
757  N  N   . ASP   A 103 ? 1.1347 1.0796 1.2368 0.1497  0.3581  0.2893  123 ASP   A N   
758  C  CA  . ASP   A 103 ? 1.1957 1.1425 1.3502 0.1495  0.3995  0.3215  123 ASP   A CA  
759  C  C   . ASP   A 103 ? 1.2868 1.2145 1.3998 0.1733  0.4473  0.3389  123 ASP   A C   
760  O  O   . ASP   A 103 ? 1.3054 1.2465 1.4234 0.1804  0.4556  0.3305  123 ASP   A O   
761  C  CB  . ASP   A 103 ? 1.2775 1.2006 1.4307 0.1455  0.4022  0.3395  123 ASP   A CB  
762  C  CG  . ASP   A 103 ? 1.2039 1.1455 1.4212 0.1216  0.3651  0.3283  123 ASP   A CG  
763  O  OD1 . ASP   A 103 ? 1.1850 1.1588 1.4891 0.1031  0.3620  0.3308  123 ASP   A OD1 
764  O  OD2 . ASP   A 103 ? 1.2565 1.1796 1.4358 0.1228  0.3377  0.3164  123 ASP   A OD2 
765  N  N   . GLU   A 104 ? 1.3850 1.2778 1.4525 0.1881  0.4804  0.3638  124 GLU   A N   
766  C  CA  . GLU   A 104 ? 1.4020 1.2752 1.4332 0.2128  0.5254  0.3791  124 GLU   A CA  
767  C  C   . GLU   A 104 ? 1.4364 1.2787 1.3660 0.2353  0.5232  0.3578  124 GLU   A C   
768  O  O   . GLU   A 104 ? 1.3886 1.2269 1.3104 0.2516  0.5442  0.3545  124 GLU   A O   
769  C  CB  . GLU   A 104 ? 1.4609 1.3013 1.4621 0.2231  0.5468  0.4015  124 GLU   A CB  
770  C  CG  . GLU   A 104 ? 1.4676 1.3344 1.5732 0.2025  0.5564  0.4249  124 GLU   A CG  
771  C  CD  . GLU   A 104 ? 1.4723 1.3776 1.6645 0.2002  0.5774  0.4339  124 GLU   A CD  
772  O  OE1 . GLU   A 104 ? 1.4865 1.3799 1.6402 0.2249  0.6037  0.4347  124 GLU   A OE1 
773  O  OE2 . GLU   A 104 ? 1.5003 1.4452 1.7974 0.1745  0.5654  0.4402  124 GLU   A OE2 
774  N  N   . GLU   A 105 ? 1.4049 1.2231 1.2602 0.2358  0.4862  0.3366  125 GLU   A N   
775  C  CA  . GLU   A 105 ? 1.4597 1.2455 1.2209 0.2529  0.4744  0.3123  125 GLU   A CA  
776  C  C   . GLU   A 105 ? 1.4529 1.2676 1.2563 0.2429  0.4560  0.2890  125 GLU   A C   
777  O  O   . GLU   A 105 ? 1.4586 1.2497 1.2144 0.2603  0.4708  0.2797  125 GLU   A O   
778  C  CB  . GLU   A 105 ? 1.4833 1.2437 1.1691 0.2524  0.4305  0.2941  125 GLU   A CB  
779  C  CG  . GLU   A 105 ? 1.5938 1.3029 1.1609 0.2747  0.4259  0.2780  125 GLU   A CG  
780  C  CD  . GLU   A 105 ? 1.6407 1.3384 1.1529 0.2688  0.3720  0.2560  125 GLU   A CD  
781  O  OE1 . GLU   A 105 ? 1.6199 1.3584 1.1927 0.2459  0.3345  0.2429  125 GLU   A OE1 
782  O  OE2 . GLU   A 105 ? 1.7566 1.4054 1.1647 0.2881  0.3670  0.2524  125 GLU   A OE2 
783  N  N   . TRP   A 106 ? 1.3677 1.2283 1.2549 0.2166  0.4239  0.2794  126 TRP   A N   
784  C  CA  . TRP   A 106 ? 1.3687 1.2574 1.2999 0.2075  0.4087  0.2620  126 TRP   A CA  
785  C  C   . TRP   A 106 ? 1.3665 1.2731 1.3556 0.2174  0.4517  0.2812  126 TRP   A C   
786  O  O   . TRP   A 106 ? 1.3274 1.2291 1.3053 0.2284  0.4584  0.2711  126 TRP   A O   
787  C  CB  . TRP   A 106 ? 1.2504 1.1821 1.2526 0.1798  0.3669  0.2496  126 TRP   A CB  
788  C  CG  . TRP   A 106 ? 1.2389 1.2050 1.3067 0.1711  0.3613  0.2429  126 TRP   A CG  
789  C  CD1 . TRP   A 106 ? 1.2101 1.1745 1.2562 0.1705  0.3407  0.2218  126 TRP   A CD1 
790  C  CD2 . TRP   A 106 ? 1.2060 1.2119 1.3725 0.1624  0.3754  0.2596  126 TRP   A CD2 
791  N  NE1 . TRP   A 106 ? 1.1633 1.1624 1.2839 0.1642  0.3418  0.2247  126 TRP   A NE1 
792  C  CE2 . TRP   A 106 ? 1.1427 1.1700 1.3393 0.1592  0.3613  0.2471  126 TRP   A CE2 
793  C  CE3 . TRP   A 106 ? 1.1787 1.2037 1.4136 0.1555  0.3964  0.2849  126 TRP   A CE3 
794  C  CZ2 . TRP   A 106 ? 1.0253 1.0946 1.3163 0.1516  0.3654  0.2586  126 TRP   A CZ2 
795  C  CZ3 . TRP   A 106 ? 1.1389 1.2073 1.4728 0.1447  0.3996  0.2956  126 TRP   A CZ3 
796  C  CH2 . TRP   A 106 ? 1.1159 1.2074 1.4763 0.1438  0.3830  0.2820  126 TRP   A CH2 
797  N  N   . LYS   A 107 ? 1.5249 1.4534 1.5815 0.2134  0.4806  0.3102  127 LYS   A N   
798  C  CA  . LYS   A 107 ? 1.5031 1.4571 1.6290 0.2218  0.5197  0.3315  127 LYS   A CA  
799  C  C   . LYS   A 107 ? 1.5828 1.4945 1.6332 0.2540  0.5487  0.3294  127 LYS   A C   
800  O  O   . LYS   A 107 ? 1.6252 1.5490 1.7086 0.2646  0.5620  0.3300  127 LYS   A O   
801  C  CB  . LYS   A 107 ? 1.5172 1.4877 1.7125 0.2106  0.5324  0.3577  127 LYS   A CB  
802  C  CG  . LYS   A 107 ? 1.4784 1.5040 1.7997 0.1903  0.5237  0.3671  127 LYS   A CG  
803  C  CD  . LYS   A 107 ? 1.5028 1.5492 1.8846 0.1602  0.4990  0.3722  127 LYS   A CD  
804  C  CE  . LYS   A 107 ? 1.4957 1.5080 1.8414 0.1629  0.5157  0.3899  127 LYS   A CE  
805  N  NZ  . LYS   A 107 ? 1.4536 1.4708 1.8351 0.1364  0.4896  0.3916  127 LYS   A NZ  
806  N  N   . ARG   A 108 ? 1.5507 1.4095 1.4962 0.2712  0.5568  0.3270  128 ARG   A N   
807  C  CA  . ARG   A 108 ? 1.5656 1.3743 1.4237 0.3029  0.5801  0.3211  128 ARG   A CA  
808  C  C   . ARG   A 108 ? 1.5357 1.3227 1.3352 0.3094  0.5623  0.2921  128 ARG   A C   
809  O  O   . ARG   A 108 ? 1.5069 1.2775 1.2927 0.3286  0.5793  0.2866  128 ARG   A O   
810  C  CB  . ARG   A 108 ? 1.6604 1.4173 1.4212 0.3183  0.5875  0.3256  128 ARG   A CB  
811  C  CG  . ARG   A 108 ? 1.7897 1.5152 1.5181 0.3472  0.6277  0.3415  128 ARG   A CG  
812  C  CD  . ARG   A 108 ? 2.0018 1.6851 1.6513 0.3586  0.6329  0.3501  128 ARG   A CD  
813  N  NE  . ARG   A 108 ? 1.9484 1.6621 1.6587 0.3356  0.6243  0.3677  128 ARG   A NE  
814  C  CZ  . ARG   A 108 ? 1.8861 1.5926 1.5631 0.3219  0.5916  0.3593  128 ARG   A CZ  
815  N  NH1 . ARG   A 108 ? 1.8580 1.5324 1.4435 0.3271  0.5621  0.3340  128 ARG   A NH1 
816  N  NH2 . ARG   A 108 ? 1.8090 1.5393 1.5458 0.3027  0.5871  0.3772  128 ARG   A NH2 
817  N  N   . LEU   A 109 ? 1.5397 1.3239 1.3066 0.2921  0.5218  0.2718  129 LEU   A N   
818  C  CA  . LEU   A 109 ? 1.5626 1.3239 1.2823 0.2902  0.4868  0.2391  129 LEU   A CA  
819  C  C   . LEU   A 109 ? 1.5216 1.3208 1.3245 0.2836  0.4857  0.2358  129 LEU   A C   
820  O  O   . LEU   A 109 ? 1.5468 1.3169 1.3108 0.2956  0.4832  0.2187  129 LEU   A O   
821  C  CB  . LEU   A 109 ? 1.4682 1.2323 1.1668 0.2651  0.4289  0.2178  129 LEU   A CB  
822  C  CG  . LEU   A 109 ? 1.4792 1.1994 1.0810 0.2737  0.4184  0.2151  129 LEU   A CG  
823  C  CD1 . LEU   A 109 ? 1.4732 1.2180 1.0911 0.2475  0.3656  0.2017  129 LEU   A CD1 
824  C  CD2 . LEU   A 109 ? 1.6136 1.2665 1.0992 0.2958  0.4184  0.1961  129 LEU   A CD2 
825  N  N   . ARG   A 110 ? 1.3747 1.2350 1.2897 0.2649  0.4849  0.2519  130 ARG   A N   
826  C  CA  . ARG   A 110 ? 1.3150 1.2141 1.3121 0.2606  0.4831  0.2521  130 ARG   A CA  
827  C  C   . ARG   A 110 ? 1.3507 1.2396 1.3516 0.2933  0.5364  0.2681  130 ARG   A C   
828  O  O   . ARG   A 110 ? 1.3416 1.2174 1.3332 0.3063  0.5365  0.2563  130 ARG   A O   
829  C  CB  . ARG   A 110 ? 1.2410 1.2042 1.3528 0.2343  0.4687  0.2662  130 ARG   A CB  
830  C  CG  . ARG   A 110 ? 1.1327 1.1381 1.3269 0.2263  0.4539  0.2640  130 ARG   A CG  
831  C  CD  . ARG   A 110 ? 1.1122 1.1147 1.2838 0.2077  0.4020  0.2361  130 ARG   A CD  
832  N  NE  . ARG   A 110 ? 1.0652 1.1015 1.3041 0.2030  0.3878  0.2352  130 ARG   A NE  
833  C  CZ  . ARG   A 110 ? 1.0094 1.0589 1.2570 0.1838  0.3448  0.2184  130 ARG   A CZ  
834  N  NH1 . ARG   A 110 ? 1.0077 1.0453 1.2097 0.1666  0.3128  0.2013  130 ARG   A NH1 
835  N  NH2 . ARG   A 110 ? 0.9454 1.0222 1.2496 0.1834  0.3347  0.2208  130 ARG   A NH2 
836  N  N   . SER   A 111 ? 1.3530 1.2405 1.3665 0.3026  0.5664  0.2918  131 SER   A N   
837  C  CA  . SER   A 111 ? 1.3707 1.2437 1.3864 0.3288  0.6007  0.3049  131 SER   A CA  
838  C  C   . SER   A 111 ? 1.4445 1.2442 1.3358 0.3592  0.6137  0.2864  131 SER   A C   
839  O  O   . SER   A 111 ? 1.4698 1.2526 1.3541 0.3823  0.6346  0.2877  131 SER   A O   
840  C  CB  . SER   A 111 ? 1.3698 1.2541 1.4214 0.3306  0.6273  0.3344  131 SER   A CB  
841  O  OG  . SER   A 111 ? 1.4499 1.3294 1.5164 0.3553  0.6625  0.3510  131 SER   A OG  
842  N  N   . LEU   A 112 ? 1.4858 1.2389 1.2757 0.3596  0.5989  0.2687  132 LEU   A N   
843  C  CA  . LEU   A 112 ? 1.5992 1.2750 1.2623 0.3859  0.6029  0.2473  132 LEU   A CA  
844  C  C   . LEU   A 112 ? 1.6220 1.2810 1.2660 0.3875  0.5847  0.2207  132 LEU   A C   
845  O  O   . LEU   A 112 ? 1.6633 1.2698 1.2458 0.4128  0.5970  0.2087  132 LEU   A O   
846  C  CB  . LEU   A 112 ? 1.6676 1.2997 1.2292 0.3832  0.5840  0.2356  132 LEU   A CB  
847  C  CG  . LEU   A 112 ? 1.7829 1.3283 1.2047 0.4104  0.5850  0.2161  132 LEU   A CG  
848  C  CD1 . LEU   A 112 ? 1.9175 1.4394 1.3095 0.4336  0.6188  0.2380  132 LEU   A CD1 
849  C  CD2 . LEU   A 112 ? 1.9004 1.4093 1.2301 0.3978  0.5423  0.1905  132 LEU   A CD2 
850  N  N   . LEU   A 113 ? 1.5827 1.2820 1.2824 0.3567  0.5454  0.2103  133 LEU   A N   
851  C  CA  . LEU   A 113 ? 1.6016 1.2827 1.2889 0.3463  0.5067  0.1838  133 LEU   A CA  
852  C  C   . LEU   A 113 ? 1.5472 1.2803 1.3416 0.3421  0.5088  0.1933  133 LEU   A C   
853  O  O   . LEU   A 113 ? 1.5703 1.2910 1.3622 0.3328  0.4779  0.1751  133 LEU   A O   
854  C  CB  . LEU   A 113 ? 1.5865 1.2715 1.2566 0.3101  0.4465  0.1637  133 LEU   A CB  
855  C  CG  . LEU   A 113 ? 1.7087 1.3272 1.2567 0.3136  0.4263  0.1429  133 LEU   A CG  
856  C  CD1 . LEU   A 113 ? 1.8476 1.3888 1.3008 0.3479  0.4513  0.1300  133 LEU   A CD1 
857  C  CD2 . LEU   A 113 ? 1.7268 1.3495 1.2492 0.3156  0.4368  0.1573  133 LEU   A CD2 
858  N  N   . SER   A 114 ? 1.5169 1.3075 1.4064 0.3478  0.5424  0.2225  134 SER   A N   
859  C  CA  . SER   A 114 ? 1.5024 1.3448 1.4959 0.3459  0.5419  0.2329  134 SER   A CA  
860  C  C   . SER   A 114 ? 1.6156 1.4179 1.5782 0.3778  0.5611  0.2249  134 SER   A C   
861  O  O   . SER   A 114 ? 1.5994 1.4116 1.5954 0.3681  0.5313  0.2155  134 SER   A O   
862  C  CB  . SER   A 114 ? 1.3476 1.2528 1.4455 0.3402  0.5629  0.2654  134 SER   A CB  
863  O  OG  . SER   A 114 ? 1.3549 1.3132 1.5213 0.3077  0.5364  0.2705  134 SER   A OG  
864  N  N   . PRO   A 115 ? 1.6513 1.4023 1.5460 0.4078  0.5945  0.2277  135 PRO   A N   
865  C  CA  . PRO   A 115 ? 1.6611 1.3778 1.5375 0.4349  0.6075  0.2223  135 PRO   A CA  
866  C  C   . PRO   A 115 ? 1.8130 1.4547 1.5950 0.4439  0.5871  0.1875  135 PRO   A C   
867  O  O   . PRO   A 115 ? 1.9245 1.5097 1.6514 0.4699  0.5993  0.1781  135 PRO   A O   
868  C  CB  . PRO   A 115 ? 1.7158 1.3995 1.5433 0.4618  0.6473  0.2367  135 PRO   A CB  
869  C  CG  . PRO   A 115 ? 1.6981 1.3563 1.4564 0.4542  0.6458  0.2328  135 PRO   A CG  
870  C  CD  . PRO   A 115 ? 1.6431 1.3659 1.4789 0.4182  0.6193  0.2383  135 PRO   A CD  
871  N  N   . THR   A 116 ? 1.8363 1.4767 1.6007 0.4084  0.5374  0.1692  136 THR   A N   
872  C  CA  . THR   A 116 ? 1.9394 1.5138 1.6259 0.3982  0.4975  0.1385  136 THR   A CA  
873  C  C   . THR   A 116 ? 1.9027 1.4989 1.6544 0.3863  0.4714  0.1377  136 THR   A C   
874  O  O   . THR   A 116 ? 1.9609 1.4936 1.6547 0.3901  0.4537  0.1177  136 THR   A O   
875  C  CB  . THR   A 116 ? 1.9938 1.5596 1.6333 0.3615  0.4511  0.1216  136 THR   A CB  
876  O  OG1 . THR   A 116 ? 1.9785 1.5438 1.5813 0.3695  0.4735  0.1300  136 THR   A OG1 
877  C  CG2 . THR   A 116 ? 2.0494 1.5304 1.5853 0.3570  0.4188  0.0900  136 THR   A CG2 
878  N  N   . PHE   A 117 ? 1.8205 1.5001 1.6875 0.3723  0.4672  0.1592  137 PHE   A N   
879  C  CA  . PHE   A 117 ? 1.7906 1.4959 1.7210 0.3619  0.4413  0.1619  137 PHE   A CA  
880  C  C   . PHE   A 117 ? 1.7376 1.5083 1.7763 0.3820  0.4705  0.1902  137 PHE   A C   
881  O  O   . PHE   A 117 ? 1.6361 1.4738 1.7650 0.3607  0.4469  0.2029  137 PHE   A O   
882  C  CB  . PHE   A 117 ? 1.6769 1.4203 1.6367 0.3161  0.3892  0.1560  137 PHE   A CB  
883  C  CG  . PHE   A 117 ? 1.6784 1.3742 1.5502 0.2932  0.3591  0.1322  137 PHE   A CG  
884  C  CD1 . PHE   A 117 ? 1.7413 1.3593 1.5309 0.2969  0.3456  0.1110  137 PHE   A CD1 
885  C  CD2 . PHE   A 117 ? 1.6017 1.3303 1.4767 0.2679  0.3422  0.1316  137 PHE   A CD2 
886  C  CE1 . PHE   A 117 ? 1.7310 1.3101 1.4484 0.2733  0.3138  0.0902  137 PHE   A CE1 
887  C  CE2 . PHE   A 117 ? 1.6169 1.3087 1.4194 0.2480  0.3127  0.1116  137 PHE   A CE2 
888  C  CZ  . PHE   A 117 ? 1.6996 1.3194 1.4261 0.2494  0.2974  0.0912  137 PHE   A CZ  
889  N  N   . THR   A 118 ? 1.8788 1.6310 1.9099 0.4244  0.5220  0.2008  138 THR   A N   
890  C  CA  . THR   A 118 ? 1.8484 1.6652 1.9831 0.4373  0.5428  0.2290  138 THR   A CA  
891  C  C   . THR   A 118 ? 1.8419 1.6539 2.0080 0.4480  0.5253  0.2280  138 THR   A C   
892  O  O   . THR   A 118 ? 1.8475 1.6123 1.9657 0.4399  0.4945  0.2085  138 THR   A O   
893  C  CB  . THR   A 118 ? 1.8611 1.6615 1.9673 0.4615  0.5863  0.2416  138 THR   A CB  
894  O  OG1 . THR   A 118 ? 1.8761 1.6034 1.9060 0.4931  0.6004  0.2276  138 THR   A OG1 
895  C  CG2 . THR   A 118 ? 1.9097 1.6855 1.9490 0.4565  0.6014  0.2379  138 THR   A CG2 
896  N  N   . SER   A 119 ? 1.9525 1.8131 2.1963 0.4583  0.5370  0.2502  139 SER   A N   
897  C  CA  . SER   A 119 ? 1.9681 1.8256 2.2420 0.4715  0.5217  0.2521  139 SER   A CA  
898  C  C   . SER   A 119 ? 2.0748 1.8343 2.2439 0.5011  0.5350  0.2316  139 SER   A C   
899  O  O   . SER   A 119 ? 2.0910 1.8002 2.2231 0.5007  0.5088  0.2162  139 SER   A O   
900  C  CB  . SER   A 119 ? 1.8755 1.8044 2.2508 0.4786  0.5335  0.2799  139 SER   A CB  
901  O  OG  . SER   A 119 ? 1.7422 1.7518 2.2070 0.4490  0.5198  0.2970  139 SER   A OG  
902  N  N   . GLY   A 120 ? 1.9748 1.7003 2.0910 0.5260  0.5745  0.2317  140 GLY   A N   
903  C  CA  . GLY   A 120 ? 1.9990 1.6265 2.0087 0.5543  0.5865  0.2103  140 GLY   A CA  
904  C  C   . GLY   A 120 ? 2.0489 1.5893 1.9362 0.5480  0.5769  0.1796  140 GLY   A C   
905  O  O   . GLY   A 120 ? 2.0656 1.5149 1.8615 0.5633  0.5719  0.1565  140 GLY   A O   
906  N  N   . LYS   A 121 ? 1.9888 1.5523 1.8708 0.5249  0.5716  0.1780  141 LYS   A N   
907  C  CA  . LYS   A 121 ? 2.0451 1.5282 1.8119 0.5172  0.5575  0.1480  141 LYS   A CA  
908  C  C   . LYS   A 121 ? 2.0151 1.4530 1.7550 0.4946  0.5094  0.1271  141 LYS   A C   
909  O  O   . LYS   A 121 ? 2.0374 1.3878 1.6711 0.4882  0.4894  0.0991  141 LYS   A O   
910  C  CB  . LYS   A 121 ? 1.9773 1.5045 1.7553 0.4950  0.5580  0.1532  141 LYS   A CB  
911  C  CG  . LYS   A 121 ? 2.0139 1.5028 1.7059 0.5089  0.5863  0.1502  141 LYS   A CG  
912  C  CD  . LYS   A 121 ? 2.0261 1.5342 1.7446 0.5366  0.6279  0.1741  141 LYS   A CD  
913  C  CE  . LYS   A 121 ? 2.0839 1.5362 1.7001 0.5556  0.6549  0.1704  141 LYS   A CE  
914  N  NZ  . LYS   A 121 ? 1.9940 1.4789 1.6135 0.5356  0.6551  0.1796  141 LYS   A NZ  
915  N  N   . LEU   A 122 ? 2.0022 1.5045 1.8365 0.4713  0.4808  0.1420  142 LEU   A N   
916  C  CA  . LEU   A 122 ? 2.0108 1.4824 1.8271 0.4404  0.4306  0.1287  142 LEU   A CA  
917  C  C   . LEU   A 122 ? 2.0013 1.4054 1.7921 0.4710  0.4369  0.1246  142 LEU   A C   
918  O  O   . LEU   A 122 ? 2.0237 1.3710 1.7693 0.4501  0.4009  0.1094  142 LEU   A O   
919  C  CB  . LEU   A 122 ? 1.9375 1.5008 1.8545 0.4051  0.3978  0.1466  142 LEU   A CB  
920  C  CG  . LEU   A 122 ? 1.8314 1.4689 1.7911 0.3782  0.3931  0.1544  142 LEU   A CG  
921  C  CD1 . LEU   A 122 ? 1.6390 1.3614 1.6988 0.3527  0.3650  0.1722  142 LEU   A CD1 
922  C  CD2 . LEU   A 122 ? 1.8082 1.4089 1.6877 0.3476  0.3679  0.1318  142 LEU   A CD2 
923  N  N   . LYS   A 123 ? 2.0404 1.4495 1.8622 0.5204  0.4827  0.1393  143 LYS   A N   
924  C  CA  . LYS   A 123 ? 2.1163 1.4753 1.9212 0.5435  0.4831  0.1371  143 LYS   A CA  
925  C  C   . LYS   A 123 ? 2.1672 1.4023 1.8383 0.5524  0.4802  0.1045  143 LYS   A C   
926  O  O   . LYS   A 123 ? 2.2174 1.3805 1.8485 0.5478  0.4539  0.0918  143 LYS   A O   
927  C  CB  . LYS   A 123 ? 2.0452 1.4652 1.9159 0.5728  0.5192  0.1599  143 LYS   A CB  
928  C  CG  . LYS   A 123 ? 2.0156 1.4625 1.9581 0.5844  0.5077  0.1767  143 LYS   A CG  
929  C  CD  . LYS   A 123 ? 2.0666 1.4113 1.9285 0.6063  0.5048  0.1584  143 LYS   A CD  
930  C  CE  . LYS   A 123 ? 2.0140 1.3828 1.9449 0.6173  0.4899  0.1760  143 LYS   A CE  
931  N  NZ  . LYS   A 123 ? 1.9288 1.4018 1.9689 0.6331  0.5118  0.2053  143 LYS   A NZ  
932  N  N   . GLU   A 124 ? 2.1177 1.3241 1.7159 0.5624  0.5036  0.0913  144 GLU   A N   
933  C  CA  . GLU   A 124 ? 2.2243 1.3130 1.6875 0.5674  0.4950  0.0577  144 GLU   A CA  
934  C  C   . GLU   A 124 ? 2.2616 1.2993 1.6631 0.5314  0.4550  0.0339  144 GLU   A C   
935  O  O   . GLU   A 124 ? 2.3374 1.3048 1.6333 0.5295  0.4491  0.0082  144 GLU   A O   
936  C  CB  . GLU   A 124 ? 2.2429 1.3208 1.6495 0.5958  0.5356  0.0566  144 GLU   A CB  
937  C  CG  . GLU   A 124 ? 2.2808 1.3782 1.7218 0.6344  0.5736  0.0748  144 GLU   A CG  
938  C  CD  . GLU   A 124 ? 2.3273 1.3447 1.7269 0.6491  0.5592  0.0593  144 GLU   A CD  
939  O  OE1 . GLU   A 124 ? 2.2534 1.2919 1.7199 0.6385  0.5364  0.0680  144 GLU   A OE1 
940  O  OE2 . GLU   A 124 ? 2.5074 1.4372 1.8041 0.6710  0.5689  0.0388  144 GLU   A OE2 
941  N  N   . MET   A 125 ? 2.2166 1.3173 1.6921 0.4861  0.4149  0.0452  145 MET   A N   
942  C  CA  . MET   A 125 ? 2.2118 1.2943 1.6511 0.4319  0.3612  0.0279  145 MET   A CA  
943  C  C   . MET   A 125 ? 2.2083 1.2455 1.6475 0.4090  0.3233  0.0237  145 MET   A C   
944  O  O   . MET   A 125 ? 2.2217 1.1904 1.5919 0.3793  0.2868  0.0010  145 MET   A O   
945  C  CB  . MET   A 125 ? 2.1275 1.3208 1.6466 0.3928  0.3434  0.0445  145 MET   A CB  
946  C  CG  . MET   A 125 ? 2.1122 1.3459 1.6254 0.4031  0.3710  0.0479  145 MET   A CG  
947  S  SD  . MET   A 125 ? 2.1264 1.4760 1.7265 0.3559  0.3446  0.0643  145 MET   A SD  
948  C  CE  . MET   A 125 ? 2.0408 1.4099 1.6152 0.3784  0.3852  0.0685  145 MET   A CE  
949  N  N   . VAL   A 126 ? 2.2650 1.3388 1.7815 0.4220  0.3303  0.0468  146 VAL   A N   
950  C  CA  . VAL   A 126 ? 2.2711 1.3099 1.7987 0.4038  0.2988  0.0507  146 VAL   A CA  
951  C  C   . VAL   A 126 ? 2.4044 1.3067 1.8273 0.4130  0.2891  0.0237  146 VAL   A C   
952  O  O   . VAL   A 126 ? 2.4653 1.3244 1.8671 0.3741  0.2482  0.0166  146 VAL   A O   
953  C  CB  . VAL   A 126 ? 2.2309 1.3206 1.8471 0.4327  0.3169  0.0802  146 VAL   A CB  
954  C  CG1 . VAL   A 126 ? 2.2185 1.2622 1.8362 0.4177  0.2863  0.0861  146 VAL   A CG1 
955  C  CG2 . VAL   A 126 ? 2.1138 1.3335 1.8338 0.4198  0.3194  0.1052  146 VAL   A CG2 
956  N  N   . PRO   A 127 ? 2.4770 1.3052 1.8334 0.4641  0.3257  0.0091  147 PRO   A N   
957  C  CA  . PRO   A 127 ? 2.5730 1.2610 1.8170 0.4700  0.3112  -0.0219 147 PRO   A CA  
958  C  C   . PRO   A 127 ? 2.6318 1.2760 1.8042 0.4217  0.2681  -0.0489 147 PRO   A C   
959  O  O   . PRO   A 127 ? 2.6637 1.2110 1.7745 0.4002  0.2339  -0.0686 147 PRO   A O   
960  C  CB  . PRO   A 127 ? 2.6525 1.3325 1.8571 0.5182  0.3544  -0.0293 147 PRO   A CB  
961  C  CG  . PRO   A 127 ? 2.5699 1.3623 1.8843 0.5457  0.3922  0.0050  147 PRO   A CG  
962  C  CD  . PRO   A 127 ? 2.4436 1.3177 1.8317 0.5165  0.3799  0.0226  147 PRO   A CD  
963  N  N   . ILE   A 128 ? 2.5176 1.2328 1.7017 0.4024  0.2664  -0.0489 148 ILE   A N   
964  C  CA  . ILE   A 128 ? 2.4868 1.1739 1.6148 0.3555  0.2217  -0.0715 148 ILE   A CA  
965  C  C   . ILE   A 128 ? 2.4273 1.1847 1.6337 0.2960  0.1789  -0.0552 148 ILE   A C   
966  O  O   . ILE   A 128 ? 2.4490 1.1585 1.6218 0.2539  0.1345  -0.0699 148 ILE   A O   
967  C  CB  . ILE   A 128 ? 2.3993 1.1203 1.4935 0.3650  0.2383  -0.0793 148 ILE   A CB  
968  C  CG1 . ILE   A 128 ? 2.4360 1.0684 1.4298 0.4233  0.2793  -0.0986 148 ILE   A CG1 
969  C  CG2 . ILE   A 128 ? 2.3447 1.0572 1.3997 0.3138  0.1873  -0.0978 148 ILE   A CG2 
970  C  CD1 . ILE   A 128 ? 2.3607 1.0089 1.3018 0.4341  0.2951  -0.1069 148 ILE   A CD1 
971  N  N   . ILE   A 129 ? 2.3146 1.1848 1.6260 0.2920  0.1915  -0.0243 149 ILE   A N   
972  C  CA  . ILE   A 129 ? 2.2719 1.2120 1.6545 0.2408  0.1564  -0.0073 149 ILE   A CA  
973  C  C   . ILE   A 129 ? 2.3084 1.1896 1.6921 0.2245  0.1335  -0.0024 149 ILE   A C   
974  O  O   . ILE   A 129 ? 2.2750 1.1618 1.6725 0.1758  0.0959  0.0001  149 ILE   A O   
975  C  CB  . ILE   A 129 ? 2.1261 1.1906 1.6108 0.2460  0.1759  0.0223  149 ILE   A CB  
976  C  CG1 . ILE   A 129 ? 2.1070 1.2228 1.5915 0.2632  0.2014  0.0198  149 ILE   A CG1 
977  C  CG2 . ILE   A 129 ? 2.0269 1.1619 1.5737 0.1965  0.1420  0.0378  149 ILE   A CG2 
978  C  CD1 . ILE   A 129 ? 2.0225 1.2477 1.6050 0.2745  0.2243  0.0475  149 ILE   A CD1 
979  N  N   . ALA   A 130 ? 2.3460 1.1691 1.7164 0.2660  0.1574  0.0009  150 ALA   A N   
980  C  CA  . ALA   A 130 ? 2.3973 1.1655 1.7739 0.2550  0.1391  0.0106  150 ALA   A CA  
981  C  C   . ALA   A 130 ? 2.5164 1.1803 1.8182 0.2189  0.1005  -0.0137 150 ALA   A C   
982  O  O   . ALA   A 130 ? 2.5429 1.1909 1.8662 0.1814  0.0714  -0.0020 150 ALA   A O   
983  C  CB  . ALA   A 130 ? 2.3784 1.0977 1.7488 0.3132  0.1738  0.0170  150 ALA   A CB  
984  N  N   . GLN   A 131 ? 2.5998 1.1903 1.8123 0.2291  0.0989  -0.0469 151 GLN   A N   
985  C  CA  . GLN   A 131 ? 2.6134 1.0997 1.7515 0.1938  0.0570  -0.0735 151 GLN   A CA  
986  C  C   . GLN   A 131 ? 2.6216 1.1720 1.8066 0.1271  0.0144  -0.0654 151 GLN   A C   
987  O  O   . GLN   A 131 ? 2.7283 1.2275 1.9085 0.0853  -0.0219 -0.0663 151 GLN   A O   
988  C  CB  . GLN   A 131 ? 2.6669 1.0702 1.6960 0.2198  0.0619  -0.1113 151 GLN   A CB  
989  C  CG  . GLN   A 131 ? 2.7502 1.1058 1.7345 0.2919  0.1135  -0.1177 151 GLN   A CG  
990  C  CD  . GLN   A 131 ? 2.9307 1.1766 1.7969 0.3115  0.1084  -0.1555 151 GLN   A CD  
991  O  OE1 . GLN   A 131 ? 2.9557 1.1405 1.7934 0.3320  0.1135  -0.1619 151 GLN   A OE1 
992  N  NE2 . GLN   A 131 ? 2.9678 1.2053 1.7716 0.3035  0.0964  -0.1780 151 GLN   A NE2 
993  N  N   . TYR   A 132 ? 2.4779 1.1409 1.7120 0.1167  0.0195  -0.0560 152 TYR   A N   
994  C  CA  . TYR   A 132 ? 2.4456 1.1777 1.7295 0.0585  -0.0165 -0.0466 152 TYR   A CA  
995  C  C   . TYR   A 132 ? 2.4478 1.2360 1.8154 0.0333  -0.0211 -0.0125 152 TYR   A C   
996  O  O   . TYR   A 132 ? 2.4183 1.2382 1.8211 -0.0174 -0.0522 -0.0031 152 TYR   A O   
997  C  CB  . TYR   A 132 ? 2.3069 1.1400 1.6186 0.0595  -0.0074 -0.0450 152 TYR   A CB  
998  C  CG  . TYR   A 132 ? 2.3559 1.1358 1.5803 0.0770  -0.0091 -0.0766 152 TYR   A CG  
999  C  CD1 . TYR   A 132 ? 2.4553 1.2023 1.6372 0.0391  -0.0531 -0.0975 152 TYR   A CD1 
1000 C  CD2 . TYR   A 132 ? 2.3799 1.1427 1.5639 0.1320  0.0329  -0.0839 152 TYR   A CD2 
1001 C  CE1 . TYR   A 132 ? 2.5771 1.2713 1.6703 0.0566  -0.0580 -0.1265 152 TYR   A CE1 
1002 C  CE2 . TYR   A 132 ? 2.4180 1.1280 1.5127 0.1506  0.0338  -0.1112 152 TYR   A CE2 
1003 C  CZ  . TYR   A 132 ? 2.5671 1.2403 1.6121 0.1133  -0.0133 -0.1333 152 TYR   A CZ  
1004 O  OH  . TYR   A 132 ? 2.7138 1.3309 1.6618 0.1332  -0.0157 -0.1606 152 TYR   A OH  
1005 N  N   . GLY   A 133 ? 2.6665 1.4716 2.0679 0.0690  0.0099  0.0078  153 GLY   A N   
1006 C  CA  . GLY   A 133 ? 2.5695 1.4129 2.0361 0.0495  0.0047  0.0401  153 GLY   A CA  
1007 C  C   . GLY   A 133 ? 2.7858 1.5377 2.2256 0.0151  -0.0252 0.0398  153 GLY   A C   
1008 O  O   . GLY   A 133 ? 2.7704 1.5599 2.2549 -0.0302 -0.0464 0.0598  153 GLY   A O   
1009 N  N   . ASP   A 134 ? 3.0412 1.6687 2.4065 0.0366  -0.0259 0.0176  154 ASP   A N   
1010 C  CA  . ASP   A 134 ? 3.0543 1.5792 2.3883 0.0035  -0.0563 0.0148  154 ASP   A CA  
1011 C  C   . ASP   A 134 ? 3.0267 1.5610 2.3633 -0.0587 -0.0980 0.0053  154 ASP   A C   
1012 O  O   . ASP   A 134 ? 3.0376 1.5614 2.4052 -0.1053 -0.1226 0.0232  154 ASP   A O   
1013 C  CB  . ASP   A 134 ? 3.1231 1.5062 2.3641 0.0409  -0.0509 -0.0150 154 ASP   A CB  
1014 C  CG  . ASP   A 134 ? 3.2297 1.4986 2.4119 -0.0014 -0.0940 -0.0378 154 ASP   A CG  
1015 O  OD1 . ASP   A 134 ? 3.2133 1.4310 2.4108 -0.0301 -0.1119 -0.0208 154 ASP   A OD1 
1016 O  OD2 . ASP   A 134 ? 3.2613 1.4919 2.3826 -0.0084 -0.1126 -0.0719 154 ASP   A OD2 
1017 N  N   . VAL   A 135 ? 2.7694 1.3250 2.0759 -0.0597 -0.1061 -0.0208 155 VAL   A N   
1018 C  CA  . VAL   A 135 ? 2.7265 1.3020 2.0412 -0.1157 -0.1477 -0.0298 155 VAL   A CA  
1019 C  C   . VAL   A 135 ? 2.6351 1.3283 2.0483 -0.1557 -0.1521 0.0065  155 VAL   A C   
1020 O  O   . VAL   A 135 ? 2.6215 1.3193 2.0636 -0.2099 -0.1854 0.0140  155 VAL   A O   
1021 C  CB  . VAL   A 135 ? 2.7163 1.3135 1.9880 -0.1013 -0.1503 -0.0585 155 VAL   A CB  
1022 C  CG1 . VAL   A 135 ? 2.7286 1.3314 2.0008 -0.1571 -0.2000 -0.0712 155 VAL   A CG1 
1023 C  CG2 . VAL   A 135 ? 2.8113 1.3001 1.9820 -0.0504 -0.1340 -0.0908 155 VAL   A CG2 
1024 N  N   . LEU   A 136 ? 2.5441 1.3341 2.0106 -0.1290 -0.1184 0.0297  156 LEU   A N   
1025 C  CA  . LEU   A 136 ? 2.4627 1.3593 2.0137 -0.1593 -0.1179 0.0642  156 LEU   A CA  
1026 C  C   . LEU   A 136 ? 2.5692 1.4259 2.1426 -0.1816 -0.1230 0.0918  156 LEU   A C   
1027 O  O   . LEU   A 136 ? 2.5226 1.4117 2.1401 -0.2302 -0.1420 0.1114  156 LEU   A O   
1028 C  CB  . LEU   A 136 ? 2.2765 1.2733 1.8690 -0.1224 -0.0834 0.0787  156 LEU   A CB  
1029 C  CG  . LEU   A 136 ? 2.0843 1.2047 1.7490 -0.1485 -0.0843 0.1014  156 LEU   A CG  
1030 C  CD1 . LEU   A 136 ? 2.0602 1.2074 1.7245 -0.1823 -0.1108 0.0848  156 LEU   A CD1 
1031 C  CD2 . LEU   A 136 ? 1.9469 1.1508 1.6427 -0.1102 -0.0540 0.1100  156 LEU   A CD2 
1032 N  N   . VAL   A 137 ? 2.5547 1.3395 2.0989 -0.1456 -0.1053 0.0956  157 VAL   A N   
1033 C  CA  . VAL   A 137 ? 2.5900 1.3328 2.1520 -0.1630 -0.1087 0.1250  157 VAL   A CA  
1034 C  C   . VAL   A 137 ? 2.6592 1.3087 2.1952 -0.2119 -0.1447 0.1162  157 VAL   A C   
1035 O  O   . VAL   A 137 ? 2.6989 1.3387 2.2679 -0.2485 -0.1545 0.1454  157 VAL   A O   
1036 C  CB  . VAL   A 137 ? 2.6208 1.3058 2.1575 -0.1090 -0.0828 0.1312  157 VAL   A CB  
1037 C  CG1 . VAL   A 137 ? 2.5414 1.3012 2.0920 -0.0571 -0.0514 0.1271  157 VAL   A CG1 
1038 C  CG2 . VAL   A 137 ? 2.8066 1.3435 2.2654 -0.0955 -0.0929 0.1040  157 VAL   A CG2 
1039 N  N   . ARG   A 138 ? 2.7292 1.3080 2.2054 -0.2147 -0.1660 0.0769  158 ARG   A N   
1040 C  CA  . ARG   A 138 ? 2.7619 1.2551 2.2157 -0.2661 -0.2077 0.0649  158 ARG   A CA  
1041 C  C   . ARG   A 138 ? 2.6671 1.2558 2.1925 -0.3257 -0.2308 0.0824  158 ARG   A C   
1042 O  O   . ARG   A 138 ? 2.6805 1.2583 2.2462 -0.3738 -0.2478 0.1075  158 ARG   A O   
1043 C  CB  . ARG   A 138 ? 2.8607 1.2537 2.2234 -0.2497 -0.2267 0.0156  158 ARG   A CB  
1044 C  CG  . ARG   A 138 ? 2.8816 1.2354 2.2315 -0.3076 -0.2787 -0.0050 158 ARG   A CG  
1045 C  CD  . ARG   A 138 ? 2.8806 1.1920 2.2576 -0.3466 -0.2993 0.0078  158 ARG   A CD  
1046 N  NE  . ARG   A 138 ? 2.8418 1.2078 2.2756 -0.4110 -0.3374 0.0136  158 ARG   A NE  
1047 C  CZ  . ARG   A 138 ? 2.9403 1.2800 2.4035 -0.4528 -0.3614 0.0210  158 ARG   A CZ  
1048 N  NH1 . ARG   A 138 ? 2.9854 1.2364 2.4206 -0.4398 -0.3542 0.0214  158 ARG   A NH1 
1049 N  NH2 . ARG   A 138 ? 2.9274 1.3335 2.4531 -0.5080 -0.3925 0.0292  158 ARG   A NH2 
1050 N  N   . ASN   A 139 ? 2.6436 1.3284 2.1887 -0.3220 -0.2296 0.0715  159 ASN   A N   
1051 C  CA  . ASN   A 139 ? 2.5686 1.3593 2.1885 -0.3701 -0.2456 0.0902  159 ASN   A CA  
1052 C  C   . ASN   A 139 ? 2.4711 1.3541 2.1665 -0.3776 -0.2189 0.1366  159 ASN   A C   
1053 O  O   . ASN   A 139 ? 2.4347 1.3890 2.1954 -0.4224 -0.2297 0.1601  159 ASN   A O   
1054 C  CB  . ASN   A 139 ? 2.5032 1.3715 2.1212 -0.3551 -0.2467 0.0684  159 ASN   A CB  
1055 C  CG  . ASN   A 139 ? 2.6297 1.4112 2.1705 -0.3541 -0.2788 0.0241  159 ASN   A CG  
1056 O  OD1 . ASN   A 139 ? 2.6709 1.4661 2.2247 -0.3948 -0.3173 0.0137  159 ASN   A OD1 
1057 N  ND2 . ASN   A 139 ? 2.6766 1.3687 2.1357 -0.3059 -0.2634 -0.0016 159 ASN   A ND2 
1058 N  N   . LEU   A 140 ? 2.5107 1.3947 2.1980 -0.3335 -0.1844 0.1510  160 LEU   A N   
1059 C  CA  . LEU   A 140 ? 2.4492 1.4049 2.1942 -0.3386 -0.1620 0.1946  160 LEU   A CA  
1060 C  C   . LEU   A 140 ? 2.5369 1.4170 2.2861 -0.3686 -0.1698 0.2216  160 LEU   A C   
1061 O  O   . LEU   A 140 ? 2.4880 1.4244 2.2913 -0.3981 -0.1631 0.2598  160 LEU   A O   
1062 C  CB  . LEU   A 140 ? 2.3772 1.3677 2.1150 -0.2808 -0.1272 0.2005  160 LEU   A CB  
1063 C  CG  . LEU   A 140 ? 2.1754 1.2964 1.9578 -0.2658 -0.1081 0.2092  160 LEU   A CG  
1064 C  CD1 . LEU   A 140 ? 2.1113 1.3056 1.9329 -0.3066 -0.1253 0.2067  160 LEU   A CD1 
1065 C  CD2 . LEU   A 140 ? 2.1030 1.2313 1.8556 -0.2136 -0.0912 0.1837  160 LEU   A CD2 
1066 N  N   . ARG   A 141 ? 2.5215 1.2705 2.2111 -0.3600 -0.1822 0.2033  161 ARG   A N   
1067 C  CA  . ARG   A 141 ? 2.6060 1.2705 2.2933 -0.3817 -0.1870 0.2299  161 ARG   A CA  
1068 C  C   . ARG   A 141 ? 2.7093 1.3997 2.4500 -0.4454 -0.2093 0.2441  161 ARG   A C   
1069 O  O   . ARG   A 141 ? 2.8353 1.5057 2.5990 -0.4614 -0.2029 0.2700  161 ARG   A O   
1070 C  CB  . ARG   A 141 ? 2.6887 1.2185 2.3022 -0.3508 -0.1929 0.1995  161 ARG   A CB  
1071 C  CG  . ARG   A 141 ? 2.7127 1.1870 2.3293 -0.3443 -0.1814 0.2237  161 ARG   A CG  
1072 C  CD  . ARG   A 141 ? 2.6025 1.1090 2.2273 -0.3012 -0.1486 0.2558  161 ARG   A CD  
1073 N  NE  . ARG   A 141 ? 2.6148 1.0759 2.1859 -0.2390 -0.1339 0.2313  161 ARG   A NE  
1074 C  CZ  . ARG   A 141 ? 2.5687 1.0636 2.1450 -0.1921 -0.1074 0.2504  161 ARG   A CZ  
1075 N  NH1 . ARG   A 141 ? 2.5310 1.1046 2.1560 -0.1984 -0.0945 0.2921  161 ARG   A NH1 
1076 N  NH2 . ARG   A 141 ? 2.5945 1.0596 2.1331 -0.1343 -0.0913 0.2257  161 ARG   A NH2 
1077 N  N   . ARG   A 142 ? 2.7027 1.4454 2.4678 -0.4781 -0.2329 0.2276  162 ARG   A N   
1078 C  CA  . ARG   A 142 ? 2.7698 1.5614 2.5989 -0.5345 -0.2526 0.2400  162 ARG   A CA  
1079 C  C   . ARG   A 142 ? 2.8358 1.7015 2.7307 -0.5507 -0.2246 0.2913  162 ARG   A C   
1080 O  O   . ARG   A 142 ? 2.7733 1.7114 2.6861 -0.5302 -0.1968 0.3163  162 ARG   A O   
1081 C  CB  . ARG   A 142 ? 2.6634 1.5363 2.5226 -0.5569 -0.2736 0.2242  162 ARG   A CB  
1082 C  CG  . ARG   A 142 ? 2.6669 1.4750 2.4572 -0.5416 -0.3022 0.1733  162 ARG   A CG  
1083 C  CD  . ARG   A 142 ? 2.6160 1.5215 2.4477 -0.5643 -0.3205 0.1664  162 ARG   A CD  
1084 N  NE  . ARG   A 142 ? 2.5185 1.5549 2.4034 -0.5425 -0.2817 0.1939  162 ARG   A NE  
1085 C  CZ  . ARG   A 142 ? 2.4671 1.6228 2.4218 -0.5648 -0.2828 0.2086  162 ARG   A CZ  
1086 N  NH1 . ARG   A 142 ? 2.4507 1.6229 2.4403 -0.6110 -0.3215 0.2010  162 ARG   A NH1 
1087 N  NH2 . ARG   A 142 ? 2.4392 1.6989 2.4300 -0.5394 -0.2455 0.2314  162 ARG   A NH2 
1088 N  N   . GLU   A 143 ? 3.0208 1.8651 2.9473 -0.5861 -0.2314 0.3069  163 GLU   A N   
1089 C  CA  . GLU   A 143 ? 3.0600 1.9615 3.0383 -0.5983 -0.2012 0.3558  163 GLU   A CA  
1090 C  C   . GLU   A 143 ? 3.0005 2.0384 3.0537 -0.6247 -0.1934 0.3767  163 GLU   A C   
1091 O  O   . GLU   A 143 ? 2.9799 2.0898 3.0369 -0.6044 -0.1834 0.3749  163 GLU   A O   
1092 C  CB  . GLU   A 143 ? 3.0802 1.9108 3.0678 -0.6275 -0.2080 0.3673  163 GLU   A CB  
1093 C  CG  . GLU   A 143 ? 3.1073 1.7977 3.0223 -0.6060 -0.2240 0.3372  163 GLU   A CG  
1094 C  CD  . GLU   A 143 ? 3.1206 1.7676 2.9761 -0.5462 -0.2011 0.3353  163 GLU   A CD  
1095 O  OE1 . GLU   A 143 ? 3.1666 1.8621 3.0375 -0.5268 -0.1693 0.3718  163 GLU   A OE1 
1096 O  OE2 . GLU   A 143 ? 3.0845 1.6502 2.8764 -0.5163 -0.2147 0.2968  163 GLU   A OE2 
1097 N  N   . ALA   A 144 ? 3.0819 2.1561 3.1962 -0.6681 -0.1965 0.3968  164 ALA   A N   
1098 C  CA  . ALA   A 144 ? 2.9929 2.1994 3.1837 -0.6897 -0.1829 0.4211  164 ALA   A CA  
1099 C  C   . ALA   A 144 ? 3.2592 2.5390 3.4516 -0.6568 -0.1405 0.4519  164 ALA   A C   
1100 O  O   . ALA   A 144 ? 3.0217 2.4102 3.2548 -0.6549 -0.1280 0.4604  164 ALA   A O   
1101 C  CB  . ALA   A 144 ? 2.6963 1.9574 2.9097 -0.7023 -0.2133 0.3906  164 ALA   A CB  
1102 N  N   . GLU   A 145 ? 3.8691 3.0874 4.0144 -0.6279 -0.1194 0.4678  165 GLU   A N   
1103 C  CA  . GLU   A 145 ? 3.8621 3.1288 3.9902 -0.5892 -0.0853 0.4915  165 GLU   A CA  
1104 C  C   . GLU   A 145 ? 3.8680 3.1965 4.0316 -0.5985 -0.0506 0.5368  165 GLU   A C   
1105 O  O   . GLU   A 145 ? 3.9028 3.2414 4.0372 -0.5662 -0.0232 0.5603  165 GLU   A O   
1106 C  CB  . GLU   A 145 ? 3.8985 3.0674 3.9547 -0.5480 -0.0833 0.4843  165 GLU   A CB  
1107 C  CG  . GLU   A 145 ? 4.0454 3.1321 4.0801 -0.5476 -0.0721 0.5078  165 GLU   A CG  
1108 C  CD  . GLU   A 145 ? 3.9881 3.0305 4.0524 -0.5949 -0.0891 0.5064  165 GLU   A CD  
1109 O  OE1 . GLU   A 145 ? 3.9944 2.9897 4.0529 -0.6119 -0.1226 0.4701  165 GLU   A OE1 
1110 O  OE2 . GLU   A 145 ? 3.9987 3.0527 4.0900 -0.6149 -0.0693 0.5417  165 GLU   A OE2 
1111 N  N   . PRO   A 149 ? 2.1354 1.9439 2.4457 -0.5647 -0.0333 0.4982  169 PRO   A N   
1112 C  CA  . PRO   A 149 ? 2.0923 1.8721 2.3487 -0.5302 -0.0375 0.4793  169 PRO   A CA  
1113 C  C   . PRO   A 149 ? 2.0884 1.8156 2.3229 -0.5323 -0.0743 0.4348  169 PRO   A C   
1114 O  O   . PRO   A 149 ? 2.0601 1.7467 2.3141 -0.5717 -0.1043 0.4261  169 PRO   A O   
1115 C  CB  . PRO   A 149 ? 2.0152 1.9058 2.2919 -0.5055 -0.0127 0.4857  169 PRO   A CB  
1116 C  CG  . PRO   A 149 ? 2.0030 1.9713 2.3499 -0.5343 -0.0161 0.4880  169 PRO   A CG  
1117 C  CD  . PRO   A 149 ? 2.0784 2.0016 2.4497 -0.5710 -0.0242 0.5018  169 PRO   A CD  
1118 N  N   . VAL   A 150 ? 1.8713 1.5996 2.0613 -0.4853 -0.0714 0.4029  170 VAL   A N   
1119 C  CA  . VAL   A 150 ? 1.8377 1.5231 1.9952 -0.4738 -0.0984 0.3574  170 VAL   A CA  
1120 C  C   . VAL   A 150 ? 1.6996 1.4583 1.8516 -0.4342 -0.0864 0.3368  170 VAL   A C   
1121 O  O   . VAL   A 150 ? 1.6994 1.4824 1.8332 -0.3979 -0.0616 0.3437  170 VAL   A O   
1122 C  CB  . VAL   A 150 ? 1.8528 1.4202 1.9442 -0.4533 -0.1064 0.3396  170 VAL   A CB  
1123 C  CG1 . VAL   A 150 ? 1.8735 1.4164 1.9202 -0.4195 -0.1175 0.2950  170 VAL   A CG1 
1124 C  CG2 . VAL   A 150 ? 2.0038 1.4819 2.0949 -0.4970 -0.1312 0.3456  170 VAL   A CG2 
1125 N  N   . THR   A 151 ? 1.5963 1.3882 1.7641 -0.4419 -0.1061 0.3125  171 THR   A N   
1126 C  CA  . THR   A 151 ? 1.4951 1.3541 1.6606 -0.4077 -0.0965 0.2939  171 THR   A CA  
1127 C  C   . THR   A 151 ? 1.4844 1.2826 1.5868 -0.3667 -0.0958 0.2635  171 THR   A C   
1128 O  O   . THR   A 151 ? 1.5741 1.3106 1.6427 -0.3678 -0.1181 0.2356  171 THR   A O   
1129 C  CB  . THR   A 151 ? 1.4948 1.4048 1.6969 -0.4287 -0.1194 0.2805  171 THR   A CB  
1130 O  OG1 . THR   A 151 ? 1.5898 1.4302 1.7469 -0.4257 -0.1483 0.2446  171 THR   A OG1 
1131 C  CG2 . THR   A 151 ? 1.4828 1.4215 1.7486 -0.4800 -0.1309 0.3081  171 THR   A CG2 
1132 N  N   . LEU   A 152 ? 1.5245 1.3419 1.6115 -0.3298 -0.0704 0.2694  172 LEU   A N   
1133 C  CA  . LEU   A 152 ? 1.5124 1.2739 1.5496 -0.2914 -0.0657 0.2482  172 LEU   A CA  
1134 C  C   . LEU   A 152 ? 1.5177 1.2839 1.5359 -0.2731 -0.0744 0.2147  172 LEU   A C   
1135 O  O   . LEU   A 152 ? 1.5555 1.2577 1.5297 -0.2503 -0.0758 0.1937  172 LEU   A O   
1136 C  CB  . LEU   A 152 ? 1.4701 1.2644 1.5057 -0.2588 -0.0409 0.2633  172 LEU   A CB  
1137 C  CG  . LEU   A 152 ? 1.4464 1.1922 1.4669 -0.2550 -0.0322 0.2875  172 LEU   A CG  
1138 C  CD1 . LEU   A 152 ? 1.5240 1.1713 1.5032 -0.2422 -0.0407 0.2716  172 LEU   A CD1 
1139 C  CD2 . LEU   A 152 ? 1.5437 1.2961 1.5910 -0.2942 -0.0323 0.3191  172 LEU   A CD2 
1140 N  N   . LYS   A 153 ? 1.4522 1.2918 1.5009 -0.2800 -0.0781 0.2109  173 LYS   A N   
1141 C  CA  . LYS   A 153 ? 1.4491 1.2966 1.4776 -0.2587 -0.0834 0.1830  173 LYS   A CA  
1142 C  C   . LYS   A 153 ? 1.5225 1.2980 1.5137 -0.2716 -0.1099 0.1590  173 LYS   A C   
1143 O  O   . LYS   A 153 ? 1.5464 1.2749 1.4902 -0.2447 -0.1082 0.1360  173 LYS   A O   
1144 C  CB  . LYS   A 153 ? 1.3506 1.2911 1.4205 -0.2619 -0.0821 0.1867  173 LYS   A CB  
1145 C  CG  . LYS   A 153 ? 1.3008 1.2725 1.3583 -0.2254 -0.0693 0.1711  173 LYS   A CG  
1146 C  CD  . LYS   A 153 ? 1.3212 1.2323 1.3298 -0.2088 -0.0783 0.1437  173 LYS   A CD  
1147 C  CE  . LYS   A 153 ? 1.3229 1.2757 1.3302 -0.1876 -0.0750 0.1302  173 LYS   A CE  
1148 N  NZ  . LYS   A 153 ? 1.2791 1.2535 1.2874 -0.1547 -0.0499 0.1319  173 LYS   A NZ  
1149 N  N   . ASP   A 154 ? 1.5035 1.2685 1.5146 -0.3125 -0.1348 0.1644  174 ASP   A N   
1150 C  CA  . ASP   A 154 ? 1.6139 1.3097 1.5864 -0.3275 -0.1669 0.1390  174 ASP   A CA  
1151 C  C   . ASP   A 154 ? 1.6580 1.2440 1.5656 -0.3105 -0.1652 0.1239  174 ASP   A C   
1152 O  O   . ASP   A 154 ? 1.7308 1.2587 1.5803 -0.2921 -0.1745 0.0953  174 ASP   A O   
1153 C  CB  . ASP   A 154 ? 1.6937 1.4003 1.7096 -0.3792 -0.1970 0.1507  174 ASP   A CB  
1154 C  CG  . ASP   A 154 ? 1.7470 1.5327 1.8032 -0.3923 -0.2153 0.1476  174 ASP   A CG  
1155 O  OD1 . ASP   A 154 ? 1.6978 1.5303 1.7472 -0.3607 -0.2019 0.1385  174 ASP   A OD1 
1156 O  OD2 . ASP   A 154 ? 1.7930 1.5937 1.8905 -0.4344 -0.2441 0.1554  174 ASP   A OD2 
1157 N  N   . VAL   A 155 ? 1.6794 1.2337 1.5927 -0.3137 -0.1519 0.1436  175 VAL   A N   
1158 C  CA  . VAL   A 155 ? 1.7113 1.1608 1.5662 -0.2939 -0.1482 0.1314  175 VAL   A CA  
1159 C  C   . VAL   A 155 ? 1.7031 1.1505 1.5238 -0.2416 -0.1221 0.1169  175 VAL   A C   
1160 O  O   . VAL   A 155 ? 1.7215 1.0925 1.4825 -0.2188 -0.1232 0.0925  175 VAL   A O   
1161 C  CB  . VAL   A 155 ? 1.7391 1.1607 1.6117 -0.3065 -0.1388 0.1601  175 VAL   A CB  
1162 C  CG1 . VAL   A 155 ? 1.6600 1.1809 1.5975 -0.3198 -0.1233 0.1937  175 VAL   A CG1 
1163 C  CG2 . VAL   A 155 ? 1.7612 1.1254 1.5938 -0.2634 -0.1160 0.1578  175 VAL   A CG2 
1164 N  N   . PHE   A 156 ? 1.6008 1.1312 1.4585 -0.2217 -0.0981 0.1319  176 PHE   A N   
1165 C  CA  . PHE   A 156 ? 1.5953 1.1336 1.4332 -0.1763 -0.0746 0.1208  176 PHE   A CA  
1166 C  C   . PHE   A 156 ? 1.5685 1.1132 1.3796 -0.1663 -0.0812 0.0955  176 PHE   A C   
1167 O  O   . PHE   A 156 ? 1.5775 1.0831 1.3469 -0.1328 -0.0676 0.0789  176 PHE   A O   
1168 C  CB  . PHE   A 156 ? 1.5176 1.1404 1.4026 -0.1621 -0.0533 0.1421  176 PHE   A CB  
1169 C  CG  . PHE   A 156 ? 1.4985 1.1055 1.3945 -0.1567 -0.0422 0.1653  176 PHE   A CG  
1170 C  CD1 . PHE   A 156 ? 1.5298 1.0489 1.3907 -0.1460 -0.0416 0.1629  176 PHE   A CD1 
1171 C  CD2 . PHE   A 156 ? 1.4228 1.0986 1.3587 -0.1597 -0.0327 0.1895  176 PHE   A CD2 
1172 C  CE1 . PHE   A 156 ? 1.4843 0.9871 1.3541 -0.1389 -0.0329 0.1862  176 PHE   A CE1 
1173 C  CE2 . PHE   A 156 ? 1.4169 1.0758 1.3564 -0.1529 -0.0245 0.2121  176 PHE   A CE2 
1174 C  CZ  . PHE   A 156 ? 1.4645 1.0381 1.3730 -0.1429 -0.0252 0.2115  176 PHE   A CZ  
1175 N  N   . GLY   A 157 ? 1.6606 1.2555 1.4958 -0.1932 -0.1008 0.0944  177 GLY   A N   
1176 C  CA  . GLY   A 157 ? 1.7138 1.3124 1.5201 -0.1841 -0.1106 0.0723  177 GLY   A CA  
1177 C  C   . GLY   A 157 ? 1.7882 1.2875 1.5234 -0.1840 -0.1301 0.0463  177 GLY   A C   
1178 O  O   . GLY   A 157 ? 1.8645 1.3356 1.5492 -0.1567 -0.1242 0.0266  177 GLY   A O   
1179 N  N   . ALA   A 158 ? 1.8214 1.2622 1.5480 -0.2143 -0.1533 0.0462  178 ALA   A N   
1180 C  CA  . ALA   A 158 ? 1.8704 1.2015 1.5209 -0.2131 -0.1733 0.0193  178 ALA   A CA  
1181 C  C   . ALA   A 158 ? 1.8866 1.1533 1.4814 -0.1652 -0.1419 0.0083  178 ALA   A C   
1182 O  O   . ALA   A 158 ? 1.9183 1.1232 1.4415 -0.1417 -0.1428 -0.0173 178 ALA   A O   
1183 C  CB  . ALA   A 158 ? 1.9725 1.2490 1.6310 -0.2549 -0.2014 0.0247  178 ALA   A CB  
1184 N  N   . TYR   A 159 ? 1.8438 1.1265 1.4708 -0.1483 -0.1133 0.0288  179 TYR   A N   
1185 C  CA  . TYR   A 159 ? 1.8397 1.0726 1.4286 -0.1015 -0.0818 0.0228  179 TYR   A CA  
1186 C  C   . TYR   A 159 ? 1.8151 1.0960 1.3996 -0.0654 -0.0557 0.0171  179 TYR   A C   
1187 O  O   . TYR   A 159 ? 1.8904 1.1143 1.4138 -0.0328 -0.0415 -0.0018 179 TYR   A O   
1188 C  CB  . TYR   A 159 ? 1.7983 1.0456 1.4312 -0.0945 -0.0629 0.0492  179 TYR   A CB  
1189 C  CG  . TYR   A 159 ? 1.7891 1.0254 1.4134 -0.0442 -0.0270 0.0514  179 TYR   A CG  
1190 C  CD1 . TYR   A 159 ? 1.9039 1.0423 1.4742 -0.0172 -0.0174 0.0397  179 TYR   A CD1 
1191 C  CD2 . TYR   A 159 ? 1.7494 1.0736 1.4233 -0.0235 -0.0033 0.0659  179 TYR   A CD2 
1192 C  CE1 . TYR   A 159 ? 1.8963 1.0324 1.4683 0.0304  0.0171  0.0445  179 TYR   A CE1 
1193 C  CE2 . TYR   A 159 ? 1.7459 1.0674 1.4236 0.0198  0.0275  0.0703  179 TYR   A CE2 
1194 C  CZ  . TYR   A 159 ? 1.7766 1.0079 1.4066 0.0473  0.0387  0.0608  179 TYR   A CZ  
1195 O  OH  . TYR   A 159 ? 1.7845 1.0205 1.4272 0.0923  0.0710  0.0678  179 TYR   A OH  
1196 N  N   . SER   A 160 ? 1.7852 1.1678 1.4320 -0.0703 -0.0476 0.0340  180 SER   A N   
1197 C  CA  . SER   A 160 ? 1.7822 1.2121 1.4346 -0.0380 -0.0213 0.0330  180 SER   A CA  
1198 C  C   . SER   A 160 ? 1.8158 1.2206 1.4115 -0.0317 -0.0301 0.0106  180 SER   A C   
1199 O  O   . SER   A 160 ? 1.7487 1.1502 1.3194 0.0027  -0.0041 0.0052  180 SER   A O   
1200 C  CB  . SER   A 160 ? 1.6519 1.1873 1.3782 -0.0482 -0.0165 0.0536  180 SER   A CB  
1201 O  OG  . SER   A 160 ? 1.5836 1.1397 1.3533 -0.0498 -0.0082 0.0745  180 SER   A OG  
1202 N  N   . MET   A 161 ? 1.7478 1.1366 1.3244 -0.0645 -0.0670 -0.0006 181 MET   A N   
1203 C  CA  . MET   A 161 ? 1.8103 1.1607 1.3199 -0.0577 -0.0814 -0.0237 181 MET   A CA  
1204 C  C   . MET   A 161 ? 1.8978 1.1351 1.3178 -0.0322 -0.0751 -0.0460 181 MET   A C   
1205 O  O   . MET   A 161 ? 1.9178 1.1226 1.2754 -0.0015 -0.0608 -0.0605 181 MET   A O   
1206 C  CB  . MET   A 161 ? 1.8675 1.2335 1.3868 -0.1009 -0.1277 -0.0290 181 MET   A CB  
1207 C  CG  . MET   A 161 ? 2.0677 1.3571 1.5006 -0.1016 -0.1575 -0.0575 181 MET   A CG  
1208 S  SD  . MET   A 161 ? 2.3378 1.6559 1.7987 -0.1557 -0.2175 -0.0608 181 MET   A SD  
1209 C  CE  . MET   A 161 ? 2.5145 1.6975 1.8593 -0.1573 -0.2550 -0.0979 181 MET   A CE  
1210 N  N   . ASP   A 162 ? 2.0662 1.2393 1.4755 -0.0423 -0.0833 -0.0481 182 ASP   A N   
1211 C  CA  . ASP   A 162 ? 2.1600 1.2166 1.4800 -0.0162 -0.0778 -0.0710 182 ASP   A CA  
1212 C  C   . ASP   A 162 ? 2.1359 1.1857 1.4410 0.0380  -0.0261 -0.0668 182 ASP   A C   
1213 O  O   . ASP   A 162 ? 2.2342 1.2011 1.4552 0.0713  -0.0121 -0.0873 182 ASP   A O   
1214 C  CB  . ASP   A 162 ? 2.2514 1.2409 1.5706 -0.0392 -0.0972 -0.0711 182 ASP   A CB  
1215 C  CG  . ASP   A 162 ? 2.3462 1.3238 1.6710 -0.0936 -0.1500 -0.0779 182 ASP   A CG  
1216 O  OD1 . ASP   A 162 ? 2.3566 1.3895 1.6953 -0.1131 -0.1720 -0.0805 182 ASP   A OD1 
1217 O  OD2 . ASP   A 162 ? 2.4844 1.3981 1.8041 -0.1171 -0.1698 -0.0789 182 ASP   A OD2 
1218 N  N   . VAL   A 163 ? 1.9971 1.1321 1.3820 0.0482  0.0023  -0.0406 183 VAL   A N   
1219 C  CA  . VAL   A 163 ? 1.9681 1.1039 1.3553 0.0967  0.0497  -0.0329 183 VAL   A CA  
1220 C  C   . VAL   A 163 ? 1.9342 1.1165 1.3156 0.1205  0.0745  -0.0321 183 VAL   A C   
1221 O  O   . VAL   A 163 ? 1.9538 1.1022 1.2954 0.1628  0.1104  -0.0364 183 VAL   A O   
1222 C  CB  . VAL   A 163 ? 1.8280 1.0238 1.3024 0.0974  0.0647  -0.0051 183 VAL   A CB  
1223 C  CG1 . VAL   A 163 ? 1.8631 1.0043 1.3363 0.0761  0.0427  -0.0031 183 VAL   A CG1 
1224 C  CG2 . VAL   A 163 ? 1.7687 1.0765 1.3226 0.0737  0.0584  0.0142  183 VAL   A CG2 
1225 N  N   . ILE   A 164 ? 1.8676 1.1257 1.2875 0.0958  0.0584  -0.0253 184 ILE   A N   
1226 C  CA  . ILE   A 164 ? 1.8414 1.1413 1.2581 0.1177  0.0822  -0.0217 184 ILE   A CA  
1227 C  C   . ILE   A 164 ? 1.9153 1.1479 1.2324 0.1269  0.0715  -0.0455 184 ILE   A C   
1228 O  O   . ILE   A 164 ? 1.9822 1.2083 1.2627 0.1596  0.1024  -0.0456 184 ILE   A O   
1229 C  CB  . ILE   A 164 ? 1.7130 1.1168 1.2091 0.0928  0.0718  -0.0043 184 ILE   A CB  
1230 C  CG1 . ILE   A 164 ? 1.6501 1.1147 1.1967 0.1196  0.1115  0.0144  184 ILE   A CG1 
1231 C  CG2 . ILE   A 164 ? 1.7044 1.1165 1.1688 0.0726  0.0415  -0.0155 184 ILE   A CG2 
1232 C  CD1 . ILE   A 164 ? 1.6343 1.0782 1.1285 0.1499  0.1380  0.0096  184 ILE   A CD1 
1233 N  N   . THR   A 165 ? 2.0113 1.1913 1.2816 0.0984  0.0275  -0.0648 185 THR   A N   
1234 C  CA  . THR   A 165 ? 2.1508 1.2524 1.3144 0.1084  0.0116  -0.0908 185 THR   A CA  
1235 C  C   . THR   A 165 ? 2.2603 1.2570 1.3362 0.1483  0.0376  -0.1079 185 THR   A C   
1236 O  O   . THR   A 165 ? 2.3903 1.3171 1.3648 0.1689  0.0359  -0.1289 185 THR   A O   
1237 C  CB  . THR   A 165 ? 2.1767 1.2546 1.3236 0.0630  -0.0488 -0.1065 185 THR   A CB  
1238 O  OG1 . THR   A 165 ? 2.2317 1.2870 1.4136 0.0381  -0.0645 -0.1044 185 THR   A OG1 
1239 C  CG2 . THR   A 165 ? 2.1161 1.2930 1.3304 0.0328  -0.0720 -0.0925 185 THR   A CG2 
1240 N  N   . SER   A 166 ? 2.2241 1.2067 1.3328 0.1623  0.0618  -0.0991 186 SER   A N   
1241 C  CA  . SER   A 166 ? 2.3701 1.2563 1.4044 0.2049  0.0912  -0.1131 186 SER   A CA  
1242 C  C   . SER   A 166 ? 2.3245 1.2460 1.3827 0.2541  0.1538  -0.0946 186 SER   A C   
1243 O  O   . SER   A 166 ? 2.3752 1.2304 1.3508 0.2974  0.1856  -0.1066 186 SER   A O   
1244 C  CB  . SER   A 166 ? 2.4197 1.2582 1.4722 0.1920  0.0770  -0.1148 186 SER   A CB  
1245 O  OG  . SER   A 166 ? 2.5276 1.3421 1.5740 0.1413  0.0200  -0.1270 186 SER   A OG  
1246 N  N   . THR   A 167 ? 2.1265 1.1509 1.2961 0.2486  0.1721  -0.0651 187 THR   A N   
1247 C  CA  . THR   A 167 ? 2.1241 1.1918 1.3314 0.2904  0.2283  -0.0447 187 THR   A CA  
1248 C  C   . THR   A 167 ? 2.1875 1.2772 1.3610 0.3059  0.2489  -0.0427 187 THR   A C   
1249 O  O   . THR   A 167 ? 2.2126 1.3033 1.3778 0.3479  0.2996  -0.0323 187 THR   A O   
1250 C  CB  . THR   A 167 ? 2.0394 1.2095 1.3737 0.2766  0.2345  -0.0153 187 THR   A CB  
1251 O  OG1 . THR   A 167 ? 2.1414 1.3537 1.5194 0.3153  0.2862  0.0051  187 THR   A OG1 
1252 C  CG2 . THR   A 167 ? 1.8580 1.1108 1.2470 0.2350  0.2043  -0.0067 187 THR   A CG2 
1253 N  N   . SER   A 168 ? 2.3208 1.4291 1.4770 0.2738  0.2119  -0.0503 188 SER   A N   
1254 C  CA  . SER   A 168 ? 2.3430 1.4711 1.4657 0.2860  0.2265  -0.0466 188 SER   A CA  
1255 C  C   . SER   A 168 ? 2.4649 1.4937 1.4509 0.3016  0.2147  -0.0743 188 SER   A C   
1256 O  O   . SER   A 168 ? 2.5591 1.5676 1.4867 0.3366  0.2505  -0.0715 188 SER   A O   
1257 C  CB  . SER   A 168 ? 2.2630 1.4777 1.4530 0.2461  0.1945  -0.0353 188 SER   A CB  
1258 O  OG  . SER   A 168 ? 2.0681 1.3701 1.3750 0.2332  0.2040  -0.0116 188 SER   A OG  
1259 N  N   . PHE   A 169 ? 2.4621 1.4269 1.3941 0.2756  0.1642  -0.1003 189 PHE   A N   
1260 C  CA  . PHE   A 169 ? 2.5833 1.4439 1.3785 0.2883  0.1443  -0.1308 189 PHE   A CA  
1261 C  C   . PHE   A 169 ? 2.7107 1.4627 1.4372 0.3025  0.1404  -0.1552 189 PHE   A C   
1262 O  O   . PHE   A 169 ? 2.7739 1.4535 1.4174 0.3508  0.1804  -0.1646 189 PHE   A O   
1263 C  CB  . PHE   A 169 ? 2.5539 1.4270 1.3365 0.2440  0.0805  -0.1428 189 PHE   A CB  
1264 C  CG  . PHE   A 169 ? 2.5502 1.5287 1.4050 0.2295  0.0812  -0.1190 189 PHE   A CG  
1265 C  CD1 . PHE   A 169 ? 2.3619 1.4342 1.3345 0.1905  0.0608  -0.1015 189 PHE   A CD1 
1266 C  CD2 . PHE   A 169 ? 2.6432 1.6221 1.4433 0.2567  0.1035  -0.1135 189 PHE   A CD2 
1267 C  CE1 . PHE   A 169 ? 2.3170 1.4789 1.3513 0.1799  0.0615  -0.0815 189 PHE   A CE1 
1268 C  CE2 . PHE   A 169 ? 2.5368 1.6056 1.4017 0.2442  0.1035  -0.0914 189 PHE   A CE2 
1269 C  CZ  . PHE   A 169 ? 2.3625 1.5215 1.3444 0.2063  0.0819  -0.0767 189 PHE   A CZ  
1270 N  N   . GLY   A 170 ? 2.6903 1.4262 1.4478 0.2633  0.0957  -0.1647 190 GLY   A N   
1271 C  CA  . GLY   A 170 ? 2.7216 1.3483 1.4160 0.2735  0.0882  -0.1876 190 GLY   A CA  
1272 C  C   . GLY   A 170 ? 2.8526 1.4132 1.4986 0.2290  0.0184  -0.2151 190 GLY   A C   
1273 O  O   . GLY   A 170 ? 2.9785 1.4525 1.5081 0.2363  -0.0064 -0.2444 190 GLY   A O   
1274 N  N   . VAL   A 171 ? 2.9483 1.5481 1.6823 0.1823  -0.0147 -0.2052 191 VAL   A N   
1275 C  CA  . VAL   A 171 ? 3.0528 1.6028 1.7632 0.1329  -0.0819 -0.2259 191 VAL   A CA  
1276 C  C   . VAL   A 171 ? 2.9979 1.5764 1.8040 0.0947  -0.0977 -0.2093 191 VAL   A C   
1277 O  O   . VAL   A 171 ? 2.9276 1.6161 1.8455 0.0802  -0.0826 -0.1782 191 VAL   A O   
1278 C  CB  . VAL   A 171 ? 3.0266 1.6377 1.7484 0.0995  -0.1237 -0.2263 191 VAL   A CB  
1279 C  CG1 . VAL   A 171 ? 2.8384 1.5915 1.6749 0.0938  -0.0982 -0.1910 191 VAL   A CG1 
1280 C  CG2 . VAL   A 171 ? 3.0469 1.6374 1.7851 0.0403  -0.1931 -0.2385 191 VAL   A CG2 
1281 N  N   . ASN   A 172 ? 3.2373 1.7116 1.9954 0.0792  -0.1281 -0.2299 192 ASN   A N   
1282 C  CA  . ASN   A 172 ? 3.2022 1.6938 2.0423 0.0347  -0.1524 -0.2145 192 ASN   A CA  
1283 C  C   . ASN   A 172 ? 3.1917 1.7204 2.0679 -0.0275 -0.2137 -0.2162 192 ASN   A C   
1284 O  O   . ASN   A 172 ? 3.2651 1.7359 2.0652 -0.0398 -0.2552 -0.2441 192 ASN   A O   
1285 C  CB  . ASN   A 172 ? 3.3135 1.6728 2.0905 0.0446  -0.1570 -0.2332 192 ASN   A CB  
1286 C  CG  . ASN   A 172 ? 3.3137 1.6821 2.1705 -0.0031 -0.1826 -0.2149 192 ASN   A CG  
1287 O  OD1 . ASN   A 172 ? 3.2164 1.6959 2.1828 -0.0230 -0.1714 -0.1809 192 ASN   A OD1 
1288 N  ND2 . ASN   A 172 ? 3.4328 1.6794 2.2305 -0.0213 -0.2171 -0.2371 192 ASN   A ND2 
1289 N  N   . ILE   A 173 ? 3.0429 1.6709 2.0361 -0.0653 -0.2194 -0.1854 193 ILE   A N   
1290 C  CA  . ILE   A 173 ? 3.0184 1.7051 2.0663 -0.1221 -0.2700 -0.1802 193 ILE   A CA  
1291 C  C   . ILE   A 173 ? 2.9847 1.7109 2.1296 -0.1654 -0.2801 -0.1533 193 ILE   A C   
1292 O  O   . ILE   A 173 ? 2.8536 1.6956 2.0958 -0.1789 -0.2651 -0.1226 193 ILE   A O   
1293 C  CB  . ILE   A 173 ? 2.9341 1.7388 2.0273 -0.1171 -0.2603 -0.1661 193 ILE   A CB  
1294 C  CG1 . ILE   A 173 ? 2.8005 1.6529 1.9079 -0.0658 -0.1970 -0.1502 193 ILE   A CG1 
1295 C  CG2 . ILE   A 173 ? 3.0213 1.7890 2.0326 -0.1163 -0.2961 -0.1937 193 ILE   A CG2 
1296 C  CD1 . ILE   A 173 ? 2.6825 1.6224 1.8080 -0.0521 -0.1846 -0.1420 193 ILE   A CD1 
1297 N  N   . ASP   A 174 ? 3.0286 1.6538 2.1428 -0.1863 -0.3046 -0.1645 194 ASP   A N   
1298 C  CA  . ASP   A 174 ? 2.9396 1.5880 2.1372 -0.2341 -0.3209 -0.1391 194 ASP   A CA  
1299 C  C   . ASP   A 174 ? 2.9239 1.6798 2.2083 -0.2851 -0.3534 -0.1215 194 ASP   A C   
1300 O  O   . ASP   A 174 ? 2.9676 1.6924 2.2438 -0.3278 -0.4063 -0.1355 194 ASP   A O   
1301 C  CB  . ASP   A 174 ? 2.9538 1.4634 2.0928 -0.2560 -0.3551 -0.1596 194 ASP   A CB  
1302 C  CG  . ASP   A 174 ? 2.9161 1.4447 2.1406 -0.3107 -0.3745 -0.1312 194 ASP   A CG  
1303 O  OD1 . ASP   A 174 ? 2.8591 1.4088 2.1291 -0.2991 -0.3388 -0.1032 194 ASP   A OD1 
1304 O  OD2 . ASP   A 174 ? 2.9327 1.4566 2.1806 -0.3655 -0.4258 -0.1351 194 ASP   A OD2 
1305 N  N   . SER   A 175 ? 2.8680 1.7503 2.2374 -0.2802 -0.3227 -0.0909 195 SER   A N   
1306 C  CA  . SER   A 175 ? 2.7949 1.7926 2.2492 -0.3171 -0.3427 -0.0720 195 SER   A CA  
1307 C  C   . SER   A 175 ? 2.7792 1.7988 2.3125 -0.3754 -0.3685 -0.0481 195 SER   A C   
1308 O  O   . SER   A 175 ? 2.7289 1.8586 2.3497 -0.4018 -0.3718 -0.0233 195 SER   A O   
1309 C  CB  . SER   A 175 ? 2.6278 1.7417 2.1382 -0.2878 -0.2979 -0.0487 195 SER   A CB  
1310 O  OG  . SER   A 175 ? 2.5850 1.6917 2.0358 -0.2393 -0.2742 -0.0659 195 SER   A OG  
1311 N  N   . LEU   A 176 ? 2.8687 1.7837 2.3716 -0.3947 -0.3856 -0.0546 196 LEU   A N   
1312 C  CA  . LEU   A 176 ? 2.8574 1.7778 2.4259 -0.4569 -0.4202 -0.0362 196 LEU   A CA  
1313 C  C   . LEU   A 176 ? 2.9335 1.8821 2.5196 -0.4969 -0.4745 -0.0494 196 LEU   A C   
1314 O  O   . LEU   A 176 ? 2.8836 1.8981 2.5598 -0.5478 -0.4969 -0.0250 196 LEU   A O   
1315 C  CB  . LEU   A 176 ? 2.8636 1.6471 2.3825 -0.4694 -0.4339 -0.0459 196 LEU   A CB  
1316 C  CG  . LEU   A 176 ? 2.8600 1.6064 2.4223 -0.5369 -0.4800 -0.0362 196 LEU   A CG  
1317 C  CD1 . LEU   A 176 ? 2.7542 1.6074 2.4341 -0.5704 -0.4604 0.0139  196 LEU   A CD1 
1318 C  CD2 . LEU   A 176 ? 2.8465 1.4642 2.3434 -0.5252 -0.4821 -0.0529 196 LEU   A CD2 
1319 N  N   . ASN   A 177 ? 3.0629 1.9650 2.5652 -0.4735 -0.4957 -0.0860 197 ASN   A N   
1320 C  CA  . ASN   A 177 ? 3.1108 2.0385 2.6212 -0.5055 -0.5509 -0.1006 197 ASN   A CA  
1321 C  C   . ASN   A 177 ? 3.0373 2.1005 2.6016 -0.4889 -0.5343 -0.0857 197 ASN   A C   
1322 O  O   . ASN   A 177 ? 2.9296 2.0989 2.5829 -0.4900 -0.4991 -0.0510 197 ASN   A O   
1323 C  CB  . ASN   A 177 ? 3.2051 2.0047 2.5862 -0.4883 -0.5869 -0.1485 197 ASN   A CB  
1324 C  CG  . ASN   A 177 ? 3.2625 1.9488 2.6023 -0.5007 -0.6036 -0.1620 197 ASN   A CG  
1325 O  OD1 . ASN   A 177 ? 3.2138 1.8866 2.5972 -0.5151 -0.5832 -0.1399 197 ASN   A OD1 
1326 N  ND2 . ASN   A 177 ? 3.3878 1.9986 2.6439 -0.4907 -0.6377 -0.1962 197 ASN   A ND2 
1327 N  N   . ASN   A 178 ? 3.0991 2.1531 2.6028 -0.4706 -0.5588 -0.1122 198 ASN   A N   
1328 C  CA  . ASN   A 178 ? 3.0868 2.2588 2.6362 -0.4576 -0.5527 -0.1005 198 ASN   A CA  
1329 C  C   . ASN   A 178 ? 3.1120 2.2721 2.5836 -0.3942 -0.5114 -0.1141 198 ASN   A C   
1330 O  O   . ASN   A 178 ? 3.1937 2.2710 2.5602 -0.3714 -0.5303 -0.1465 198 ASN   A O   
1331 C  CB  . ASN   A 178 ? 3.0952 2.2800 2.6511 -0.4924 -0.6203 -0.1143 198 ASN   A CB  
1332 C  CG  . ASN   A 178 ? 3.1798 2.2230 2.6332 -0.5058 -0.6723 -0.1534 198 ASN   A CG  
1333 O  OD1 . ASN   A 178 ? 3.1821 2.1935 2.6672 -0.5387 -0.6905 -0.1490 198 ASN   A OD1 
1334 N  ND2 . ASN   A 178 ? 3.2425 2.2191 2.5797 -0.4657 -0.6794 -0.1858 198 ASN   A ND2 
1335 N  N   . PRO   A 179 ? 2.9164 2.1542 2.4335 -0.3646 -0.4558 -0.0903 199 PRO   A N   
1336 C  CA  . PRO   A 179 ? 2.7875 2.0206 2.2419 -0.3078 -0.4164 -0.0999 199 PRO   A CA  
1337 C  C   . PRO   A 179 ? 2.7111 1.9937 2.1531 -0.2987 -0.4379 -0.1069 199 PRO   A C   
1338 O  O   . PRO   A 179 ? 2.6911 2.0655 2.2127 -0.3262 -0.4608 -0.0905 199 PRO   A O   
1339 C  CB  . PRO   A 179 ? 2.6852 1.9991 2.2120 -0.2902 -0.3608 -0.0693 199 PRO   A CB  
1340 C  CG  . PRO   A 179 ? 2.7295 2.0516 2.3245 -0.3299 -0.3661 -0.0490 199 PRO   A CG  
1341 C  CD  . PRO   A 179 ? 2.8072 2.1274 2.4269 -0.3807 -0.4248 -0.0541 199 PRO   A CD  
1342 N  N   . GLN   A 180 ? 2.6867 1.9073 2.0267 -0.2571 -0.4282 -0.1296 200 GLN   A N   
1343 C  CA  . GLN   A 180 ? 2.5641 1.8178 1.8745 -0.2405 -0.4444 -0.1361 200 GLN   A CA  
1344 C  C   . GLN   A 180 ? 2.5008 1.8421 1.8511 -0.2060 -0.3941 -0.1143 200 GLN   A C   
1345 O  O   . GLN   A 180 ? 2.4898 1.8254 1.7826 -0.1738 -0.3871 -0.1216 200 GLN   A O   
1346 C  CB  . GLN   A 180 ? 2.5303 1.6666 1.7005 -0.2123 -0.4597 -0.1705 200 GLN   A CB  
1347 C  CG  . GLN   A 180 ? 2.5074 1.5613 1.6255 -0.2472 -0.5279 -0.1976 200 GLN   A CG  
1348 C  CD  . GLN   A 180 ? 2.4950 1.4274 1.4602 -0.2125 -0.5393 -0.2332 200 GLN   A CD  
1349 O  OE1 . GLN   A 180 ? 2.5412 1.4234 1.4367 -0.1648 -0.4879 -0.2388 200 GLN   A OE1 
1350 N  NE2 . GLN   A 180 ? 2.4897 1.3754 1.4019 -0.2353 -0.6068 -0.2566 200 GLN   A NE2 
1351 N  N   . ASP   A 181 ? 2.4010 1.8184 1.8437 -0.2117 -0.3598 -0.0876 201 ASP   A N   
1352 C  CA  . ASP   A 181 ? 2.3895 1.8753 1.8641 -0.1781 -0.3107 -0.0696 201 ASP   A CA  
1353 C  C   . ASP   A 181 ? 2.3206 1.9244 1.9077 -0.1994 -0.3092 -0.0426 201 ASP   A C   
1354 O  O   . ASP   A 181 ? 2.2812 1.9173 1.9335 -0.2180 -0.2952 -0.0257 201 ASP   A O   
1355 C  CB  . ASP   A 181 ? 2.3823 1.8308 1.8407 -0.1504 -0.2605 -0.0663 201 ASP   A CB  
1356 C  CG  . ASP   A 181 ? 2.4393 1.7769 1.7848 -0.1190 -0.2514 -0.0912 201 ASP   A CG  
1357 O  OD1 . ASP   A 181 ? 2.4569 1.7105 1.7455 -0.1349 -0.2850 -0.1124 201 ASP   A OD1 
1358 O  OD2 . ASP   A 181 ? 2.4079 1.7408 1.7214 -0.0780 -0.2099 -0.0893 201 ASP   A OD2 
1359 N  N   . PRO   A 182 ? 2.2977 1.9654 1.9064 -0.1948 -0.3224 -0.0372 202 PRO   A N   
1360 C  CA  . PRO   A 182 ? 2.2398 2.0189 1.9494 -0.2048 -0.3119 -0.0117 202 PRO   A CA  
1361 C  C   . PRO   A 182 ? 2.2196 2.0376 1.9390 -0.1676 -0.2640 -0.0006 202 PRO   A C   
1362 O  O   . PRO   A 182 ? 2.2698 2.0374 1.9413 -0.1405 -0.2313 -0.0065 202 PRO   A O   
1363 C  CB  . PRO   A 182 ? 2.3012 2.1212 2.0269 -0.2196 -0.3579 -0.0133 202 PRO   A CB  
1364 C  CG  . PRO   A 182 ? 2.3363 2.0785 1.9550 -0.1938 -0.3716 -0.0366 202 PRO   A CG  
1365 C  CD  . PRO   A 182 ? 2.3493 1.9869 1.8912 -0.1848 -0.3559 -0.0543 202 PRO   A CD  
1366 N  N   . PHE   A 183 ? 2.0960 2.0029 1.8795 -0.1659 -0.2600 0.0157  203 PHE   A N   
1367 C  CA  . PHE   A 183 ? 1.9844 1.9278 1.7787 -0.1331 -0.2211 0.0252  203 PHE   A CA  
1368 C  C   . PHE   A 183 ? 1.8925 1.9221 1.7445 -0.1322 -0.2301 0.0383  203 PHE   A C   
1369 O  O   . PHE   A 183 ? 1.8104 1.8892 1.7003 -0.1155 -0.2009 0.0505  203 PHE   A O   
1370 C  CB  . PHE   A 183 ? 1.8791 1.8341 1.7078 -0.1288 -0.1823 0.0363  203 PHE   A CB  
1371 C  CG  . PHE   A 183 ? 1.8297 1.8293 1.7266 -0.1600 -0.1886 0.0506  203 PHE   A CG  
1372 C  CD1 . PHE   A 183 ? 1.8615 1.8125 1.7489 -0.1836 -0.1992 0.0475  203 PHE   A CD1 
1373 C  CD2 . PHE   A 183 ? 1.7606 1.8470 1.7281 -0.1638 -0.1814 0.0681  203 PHE   A CD2 
1374 C  CE1 . PHE   A 183 ? 1.8009 1.7913 1.7506 -0.2129 -0.2022 0.0644  203 PHE   A CE1 
1375 C  CE2 . PHE   A 183 ? 1.7467 1.8746 1.7738 -0.1905 -0.1823 0.0841  203 PHE   A CE2 
1376 C  CZ  . PHE   A 183 ? 1.7522 1.8331 1.7716 -0.2162 -0.1924 0.0836  203 PHE   A CZ  
1377 N  N   . PRO   A 198 ? 1.7705 2.2328 1.9668 -0.0811 -0.1441 0.1211  218 PRO   A N   
1378 C  CA  . PRO   A 198 ? 1.7481 2.2106 1.9544 -0.0829 -0.1143 0.1259  218 PRO   A CA  
1379 C  C   . PRO   A 198 ? 1.8155 2.3391 2.0628 -0.0651 -0.0919 0.1363  218 PRO   A C   
1380 O  O   . PRO   A 198 ? 1.7833 2.3179 2.0431 -0.0680 -0.0706 0.1429  218 PRO   A O   
1381 C  CB  . PRO   A 198 ? 1.6768 2.1409 1.9056 -0.1182 -0.1261 0.1332  218 PRO   A CB  
1382 C  CG  . PRO   A 198 ? 1.6245 2.0478 1.8235 -0.1331 -0.1605 0.1225  218 PRO   A CG  
1383 C  CD  . PRO   A 198 ? 1.6780 2.1241 1.8742 -0.1127 -0.1758 0.1192  218 PRO   A CD  
1384 N  N   . PHE   A 199 ? 1.8538 2.4120 2.1161 -0.0444 -0.0969 0.1374  219 PHE   A N   
1385 C  CA  . PHE   A 199 ? 1.8394 2.4527 2.1369 -0.0234 -0.0762 0.1457  219 PHE   A CA  
1386 C  C   . PHE   A 199 ? 1.7836 2.4111 2.0806 0.0057  -0.0823 0.1430  219 PHE   A C   
1387 O  O   . PHE   A 199 ? 1.7448 2.4324 2.0846 0.0201  -0.0777 0.1525  219 PHE   A O   
1388 C  CB  . PHE   A 199 ? 1.8533 2.5363 2.2130 -0.0409 -0.0750 0.1636  219 PHE   A CB  
1389 C  CG  . PHE   A 199 ? 1.8369 2.5400 2.2267 -0.0682 -0.1082 0.1696  219 PHE   A CG  
1390 C  CD1 . PHE   A 199 ? 1.7932 2.5267 2.2024 -0.0579 -0.1320 0.1706  219 PHE   A CD1 
1391 C  CD2 . PHE   A 199 ? 1.7944 2.4833 2.1929 -0.1045 -0.1184 0.1746  219 PHE   A CD2 
1392 C  CE1 . PHE   A 199 ? 1.8110 2.5630 2.2486 -0.0845 -0.1685 0.1752  219 PHE   A CE1 
1393 C  CE2 . PHE   A 199 ? 1.7891 2.4919 2.2155 -0.1325 -0.1535 0.1785  219 PHE   A CE2 
1394 C  CZ  . PHE   A 199 ? 1.8127 2.5485 2.2593 -0.1232 -0.1801 0.1783  219 PHE   A CZ  
1395 N  N   . PHE   A 200 ? 1.8027 2.3748 2.0512 0.0165  -0.0906 0.1319  220 PHE   A N   
1396 C  CA  . PHE   A 200 ? 1.7577 2.3319 1.9976 0.0447  -0.0965 0.1309  220 PHE   A CA  
1397 C  C   . PHE   A 200 ? 1.7291 2.2612 1.9363 0.0675  -0.0725 0.1230  220 PHE   A C   
1398 O  O   . PHE   A 200 ? 1.7449 2.2190 1.9105 0.0636  -0.0676 0.1155  220 PHE   A O   
1399 C  CB  . PHE   A 200 ? 1.7911 2.3341 1.9985 0.0401  -0.1263 0.1275  220 PHE   A CB  
1400 C  CG  . PHE   A 200 ? 1.7866 2.2962 1.9565 0.0694  -0.1258 0.1248  220 PHE   A CG  
1401 C  CD1 . PHE   A 200 ? 1.7366 2.2849 1.9324 0.0951  -0.1289 0.1321  220 PHE   A CD1 
1402 C  CD2 . PHE   A 200 ? 1.7955 2.2342 1.9053 0.0724  -0.1200 0.1171  220 PHE   A CD2 
1403 C  CE1 . PHE   A 200 ? 1.7653 2.2770 1.9248 0.1218  -0.1282 0.1318  220 PHE   A CE1 
1404 C  CE2 . PHE   A 200 ? 1.7656 2.1719 1.8415 0.0978  -0.1168 0.1183  220 PHE   A CE2 
1405 C  CZ  . PHE   A 200 ? 1.7870 2.2272 1.8863 0.1217  -0.1219 0.1257  220 PHE   A CZ  
1406 N  N   . LEU   A 201 ? 1.7894 2.3503 2.0174 0.0914  -0.0576 0.1250  221 LEU   A N   
1407 C  CA  . LEU   A 201 ? 1.7322 2.2509 1.9314 0.1140  -0.0420 0.1172  221 LEU   A CA  
1408 C  C   . LEU   A 201 ? 1.7401 2.2720 1.9455 0.1440  -0.0466 0.1206  221 LEU   A C   
1409 O  O   . LEU   A 201 ? 1.8236 2.3463 2.0165 0.1483  -0.0654 0.1247  221 LEU   A O   
1410 C  CB  . LEU   A 201 ? 1.5720 2.0920 1.7759 0.1168  -0.0196 0.1121  221 LEU   A CB  
1411 C  CG  . LEU   A 201 ? 1.5039 1.9736 1.6800 0.1013  -0.0120 0.1049  221 LEU   A CG  
1412 C  CD1 . LEU   A 201 ? 1.5469 1.9610 1.6905 0.1073  -0.0143 0.1011  221 LEU   A CD1 
1413 C  CD2 . LEU   A 201 ? 1.4615 1.9371 1.6424 0.0723  -0.0182 0.1089  221 LEU   A CD2 
1414 N  N   . SER   A 202 ? 1.7115 2.2587 1.9301 0.1671  -0.0302 0.1183  222 SER   A N   
1415 C  CA  . SER   A 202 ? 1.7271 2.2760 1.9474 0.2006  -0.0306 0.1201  222 SER   A CA  
1416 C  C   . SER   A 202 ? 1.8690 2.3489 2.0465 0.2091  -0.0329 0.1165  222 SER   A C   
1417 O  O   . SER   A 202 ? 1.8737 2.3344 2.0433 0.2366  -0.0292 0.1162  222 SER   A O   
1418 C  CB  . SER   A 202 ? 1.7147 2.3223 1.9715 0.2084  -0.0490 0.1328  222 SER   A CB  
1419 O  OG  . SER   A 202 ? 1.6823 2.3092 1.9544 0.2452  -0.0435 0.1358  222 SER   A OG  
1420 N  N   . ILE   A 203 ? 1.6753 2.1158 1.8249 0.1867  -0.0370 0.1152  223 ILE   A N   
1421 C  CA  . ILE   A 203 ? 1.7328 2.1078 1.8441 0.1914  -0.0317 0.1142  223 ILE   A CA  
1422 C  C   . ILE   A 203 ? 1.7258 2.0688 1.8341 0.1901  -0.0128 0.1049  223 ILE   A C   
1423 O  O   . ILE   A 203 ? 1.7898 2.0910 1.8843 0.2040  -0.0061 0.1042  223 ILE   A O   
1424 C  CB  . ILE   A 203 ? 1.7314 2.0780 1.8126 0.1714  -0.0398 0.1170  223 ILE   A CB  
1425 C  CG1 . ILE   A 203 ? 1.6651 2.0347 1.7600 0.1438  -0.0413 0.1125  223 ILE   A CG1 
1426 C  CG2 . ILE   A 203 ? 1.7509 2.1018 1.8151 0.1810  -0.0619 0.1257  223 ILE   A CG2 
1427 C  CD1 . ILE   A 203 ? 1.6539 1.9852 1.7140 0.1262  -0.0453 0.1118  223 ILE   A CD1 
1428 N  N   . THR   A 204 ? 1.6729 2.0324 1.7942 0.1725  -0.0062 0.0984  224 THR   A N   
1429 C  CA  . THR   A 204 ? 1.5818 1.9162 1.7018 0.1725  0.0061  0.0886  224 THR   A CA  
1430 C  C   . THR   A 204 ? 1.5570 1.8890 1.6795 0.1998  0.0098  0.0828  224 THR   A C   
1431 O  O   . THR   A 204 ? 1.4742 1.7634 1.5862 0.2055  0.0144  0.0751  224 THR   A O   
1432 C  CB  . THR   A 204 ? 1.4590 1.8198 1.5910 0.1546  0.0101  0.0844  224 THR   A CB  
1433 O  OG1 . THR   A 204 ? 1.3997 1.7347 1.5228 0.1325  0.0111  0.0854  224 THR   A OG1 
1434 C  CG2 . THR   A 204 ? 1.3309 1.6874 1.4629 0.1648  0.0179  0.0734  224 THR   A CG2 
1435 N  N   . VAL   A 205 ? 1.5747 1.9513 1.7128 0.2174  0.0071  0.0866  225 VAL   A N   
1436 C  CA  . VAL   A 205 ? 1.6129 1.9842 1.7503 0.2494  0.0112  0.0821  225 VAL   A CA  
1437 C  C   . VAL   A 205 ? 1.7113 2.0454 1.8346 0.2651  0.0043  0.0893  225 VAL   A C   
1438 O  O   . VAL   A 205 ? 1.7134 2.0002 1.8216 0.2813  0.0083  0.0837  225 VAL   A O   
1439 C  CB  . VAL   A 205 ? 1.5740 2.0128 1.7393 0.2657  0.0146  0.0862  225 VAL   A CB  
1440 C  CG1 . VAL   A 205 ? 1.4256 1.8559 1.5832 0.2968  0.0273  0.0748  225 VAL   A CG1 
1441 C  CG2 . VAL   A 205 ? 1.5187 2.0033 1.7029 0.2398  0.0172  0.0897  225 VAL   A CG2 
1442 N  N   . PHE   A 206 ? 1.8859 2.2359 2.0101 0.2602  -0.0076 0.1022  226 PHE   A N   
1443 C  CA  . PHE   A 206 ? 1.9079 2.2307 2.0157 0.2794  -0.0160 0.1127  226 PHE   A CA  
1444 C  C   . PHE   A 206 ? 1.9819 2.2761 2.0638 0.2593  -0.0224 0.1212  226 PHE   A C   
1445 O  O   . PHE   A 206 ? 1.9771 2.2970 2.0567 0.2553  -0.0382 0.1294  226 PHE   A O   
1446 C  CB  . PHE   A 206 ? 1.8524 2.2300 1.9845 0.3030  -0.0275 0.1211  226 PHE   A CB  
1447 C  CG  . PHE   A 206 ? 1.9002 2.3162 2.0597 0.3241  -0.0163 0.1139  226 PHE   A CG  
1448 C  CD1 . PHE   A 206 ? 2.0144 2.3886 2.1591 0.3481  -0.0042 0.1039  226 PHE   A CD1 
1449 C  CD2 . PHE   A 206 ? 1.8734 2.3641 2.0716 0.3198  -0.0165 0.1173  226 PHE   A CD2 
1450 C  CE1 . PHE   A 206 ? 1.9565 2.3596 2.1162 0.3714  0.0084  0.0954  226 PHE   A CE1 
1451 C  CE2 . PHE   A 206 ? 1.9287 2.4551 2.1484 0.3423  -0.0006 0.1124  226 PHE   A CE2 
1452 C  CZ  . PHE   A 206 ? 1.9361 2.4171 2.1324 0.3700  0.0124  0.1005  226 PHE   A CZ  
1453 N  N   . PRO   A 207 ? 2.0117 2.2520 2.0735 0.2467  -0.0108 0.1197  227 PRO   A N   
1454 C  CA  . PRO   A 207 ? 2.0246 2.2396 2.0598 0.2290  -0.0110 0.1274  227 PRO   A CA  
1455 C  C   . PRO   A 207 ? 2.0252 2.1994 2.0262 0.2453  -0.0137 0.1422  227 PRO   A C   
1456 O  O   . PRO   A 207 ? 2.0386 2.1886 2.0072 0.2367  -0.0132 0.1501  227 PRO   A O   
1457 C  CB  . PRO   A 207 ? 1.9800 2.1637 2.0184 0.2098  0.0060  0.1213  227 PRO   A CB  
1458 C  CG  . PRO   A 207 ? 2.0231 2.1878 2.0754 0.2230  0.0118  0.1145  227 PRO   A CG  
1459 C  CD  . PRO   A 207 ? 2.0683 2.2704 2.1330 0.2466  0.0027  0.1105  227 PRO   A CD  
1460 N  N   . PHE   A 208 ? 1.8580 2.0183 1.8612 0.2709  -0.0146 0.1463  228 PHE   A N   
1461 C  CA  . PHE   A 208 ? 1.8205 1.9347 1.7906 0.2897  -0.0151 0.1628  228 PHE   A CA  
1462 C  C   . PHE   A 208 ? 1.7546 1.8910 1.7012 0.2979  -0.0365 0.1729  228 PHE   A C   
1463 O  O   . PHE   A 208 ? 1.7287 1.8285 1.6359 0.3125  -0.0405 0.1886  228 PHE   A O   
1464 C  CB  . PHE   A 208 ? 1.8018 1.8987 1.7832 0.3172  -0.0139 0.1629  228 PHE   A CB  
1465 C  CG  . PHE   A 208 ? 1.8001 1.9552 1.8118 0.3363  -0.0263 0.1552  228 PHE   A CG  
1466 C  CD1 . PHE   A 208 ? 1.7558 1.9389 1.7656 0.3594  -0.0446 0.1667  228 PHE   A CD1 
1467 C  CD2 . PHE   A 208 ? 1.7928 1.9761 1.8349 0.3328  -0.0190 0.1380  228 PHE   A CD2 
1468 C  CE1 . PHE   A 208 ? 1.7335 1.9770 1.7803 0.3784  -0.0533 0.1627  228 PHE   A CE1 
1469 C  CE2 . PHE   A 208 ? 1.7808 2.0202 1.8516 0.3532  -0.0248 0.1337  228 PHE   A CE2 
1470 C  CZ  . PHE   A 208 ? 1.7418 2.0144 1.8196 0.3758  -0.0409 0.1468  228 PHE   A CZ  
1471 N  N   . LEU   A 209 ? 1.7648 1.9614 1.7363 0.2880  -0.0518 0.1644  229 LEU   A N   
1472 C  CA  . LEU   A 209 ? 1.7392 1.9648 1.6972 0.2878  -0.0782 0.1701  229 LEU   A CA  
1473 C  C   . LEU   A 209 ? 1.7768 1.9789 1.6968 0.2633  -0.0793 0.1682  229 LEU   A C   
1474 O  O   . LEU   A 209 ? 1.7470 1.9591 1.6430 0.2618  -0.1042 0.1713  229 LEU   A O   
1475 C  CB  . LEU   A 209 ? 1.7023 2.0059 1.7140 0.2858  -0.0939 0.1635  229 LEU   A CB  
1476 C  CG  . LEU   A 209 ? 1.6903 2.0234 1.7392 0.3156  -0.0917 0.1654  229 LEU   A CG  
1477 C  CD1 . LEU   A 209 ? 1.6542 2.0657 1.7605 0.3101  -0.0959 0.1595  229 LEU   A CD1 
1478 C  CD2 . LEU   A 209 ? 1.6959 2.0223 1.7287 0.3464  -0.1108 0.1808  229 LEU   A CD2 
1479 N  N   . ILE   A 210 ? 1.6697 1.8401 1.5831 0.2455  -0.0547 0.1627  230 ILE   A N   
1480 C  CA  . ILE   A 210 ? 1.6762 1.8165 1.5480 0.2283  -0.0511 0.1620  230 ILE   A CA  
1481 C  C   . ILE   A 210 ? 1.7575 1.8454 1.5645 0.2446  -0.0519 0.1769  230 ILE   A C   
1482 O  O   . ILE   A 210 ? 1.7940 1.8735 1.5579 0.2411  -0.0697 0.1760  230 ILE   A O   
1483 C  CB  . ILE   A 210 ? 1.6270 1.7494 1.5136 0.2095  -0.0232 0.1554  230 ILE   A CB  
1484 C  CG1 . ILE   A 210 ? 1.5717 1.7439 1.5052 0.1906  -0.0280 0.1409  230 ILE   A CG1 
1485 C  CG2 . ILE   A 210 ? 1.5697 1.6481 1.4071 0.2010  -0.0110 0.1588  230 ILE   A CG2 
1486 C  CD1 . ILE   A 210 ? 1.5255 1.6841 1.4739 0.1727  -0.0058 0.1345  230 ILE   A CD1 
1487 N  N   . PRO   A 211 ? 1.7873 1.8347 1.5803 0.2622  -0.0344 0.1910  231 PRO   A N   
1488 C  CA  . PRO   A 211 ? 1.8177 1.8153 1.5432 0.2801  -0.0351 0.2087  231 PRO   A CA  
1489 C  C   . PRO   A 211 ? 1.8347 1.8528 1.5370 0.2975  -0.0730 0.2126  231 PRO   A C   
1490 O  O   . PRO   A 211 ? 1.8562 1.8366 1.4906 0.3090  -0.0818 0.2232  231 PRO   A O   
1491 C  CB  . PRO   A 211 ? 1.7836 1.7412 1.5152 0.2940  -0.0102 0.2243  231 PRO   A CB  
1492 C  CG  . PRO   A 211 ? 1.7231 1.6957 1.5135 0.2755  0.0088  0.2122  231 PRO   A CG  
1493 C  CD  . PRO   A 211 ? 1.7413 1.7776 1.5728 0.2651  -0.0125 0.1924  231 PRO   A CD  
1494 N  N   . ILE   A 212 ? 1.8926 1.9700 1.6486 0.3013  -0.0957 0.2054  232 ILE   A N   
1495 C  CA  . ILE   A 212 ? 1.8899 2.0002 1.6378 0.3138  -0.1361 0.2087  232 ILE   A CA  
1496 C  C   . ILE   A 212 ? 1.9221 2.0388 1.6399 0.2925  -0.1587 0.1980  232 ILE   A C   
1497 O  O   . ILE   A 212 ? 1.9641 2.0613 1.6262 0.3016  -0.1861 0.2035  232 ILE   A O   
1498 C  CB  . ILE   A 212 ? 1.8930 2.0745 1.7168 0.3214  -0.1503 0.2043  232 ILE   A CB  
1499 C  CG1 . ILE   A 212 ? 1.9136 2.0803 1.7452 0.3549  -0.1436 0.2180  232 ILE   A CG1 
1500 C  CG2 . ILE   A 212 ? 1.9028 2.1418 1.7439 0.3172  -0.1930 0.2019  232 ILE   A CG2 
1501 C  CD1 . ILE   A 212 ? 1.9217 2.1564 1.8098 0.3740  -0.1667 0.2192  232 ILE   A CD1 
1502 N  N   . LEU   A 213 ? 1.9207 2.0599 1.6711 0.2643  -0.1493 0.1821  233 LEU   A N   
1503 C  CA  . LEU   A 213 ? 1.8985 2.0421 1.6267 0.2419  -0.1720 0.1699  233 LEU   A CA  
1504 C  C   . LEU   A 213 ? 1.9674 2.0384 1.6135 0.2395  -0.1564 0.1691  233 LEU   A C   
1505 O  O   . LEU   A 213 ? 2.0195 2.0743 1.6199 0.2298  -0.1812 0.1603  233 LEU   A O   
1506 C  CB  . LEU   A 213 ? 1.7899 1.9821 1.5835 0.2142  -0.1666 0.1558  233 LEU   A CB  
1507 C  CG  . LEU   A 213 ? 1.6933 1.9563 1.5677 0.2193  -0.1708 0.1577  233 LEU   A CG  
1508 C  CD1 . LEU   A 213 ? 1.5895 1.8917 1.5183 0.1934  -0.1587 0.1465  233 LEU   A CD1 
1509 C  CD2 . LEU   A 213 ? 1.7162 2.0267 1.6095 0.2285  -0.2125 0.1640  233 LEU   A CD2 
1510 N  N   . GLU   A 214 ? 1.8175 1.8437 1.4445 0.2484  -0.1159 0.1783  234 GLU   A N   
1511 C  CA  . GLU   A 214 ? 1.8641 1.8222 1.4119 0.2528  -0.0953 0.1827  234 GLU   A CA  
1512 C  C   . GLU   A 214 ? 1.9754 1.8937 1.4413 0.2765  -0.1165 0.1945  234 GLU   A C   
1513 O  O   . GLU   A 214 ? 2.0979 1.9599 1.4834 0.2817  -0.1072 0.1955  234 GLU   A O   
1514 C  CB  . GLU   A 214 ? 1.8579 1.7858 1.4179 0.2566  -0.0465 0.1945  234 GLU   A CB  
1515 C  CG  . GLU   A 214 ? 1.8004 1.7605 1.4334 0.2345  -0.0263 0.1832  234 GLU   A CG  
1516 C  CD  . GLU   A 214 ? 1.7694 1.7152 1.3857 0.2165  -0.0146 0.1708  234 GLU   A CD  
1517 O  OE1 . GLU   A 214 ? 1.8241 1.7295 1.3682 0.2219  -0.0189 0.1697  234 GLU   A OE1 
1518 O  OE2 . GLU   A 214 ? 1.6845 1.6560 1.3560 0.1988  -0.0016 0.1619  234 GLU   A OE2 
1519 N  N   . VAL   A 215 ? 2.0997 2.0441 1.5810 0.2937  -0.1439 0.2042  235 VAL   A N   
1520 C  CA  . VAL   A 215 ? 2.1754 2.0899 1.5818 0.3165  -0.1745 0.2149  235 VAL   A CA  
1521 C  C   . VAL   A 215 ? 2.2140 2.1810 1.6424 0.3107  -0.2318 0.2046  235 VAL   A C   
1522 O  O   . VAL   A 215 ? 2.2514 2.1951 1.6134 0.3251  -0.2673 0.2089  235 VAL   A O   
1523 C  CB  . VAL   A 215 ? 2.1014 1.9924 1.4962 0.3470  -0.1611 0.2404  235 VAL   A CB  
1524 C  CG1 . VAL   A 215 ? 2.0656 1.9138 1.4604 0.3472  -0.1048 0.2522  235 VAL   A CG1 
1525 C  CG2 . VAL   A 215 ? 2.0504 2.0052 1.5273 0.3545  -0.1818 0.2423  235 VAL   A CG2 
1526 N  N   . LEU   A 216 ? 2.2597 2.2976 1.7795 0.2903  -0.2426 0.1926  236 LEU   A N   
1527 C  CA  . LEU   A 216 ? 2.2530 2.3489 1.8088 0.2781  -0.2942 0.1837  236 LEU   A CA  
1528 C  C   . LEU   A 216 ? 2.3209 2.3980 1.8402 0.2501  -0.3149 0.1640  236 LEU   A C   
1529 O  O   . LEU   A 216 ? 2.3452 2.4710 1.9042 0.2313  -0.3570 0.1550  236 LEU   A O   
1530 C  CB  . LEU   A 216 ? 2.1943 2.3737 1.8632 0.2683  -0.2912 0.1818  236 LEU   A CB  
1531 C  CG  . LEU   A 216 ? 2.1840 2.4308 1.9100 0.2850  -0.3266 0.1924  236 LEU   A CG  
1532 C  CD1 . LEU   A 216 ? 2.0553 2.3723 1.8827 0.2813  -0.3066 0.1918  236 LEU   A CD1 
1533 C  CD2 . LEU   A 216 ? 2.0921 2.3699 1.8170 0.2701  -0.3838 0.1865  236 LEU   A CD2 
1534 N  N   . ASN   A 217 ? 2.2780 2.2851 1.7257 0.2475  -0.2853 0.1580  237 ASN   A N   
1535 C  CA  . ASN   A 217 ? 2.3451 2.3179 1.7447 0.2254  -0.2995 0.1380  237 ASN   A CA  
1536 C  C   . ASN   A 217 ? 2.2876 2.3171 1.7737 0.1906  -0.3055 0.1234  237 ASN   A C   
1537 O  O   . ASN   A 217 ? 2.2634 2.3272 1.7754 0.1703  -0.3506 0.1138  237 ASN   A O   
1538 C  CB  . ASN   A 217 ? 2.4204 2.3658 1.7445 0.2314  -0.3550 0.1329  237 ASN   A CB  
1539 C  CG  . ASN   A 217 ? 2.4946 2.3661 1.7089 0.2657  -0.3443 0.1463  237 ASN   A CG  
1540 O  OD1 . ASN   A 217 ? 2.5966 2.3944 1.7197 0.2710  -0.3242 0.1397  237 ASN   A OD1 
1541 N  ND2 . ASN   A 217 ? 2.4388 2.3282 1.6597 0.2915  -0.3557 0.1667  237 ASN   A ND2 
1542 N  N   . ILE   A 218 ? 2.1224 2.1604 1.6538 0.1835  -0.2591 0.1238  238 ILE   A N   
1543 C  CA  . ILE   A 218 ? 1.9966 2.0820 1.6045 0.1537  -0.2554 0.1133  238 ILE   A CA  
1544 C  C   . ILE   A 218 ? 1.9257 1.9612 1.5034 0.1439  -0.2182 0.1039  238 ILE   A C   
1545 O  O   . ILE   A 218 ? 1.8869 1.8854 1.4377 0.1609  -0.1778 0.1119  238 ILE   A O   
1546 C  CB  . ILE   A 218 ? 1.8854 2.0401 1.5879 0.1565  -0.2381 0.1233  238 ILE   A CB  
1547 C  CG1 . ILE   A 218 ? 1.8723 2.0691 1.5987 0.1767  -0.2664 0.1361  238 ILE   A CG1 
1548 C  CG2 . ILE   A 218 ? 1.7818 1.9901 1.5585 0.1264  -0.2411 0.1149  238 ILE   A CG2 
1549 C  CD1 . ILE   A 218 ? 1.9385 2.1815 1.6914 0.1612  -0.3196 0.1322  238 ILE   A CD1 
1550 N  N   . CYS   A 219 ? 1.9291 1.9642 1.5153 0.1168  -0.2320 0.0888  239 CYS   A N   
1551 C  CA  . CYS   A 219 ? 1.8915 1.8828 1.4553 0.1083  -0.1994 0.0797  239 CYS   A CA  
1552 C  C   . CYS   A 219 ? 1.7530 1.7949 1.4025 0.0849  -0.1862 0.0777  239 CYS   A C   
1553 O  O   . CYS   A 219 ? 1.6923 1.7416 1.3585 0.0593  -0.2065 0.0673  239 CYS   A O   
1554 C  CB  . CYS   A 219 ? 1.9822 1.9109 1.4665 0.0998  -0.2232 0.0625  239 CYS   A CB  
1555 S  SG  . CYS   A 219 ? 2.1716 2.0226 1.5301 0.1314  -0.2316 0.0634  239 CYS   A SG  
1556 N  N   . THR   A 226 ? 2.3037 2.1673 1.7729 0.0238  -0.2754 0.0147  246 THR   A N   
1557 C  CA  . THR   A 226 ? 2.4290 2.2202 1.8350 0.0106  -0.2920 -0.0061 246 THR   A CA  
1558 C  C   . THR   A 226 ? 2.5933 2.3218 1.8972 0.0213  -0.3313 -0.0201 246 THR   A C   
1559 O  O   . THR   A 226 ? 2.6383 2.3641 1.9023 0.0476  -0.3309 -0.0116 246 THR   A O   
1560 C  CB  . THR   A 226 ? 2.4213 2.1571 1.7909 0.0261  -0.2406 -0.0097 246 THR   A CB  
1561 O  OG1 . THR   A 226 ? 2.5146 2.1708 1.8127 0.0180  -0.2573 -0.0316 246 THR   A OG1 
1562 C  CG2 . THR   A 226 ? 2.4275 2.1345 1.7416 0.0648  -0.2012 -0.0001 246 THR   A CG2 
1563 N  N   . ASN   A 227 ? 2.6266 2.3003 1.8850 0.0009  -0.3674 -0.0415 247 ASN   A N   
1564 C  CA  . ASN   A 227 ? 2.7278 2.3266 1.8735 0.0113  -0.4072 -0.0595 247 ASN   A CA  
1565 C  C   . ASN   A 227 ? 2.8099 2.3169 1.8828 -0.0007 -0.4209 -0.0864 247 ASN   A C   
1566 O  O   . ASN   A 227 ? 2.8746 2.2904 1.8292 0.0270  -0.4090 -0.1009 247 ASN   A O   
1567 C  CB  . ASN   A 227 ? 2.7182 2.3660 1.8954 -0.0072 -0.4724 -0.0580 247 ASN   A CB  
1568 C  CG  . ASN   A 227 ? 2.7843 2.3568 1.8385 0.0090  -0.5153 -0.0745 247 ASN   A CG  
1569 O  OD1 . ASN   A 227 ? 2.8881 2.3922 1.8389 0.0457  -0.4851 -0.0771 247 ASN   A OD1 
1570 N  ND2 . ASN   A 227 ? 2.8082 2.3919 1.8717 -0.0182 -0.5861 -0.0850 247 ASN   A ND2 
1571 N  N   . PHE   A 228 ? 2.6926 2.2195 1.8324 -0.0409 -0.4457 -0.0927 248 PHE   A N   
1572 C  CA  . PHE   A 228 ? 2.6645 2.1013 1.7436 -0.0537 -0.4558 -0.1173 248 PHE   A CA  
1573 C  C   . PHE   A 228 ? 2.7090 2.0889 1.7371 -0.0211 -0.3902 -0.1188 248 PHE   A C   
1574 O  O   . PHE   A 228 ? 2.8211 2.1007 1.7336 0.0009  -0.3858 -0.1393 248 PHE   A O   
1575 C  CB  . PHE   A 228 ? 2.5460 2.0239 1.7240 -0.1022 -0.4808 -0.1158 248 PHE   A CB  
1576 C  CG  . PHE   A 228 ? 2.5215 1.9448 1.6917 -0.1071 -0.4488 -0.1238 248 PHE   A CG  
1577 C  CD1 . PHE   A 228 ? 2.5924 1.9017 1.6621 -0.1070 -0.4674 -0.1522 248 PHE   A CD1 
1578 C  CD2 . PHE   A 228 ? 2.4647 1.9469 1.7239 -0.1096 -0.4015 -0.1032 248 PHE   A CD2 
1579 C  CE1 . PHE   A 228 ? 2.5750 1.8321 1.6376 -0.1079 -0.4372 -0.1584 248 PHE   A CE1 
1580 C  CE2 . PHE   A 228 ? 2.4590 1.8918 1.7113 -0.1116 -0.3738 -0.1085 248 PHE   A CE2 
1581 C  CZ  . PHE   A 228 ? 2.5095 1.8306 1.6657 -0.1100 -0.3907 -0.1354 248 PHE   A CZ  
1582 N  N   . LEU   A 229 ? 2.6766 2.1199 1.7891 -0.0157 -0.3391 -0.0970 249 LEU   A N   
1583 C  CA  . LEU   A 229 ? 2.6827 2.0845 1.7639 0.0140  -0.2778 -0.0950 249 LEU   A CA  
1584 C  C   . LEU   A 229 ? 2.7678 2.1534 1.7871 0.0578  -0.2394 -0.0858 249 LEU   A C   
1585 O  O   . LEU   A 229 ? 2.7848 2.1178 1.7520 0.0872  -0.1926 -0.0873 249 LEU   A O   
1586 C  CB  . LEU   A 229 ? 2.5310 2.0040 1.7252 0.0019  -0.2419 -0.0755 249 LEU   A CB  
1587 C  CG  . LEU   A 229 ? 2.4972 1.9289 1.6999 -0.0093 -0.2276 -0.0836 249 LEU   A CG  
1588 C  CD1 . LEU   A 229 ? 2.3138 1.7803 1.5700 0.0097  -0.1684 -0.0651 249 LEU   A CD1 
1589 C  CD2 . LEU   A 229 ? 2.6018 1.9159 1.6861 0.0049  -0.2362 -0.1105 249 LEU   A CD2 
1590 N  N   . ARG   A 230 ? 2.8078 2.2372 1.8331 0.0639  -0.2566 -0.0742 250 ARG   A N   
1591 C  CA  . ARG   A 230 ? 2.8452 2.2570 1.8119 0.1042  -0.2195 -0.0619 250 ARG   A CA  
1592 C  C   . ARG   A 230 ? 2.9801 2.2834 1.8006 0.1326  -0.2199 -0.0808 250 ARG   A C   
1593 O  O   . ARG   A 230 ? 3.0454 2.3206 1.8071 0.1697  -0.1768 -0.0695 250 ARG   A O   
1594 C  CB  . ARG   A 230 ? 2.8514 2.3272 1.8521 0.1051  -0.2425 -0.0453 250 ARG   A CB  
1595 C  CG  . ARG   A 230 ? 2.9293 2.3574 1.8325 0.1132  -0.2923 -0.0576 250 ARG   A CG  
1596 C  CD  . ARG   A 230 ? 2.9581 2.3921 1.8219 0.1467  -0.2751 -0.0380 250 ARG   A CD  
1597 N  NE  . ARG   A 230 ? 2.8851 2.4136 1.8606 0.1421  -0.2594 -0.0126 250 ARG   A NE  
1598 C  CZ  . ARG   A 230 ? 2.8159 2.4143 1.8608 0.1238  -0.3021 -0.0064 250 ARG   A CZ  
1599 N  NH1 . ARG   A 230 ? 2.8657 2.4591 1.8918 0.1045  -0.3662 -0.0216 250 ARG   A NH1 
1600 N  NH2 . ARG   A 230 ? 2.6714 2.3461 1.8087 0.1254  -0.2807 0.0154  250 ARG   A NH2 
1601 N  N   . LYS   A 231 ? 3.1084 2.3474 1.8672 0.1166  -0.2660 -0.1086 251 LYS   A N   
1602 C  CA  . LYS   A 231 ? 3.2401 2.3649 1.8498 0.1459  -0.2647 -0.1305 251 LYS   A CA  
1603 C  C   . LYS   A 231 ? 3.2773 2.3282 1.8525 0.1357  -0.2687 -0.1565 251 LYS   A C   
1604 O  O   . LYS   A 231 ? 3.3870 2.3430 1.8492 0.1682  -0.2435 -0.1720 251 LYS   A O   
1605 C  CB  . LYS   A 231 ? 3.3465 2.4379 1.8710 0.1458  -0.3273 -0.1437 251 LYS   A CB  
1606 C  CG  . LYS   A 231 ? 3.2672 2.4398 1.8856 0.1045  -0.3909 -0.1396 251 LYS   A CG  
1607 C  CD  . LYS   A 231 ? 3.1904 2.3978 1.7899 0.1217  -0.4100 -0.1234 251 LYS   A CD  
1608 C  CE  . LYS   A 231 ? 3.2682 2.3989 1.7541 0.1551  -0.4024 -0.1320 251 LYS   A CE  
1609 N  NZ  . LYS   A 231 ? 3.2933 2.3614 1.7294 0.1369  -0.4540 -0.1623 251 LYS   A NZ  
1610 N  N   . SER   A 232 ? 3.1904 2.2804 1.8586 0.0927  -0.2983 -0.1606 252 SER   A N   
1611 C  CA  . SER   A 232 ? 3.1382 2.1605 1.7861 0.0821  -0.2979 -0.1812 252 SER   A CA  
1612 C  C   . SER   A 232 ? 3.1949 2.1923 1.8318 0.1183  -0.2229 -0.1728 252 SER   A C   
1613 O  O   . SER   A 232 ? 3.2142 2.1165 1.7673 0.1370  -0.2094 -0.1934 252 SER   A O   
1614 C  CB  . SER   A 232 ? 2.9294 2.0158 1.6999 0.0312  -0.3287 -0.1762 252 SER   A CB  
1615 O  OG  . SER   A 232 ? 2.8025 1.8343 1.5711 0.0246  -0.3142 -0.1879 252 SER   A OG  
1616 N  N   . VAL   A 233 ? 3.0539 2.1364 1.7789 0.1286  -0.1749 -0.1426 253 VAL   A N   
1617 C  CA  . VAL   A 233 ? 3.0144 2.0836 1.7343 0.1656  -0.1034 -0.1304 253 VAL   A CA  
1618 C  C   . VAL   A 233 ? 3.0764 2.0770 1.6717 0.2123  -0.0743 -0.1337 253 VAL   A C   
1619 O  O   . VAL   A 233 ? 3.1573 2.0847 1.6796 0.2457  -0.0351 -0.1426 253 VAL   A O   
1620 C  CB  . VAL   A 233 ? 2.7913 1.9697 1.6399 0.1606  -0.0670 -0.0978 253 VAL   A CB  
1621 C  CG1 . VAL   A 233 ? 2.7054 1.8755 1.5537 0.1986  0.0042  -0.0827 253 VAL   A CG1 
1622 C  CG2 . VAL   A 233 ? 2.6963 1.9351 1.6569 0.1190  -0.0900 -0.0941 253 VAL   A CG2 
1623 N  N   . LYS   A 234 ? 3.0788 2.1009 1.6455 0.2174  -0.0923 -0.1253 254 LYS   A N   
1624 C  CA  . LYS   A 234 ? 3.1888 2.1554 1.6406 0.2619  -0.0628 -0.1218 254 LYS   A CA  
1625 C  C   . LYS   A 234 ? 3.2848 2.1351 1.6060 0.2837  -0.0705 -0.1510 254 LYS   A C   
1626 O  O   . LYS   A 234 ? 3.3050 2.1190 1.5762 0.3233  -0.0219 -0.1418 254 LYS   A O   
1627 C  CB  . LYS   A 234 ? 3.1960 2.1971 1.6342 0.2572  -0.0994 -0.1118 254 LYS   A CB  
1628 C  CG  . LYS   A 234 ? 3.2644 2.1929 1.5913 0.2724  -0.1315 -0.1287 254 LYS   A CG  
1629 C  CD  . LYS   A 234 ? 3.2123 2.1862 1.5495 0.2628  -0.1753 -0.1183 254 LYS   A CD  
1630 C  CE  . LYS   A 234 ? 3.1902 2.0999 1.4420 0.2646  -0.2242 -0.1405 254 LYS   A CE  
1631 N  NZ  . LYS   A 234 ? 3.2034 2.0299 1.3592 0.3054  -0.1795 -0.1449 254 LYS   A NZ  
1632 N  N   . ARG   A 235 ? 3.3047 2.1136 1.6064 0.2527  -0.1316 -0.1804 255 ARG   A N   
1633 C  CA  . ARG   A 235 ? 3.4382 2.1491 1.6498 0.2645  -0.1478 -0.2062 255 ARG   A CA  
1634 C  C   . ARG   A 235 ? 3.5322 2.1924 1.7163 0.3010  -0.0822 -0.2053 255 ARG   A C   
1635 O  O   . ARG   A 235 ? 3.6245 2.2157 1.7255 0.3342  -0.0632 -0.2113 255 ARG   A O   
1636 C  CB  . ARG   A 235 ? 3.5090 2.1938 1.7314 0.2183  -0.2206 -0.2341 255 ARG   A CB  
1637 C  CG  . ARG   A 235 ? 3.5547 2.2836 1.8023 0.1830  -0.2924 -0.2364 255 ARG   A CG  
1638 C  CD  . ARG   A 235 ? 3.6182 2.3246 1.8908 0.1351  -0.3599 -0.2604 255 ARG   A CD  
1639 N  NE  . ARG   A 235 ? 3.6668 2.4261 1.9800 0.1006  -0.4278 -0.2596 255 ARG   A NE  
1640 C  CZ  . ARG   A 235 ? 3.7728 2.4974 2.0261 0.1044  -0.4677 -0.2709 255 ARG   A CZ  
1641 N  NH1 . ARG   A 235 ? 3.8445 2.4779 1.9874 0.1410  -0.4483 -0.2842 255 ARG   A NH1 
1642 N  NH2 . ARG   A 235 ? 3.7664 2.5511 2.0739 0.0719  -0.5280 -0.2677 255 ARG   A NH2 
1643 N  N   . MET   A 236 ? 3.3405 2.0374 1.5964 0.2970  -0.0465 -0.1963 256 MET   A N   
1644 C  CA  . MET   A 236 ? 3.2857 1.9488 1.5395 0.3288  0.0143  -0.1930 256 MET   A CA  
1645 C  C   . MET   A 236 ? 3.2791 1.9275 1.4890 0.3784  0.0740  -0.1731 256 MET   A C   
1646 O  O   . MET   A 236 ? 3.2436 1.9567 1.4991 0.3932  0.1166  -0.1431 256 MET   A O   
1647 C  CB  . MET   A 236 ? 3.2233 1.9636 1.5945 0.3171  0.0478  -0.1740 256 MET   A CB  
1648 C  CG  . MET   A 236 ? 3.1571 1.8983 1.5950 0.2776  0.0107  -0.1873 256 MET   A CG  
1649 S  SD  . MET   A 236 ? 3.2726 2.1456 1.8713 0.2184  -0.0303 -0.1661 256 MET   A SD  
1650 C  CE  . MET   A 236 ? 2.9364 1.7809 1.5819 0.1824  -0.0620 -0.1817 256 MET   A CE  
1651 N  N   . LYS   A 237 ? 3.3667 1.9286 1.4894 0.4028  0.0762  -0.1887 257 LYS   A N   
1652 C  CA  . LYS   A 237 ? 3.3764 1.9107 1.4452 0.4507  0.1299  -0.1721 257 LYS   A CA  
1653 C  C   . LYS   A 237 ? 3.4422 1.9391 1.5078 0.4827  0.1823  -0.1694 257 LYS   A C   
1654 O  O   . LYS   A 237 ? 3.4242 1.9520 1.5178 0.5162  0.2477  -0.1405 257 LYS   A O   
1655 C  CB  . LYS   A 237 ? 3.3966 1.8582 1.3510 0.4590  0.0892  -0.1901 257 LYS   A CB  
1656 C  CG  . LYS   A 237 ? 3.4189 1.7861 1.2975 0.4473  0.0372  -0.2276 257 LYS   A CG  
1657 C  CD  . LYS   A 237 ? 3.3690 1.7416 1.2604 0.3948  -0.0482 -0.2512 257 LYS   A CD  
1658 C  CE  . LYS   A 237 ? 3.3810 1.7768 1.3530 0.3574  -0.0671 -0.2609 257 LYS   A CE  
1659 N  NZ  . LYS   A 237 ? 3.4399 1.7940 1.4109 0.3824  -0.0193 -0.2624 257 LYS   A NZ  
1660 N  N   . GLU   A 238 ? 3.4842 1.9200 1.5252 0.4714  0.1543  -0.1967 258 GLU   A N   
1661 C  CA  . GLU   A 238 ? 3.4775 1.8759 1.5183 0.5002  0.1979  -0.1960 258 GLU   A CA  
1662 C  C   . GLU   A 238 ? 3.5416 1.9059 1.5188 0.5521  0.2519  -0.1802 258 GLU   A C   
1663 O  O   . GLU   A 238 ? 3.5546 1.9527 1.5813 0.5819  0.3159  -0.1544 258 GLU   A O   
1664 C  CB  . GLU   A 238 ? 3.4534 1.9297 1.6159 0.4942  0.2361  -0.1759 258 GLU   A CB  
1665 C  CG  . GLU   A 238 ? 3.4880 1.9894 1.7092 0.4452  0.1860  -0.1919 258 GLU   A CG  
1666 C  CD  . GLU   A 238 ? 3.6556 2.0706 1.8269 0.4258  0.1362  -0.2257 258 GLU   A CD  
1667 O  OE1 . GLU   A 238 ? 3.6961 2.0487 1.8246 0.4549  0.1595  -0.2316 258 GLU   A OE1 
1668 O  OE2 . GLU   A 238 ? 3.7564 2.1674 1.9349 0.3803  0.0729  -0.2448 258 GLU   A OE2 
1669 N  N   . SER   A 239 ? 3.5314 1.8291 1.4001 0.5625  0.2241  -0.1949 259 SER   A N   
1670 C  CA  . SER   A 239 ? 3.5577 1.8102 1.3484 0.6120  0.2699  -0.1827 259 SER   A CA  
1671 C  C   . SER   A 239 ? 3.5299 1.6801 1.1846 0.6182  0.2218  -0.2128 259 SER   A C   
1672 O  O   . SER   A 239 ? 3.5475 1.6786 1.1798 0.5812  0.1516  -0.2380 259 SER   A O   
1673 C  CB  . SER   A 239 ? 3.5402 1.8657 1.3726 0.6272  0.3142  -0.1457 259 SER   A CB  
1674 O  OG  . SER   A 239 ? 3.4942 1.9093 1.4503 0.6269  0.3645  -0.1156 259 SER   A OG  
1675 N  N   . ASP   A 250 ? 2.3224 1.3977 1.4247 0.5145  0.5083  0.0140  270 ASP   A N   
1676 C  CA  . ASP   A 250 ? 2.4836 1.5050 1.4914 0.4887  0.4618  -0.0140 270 ASP   A CA  
1677 C  C   . ASP   A 250 ? 2.5075 1.6051 1.5555 0.4640  0.4547  0.0035  270 ASP   A C   
1678 O  O   . ASP   A 250 ? 2.5600 1.6686 1.5869 0.4904  0.4972  0.0195  270 ASP   A O   
1679 C  CB  . ASP   A 250 ? 2.6505 1.5705 1.5205 0.5139  0.4632  -0.0350 270 ASP   A CB  
1680 C  CG  . ASP   A 250 ? 2.7130 1.5566 1.4782 0.4880  0.4051  -0.0720 270 ASP   A CG  
1681 O  OD1 . ASP   A 250 ? 2.6394 1.5304 1.4602 0.4413  0.3583  -0.0734 270 ASP   A OD1 
1682 O  OD2 . ASP   A 250 ? 2.7879 1.5502 1.4449 0.5010  0.3929  -0.0902 270 ASP   A OD2 
1683 N  N   . PHE   A 251 ? 2.3567 1.5055 1.4628 0.4141  0.4019  0.0020  271 PHE   A N   
1684 C  CA  . PHE   A 251 ? 2.2874 1.5082 1.4372 0.3901  0.3916  0.0179  271 PHE   A CA  
1685 C  C   . PHE   A 251 ? 2.4552 1.6209 1.4894 0.3983  0.3833  0.0043  271 PHE   A C   
1686 O  O   . PHE   A 251 ? 2.5228 1.7221 1.5609 0.4077  0.4082  0.0233  271 PHE   A O   
1687 C  CB  . PHE   A 251 ? 2.1807 1.4608 1.4092 0.3391  0.3377  0.0169  271 PHE   A CB  
1688 C  CG  . PHE   A 251 ? 2.0907 1.4326 1.3514 0.3140  0.3191  0.0276  271 PHE   A CG  
1689 C  CD1 . PHE   A 251 ? 2.0489 1.4728 1.4031 0.3131  0.3452  0.0558  271 PHE   A CD1 
1690 C  CD2 . PHE   A 251 ? 2.1115 1.4288 1.3123 0.2909  0.2730  0.0095  271 PHE   A CD2 
1691 C  CE1 . PHE   A 251 ? 1.9164 1.3896 1.2969 0.2920  0.3280  0.0648  271 PHE   A CE1 
1692 C  CE2 . PHE   A 251 ? 2.0378 1.4111 1.2693 0.2714  0.2564  0.0202  271 PHE   A CE2 
1693 C  CZ  . PHE   A 251 ? 1.9336 1.3818 1.2522 0.2729  0.2849  0.0473  271 PHE   A CZ  
1694 N  N   . LEU   A 252 ? 2.5218 1.6002 1.4513 0.3942  0.3460  -0.0278 272 LEU   A N   
1695 C  CA  . LEU   A 252 ? 2.6397 1.6596 1.4504 0.4026  0.3309  -0.0430 272 LEU   A CA  
1696 C  C   . LEU   A 252 ? 2.7783 1.7456 1.5034 0.4574  0.3920  -0.0366 272 LEU   A C   
1697 O  O   . LEU   A 252 ? 2.8495 1.8312 1.5497 0.4637  0.3999  -0.0215 272 LEU   A O   
1698 C  CB  . LEU   A 252 ? 2.7186 1.6553 1.4422 0.3829  0.2716  -0.0803 272 LEU   A CB  
1699 C  CG  . LEU   A 252 ? 2.9049 1.7602 1.4853 0.3959  0.2498  -0.1024 272 LEU   A CG  
1700 C  CD1 . LEU   A 252 ? 2.8775 1.7936 1.4820 0.3682  0.2164  -0.0919 272 LEU   A CD1 
1701 C  CD2 . LEU   A 252 ? 2.9976 1.7537 1.4892 0.3836  0.1991  -0.1414 272 LEU   A CD2 
1702 N  N   . GLN   A 253 ? 2.8545 1.7873 1.5779 0.4837  0.4202  -0.0363 273 GLN   A N   
1703 C  CA  . GLN   A 253 ? 2.9646 1.8734 1.6490 0.5215  0.4623  -0.0193 273 GLN   A CA  
1704 C  C   . GLN   A 253 ? 2.9440 1.9427 1.7262 0.5317  0.5132  0.0233  273 GLN   A C   
1705 O  O   . GLN   A 253 ? 2.9625 1.9595 1.7119 0.5471  0.5333  0.0401  273 GLN   A O   
1706 C  CB  . GLN   A 253 ? 2.9399 1.7932 1.6012 0.5466  0.4789  -0.0286 273 GLN   A CB  
1707 C  CG  . GLN   A 253 ? 3.0007 1.8295 1.6230 0.5887  0.5269  -0.0101 273 GLN   A CG  
1708 C  CD  . GLN   A 253 ? 2.9631 1.8704 1.7016 0.6063  0.5830  0.0274  273 GLN   A CD  
1709 O  OE1 . GLN   A 253 ? 2.9495 1.8727 1.7486 0.6085  0.5905  0.0279  273 GLN   A OE1 
1710 N  NE2 . GLN   A 253 ? 2.9949 1.9520 1.7688 0.6175  0.6199  0.0598  273 GLN   A NE2 
1711 N  N   . LEU   A 254 ? 2.8096 1.8861 1.7152 0.5218  0.5315  0.0418  274 LEU   A N   
1712 C  CA  . LEU   A 254 ? 2.7886 1.9550 1.8023 0.5244  0.5724  0.0824  274 LEU   A CA  
1713 C  C   . LEU   A 254 ? 2.7516 1.9707 1.7966 0.4959  0.5539  0.0908  274 LEU   A C   
1714 O  O   . LEU   A 254 ? 2.6483 1.9486 1.8033 0.4758  0.5578  0.1086  274 LEU   A O   
1715 C  CB  . LEU   A 254 ? 2.7136 1.9428 1.8493 0.5236  0.5925  0.0987  274 LEU   A CB  
1716 C  CG  . LEU   A 254 ? 2.7447 1.9452 1.8765 0.5563  0.6241  0.1044  274 LEU   A CG  
1717 C  CD1 . LEU   A 254 ? 2.5979 1.8650 1.8545 0.5512  0.6330  0.1190  274 LEU   A CD1 
1718 C  CD2 . LEU   A 254 ? 2.8018 2.0055 1.9220 0.5838  0.6689  0.1322  274 LEU   A CD2 
1719 N  N   . MET   A 255 ? 2.8256 1.9961 1.7704 0.4949  0.5307  0.0779  275 MET   A N   
1720 C  CA  . MET   A 255 ? 2.8406 2.0532 1.8012 0.4722  0.5128  0.0875  275 MET   A CA  
1721 C  C   . MET   A 255 ? 2.9763 2.1325 1.8295 0.4865  0.5046  0.0842  275 MET   A C   
1722 O  O   . MET   A 255 ? 2.9190 2.1080 1.7885 0.4807  0.5081  0.1037  275 MET   A O   
1723 C  CB  . MET   A 255 ? 2.7605 1.9876 1.7288 0.4372  0.4629  0.0650  275 MET   A CB  
1724 C  CG  . MET   A 255 ? 2.6245 1.9310 1.6733 0.4056  0.4433  0.0847  275 MET   A CG  
1725 S  SD  . MET   A 255 ? 2.5562 1.9363 1.7231 0.3527  0.3845  0.0769  275 MET   A SD  
1726 C  CE  . MET   A 255 ? 2.4428 1.7640 1.5140 0.3306  0.3148  0.0408  275 MET   A CE  
1727 N  N   . ILE   A 256 ? 2.9787 2.0475 1.7222 0.5059  0.4926  0.0599  276 ILE   A N   
1728 C  CA  . ILE   A 256 ? 3.0321 2.0418 1.6704 0.5255  0.4884  0.0574  276 ILE   A CA  
1729 C  C   . ILE   A 256 ? 3.0875 2.0892 1.7291 0.5629  0.5480  0.0839  276 ILE   A C   
1730 O  O   . ILE   A 256 ? 3.1399 2.0756 1.6823 0.5895  0.5544  0.0797  276 ILE   A O   
1731 C  CB  . ILE   A 256 ? 3.0497 1.9665 1.5645 0.5250  0.4386  0.0168  276 ILE   A CB  
1732 C  CG1 . ILE   A 256 ? 3.0205 1.9041 1.5380 0.5259  0.4349  -0.0046 276 ILE   A CG1 
1733 C  CG2 . ILE   A 256 ? 2.9921 1.9145 1.4815 0.4909  0.3764  -0.0017 276 ILE   A CG2 
1734 C  CD1 . ILE   A 256 ? 3.0081 1.7982 1.4134 0.5198  0.3810  -0.0455 276 ILE   A CD1 
1735 N  N   . ASP   A 257 ? 3.1401 2.2102 1.8975 0.5649  0.5903  0.1121  277 ASP   A N   
1736 C  CA  . ASP   A 257 ? 3.1659 2.2458 1.9483 0.5959  0.6478  0.1438  277 ASP   A CA  
1737 C  C   . ASP   A 257 ? 3.1256 2.2179 1.8975 0.6014  0.6641  0.1682  277 ASP   A C   
1738 O  O   . ASP   A 257 ? 3.0983 2.1872 1.8722 0.6292  0.7109  0.1940  277 ASP   A O   
1739 C  CB  . ASP   A 257 ? 3.1150 2.2760 2.0390 0.5897  0.6802  0.1694  277 ASP   A CB  
1740 C  CG  . ASP   A 257 ? 3.0660 2.2094 1.9987 0.5947  0.6759  0.1509  277 ASP   A CG  
1741 O  OD1 . ASP   A 257 ? 3.0474 2.1522 1.9292 0.5795  0.6325  0.1171  277 ASP   A OD1 
1742 O  OD2 . ASP   A 257 ? 3.0325 2.2007 2.0254 0.6134  0.7148  0.1710  277 ASP   A OD2 
1743 N  N   . SER   A 258 ? 3.0173 2.1236 1.7786 0.5765  0.6274  0.1618  278 SER   A N   
1744 C  CA  . SER   A 258 ? 2.9399 2.0577 1.6924 0.5795  0.6382  0.1843  278 SER   A CA  
1745 C  C   . SER   A 258 ? 2.9583 1.9996 1.5939 0.6169  0.6569  0.1847  278 SER   A C   
1746 O  O   . SER   A 258 ? 2.9799 1.9688 1.5141 0.6190  0.6229  0.1667  278 SER   A O   
1747 C  CB  . SER   A 258 ? 2.9150 2.0456 1.6522 0.5492  0.5861  0.1704  278 SER   A CB  
1748 O  OG  . SER   A 258 ? 2.8708 2.0558 1.6905 0.5170  0.5623  0.1619  278 SER   A OG  
1749 N  N   . SER   A 266 ? 2.7209 2.0664 1.8314 0.5748  0.8313  0.4068  286 SER   A N   
1750 C  CA  . SER   A 266 ? 2.6792 2.0906 1.9257 0.5635  0.8612  0.4302  286 SER   A CA  
1751 C  C   . SER   A 266 ? 2.6824 2.1587 2.0364 0.5212  0.8273  0.4257  286 SER   A C   
1752 O  O   . SER   A 266 ? 2.6715 2.2040 2.1383 0.5067  0.8372  0.4364  286 SER   A O   
1753 C  CB  . SER   A 266 ? 2.6728 2.0727 1.9135 0.5844  0.8793  0.4209  286 SER   A CB  
1754 O  OG  . SER   A 266 ? 2.7324 2.1407 1.9798 0.5660  0.8384  0.3893  286 SER   A OG  
1755 N  N   . HIS   A 267 ? 2.7422 2.2096 2.0583 0.5027  0.7858  0.4100  287 HIS   A N   
1756 C  CA  . HIS   A 267 ? 2.7672 2.2873 2.1667 0.4647  0.7501  0.4030  287 HIS   A CA  
1757 C  C   . HIS   A 267 ? 2.7588 2.2986 2.1871 0.4541  0.7282  0.3781  287 HIS   A C   
1758 O  O   . HIS   A 267 ? 2.6169 2.2133 2.1461 0.4259  0.7133  0.3793  287 HIS   A O   
1759 C  CB  . HIS   A 267 ? 2.6192 2.1988 2.1473 0.4435  0.7705  0.4357  287 HIS   A CB  
1760 C  CG  . HIS   A 267 ? 2.5049 2.1288 2.1062 0.4061  0.7337  0.4308  287 HIS   A CG  
1761 N  ND1 . HIS   A 267 ? 2.4841 2.0883 2.0253 0.3957  0.6940  0.4131  287 HIS   A ND1 
1762 C  CD2 . HIS   A 267 ? 2.3946 2.0801 2.1236 0.3776  0.7299  0.4421  287 HIS   A CD2 
1763 C  CE1 . HIS   A 267 ? 2.3647 2.0148 1.9913 0.3639  0.6705  0.4143  287 HIS   A CE1 
1764 N  NE2 . HIS   A 267 ? 2.3596 2.0580 2.0995 0.3518  0.6905  0.4306  287 HIS   A NE2 
1765 N  N   . LYS   A 268 ? 2.8467 2.3367 2.1842 0.4767  0.7250  0.3549  288 LYS   A N   
1766 C  CA  . LYS   A 268 ? 2.8661 2.3658 2.2198 0.4695  0.7059  0.3308  288 LYS   A CA  
1767 C  C   . LYS   A 268 ? 2.9920 2.4211 2.2115 0.4845  0.6782  0.2963  288 LYS   A C   
1768 O  O   . LYS   A 268 ? 2.9742 2.3704 2.1537 0.5027  0.6855  0.2813  288 LYS   A O   
1769 C  CB  . LYS   A 268 ? 2.7919 2.3152 2.2144 0.4830  0.7436  0.3458  288 LYS   A CB  
1770 C  CG  . LYS   A 268 ? 2.6456 2.2467 2.2166 0.4613  0.7592  0.3746  288 LYS   A CG  
1771 C  CD  . LYS   A 268 ? 2.6370 2.2582 2.2675 0.4786  0.7959  0.3913  288 LYS   A CD  
1772 C  CE  . LYS   A 268 ? 2.5509 2.2483 2.3289 0.4558  0.8071  0.4205  288 LYS   A CE  
1773 N  NZ  . LYS   A 268 ? 2.5023 2.2249 2.3443 0.4721  0.8406  0.4389  288 LYS   A NZ  
1774 N  N   . ALA   A 269 ? 3.1406 2.5441 2.2896 0.4765  0.6432  0.2834  289 ALA   A N   
1775 C  CA  . ALA   A 269 ? 3.1363 2.4717 2.1572 0.4877  0.6096  0.2510  289 ALA   A CA  
1776 C  C   . ALA   A 269 ? 3.0817 2.4332 2.1100 0.4600  0.5609  0.2238  289 ALA   A C   
1777 O  O   . ALA   A 269 ? 3.0772 2.4894 2.2066 0.4367  0.5591  0.2293  289 ALA   A O   
1778 C  CB  . ALA   A 269 ? 3.1408 2.4344 2.0723 0.4991  0.5986  0.2545  289 ALA   A CB  
1779 N  N   . LEU   A 270 ? 2.8504 2.1464 1.7704 0.4622  0.5193  0.1944  290 LEU   A N   
1780 C  CA  . LEU   A 270 ? 2.6747 1.9775 1.5865 0.4368  0.4690  0.1674  290 LEU   A CA  
1781 C  C   . LEU   A 270 ? 2.6690 1.9065 1.4565 0.4406  0.4207  0.1397  290 LEU   A C   
1782 O  O   . LEU   A 270 ? 2.6936 1.8651 1.3959 0.4601  0.4185  0.1201  290 LEU   A O   
1783 C  CB  . LEU   A 270 ? 2.5809 1.8895 1.5293 0.4337  0.4763  0.1527  290 LEU   A CB  
1784 C  CG  . LEU   A 270 ? 2.5156 1.8157 1.4375 0.4106  0.4254  0.1215  290 LEU   A CG  
1785 C  CD1 . LEU   A 270 ? 2.4329 1.8026 1.4750 0.3872  0.4290  0.1273  290 LEU   A CD1 
1786 C  CD2 . LEU   A 270 ? 2.6022 1.8224 1.4255 0.4260  0.4103  0.0901  290 LEU   A CD2 
1787 N  N   . SER   A 271 ? 2.6274 1.8827 1.4062 0.4223  0.3796  0.1388  291 SER   A N   
1788 C  CA  . SER   A 271 ? 2.6676 1.8709 1.3424 0.4218  0.3254  0.1134  291 SER   A CA  
1789 C  C   . SER   A 271 ? 2.7322 1.9121 1.3788 0.4053  0.2837  0.0787  291 SER   A C   
1790 O  O   . SER   A 271 ? 2.6039 1.8121 1.3119 0.3932  0.2956  0.0755  291 SER   A O   
1791 C  CB  . SER   A 271 ? 2.6035 1.8402 1.2894 0.4065  0.2895  0.1237  291 SER   A CB  
1792 O  OG  . SER   A 271 ? 2.5764 1.8566 1.3097 0.3765  0.2486  0.1137  291 SER   A OG  
1793 N  N   . ASP   A 272 ? 2.9818 2.1074 1.5349 0.4040  0.2325  0.0526  292 ASP   A N   
1794 C  CA  . ASP   A 272 ? 2.9940 2.0949 1.5204 0.3823  0.1818  0.0187  292 ASP   A CA  
1795 C  C   . ASP   A 272 ? 2.8061 1.9806 1.4254 0.3459  0.1498  0.0209  292 ASP   A C   
1796 O  O   . ASP   A 272 ? 2.7978 1.9939 1.4838 0.3223  0.1367  0.0072  292 ASP   A O   
1797 C  CB  . ASP   A 272 ? 3.0129 2.0533 1.4395 0.3819  0.1249  -0.0064 292 ASP   A CB  
1798 C  CG  . ASP   A 272 ? 3.0821 2.1138 1.5023 0.3487  0.0586  -0.0374 292 ASP   A CG  
1799 O  OD1 . ASP   A 272 ? 3.1756 2.1884 1.6072 0.3412  0.0649  -0.0533 292 ASP   A OD1 
1800 O  OD2 . ASP   A 272 ? 2.9884 2.0348 1.3995 0.3292  -0.0001 -0.0445 292 ASP   A OD2 
1801 N  N   . LEU   A 273 ? 2.6446 1.8718 1.3057 0.3359  0.1327  0.0394  293 LEU   A N   
1802 C  CA  . LEU   A 273 ? 2.4802 1.7956 1.2702 0.2983  0.1017  0.0434  293 LEU   A CA  
1803 C  C   . LEU   A 273 ? 2.3843 1.7558 1.2893 0.2905  0.1460  0.0589  293 LEU   A C   
1804 O  O   . LEU   A 273 ? 2.3293 1.7504 1.3236 0.2609  0.1244  0.0512  293 LEU   A O   
1805 C  CB  . LEU   A 273 ? 2.4668 1.8213 1.2734 0.2967  0.0821  0.0619  293 LEU   A CB  
1806 C  CG  . LEU   A 273 ? 2.4939 1.8198 1.2224 0.2937  0.0192  0.0463  293 LEU   A CG  
1807 C  CD1 . LEU   A 273 ? 2.4686 1.8398 1.2275 0.2957  0.0060  0.0689  293 LEU   A CD1 
1808 C  CD2 . LEU   A 273 ? 2.4886 1.8345 1.2577 0.2579  -0.0377 0.0195  293 LEU   A CD2 
1809 N  N   . GLU   A 274 ? 2.3895 1.7543 1.2937 0.3169  0.2077  0.0823  294 GLU   A N   
1810 C  CA  . GLU   A 274 ? 2.2681 1.6831 1.2792 0.3115  0.2492  0.0975  294 GLU   A CA  
1811 C  C   . GLU   A 274 ? 2.2130 1.6094 1.2330 0.3060  0.2480  0.0766  294 GLU   A C   
1812 O  O   . GLU   A 274 ? 2.0883 1.5377 1.2071 0.2821  0.2398  0.0757  294 GLU   A O   
1813 C  CB  . GLU   A 274 ? 2.2939 1.6993 1.2963 0.3422  0.3162  0.1273  294 GLU   A CB  
1814 C  CG  . GLU   A 274 ? 2.3036 1.7311 1.3153 0.3459  0.3248  0.1544  294 GLU   A CG  
1815 C  CD  . GLU   A 274 ? 2.2965 1.7488 1.3671 0.3593  0.3892  0.1889  294 GLU   A CD  
1816 O  OE1 . GLU   A 274 ? 2.3775 1.8284 1.4763 0.3699  0.4269  0.1910  294 GLU   A OE1 
1817 O  OE2 . GLU   A 274 ? 2.2229 1.7003 1.3273 0.3563  0.3967  0.2128  294 GLU   A OE2 
1818 N  N   . LEU   A 275 ? 2.3451 1.6606 1.2559 0.3299  0.2555  0.0593  295 LEU   A N   
1819 C  CA  . LEU   A 275 ? 2.3270 1.6087 1.2286 0.3256  0.2466  0.0355  295 LEU   A CA  
1820 C  C   . LEU   A 275 ? 2.2076 1.5253 1.1683 0.2831  0.1862  0.0183  295 LEU   A C   
1821 O  O   . LEU   A 275 ? 2.1329 1.4836 1.1732 0.2659  0.1866  0.0169  295 LEU   A O   
1822 C  CB  . LEU   A 275 ? 2.4817 1.6583 1.2350 0.3545  0.2462  0.0128  295 LEU   A CB  
1823 C  CG  . LEU   A 275 ? 2.5199 1.6257 1.2191 0.3677  0.2522  -0.0122 295 LEU   A CG  
1824 C  CD1 . LEU   A 275 ? 2.4702 1.5903 1.2280 0.3293  0.2036  -0.0327 295 LEU   A CD1 
1825 C  CD2 . LEU   A 275 ? 2.6708 1.7746 1.3913 0.4029  0.3256  0.0060  295 LEU   A CD2 
1826 N  N   . VAL   A 276 ? 2.2464 1.5607 1.1708 0.2664  0.1342  0.0074  296 VAL   A N   
1827 C  CA  . VAL   A 276 ? 2.1983 1.5475 1.1777 0.2263  0.0777  -0.0072 296 VAL   A CA  
1828 C  C   . VAL   A 276 ? 2.0977 1.5435 1.2104 0.2037  0.0830  0.0124  296 VAL   A C   
1829 O  O   . VAL   A 276 ? 1.9985 1.4767 1.1805 0.1783  0.0675  0.0072  296 VAL   A O   
1830 C  CB  . VAL   A 276 ? 2.3290 1.6595 1.2462 0.2155  0.0211  -0.0203 296 VAL   A CB  
1831 C  CG1 . VAL   A 276 ? 2.3549 1.7271 1.3385 0.1731  -0.0339 -0.0323 296 VAL   A CG1 
1832 C  CG2 . VAL   A 276 ? 2.6195 1.8458 1.3931 0.2393  0.0128  -0.0423 296 VAL   A CG2 
1833 N  N   . ALA   A 277 ? 2.1425 1.6302 1.2878 0.2137  0.1057  0.0354  297 ALA   A N   
1834 C  CA  . ALA   A 277 ? 1.9646 1.5364 1.2260 0.1947  0.1087  0.0520  297 ALA   A CA  
1835 C  C   . ALA   A 277 ? 1.8943 1.4912 1.2295 0.1907  0.1384  0.0574  297 ALA   A C   
1836 O  O   . ALA   A 277 ? 1.7885 1.4425 1.2087 0.1668  0.1234  0.0595  297 ALA   A O   
1837 C  CB  . ALA   A 277 ? 1.8881 1.4831 1.1600 0.2102  0.1329  0.0756  297 ALA   A CB  
1838 N  N   . GLN   A 278 ? 1.8044 1.3602 1.1076 0.2159  0.1807  0.0606  298 GLN   A N   
1839 C  CA  . GLN   A 278 ? 1.7254 1.3023 1.0963 0.2140  0.2042  0.0649  298 GLN   A CA  
1840 C  C   . GLN   A 278 ? 1.7808 1.3302 1.1387 0.1977  0.1738  0.0429  298 GLN   A C   
1841 O  O   . GLN   A 278 ? 1.7161 1.3028 1.1481 0.1810  0.1693  0.0452  298 GLN   A O   
1842 C  CB  . GLN   A 278 ? 1.7547 1.3015 1.1033 0.2486  0.2612  0.0778  298 GLN   A CB  
1843 C  CG  . GLN   A 278 ? 1.8341 1.3846 1.1652 0.2685  0.2941  0.0995  298 GLN   A CG  
1844 C  CD  . GLN   A 278 ? 1.6654 1.2864 1.0827 0.2486  0.2854  0.1168  298 GLN   A CD  
1845 O  OE1 . GLN   A 278 ? 1.5650 1.2408 1.0780 0.2318  0.2847  0.1234  298 GLN   A OE1 
1846 N  NE2 . GLN   A 278 ? 1.7238 1.3390 1.1026 0.2521  0.2771  0.1238  298 GLN   A NE2 
1847 N  N   . SER   A 279 ? 1.8134 1.2939 1.0750 0.2017  0.1506  0.0218  299 SER   A N   
1848 C  CA  . SER   A 279 ? 1.8265 1.2709 1.0713 0.1841  0.1195  0.0006  299 SER   A CA  
1849 C  C   . SER   A 279 ? 1.7156 1.2187 1.0322 0.1437  0.0751  -0.0004 299 SER   A C   
1850 O  O   . SER   A 279 ? 1.5956 1.1035 0.9513 0.1247  0.0626  -0.0051 299 SER   A O   
1851 C  CB  . SER   A 279 ? 1.9746 1.3285 1.0966 0.1950  0.0983  -0.0234 299 SER   A CB  
1852 O  OG  . SER   A 279 ? 2.0494 1.3506 1.0945 0.2364  0.1422  -0.0204 299 SER   A OG  
1853 N  N   . ILE   A 280 ? 1.6700 1.2177 1.0044 0.1320  0.0531  0.0056  300 ILE   A N   
1854 C  CA  . ILE   A 280 ? 1.6520 1.2607 1.0559 0.0973  0.0152  0.0067  300 ILE   A CA  
1855 C  C   . ILE   A 280 ? 1.5797 1.2507 1.0812 0.0883  0.0350  0.0219  300 ILE   A C   
1856 O  O   . ILE   A 280 ? 1.5356 1.2343 1.0856 0.0626  0.0142  0.0206  300 ILE   A O   
1857 C  CB  . ILE   A 280 ? 1.6734 1.3176 1.0764 0.0941  -0.0075 0.0119  300 ILE   A CB  
1858 C  CG1 . ILE   A 280 ? 1.7152 1.2963 1.0185 0.1001  -0.0373 -0.0048 300 ILE   A CG1 
1859 C  CG2 . ILE   A 280 ? 1.6371 1.3546 1.1224 0.0633  -0.0380 0.0167  300 ILE   A CG2 
1860 C  CD1 . ILE   A 280 ? 1.8472 1.4575 1.1416 0.1019  -0.0606 0.0016  300 ILE   A CD1 
1861 N  N   . ILE   A 281 ? 1.6010 1.2932 1.1313 0.1088  0.0748  0.0376  301 ILE   A N   
1862 C  CA  . ILE   A 281 ? 1.4709 1.2189 1.0893 0.1018  0.0905  0.0511  301 ILE   A CA  
1863 C  C   . ILE   A 281 ? 1.4241 1.1462 1.0506 0.1013  0.0989  0.0470  301 ILE   A C   
1864 O  O   . ILE   A 281 ? 1.3630 1.1176 1.0430 0.0816  0.0854  0.0496  301 ILE   A O   
1865 C  CB  . ILE   A 281 ? 1.4111 1.1843 1.0598 0.1218  0.1275  0.0689  301 ILE   A CB  
1866 C  CG1 . ILE   A 281 ? 1.3878 1.1819 1.0277 0.1226  0.1179  0.0744  301 ILE   A CG1 
1867 C  CG2 . ILE   A 281 ? 1.3109 1.1373 1.0476 0.1142  0.1384  0.0808  301 ILE   A CG2 
1868 C  CD1 . ILE   A 281 ? 1.3196 1.1661 1.0045 0.0983  0.0829  0.0724  301 ILE   A CD1 
1869 N  N   . PHE   A 282 ? 1.4871 1.1475 1.0567 0.1255  0.1227  0.0416  302 PHE   A N   
1870 C  CA  . PHE   A 282 ? 1.4978 1.1289 1.0739 0.1313  0.1346  0.0390  302 PHE   A CA  
1871 C  C   . PHE   A 282 ? 1.4839 1.0893 1.0457 0.1047  0.0964  0.0246  302 PHE   A C   
1872 O  O   . PHE   A 282 ? 1.3600 0.9727 0.9622 0.0956  0.0950  0.0287  302 PHE   A O   
1873 C  CB  . PHE   A 282 ? 1.6160 1.1808 1.1250 0.1670  0.1694  0.0347  302 PHE   A CB  
1874 C  CG  . PHE   A 282 ? 1.6096 1.2059 1.1617 0.1929  0.2164  0.0554  302 PHE   A CG  
1875 C  CD1 . PHE   A 282 ? 1.5726 1.2153 1.1541 0.1934  0.2270  0.0700  302 PHE   A CD1 
1876 C  CD2 . PHE   A 282 ? 1.6382 1.2172 1.2050 0.2167  0.2495  0.0616  302 PHE   A CD2 
1877 C  CE1 . PHE   A 282 ? 1.6099 1.2820 1.2383 0.2131  0.2688  0.0909  302 PHE   A CE1 
1878 C  CE2 . PHE   A 282 ? 1.6457 1.2607 1.2634 0.2385  0.2918  0.0831  302 PHE   A CE2 
1879 C  CZ  . PHE   A 282 ? 1.6075 1.2690 1.2572 0.2348  0.3011  0.0979  302 PHE   A CZ  
1880 N  N   . ILE   A 283 ? 1.5254 1.1007 1.0321 0.0909  0.0636  0.0094  303 ILE   A N   
1881 C  CA  . ILE   A 283 ? 1.5081 1.0593 1.0066 0.0612  0.0249  -0.0029 303 ILE   A CA  
1882 C  C   . ILE   A 283 ? 1.4182 1.0465 1.0032 0.0306  0.0069  0.0103  303 ILE   A C   
1883 O  O   . ILE   A 283 ? 1.4853 1.1123 1.1003 0.0133  -0.0015 0.0132  303 ILE   A O   
1884 C  CB  . ILE   A 283 ? 1.5828 1.0872 1.0059 0.0527  -0.0101 -0.0220 303 ILE   A CB  
1885 C  CG1 . ILE   A 283 ? 1.6833 1.0926 1.0049 0.0830  0.0052  -0.0391 303 ILE   A CG1 
1886 C  CG2 . ILE   A 283 ? 1.5855 1.0877 1.0252 0.0131  -0.0558 -0.0299 303 ILE   A CG2 
1887 C  CD1 . ILE   A 283 ? 1.8054 1.1612 1.0402 0.0784  -0.0313 -0.0596 303 ILE   A CD1 
1888 N  N   . PHE   A 284 ? 1.4161 1.1092 1.0385 0.0256  0.0026  0.0195  304 PHE   A N   
1889 C  CA  . PHE   A 284 ? 1.3434 1.1092 1.0414 0.0010  -0.0113 0.0315  304 PHE   A CA  
1890 C  C   . PHE   A 284 ? 1.3060 1.0995 1.0586 0.0060  0.0127  0.0452  304 PHE   A C   
1891 O  O   . PHE   A 284 ? 1.2478 1.0627 1.0385 -0.0142 0.0016  0.0516  304 PHE   A O   
1892 C  CB  . PHE   A 284 ? 1.3091 1.1319 1.0307 0.0022  -0.0161 0.0378  304 PHE   A CB  
1893 C  CG  . PHE   A 284 ? 1.2508 1.1469 1.0436 -0.0181 -0.0275 0.0492  304 PHE   A CG  
1894 C  CD1 . PHE   A 284 ? 1.2586 1.1777 1.0662 -0.0444 -0.0599 0.0476  304 PHE   A CD1 
1895 C  CD2 . PHE   A 284 ? 1.1947 1.1363 1.0393 -0.0104 -0.0059 0.0616  304 PHE   A CD2 
1896 C  CE1 . PHE   A 284 ? 1.2266 1.2142 1.0978 -0.0594 -0.0649 0.0597  304 PHE   A CE1 
1897 C  CE2 . PHE   A 284 ? 1.1226 1.1256 1.0218 -0.0252 -0.0144 0.0706  304 PHE   A CE2 
1898 C  CZ  . PHE   A 284 ? 1.1622 1.1889 1.0740 -0.0482 -0.0411 0.0704  304 PHE   A CZ  
1899 N  N   . ALA   A 285 ? 1.2717 1.0662 1.0300 0.0327  0.0450  0.0514  305 ALA   A N   
1900 C  CA  . ALA   A 285 ? 1.2701 1.0933 1.0827 0.0387  0.0639  0.0645  305 ALA   A CA  
1901 C  C   . ALA   A 285 ? 1.3207 1.0992 1.1221 0.0379  0.0644  0.0628  305 ALA   A C   
1902 O  O   . ALA   A 285 ? 1.3128 1.1167 1.1573 0.0279  0.0609  0.0730  305 ALA   A O   
1903 C  CB  . ALA   A 285 ? 1.2364 1.0686 1.0615 0.0661  0.0967  0.0725  305 ALA   A CB  
1904 N  N   . GLY   A 286 ? 1.3871 1.0938 1.1254 0.0504  0.0687  0.0501  306 GLY   A N   
1905 C  CA  . GLY   A 286 ? 1.4493 1.1029 1.1707 0.0525  0.0694  0.0472  306 GLY   A CA  
1906 C  C   . GLY   A 286 ? 1.4283 1.0716 1.1518 0.0185  0.0361  0.0445  306 GLY   A C   
1907 O  O   . GLY   A 286 ? 1.4850 1.1040 1.2183 0.0143  0.0351  0.0497  306 GLY   A O   
1908 N  N   . TYR   A 287 ? 1.3749 1.0379 1.0934 -0.0061 0.0088  0.0387  307 TYR   A N   
1909 C  CA  . TYR   A 287 ? 1.4341 1.0967 1.1659 -0.0418 -0.0222 0.0395  307 TYR   A CA  
1910 C  C   . TYR   A 287 ? 1.3695 1.1119 1.1740 -0.0593 -0.0237 0.0592  307 TYR   A C   
1911 O  O   . TYR   A 287 ? 1.3695 1.1104 1.1979 -0.0741 -0.0273 0.0703  307 TYR   A O   
1912 C  CB  . TYR   A 287 ? 1.4585 1.1066 1.1551 -0.0604 -0.0537 0.0249  307 TYR   A CB  
1913 C  CG  . TYR   A 287 ? 1.5410 1.2257 1.2800 -0.1006 -0.0844 0.0324  307 TYR   A CG  
1914 C  CD1 . TYR   A 287 ? 1.5559 1.1941 1.2888 -0.1255 -0.1031 0.0314  307 TYR   A CD1 
1915 C  CD2 . TYR   A 287 ? 1.4672 1.2328 1.2551 -0.1128 -0.0930 0.0422  307 TYR   A CD2 
1916 C  CE1 . TYR   A 287 ? 1.5817 1.2575 1.3607 -0.1639 -0.1281 0.0422  307 TYR   A CE1 
1917 C  CE2 . TYR   A 287 ? 1.4726 1.2781 1.3055 -0.1474 -0.1165 0.0520  307 TYR   A CE2 
1918 C  CZ  . TYR   A 287 ? 1.5207 1.2836 1.3515 -0.1741 -0.1334 0.0531  307 TYR   A CZ  
1919 O  OH  . TYR   A 287 ? 1.5848 1.3914 1.4676 -0.2106 -0.1542 0.0666  307 TYR   A OH  
1920 N  N   . GLU   A 288 ? 1.3490 1.1567 1.1839 -0.0558 -0.0199 0.0641  308 GLU   A N   
1921 C  CA  . GLU   A 288 ? 1.3206 1.2007 1.2144 -0.0716 -0.0235 0.0797  308 GLU   A CA  
1922 C  C   . GLU   A 288 ? 1.2961 1.1977 1.2226 -0.0577 -0.0027 0.0932  308 GLU   A C   
1923 O  O   . GLU   A 288 ? 1.2741 1.1910 1.2259 -0.0719 -0.0063 0.1061  308 GLU   A O   
1924 C  CB  . GLU   A 288 ? 1.2780 1.2135 1.1886 -0.0692 -0.0271 0.0788  308 GLU   A CB  
1925 C  CG  . GLU   A 288 ? 1.3343 1.2964 1.2569 -0.0960 -0.0547 0.0785  308 GLU   A CG  
1926 C  CD  . GLU   A 288 ? 1.3072 1.3125 1.2784 -0.1193 -0.0593 0.0949  308 GLU   A CD  
1927 O  OE1 . GLU   A 288 ? 1.2196 1.2495 1.2156 -0.1106 -0.0410 0.1063  308 GLU   A OE1 
1928 O  OE2 . GLU   A 288 ? 1.3129 1.3277 1.2974 -0.1466 -0.0815 0.0974  308 GLU   A OE2 
1929 N  N   . THR   A 289 ? 1.2582 1.1622 1.1856 -0.0306 0.0183  0.0921  309 THR   A N   
1930 C  CA  . THR   A 289 ? 1.2219 1.1528 1.1861 -0.0179 0.0328  0.1046  309 THR   A CA  
1931 C  C   . THR   A 289 ? 1.2157 1.1081 1.1755 -0.0182 0.0339  0.1117  309 THR   A C   
1932 O  O   . THR   A 289 ? 1.1240 1.0421 1.1123 -0.0233 0.0318  0.1254  309 THR   A O   
1933 C  CB  . THR   A 289 ? 1.1402 1.0748 1.1102 0.0092  0.0541  0.1029  309 THR   A CB  
1934 O  OG1 . THR   A 289 ? 1.2149 1.0894 1.1463 0.0261  0.0671  0.0956  309 THR   A OG1 
1935 C  CG2 . THR   A 289 ? 1.0921 1.0574 1.0628 0.0098  0.0532  0.0976  309 THR   A CG2 
1936 N  N   . THR   A 290 ? 1.2499 1.0758 1.1688 -0.0107 0.0369  0.1025  310 THR   A N   
1937 C  CA  . THR   A 290 ? 1.3105 1.0901 1.2209 -0.0086 0.0378  0.1088  310 THR   A CA  
1938 C  C   . THR   A 290 ? 1.2739 1.0576 1.1934 -0.0402 0.0179  0.1184  310 THR   A C   
1939 O  O   . THR   A 290 ? 1.1883 0.9887 1.1332 -0.0423 0.0190  0.1353  310 THR   A O   
1940 C  CB  . THR   A 290 ? 1.3517 1.0508 1.2068 0.0056  0.0435  0.0936  310 THR   A CB  
1941 O  OG1 . THR   A 290 ? 1.3414 1.0421 1.1874 0.0349  0.0662  0.0871  310 THR   A OG1 
1942 C  CG2 . THR   A 290 ? 1.3710 1.0190 1.2190 0.0157  0.0486  0.1006  310 THR   A CG2 
1943 N  N   . SER   A 291 ? 1.2985 1.0696 1.1993 -0.0655 -0.0010 0.1097  311 SER   A N   
1944 C  CA  . SER   A 291 ? 1.3243 1.0968 1.2384 -0.0986 -0.0186 0.1210  311 SER   A CA  
1945 C  C   . SER   A 291 ? 1.2163 1.0664 1.1783 -0.1079 -0.0157 0.1400  311 SER   A C   
1946 O  O   . SER   A 291 ? 1.2176 1.0707 1.1948 -0.1224 -0.0174 0.1581  311 SER   A O   
1947 C  CB  . SER   A 291 ? 1.3460 1.0998 1.2403 -0.1247 -0.0424 0.1080  311 SER   A CB  
1948 O  OG  . SER   A 291 ? 1.3141 1.1242 1.2221 -0.1240 -0.0456 0.1020  311 SER   A OG  
1949 N  N   . SER   A 292 ? 1.1801 1.0889 1.1614 -0.0985 -0.0105 0.1365  312 SER   A N   
1950 C  CA  . SER   A 292 ? 1.1418 1.1195 1.1602 -0.1039 -0.0073 0.1512  312 SER   A CA  
1951 C  C   . SER   A 292 ? 1.1016 1.0839 1.1300 -0.0885 0.0039  0.1652  312 SER   A C   
1952 O  O   . SER   A 292 ? 1.1130 1.1177 1.1549 -0.0995 0.0037  0.1829  312 SER   A O   
1953 C  CB  . SER   A 292 ? 1.1251 1.1531 1.1563 -0.0930 -0.0044 0.1420  312 SER   A CB  
1954 O  OG  . SER   A 292 ? 1.1229 1.2110 1.1830 -0.0940 -0.0002 0.1536  312 SER   A OG  
1955 N  N   . VAL   A 293 ? 1.1145 1.0770 1.1372 -0.0622 0.0136  0.1592  313 VAL   A N   
1956 C  CA  . VAL   A 293 ? 1.1156 1.0841 1.1515 -0.0463 0.0195  0.1724  313 VAL   A CA  
1957 C  C   . VAL   A 293 ? 1.1741 1.0940 1.1956 -0.0531 0.0165  0.1858  313 VAL   A C   
1958 O  O   . VAL   A 293 ? 1.1202 1.0525 1.1496 -0.0526 0.0156  0.2038  313 VAL   A O   
1959 C  CB  . VAL   A 293 ? 1.0650 1.0309 1.1097 -0.0176 0.0302  0.1646  313 VAL   A CB  
1960 C  CG1 . VAL   A 293 ? 1.0376 1.0107 1.1009 -0.0014 0.0310  0.1788  313 VAL   A CG1 
1961 C  CG2 . VAL   A 293 ? 1.1121 1.1241 1.1727 -0.0131 0.0327  0.1546  313 VAL   A CG2 
1962 N  N   . LEU   A 294 ? 1.2036 1.0623 1.1986 -0.0584 0.0141  0.1773  314 LEU   A N   
1963 C  CA  . LEU   A 294 ? 1.2431 1.0457 1.2218 -0.0664 0.0101  0.1895  314 LEU   A CA  
1964 C  C   . LEU   A 294 ? 1.2410 1.0662 1.2314 -0.0960 0.0025  0.2091  314 LEU   A C   
1965 O  O   . LEU   A 294 ? 1.1894 0.9998 1.1793 -0.0962 0.0036  0.2297  314 LEU   A O   
1966 C  CB  . LEU   A 294 ? 1.3104 1.0389 1.2526 -0.0710 0.0052  0.1730  314 LEU   A CB  
1967 C  CG  . LEU   A 294 ? 1.3245 1.0102 1.2432 -0.0386 0.0179  0.1563  314 LEU   A CG  
1968 C  CD1 . LEU   A 294 ? 1.4414 1.0472 1.3116 -0.0465 0.0096  0.1385  314 LEU   A CD1 
1969 C  CD2 . LEU   A 294 ? 1.3135 0.9850 1.2432 -0.0096 0.0300  0.1693  314 LEU   A CD2 
1970 N  N   . SER   A 295 ? 1.1768 1.0401 1.1791 -0.1197 -0.0040 0.2054  315 SER   A N   
1971 C  CA  . SER   A 295 ? 1.1526 1.0466 1.1732 -0.1472 -0.0066 0.2267  315 SER   A CA  
1972 C  C   . SER   A 295 ? 1.1415 1.0903 1.1761 -0.1338 0.0041  0.2434  315 SER   A C   
1973 O  O   . SER   A 295 ? 1.1095 1.0622 1.1458 -0.1447 0.0078  0.2677  315 SER   A O   
1974 C  CB  . SER   A 295 ? 1.1694 1.0991 1.2074 -0.1724 -0.0158 0.2192  315 SER   A CB  
1975 O  OG  . SER   A 295 ? 1.1899 1.1744 1.2391 -0.1561 -0.0114 0.2061  315 SER   A OG  
1976 N  N   . PHE   A 296 ? 1.1077 1.0954 1.1489 -0.1102 0.0085  0.2311  316 PHE   A N   
1977 C  CA  . PHE   A 296 ? 1.0755 1.1059 1.1222 -0.0951 0.0142  0.2427  316 PHE   A CA  
1978 C  C   . PHE   A 296 ? 1.0412 1.0367 1.0746 -0.0793 0.0138  0.2571  316 PHE   A C   
1979 O  O   . PHE   A 296 ? 0.9981 1.0099 1.0247 -0.0773 0.0156  0.2767  316 PHE   A O   
1980 C  CB  . PHE   A 296 ? 1.0459 1.1155 1.1031 -0.0751 0.0153  0.2243  316 PHE   A CB  
1981 C  CG  . PHE   A 296 ? 1.0392 1.1599 1.1094 -0.0849 0.0171  0.2180  316 PHE   A CG  
1982 C  CD1 . PHE   A 296 ? 0.9800 1.1420 1.0535 -0.0913 0.0228  0.2328  316 PHE   A CD1 
1983 C  CD2 . PHE   A 296 ? 1.0555 1.1823 1.1322 -0.0845 0.0147  0.1986  316 PHE   A CD2 
1984 C  CE1 . PHE   A 296 ? 0.9824 1.1932 1.0707 -0.0962 0.0266  0.2278  316 PHE   A CE1 
1985 C  CE2 . PHE   A 296 ? 1.0217 1.1956 1.1121 -0.0905 0.0154  0.1941  316 PHE   A CE2 
1986 C  CZ  . PHE   A 296 ? 1.0180 1.2352 1.1169 -0.0958 0.0216  0.2084  316 PHE   A CZ  
1987 N  N   . ILE   A 297 ? 1.0008 0.9477 1.0280 -0.0654 0.0121  0.2487  317 ILE   A N   
1988 C  CA  . ILE   A 297 ? 1.1222 1.0346 1.1409 -0.0475 0.0107  0.2635  317 ILE   A CA  
1989 C  C   . ILE   A 297 ? 1.1241 1.0008 1.1261 -0.0667 0.0099  0.2874  317 ILE   A C   
1990 O  O   . ILE   A 297 ? 1.1403 1.0160 1.1333 -0.0586 0.0089  0.3093  317 ILE   A O   
1991 C  CB  . ILE   A 297 ? 1.1271 0.9945 1.1450 -0.0266 0.0130  0.2497  317 ILE   A CB  
1992 C  CG1 . ILE   A 297 ? 1.0794 0.9863 1.1195 -0.0065 0.0165  0.2325  317 ILE   A CG1 
1993 C  CG2 . ILE   A 297 ? 1.1840 1.0102 1.1951 -0.0081 0.0113  0.2672  317 ILE   A CG2 
1994 C  CD1 . ILE   A 297 ? 1.1633 1.0324 1.2031 0.0128  0.0254  0.2184  317 ILE   A CD1 
1995 N  N   . MET   A 298 ? 1.1646 1.0096 1.1616 -0.0935 0.0087  0.2846  318 MET   A N   
1996 C  CA  . MET   A 298 ? 1.2412 1.0473 1.2275 -0.1166 0.0078  0.3086  318 MET   A CA  
1997 C  C   . MET   A 298 ? 1.2538 1.1118 1.2475 -0.1314 0.0146  0.3331  318 MET   A C   
1998 O  O   . MET   A 298 ? 1.2403 1.0750 1.2216 -0.1380 0.0179  0.3612  318 MET   A O   
1999 C  CB  . MET   A 298 ? 1.2326 0.9950 1.2163 -0.1454 0.0005  0.2975  318 MET   A CB  
2000 C  CG  . MET   A 298 ? 1.2955 0.9827 1.2558 -0.1293 -0.0040 0.2788  318 MET   A CG  
2001 S  SD  . MET   A 298 ? 1.6100 1.2311 1.5502 -0.1073 -0.0013 0.3008  318 MET   A SD  
2002 C  CE  . MET   A 298 ? 1.4515 1.0482 1.3838 -0.0629 0.0041  0.2756  318 MET   A CE  
2003 N  N   . TYR   A 299 ? 1.1983 1.1239 1.2089 -0.1346 0.0187  0.3241  319 TYR   A N   
2004 C  CA  . TYR   A 299 ? 1.2126 1.1894 1.2258 -0.1423 0.0295  0.3463  319 TYR   A CA  
2005 C  C   . TYR   A 299 ? 1.1879 1.1670 1.1761 -0.1156 0.0313  0.3616  319 TYR   A C   
2006 O  O   . TYR   A 299 ? 1.1824 1.1609 1.1546 -0.1214 0.0397  0.3909  319 TYR   A O   
2007 C  CB  . TYR   A 299 ? 1.1615 1.2068 1.1950 -0.1434 0.0337  0.3306  319 TYR   A CB  
2008 C  CG  . TYR   A 299 ? 1.1657 1.2647 1.1950 -0.1408 0.0482  0.3500  319 TYR   A CG  
2009 C  CD1 . TYR   A 299 ? 1.1916 1.3113 1.2351 -0.1672 0.0613  0.3755  319 TYR   A CD1 
2010 C  CD2 . TYR   A 299 ? 1.1393 1.2666 1.1496 -0.1117 0.0490  0.3434  319 TYR   A CD2 
2011 C  CE1 . TYR   A 299 ? 1.2151 1.3832 1.2501 -0.1609 0.0797  0.3945  319 TYR   A CE1 
2012 C  CE2 . TYR   A 299 ? 1.1770 1.3459 1.1721 -0.1056 0.0629  0.3590  319 TYR   A CE2 
2013 C  CZ  . TYR   A 299 ? 1.2236 1.4131 1.2292 -0.1284 0.0807  0.3850  319 TYR   A CZ  
2014 O  OH  . TYR   A 299 ? 1.3224 1.5533 1.3089 -0.1186 0.0996  0.4017  319 TYR   A OH  
2015 N  N   . GLU   A 300 ? 1.1601 1.1421 1.1452 -0.0864 0.0226  0.3435  320 GLU   A N   
2016 C  CA  . GLU   A 300 ? 1.1782 1.1629 1.1417 -0.0607 0.0175  0.3559  320 GLU   A CA  
2017 C  C   . GLU   A 300 ? 1.1893 1.1135 1.1352 -0.0558 0.0134  0.3783  320 GLU   A C   
2018 O  O   . GLU   A 300 ? 1.2141 1.1355 1.1341 -0.0435 0.0113  0.4010  320 GLU   A O   
2019 C  CB  . GLU   A 300 ? 1.1290 1.1352 1.1048 -0.0344 0.0064  0.3314  320 GLU   A CB  
2020 C  CG  . GLU   A 300 ? 1.1088 1.1696 1.0976 -0.0360 0.0093  0.3105  320 GLU   A CG  
2021 C  CD  . GLU   A 300 ? 1.1188 1.2189 1.0848 -0.0343 0.0147  0.3218  320 GLU   A CD  
2022 O  OE1 . GLU   A 300 ? 1.0294 1.1178 0.9655 -0.0246 0.0120  0.3428  320 GLU   A OE1 
2023 O  OE2 . GLU   A 300 ? 1.1332 1.2739 1.1075 -0.0402 0.0225  0.3101  320 GLU   A OE2 
2024 N  N   . LEU   A 301 ? 1.1965 1.0677 1.1507 -0.0630 0.0116  0.3723  321 LEU   A N   
2025 C  CA  . LEU   A 301 ? 1.3157 1.1217 1.2521 -0.0575 0.0085  0.3937  321 LEU   A CA  
2026 C  C   . LEU   A 301 ? 1.2813 1.0687 1.2015 -0.0845 0.0174  0.4257  321 LEU   A C   
2027 O  O   . LEU   A 301 ? 1.3378 1.0921 1.2338 -0.0758 0.0167  0.4539  321 LEU   A O   
2028 C  CB  . LEU   A 301 ? 1.3386 1.0863 1.2821 -0.0557 0.0056  0.3759  321 LEU   A CB  
2029 C  CG  . LEU   A 301 ? 1.2883 1.0458 1.2485 -0.0249 0.0015  0.3506  321 LEU   A CG  
2030 C  CD1 . LEU   A 301 ? 1.3738 1.0667 1.3306 -0.0216 0.0036  0.3348  321 LEU   A CD1 
2031 C  CD2 . LEU   A 301 ? 1.2401 1.0082 1.2008 0.0079  -0.0068 0.3638  321 LEU   A CD2 
2032 N  N   . ALA   A 302 ? 1.3227 1.1327 1.2590 -0.1174 0.0260  0.4244  322 ALA   A N   
2033 C  CA  . ALA   A 302 ? 1.3302 1.1307 1.2617 -0.1464 0.0374  0.4580  322 ALA   A CA  
2034 C  C   . ALA   A 302 ? 1.2911 1.1383 1.2011 -0.1355 0.0493  0.4829  322 ALA   A C   
2035 O  O   . ALA   A 302 ? 1.4289 1.2505 1.3164 -0.1413 0.0579  0.5187  322 ALA   A O   
2036 C  CB  . ALA   A 302 ? 1.3889 1.2106 1.3535 -0.1845 0.0413  0.4503  322 ALA   A CB  
2037 N  N   . THR   A 303 ? 1.2382 1.1488 1.1497 -0.1186 0.0504  0.4650  323 THR   A N   
2038 C  CA  . THR   A 303 ? 1.2453 1.1968 1.1267 -0.1043 0.0609  0.4834  323 THR   A CA  
2039 C  C   . THR   A 303 ? 1.2454 1.1754 1.0883 -0.0693 0.0464  0.4894  323 THR   A C   
2040 O  O   . THR   A 303 ? 1.2696 1.2231 1.0750 -0.0540 0.0511  0.5045  323 THR   A O   
2041 C  CB  . THR   A 303 ? 1.2859 1.3075 1.1807 -0.0995 0.0664  0.4598  323 THR   A CB  
2042 O  OG1 . THR   A 303 ? 1.2013 1.2277 1.1108 -0.0813 0.0484  0.4236  323 THR   A OG1 
2043 C  CG2 . THR   A 303 ? 1.2858 1.3382 1.2198 -0.1329 0.0813  0.4609  323 THR   A CG2 
2044 N  N   . HIS   A 304 ? 1.2084 1.0950 1.0587 -0.0547 0.0285  0.4783  324 HIS   A N   
2045 C  CA  . HIS   A 304 ? 1.3146 1.1806 1.1385 -0.0216 0.0109  0.4863  324 HIS   A CA  
2046 C  C   . HIS   A 304 ? 1.3836 1.1776 1.2089 -0.0200 0.0054  0.5007  324 HIS   A C   
2047 O  O   . HIS   A 304 ? 1.3318 1.1044 1.1811 -0.0064 -0.0058 0.4803  324 HIS   A O   
2048 C  CB  . HIS   A 304 ? 1.2395 1.1401 1.0820 0.0031  -0.0072 0.4534  324 HIS   A CB  
2049 C  CG  . HIS   A 304 ? 1.2475 1.2095 1.0851 0.0038  -0.0038 0.4370  324 HIS   A CG  
2050 N  ND1 . HIS   A 304 ? 1.2120 1.2076 1.0769 -0.0159 0.0093  0.4172  324 HIS   A ND1 
2051 C  CD2 . HIS   A 304 ? 1.2719 1.2634 1.0768 0.0235  -0.0132 0.4368  324 HIS   A CD2 
2052 C  CE1 . HIS   A 304 ? 1.2304 1.2732 1.0817 -0.0070 0.0101  0.4061  324 HIS   A CE1 
2053 N  NE2 . HIS   A 304 ? 1.2620 1.3009 1.0745 0.0164  -0.0036 0.4164  324 HIS   A NE2 
2054 N  N   . PRO   A 305 ? 1.3032 1.0560 1.1020 -0.0325 0.0150  0.5370  325 PRO   A N   
2055 C  CA  . PRO   A 305 ? 1.4204 1.0949 1.2171 -0.0312 0.0099  0.5515  325 PRO   A CA  
2056 C  C   . PRO   A 305 ? 1.4125 1.0647 1.2021 0.0095  -0.0107 0.5504  325 PRO   A C   
2057 O  O   . PRO   A 305 ? 1.4349 1.0340 1.2387 0.0184  -0.0161 0.5444  325 PRO   A O   
2058 C  CB  . PRO   A 305 ? 1.3625 1.0064 1.1276 -0.0507 0.0250  0.5960  325 PRO   A CB  
2059 C  CG  . PRO   A 305 ? 1.3948 1.1028 1.1651 -0.0749 0.0443  0.5978  325 PRO   A CG  
2060 C  CD  . PRO   A 305 ? 1.4490 1.2227 1.2223 -0.0513 0.0350  0.5669  325 PRO   A CD  
2061 N  N   . ASP   A 306 ? 1.4356 1.1262 1.2039 0.0355  -0.0235 0.5556  326 ASP   A N   
2062 C  CA  . ASP   A 306 ? 1.3334 1.0112 1.1040 0.0738  -0.0473 0.5559  326 ASP   A CA  
2063 C  C   . ASP   A 306 ? 1.4286 1.1250 1.2513 0.0859  -0.0550 0.5189  326 ASP   A C   
2064 O  O   . ASP   A 306 ? 1.4732 1.1374 1.3149 0.1101  -0.0647 0.5189  326 ASP   A O   
2065 C  CB  . ASP   A 306 ? 1.4074 1.1251 1.1433 0.0960  -0.0645 0.5661  326 ASP   A CB  
2066 C  CG  . ASP   A 306 ? 1.4588 1.2466 1.2022 0.0895  -0.0642 0.5377  326 ASP   A CG  
2067 O  OD1 . ASP   A 306 ? 1.3254 1.1337 1.0989 0.0657  -0.0475 0.5154  326 ASP   A OD1 
2068 O  OD2 . ASP   A 306 ? 1.5317 1.3505 1.2483 0.1093  -0.0829 0.5373  326 ASP   A OD2 
2069 N  N   . VAL   A 307 ? 1.3168 1.0647 1.1632 0.0713  -0.0486 0.4891  327 VAL   A N   
2070 C  CA  . VAL   A 307 ? 1.3175 1.0829 1.2110 0.0810  -0.0516 0.4564  327 VAL   A CA  
2071 C  C   . VAL   A 307 ? 1.2605 0.9708 1.1670 0.0689  -0.0373 0.4483  327 VAL   A C   
2072 O  O   . VAL   A 307 ? 1.3340 1.0224 1.2652 0.0899  -0.0393 0.4364  327 VAL   A O   
2073 C  CB  . VAL   A 307 ? 1.2568 1.0882 1.1665 0.0695  -0.0493 0.4292  327 VAL   A CB  
2074 C  CG1 . VAL   A 307 ? 1.2507 1.0946 1.2063 0.0752  -0.0470 0.3984  327 VAL   A CG1 
2075 C  CG2 . VAL   A 307 ? 1.1624 1.0392 1.0567 0.0865  -0.0682 0.4321  327 VAL   A CG2 
2076 N  N   . GLN   A 308 ? 1.3093 0.9954 1.1990 0.0354  -0.0230 0.4547  328 GLN   A N   
2077 C  CA  . GLN   A 308 ? 1.3993 1.0238 1.2934 0.0209  -0.0144 0.4460  328 GLN   A CA  
2078 C  C   . GLN   A 308 ? 1.4776 1.0261 1.3565 0.0411  -0.0187 0.4658  328 GLN   A C   
2079 O  O   . GLN   A 308 ? 1.4024 0.9003 1.2883 0.0509  -0.0159 0.4508  328 GLN   A O   
2080 C  CB  . GLN   A 308 ? 1.4142 1.0318 1.2987 -0.0223 -0.0033 0.4529  328 GLN   A CB  
2081 C  CG  . GLN   A 308 ? 1.4827 1.0323 1.3677 -0.0426 0.0000  0.4420  328 GLN   A CG  
2082 C  CD  . GLN   A 308 ? 1.5283 1.0745 1.4127 -0.0886 0.0067  0.4534  328 GLN   A CD  
2083 O  OE1 . GLN   A 308 ? 1.7251 1.2165 1.6093 -0.1118 0.0049  0.4452  328 GLN   A OE1 
2084 N  NE2 . GLN   A 308 ? 1.4679 1.0727 1.3526 -0.1014 0.0142  0.4724  328 GLN   A NE2 
2085 N  N   . GLN   A 309 ? 1.3963 0.9324 1.2497 0.0503  -0.0248 0.4997  329 GLN   A N   
2086 C  CA  . GLN   A 309 ? 1.5503 1.0131 1.3880 0.0727  -0.0300 0.5219  329 GLN   A CA  
2087 C  C   . GLN   A 309 ? 1.5845 1.0597 1.4481 0.1182  -0.0421 0.5124  329 GLN   A C   
2088 O  O   . GLN   A 309 ? 1.5072 0.9244 1.3769 0.1390  -0.0401 0.5097  329 GLN   A O   
2089 C  CB  . GLN   A 309 ? 1.5124 0.9580 1.3113 0.0694  -0.0327 0.5644  329 GLN   A CB  
2090 C  CG  . GLN   A 309 ? 1.6220 1.0356 1.4085 0.1105  -0.0482 0.5882  329 GLN   A CG  
2091 C  CD  . GLN   A 309 ? 1.6053 0.9433 1.3508 0.1036  -0.0447 0.6293  329 GLN   A CD  
2092 O  OE1 . GLN   A 309 ? 1.6327 0.9462 1.3613 0.0651  -0.0298 0.6425  329 GLN   A OE1 
2093 N  NE2 . GLN   A 309 ? 1.6931 0.9940 1.4261 0.1409  -0.0587 0.6519  329 GLN   A NE2 
2094 N  N   . LYS   A 310 ? 1.5102 1.0596 1.3911 0.1346  -0.0550 0.5075  330 LYS   A N   
2095 C  CA  . LYS   A 310 ? 1.5066 1.0786 1.4250 0.1748  -0.0681 0.5000  330 LYS   A CA  
2096 C  C   . LYS   A 310 ? 1.4553 1.0278 1.4121 0.1803  -0.0544 0.4675  330 LYS   A C   
2097 O  O   . LYS   A 310 ? 1.4985 1.0562 1.4838 0.2141  -0.0548 0.4656  330 LYS   A O   
2098 C  CB  . LYS   A 310 ? 1.5355 1.1867 1.4662 0.1847  -0.0882 0.4986  330 LYS   A CB  
2099 C  CG  . LYS   A 310 ? 1.5021 1.1821 1.4786 0.2244  -0.1075 0.4976  330 LYS   A CG  
2100 C  CD  . LYS   A 310 ? 1.4820 1.2386 1.4733 0.2282  -0.1312 0.4904  330 LYS   A CD  
2101 C  CE  . LYS   A 310 ? 1.5123 1.3032 1.5618 0.2640  -0.1531 0.4906  330 LYS   A CE  
2102 N  NZ  . LYS   A 310 ? 1.5619 1.4246 1.6312 0.2637  -0.1798 0.4792  330 LYS   A NZ  
2103 N  N   . LEU   A 311 ? 1.4549 1.0442 1.4117 0.1498  -0.0410 0.4432  331 LEU   A N   
2104 C  CA  . LEU   A 311 ? 1.4605 1.0420 1.4416 0.1545  -0.0265 0.4134  331 LEU   A CA  
2105 C  C   . LEU   A 311 ? 1.4934 0.9819 1.4510 0.1584  -0.0151 0.4136  331 LEU   A C   
2106 O  O   . LEU   A 311 ? 1.5087 0.9729 1.4828 0.1868  -0.0057 0.4007  331 LEU   A O   
2107 C  CB  . LEU   A 311 ? 1.3590 0.9810 1.3415 0.1216  -0.0186 0.3891  331 LEU   A CB  
2108 C  CG  . LEU   A 311 ? 1.3374 0.9534 1.3370 0.1257  -0.0039 0.3584  331 LEU   A CG  
2109 C  CD1 . LEU   A 311 ? 1.2998 0.9466 1.3432 0.1645  -0.0026 0.3533  331 LEU   A CD1 
2110 C  CD2 . LEU   A 311 ? 1.3436 1.0067 1.3456 0.0959  0.0000  0.3377  331 LEU   A CD2 
2111 N  N   . GLN   A 312 ? 1.5281 0.9613 1.4466 0.1307  -0.0149 0.4288  332 GLN   A N   
2112 C  CA  . GLN   A 312 ? 1.5989 0.9329 1.4903 0.1320  -0.0079 0.4288  332 GLN   A CA  
2113 C  C   . GLN   A 312 ? 1.6281 0.9183 1.5223 0.1770  -0.0109 0.4468  332 GLN   A C   
2114 O  O   . GLN   A 312 ? 1.6589 0.8770 1.5419 0.1961  -0.0016 0.4365  332 GLN   A O   
2115 C  CB  . GLN   A 312 ? 1.5402 0.8277 1.3971 0.0898  -0.0095 0.4465  332 GLN   A CB  
2116 C  CG  . GLN   A 312 ? 1.6595 0.9609 1.5145 0.0465  -0.0049 0.4238  332 GLN   A CG  
2117 C  CD  . GLN   A 312 ? 1.6425 0.9203 1.4787 0.0023  -0.0066 0.4469  332 GLN   A CD  
2118 O  OE1 . GLN   A 312 ? 1.6595 0.9247 1.4821 0.0029  -0.0088 0.4818  332 GLN   A OE1 
2119 N  NE2 . GLN   A 312 ? 1.7032 0.9767 1.5403 -0.0363 -0.0057 0.4295  332 GLN   A NE2 
2120 N  N   . GLU   A 313 ? 1.5588 0.8890 1.4649 0.1965  -0.0247 0.4731  333 GLU   A N   
2121 C  CA  . GLU   A 313 ? 1.6533 0.9572 1.5730 0.2441  -0.0305 0.4903  333 GLU   A CA  
2122 C  C   . GLU   A 313 ? 1.6620 1.0012 1.6300 0.2793  -0.0214 0.4671  333 GLU   A C   
2123 O  O   . GLU   A 313 ? 1.6657 0.9570 1.6419 0.3169  -0.0135 0.4691  333 GLU   A O   
2124 C  CB  . GLU   A 313 ? 1.5543 0.9020 1.4762 0.2566  -0.0523 0.5222  333 GLU   A CB  
2125 C  CG  . GLU   A 313 ? 1.6904 0.9971 1.5610 0.2302  -0.0574 0.5532  333 GLU   A CG  
2126 C  CD  . GLU   A 313 ? 1.6649 1.0195 1.5279 0.2438  -0.0792 0.5817  333 GLU   A CD  
2127 O  OE1 . GLU   A 313 ? 1.6161 1.0489 1.5144 0.2606  -0.0929 0.5708  333 GLU   A OE1 
2128 O  OE2 . GLU   A 313 ? 1.6660 0.9770 1.4853 0.2374  -0.0835 0.6155  333 GLU   A OE2 
2129 N  N   . GLU   A 314 ? 1.6052 1.0277 1.6064 0.2687  -0.0205 0.4464  334 GLU   A N   
2130 C  CA  . GLU   A 314 ? 1.5438 1.0073 1.5961 0.2987  -0.0091 0.4275  334 GLU   A CA  
2131 C  C   . GLU   A 314 ? 1.6297 1.0255 1.6631 0.3067  0.0168  0.4042  334 GLU   A C   
2132 O  O   . GLU   A 314 ? 1.6823 1.0699 1.7438 0.3472  0.0314  0.4000  334 GLU   A O   
2133 C  CB  . GLU   A 314 ? 1.5640 1.1205 1.6487 0.2792  -0.0131 0.4106  334 GLU   A CB  
2134 C  CG  . GLU   A 314 ? 1.5235 1.1214 1.6590 0.3006  0.0038  0.3898  334 GLU   A CG  
2135 C  CD  . GLU   A 314 ? 1.4610 1.1444 1.6633 0.3217  -0.0124 0.3997  334 GLU   A CD  
2136 O  OE1 . GLU   A 314 ? 1.4907 1.1757 1.7103 0.3474  -0.0303 0.4244  334 GLU   A OE1 
2137 O  OE2 . GLU   A 314 ? 1.3754 1.1230 1.6135 0.3117  -0.0096 0.3836  334 GLU   A OE2 
2138 N  N   . ILE   A 315 ? 1.6123 0.9585 1.5975 0.2695  0.0225  0.3892  335 ILE   A N   
2139 C  CA  . ILE   A 315 ? 1.6793 0.9550 1.6356 0.2752  0.0427  0.3636  335 ILE   A CA  
2140 C  C   . ILE   A 315 ? 1.8443 1.0180 1.7698 0.3029  0.0469  0.3749  335 ILE   A C   
2141 O  O   . ILE   A 315 ? 1.9228 1.0438 1.8364 0.3332  0.0662  0.3577  335 ILE   A O   
2142 C  CB  . ILE   A 315 ? 1.7137 0.9691 1.6307 0.2253  0.0414  0.3436  335 ILE   A CB  
2143 C  CG1 . ILE   A 315 ? 1.7345 1.0866 1.6772 0.1945  0.0315  0.3432  335 ILE   A CG1 
2144 C  CG2 . ILE   A 315 ? 1.7973 1.0127 1.6924 0.2334  0.0601  0.3103  335 ILE   A CG2 
2145 C  CD1 . ILE   A 315 ? 1.6665 1.0156 1.5837 0.1507  0.0316  0.3222  335 ILE   A CD1 
2146 N  N   . ASP   A 316 ? 1.7454 0.8851 1.6531 0.2952  0.0305  0.4042  336 ASP   A N   
2147 C  CA  . ASP   A 316 ? 1.9166 0.9527 1.7933 0.3217  0.0331  0.4172  336 ASP   A CA  
2148 C  C   . ASP   A 316 ? 1.8965 0.9513 1.8148 0.3815  0.0403  0.4248  336 ASP   A C   
2149 O  O   . ASP   A 316 ? 2.0203 1.0131 1.9229 0.4070  0.0500  0.4103  336 ASP   A O   
2150 C  CB  . ASP   A 316 ? 1.8608 0.8603 1.7102 0.2982  0.0145  0.4510  336 ASP   A CB  
2151 C  CG  . ASP   A 316 ? 1.8360 0.7989 1.6456 0.2396  0.0102  0.4444  336 ASP   A CG  
2152 O  OD1 . ASP   A 316 ? 1.9503 0.8722 1.7378 0.2236  0.0189  0.4131  336 ASP   A OD1 
2153 O  OD2 . ASP   A 316 ? 1.8101 0.7860 1.6107 0.2102  -0.0020 0.4716  336 ASP   A OD2 
2154 N  N   . ALA   A 317 ? 1.9072 1.0613 1.8832 0.3977  0.0304  0.4406  337 ALA   A N   
2155 C  CA  . ALA   A 317 ? 1.8916 1.0847 1.9177 0.4444  0.0292  0.4437  337 ALA   A CA  
2156 C  C   . ALA   A 317 ? 1.9128 1.1274 1.9690 0.4709  0.0579  0.4158  337 ALA   A C   
2157 O  O   . ALA   A 317 ? 1.9601 1.1297 2.0106 0.5019  0.0727  0.4041  337 ALA   A O   
2158 C  CB  . ALA   A 317 ? 1.8428 1.1343 1.9205 0.4492  0.0044  0.4669  337 ALA   A CB  
2159 N  N   . VAL   A 318 ? 1.8717 1.1552 1.9588 0.4591  0.0674  0.4055  338 VAL   A N   
2160 C  CA  . VAL   A 318 ? 1.9010 1.2142 2.0187 0.4826  0.0968  0.3820  338 VAL   A CA  
2161 C  C   . VAL   A 318 ? 1.9255 1.1375 1.9762 0.4860  0.1208  0.3549  338 VAL   A C   
2162 O  O   . VAL   A 318 ? 1.9392 1.1407 1.9973 0.5199  0.1445  0.3397  338 VAL   A O   
2163 C  CB  . VAL   A 318 ? 1.8522 1.2521 2.0074 0.4603  0.0992  0.3750  338 VAL   A CB  
2164 C  CG1 . VAL   A 318 ? 1.8683 1.2609 2.0163 0.4694  0.1339  0.3463  338 VAL   A CG1 
2165 C  CG2 . VAL   A 318 ? 1.8312 1.3385 2.0716 0.4750  0.0826  0.3946  338 VAL   A CG2 
2166 N  N   . LEU   A 319 ? 1.9208 1.0576 1.9042 0.4498  0.1141  0.3482  339 LEU   A N   
2167 C  CA  . LEU   A 319 ? 2.0198 1.0510 1.9318 0.4471  0.1278  0.3206  339 LEU   A CA  
2168 C  C   . LEU   A 319 ? 2.1519 1.0929 2.0187 0.4355  0.1084  0.3310  339 LEU   A C   
2169 O  O   . LEU   A 319 ? 2.1858 1.0805 2.0111 0.3923  0.0925  0.3353  339 LEU   A O   
2170 C  CB  . LEU   A 319 ? 2.0350 1.0584 1.9078 0.4046  0.1291  0.2962  339 LEU   A CB  
2171 C  CG  . LEU   A 319 ? 2.0087 1.1171 1.9175 0.4097  0.1479  0.2790  339 LEU   A CG  
2172 C  CD1 . LEU   A 319 ? 1.8455 1.0352 1.7733 0.3586  0.1281  0.2779  339 LEU   A CD1 
2173 C  CD2 . LEU   A 319 ? 2.0127 1.0505 1.8630 0.4227  0.1728  0.2458  339 LEU   A CD2 
2174 N  N   . PRO   A 320 ? 2.1148 1.0307 1.9917 0.4715  0.1096  0.3370  340 PRO   A N   
2175 C  CA  . PRO   A 320 ? 2.2290 1.0608 2.0686 0.4614  0.0905  0.3503  340 PRO   A CA  
2176 C  C   . PRO   A 320 ? 2.3087 1.0266 2.0756 0.4427  0.0946  0.3226  340 PRO   A C   
2177 O  O   . PRO   A 320 ? 2.4423 1.1357 2.1840 0.4569  0.1154  0.2907  340 PRO   A O   
2178 C  CB  . PRO   A 320 ? 2.1274 0.9740 2.0056 0.5117  0.0933  0.3622  340 PRO   A CB  
2179 C  CG  . PRO   A 320 ? 2.1625 1.0566 2.0709 0.5474  0.1235  0.3403  340 PRO   A CG  
2180 C  CD  . PRO   A 320 ? 2.0926 1.0574 2.0189 0.5226  0.1295  0.3333  340 PRO   A CD  
2181 N  N   . ASN   A 321 ? 2.3415 0.9907 2.0742 0.4089  0.0732  0.3358  341 ASN   A N   
2182 C  CA  . ASN   A 321 ? 2.5140 1.0529 2.1827 0.3832  0.0693  0.3124  341 ASN   A CA  
2183 C  C   . ASN   A 321 ? 2.4228 0.9551 2.0576 0.3510  0.0736  0.2825  341 ASN   A C   
2184 O  O   . ASN   A 321 ? 2.4382 0.8918 2.0201 0.3453  0.0762  0.2502  341 ASN   A O   
2185 C  CB  . ASN   A 321 ? 2.4905 0.9612 2.1374 0.4270  0.0830  0.2929  341 ASN   A CB  
2186 C  CG  . ASN   A 321 ? 2.3963 0.8949 2.0880 0.4709  0.0831  0.3197  341 ASN   A CG  
2187 O  OD1 . ASN   A 321 ? 2.4390 0.9680 2.1585 0.4596  0.0641  0.3545  341 ASN   A OD1 
2188 N  ND2 . ASN   A 321 ? 2.3952 0.8846 2.0919 0.5217  0.1044  0.3041  341 ASN   A ND2 
2189 N  N   . LYS   A 322 ? 2.4099 1.0232 2.0723 0.3301  0.0725  0.2927  342 LYS   A N   
2190 C  CA  . LYS   A 322 ? 2.4016 1.0220 2.0385 0.3027  0.0764  0.2671  342 LYS   A CA  
2191 C  C   . LYS   A 322 ? 2.4869 1.0884 2.0996 0.3393  0.1003  0.2304  342 LYS   A C   
2192 O  O   . LYS   A 322 ? 2.5839 1.1185 2.1385 0.3221  0.0979  0.1984  342 LYS   A O   
2193 C  CB  . LYS   A 322 ? 2.4661 1.0170 2.0572 0.2425  0.0530  0.2603  342 LYS   A CB  
2194 C  CG  . LYS   A 322 ? 2.4361 1.0500 2.0585 0.1954  0.0358  0.2910  342 LYS   A CG  
2195 C  CD  . LYS   A 322 ? 2.4384 1.0151 2.0328 0.1313  0.0146  0.2803  342 LYS   A CD  
2196 C  CE  . LYS   A 322 ? 2.4455 0.9428 2.0243 0.1050  -0.0013 0.3038  342 LYS   A CE  
2197 N  NZ  . LYS   A 322 ? 2.4266 0.9337 2.0091 0.0372  -0.0207 0.3149  342 LYS   A NZ  
2198 N  N   . ALA   A 323 ? 2.4604 1.1252 2.1194 0.3898  0.1227  0.2362  343 ALA   A N   
2199 C  CA  . ALA   A 323 ? 2.4724 1.1346 2.1158 0.4280  0.1515  0.2071  343 ALA   A CA  
2200 C  C   . ALA   A 323 ? 2.4265 1.1158 2.0512 0.4078  0.1592  0.1867  343 ALA   A C   
2201 O  O   . ALA   A 323 ? 2.3390 1.0925 1.9951 0.3771  0.1482  0.2013  343 ALA   A O   
2202 C  CB  . ALA   A 323 ? 2.3492 1.0944 2.0627 0.4794  0.1731  0.2234  343 ALA   A CB  
2203 N  N   . PRO   A 324 ? 2.3302 0.9748 1.9016 0.4234  0.1767  0.1526  344 PRO   A N   
2204 C  CA  . PRO   A 324 ? 2.3260 0.9891 1.8716 0.4053  0.1825  0.1323  344 PRO   A CA  
2205 C  C   . PRO   A 324 ? 2.2356 1.0241 1.8585 0.4192  0.2013  0.1501  344 PRO   A C   
2206 O  O   . PRO   A 324 ? 2.1885 1.0325 1.8638 0.4628  0.2262  0.1622  344 PRO   A O   
2207 C  CB  . PRO   A 324 ? 2.3834 0.9807 1.8595 0.4334  0.2025  0.0962  344 PRO   A CB  
2208 C  CG  . PRO   A 324 ? 2.4567 0.9681 1.9010 0.4444  0.1934  0.0924  344 PRO   A CG  
2209 C  CD  . PRO   A 324 ? 2.4066 0.9714 1.9281 0.4561  0.1897  0.1303  344 PRO   A CD  
2210 N  N   . PRO   A 325 ? 2.2281 1.0948 1.8753 0.3721  0.1831  0.1492  345 PRO   A N   
2211 C  CA  . PRO   A 325 ? 2.1620 1.1579 1.8871 0.3767  0.1951  0.1631  345 PRO   A CA  
2212 C  C   . PRO   A 325 ? 2.2127 1.2199 1.9291 0.4156  0.2331  0.1472  345 PRO   A C   
2213 O  O   . PRO   A 325 ? 2.3057 1.2689 1.9574 0.4068  0.2376  0.1197  345 PRO   A O   
2214 C  CB  . PRO   A 325 ? 2.1329 1.1824 1.8642 0.3168  0.1664  0.1597  345 PRO   A CB  
2215 C  CG  . PRO   A 325 ? 2.2208 1.1883 1.9032 0.2802  0.1371  0.1568  345 PRO   A CG  
2216 C  CD  . PRO   A 325 ? 2.2849 1.1276 1.8966 0.3114  0.1489  0.1383  345 PRO   A CD  
2217 N  N   . THR   A 326 ? 2.1638 1.2313 1.9467 0.4590  0.2601  0.1664  346 THR   A N   
2218 C  CA  . THR   A 326 ? 2.1744 1.2675 1.9651 0.4981  0.3019  0.1591  346 THR   A CA  
2219 C  C   . THR   A 326 ? 2.1231 1.3421 1.9909 0.4790  0.3031  0.1714  346 THR   A C   
2220 O  O   . THR   A 326 ? 2.0899 1.3702 1.9976 0.4381  0.2711  0.1823  346 THR   A O   
2221 C  CB  . THR   A 326 ? 2.0417 1.1473 1.8665 0.5443  0.3256  0.1686  346 THR   A CB  
2222 O  OG1 . THR   A 326 ? 2.0030 1.1899 1.9224 0.5474  0.3119  0.2003  346 THR   A OG1 
2223 C  CG2 . THR   A 326 ? 2.1678 1.1590 1.9151 0.5551  0.3193  0.1516  346 THR   A CG2 
2224 N  N   . TYR   A 327 ? 2.2143 1.4686 2.1010 0.5102  0.3421  0.1702  347 TYR   A N   
2225 C  CA  . TYR   A 327 ? 2.2055 1.5715 2.1646 0.4930  0.3454  0.1818  347 TYR   A CA  
2226 C  C   . TYR   A 327 ? 2.0887 1.5486 2.1594 0.5007  0.3372  0.2134  347 TYR   A C   
2227 O  O   . TYR   A 327 ? 2.0562 1.6032 2.1864 0.4712  0.3197  0.2232  347 TYR   A O   
2228 C  CB  . TYR   A 327 ? 2.2430 1.6153 2.1888 0.5238  0.3921  0.1745  347 TYR   A CB  
2229 C  CG  . TYR   A 327 ? 2.1432 1.6204 2.1582 0.5048  0.3976  0.1861  347 TYR   A CG  
2230 C  CD1 . TYR   A 327 ? 2.1273 1.6139 2.1060 0.4629  0.3790  0.1708  347 TYR   A CD1 
2231 C  CD2 . TYR   A 327 ? 2.0268 1.5980 2.1440 0.5218  0.4159  0.2113  347 TYR   A CD2 
2232 C  CE1 . TYR   A 327 ? 2.1105 1.6850 2.1494 0.4466  0.3838  0.1814  347 TYR   A CE1 
2233 C  CE2 . TYR   A 327 ? 2.0140 1.6715 2.1956 0.5049  0.4209  0.2226  347 TYR   A CE2 
2234 C  CZ  . TYR   A 327 ? 2.1050 1.7605 2.2448 0.4686  0.4058  0.2074  347 TYR   A CZ  
2235 O  OH  . TYR   A 327 ? 2.0863 1.8231 2.2868 0.4499  0.4088  0.2179  347 TYR   A OH  
2236 N  N   . ASP   A 328 ? 1.9407 1.3901 2.0372 0.5325  0.3423  0.2261  348 ASP   A N   
2237 C  CA  . ASP   A 328 ? 1.8479 1.3903 2.0477 0.5377  0.3290  0.2536  348 ASP   A CA  
2238 C  C   . ASP   A 328 ? 1.8436 1.3758 2.0532 0.5209  0.2870  0.2687  348 ASP   A C   
2239 O  O   . ASP   A 328 ? 1.7924 1.4063 2.0816 0.5153  0.2658  0.2903  348 ASP   A O   
2240 C  CB  . ASP   A 328 ? 1.8557 1.4112 2.0856 0.5766  0.3544  0.2598  348 ASP   A CB  
2241 C  CG  . ASP   A 328 ? 1.8562 1.4580 2.1085 0.5907  0.3958  0.2576  348 ASP   A CG  
2242 O  OD1 . ASP   A 328 ? 1.9087 1.4496 2.0817 0.5967  0.4215  0.2365  348 ASP   A OD1 
2243 O  OD2 . ASP   A 328 ? 1.8277 1.5246 2.1743 0.5941  0.4008  0.2777  348 ASP   A OD2 
2244 N  N   . THR   A 329 ? 1.8605 1.2936 1.9883 0.5100  0.2726  0.2582  349 THR   A N   
2245 C  CA  . THR   A 329 ? 1.8762 1.3049 2.0045 0.4829  0.2314  0.2721  349 THR   A CA  
2246 C  C   . THR   A 329 ? 1.8189 1.3111 1.9589 0.4294  0.2015  0.2702  349 THR   A C   
2247 O  O   . THR   A 329 ? 1.7836 1.3172 1.9567 0.4132  0.1713  0.2889  349 THR   A O   
2248 C  CB  . THR   A 329 ? 1.9199 1.2277 1.9592 0.4781  0.2233  0.2607  349 THR   A CB  
2249 O  OG1 . THR   A 329 ? 1.9411 1.1782 1.9068 0.4806  0.2459  0.2306  349 THR   A OG1 
2250 C  CG2 . THR   A 329 ? 1.9249 1.1979 1.9750 0.5159  0.2250  0.2742  349 THR   A CG2 
2251 N  N   . VAL   A 330 ? 1.7716 1.2695 1.8808 0.4045  0.2097  0.2483  350 VAL   A N   
2252 C  CA  . VAL   A 330 ? 1.7415 1.3015 1.8639 0.3583  0.1850  0.2458  350 VAL   A CA  
2253 C  C   . VAL   A 330 ? 1.7046 1.3699 1.9177 0.3634  0.1803  0.2632  350 VAL   A C   
2254 O  O   . VAL   A 330 ? 1.6263 1.3413 1.8645 0.3371  0.1501  0.2728  350 VAL   A O   
2255 C  CB  . VAL   A 330 ? 1.7095 1.2505 1.7803 0.3361  0.1957  0.2194  350 VAL   A CB  
2256 C  CG1 . VAL   A 330 ? 1.5701 1.1848 1.6657 0.2962  0.1752  0.2182  350 VAL   A CG1 
2257 C  CG2 . VAL   A 330 ? 1.7164 1.1556 1.6990 0.3215  0.1886  0.2014  350 VAL   A CG2 
2258 N  N   . LEU   A 331 ? 1.7168 1.4157 1.9802 0.3978  0.2101  0.2682  351 LEU   A N   
2259 C  CA  . LEU   A 331 ? 1.6845 1.4835 2.0396 0.3992  0.2073  0.2828  351 LEU   A CA  
2260 C  C   . LEU   A 331 ? 1.6870 1.5310 2.1074 0.4110  0.1804  0.3081  351 LEU   A C   
2261 O  O   . LEU   A 331 ? 1.6142 1.5412 2.1152 0.4104  0.1711  0.3205  351 LEU   A O   
2262 C  CB  . LEU   A 331 ? 1.6718 1.4920 2.0650 0.4329  0.2514  0.2840  351 LEU   A CB  
2263 C  CG  . LEU   A 331 ? 1.7170 1.4990 2.0464 0.4255  0.2797  0.2609  351 LEU   A CG  
2264 C  CD1 . LEU   A 331 ? 1.7563 1.5538 2.1198 0.4662  0.3288  0.2672  351 LEU   A CD1 
2265 C  CD2 . LEU   A 331 ? 1.5836 1.4104 1.9127 0.3808  0.2598  0.2514  351 LEU   A CD2 
2266 N  N   . GLN   A 332 ? 1.9330 1.7232 2.3213 0.4213  0.1654  0.3169  352 GLN   A N   
2267 C  CA  . GLN   A 332 ? 1.8853 1.7132 2.3279 0.4352  0.1373  0.3425  352 GLN   A CA  
2268 C  C   . GLN   A 332 ? 1.9076 1.7151 2.3056 0.4052  0.0983  0.3478  352 GLN   A C   
2269 O  O   . GLN   A 332 ? 1.8915 1.7407 2.3296 0.4098  0.0684  0.3678  352 GLN   A O   
2270 C  CB  . GLN   A 332 ? 1.8606 1.6521 2.3160 0.4823  0.1547  0.3543  352 GLN   A CB  
2271 C  CG  . GLN   A 332 ? 1.9777 1.6559 2.3447 0.4906  0.1631  0.3471  352 GLN   A CG  
2272 C  CD  . GLN   A 332 ? 2.0915 1.7397 2.4617 0.5283  0.1770  0.3485  352 GLN   A CD  
2273 O  OE1 . GLN   A 332 ? 2.2444 1.8047 2.5531 0.5368  0.1755  0.3461  352 GLN   A OE1 
2274 N  NE2 . GLN   A 332 ? 2.0648 1.7855 2.5087 0.5498  0.1904  0.3533  352 GLN   A NE2 
2275 N  N   . MET   A 333 ? 1.6365 1.3833 1.9542 0.3751  0.0973  0.3319  353 MET   A N   
2276 C  CA  . MET   A 333 ? 1.5138 1.2464 1.7912 0.3446  0.0657  0.3394  353 MET   A CA  
2277 C  C   . MET   A 333 ? 1.4471 1.2607 1.7551 0.3170  0.0418  0.3391  353 MET   A C   
2278 O  O   . MET   A 333 ? 1.3891 1.2161 1.6748 0.2861  0.0447  0.3210  353 MET   A O   
2279 C  CB  . MET   A 333 ? 1.5261 1.1812 1.7220 0.3169  0.0723  0.3233  353 MET   A CB  
2280 C  CG  . MET   A 333 ? 1.6614 1.2218 1.8166 0.3422  0.0896  0.3226  353 MET   A CG  
2281 S  SD  . MET   A 333 ? 1.7122 1.1805 1.7768 0.3035  0.0890  0.3040  353 MET   A SD  
2282 C  CE  . MET   A 333 ? 1.5902 1.1049 1.6513 0.2577  0.0572  0.3183  353 MET   A CE  
2283 N  N   . GLU   A 334 ? 1.3906 1.2551 1.7471 0.3295  0.0160  0.3586  354 GLU   A N   
2284 C  CA  . GLU   A 334 ? 1.2857 1.2270 1.6783 0.3099  -0.0076 0.3563  354 GLU   A CA  
2285 C  C   . GLU   A 334 ? 1.2307 1.1639 1.5630 0.2726  -0.0260 0.3507  354 GLU   A C   
2286 O  O   . GLU   A 334 ? 1.2316 1.2003 1.5632 0.2476  -0.0276 0.3347  354 GLU   A O   
2287 C  CB  . GLU   A 334 ? 1.2387 1.2306 1.6952 0.3338  -0.0356 0.3781  354 GLU   A CB  
2288 C  CG  . GLU   A 334 ? 1.2245 1.2962 1.7339 0.3189  -0.0593 0.3733  354 GLU   A CG  
2289 C  CD  . GLU   A 334 ? 1.2475 1.3641 1.8103 0.3378  -0.0974 0.3945  354 GLU   A CD  
2290 O  OE1 . GLU   A 334 ? 1.2389 1.3305 1.8080 0.3677  -0.1008 0.4147  354 GLU   A OE1 
2291 O  OE2 . GLU   A 334 ? 1.2473 1.4209 1.8440 0.3233  -0.1263 0.3906  354 GLU   A OE2 
2292 N  N   . TYR   A 335 ? 1.2430 1.1293 1.5249 0.2700  -0.0380 0.3658  355 TYR   A N   
2293 C  CA  . TYR   A 335 ? 1.2526 1.1339 1.4796 0.2369  -0.0509 0.3648  355 TYR   A CA  
2294 C  C   . TYR   A 335 ? 1.1902 1.0496 1.3822 0.2078  -0.0289 0.3431  355 TYR   A C   
2295 O  O   . TYR   A 335 ? 1.1297 1.0153 1.3011 0.1804  -0.0352 0.3348  355 TYR   A O   
2296 C  CB  . TYR   A 335 ? 1.2394 1.0695 1.4202 0.2406  -0.0626 0.3894  355 TYR   A CB  
2297 C  CG  . TYR   A 335 ? 1.2413 1.0796 1.3735 0.2129  -0.0773 0.3959  355 TYR   A CG  
2298 C  CD1 . TYR   A 335 ? 1.2478 1.1350 1.3851 0.2162  -0.1056 0.4038  355 TYR   A CD1 
2299 C  CD2 . TYR   A 335 ? 1.2180 1.0146 1.2990 0.1841  -0.0630 0.3948  355 TYR   A CD2 
2300 C  CE1 . TYR   A 335 ? 1.2835 1.1757 1.3694 0.1953  -0.1148 0.4099  355 TYR   A CE1 
2301 C  CE2 . TYR   A 335 ? 1.2574 1.0662 1.2981 0.1612  -0.0710 0.4037  355 TYR   A CE2 
2302 C  CZ  . TYR   A 335 ? 1.2585 1.1138 1.2982 0.1688  -0.0948 0.4111  355 TYR   A CZ  
2303 O  OH  . TYR   A 335 ? 1.1899 1.0550 1.1826 0.1503  -0.0989 0.4200  355 TYR   A OH  
2304 N  N   . LEU   A 336 ? 1.2431 1.0535 1.4259 0.2153  -0.0043 0.3333  356 LEU   A N   
2305 C  CA  . LEU   A 336 ? 1.2589 1.0513 1.4118 0.1898  0.0128  0.3109  356 LEU   A CA  
2306 C  C   . LEU   A 336 ? 1.2127 1.0698 1.3986 0.1811  0.0155  0.2938  356 LEU   A C   
2307 O  O   . LEU   A 336 ? 1.1329 1.0042 1.2968 0.1529  0.0148  0.2814  356 LEU   A O   
2308 C  CB  . LEU   A 336 ? 1.3160 1.0417 1.4502 0.2052  0.0363  0.3011  356 LEU   A CB  
2309 C  CG  . LEU   A 336 ? 1.2576 0.9613 1.3597 0.1836  0.0516  0.2759  356 LEU   A CG  
2310 C  CD1 . LEU   A 336 ? 1.2599 0.9444 1.3189 0.1442  0.0397  0.2753  356 LEU   A CD1 
2311 C  CD2 . LEU   A 336 ? 1.3841 1.0183 1.4622 0.2058  0.0738  0.2645  356 LEU   A CD2 
2312 N  N   . ASP   A 337 ? 1.1994 1.0976 1.4425 0.2052  0.0184  0.2951  357 ASP   A N   
2313 C  CA  . ASP   A 337 ? 1.0812 1.0380 1.3605 0.1967  0.0205  0.2817  357 ASP   A CA  
2314 C  C   . ASP   A 337 ? 1.0498 1.0508 1.3254 0.1746  -0.0059 0.2819  357 ASP   A C   
2315 O  O   . ASP   A 337 ? 1.0179 1.0447 1.2895 0.1550  -0.0040 0.2666  357 ASP   A O   
2316 C  CB  . ASP   A 337 ? 1.0811 1.0760 1.4320 0.2255  0.0275  0.2884  357 ASP   A CB  
2317 C  CG  . ASP   A 337 ? 0.9908 1.0451 1.3855 0.2150  0.0282  0.2779  357 ASP   A CG  
2318 O  OD1 . ASP   A 337 ? 0.9362 0.9816 1.3153 0.2062  0.0508  0.2624  357 ASP   A OD1 
2319 O  OD2 . ASP   A 337 ? 0.9149 1.0213 1.3575 0.2153  0.0042  0.2854  357 ASP   A OD2 
2320 N  N   . MET   A 338 ? 1.0360 1.0424 1.3076 0.1798  -0.0305 0.2992  358 MET   A N   
2321 C  CA  . MET   A 338 ? 1.0494 1.0903 1.3054 0.1628  -0.0550 0.2989  358 MET   A CA  
2322 C  C   . MET   A 338 ? 1.0709 1.0911 1.2687 0.1352  -0.0474 0.2919  358 MET   A C   
2323 O  O   . MET   A 338 ? 1.0479 1.1001 1.2355 0.1189  -0.0544 0.2816  358 MET   A O   
2324 C  CB  . MET   A 338 ? 0.9946 1.0377 1.2474 0.1775  -0.0830 0.3205  358 MET   A CB  
2325 C  CG  . MET   A 338 ? 1.0680 1.1293 1.3824 0.2074  -0.0928 0.3327  358 MET   A CG  
2326 S  SD  . MET   A 338 ? 1.0994 1.1580 1.3990 0.2248  -0.1304 0.3595  358 MET   A SD  
2327 C  CE  . MET   A 338 ? 1.2064 1.2814 1.5876 0.2628  -0.1326 0.3743  358 MET   A CE  
2328 N  N   . VAL   A 339 ? 1.0628 1.0294 1.2247 0.1297  -0.0335 0.2980  359 VAL   A N   
2329 C  CA  . VAL   A 339 ? 1.0869 1.0375 1.2028 0.1016  -0.0278 0.2959  359 VAL   A CA  
2330 C  C   . VAL   A 339 ? 0.9782 0.9459 1.0980 0.0848  -0.0141 0.2726  359 VAL   A C   
2331 O  O   . VAL   A 339 ? 0.9438 0.9374 1.0477 0.0653  -0.0161 0.2670  359 VAL   A O   
2332 C  CB  . VAL   A 339 ? 1.1076 0.9926 1.1902 0.0975  -0.0197 0.3094  359 VAL   A CB  
2333 C  CG1 . VAL   A 339 ? 1.1007 0.9727 1.1494 0.0647  -0.0120 0.3064  359 VAL   A CG1 
2334 C  CG2 . VAL   A 339 ? 1.2031 1.0720 1.2731 0.1118  -0.0347 0.3361  359 VAL   A CG2 
2335 N  N   . VAL   A 340 ? 1.0179 0.9712 1.1566 0.0947  0.0010  0.2599  360 VAL   A N   
2336 C  CA  . VAL   A 340 ? 1.0464 1.0139 1.1848 0.0813  0.0127  0.2394  360 VAL   A CA  
2337 C  C   . VAL   A 340 ? 0.9568 0.9833 1.1277 0.0826  0.0052  0.2315  360 VAL   A C   
2338 O  O   . VAL   A 340 ? 0.9160 0.9630 1.0806 0.0678  0.0085  0.2180  360 VAL   A O   
2339 C  CB  . VAL   A 340 ? 1.1204 1.0498 1.2591 0.0938  0.0326  0.2288  360 VAL   A CB  
2340 C  CG1 . VAL   A 340 ? 1.0797 0.9462 1.1955 0.1043  0.0365  0.2388  360 VAL   A CG1 
2341 C  CG2 . VAL   A 340 ? 1.0309 0.9924 1.2174 0.1165  0.0414  0.2254  360 VAL   A CG2 
2342 N  N   . ASN   A 341 ? 0.9119 0.9648 1.1187 0.1000  -0.0075 0.2398  361 ASN   A N   
2343 C  CA  . ASN   A 341 ? 0.9085 1.0116 1.1474 0.0989  -0.0190 0.2318  361 ASN   A CA  
2344 C  C   . ASN   A 341 ? 0.8981 1.0209 1.1059 0.0841  -0.0360 0.2304  361 ASN   A C   
2345 O  O   . ASN   A 341 ? 0.8418 0.9897 1.0496 0.0737  -0.0367 0.2165  361 ASN   A O   
2346 C  CB  . ASN   A 341 ? 0.9034 1.0299 1.1953 0.1197  -0.0320 0.2417  361 ASN   A CB  
2347 C  CG  . ASN   A 341 ? 0.9442 1.0744 1.2830 0.1342  -0.0106 0.2393  361 ASN   A CG  
2348 O  OD1 . ASN   A 341 ? 0.9738 1.0771 1.2936 0.1324  0.0145  0.2307  361 ASN   A OD1 
2349 N  ND2 . ASN   A 341 ? 0.9748 1.1392 1.3752 0.1492  -0.0208 0.2477  361 ASN   A ND2 
2350 N  N   . GLU   A 342 ? 0.8241 0.9331 1.0022 0.0851  -0.0479 0.2458  362 GLU   A N   
2351 C  CA  . GLU   A 342 ? 0.8882 1.0134 1.0296 0.0748  -0.0597 0.2468  362 GLU   A CA  
2352 C  C   . GLU   A 342 ? 0.8848 1.0077 0.9975 0.0544  -0.0423 0.2393  362 GLU   A C   
2353 O  O   . GLU   A 342 ? 0.8700 1.0184 0.9660 0.0475  -0.0455 0.2317  362 GLU   A O   
2354 C  CB  . GLU   A 342 ? 0.9841 1.0908 1.0952 0.0823  -0.0727 0.2689  362 GLU   A CB  
2355 C  CG  . GLU   A 342 ? 0.9983 1.1145 1.0595 0.0738  -0.0782 0.2742  362 GLU   A CG  
2356 C  CD  . GLU   A 342 ? 1.0088 1.1572 1.0666 0.0817  -0.1013 0.2632  362 GLU   A CD  
2357 O  OE1 . GLU   A 342 ? 0.9617 1.1313 1.0613 0.0853  -0.1100 0.2469  362 GLU   A OE1 
2358 O  OE2 . GLU   A 342 ? 1.0299 1.1790 1.0402 0.0844  -0.1106 0.2713  362 GLU   A OE2 
2359 N  N   . THR   A 343 ? 0.8310 0.9228 0.9381 0.0455  -0.0254 0.2406  363 THR   A N   
2360 C  CA  . THR   A 343 ? 0.8775 0.9714 0.9665 0.0246  -0.0128 0.2336  363 THR   A CA  
2361 C  C   . THR   A 343 ? 0.9088 1.0299 1.0169 0.0230  -0.0083 0.2127  363 THR   A C   
2362 O  O   . THR   A 343 ? 0.8067 0.9510 0.9042 0.0115  -0.0052 0.2061  363 THR   A O   
2363 C  CB  . THR   A 343 ? 0.9162 0.9643 0.9939 0.0143  -0.0017 0.2382  363 THR   A CB  
2364 O  OG1 . THR   A 343 ? 0.9499 0.9671 1.0098 0.0163  -0.0058 0.2597  363 THR   A OG1 
2365 C  CG2 . THR   A 343 ? 0.8830 0.9375 0.9476 -0.0100 0.0058  0.2331  363 THR   A CG2 
2366 N  N   . LEU   A 344 ? 0.8269 0.9464 0.9650 0.0357  -0.0062 0.2042  364 LEU   A N   
2367 C  CA  . LEU   A 344 ? 0.9219 1.0639 1.0783 0.0353  -0.0013 0.1875  364 LEU   A CA  
2368 C  C   . LEU   A 344 ? 0.8800 1.0584 1.0432 0.0371  -0.0153 0.1817  364 LEU   A C   
2369 O  O   . LEU   A 344 ? 0.7262 0.9218 0.8932 0.0329  -0.0120 0.1687  364 LEU   A O   
2370 C  CB  . LEU   A 344 ? 0.8279 0.9597 1.0166 0.0494  0.0080  0.1844  364 LEU   A CB  
2371 C  CG  . LEU   A 344 ? 0.8835 0.9742 1.0566 0.0501  0.0256  0.1824  364 LEU   A CG  
2372 C  CD1 . LEU   A 344 ? 0.9144 0.9969 1.1186 0.0703  0.0387  0.1831  364 LEU   A CD1 
2373 C  CD2 . LEU   A 344 ? 0.8209 0.9097 0.9711 0.0356  0.0327  0.1695  364 LEU   A CD2 
2374 N  N   . ARG   A 345 ? 0.8658 1.0514 1.0263 0.0446  -0.0325 0.1903  365 ARG   A N   
2375 C  CA  . ARG   A 345 ? 0.8686 1.0799 1.0230 0.0469  -0.0491 0.1824  365 ARG   A CA  
2376 C  C   . ARG   A 345 ? 0.9066 1.1269 1.0204 0.0379  -0.0427 0.1800  365 ARG   A C   
2377 O  O   . ARG   A 345 ? 0.8508 1.0884 0.9618 0.0368  -0.0424 0.1659  365 ARG   A O   
2378 C  CB  . ARG   A 345 ? 0.8472 1.0596 1.0014 0.0584  -0.0729 0.1922  365 ARG   A CB  
2379 C  CG  . ARG   A 345 ? 0.8434 1.0742 0.9860 0.0622  -0.0956 0.1810  365 ARG   A CG  
2380 C  CD  . ARG   A 345 ? 0.8867 1.1146 1.0173 0.0736  -0.1232 0.1916  365 ARG   A CD  
2381 N  NE  . ARG   A 345 ? 0.9495 1.1613 1.0287 0.0749  -0.1177 0.2086  365 ARG   A NE  
2382 C  CZ  . ARG   A 345 ? 1.0050 1.2180 1.0292 0.0751  -0.1179 0.2083  365 ARG   A CZ  
2383 N  NH1 . ARG   A 345 ? 1.0435 1.2695 1.0518 0.0763  -0.1248 0.1893  365 ARG   A NH1 
2384 N  NH2 . ARG   A 345 ? 1.0274 1.2256 1.0102 0.0755  -0.1091 0.2287  365 ARG   A NH2 
2385 N  N   . LEU   A 346 ? 0.8599 1.0685 0.9447 0.0320  -0.0358 0.1954  366 LEU   A N   
2386 C  CA  . LEU   A 346 ? 0.9247 1.1481 0.9775 0.0242  -0.0263 0.1980  366 LEU   A CA  
2387 C  C   . LEU   A 346 ? 0.8525 1.0848 0.9166 0.0109  -0.0098 0.1904  366 LEU   A C   
2388 O  O   . LEU   A 346 ? 0.8574 1.1139 0.9096 0.0082  -0.0027 0.1866  366 LEU   A O   
2389 C  CB  . LEU   A 346 ? 0.8927 1.1017 0.9162 0.0201  -0.0225 0.2213  366 LEU   A CB  
2390 C  CG  . LEU   A 346 ? 0.9775 1.1797 0.9754 0.0352  -0.0402 0.2315  366 LEU   A CG  
2391 C  CD1 . LEU   A 346 ? 1.0255 1.2005 1.0047 0.0318  -0.0362 0.2576  366 LEU   A CD1 
2392 C  CD2 . LEU   A 346 ? 1.0535 1.2767 1.0129 0.0430  -0.0430 0.2264  366 LEU   A CD2 
2393 N  N   . PHE   A 347 ? 0.8495 1.0622 0.9342 0.0047  -0.0042 0.1880  367 PHE   A N   
2394 C  CA  . PHE   A 347 ? 0.8625 1.0783 0.9536 -0.0078 0.0066  0.1807  367 PHE   A CA  
2395 C  C   . PHE   A 347 ? 0.8278 1.0329 0.9398 -0.0014 0.0079  0.1665  367 PHE   A C   
2396 O  O   . PHE   A 347 ? 0.7942 0.9697 0.9086 -0.0038 0.0131  0.1670  367 PHE   A O   
2397 C  CB  . PHE   A 347 ? 0.8913 1.0844 0.9736 -0.0248 0.0126  0.1936  367 PHE   A CB  
2398 C  CG  . PHE   A 347 ? 0.8988 1.0997 0.9631 -0.0321 0.0149  0.2131  367 PHE   A CG  
2399 C  CD1 . PHE   A 347 ? 0.8997 1.1379 0.9592 -0.0380 0.0224  0.2167  367 PHE   A CD1 
2400 C  CD2 . PHE   A 347 ? 0.9196 1.0905 0.9715 -0.0310 0.0120  0.2299  367 PHE   A CD2 
2401 C  CE1 . PHE   A 347 ? 0.9628 1.2096 1.0047 -0.0435 0.0296  0.2377  367 PHE   A CE1 
2402 C  CE2 . PHE   A 347 ? 0.9733 1.1487 1.0049 -0.0374 0.0166  0.2512  367 PHE   A CE2 
2403 C  CZ  . PHE   A 347 ? 0.9749 1.1890 1.0011 -0.0441 0.0268  0.2556  367 PHE   A CZ  
2404 N  N   . PRO   A 348 ? 0.8339 1.0585 0.9582 0.0074  0.0046  0.1544  368 PRO   A N   
2405 C  CA  . PRO   A 348 ? 0.8112 1.0269 0.9554 0.0126  0.0098  0.1443  368 PRO   A CA  
2406 C  C   . PRO   A 348 ? 0.8580 1.0725 0.9930 0.0043  0.0183  0.1378  368 PRO   A C   
2407 O  O   . PRO   A 348 ? 0.8734 1.1102 0.9995 -0.0020 0.0176  0.1360  368 PRO   A O   
2408 C  CB  . PRO   A 348 ? 0.8039 1.0393 0.9637 0.0217  0.0011  0.1356  368 PRO   A CB  
2409 C  CG  . PRO   A 348 ? 0.8660 1.1220 1.0024 0.0205  -0.0048 0.1346  368 PRO   A CG  
2410 C  CD  . PRO   A 348 ? 0.7822 1.0322 0.8987 0.0141  -0.0034 0.1496  368 PRO   A CD  
2411 N  N   . ILE   A 349 ? 0.8926 1.0810 1.0286 0.0062  0.0263  0.1347  369 ILE   A N   
2412 C  CA  . ILE   A 349 ? 0.9157 1.0980 1.0374 0.0001  0.0304  0.1276  369 ILE   A CA  
2413 C  C   . ILE   A 349 ? 0.8889 1.0924 1.0196 0.0069  0.0314  0.1193  369 ILE   A C   
2414 O  O   . ILE   A 349 ? 0.8049 1.0197 0.9260 0.0023  0.0296  0.1150  369 ILE   A O   
2415 C  CB  . ILE   A 349 ? 0.9515 1.0914 1.0594 0.0035  0.0389  0.1258  369 ILE   A CB  
2416 C  CG1 . ILE   A 349 ? 0.9926 1.1076 1.0764 -0.0116 0.0334  0.1280  369 ILE   A CG1 
2417 C  CG2 . ILE   A 349 ? 0.9374 1.0696 1.0376 0.0110  0.0469  0.1173  369 ILE   A CG2 
2418 C  CD1 . ILE   A 349 ? 1.0477 1.1108 1.1113 -0.0054 0.0405  0.1261  369 ILE   A CD1 
2419 N  N   . ALA   A 350 ? 0.9280 1.1372 1.0802 0.0175  0.0324  0.1180  370 ALA   A N   
2420 C  CA  . ALA   A 350 ? 0.8744 1.0961 1.0358 0.0234  0.0329  0.1109  370 ALA   A CA  
2421 C  C   . ALA   A 350 ? 0.8733 1.1224 1.0309 0.0231  0.0231  0.1066  370 ALA   A C   
2422 O  O   . ALA   A 350 ? 0.9421 1.2031 1.0914 0.0242  0.0237  0.1018  370 ALA   A O   
2423 C  CB  . ALA   A 350 ? 0.8610 1.0772 1.0527 0.0316  0.0363  0.1124  370 ALA   A CB  
2424 N  N   . MET   A 351 ? 0.8007 1.0587 0.9616 0.0243  0.0141  0.1085  371 MET   A N   
2425 C  CA  . MET   A 351 ? 0.8344 1.1118 0.9848 0.0290  0.0059  0.1029  371 MET   A CA  
2426 C  C   . MET   A 351 ? 0.8085 1.0833 0.9698 0.0373  0.0010  0.0917  371 MET   A C   
2427 O  O   . MET   A 351 ? 0.7213 0.9994 0.8758 0.0434  -0.0104 0.0844  371 MET   A O   
2428 C  CB  . MET   A 351 ? 0.8316 1.1298 0.9640 0.0256  0.0116  0.1049  371 MET   A CB  
2429 C  CG  . MET   A 351 ? 0.8720 1.1744 0.9944 0.0148  0.0141  0.1177  371 MET   A CG  
2430 S  SD  . MET   A 351 ? 0.9970 1.3287 1.1165 0.0059  0.0217  0.1232  371 MET   A SD  
2431 C  CE  . MET   A 351 ? 1.0654 1.3823 1.1935 0.0031  0.0214  0.1160  371 MET   A CE  
2432 N  N   . ARG   A 352 ? 0.7379 1.0021 0.9116 0.0379  0.0092  0.0904  372 ARG   A N   
2433 C  CA  . ARG   A 352 ? 0.8128 1.0680 1.0013 0.0435  0.0063  0.0832  372 ARG   A CA  
2434 C  C   . ARG   A 352 ? 0.7515 0.9901 0.9635 0.0417  0.0175  0.0903  372 ARG   A C   
2435 O  O   . ARG   A 352 ? 0.7576 0.9890 0.9580 0.0411  0.0304  0.0953  372 ARG   A O   
2436 C  CB  . ARG   A 352 ? 0.7845 1.0454 0.9559 0.0509  0.0088  0.0762  372 ARG   A CB  
2437 C  CG  . ARG   A 352 ? 0.8003 1.0758 0.9510 0.0587  0.0010  0.0678  372 ARG   A CG  
2438 C  CD  . ARG   A 352 ? 0.8524 1.1356 0.9918 0.0696  0.0064  0.0629  372 ARG   A CD  
2439 N  NE  . ARG   A 352 ? 0.8121 1.0995 0.9323 0.0832  0.0009  0.0518  372 ARG   A NE  
2440 C  CZ  . ARG   A 352 ? 0.8478 1.1391 0.9580 0.0982  0.0047  0.0456  372 ARG   A CZ  
2441 N  NH1 . ARG   A 352 ? 0.8941 1.1885 1.0134 0.1006  0.0114  0.0505  372 ARG   A NH1 
2442 N  NH2 . ARG   A 352 ? 0.8512 1.1408 0.9378 0.1136  0.0014  0.0341  372 ARG   A NH2 
2443 N  N   . LEU   A 353 ? 0.6698 0.9021 0.9144 0.0409  0.0125  0.0911  373 LEU   A N   
2444 C  CA  . LEU   A 353 ? 0.7431 0.9628 1.0156 0.0409  0.0272  0.0998  373 LEU   A CA  
2445 C  C   . LEU   A 353 ? 0.7350 0.9438 1.0140 0.0426  0.0257  0.0952  373 LEU   A C   
2446 O  O   . LEU   A 353 ? 0.6567 0.8651 0.9376 0.0421  0.0077  0.0847  373 LEU   A O   
2447 C  CB  . LEU   A 353 ? 0.6936 0.9183 1.0110 0.0377  0.0246  0.1082  373 LEU   A CB  
2448 C  CG  . LEU   A 353 ? 0.7578 0.9888 1.0739 0.0388  0.0252  0.1146  373 LEU   A CG  
2449 C  CD1 . LEU   A 353 ? 0.7550 0.9961 1.1251 0.0383  0.0201  0.1238  373 LEU   A CD1 
2450 C  CD2 . LEU   A 353 ? 0.7553 0.9718 1.0457 0.0430  0.0475  0.1203  373 LEU   A CD2 
2451 N  N   . GLU   A 354 ? 0.6630 0.8576 0.9397 0.0459  0.0444  0.1030  374 GLU   A N   
2452 C  CA  . GLU   A 354 ? 0.8158 0.9947 1.0932 0.0487  0.0447  0.1013  374 GLU   A CA  
2453 C  C   . GLU   A 354 ? 0.7855 0.9480 1.0855 0.0486  0.0664  0.1173  374 GLU   A C   
2454 O  O   . GLU   A 354 ? 0.7884 0.9485 1.0810 0.0520  0.0860  0.1277  374 GLU   A O   
2455 C  CB  . GLU   A 354 ? 0.7396 0.9175 0.9732 0.0580  0.0441  0.0945  374 GLU   A CB  
2456 C  CG  . GLU   A 354 ? 0.7679 0.9621 0.9838 0.0609  0.0265  0.0803  374 GLU   A CG  
2457 C  CD  . GLU   A 354 ? 0.7540 0.9559 0.9382 0.0712  0.0279  0.0768  374 GLU   A CD  
2458 O  OE1 . GLU   A 354 ? 0.7808 0.9727 0.9541 0.0756  0.0381  0.0843  374 GLU   A OE1 
2459 O  OE2 . GLU   A 354 ? 0.7663 0.9857 0.9365 0.0764  0.0190  0.0678  374 GLU   A OE2 
2460 N  N   . ARG   A 355 ? 0.7580 0.9058 1.0831 0.0451  0.0636  0.1195  375 ARG   A N   
2461 C  CA  . ARG   A 355 ? 0.8286 0.9590 1.1762 0.0445  0.0862  0.1378  375 ARG   A CA  
2462 C  C   . ARG   A 355 ? 0.7964 0.9007 1.1340 0.0469  0.0813  0.1358  375 ARG   A C   
2463 O  O   . ARG   A 355 ? 0.6279 0.7267 0.9721 0.0431  0.0578  0.1214  375 ARG   A O   
2464 C  CB  . ARG   A 355 ? 0.7452 0.8867 1.1604 0.0324  0.0894  0.1498  375 ARG   A CB  
2465 C  CG  . ARG   A 355 ? 0.7557 0.9204 1.1868 0.0338  0.0983  0.1559  375 ARG   A CG  
2466 C  CD  . ARG   A 355 ? 0.7190 0.8737 1.1206 0.0463  0.1320  0.1692  375 ARG   A CD  
2467 N  NE  . ARG   A 355 ? 0.7903 0.9614 1.2150 0.0499  0.1445  0.1771  375 ARG   A NE  
2468 C  CZ  . ARG   A 355 ? 0.7477 0.9263 1.1467 0.0537  0.1351  0.1672  375 ARG   A CZ  
2469 N  NH1 . ARG   A 355 ? 0.6416 0.8176 0.9945 0.0526  0.1147  0.1503  375 ARG   A NH1 
2470 N  NH2 . ARG   A 355 ? 0.7038 0.8929 1.1267 0.0594  0.1478  0.1761  375 ARG   A NH2 
2471 N  N   . VAL   A 356 ? 0.8617 0.9452 1.1783 0.0551  0.1030  0.1499  376 VAL   A N   
2472 C  CA  . VAL   A 356 ? 0.9007 0.9539 1.2063 0.0597  0.1009  0.1520  376 VAL   A CA  
2473 C  C   . VAL   A 356 ? 0.7962 0.8323 1.1575 0.0459  0.1090  0.1678  376 VAL   A C   
2474 O  O   . VAL   A 356 ? 0.7996 0.8390 1.1873 0.0421  0.1351  0.1892  376 VAL   A O   
2475 C  CB  . VAL   A 356 ? 0.9242 0.9610 1.1768 0.0762  0.1175  0.1616  376 VAL   A CB  
2476 C  CG1 . VAL   A 356 ? 0.8848 0.8858 1.1316 0.0818  0.1190  0.1697  376 VAL   A CG1 
2477 C  CG2 . VAL   A 356 ? 0.8832 0.9391 1.0907 0.0866  0.1028  0.1452  376 VAL   A CG2 
2478 N  N   . CYS   A 357 ? 0.9295 0.9464 1.3095 0.0385  0.0871  0.1576  377 CYS   A N   
2479 C  CA  . CYS   A 357 ? 0.9461 0.9421 1.3828 0.0215  0.0900  0.1723  377 CYS   A CA  
2480 C  C   . CYS   A 357 ? 0.9478 0.9106 1.3680 0.0291  0.1173  0.1959  377 CYS   A C   
2481 O  O   . CYS   A 357 ? 1.0846 1.0197 1.4572 0.0439  0.1126  0.1902  377 CYS   A O   
2482 C  CB  . CYS   A 357 ? 0.9171 0.8917 1.3676 0.0122  0.0545  0.1510  377 CYS   A CB  
2483 S  SG  . CYS   A 357 ? 1.0664 1.0127 1.5947 -0.0152 0.0484  0.1661  377 CYS   A SG  
2484 N  N   . LYS   A 358 ? 0.9602 0.9265 1.4185 0.0213  0.1474  0.2242  378 LYS   A N   
2485 C  CA  . LYS   A 358 ? 1.1101 1.0449 1.5447 0.0307  0.1788  0.2507  378 LYS   A CA  
2486 C  C   . LYS   A 358 ? 1.0856 0.9831 1.5638 0.0151  0.1789  0.2664  378 LYS   A C   
2487 O  O   . LYS   A 358 ? 1.1139 0.9726 1.5594 0.0253  0.1949  0.2832  378 LYS   A O   
2488 C  CB  . LYS   A 358 ? 1.1048 1.0592 1.5456 0.0355  0.2185  0.2755  378 LYS   A CB  
2489 C  CG  . LYS   A 358 ? 1.1040 1.0463 1.4602 0.0612  0.2367  0.2785  378 LYS   A CG  
2490 C  CD  . LYS   A 358 ? 1.1140 1.0710 1.4196 0.0718  0.2068  0.2472  378 LYS   A CD  
2491 C  CE  . LYS   A 358 ? 1.1900 1.1345 1.4159 0.0942  0.2185  0.2498  378 LYS   A CE  
2492 N  NZ  . LYS   A 358 ? 1.0117 0.9768 1.2002 0.1009  0.1901  0.2224  378 LYS   A NZ  
2493 N  N   . LYS   A 359 ? 1.0777 0.9837 1.6289 -0.0101 0.1594  0.2624  379 LYS   A N   
2494 C  CA  . LYS   A 359 ? 1.1560 1.0226 1.7540 -0.0297 0.1532  0.2748  379 LYS   A CA  
2495 C  C   . LYS   A 359 ? 1.1802 1.0502 1.8256 -0.0515 0.1085  0.2490  379 LYS   A C   
2496 O  O   . LYS   A 359 ? 1.1268 1.0374 1.7832 -0.0536 0.0905  0.2307  379 LYS   A O   
2497 C  CB  . LYS   A 359 ? 1.1888 1.0606 1.8482 -0.0438 0.1930  0.3170  379 LYS   A CB  
2498 C  CG  . LYS   A 359 ? 1.1205 1.0500 1.8524 -0.0576 0.2027  0.3265  379 LYS   A CG  
2499 C  CD  . LYS   A 359 ? 1.1179 1.0556 1.9060 -0.0658 0.2506  0.3719  379 LYS   A CD  
2500 C  CE  . LYS   A 359 ? 1.1795 1.0997 1.8889 -0.0364 0.2956  0.3918  379 LYS   A CE  
2501 N  NZ  . LYS   A 359 ? 1.2457 1.1720 2.0021 -0.0407 0.3482  0.4382  379 LYS   A NZ  
2502 N  N   . ASP   A 360 ? 1.2247 1.0461 1.8928 -0.0669 0.0894  0.2477  380 ASP   A N   
2503 C  CA  . ASP   A 360 ? 1.2630 1.0729 1.9622 -0.0861 0.0415  0.2194  380 ASP   A CA  
2504 C  C   . ASP   A 360 ? 1.2523 1.1126 2.0383 -0.1120 0.0322  0.2263  380 ASP   A C   
2505 O  O   . ASP   A 360 ? 1.2715 1.1537 2.1275 -0.1280 0.0604  0.2608  380 ASP   A O   
2506 C  CB  . ASP   A 360 ? 1.3503 1.0916 2.0654 -0.1012 0.0260  0.2217  380 ASP   A CB  
2507 C  CG  . ASP   A 360 ? 1.3650 1.0574 2.0096 -0.0755 0.0463  0.2291  380 ASP   A CG  
2508 O  OD1 . ASP   A 360 ? 1.2031 0.9017 1.8412 -0.0668 0.0884  0.2625  380 ASP   A OD1 
2509 O  OD2 . ASP   A 360 ? 1.4486 1.0954 2.0414 -0.0614 0.0204  0.2020  380 ASP   A OD2 
2510 N  N   . VAL   A 361 ? 1.3035 1.1840 2.0849 -0.1141 -0.0066 0.1950  381 VAL   A N   
2511 C  CA  . VAL   A 361 ? 1.2625 1.1931 2.1212 -0.1350 -0.0226 0.1985  381 VAL   A CA  
2512 C  C   . VAL   A 361 ? 1.2758 1.1860 2.1408 -0.1502 -0.0815 0.1647  381 VAL   A C   
2513 O  O   . VAL   A 361 ? 1.3105 1.1781 2.1021 -0.1360 -0.1057 0.1334  381 VAL   A O   
2514 C  CB  . VAL   A 361 ? 1.1965 1.1862 2.0359 -0.1162 -0.0046 0.1990  381 VAL   A CB  
2515 C  CG1 . VAL   A 361 ? 1.1709 1.2046 2.0809 -0.1227 0.0364  0.2375  381 VAL   A CG1 
2516 C  CG2 . VAL   A 361 ? 1.1738 1.1524 1.9122 -0.0836 0.0133  0.1866  381 VAL   A CG2 
2517 N  N   . GLU   A 362 ? 1.2936 1.2355 2.2473 -0.1776 -0.1045 0.1718  382 GLU   A N   
2518 C  CA  . GLU   A 362 ? 1.3884 1.3239 2.3493 -0.1911 -0.1639 0.1402  382 GLU   A CA  
2519 C  C   . GLU   A 362 ? 1.3708 1.3783 2.3802 -0.1931 -0.1689 0.1475  382 GLU   A C   
2520 O  O   . GLU   A 362 ? 1.3877 1.4374 2.4986 -0.2140 -0.1596 0.1767  382 GLU   A O   
2521 C  CB  . GLU   A 362 ? 1.3966 1.2906 2.4249 -0.2272 -0.1999 0.1402  382 GLU   A CB  
2522 C  CG  . GLU   A 362 ? 1.4103 1.2942 2.4451 -0.2427 -0.2669 0.1067  382 GLU   A CG  
2523 C  CD  . GLU   A 362 ? 1.4533 1.2710 2.5212 -0.2738 -0.3089 0.0956  382 GLU   A CD  
2524 O  OE1 . GLU   A 362 ? 1.4308 1.1941 2.4821 -0.2744 -0.2881 0.1039  382 GLU   A OE1 
2525 O  OE2 . GLU   A 362 ? 1.4356 1.2523 2.5444 -0.2977 -0.3648 0.0784  382 GLU   A OE2 
2526 N  N   . ILE   A 363 ? 1.3338 1.3565 2.2736 -0.1702 -0.1815 0.1233  383 ILE   A N   
2527 C  CA  . ILE   A 363 ? 1.3079 1.3934 2.2782 -0.1661 -0.1841 0.1297  383 ILE   A CA  
2528 C  C   . ILE   A 363 ? 1.3076 1.3855 2.2522 -0.1692 -0.2434 0.0970  383 ILE   A C   
2529 O  O   . ILE   A 363 ? 1.3839 1.4204 2.2359 -0.1532 -0.2616 0.0659  383 ILE   A O   
2530 C  CB  . ILE   A 363 ? 1.3252 1.4370 2.2346 -0.1350 -0.1398 0.1364  383 ILE   A CB  
2531 C  CG1 . ILE   A 363 ? 1.3041 1.3801 2.0999 -0.1110 -0.1462 0.1062  383 ILE   A CG1 
2532 C  CG2 . ILE   A 363 ? 1.2856 1.4026 2.2166 -0.1310 -0.0836 0.1690  383 ILE   A CG2 
2533 C  CD1 . ILE   A 363 ? 1.2723 1.3753 2.0127 -0.0848 -0.1115 0.1106  383 ILE   A CD1 
2534 N  N   . ASN   A 364 ? 1.2815 1.3995 2.3081 -0.1882 -0.2731 0.1053  384 ASN   A N   
2535 C  CA  . ASN   A 364 ? 1.2748 1.3885 2.2822 -0.1922 -0.3338 0.0773  384 ASN   A CA  
2536 C  C   . ASN   A 364 ? 1.3594 1.3988 2.3121 -0.2004 -0.3774 0.0428  384 ASN   A C   
2537 O  O   . ASN   A 364 ? 1.3934 1.4052 2.2644 -0.1867 -0.4125 0.0103  384 ASN   A O   
2538 C  CB  . ASN   A 364 ? 1.2059 1.3416 2.1345 -0.1618 -0.3280 0.0657  384 ASN   A CB  
2539 C  CG  . ASN   A 364 ? 1.1207 1.3246 2.1072 -0.1550 -0.2983 0.0957  384 ASN   A CG  
2540 O  OD1 . ASN   A 364 ? 1.0200 1.2400 1.9964 -0.1399 -0.2445 0.1145  384 ASN   A OD1 
2541 N  ND2 . ASN   A 364 ? 1.0921 1.3337 2.1370 -0.1643 -0.3349 0.0996  384 ASN   A ND2 
2542 N  N   . GLY   A 365 ? 1.4105 1.4131 2.4049 -0.2216 -0.3733 0.0508  385 GLY   A N   
2543 C  CA  . GLY   A 365 ? 1.4084 1.3319 2.3559 -0.2303 -0.4140 0.0189  385 GLY   A CA  
2544 C  C   . GLY   A 365 ? 1.5106 1.3816 2.3348 -0.1974 -0.3948 -0.0055 385 GLY   A C   
2545 O  O   . GLY   A 365 ? 1.5932 1.4123 2.3391 -0.1873 -0.4333 -0.0428 385 GLY   A O   
2546 N  N   . MET   A 366 ? 1.4766 1.3599 2.2807 -0.1787 -0.3366 0.0147  386 MET   A N   
2547 C  CA  . MET   A 366 ? 1.4792 1.3210 2.1779 -0.1468 -0.3163 -0.0041 386 MET   A CA  
2548 C  C   . MET   A 366 ? 1.4284 1.2715 2.1397 -0.1405 -0.2614 0.0251  386 MET   A C   
2549 O  O   . MET   A 366 ? 1.3726 1.2699 2.1283 -0.1410 -0.2242 0.0557  386 MET   A O   
2550 C  CB  . MET   A 366 ? 1.4364 1.3106 2.0589 -0.1164 -0.3093 -0.0181 386 MET   A CB  
2551 C  CG  . MET   A 366 ? 1.4303 1.2684 1.9503 -0.0833 -0.2921 -0.0383 386 MET   A CG  
2552 S  SD  . MET   A 366 ? 1.2899 1.1832 1.7471 -0.0519 -0.2619 -0.0368 386 MET   A SD  
2553 C  CE  . MET   A 366 ? 1.2034 1.1233 1.6675 -0.0607 -0.3065 -0.0495 386 MET   A CE  
2554 N  N   . PHE   A 367 ? 1.4294 1.2095 2.0963 -0.1320 -0.2570 0.0154  387 PHE   A N   
2555 C  CA  . PHE   A 367 ? 1.4025 1.1739 2.0731 -0.1246 -0.2097 0.0426  387 PHE   A CA  
2556 C  C   . PHE   A 367 ? 1.3875 1.1761 1.9766 -0.0869 -0.1765 0.0391  387 PHE   A C   
2557 O  O   . PHE   A 367 ? 1.4501 1.2232 1.9644 -0.0639 -0.1917 0.0096  387 PHE   A O   
2558 C  CB  . PHE   A 367 ? 1.4080 1.0998 2.0744 -0.1335 -0.2221 0.0371  387 PHE   A CB  
2559 C  CG  . PHE   A 367 ? 1.4312 1.1050 2.0854 -0.1206 -0.1762 0.0635  387 PHE   A CG  
2560 C  CD1 . PHE   A 367 ? 1.4578 1.1554 2.1851 -0.1395 -0.1425 0.1051  387 PHE   A CD1 
2561 C  CD2 . PHE   A 367 ? 1.4606 1.0945 2.0292 -0.0876 -0.1661 0.0483  387 PHE   A CD2 
2562 C  CE1 . PHE   A 367 ? 1.4537 1.1306 2.1607 -0.1258 -0.1012 0.1305  387 PHE   A CE1 
2563 C  CE2 . PHE   A 367 ? 1.4362 1.0530 1.9911 -0.0743 -0.1278 0.0735  387 PHE   A CE2 
2564 C  CZ  . PHE   A 367 ? 1.4194 1.0551 2.0394 -0.0936 -0.0961 0.1144  387 PHE   A CZ  
2565 N  N   . ILE   A 368 ? 1.3208 1.1416 1.9252 -0.0807 -0.1310 0.0700  388 ILE   A N   
2566 C  CA  . ILE   A 368 ? 1.3049 1.1443 1.8414 -0.0489 -0.1005 0.0705  388 ILE   A CA  
2567 C  C   . ILE   A 368 ? 1.3079 1.1221 1.8387 -0.0414 -0.0654 0.0954  388 ILE   A C   
2568 O  O   . ILE   A 368 ? 1.2973 1.1228 1.8841 -0.0573 -0.0411 0.1268  388 ILE   A O   
2569 C  CB  . ILE   A 368 ? 1.2647 1.1712 1.8105 -0.0448 -0.0830 0.0810  388 ILE   A CB  
2570 C  CG1 . ILE   A 368 ? 1.2937 1.2222 1.8383 -0.0495 -0.1186 0.0581  388 ILE   A CG1 
2571 C  CG2 . ILE   A 368 ? 1.1888 1.1114 1.6697 -0.0163 -0.0543 0.0827  388 ILE   A CG2 
2572 C  CD1 . ILE   A 368 ? 1.2109 1.1998 1.7694 -0.0467 -0.1042 0.0694  388 ILE   A CD1 
2573 N  N   . PRO   A 369 ? 1.2559 1.0372 1.7206 -0.0156 -0.0605 0.0846  389 PRO   A N   
2574 C  CA  . PRO   A 369 ? 1.2316 0.9861 1.6843 -0.0055 -0.0300 0.1091  389 PRO   A CA  
2575 C  C   . PRO   A 369 ? 1.1752 0.9764 1.6115 0.0082  0.0063  0.1306  389 PRO   A C   
2576 O  O   . PRO   A 369 ? 1.1385 0.9883 1.5622 0.0141  0.0077  0.1229  389 PRO   A O   
2577 C  CB  . PRO   A 369 ? 1.2676 0.9763 1.6538 0.0216  -0.0426 0.0863  389 PRO   A CB  
2578 C  CG  . PRO   A 369 ? 1.2755 0.9759 1.6455 0.0208  -0.0806 0.0497  389 PRO   A CG  
2579 C  CD  . PRO   A 369 ? 1.2684 1.0303 1.6682 0.0065  -0.0843 0.0498  389 PRO   A CD  
2580 N  N   . LYS   A 370 ? 1.1783 0.9579 1.6104 0.0134  0.0350  0.1583  390 LYS   A N   
2581 C  CA  . LYS   A 370 ? 1.1113 0.9217 1.5144 0.0292  0.0677  0.1776  390 LYS   A CA  
2582 C  C   . LYS   A 370 ? 1.1091 0.9315 1.4428 0.0585  0.0613  0.1586  390 LYS   A C   
2583 O  O   . LYS   A 370 ? 1.1004 0.8931 1.4026 0.0734  0.0441  0.1414  390 LYS   A O   
2584 C  CB  . LYS   A 370 ? 1.1840 0.9605 1.5905 0.0299  0.0983  0.2123  390 LYS   A CB  
2585 C  CG  . LYS   A 370 ? 1.2111 0.9875 1.5512 0.0583  0.1204  0.2242  390 LYS   A CG  
2586 C  CD  . LYS   A 370 ? 1.2434 0.9745 1.5363 0.0801  0.1081  0.2169  390 LYS   A CD  
2587 C  CE  . LYS   A 370 ? 1.2376 0.9856 1.4650 0.1099  0.1154  0.2175  390 LYS   A CE  
2588 N  NZ  . LYS   A 370 ? 1.2776 0.9940 1.4652 0.1347  0.0989  0.2061  390 LYS   A NZ  
2589 N  N   . GLY   A 371 ? 1.0771 0.9436 1.3898 0.0668  0.0753  0.1619  391 GLY   A N   
2590 C  CA  . GLY   A 371 ? 1.0557 0.9409 1.3123 0.0910  0.0708  0.1488  391 GLY   A CA  
2591 C  C   . GLY   A 371 ? 0.9293 0.8471 1.1780 0.0930  0.0484  0.1207  391 GLY   A C   
2592 O  O   . GLY   A 371 ? 0.9213 0.8631 1.1322 0.1106  0.0461  0.1119  391 GLY   A O   
2593 N  N   . VAL   A 372 ? 0.8886 0.8084 1.1720 0.0755  0.0313  0.1081  392 VAL   A N   
2594 C  CA  . VAL   A 372 ? 0.9015 0.8502 1.1727 0.0777  0.0116  0.0839  392 VAL   A CA  
2595 C  C   . VAL   A 372 ? 0.8731 0.8687 1.1547 0.0698  0.0216  0.0908  392 VAL   A C   
2596 O  O   . VAL   A 372 ? 0.8469 0.8496 1.1665 0.0548  0.0343  0.1077  392 VAL   A O   
2597 C  CB  . VAL   A 372 ? 0.9720 0.8968 1.2675 0.0639  -0.0156 0.0663  392 VAL   A CB  
2598 C  CG1 . VAL   A 372 ? 0.8842 0.8379 1.1610 0.0670  -0.0343 0.0441  392 VAL   A CG1 
2599 C  CG2 . VAL   A 372 ? 1.0219 0.8912 1.2988 0.0741  -0.0268 0.0563  392 VAL   A CG2 
2600 N  N   . VAL   A 373 ? 0.8965 0.9236 1.1460 0.0808  0.0176  0.0791  393 VAL   A N   
2601 C  CA  . VAL   A 373 ? 0.8024 0.8680 1.0573 0.0737  0.0232  0.0826  393 VAL   A CA  
2602 C  C   . VAL   A 373 ? 0.7743 0.8508 1.0496 0.0624  0.0026  0.0692  393 VAL   A C   
2603 O  O   . VAL   A 373 ? 0.7910 0.8647 1.0431 0.0699  -0.0153 0.0502  393 VAL   A O   
2604 C  CB  . VAL   A 373 ? 0.8366 0.9295 1.0514 0.0876  0.0275  0.0791  393 VAL   A CB  
2605 C  CG1 . VAL   A 373 ? 0.7294 0.8549 0.9483 0.0787  0.0293  0.0801  393 VAL   A CG1 
2606 C  CG2 . VAL   A 373 ? 0.7450 0.8281 0.9390 0.0978  0.0437  0.0935  393 VAL   A CG2 
2607 N  N   . VAL   A 374 ? 0.7682 0.8565 1.0850 0.0467  0.0053  0.0797  394 VAL   A N   
2608 C  CA  . VAL   A 374 ? 0.7574 0.8596 1.0959 0.0363  -0.0166 0.0700  394 VAL   A CA  
2609 C  C   . VAL   A 374 ? 0.7729 0.9089 1.0916 0.0403  -0.0120 0.0702  394 VAL   A C   
2610 O  O   . VAL   A 374 ? 0.7214 0.8712 1.0481 0.0393  0.0082  0.0851  394 VAL   A O   
2611 C  CB  . VAL   A 374 ? 0.7607 0.8621 1.1648 0.0176  -0.0186 0.0832  394 VAL   A CB  
2612 C  CG1 . VAL   A 374 ? 0.7683 0.8863 1.1943 0.0082  -0.0464 0.0734  394 VAL   A CG1 
2613 C  CG2 . VAL   A 374 ? 0.8695 0.9336 1.2963 0.0102  -0.0229 0.0853  394 VAL   A CG2 
2614 N  N   . MET   A 375 ? 0.7446 0.8894 1.0339 0.0457  -0.0296 0.0543  395 MET   A N   
2615 C  CA  A MET   A 375 ? 0.7431 0.9161 1.0104 0.0489  -0.0259 0.0555  395 MET   A CA  
2616 C  CA  B MET   A 375 ? 0.8369 1.0099 1.1040 0.0490  -0.0260 0.0554  395 MET   A CA  
2617 C  C   . MET   A 375 ? 0.7843 0.9676 1.0664 0.0415  -0.0461 0.0519  395 MET   A C   
2618 O  O   . MET   A 375 ? 0.7622 0.9314 1.0437 0.0401  -0.0703 0.0386  395 MET   A O   
2619 C  CB  A MET   A 375 ? 0.7782 0.9586 0.9970 0.0632  -0.0247 0.0451  395 MET   A CB  
2620 C  CB  B MET   A 375 ? 0.7477 0.9279 0.9662 0.0633  -0.0254 0.0446  395 MET   A CB  
2621 C  CG  A MET   A 375 ? 0.7792 0.9884 0.9780 0.0638  -0.0195 0.0491  395 MET   A CG  
2622 C  CG  B MET   A 375 ? 0.8519 1.0609 1.0505 0.0639  -0.0202 0.0486  395 MET   A CG  
2623 S  SD  A MET   A 375 ? 0.5560 0.7726 0.7306 0.0669  -0.0394 0.0376  395 MET   A SD  
2624 S  SD  B MET   A 375 ? 0.8455 1.0687 0.9980 0.0793  -0.0233 0.0364  395 MET   A SD  
2625 C  CE  A MET   A 375 ? 0.7922 0.9978 0.9274 0.0860  -0.0421 0.0203  395 MET   A CE  
2626 C  CE  B MET   A 375 ? 0.8031 1.0109 0.9437 0.0802  -0.0487 0.0219  395 MET   A CE  
2627 N  N   . ILE   A 376 ? 0.7535 0.9571 1.0452 0.0381  -0.0381 0.0634  396 ILE   A N   
2628 C  CA  . ILE   A 376 ? 0.7622 0.9779 1.0641 0.0341  -0.0562 0.0634  396 ILE   A CA  
2629 C  C   . ILE   A 376 ? 0.6875 0.9170 0.9446 0.0409  -0.0522 0.0628  396 ILE   A C   
2630 O  O   . ILE   A 376 ? 0.7210 0.9596 0.9744 0.0405  -0.0336 0.0738  396 ILE   A O   
2631 C  CB  . ILE   A 376 ? 0.7364 0.9631 1.0918 0.0266  -0.0495 0.0801  396 ILE   A CB  
2632 C  CG1 . ILE   A 376 ? 0.7835 1.0020 1.1937 0.0170  -0.0550 0.0837  396 ILE   A CG1 
2633 C  CG2 . ILE   A 376 ? 0.6895 0.9308 1.0501 0.0262  -0.0673 0.0826  396 ILE   A CG2 
2634 C  CD1 . ILE   A 376 ? 0.7601 0.9668 1.1804 0.0173  -0.0271 0.0934  396 ILE   A CD1 
2635 N  N   . PRO   A 377 ? 0.6387 0.8673 0.8586 0.0473  -0.0682 0.0508  397 PRO   A N   
2636 C  CA  . PRO   A 377 ? 0.7589 1.0026 0.9380 0.0532  -0.0604 0.0538  397 PRO   A CA  
2637 C  C   . PRO   A 377 ? 0.7299 0.9830 0.9159 0.0485  -0.0649 0.0662  397 PRO   A C   
2638 O  O   . PRO   A 377 ? 0.7010 0.9533 0.8694 0.0516  -0.0835 0.0638  397 PRO   A O   
2639 C  CB  . PRO   A 377 ? 0.7455 0.9810 0.8821 0.0646  -0.0741 0.0376  397 PRO   A CB  
2640 C  CG  . PRO   A 377 ? 0.7080 0.9221 0.8632 0.0610  -0.1012 0.0265  397 PRO   A CG  
2641 C  CD  . PRO   A 377 ? 0.7431 0.9531 0.9538 0.0498  -0.0941 0.0341  397 PRO   A CD  
2642 N  N   . SER   A 378 ? 0.6609 0.9187 0.8682 0.0430  -0.0477 0.0796  398 SER   A N   
2643 C  CA  . SER   A 378 ? 0.7662 1.0274 0.9836 0.0407  -0.0499 0.0924  398 SER   A CA  
2644 C  C   . SER   A 378 ? 0.7141 0.9807 0.8894 0.0435  -0.0537 0.0959  398 SER   A C   
2645 O  O   . SER   A 378 ? 0.7630 1.0287 0.9344 0.0458  -0.0692 0.1013  398 SER   A O   
2646 C  CB  . SER   A 378 ? 0.7532 1.0104 0.9878 0.0374  -0.0278 0.1034  398 SER   A CB  
2647 O  OG  . SER   A 378 ? 0.7119 0.9638 0.9806 0.0368  -0.0194 0.1031  398 SER   A OG  
2648 N  N   . TYR   A 379 ? 0.7207 0.9946 0.8660 0.0436  -0.0394 0.0952  399 TYR   A N   
2649 C  CA  . TYR   A 379 ? 0.7667 1.0487 0.8750 0.0454  -0.0378 0.1023  399 TYR   A CA  
2650 C  C   . TYR   A 379 ? 0.8433 1.1225 0.9216 0.0559  -0.0564 0.0939  399 TYR   A C   
2651 O  O   . TYR   A 379 ? 0.7990 1.0759 0.8536 0.0587  -0.0645 0.1027  399 TYR   A O   
2652 C  CB  . TYR   A 379 ? 0.7684 1.0663 0.8614 0.0432  -0.0190 0.1039  399 TYR   A CB  
2653 C  CG  . TYR   A 379 ? 0.8386 1.1491 0.9029 0.0417  -0.0112 0.1169  399 TYR   A CG  
2654 C  CD1 . TYR   A 379 ? 0.8774 1.1975 0.9061 0.0536  -0.0116 0.1138  399 TYR   A CD1 
2655 C  CD2 . TYR   A 379 ? 0.8902 1.1992 0.9606 0.0288  -0.0022 0.1329  399 TYR   A CD2 
2656 C  CE1 . TYR   A 379 ? 0.9516 1.2848 0.9546 0.0527  0.0002  0.1295  399 TYR   A CE1 
2657 C  CE2 . TYR   A 379 ? 0.9253 1.2449 0.9738 0.0248  0.0065  0.1483  399 TYR   A CE2 
2658 C  CZ  . TYR   A 379 ? 0.9339 1.2683 0.9504 0.0368  0.0093  0.1482  399 TYR   A CZ  
2659 O  OH  . TYR   A 379 ? 0.9519 1.2985 0.9471 0.0333  0.0223  0.1672  399 TYR   A OH  
2660 N  N   . ALA   A 380 ? 0.8549 1.1287 0.9283 0.0628  -0.0645 0.0765  400 ALA   A N   
2661 C  CA  . ALA   A 380 ? 0.8430 1.1053 0.8794 0.0742  -0.0853 0.0643  400 ALA   A CA  
2662 C  C   . ALA   A 380 ? 0.8364 1.0872 0.8900 0.0712  -0.1140 0.0651  400 ALA   A C   
2663 O  O   . ALA   A 380 ? 0.9146 1.1573 0.9300 0.0792  -0.1326 0.0638  400 ALA   A O   
2664 C  CB  . ALA   A 380 ? 0.8472 1.0978 0.8755 0.0822  -0.0892 0.0437  400 ALA   A CB  
2665 N  N   . LEU   A 381 ? 0.7560 1.0075 0.8672 0.0611  -0.1177 0.0689  401 LEU   A N   
2666 C  CA  . LEU   A 381 ? 0.8485 1.0977 0.9913 0.0581  -0.1444 0.0728  401 LEU   A CA  
2667 C  C   . LEU   A 381 ? 0.8744 1.1302 1.0132 0.0596  -0.1422 0.0924  401 LEU   A C   
2668 O  O   . LEU   A 381 ? 0.9246 1.1778 1.0606 0.0637  -0.1688 0.0960  401 LEU   A O   
2669 C  CB  . LEU   A 381 ? 0.8150 1.0679 1.0269 0.0484  -0.1429 0.0741  401 LEU   A CB  
2670 C  CG  . LEU   A 381 ? 0.8320 1.0724 1.0544 0.0452  -0.1495 0.0570  401 LEU   A CG  
2671 C  CD1 . LEU   A 381 ? 0.7592 1.0048 1.0515 0.0348  -0.1414 0.0645  401 LEU   A CD1 
2672 C  CD2 . LEU   A 381 ? 0.8994 1.1232 1.0985 0.0480  -0.1874 0.0401  401 LEU   A CD2 
2673 N  N   . HIS   A 382 ? 0.7943 1.0553 0.9316 0.0564  -0.1135 0.1053  402 HIS   A N   
2674 C  CA  . HIS   A 382 ? 0.9107 1.1699 1.0400 0.0576  -0.1103 0.1244  402 HIS   A CA  
2675 C  C   . HIS   A 382 ? 0.9509 1.2058 1.0191 0.0651  -0.1176 0.1288  402 HIS   A C   
2676 O  O   . HIS   A 382 ? 0.8965 1.1452 0.9533 0.0693  -0.1271 0.1439  402 HIS   A O   
2677 C  CB  . HIS   A 382 ? 0.8408 1.0990 0.9791 0.0503  -0.0803 0.1346  402 HIS   A CB  
2678 C  CG  . HIS   A 382 ? 0.7754 1.0323 0.9644 0.0468  -0.0703 0.1345  402 HIS   A CG  
2679 N  ND1 . HIS   A 382 ? 0.7519 0.9999 0.9458 0.0422  -0.0473 0.1414  402 HIS   A ND1 
2680 C  CD2 . HIS   A 382 ? 0.8012 1.0631 1.0362 0.0477  -0.0790 0.1294  402 HIS   A CD2 
2681 C  CE1 . HIS   A 382 ? 0.7647 1.0110 0.9989 0.0435  -0.0397 0.1402  402 HIS   A CE1 
2682 N  NE2 . HIS   A 382 ? 0.7029 0.9604 0.9671 0.0460  -0.0570 0.1348  402 HIS   A NE2 
2683 N  N   . ARG   A 383 ? 0.9329 1.1900 0.9597 0.0693  -0.1114 0.1174  403 ARG   A N   
2684 C  CA  . ARG   A 383 ? 0.9912 1.2446 0.9539 0.0796  -0.1126 0.1220  403 ARG   A CA  
2685 C  C   . ARG   A 383 ? 1.0824 1.3221 1.0089 0.0922  -0.1426 0.1039  403 ARG   A C   
2686 O  O   . ARG   A 383 ? 1.1039 1.3376 0.9669 0.1048  -0.1398 0.1011  403 ARG   A O   
2687 C  CB  . ARG   A 383 ? 0.9313 1.1986 0.8698 0.0790  -0.0812 0.1240  403 ARG   A CB  
2688 C  CG  . ARG   A 383 ? 0.9675 1.2457 0.9384 0.0641  -0.0560 0.1393  403 ARG   A CG  
2689 C  CD  . ARG   A 383 ? 1.0120 1.2817 0.9730 0.0593  -0.0527 0.1634  403 ARG   A CD  
2690 N  NE  . ARG   A 383 ? 0.9861 1.2604 0.9690 0.0437  -0.0301 0.1762  403 ARG   A NE  
2691 C  CZ  . ARG   A 383 ? 0.9974 1.2862 0.9639 0.0369  -0.0092 0.1884  403 ARG   A CZ  
2692 N  NH1 . ARG   A 383 ? 1.0307 1.3327 0.9565 0.0474  -0.0019 0.1915  403 ARG   A NH1 
2693 N  NH2 . ARG   A 383 ? 0.9334 1.2230 0.9252 0.0196  0.0047  0.1982  403 ARG   A NH2 
2694 N  N   . ASP   A 384 ? 1.1030 1.3364 1.0679 0.0891  -0.1712 0.0920  404 ASP   A N   
2695 C  CA  . ASP   A 384 ? 1.1735 1.3885 1.1078 0.0976  -0.2051 0.0708  404 ASP   A CA  
2696 C  C   . ASP   A 384 ? 1.2505 1.4542 1.1474 0.1069  -0.2358 0.0785  404 ASP   A C   
2697 O  O   . ASP   A 384 ? 1.2708 1.4821 1.2121 0.1018  -0.2520 0.0922  404 ASP   A O   
2698 C  CB  . ASP   A 384 ? 1.1601 1.3740 1.1588 0.0866  -0.2251 0.0569  404 ASP   A CB  
2699 C  CG  . ASP   A 384 ? 1.2671 1.4553 1.2343 0.0920  -0.2571 0.0301  404 ASP   A CG  
2700 O  OD1 . ASP   A 384 ? 1.3127 1.4820 1.2014 0.1076  -0.2655 0.0210  404 ASP   A OD1 
2701 O  OD2 . ASP   A 384 ? 1.2348 1.4185 1.2535 0.0810  -0.2731 0.0185  404 ASP   A OD2 
2702 N  N   . PRO   A 385 ? 1.3669 1.5519 1.1805 0.1229  -0.2440 0.0713  405 PRO   A N   
2703 C  CA  . PRO   A 385 ? 1.4172 1.5869 1.1859 0.1338  -0.2773 0.0784  405 PRO   A CA  
2704 C  C   . PRO   A 385 ? 1.4732 1.6336 1.2747 0.1297  -0.3304 0.0639  405 PRO   A C   
2705 O  O   . PRO   A 385 ? 1.5537 1.7067 1.3348 0.1369  -0.3634 0.0726  405 PRO   A O   
2706 C  CB  . PRO   A 385 ? 1.4568 1.6049 1.1220 0.1542  -0.2697 0.0697  405 PRO   A CB  
2707 C  CG  . PRO   A 385 ? 1.4623 1.6270 1.1303 0.1528  -0.2207 0.0705  405 PRO   A CG  
2708 C  CD  . PRO   A 385 ? 1.3777 1.5561 1.1308 0.1350  -0.2184 0.0600  405 PRO   A CD  
2709 N  N   . LYS   A 386 ? 1.4481 1.6088 1.3015 0.1179  -0.3410 0.0437  406 LYS   A N   
2710 C  CA  . LYS   A 386 ? 1.5356 1.6923 1.4361 0.1090  -0.3915 0.0323  406 LYS   A CA  
2711 C  C   . LYS   A 386 ? 1.4848 1.6742 1.4817 0.0970  -0.3951 0.0549  406 LYS   A C   
2712 O  O   . LYS   A 386 ? 1.5989 1.7936 1.6357 0.0927  -0.4396 0.0545  406 LYS   A O   
2713 C  CB  . LYS   A 386 ? 1.5671 1.7095 1.4923 0.0988  -0.3997 0.0054  406 LYS   A CB  
2714 C  CG  . LYS   A 386 ? 1.7907 1.8895 1.6236 0.1128  -0.4207 -0.0241 406 LYS   A CG  
2715 C  CD  . LYS   A 386 ? 1.9462 2.0209 1.7578 0.1136  -0.4853 -0.0380 406 LYS   A CD  
2716 C  CE  . LYS   A 386 ? 2.0299 2.0512 1.7442 0.1283  -0.5084 -0.0720 406 LYS   A CE  
2717 N  NZ  . LYS   A 386 ? 2.0326 2.0255 1.7313 0.1251  -0.5790 -0.0899 406 LYS   A NZ  
2718 N  N   . TYR   A 387 ? 1.3615 1.5725 1.3968 0.0926  -0.3505 0.0742  407 TYR   A N   
2719 C  CA  . TYR   A 387 ? 1.3106 1.5484 1.4294 0.0862  -0.3471 0.0958  407 TYR   A CA  
2720 C  C   . TYR   A 387 ? 1.2863 1.5269 1.3825 0.0963  -0.3278 0.1219  407 TYR   A C   
2721 O  O   . TYR   A 387 ? 1.2741 1.5312 1.4284 0.0970  -0.3312 0.1403  407 TYR   A O   
2722 C  CB  . TYR   A 387 ? 1.2176 1.4715 1.4061 0.0728  -0.3130 0.0960  407 TYR   A CB  
2723 C  CG  . TYR   A 387 ? 1.2520 1.5033 1.4798 0.0605  -0.3310 0.0758  407 TYR   A CG  
2724 C  CD1 . TYR   A 387 ? 1.2494 1.5135 1.5440 0.0519  -0.3701 0.0753  407 TYR   A CD1 
2725 C  CD2 . TYR   A 387 ? 1.3242 1.5605 1.5268 0.0570  -0.3096 0.0590  407 TYR   A CD2 
2726 C  CE1 . TYR   A 387 ? 1.2357 1.4941 1.5702 0.0372  -0.3873 0.0587  407 TYR   A CE1 
2727 C  CE2 . TYR   A 387 ? 1.3193 1.5464 1.5562 0.0455  -0.3259 0.0420  407 TYR   A CE2 
2728 C  CZ  . TYR   A 387 ? 1.3133 1.5499 1.6159 0.0341  -0.3645 0.0420  407 TYR   A CZ  
2729 O  OH  . TYR   A 387 ? 1.3476 1.5720 1.6881 0.0194  -0.3814 0.0268  407 TYR   A OH  
2730 N  N   . TRP   A 388 ? 1.2913 1.5157 1.3076 0.1045  -0.3065 0.1254  408 TRP   A N   
2731 C  CA  . TRP   A 388 ? 1.2925 1.5134 1.2827 0.1119  -0.2885 0.1517  408 TRP   A CA  
2732 C  C   . TRP   A 388 ? 1.3666 1.5658 1.2590 0.1262  -0.2987 0.1539  408 TRP   A C   
2733 O  O   . TRP   A 388 ? 1.3944 1.5838 1.2311 0.1293  -0.2876 0.1385  408 TRP   A O   
2734 C  CB  . TRP   A 388 ? 1.2388 1.4645 1.2410 0.1032  -0.2385 0.1611  408 TRP   A CB  
2735 C  CG  . TRP   A 388 ? 1.1755 1.4162 1.2485 0.0907  -0.2218 0.1517  408 TRP   A CG  
2736 C  CD1 . TRP   A 388 ? 1.1398 1.3835 1.2157 0.0834  -0.2090 0.1324  408 TRP   A CD1 
2737 C  CD2 . TRP   A 388 ? 1.0796 1.3316 1.2257 0.0870  -0.2138 0.1627  408 TRP   A CD2 
2738 N  NE1 . TRP   A 388 ? 1.0242 1.2797 1.1679 0.0741  -0.1944 0.1319  408 TRP   A NE1 
2739 C  CE2 . TRP   A 388 ? 0.9566 1.2177 1.1432 0.0766  -0.1955 0.1500  408 TRP   A CE2 
2740 C  CE3 . TRP   A 388 ? 1.0287 1.2822 1.2075 0.0941  -0.2189 0.1830  408 TRP   A CE3 
2741 C  CZ2 . TRP   A 388 ? 0.8643 1.1359 1.1184 0.0733  -0.1801 0.1570  408 TRP   A CZ2 
2742 C  CZ3 . TRP   A 388 ? 0.9946 1.2596 1.2439 0.0921  -0.2031 0.1886  408 TRP   A CZ3 
2743 C  CH2 . TRP   A 388 ? 0.9177 1.1916 1.2019 0.0818  -0.1830 0.1757  408 TRP   A CH2 
2744 N  N   . THR   A 389 ? 1.3757 1.5662 1.2451 0.1374  -0.3179 0.1742  409 THR   A N   
2745 C  CA  . THR   A 389 ? 1.4980 1.6652 1.2682 0.1529  -0.3227 0.1823  409 THR   A CA  
2746 C  C   . THR   A 389 ? 1.4833 1.6472 1.2224 0.1506  -0.2730 0.2043  409 THR   A C   
2747 O  O   . THR   A 389 ? 1.4257 1.5941 1.2089 0.1432  -0.2533 0.2248  409 THR   A O   
2748 C  CB  . THR   A 389 ? 1.5204 1.6776 1.2761 0.1667  -0.3653 0.1979  409 THR   A CB  
2749 O  OG1 . THR   A 389 ? 1.5048 1.6700 1.3150 0.1650  -0.3523 0.2251  409 THR   A OG1 
2750 C  CG2 . THR   A 389 ? 1.5160 1.6807 1.3114 0.1658  -0.4197 0.1766  409 THR   A CG2 
2751 N  N   . GLU   A 390 ? 1.4497 1.6046 1.1133 0.1574  -0.2530 0.2004  410 GLU   A N   
2752 C  CA  . GLU   A 390 ? 1.4181 1.5772 1.0610 0.1517  -0.2039 0.2199  410 GLU   A CA  
2753 C  C   . GLU   A 390 ? 1.3171 1.4968 1.0410 0.1311  -0.1764 0.2178  410 GLU   A C   
2754 O  O   . GLU   A 390 ? 1.2356 1.4137 0.9904 0.1216  -0.1592 0.2396  410 GLU   A O   
2755 C  CB  . GLU   A 390 ? 1.4536 1.5953 1.0597 0.1580  -0.1985 0.2554  410 GLU   A CB  
2756 C  CG  . GLU   A 390 ? 1.5595 1.6782 1.0653 0.1803  -0.2150 0.2618  410 GLU   A CG  
2757 C  CD  . GLU   A 390 ? 1.6692 1.7668 1.1393 0.1875  -0.2127 0.2999  410 GLU   A CD  
2758 O  OE1 . GLU   A 390 ? 1.6537 1.7487 1.1800 0.1813  -0.2227 0.3147  410 GLU   A OE1 
2759 O  OE2 . GLU   A 390 ? 1.7585 1.8399 1.1422 0.2012  -0.1990 0.3163  410 GLU   A OE2 
2760 N  N   . PRO   A 391 ? 1.2916 1.4857 1.0461 0.1248  -0.1727 0.1917  411 PRO   A N   
2761 C  CA  . PRO   A 391 ? 1.2577 1.4677 1.0883 0.1075  -0.1541 0.1881  411 PRO   A CA  
2762 C  C   . PRO   A 391 ? 1.1804 1.3989 1.0139 0.0955  -0.1130 0.2037  411 PRO   A C   
2763 O  O   . PRO   A 391 ? 1.1202 1.3434 1.0074 0.0818  -0.0999 0.2062  411 PRO   A O   
2764 C  CB  . PRO   A 391 ? 1.2399 1.4582 1.0874 0.1068  -0.1626 0.1578  411 PRO   A CB  
2765 C  CG  . PRO   A 391 ? 1.3444 1.5532 1.1141 0.1221  -0.1654 0.1476  411 PRO   A CG  
2766 C  CD  . PRO   A 391 ? 1.3313 1.5222 1.0451 0.1350  -0.1838 0.1647  411 PRO   A CD  
2767 N  N   . GLU   A 392 ? 1.2238 1.4444 1.0019 0.1000  -0.0924 0.2148  412 GLU   A N   
2768 C  CA  . GLU   A 392 ? 1.1930 1.4260 0.9821 0.0854  -0.0557 0.2323  412 GLU   A CA  
2769 C  C   . GLU   A 392 ? 1.1621 1.3770 0.9559 0.0765  -0.0498 0.2621  412 GLU   A C   
2770 O  O   . GLU   A 392 ? 1.1136 1.3339 0.9231 0.0600  -0.0235 0.2777  412 GLU   A O   
2771 C  CB  . GLU   A 392 ? 1.2016 1.4496 0.9383 0.0938  -0.0317 0.2365  412 GLU   A CB  
2772 C  CG  . GLU   A 392 ? 1.2141 1.4926 0.9844 0.0811  -0.0013 0.2337  412 GLU   A CG  
2773 C  CD  . GLU   A 392 ? 1.2566 1.5463 1.0500 0.0861  -0.0093 0.2020  412 GLU   A CD  
2774 O  OE1 . GLU   A 392 ? 1.2284 1.5013 1.0143 0.0967  -0.0381 0.1820  412 GLU   A OE1 
2775 O  OE2 . GLU   A 392 ? 1.2136 1.5287 1.0347 0.0788  0.0117  0.1983  412 GLU   A OE2 
2776 N  N   . LYS   A 393 ? 1.2047 1.3970 0.9875 0.0869  -0.0755 0.2705  413 LYS   A N   
2777 C  CA  . LYS   A 393 ? 1.2599 1.4280 1.0410 0.0827  -0.0717 0.2998  413 LYS   A CA  
2778 C  C   . LYS   A 393 ? 1.2040 1.3615 1.0490 0.0740  -0.0768 0.2968  413 LYS   A C   
2779 O  O   . LYS   A 393 ? 1.1703 1.3367 1.0549 0.0783  -0.0941 0.2763  413 LYS   A O   
2780 C  CB  . LYS   A 393 ? 1.3239 1.4711 1.0533 0.1028  -0.0972 0.3138  413 LYS   A CB  
2781 C  CG  . LYS   A 393 ? 1.3847 1.5310 1.0347 0.1138  -0.0860 0.3258  413 LYS   A CG  
2782 C  CD  . LYS   A 393 ? 1.4900 1.6080 1.0839 0.1332  -0.1109 0.3454  413 LYS   A CD  
2783 C  CE  . LYS   A 393 ? 1.5507 1.6616 1.0579 0.1445  -0.0915 0.3651  413 LYS   A CE  
2784 N  NZ  . LYS   A 393 ? 1.5288 1.6077 0.9736 0.1649  -0.1168 0.3867  413 LYS   A NZ  
2785 N  N   . PHE   A 394 ? 1.1730 1.3088 1.0264 0.0619  -0.0601 0.3184  414 PHE   A N   
2786 C  CA  . PHE   A 394 ? 1.1250 1.2401 1.0263 0.0574  -0.0619 0.3180  414 PHE   A CA  
2787 C  C   . PHE   A 394 ? 1.1375 1.2285 1.0339 0.0762  -0.0850 0.3332  414 PHE   A C   
2788 O  O   . PHE   A 394 ? 1.2025 1.2660 1.0652 0.0785  -0.0826 0.3602  414 PHE   A O   
2789 C  CB  . PHE   A 394 ? 1.1505 1.2460 1.0588 0.0355  -0.0366 0.3315  414 PHE   A CB  
2790 C  CG  . PHE   A 394 ? 1.1480 1.2061 1.0859 0.0348  -0.0379 0.3355  414 PHE   A CG  
2791 C  CD1 . PHE   A 394 ? 1.0275 1.0878 1.0076 0.0343  -0.0371 0.3135  414 PHE   A CD1 
2792 C  CD2 . PHE   A 394 ? 1.1837 1.2002 1.1026 0.0367  -0.0379 0.3623  414 PHE   A CD2 
2793 C  CE1 . PHE   A 394 ? 1.0167 1.0388 1.0169 0.0379  -0.0351 0.3162  414 PHE   A CE1 
2794 C  CE2 . PHE   A 394 ? 1.1457 1.1216 1.0872 0.0396  -0.0381 0.3646  414 PHE   A CE2 
2795 C  CZ  . PHE   A 394 ? 1.1568 1.1358 1.1378 0.0412  -0.0360 0.3407  414 PHE   A CZ  
2796 N  N   . LEU   A 395 ? 1.1443 1.2471 1.0775 0.0898  -0.1077 0.3182  415 LEU   A N   
2797 C  CA  . LEU   A 395 ? 1.1421 1.2315 1.0819 0.1101  -0.1340 0.3316  415 LEU   A CA  
2798 C  C   . LEU   A 395 ? 1.1530 1.2478 1.1623 0.1163  -0.1380 0.3210  415 LEU   A C   
2799 O  O   . LEU   A 395 ? 1.1718 1.2967 1.2188 0.1208  -0.1540 0.3027  415 LEU   A O   
2800 C  CB  . LEU   A 395 ? 1.1348 1.2414 1.0428 0.1248  -0.1661 0.3273  415 LEU   A CB  
2801 C  CG  . LEU   A 395 ? 1.2374 1.3318 1.0647 0.1279  -0.1639 0.3434  415 LEU   A CG  
2802 C  CD1 . LEU   A 395 ? 1.2911 1.4007 1.0819 0.1418  -0.1957 0.3289  415 LEU   A CD1 
2803 C  CD2 . LEU   A 395 ? 1.2048 1.2630 1.0040 0.1370  -0.1653 0.3777  415 LEU   A CD2 
2804 N  N   . PRO   A 396 ? 1.1755 1.2391 1.2029 0.1171  -0.1225 0.3328  416 PRO   A N   
2805 C  CA  . PRO   A 396 ? 1.1403 1.2072 1.2301 0.1270  -0.1200 0.3241  416 PRO   A CA  
2806 C  C   . PRO   A 396 ? 1.1516 1.2371 1.2797 0.1507  -0.1494 0.3307  416 PRO   A C   
2807 O  O   . PRO   A 396 ? 1.0485 1.1487 1.2372 0.1603  -0.1466 0.3241  416 PRO   A O   
2808 C  CB  . PRO   A 396 ? 1.1405 1.1580 1.2227 0.1252  -0.0975 0.3367  416 PRO   A CB  
2809 C  CG  . PRO   A 396 ? 1.2114 1.1999 1.2373 0.1211  -0.1000 0.3607  416 PRO   A CG  
2810 C  CD  . PRO   A 396 ? 1.1530 1.1733 1.1436 0.1091  -0.1048 0.3547  416 PRO   A CD  
2811 N  N   . GLU   A 397 ? 1.2570 1.3440 1.3526 0.1612  -0.1775 0.3447  417 GLU   A N   
2812 C  CA  . GLU   A 397 ? 1.2519 1.3620 1.3874 0.1824  -0.2124 0.3504  417 GLU   A CA  
2813 C  C   . GLU   A 397 ? 1.2068 1.3640 1.3882 0.1773  -0.2308 0.3272  417 GLU   A C   
2814 O  O   . GLU   A 397 ? 1.1990 1.3831 1.4367 0.1912  -0.2578 0.3301  417 GLU   A O   
2815 C  CB  . GLU   A 397 ? 1.2993 1.3951 1.3779 0.1949  -0.2416 0.3707  417 GLU   A CB  
2816 C  CG  . GLU   A 397 ? 1.4783 1.5351 1.5485 0.2133  -0.2401 0.4006  417 GLU   A CG  
2817 C  CD  . GLU   A 397 ? 1.5251 1.5976 1.6742 0.2359  -0.2522 0.4062  417 GLU   A CD  
2818 O  OE1 . GLU   A 397 ? 1.5165 1.6283 1.7041 0.2474  -0.2886 0.4036  417 GLU   A OE1 
2819 O  OE2 . GLU   A 397 ? 1.4889 1.5347 1.6632 0.2426  -0.2255 0.4129  417 GLU   A OE2 
2820 N  N   . ARG   A 398 ? 1.1432 1.3111 1.3068 0.1577  -0.2174 0.3056  418 ARG   A N   
2821 C  CA  . ARG   A 398 ? 1.1619 1.3673 1.3727 0.1513  -0.2316 0.2837  418 ARG   A CA  
2822 C  C   . ARG   A 398 ? 1.1691 1.3938 1.4662 0.1564  -0.2194 0.2833  418 ARG   A C   
2823 O  O   . ARG   A 398 ? 1.1878 1.4473 1.5445 0.1568  -0.2398 0.2756  418 ARG   A O   
2824 C  CB  . ARG   A 398 ? 1.1126 1.3204 1.2915 0.1317  -0.2126 0.2622  418 ARG   A CB  
2825 C  CG  . ARG   A 398 ? 1.1168 1.3097 1.2117 0.1280  -0.2159 0.2619  418 ARG   A CG  
2826 C  CD  . ARG   A 398 ? 0.9753 1.1769 1.0534 0.1122  -0.1960 0.2403  418 ARG   A CD  
2827 N  NE  . ARG   A 398 ? 1.0694 1.2588 1.0717 0.1096  -0.1863 0.2433  418 ARG   A NE  
2828 C  CZ  . ARG   A 398 ? 1.2040 1.3946 1.1551 0.1164  -0.2072 0.2352  418 ARG   A CZ  
2829 N  NH1 . ARG   A 398 ? 1.2106 1.4104 1.1759 0.1236  -0.2452 0.2219  418 ARG   A NH1 
2830 N  NH2 . ARG   A 398 ? 1.2212 1.4026 1.1051 0.1160  -0.1896 0.2406  418 ARG   A NH2 
2831 N  N   . PHE   A 399 ? 1.0759 1.2764 1.3800 0.1603  -0.1857 0.2917  419 PHE   A N   
2832 C  CA  . PHE   A 399 ? 1.0701 1.2828 1.4452 0.1690  -0.1659 0.2921  419 PHE   A CA  
2833 C  C   . PHE   A 399 ? 1.1332 1.3390 1.5426 0.1952  -0.1712 0.3146  419 PHE   A C   
2834 O  O   . PHE   A 399 ? 1.1418 1.3389 1.5877 0.2075  -0.1436 0.3187  419 PHE   A O   
2835 C  CB  . PHE   A 399 ? 1.0243 1.2105 1.3797 0.1582  -0.1241 0.2819  419 PHE   A CB  
2836 C  CG  . PHE   A 399 ? 0.9947 1.1941 1.3323 0.1362  -0.1169 0.2606  419 PHE   A CG  
2837 C  CD1 . PHE   A 399 ? 0.9792 1.1665 1.2520 0.1215  -0.1199 0.2551  419 PHE   A CD1 
2838 C  CD2 . PHE   A 399 ? 0.9504 1.1746 1.3374 0.1320  -0.1053 0.2483  419 PHE   A CD2 
2839 C  CE1 . PHE   A 399 ? 0.9004 1.1004 1.1590 0.1051  -0.1129 0.2362  419 PHE   A CE1 
2840 C  CE2 . PHE   A 399 ? 0.9017 1.1343 1.2711 0.1140  -0.0996 0.2299  419 PHE   A CE2 
2841 C  CZ  . PHE   A 399 ? 0.9187 1.1394 1.2243 0.1016  -0.1041 0.2231  419 PHE   A CZ  
2842 N  N   . SER   A 400 ? 1.1929 1.4002 1.5875 0.2067  -0.2060 0.3296  420 SER   A N   
2843 C  CA  . SER   A 400 ? 1.2648 1.4685 1.6954 0.2346  -0.2155 0.3528  420 SER   A CA  
2844 C  C   . SER   A 400 ? 1.3068 1.5652 1.8401 0.2466  -0.2271 0.3544  420 SER   A C   
2845 O  O   . SER   A 400 ? 1.3039 1.5989 1.8770 0.2309  -0.2294 0.3383  420 SER   A O   
2846 C  CB  . SER   A 400 ? 1.3828 1.5723 1.7637 0.2441  -0.2522 0.3699  420 SER   A CB  
2847 O  OG  . SER   A 400 ? 1.4673 1.6944 1.8551 0.2379  -0.2946 0.3616  420 SER   A OG  
2848 N  N   . LYS   A 401 ? 1.2970 1.5612 1.8774 0.2754  -0.2339 0.3763  421 LYS   A N   
2849 C  CA  . LYS   A 401 ? 1.3005 1.6215 1.9881 0.2886  -0.2413 0.3819  421 LYS   A CA  
2850 C  C   . LYS   A 401 ? 1.3481 1.7147 2.0599 0.2701  -0.2854 0.3680  421 LYS   A C   
2851 O  O   . LYS   A 401 ? 1.2774 1.6841 2.0526 0.2567  -0.2802 0.3551  421 LYS   A O   
2852 C  CB  . LYS   A 401 ? 1.2577 1.5690 1.9657 0.3188  -0.2406 0.3981  421 LYS   A CB  
2853 C  CG  . LYS   A 401 ? 1.2219 1.5902 2.0170 0.3248  -0.2532 0.3953  421 LYS   A CG  
2854 C  CD  . LYS   A 401 ? 1.2224 1.5880 2.0227 0.3517  -0.2769 0.4114  421 LYS   A CD  
2855 C  CE  . LYS   A 401 ? 1.1998 1.6296 2.0857 0.3525  -0.3000 0.4093  421 LYS   A CE  
2856 N  NZ  . LYS   A 401 ? 1.2150 1.6781 2.1044 0.3234  -0.3409 0.3939  421 LYS   A NZ  
2857 N  N   . LYS   A 402 ? 1.5141 1.8698 2.1702 0.2689  -0.3284 0.3703  422 LYS   A N   
2858 C  CA  . LYS   A 402 ? 1.4611 1.8503 2.1286 0.2539  -0.3741 0.3548  422 LYS   A CA  
2859 C  C   . LYS   A 402 ? 1.5093 1.8979 2.1435 0.2268  -0.3801 0.3348  422 LYS   A C   
2860 O  O   . LYS   A 402 ? 1.5543 1.9735 2.2253 0.2095  -0.4015 0.3167  422 LYS   A O   
2861 C  CB  . LYS   A 402 ? 1.5214 1.8952 2.1338 0.2676  -0.4179 0.3638  422 LYS   A CB  
2862 C  CG  . LYS   A 402 ? 1.5671 1.8893 2.0717 0.2687  -0.4198 0.3731  422 LYS   A CG  
2863 C  CD  . LYS   A 402 ? 1.6913 1.9783 2.1595 0.2953  -0.4197 0.3986  422 LYS   A CD  
2864 C  CE  . LYS   A 402 ? 1.7569 1.9920 2.1156 0.2930  -0.4191 0.4112  422 LYS   A CE  
2865 N  NZ  . LYS   A 402 ? 1.7436 1.9536 2.0694 0.2722  -0.3706 0.3999  422 LYS   A NZ  
2866 N  N   . ASN   A 403 ? 1.4053 1.7532 1.9608 0.2197  -0.3551 0.3319  423 ASN   A N   
2867 C  CA  . ASN   A 403 ? 1.3489 1.6883 1.8534 0.1944  -0.3530 0.3060  423 ASN   A CA  
2868 C  C   . ASN   A 403 ? 1.2959 1.6476 1.8435 0.1787  -0.3133 0.2911  423 ASN   A C   
2869 O  O   . ASN   A 403 ? 1.3174 1.6651 1.8338 0.1590  -0.3110 0.2697  423 ASN   A O   
2870 C  CB  . ASN   A 403 ? 1.3592 1.6498 1.7512 0.1913  -0.3386 0.3051  423 ASN   A CB  
2871 C  CG  . ASN   A 403 ? 1.4176 1.6895 1.7553 0.2084  -0.3730 0.3233  423 ASN   A CG  
2872 O  OD1 . ASN   A 403 ? 1.3473 1.5803 1.6212 0.2147  -0.3540 0.3378  423 ASN   A OD1 
2873 N  ND2 . ASN   A 403 ? 1.5535 1.8513 1.9168 0.2152  -0.4254 0.3239  423 ASN   A ND2 
2874 N  N   . LYS   A 404 ? 1.3249 1.6885 1.9385 0.1896  -0.2813 0.3026  424 LYS   A N   
2875 C  CA  . LYS   A 404 ? 1.2746 1.6492 1.9279 0.1779  -0.2431 0.2914  424 LYS   A CA  
2876 C  C   . LYS   A 404 ? 1.2855 1.7042 2.0085 0.1622  -0.2659 0.2813  424 LYS   A C   
2877 O  O   . LYS   A 404 ? 1.2717 1.6913 2.0005 0.1457  -0.2426 0.2669  424 LYS   A O   
2878 C  CB  . LYS   A 404 ? 1.2562 1.6303 1.9586 0.1988  -0.2044 0.3078  424 LYS   A CB  
2879 C  CG  . LYS   A 404 ? 1.2656 1.6628 2.0315 0.1943  -0.1687 0.3034  424 LYS   A CG  
2880 C  CD  . LYS   A 404 ? 1.2430 1.6904 2.1139 0.2063  -0.1758 0.3179  424 LYS   A CD  
2881 C  CE  . LYS   A 404 ? 1.1887 1.6551 2.1121 0.1984  -0.1362 0.3135  424 LYS   A CE  
2882 N  NZ  . LYS   A 404 ? 1.0765 1.5816 2.0791 0.2019  -0.1365 0.3217  424 LYS   A NZ  
2883 N  N   . ASP   A 405 ? 1.2887 1.7401 2.0611 0.1655  -0.3125 0.2878  425 ASP   A N   
2884 C  CA  . ASP   A 405 ? 1.2758 1.7575 2.1047 0.1449  -0.3299 0.2731  425 ASP   A CA  
2885 C  C   . ASP   A 405 ? 1.3013 1.7701 2.0814 0.1239  -0.3609 0.2510  425 ASP   A C   
2886 O  O   . ASP   A 405 ? 1.2712 1.7524 2.0886 0.1038  -0.3604 0.2374  425 ASP   A O   
2887 C  CB  . ASP   A 405 ? 1.2935 1.8021 2.1703 0.1507  -0.3628 0.2792  425 ASP   A CB  
2888 C  CG  . ASP   A 405 ? 1.3676 1.8941 2.3044 0.1718  -0.3306 0.2998  425 ASP   A CG  
2889 O  OD1 . ASP   A 405 ? 1.3199 1.8370 2.2647 0.1796  -0.2808 0.3063  425 ASP   A OD1 
2890 O  OD2 . ASP   A 405 ? 1.4019 1.9503 2.3746 0.1823  -0.3552 0.3089  425 ASP   A OD2 
2891 N  N   . ASN   A 406 ? 1.2751 1.7124 1.9633 0.1283  -0.3835 0.2459  426 ASN   A N   
2892 C  CA  . ASN   A 406 ? 1.2741 1.6892 1.8960 0.1118  -0.4077 0.2201  426 ASN   A CA  
2893 C  C   . ASN   A 406 ? 1.2732 1.6668 1.8580 0.0983  -0.3641 0.2034  426 ASN   A C   
2894 O  O   . ASN   A 406 ? 1.2923 1.6683 1.8299 0.0860  -0.3788 0.1812  426 ASN   A O   
2895 C  CB  . ASN   A 406 ? 1.3489 1.7313 1.8682 0.1233  -0.4339 0.2191  426 ASN   A CB  
2896 C  CG  . ASN   A 406 ? 1.3858 1.7849 1.9296 0.1382  -0.4820 0.2349  426 ASN   A CG  
2897 O  OD1 . ASN   A 406 ? 1.4034 1.8026 1.9539 0.1571  -0.4695 0.2575  426 ASN   A OD1 
2898 N  ND2 . ASN   A 406 ? 1.3894 1.7920 1.9297 0.1286  -0.5257 0.2164  426 ASN   A ND2 
2899 N  N   . ILE   A 407 ? 1.2049 1.5969 1.8069 0.1020  -0.3130 0.2128  427 ILE   A N   
2900 C  CA  . ILE   A 407 ? 1.1393 1.5110 1.7044 0.0911  -0.2731 0.1990  427 ILE   A CA  
2901 C  C   . ILE   A 407 ? 1.0460 1.4410 1.6886 0.0780  -0.2610 0.1950  427 ILE   A C   
2902 O  O   . ILE   A 407 ? 1.0226 1.4460 1.7473 0.0834  -0.2479 0.2115  427 ILE   A O   
2903 C  CB  . ILE   A 407 ? 1.1069 1.4572 1.6387 0.1012  -0.2281 0.2100  427 ILE   A CB  
2904 C  CG1 . ILE   A 407 ? 1.1298 1.4561 1.5919 0.1126  -0.2398 0.2189  427 ILE   A CG1 
2905 C  CG2 . ILE   A 407 ? 1.0239 1.3553 1.5166 0.0896  -0.1929 0.1957  427 ILE   A CG2 
2906 C  CD1 . ILE   A 407 ? 1.0568 1.3572 1.4909 0.1206  -0.2013 0.2311  427 ILE   A CD1 
2907 N  N   . ASP   A 408 ? 0.9918 1.3742 1.6088 0.0625  -0.2631 0.1748  428 ASP   A N   
2908 C  CA  . ASP   A 408 ? 0.8844 1.2817 1.5669 0.0489  -0.2486 0.1723  428 ASP   A CA  
2909 C  C   . ASP   A 408 ? 0.8063 1.1917 1.4752 0.0521  -0.1932 0.1764  428 ASP   A C   
2910 O  O   . ASP   A 408 ? 0.8025 1.1598 1.3946 0.0532  -0.1762 0.1661  428 ASP   A O   
2911 C  CB  . ASP   A 408 ? 0.8931 1.2744 1.5508 0.0324  -0.2759 0.1488  428 ASP   A CB  
2912 C  CG  . ASP   A 408 ? 0.8265 1.2234 1.5639 0.0155  -0.2715 0.1494  428 ASP   A CG  
2913 O  OD1 . ASP   A 408 ? 0.7661 1.1660 1.5269 0.0155  -0.2268 0.1584  428 ASP   A OD1 
2914 O  OD2 . ASP   A 408 ? 0.8029 1.2060 1.5773 0.0017  -0.3138 0.1412  428 ASP   A OD2 
2915 N  N   . PRO   A 409 ? 0.7875 1.1939 1.5281 0.0547  -0.1645 0.1920  429 PRO   A N   
2916 C  CA  . PRO   A 409 ? 0.7098 1.0991 1.4277 0.0604  -0.1136 0.1952  429 PRO   A CA  
2917 C  C   . PRO   A 409 ? 0.7477 1.1176 1.4328 0.0471  -0.0997 0.1800  429 PRO   A C   
2918 O  O   . PRO   A 409 ? 0.7489 1.1045 1.4153 0.0511  -0.0610 0.1823  429 PRO   A O   
2919 C  CB  . PRO   A 409 ? 0.7312 1.1504 1.5382 0.0691  -0.0893 0.2169  429 PRO   A CB  
2920 C  CG  . PRO   A 409 ? 0.7464 1.2021 1.6352 0.0569  -0.1261 0.2214  429 PRO   A CG  
2921 C  CD  . PRO   A 409 ? 0.7379 1.1859 1.5839 0.0539  -0.1768 0.2089  429 PRO   A CD  
2922 N  N   . TYR   A 410 ? 0.7283 1.0937 1.4024 0.0333  -0.1310 0.1641  430 TYR   A N   
2923 C  CA  . TYR   A 410 ? 0.7711 1.1143 1.4086 0.0237  -0.1204 0.1491  430 TYR   A CA  
2924 C  C   . TYR   A 410 ? 0.8443 1.1640 1.3983 0.0240  -0.1397 0.1291  430 TYR   A C   
2925 O  O   . TYR   A 410 ? 0.8287 1.1300 1.3501 0.0186  -0.1362 0.1148  430 TYR   A O   
2926 C  CB  . TYR   A 410 ? 0.7591 1.1118 1.4617 0.0079  -0.1335 0.1485  430 TYR   A CB  
2927 C  CG  . TYR   A 410 ? 0.7367 1.1171 1.5259 0.0081  -0.1071 0.1721  430 TYR   A CG  
2928 C  CD1 . TYR   A 410 ? 0.7370 1.1086 1.5219 0.0135  -0.0599 0.1815  430 TYR   A CD1 
2929 C  CD2 . TYR   A 410 ? 0.7347 1.1513 1.6090 0.0050  -0.1287 0.1863  430 TYR   A CD2 
2930 C  CE1 . TYR   A 410 ? 0.7043 1.1003 1.5628 0.0173  -0.0303 0.2046  430 TYR   A CE1 
2931 C  CE2 . TYR   A 410 ? 0.6912 1.1387 1.6502 0.0076  -0.0997 0.2107  430 TYR   A CE2 
2932 C  CZ  . TYR   A 410 ? 0.6703 1.1063 1.6186 0.0146  -0.0481 0.2199  430 TYR   A CZ  
2933 O  OH  . TYR   A 410 ? 0.7349 1.1993 1.7603 0.0203  -0.0142 0.2453  430 TYR   A OH  
2934 N  N   . ILE   A 411 ? 0.8092 1.1287 1.3279 0.0321  -0.1579 0.1296  431 ILE   A N   
2935 C  CA  . ILE   A 411 ? 0.8737 1.1732 1.3083 0.0363  -0.1639 0.1166  431 ILE   A CA  
2936 C  C   . ILE   A 411 ? 0.8264 1.1191 1.2213 0.0441  -0.1334 0.1261  431 ILE   A C   
2937 O  O   . ILE   A 411 ? 0.7899 1.0700 1.1318 0.0439  -0.1183 0.1183  431 ILE   A O   
2938 C  CB  . ILE   A 411 ? 0.8413 1.1400 1.2533 0.0396  -0.2069 0.1112  431 ILE   A CB  
2939 C  CG1 . ILE   A 411 ? 0.9354 1.2370 1.3901 0.0289  -0.2431 0.1001  431 ILE   A CG1 
2940 C  CG2 . ILE   A 411 ? 0.9182 1.1965 1.2403 0.0461  -0.2081 0.0994  431 ILE   A CG2 
2941 C  CD1 . ILE   A 411 ? 0.9702 1.2508 1.4048 0.0210  -0.2397 0.0808  431 ILE   A CD1 
2942 N  N   . TYR   A 412 ? 0.8256 1.1259 1.2491 0.0512  -0.1249 0.1432  432 TYR   A N   
2943 C  CA  . TYR   A 412 ? 0.7572 1.0440 1.1497 0.0572  -0.0970 0.1525  432 TYR   A CA  
2944 C  C   . TYR   A 412 ? 0.7039 0.9894 1.1309 0.0582  -0.0642 0.1579  432 TYR   A C   
2945 O  O   . TYR   A 412 ? 0.6911 0.9879 1.1720 0.0654  -0.0573 0.1705  432 TYR   A O   
2946 C  CB  . TYR   A 412 ? 0.8018 1.0882 1.1947 0.0676  -0.1088 0.1675  432 TYR   A CB  
2947 C  CG  . TYR   A 412 ? 0.7523 1.0179 1.1208 0.0734  -0.0817 0.1780  432 TYR   A CG  
2948 C  CD1 . TYR   A 412 ? 0.7578 1.0043 1.0639 0.0682  -0.0731 0.1756  432 TYR   A CD1 
2949 C  CD2 . TYR   A 412 ? 0.7308 0.9945 1.1399 0.0843  -0.0648 0.1906  432 TYR   A CD2 
2950 C  CE1 . TYR   A 412 ? 0.7740 0.9964 1.0591 0.0700  -0.0525 0.1843  432 TYR   A CE1 
2951 C  CE2 . TYR   A 412 ? 0.7736 1.0087 1.1541 0.0902  -0.0425 0.1974  432 TYR   A CE2 
2952 C  CZ  . TYR   A 412 ? 0.7471 0.9597 1.0656 0.0812  -0.0386 0.1937  432 TYR   A CZ  
2953 O  OH  . TYR   A 412 ? 0.8793 1.0585 1.1707 0.0836  -0.0203 0.1996  432 TYR   A OH  
2954 N  N   . THR   A 413 ? 0.7228 0.9950 1.1173 0.0530  -0.0434 0.1493  433 THR   A N   
2955 C  CA  . THR   A 413 ? 0.7065 0.9714 1.1180 0.0551  -0.0124 0.1528  433 THR   A CA  
2956 C  C   . THR   A 413 ? 0.7204 0.9619 1.0753 0.0543  0.0066  0.1489  433 THR   A C   
2957 O  O   . THR   A 413 ? 0.7870 1.0230 1.1180 0.0489  0.0148  0.1399  433 THR   A O   
2958 C  CB  . THR   A 413 ? 0.7448 1.0173 1.1832 0.0479  -0.0111 0.1466  433 THR   A CB  
2959 O  OG1 . THR   A 413 ? 0.8040 1.0727 1.2037 0.0407  -0.0276 0.1313  433 THR   A OG1 
2960 C  CG2 . THR   A 413 ? 0.6702 0.9657 1.1803 0.0461  -0.0262 0.1542  433 THR   A CG2 
2961 N  N   . PRO   A 414 ? 0.7484 0.9743 1.0826 0.0594  0.0118  0.1560  434 PRO   A N   
2962 C  CA  . PRO   A 414 ? 0.7875 0.9892 1.0716 0.0549  0.0253  0.1520  434 PRO   A CA  
2963 C  C   . PRO   A 414 ? 0.7223 0.9051 1.0017 0.0593  0.0505  0.1500  434 PRO   A C   
2964 O  O   . PRO   A 414 ? 0.7096 0.8777 0.9502 0.0527  0.0563  0.1427  434 PRO   A O   
2965 C  CB  . PRO   A 414 ? 0.7480 0.9324 1.0174 0.0590  0.0219  0.1618  434 PRO   A CB  
2966 C  CG  . PRO   A 414 ? 0.6694 0.8641 0.9876 0.0727  0.0190  0.1724  434 PRO   A CG  
2967 C  CD  . PRO   A 414 ? 0.7105 0.9378 1.0673 0.0692  0.0036  0.1685  434 PRO   A CD  
2968 N  N   . PHE   A 415 ? 0.7176 0.9015 1.0354 0.0712  0.0655  0.1576  435 PHE   A N   
2969 C  CA  . PHE   A 415 ? 0.7772 0.9422 1.0870 0.0791  0.0930  0.1576  435 PHE   A CA  
2970 C  C   . PHE   A 415 ? 0.7864 0.9720 1.1328 0.0778  0.0998  0.1594  435 PHE   A C   
2971 O  O   . PHE   A 415 ? 0.7448 0.9188 1.0939 0.0869  0.1259  0.1644  435 PHE   A O   
2972 C  CB  . PHE   A 415 ? 0.7613 0.9071 1.0820 0.0975  0.1136  0.1675  435 PHE   A CB  
2973 C  CG  . PHE   A 415 ? 0.8783 0.9900 1.1557 0.0993  0.1100  0.1653  435 PHE   A CG  
2974 C  CD1 . PHE   A 415 ? 0.9110 0.9800 1.1314 0.0997  0.1218  0.1565  435 PHE   A CD1 
2975 C  CD2 . PHE   A 415 ? 0.7734 0.8916 1.0651 0.1002  0.0926  0.1725  435 PHE   A CD2 
2976 C  CE1 . PHE   A 415 ? 0.9830 1.0151 1.1658 0.0983  0.1162  0.1543  435 PHE   A CE1 
2977 C  CE2 . PHE   A 415 ? 0.9087 0.9904 1.1614 0.1007  0.0900  0.1728  435 PHE   A CE2 
2978 C  CZ  . PHE   A 415 ? 0.8793 0.9173 1.0796 0.0985  0.1017  0.1634  435 PHE   A CZ  
2979 N  N   . GLY   A 416 ? 0.7780 0.9892 1.1484 0.0671  0.0772  0.1558  436 GLY   A N   
2980 C  CA  . GLY   A 416 ? 0.7569 0.9818 1.1666 0.0643  0.0829  0.1589  436 GLY   A CA  
2981 C  C   . GLY   A 416 ? 0.7735 1.0173 1.2516 0.0720  0.0933  0.1750  436 GLY   A C   
2982 O  O   . GLY   A 416 ? 0.7843 1.0349 1.2820 0.0806  0.0906  0.1824  436 GLY   A O   
2983 N  N   . SER   A 417 ? 0.7512 1.0050 1.2701 0.0692  0.1059  0.1826  437 SER   A N   
2984 C  CA  . SER   A 417 ? 0.7090 0.9863 1.3027 0.0759  0.1220  0.2019  437 SER   A CA  
2985 C  C   . SER   A 417 ? 0.7352 1.0102 1.3496 0.0734  0.1479  0.2116  437 SER   A C   
2986 O  O   . SER   A 417 ? 0.6816 0.9373 1.2557 0.0658  0.1462  0.2023  437 SER   A O   
2987 C  CB  . SER   A 417 ? 0.7165 1.0287 1.3758 0.0665  0.0879  0.2049  437 SER   A CB  
2988 O  OG  . SER   A 417 ? 0.7539 1.0702 1.4228 0.0482  0.0621  0.1951  437 SER   A OG  
2989 N  N   . GLY   A 418 ? 0.7353 1.0310 1.4151 0.0813  0.1738  0.2329  438 GLY   A N   
2990 C  CA  . GLY   A 418 ? 0.7446 1.0395 1.4503 0.0796  0.2036  0.2480  438 GLY   A CA  
2991 C  C   . GLY   A 418 ? 0.7701 1.0318 1.4151 0.1002  0.2476  0.2533  438 GLY   A C   
2992 O  O   . GLY   A 418 ? 0.7678 1.0073 1.3583 0.1159  0.2550  0.2451  438 GLY   A O   
2993 N  N   . PRO   A 419 ? 0.8020 1.0549 1.4516 0.1004  0.2766  0.2672  439 PRO   A N   
2994 C  CA  . PRO   A 419 ? 0.8095 1.0265 1.3935 0.1225  0.3193  0.2732  439 PRO   A CA  
2995 C  C   . PRO   A 419 ? 0.8697 1.0427 1.3477 0.1258  0.3062  0.2496  439 PRO   A C   
2996 O  O   . PRO   A 419 ? 0.8704 1.0087 1.2833 0.1456  0.3326  0.2487  439 PRO   A O   
2997 C  CB  . PRO   A 419 ? 0.9506 1.1693 1.5656 0.1178  0.3469  0.2950  439 PRO   A CB  
2998 C  CG  . PRO   A 419 ? 0.8612 1.1268 1.5862 0.0968  0.3282  0.3071  439 PRO   A CG  
2999 C  CD  . PRO   A 419 ? 0.8141 1.0889 1.5356 0.0820  0.2745  0.2820  439 PRO   A CD  
3000 N  N   . ARG   A 420 ? 0.8145 0.9875 1.2729 0.1077  0.2663  0.2308  440 ARG   A N   
3001 C  CA  . ARG   A 420 ? 0.9193 1.0602 1.2904 0.1085  0.2511  0.2105  440 ARG   A CA  
3002 C  C   . ARG   A 420 ? 0.8388 0.9844 1.1946 0.1040  0.2221  0.1939  440 ARG   A C   
3003 O  O   . ARG   A 420 ? 0.8727 1.0085 1.1823 0.0957  0.1981  0.1775  440 ARG   A O   
3004 C  CB  . ARG   A 420 ? 0.8733 1.0092 1.2271 0.0954  0.2327  0.2036  440 ARG   A CB  
3005 C  CG  . ARG   A 420 ? 0.9366 1.0503 1.2707 0.1028  0.2613  0.2180  440 ARG   A CG  
3006 C  CD  . ARG   A 420 ? 0.9444 1.0357 1.2181 0.1002  0.2445  0.2061  440 ARG   A CD  
3007 N  NE  . ARG   A 420 ? 1.0066 1.0678 1.1986 0.1127  0.2473  0.1960  440 ARG   A NE  
3008 C  CZ  . ARG   A 420 ? 1.0361 1.0704 1.1682 0.1191  0.2474  0.1943  440 ARG   A CZ  
3009 N  NH1 . ARG   A 420 ? 1.0223 1.0533 1.1639 0.1166  0.2490  0.2037  440 ARG   A NH1 
3010 N  NH2 . ARG   A 420 ? 1.0049 1.0124 1.0656 0.1282  0.2437  0.1832  440 ARG   A NH2 
3011 N  N   . ASN   A 421 ? 0.8861 1.0479 1.2822 0.1103  0.2249  0.2002  441 ASN   A N   
3012 C  CA  . ASN   A 421 ? 0.8294 0.9901 1.2072 0.1078  0.2005  0.1880  441 ASN   A CA  
3013 C  C   . ASN   A 421 ? 0.8763 0.9933 1.1760 0.1186  0.2108  0.1782  441 ASN   A C   
3014 O  O   . ASN   A 421 ? 0.8774 0.9650 1.1334 0.1295  0.2346  0.1792  441 ASN   A O   
3015 C  CB  . ASN   A 421 ? 0.7996 0.9877 1.2429 0.1139  0.1993  0.1995  441 ASN   A CB  
3016 C  CG  . ASN   A 421 ? 0.8160 0.9887 1.2599 0.1385  0.2360  0.2114  441 ASN   A CG  
3017 O  OD1 . ASN   A 421 ? 0.8987 1.0523 1.3214 0.1509  0.2697  0.2182  441 ASN   A OD1 
3018 N  ND2 . ASN   A 421 ? 0.8709 1.0490 1.3351 0.1485  0.2308  0.2145  441 ASN   A ND2 
3019 N  N   . CYS   A 422 ? 0.9393 1.0484 1.2182 0.1151  0.1911  0.1690  442 CYS   A N   
3020 C  CA  . CYS   A 422 ? 0.9948 1.0587 1.2036 0.1214  0.1951  0.1586  442 CYS   A CA  
3021 C  C   . CYS   A 422 ? 0.9962 1.0320 1.1965 0.1469  0.2298  0.1666  442 CYS   A C   
3022 O  O   . CYS   A 422 ? 0.9181 0.9644 1.1592 0.1584  0.2370  0.1759  442 CYS   A O   
3023 C  CB  . CYS   A 422 ? 0.9690 1.0311 1.1673 0.1104  0.1679  0.1511  442 CYS   A CB  
3024 S  SG  . CYS   A 422 ? 0.8607 0.8634 0.9786 0.1117  0.1663  0.1380  442 CYS   A SG  
3025 N  N   . ILE   A 423 ? 0.9790 0.9781 1.1233 0.1584  0.2516  0.1633  443 ILE   A N   
3026 C  CA  . ILE   A 423 ? 1.0355 1.0035 1.1616 0.1870  0.2898  0.1705  443 ILE   A CA  
3027 C  C   . ILE   A 423 ? 1.1374 1.0608 1.2202 0.1975  0.2862  0.1598  443 ILE   A C   
3028 O  O   . ILE   A 423 ? 1.1629 1.0672 1.2481 0.2241  0.3156  0.1669  443 ILE   A O   
3029 C  CB  . ILE   A 423 ? 1.0057 0.9408 1.0713 0.1982  0.3135  0.1698  443 ILE   A CB  
3030 C  CG1 . ILE   A 423 ? 1.1606 1.0752 1.2209 0.2312  0.3622  0.1833  443 ILE   A CG1 
3031 C  CG2 . ILE   A 423 ? 1.1061 0.9905 1.0797 0.1918  0.2919  0.1480  443 ILE   A CG2 
3032 C  CD1 . ILE   A 423 ? 1.2674 1.1427 1.2558 0.2461  0.3884  0.1841  443 ILE   A CD1 
3033 N  N   . GLY   A 424 ? 1.0924 0.9982 1.1385 0.1778  0.2523  0.1442  444 GLY   A N   
3034 C  CA  . GLY   A 424 ? 1.2141 1.0723 1.2201 0.1835  0.2455  0.1346  444 GLY   A CA  
3035 C  C   . GLY   A 424 ? 1.1849 1.0711 1.2413 0.1725  0.2234  0.1405  444 GLY   A C   
3036 O  O   . GLY   A 424 ? 1.2678 1.1215 1.2927 0.1637  0.2044  0.1323  444 GLY   A O   
3037 N  N   . MET   A 425 ? 1.0730 1.0172 1.2070 0.1721  0.2243  0.1557  445 MET   A N   
3038 C  CA  . MET   A 425 ? 1.0320 1.0049 1.2108 0.1628  0.2003  0.1624  445 MET   A CA  
3039 C  C   . MET   A 425 ? 1.1131 1.0503 1.2841 0.1826  0.2080  0.1662  445 MET   A C   
3040 O  O   . MET   A 425 ? 1.0767 0.9944 1.2283 0.1720  0.1859  0.1632  445 MET   A O   
3041 C  CB  . MET   A 425 ? 0.9245 0.9609 1.1857 0.1615  0.1985  0.1769  445 MET   A CB  
3042 C  CG  . MET   A 425 ? 0.8876 0.9502 1.1961 0.1612  0.1776  0.1866  445 MET   A CG  
3043 S  SD  . MET   A 425 ? 0.9060 1.0373 1.3159 0.1634  0.1748  0.2039  445 MET   A SD  
3044 C  CE  . MET   A 425 ? 0.9840 1.1107 1.4211 0.1931  0.2240  0.2170  445 MET   A CE  
3045 N  N   . ARG   A 426 ? 1.1727 1.0996 1.3589 0.2129  0.2414  0.1746  446 ARG   A N   
3046 C  CA  A ARG   A 426 ? 1.1750 1.0679 1.3581 0.2372  0.2512  0.1794  446 ARG   A CA  
3047 C  CA  B ARG   A 426 ? 1.2632 1.1561 1.4463 0.2372  0.2511  0.1794  446 ARG   A CA  
3048 C  C   . ARG   A 426 ? 1.2558 1.0669 1.3481 0.2392  0.2500  0.1614  446 ARG   A C   
3049 O  O   . ARG   A 426 ? 1.2500 1.0243 1.3282 0.2464  0.2420  0.1617  446 ARG   A O   
3050 C  CB  A ARG   A 426 ? 1.2126 1.1214 1.4415 0.2724  0.2911  0.1948  446 ARG   A CB  
3051 C  CB  B ARG   A 426 ? 1.2307 1.1402 1.4602 0.2722  0.2909  0.1949  446 ARG   A CB  
3052 C  CG  A ARG   A 426 ? 1.1600 1.1504 1.4904 0.2685  0.2886  0.2146  446 ARG   A CG  
3053 C  CG  B ARG   A 426 ? 1.1779 1.1690 1.5090 0.2676  0.2870  0.2145  446 ARG   A CG  
3054 C  CD  A ARG   A 426 ? 1.1704 1.1824 1.5618 0.3042  0.3253  0.2344  446 ARG   A CD  
3055 C  CD  B ARG   A 426 ? 1.1727 1.1887 1.5623 0.3006  0.3283  0.2337  446 ARG   A CD  
3056 N  NE  A ARG   A 426 ? 1.2628 1.2520 1.6237 0.3252  0.3709  0.2348  446 ARG   A NE  
3057 N  NE  B ARG   A 426 ? 1.1054 1.2008 1.6001 0.2915  0.3182  0.2528  446 ARG   A NE  
3058 C  CZ  A ARG   A 426 ? 1.3316 1.3348 1.7350 0.3599  0.4137  0.2525  446 ARG   A CZ  
3059 C  CZ  B ARG   A 426 ? 1.0945 1.2335 1.6681 0.3126  0.3484  0.2746  446 ARG   A CZ  
3060 N  NH1 A ARG   A 426 ? 1.2665 1.3091 1.7507 0.3780  0.4152  0.2711  446 ARG   A NH1 
3061 N  NH1 B ARG   A 426 ? 1.1585 1.2706 1.7150 0.3472  0.3955  0.2810  446 ARG   A NH1 
3062 N  NH2 A ARG   A 426 ? 1.4241 1.4027 1.7879 0.3785  0.4568  0.2531  446 ARG   A NH2 
3063 N  NH2 B ARG   A 426 ? 1.0468 1.2568 1.7176 0.2979  0.3302  0.2902  446 ARG   A NH2 
3064 N  N   . PHE   A 427 ? 1.2752 1.0535 1.3044 0.2326  0.2552  0.1458  447 PHE   A N   
3065 C  CA  . PHE   A 427 ? 1.3632 1.0637 1.3062 0.2276  0.2443  0.1262  447 PHE   A CA  
3066 C  C   . PHE   A 427 ? 1.3698 1.0741 1.3091 0.1916  0.2035  0.1219  447 PHE   A C   
3067 O  O   . PHE   A 427 ? 1.3976 1.0471 1.2992 0.1872  0.1904  0.1153  447 PHE   A O   
3068 C  CB  . PHE   A 427 ? 1.4227 1.0902 1.2985 0.2289  0.2546  0.1110  447 PHE   A CB  
3069 C  CG  . PHE   A 427 ? 1.4956 1.0930 1.2880 0.2126  0.2300  0.0889  447 PHE   A CG  
3070 C  CD1 . PHE   A 427 ? 1.6120 1.1284 1.3466 0.2308  0.2359  0.0775  447 PHE   A CD1 
3071 C  CD2 . PHE   A 427 ? 1.5104 1.1222 1.2850 0.1794  0.1997  0.0796  447 PHE   A CD2 
3072 C  CE1 . PHE   A 427 ? 1.7078 1.1563 1.3683 0.2123  0.2087  0.0564  447 PHE   A CE1 
3073 C  CE2 . PHE   A 427 ? 1.5446 1.0971 1.2521 0.1615  0.1735  0.0607  447 PHE   A CE2 
3074 C  CZ  . PHE   A 427 ? 1.6861 1.1556 1.3364 0.1761  0.1764  0.0486  447 PHE   A CZ  
3075 N  N   . ALA   A 428 ? 1.2978 1.0645 1.2761 0.1662  0.1848  0.1267  448 ALA   A N   
3076 C  CA  . ALA   A 428 ? 1.3241 1.1025 1.3032 0.1343  0.1513  0.1258  448 ALA   A CA  
3077 C  C   . ALA   A 428 ? 1.2598 1.0447 1.2737 0.1374  0.1427  0.1402  448 ALA   A C   
3078 O  O   . ALA   A 428 ? 1.2270 0.9810 1.2171 0.1213  0.1242  0.1397  448 ALA   A O   
3079 C  CB  . ALA   A 428 ? 1.2394 1.0819 1.2497 0.1130  0.1379  0.1274  448 ALA   A CB  
3080 N  N   . LEU   A 429 ? 1.2344 1.0597 1.3067 0.1572  0.1544  0.1549  449 LEU   A N   
3081 C  CA  . LEU   A 429 ? 1.2077 1.0397 1.3122 0.1638  0.1439  0.1702  449 LEU   A CA  
3082 C  C   . LEU   A 429 ? 1.3047 1.0640 1.3712 0.1829  0.1532  0.1690  449 LEU   A C   
3083 O  O   . LEU   A 429 ? 1.2188 0.9539 1.2760 0.1754  0.1363  0.1761  449 LEU   A O   
3084 C  CB  . LEU   A 429 ? 1.1323 1.0239 1.3114 0.1821  0.1517  0.1857  449 LEU   A CB  
3085 C  CG  . LEU   A 429 ? 1.0399 0.9996 1.2617 0.1629  0.1358  0.1882  449 LEU   A CG  
3086 C  CD1 . LEU   A 429 ? 0.9729 0.9850 1.2719 0.1793  0.1380  0.2040  449 LEU   A CD1 
3087 C  CD2 . LEU   A 429 ? 0.9996 0.9685 1.2041 0.1362  0.1053  0.1878  449 LEU   A CD2 
3088 N  N   . MET   A 430 ? 1.3389 1.0581 1.3788 0.2090  0.1813  0.1607  450 MET   A N   
3089 C  CA  . MET   A 430 ? 1.3843 1.0249 1.3803 0.2313  0.1918  0.1566  450 MET   A CA  
3090 C  C   . MET   A 430 ? 1.4550 1.0276 1.3786 0.2050  0.1711  0.1399  450 MET   A C   
3091 O  O   . MET   A 430 ? 1.4708 0.9913 1.3728 0.2037  0.1598  0.1426  450 MET   A O   
3092 C  CB  . MET   A 430 ? 1.4576 1.0723 1.4382 0.2695  0.2308  0.1514  450 MET   A CB  
3093 C  CG  . MET   A 430 ? 1.5561 1.0790 1.4791 0.2972  0.2447  0.1428  450 MET   A CG  
3094 S  SD  . MET   A 430 ? 1.7298 1.2464 1.6968 0.3165  0.2375  0.1641  450 MET   A SD  
3095 C  CE  . MET   A 430 ? 1.6787 1.2931 1.7510 0.3455  0.2610  0.1886  450 MET   A CE  
3096 N  N   . ASN   A 431 ? 1.4458 1.0177 1.3341 0.1833  0.1641  0.1239  451 ASN   A N   
3097 C  CA  . ASN   A 431 ? 1.4935 1.0056 1.3199 0.1558  0.1410  0.1079  451 ASN   A CA  
3098 C  C   . ASN   A 431 ? 1.5537 1.0852 1.4035 0.1223  0.1119  0.1199  451 ASN   A C   
3099 O  O   . ASN   A 431 ? 1.5518 1.0227 1.3653 0.1060  0.0957  0.1160  451 ASN   A O   
3100 C  CB  . ASN   A 431 ? 1.5322 1.0527 1.3258 0.1402  0.1363  0.0912  451 ASN   A CB  
3101 C  CG  . ASN   A 431 ? 1.6112 1.0716 1.3446 0.1116  0.1090  0.0738  451 ASN   A CG  
3102 O  OD1 . ASN   A 431 ? 1.5557 1.0489 1.2923 0.0805  0.0873  0.0700  451 ASN   A OD1 
3103 N  ND2 . ASN   A 431 ? 1.6664 1.0378 1.3470 0.1221  0.1087  0.0632  451 ASN   A ND2 
3104 N  N   . MET   A 432 ? 1.3475 0.9597 1.2553 0.1119  0.1056  0.1353  452 MET   A N   
3105 C  CA  . MET   A 432 ? 1.3834 1.0163 1.3098 0.0845  0.0828  0.1495  452 MET   A CA  
3106 C  C   . MET   A 432 ? 1.4098 1.0116 1.3454 0.1006  0.0835  0.1661  452 MET   A C   
3107 O  O   . MET   A 432 ? 1.3795 0.9401 1.2941 0.0822  0.0689  0.1726  452 MET   A O   
3108 C  CB  . MET   A 432 ? 1.2902 1.0115 1.2656 0.0732  0.0765  0.1587  452 MET   A CB  
3109 C  CG  . MET   A 432 ? 1.2596 1.0119 1.2266 0.0524  0.0705  0.1456  452 MET   A CG  
3110 S  SD  . MET   A 432 ? 0.9843 0.8260 0.9983 0.0362  0.0592  0.1562  452 MET   A SD  
3111 C  CE  . MET   A 432 ? 0.9977 0.8763 1.0610 0.0672  0.0715  0.1668  452 MET   A CE  
3112 N  N   . LYS   A 433 ? 1.4191 1.0410 1.3895 0.1348  0.0998  0.1754  453 LYS   A N   
3113 C  CA  . LYS   A 433 ? 1.4035 1.0019 1.3878 0.1542  0.0988  0.1935  453 LYS   A CA  
3114 C  C   . LYS   A 433 ? 1.5388 1.0383 1.4697 0.1655  0.1045  0.1858  453 LYS   A C   
3115 O  O   . LYS   A 433 ? 1.5303 0.9895 1.4520 0.1640  0.0940  0.1994  453 LYS   A O   
3116 C  CB  . LYS   A 433 ? 1.3213 0.9684 1.3625 0.1893  0.1138  0.2049  453 LYS   A CB  
3117 C  CG  . LYS   A 433 ? 1.2611 0.9959 1.3571 0.1782  0.0996  0.2167  453 LYS   A CG  
3118 C  CD  . LYS   A 433 ? 1.2443 1.0276 1.4035 0.2097  0.1119  0.2270  453 LYS   A CD  
3119 C  CE  . LYS   A 433 ? 1.1967 1.0589 1.4062 0.1969  0.0917  0.2364  453 LYS   A CE  
3120 N  NZ  . LYS   A 433 ? 1.1661 1.0797 1.4460 0.2226  0.1002  0.2463  453 LYS   A NZ  
3121 N  N   . LEU   A 434 ? 1.5645 1.0182 1.4543 0.1781  0.1207  0.1641  454 LEU   A N   
3122 C  CA  . LEU   A 434 ? 1.6401 0.9888 1.4663 0.1857  0.1221  0.1514  454 LEU   A CA  
3123 C  C   . LEU   A 434 ? 1.6966 1.0054 1.4894 0.1411  0.0930  0.1485  454 LEU   A C   
3124 O  O   . LEU   A 434 ? 1.8222 1.0476 1.5778 0.1402  0.0857  0.1480  454 LEU   A O   
3125 C  CB  . LEU   A 434 ? 1.7126 1.0196 1.4903 0.2064  0.1431  0.1263  454 LEU   A CB  
3126 C  CG  . LEU   A 434 ? 1.7796 1.0848 1.5709 0.2593  0.1798  0.1288  454 LEU   A CG  
3127 C  CD1 . LEU   A 434 ? 1.8289 1.1061 1.5689 0.2748  0.2016  0.1058  454 LEU   A CD1 
3128 C  CD2 . LEU   A 434 ? 1.8540 1.0827 1.6253 0.2896  0.1872  0.1340  454 LEU   A CD2 
3129 N  N   . ALA   A 435 ? 1.6337 1.0006 1.4426 0.1042  0.0767  0.1479  455 ALA   A N   
3130 C  CA  . ALA   A 435 ? 1.6719 1.0160 1.4636 0.0598  0.0507  0.1496  455 ALA   A CA  
3131 C  C   . ALA   A 435 ? 1.6929 1.0589 1.5178 0.0478  0.0413  0.1789  455 ALA   A C   
3132 O  O   . ALA   A 435 ? 1.7478 1.0544 1.5512 0.0286  0.0285  0.1869  455 ALA   A O   
3133 C  CB  . ALA   A 435 ? 1.6358 1.0376 1.4357 0.0288  0.0391  0.1396  455 ALA   A CB  
3134 N  N   . LEU   A 436 ? 1.5952 1.0422 1.4692 0.0589  0.0465  0.1956  456 LEU   A N   
3135 C  CA  . LEU   A 436 ? 1.5637 1.0330 1.4615 0.0514  0.0374  0.2239  456 LEU   A CA  
3136 C  C   . LEU   A 436 ? 1.6145 1.0138 1.4977 0.0751  0.0401  0.2377  456 LEU   A C   
3137 O  O   . LEU   A 436 ? 1.6132 0.9998 1.4967 0.0626  0.0300  0.2612  456 LEU   A O   
3138 C  CB  . LEU   A 436 ? 1.4597 1.0206 1.4055 0.0646  0.0399  0.2349  456 LEU   A CB  
3139 C  CG  . LEU   A 436 ? 1.4350 1.0686 1.3998 0.0483  0.0389  0.2227  456 LEU   A CG  
3140 C  CD1 . LEU   A 436 ? 1.3095 1.0183 1.3180 0.0638  0.0385  0.2333  456 LEU   A CD1 
3141 C  CD2 . LEU   A 436 ? 1.4371 1.0819 1.3908 0.0072  0.0260  0.2253  456 LEU   A CD2 
3142 N  N   . ILE   A 437 ? 1.6832 1.0359 1.5521 0.1112  0.0556  0.2251  457 ILE   A N   
3143 C  CA  . ILE   A 437 ? 1.8648 1.1545 1.7243 0.1417  0.0605  0.2386  457 ILE   A CA  
3144 C  C   . ILE   A 437 ? 1.9807 1.1658 1.7868 0.1219  0.0503  0.2350  457 ILE   A C   
3145 O  O   . ILE   A 437 ? 2.0092 1.1570 1.8111 0.1176  0.0413  0.2579  457 ILE   A O   
3146 C  CB  . ILE   A 437 ? 1.7951 1.0778 1.6633 0.1913  0.0848  0.2278  457 ILE   A CB  
3147 C  CG1 . ILE   A 437 ? 1.6744 1.0534 1.6099 0.2136  0.0899  0.2441  457 ILE   A CG1 
3148 C  CG2 . ILE   A 437 ? 1.9107 1.0966 1.7468 0.2228  0.0928  0.2306  457 ILE   A CG2 
3149 C  CD1 . ILE   A 437 ? 1.6624 1.0570 1.6217 0.2565  0.1166  0.2354  457 ILE   A CD1 
3150 N  N   . ARG   A 438 ? 2.0167 1.1496 1.7793 0.1087  0.0495  0.2066  458 ARG   A N   
3151 C  CA  . ARG   A 438 ? 2.1573 1.1821 1.8675 0.0889  0.0361  0.1995  458 ARG   A CA  
3152 C  C   . ARG   A 438 ? 2.1264 1.1630 1.8456 0.0337  0.0129  0.2151  458 ARG   A C   
3153 O  O   . ARG   A 438 ? 2.2118 1.1730 1.9093 0.0166  0.0014  0.2269  458 ARG   A O   
3154 C  CB  . ARG   A 438 ? 2.2081 1.1704 1.8633 0.0925  0.0383  0.1624  458 ARG   A CB  
3155 C  CG  . ARG   A 438 ? 2.2532 1.1241 1.8642 0.1416  0.0570  0.1488  458 ARG   A CG  
3156 C  CD  . ARG   A 438 ? 2.3458 1.1135 1.9267 0.1382  0.0454  0.1597  458 ARG   A CD  
3157 N  NE  . ARG   A 438 ? 2.4556 1.1149 1.9773 0.1807  0.0599  0.1390  458 ARG   A NE  
3158 C  CZ  . ARG   A 438 ? 2.4342 1.0716 1.9644 0.2334  0.0823  0.1509  458 ARG   A CZ  
3159 N  NH1 . ARG   A 438 ? 2.3596 1.0754 1.9558 0.2493  0.0890  0.1834  458 ARG   A NH1 
3160 N  NH2 . ARG   A 438 ? 2.4401 0.9736 1.9098 0.2728  0.0973  0.1293  458 ARG   A NH2 
3161 N  N   . VAL   A 439 ? 1.8835 1.0124 1.6362 0.0062  0.0075  0.2170  459 VAL   A N   
3162 C  CA  . VAL   A 439 ? 1.8733 1.0209 1.6397 -0.0448 -0.0102 0.2332  459 VAL   A CA  
3163 C  C   . VAL   A 439 ? 1.9047 1.0725 1.6954 -0.0455 -0.0087 0.2714  459 VAL   A C   
3164 O  O   . VAL   A 439 ? 1.9472 1.0940 1.7386 -0.0818 -0.0193 0.2916  459 VAL   A O   
3165 C  CB  . VAL   A 439 ? 1.8439 1.0838 1.6380 -0.0690 -0.0141 0.2238  459 VAL   A CB  
3166 C  CG1 . VAL   A 439 ? 1.7581 1.0988 1.5956 -0.0510 -0.0022 0.2393  459 VAL   A CG1 
3167 C  CG2 . VAL   A 439 ? 1.8728 1.1168 1.6765 -0.1228 -0.0326 0.2335  459 VAL   A CG2 
3168 N  N   . LEU   A 440 ? 1.9479 1.1563 1.7593 -0.0062 0.0035  0.2836  460 LEU   A N   
3169 C  CA  . LEU   A 440 ? 1.8930 1.1147 1.7186 -0.0009 0.0024  0.3196  460 LEU   A CA  
3170 C  C   . LEU   A 440 ? 1.9251 1.0539 1.7255 0.0258  0.0038  0.3319  460 LEU   A C   
3171 O  O   . LEU   A 440 ? 1.9573 1.0713 1.7572 0.0230  -0.0003 0.3643  460 LEU   A O   
3172 C  CB  . LEU   A 440 ? 1.7794 1.0968 1.6420 0.0253  0.0082  0.3277  460 LEU   A CB  
3173 C  CG  . LEU   A 440 ? 1.6994 1.1100 1.5864 -0.0007 0.0060  0.3243  460 LEU   A CG  
3174 C  CD1 . LEU   A 440 ? 1.5870 1.0784 1.5059 0.0275  0.0087  0.3276  460 LEU   A CD1 
3175 C  CD2 . LEU   A 440 ? 1.7042 1.1225 1.5880 -0.0395 -0.0001 0.3497  460 LEU   A CD2 
3176 N  N   . GLN   A 441 ? 2.0045 1.0677 1.7802 0.0540  0.0109  0.3078  461 GLN   A N   
3177 C  CA  . GLN   A 441 ? 2.0743 1.0362 1.8203 0.0798  0.0127  0.3165  461 GLN   A CA  
3178 C  C   . GLN   A 441 ? 2.1705 1.0420 1.8824 0.0392  -0.0018 0.3247  461 GLN   A C   
3179 O  O   . GLN   A 441 ? 2.2480 1.0381 1.9385 0.0530  -0.0033 0.3425  461 GLN   A O   
3180 C  CB  . GLN   A 441 ? 2.1422 1.0530 1.8645 0.1213  0.0272  0.2861  461 GLN   A CB  
3181 C  CG  . GLN   A 441 ? 2.1025 1.0567 1.8582 0.1778  0.0442  0.2940  461 GLN   A CG  
3182 C  CD  . GLN   A 441 ? 2.1609 1.0663 1.8935 0.2204  0.0648  0.2662  461 GLN   A CD  
3183 O  OE1 . GLN   A 441 ? 2.2156 1.0780 1.9074 0.2073  0.0667  0.2357  461 GLN   A OE1 
3184 N  NE2 . GLN   A 441 ? 2.1236 1.0362 1.8815 0.2734  0.0805  0.2777  461 GLN   A NE2 
3185 N  N   . ASN   A 442 ? 2.1027 0.9873 1.8132 -0.0107 -0.0135 0.3138  462 ASN   A N   
3186 C  CA  . ASN   A 442 ? 2.2453 1.0475 1.9318 -0.0553 -0.0298 0.3197  462 ASN   A CA  
3187 C  C   . ASN   A 442 ? 2.1813 1.0437 1.9009 -0.1060 -0.0372 0.3488  462 ASN   A C   
3188 O  O   . ASN   A 442 ? 2.2367 1.0393 1.9486 -0.1356 -0.0453 0.3732  462 ASN   A O   
3189 C  CB  . ASN   A 442 ? 2.2632 1.0069 1.9148 -0.0731 -0.0416 0.2787  462 ASN   A CB  
3190 C  CG  . ASN   A 442 ? 2.3626 1.0170 1.9658 -0.0249 -0.0327 0.2511  462 ASN   A CG  
3191 O  OD1 . ASN   A 442 ? 2.4380 0.9776 2.0014 -0.0198 -0.0386 0.2512  462 ASN   A OD1 
3192 N  ND2 . ASN   A 442 ? 2.3095 1.0137 1.9150 0.0117  -0.0167 0.2282  462 ASN   A ND2 
3193 N  N   . PHE   A 443 ? 2.0841 1.0605 1.8402 -0.1156 -0.0327 0.3486  463 PHE   A N   
3194 C  CA  . PHE   A 443 ? 2.0412 1.0786 1.8284 -0.1628 -0.0366 0.3719  463 PHE   A CA  
3195 C  C   . PHE   A 443 ? 1.9146 1.0475 1.7285 -0.1465 -0.0235 0.3992  463 PHE   A C   
3196 O  O   . PHE   A 443 ? 1.8791 1.0533 1.6973 -0.1045 -0.0159 0.3917  463 PHE   A O   
3197 C  CB  . PHE   A 443 ? 2.0818 1.1661 1.8854 -0.1950 -0.0460 0.3447  463 PHE   A CB  
3198 C  CG  . PHE   A 443 ? 2.1708 1.1643 1.9416 -0.2105 -0.0637 0.3131  463 PHE   A CG  
3199 C  CD1 . PHE   A 443 ? 2.2435 1.1786 2.0139 -0.2602 -0.0824 0.3213  463 PHE   A CD1 
3200 C  CD2 . PHE   A 443 ? 2.1931 1.1576 1.9318 -0.1756 -0.0621 0.2755  463 PHE   A CD2 
3201 C  CE1 . PHE   A 443 ? 2.3600 1.2051 2.0943 -0.2752 -0.1040 0.2892  463 PHE   A CE1 
3202 C  CE2 . PHE   A 443 ? 2.2774 1.1517 1.9739 -0.1869 -0.0794 0.2444  463 PHE   A CE2 
3203 C  CZ  . PHE   A 443 ? 2.3937 1.2059 2.0859 -0.2369 -0.1028 0.2495  463 PHE   A CZ  
3204 N  N   . SER   A 444 ? 1.9847 1.1507 1.8161 -0.1811 -0.0214 0.4316  464 SER   A N   
3205 C  CA  . SER   A 444 ? 1.8785 1.1393 1.7293 -0.1739 -0.0099 0.4548  464 SER   A CA  
3206 C  C   . SER   A 444 ? 1.8654 1.2032 1.7486 -0.2133 -0.0078 0.4534  464 SER   A C   
3207 O  O   . SER   A 444 ? 1.9397 1.2514 1.8351 -0.2557 -0.0155 0.4532  464 SER   A O   
3208 C  CB  . SER   A 444 ? 1.8087 1.0428 1.6449 -0.1719 -0.0036 0.5008  464 SER   A CB  
3209 O  OG  . SER   A 444 ? 1.8416 1.0571 1.6586 -0.1225 -0.0036 0.5056  464 SER   A OG  
3210 N  N   . PHE   A 445 ? 1.7379 1.1702 1.6369 -0.1986 0.0011  0.4522  465 PHE   A N   
3211 C  CA  . PHE   A 445 ? 1.7219 1.2351 1.6528 -0.2264 0.0051  0.4474  465 PHE   A CA  
3212 C  C   . PHE   A 445 ? 1.6711 1.2480 1.6075 -0.2285 0.0214  0.4823  465 PHE   A C   
3213 O  O   . PHE   A 445 ? 1.6242 1.2138 1.5390 -0.1952 0.0263  0.4942  465 PHE   A O   
3214 C  CB  . PHE   A 445 ? 1.6491 1.2135 1.5897 -0.2057 0.0016  0.4086  465 PHE   A CB  
3215 C  CG  . PHE   A 445 ? 1.7003 1.2044 1.6292 -0.2036 -0.0113 0.3745  465 PHE   A CG  
3216 C  CD1 . PHE   A 445 ? 1.7207 1.1640 1.6227 -0.1679 -0.0126 0.3626  465 PHE   A CD1 
3217 C  CD2 . PHE   A 445 ? 1.6793 1.1864 1.6218 -0.2354 -0.0223 0.3552  465 PHE   A CD2 
3218 C  CE1 . PHE   A 445 ? 1.7741 1.1575 1.6567 -0.1622 -0.0207 0.3314  465 PHE   A CE1 
3219 C  CE2 . PHE   A 445 ? 1.7158 1.1610 1.6357 -0.2314 -0.0352 0.3229  465 PHE   A CE2 
3220 C  CZ  . PHE   A 445 ? 1.7494 1.1308 1.6360 -0.1939 -0.0325 0.3107  465 PHE   A CZ  
3221 N  N   . LYS   A 446 ? 1.6063 1.2237 1.5712 -0.2668 0.0293  0.4989  466 LYS   A N   
3222 C  CA  . LYS   A 446 ? 1.6547 1.3150 1.6206 -0.2750 0.0496  0.5396  466 LYS   A CA  
3223 C  C   . LYS   A 446 ? 1.6087 1.3563 1.6162 -0.2996 0.0604  0.5393  466 LYS   A C   
3224 O  O   . LYS   A 446 ? 1.6130 1.3654 1.6548 -0.3278 0.0489  0.5204  466 LYS   A O   
3225 C  CB  . LYS   A 446 ? 1.7458 1.3354 1.7043 -0.3017 0.0533  0.5786  466 LYS   A CB  
3226 C  CG  . LYS   A 446 ? 1.7624 1.3955 1.7320 -0.3223 0.0782  0.6184  466 LYS   A CG  
3227 C  CD  . LYS   A 446 ? 1.8812 1.4366 1.8326 -0.3350 0.0826  0.6416  466 LYS   A CD  
3228 C  CE  . LYS   A 446 ? 1.9584 1.5557 1.9282 -0.3588 0.1091  0.6692  466 LYS   A CE  
3229 N  NZ  . LYS   A 446 ? 1.9506 1.5901 1.9836 -0.4013 0.1074  0.6583  466 LYS   A NZ  
3230 N  N   . PRO   A 447 ? 1.5989 1.4151 1.6017 -0.2870 0.0814  0.5588  467 PRO   A N   
3231 C  CA  . PRO   A 447 ? 1.6015 1.5035 1.6456 -0.3061 0.0957  0.5612  467 PRO   A CA  
3232 C  C   . PRO   A 447 ? 1.6980 1.5973 1.7876 -0.3556 0.1014  0.5867  467 PRO   A C   
3233 O  O   . PRO   A 447 ? 1.7905 1.6193 1.8732 -0.3729 0.0962  0.5987  467 PRO   A O   
3234 C  CB  . PRO   A 447 ? 1.5899 1.5437 1.6037 -0.2782 0.1198  0.5828  467 PRO   A CB  
3235 C  CG  . PRO   A 447 ? 1.5508 1.4612 1.5119 -0.2378 0.1074  0.5722  467 PRO   A CG  
3236 C  CD  . PRO   A 447 ? 1.6083 1.4281 1.5638 -0.2485 0.0902  0.5739  467 PRO   A CD  
3237 N  N   . CYS   A 448 ? 1.7684 1.7469 1.9048 -0.3706 0.1112  0.5821  468 CYS   A N   
3238 C  CA  . CYS   A 448 ? 1.7802 1.7712 1.9692 -0.4106 0.1136  0.5912  468 CYS   A CA  
3239 C  C   . CYS   A 448 ? 1.7582 1.8496 1.9835 -0.4076 0.1393  0.5993  468 CYS   A C   
3240 O  O   . CYS   A 448 ? 1.7313 1.8765 1.9385 -0.3758 0.1522  0.5925  468 CYS   A O   
3241 C  CB  . CYS   A 448 ? 1.7925 1.7538 2.0163 -0.4419 0.0801  0.5653  468 CYS   A CB  
3242 S  SG  . CYS   A 448 ? 2.0224 2.0261 2.3251 -0.4896 0.0762  0.5705  468 CYS   A SG  
3243 N  N   . LYS   A 449 ? 1.7602 1.8740 2.0373 -0.4401 0.1467  0.6138  469 LYS   A N   
3244 C  CA  . LYS   A 449 ? 1.7295 1.9385 2.0501 -0.4380 0.1707  0.6215  469 LYS   A CA  
3245 C  C   . LYS   A 449 ? 1.6863 1.9541 2.0453 -0.4361 0.1538  0.5923  469 LYS   A C   
3246 O  O   . LYS   A 449 ? 1.6341 1.9799 2.0094 -0.4160 0.1736  0.5913  469 LYS   A O   
3247 C  CB  . LYS   A 449 ? 1.6782 1.8966 2.0518 -0.4749 0.1811  0.6459  469 LYS   A CB  
3248 C  CG  . LYS   A 449 ? 1.7274 1.9028 2.1451 -0.5184 0.1456  0.6338  469 LYS   A CG  
3249 C  CD  . LYS   A 449 ? 1.7172 1.9121 2.1950 -0.5556 0.1559  0.6588  469 LYS   A CD  
3250 C  CE  . LYS   A 449 ? 1.8549 2.0022 2.3725 -0.5992 0.1159  0.6440  469 LYS   A CE  
3251 N  NZ  . LYS   A 449 ? 1.9204 2.0928 2.5049 -0.6379 0.1232  0.6679  469 LYS   A NZ  
3252 N  N   . GLU   A 450 ? 1.6817 1.9091 2.0507 -0.4547 0.1176  0.5679  470 GLU   A N   
3253 C  CA  . GLU   A 450 ? 1.6383 1.9110 2.0355 -0.4527 0.0979  0.5394  470 GLU   A CA  
3254 C  C   . GLU   A 450 ? 1.5787 1.8433 1.9255 -0.4178 0.0944  0.5195  470 GLU   A C   
3255 O  O   . GLU   A 450 ? 1.5670 1.8356 1.9217 -0.4183 0.0708  0.4917  470 GLU   A O   
3256 C  CB  . GLU   A 450 ? 1.7119 1.9429 2.1415 -0.4917 0.0584  0.5220  470 GLU   A CB  
3257 C  CG  . GLU   A 450 ? 1.8187 2.0563 2.3041 -0.5301 0.0560  0.5396  470 GLU   A CG  
3258 C  CD  . GLU   A 450 ? 1.8933 2.0898 2.4058 -0.5668 0.0115  0.5177  470 GLU   A CD  
3259 O  OE1 . GLU   A 450 ? 1.8613 2.0460 2.3579 -0.5607 -0.0151 0.4880  470 GLU   A OE1 
3260 O  OE2 . GLU   A 450 ? 1.9110 2.0841 2.4573 -0.6016 0.0023  0.5296  470 GLU   A OE2 
3261 N  N   . THR   A 451 ? 1.5622 1.8137 1.8555 -0.3864 0.1157  0.5316  471 THR   A N   
3262 C  CA  . THR   A 451 ? 1.5504 1.7877 1.7912 -0.3460 0.1104  0.5056  471 THR   A CA  
3263 C  C   . THR   A 451 ? 1.4660 1.7773 1.6965 -0.3130 0.1368  0.5082  471 THR   A C   
3264 O  O   . THR   A 451 ? 1.4173 1.7565 1.6423 -0.3084 0.1654  0.5376  471 THR   A O   
3265 C  CB  . THR   A 451 ? 1.5563 1.7123 1.7382 -0.3302 0.1067  0.5107  471 THR   A CB  
3266 O  OG1 . THR   A 451 ? 1.6123 1.6927 1.8003 -0.3593 0.0842  0.5087  471 THR   A OG1 
3267 C  CG2 . THR   A 451 ? 1.4712 1.6130 1.6071 -0.2865 0.0965  0.4764  471 THR   A CG2 
3268 N  N   . GLN   A 452 ? 1.4602 1.7946 1.6817 -0.2860 0.1265  0.4721  472 GLN   A N   
3269 C  CA  . GLN   A 452 ? 1.3504 1.7431 1.5545 -0.2513 0.1471  0.4678  472 GLN   A CA  
3270 C  C   . GLN   A 452 ? 1.3811 1.7336 1.5157 -0.2166 0.1488  0.4633  472 GLN   A C   
3271 O  O   . GLN   A 452 ? 1.3637 1.6741 1.4727 -0.2003 0.1265  0.4349  472 GLN   A O   
3272 C  CB  . GLN   A 452 ? 1.2850 1.7146 1.5103 -0.2386 0.1337  0.4326  472 GLN   A CB  
3273 C  CG  . GLN   A 452 ? 1.2668 1.7430 1.4673 -0.1998 0.1513  0.4226  472 GLN   A CG  
3274 C  CD  . GLN   A 452 ? 1.2902 1.7999 1.5133 -0.1877 0.1390  0.3909  472 GLN   A CD  
3275 O  OE1 . GLN   A 452 ? 1.2292 1.7023 1.4348 -0.1777 0.1161  0.3608  472 GLN   A OE1 
3276 N  NE2 . GLN   A 452 ? 1.2950 1.8755 1.5585 -0.1869 0.1560  0.3998  472 GLN   A NE2 
3277 N  N   . ILE   A 453 ? 1.3083 1.6749 1.4129 -0.2050 0.1749  0.4929  473 ILE   A N   
3278 C  CA  . ILE   A 453 ? 1.3468 1.6805 1.3827 -0.1714 0.1745  0.4917  473 ILE   A CA  
3279 C  C   . ILE   A 453 ? 1.3611 1.7473 1.3679 -0.1440 0.2018  0.4997  473 ILE   A C   
3280 O  O   . ILE   A 453 ? 1.4041 1.8235 1.4203 -0.1534 0.2324  0.5333  473 ILE   A O   
3281 C  CB  . ILE   A 453 ? 1.3989 1.6734 1.4060 -0.1816 0.1756  0.5231  473 ILE   A CB  
3282 C  CG1 . ILE   A 453 ? 1.4146 1.6317 1.4494 -0.2089 0.1511  0.5157  473 ILE   A CG1 
3283 C  CG2 . ILE   A 453 ? 1.5057 1.7479 1.4426 -0.1445 0.1684  0.5195  473 ILE   A CG2 
3284 C  CD1 . ILE   A 453 ? 1.4087 1.5580 1.4136 -0.2157 0.1495  0.5442  473 ILE   A CD1 
3285 N  N   . PRO   A 454 ? 1.3343 1.7270 1.3046 -0.1093 0.1927  0.4696  474 PRO   A N   
3286 C  CA  . PRO   A 454 ? 1.3559 1.7164 1.3183 -0.0957 0.1598  0.4311  474 PRO   A CA  
3287 C  C   . PRO   A 454 ? 1.2976 1.6816 1.3152 -0.1090 0.1483  0.4048  474 PRO   A C   
3288 O  O   . PRO   A 454 ? 1.2923 1.7307 1.3415 -0.1123 0.1638  0.4055  474 PRO   A O   
3289 C  CB  . PRO   A 454 ? 1.3551 1.7236 1.2611 -0.0568 0.1598  0.4156  474 PRO   A CB  
3290 C  CG  . PRO   A 454 ? 1.3789 1.8032 1.2831 -0.0497 0.1937  0.4310  474 PRO   A CG  
3291 C  CD  . PRO   A 454 ? 1.3886 1.8209 1.3194 -0.0793 0.2172  0.4734  474 PRO   A CD  
3292 N  N   . LEU   A 455 ? 1.3173 1.6612 1.3460 -0.1146 0.1222  0.3827  475 LEU   A N   
3293 C  CA  . LEU   A 455 ? 1.2789 1.6381 1.3494 -0.1248 0.1099  0.3577  475 LEU   A CA  
3294 C  C   . LEU   A 455 ? 1.2566 1.6534 1.3214 -0.0982 0.1111  0.3330  475 LEU   A C   
3295 O  O   . LEU   A 455 ? 1.2647 1.6473 1.2920 -0.0718 0.1045  0.3191  475 LEU   A O   
3296 C  CB  . LEU   A 455 ? 1.2523 1.5546 1.3231 -0.1298 0.0855  0.3396  475 LEU   A CB  
3297 C  CG  . LEU   A 455 ? 1.2044 1.5087 1.3083 -0.1414 0.0714  0.3157  475 LEU   A CG  
3298 C  CD1 . LEU   A 455 ? 1.2098 1.5258 1.3528 -0.1767 0.0726  0.3311  475 LEU   A CD1 
3299 C  CD2 . LEU   A 455 ? 1.1500 1.3971 1.2401 -0.1345 0.0529  0.2961  475 LEU   A CD2 
3300 N  N   . LYS   A 456 ? 1.1991 1.6424 1.3030 -0.1056 0.1172  0.3279  476 LYS   A N   
3301 C  CA  . LYS   A 456 ? 1.2261 1.7026 1.3284 -0.0810 0.1187  0.3052  476 LYS   A CA  
3302 C  C   . LYS   A 456 ? 1.1686 1.6382 1.2993 -0.0872 0.0986  0.2802  476 LYS   A C   
3303 O  O   . LYS   A 456 ? 1.1836 1.6549 1.3500 -0.1131 0.0912  0.2849  476 LYS   A O   
3304 C  CB  . LYS   A 456 ? 1.2340 1.7745 1.3561 -0.0767 0.1452  0.3210  476 LYS   A CB  
3305 C  CG  . LYS   A 456 ? 1.2466 1.8148 1.3575 -0.0454 0.1494  0.2985  476 LYS   A CG  
3306 C  CD  . LYS   A 456 ? 1.2605 1.7952 1.3083 -0.0160 0.1453  0.2844  476 LYS   A CD  
3307 C  CE  . LYS   A 456 ? 1.2662 1.7835 1.3080 0.0012  0.1249  0.2499  476 LYS   A CE  
3308 N  NZ  . LYS   A 456 ? 1.1890 1.6534 1.2176 -0.0036 0.0999  0.2377  476 LYS   A NZ  
3309 N  N   . LEU   A 457 ? 1.2380 1.6968 1.3504 -0.0639 0.0888  0.2543  477 LEU   A N   
3310 C  CA  . LEU   A 457 ? 1.2003 1.6519 1.3328 -0.0653 0.0731  0.2322  477 LEU   A CA  
3311 C  C   . LEU   A 457 ? 1.2250 1.7286 1.3868 -0.0611 0.0800  0.2289  477 LEU   A C   
3312 O  O   . LEU   A 457 ? 1.2401 1.7829 1.3993 -0.0461 0.0979  0.2361  477 LEU   A O   
3313 C  CB  . LEU   A 457 ? 1.1392 1.5588 1.2466 -0.0439 0.0614  0.2095  477 LEU   A CB  
3314 C  CG  . LEU   A 457 ? 1.0972 1.4671 1.1866 -0.0462 0.0509  0.2106  477 LEU   A CG  
3315 C  CD1 . LEU   A 457 ? 1.0415 1.3913 1.1194 -0.0262 0.0396  0.1903  477 LEU   A CD1 
3316 C  CD2 . LEU   A 457 ? 1.0731 1.4142 1.1790 -0.0684 0.0434  0.2134  477 LEU   A CD2 
3317 N  N   . SER   A 458 ? 1.1797 1.6823 1.3667 -0.0719 0.0659  0.2183  478 SER   A N   
3318 C  CA  . SER   A 458 ? 1.1661 1.7173 1.3846 -0.0672 0.0678  0.2156  478 SER   A CA  
3319 C  C   . SER   A 458 ? 1.1890 1.7464 1.3875 -0.0343 0.0726  0.1978  478 SER   A C   
3320 O  O   . SER   A 458 ? 1.1647 1.6867 1.3458 -0.0245 0.0603  0.1785  478 SER   A O   
3321 C  CB  . SER   A 458 ? 1.1178 1.6568 1.3573 -0.0847 0.0465  0.2070  478 SER   A CB  
3322 O  OG  . SER   A 458 ? 1.1294 1.6182 1.3400 -0.0748 0.0342  0.1863  478 SER   A OG  
3323 N  N   . LEU   A 459 ? 1.2545 1.8542 1.4547 -0.0167 0.0918  0.2050  479 LEU   A N   
3324 C  CA  . LEU   A 459 ? 1.1650 1.7668 1.3438 0.0155  0.0961  0.1872  479 LEU   A CA  
3325 C  C   . LEU   A 459 ? 1.1119 1.7200 1.3134 0.0208  0.0834  0.1735  479 LEU   A C   
3326 O  O   . LEU   A 459 ? 1.0512 1.7039 1.2773 0.0336  0.0917  0.1765  479 LEU   A O   
3327 C  CB  . LEU   A 459 ? 1.1418 1.7881 1.3165 0.0356  0.1222  0.1984  479 LEU   A CB  
3328 C  CG  . LEU   A 459 ? 1.1976 1.8192 1.3166 0.0546  0.1324  0.1957  479 LEU   A CG  
3329 C  CD1 . LEU   A 459 ? 1.2337 1.8201 1.3346 0.0339  0.1250  0.2064  479 LEU   A CD1 
3330 C  CD2 . LEU   A 459 ? 1.2034 1.8707 1.3160 0.0742  0.1633  0.2107  479 LEU   A CD2 
3331 N  N   . GLY   A 460 ? 1.1252 1.6894 1.3179 0.0131  0.0647  0.1601  480 GLY   A N   
3332 C  CA  . GLY   A 460 ? 1.0778 1.6400 1.2838 0.0176  0.0522  0.1492  480 GLY   A CA  
3333 C  C   . GLY   A 460 ? 1.1419 1.6487 1.3264 0.0154  0.0386  0.1349  480 GLY   A C   
3334 O  O   . GLY   A 460 ? 1.1525 1.6292 1.3134 0.0274  0.0397  0.1248  480 GLY   A O   
3335 N  N   . GLY   A 461 ? 1.1146 1.6075 1.3071 0.0002  0.0254  0.1345  481 GLY   A N   
3336 C  CA  . GLY   A 461 ? 1.1623 1.6059 1.3343 0.0017  0.0171  0.1228  481 GLY   A CA  
3337 C  C   . GLY   A 461 ? 1.2505 1.6540 1.4062 -0.0085 0.0176  0.1230  481 GLY   A C   
3338 O  O   . GLY   A 461 ? 1.2145 1.6127 1.3622 -0.0022 0.0240  0.1233  481 GLY   A O   
3339 N  N   . LEU   A 462 ? 1.3115 1.6846 1.4596 -0.0223 0.0095  0.1224  482 LEU   A N   
3340 C  CA  . LEU   A 462 ? 1.3323 1.6613 1.4644 -0.0269 0.0108  0.1213  482 LEU   A CA  
3341 C  C   . LEU   A 462 ? 1.2869 1.6176 1.4220 -0.0408 0.0131  0.1333  482 LEU   A C   
3342 O  O   . LEU   A 462 ? 1.2551 1.6206 1.4048 -0.0501 0.0150  0.1440  482 LEU   A O   
3343 C  CB  . LEU   A 462 ? 1.3161 1.6074 1.4311 -0.0333 0.0033  0.1157  482 LEU   A CB  
3344 C  CG  . LEU   A 462 ? 1.3079 1.6143 1.4242 -0.0386 -0.0093 0.1134  482 LEU   A CG  
3345 C  CD1 . LEU   A 462 ? 1.2813 1.6033 1.4117 -0.0632 -0.0212 0.1217  482 LEU   A CD1 
3346 C  CD2 . LEU   A 462 ? 1.4424 1.7057 1.5279 -0.0315 -0.0133 0.1039  482 LEU   A CD2 
3347 N  N   . LEU   A 463 ? 1.2002 1.4929 1.3229 -0.0408 0.0147  0.1336  483 LEU   A N   
3348 C  CA  . LEU   A 463 ? 1.1518 1.4368 1.2722 -0.0500 0.0168  0.1462  483 LEU   A CA  
3349 C  C   . LEU   A 463 ? 1.1397 1.4173 1.2629 -0.0740 0.0110  0.1551  483 LEU   A C   
3350 O  O   . LEU   A 463 ? 1.1730 1.4081 1.2831 -0.0818 0.0047  0.1508  483 LEU   A O   
3351 C  CB  . LEU   A 463 ? 1.0801 1.3258 1.1905 -0.0407 0.0182  0.1442  483 LEU   A CB  
3352 C  CG  . LEU   A 463 ? 1.0253 1.2545 1.1298 -0.0465 0.0187  0.1581  483 LEU   A CG  
3353 C  CD1 . LEU   A 463 ? 0.9606 1.2182 1.0643 -0.0378 0.0208  0.1653  483 LEU   A CD1 
3354 C  CD2 . LEU   A 463 ? 0.8908 1.0763 0.9894 -0.0379 0.0191  0.1558  483 LEU   A CD2 
3355 N  N   . GLN   A 464 ? 1.1614 1.4791 1.3022 -0.0857 0.0137  0.1682  484 GLN   A N   
3356 C  CA  . GLN   A 464 ? 1.0921 1.4101 1.2462 -0.1130 0.0075  0.1805  484 GLN   A CA  
3357 C  C   . GLN   A 464 ? 1.0964 1.4514 1.2651 -0.1195 0.0203  0.2020  484 GLN   A C   
3358 O  O   . GLN   A 464 ? 1.1215 1.5185 1.2953 -0.1033 0.0317  0.2036  484 GLN   A O   
3359 C  CB  . GLN   A 464 ? 1.1344 1.4754 1.3075 -0.1241 -0.0052 0.1749  484 GLN   A CB  
3360 C  CG  . GLN   A 464 ? 1.1961 1.4943 1.3455 -0.1196 -0.0187 0.1558  484 GLN   A CG  
3361 C  CD  . GLN   A 464 ? 1.2955 1.5502 1.4345 -0.1440 -0.0359 0.1545  484 GLN   A CD  
3362 O  OE1 . GLN   A 464 ? 1.3069 1.5767 1.4699 -0.1698 -0.0431 0.1678  484 GLN   A OE1 
3363 N  NE2 . GLN   A 464 ? 1.2959 1.4940 1.3980 -0.1359 -0.0420 0.1386  484 GLN   A NE2 
3364 N  N   . PRO   A 465 ? 1.1992 1.5358 1.3709 -0.1413 0.0203  0.2191  485 PRO   A N   
3365 C  CA  . PRO   A 465 ? 1.2306 1.6034 1.4155 -0.1486 0.0361  0.2440  485 PRO   A CA  
3366 C  C   . PRO   A 465 ? 1.2018 1.6356 1.4300 -0.1629 0.0393  0.2543  485 PRO   A C   
3367 O  O   . PRO   A 465 ? 1.1694 1.6090 1.4196 -0.1763 0.0229  0.2455  485 PRO   A O   
3368 C  CB  . PRO   A 465 ? 1.1840 1.5095 1.3604 -0.1699 0.0331  0.2599  485 PRO   A CB  
3369 C  CG  . PRO   A 465 ? 1.2007 1.4623 1.3519 -0.1649 0.0180  0.2400  485 PRO   A CG  
3370 C  CD  . PRO   A 465 ? 1.1865 1.4610 1.3434 -0.1571 0.0081  0.2172  485 PRO   A CD  
3371 N  N   . GLU   A 466 ? 1.1649 1.6459 1.4045 -0.1580 0.0609  0.2743  486 GLU   A N   
3372 C  CA  . GLU   A 466 ? 1.1724 1.7192 1.4626 -0.1715 0.0688  0.2904  486 GLU   A CA  
3373 C  C   . GLU   A 466 ? 1.2137 1.7526 1.5395 -0.2127 0.0575  0.3083  486 GLU   A C   
3374 O  O   . GLU   A 466 ? 1.2144 1.7795 1.5823 -0.2315 0.0412  0.3064  486 GLU   A O   
3375 C  CB  . GLU   A 466 ? 1.2900 1.8850 1.5789 -0.1543 0.0999  0.3101  486 GLU   A CB  
3376 C  CG  . GLU   A 466 ? 1.3228 1.9376 1.5871 -0.1153 0.1090  0.2913  486 GLU   A CG  
3377 C  CD  . GLU   A 466 ? 1.3104 1.9762 1.5734 -0.0970 0.1410  0.3100  486 GLU   A CD  
3378 O  OE1 . GLU   A 466 ? 1.3742 2.0657 1.6599 -0.1153 0.1587  0.3405  486 GLU   A OE1 
3379 O  OE2 . GLU   A 466 ? 1.2865 1.9636 1.5236 -0.0638 0.1494  0.2946  486 GLU   A OE2 
3380 N  N   . LYS   A 467 ? 1.2229 1.7233 1.5325 -0.2275 0.0634  0.3261  487 LYS   A N   
3381 C  CA  . LYS   A 467 ? 1.2128 1.6866 1.5479 -0.2677 0.0503  0.3417  487 LYS   A CA  
3382 C  C   . LYS   A 467 ? 1.2462 1.6305 1.5366 -0.2704 0.0312  0.3254  487 LYS   A C   
3383 O  O   . LYS   A 467 ? 1.2934 1.6432 1.5382 -0.2443 0.0382  0.3175  487 LYS   A O   
3384 C  CB  . LYS   A 467 ? 1.2159 1.7129 1.5704 -0.2843 0.0754  0.3809  487 LYS   A CB  
3385 C  CG  . LYS   A 467 ? 1.1870 1.7749 1.5857 -0.2784 0.1017  0.4014  487 LYS   A CG  
3386 C  CD  . LYS   A 467 ? 1.2411 1.8462 1.6449 -0.2877 0.1335  0.4418  487 LYS   A CD  
3387 C  CE  . LYS   A 467 ? 1.2126 1.8925 1.6418 -0.2664 0.1624  0.4517  487 LYS   A CE  
3388 N  NZ  . LYS   A 467 ? 1.1932 1.8706 1.6032 -0.2613 0.1936  0.4795  487 LYS   A NZ  
3389 N  N   . PRO   A 468 ? 1.2359 1.5803 1.5381 -0.3002 0.0061  0.3195  488 PRO   A N   
3390 C  CA  . PRO   A 468 ? 1.2697 1.5247 1.5255 -0.2987 -0.0097 0.3026  488 PRO   A CA  
3391 C  C   . PRO   A 468 ? 1.3011 1.5138 1.5317 -0.2979 0.0048  0.3236  488 PRO   A C   
3392 O  O   . PRO   A 468 ? 1.2805 1.5218 1.5322 -0.3115 0.0223  0.3549  488 PRO   A O   
3393 C  CB  . PRO   A 468 ? 1.2921 1.5166 1.5677 -0.3353 -0.0394 0.2963  488 PRO   A CB  
3394 C  CG  . PRO   A 468 ? 1.2839 1.5886 1.6142 -0.3468 -0.0450 0.2996  488 PRO   A CG  
3395 C  CD  . PRO   A 468 ? 1.2386 1.6171 1.5962 -0.3345 -0.0117 0.3257  488 PRO   A CD  
3396 N  N   . VAL   A 469 ? 1.3104 1.4549 1.4950 -0.2794 -0.0011 0.3078  489 VAL   A N   
3397 C  CA  . VAL   A 469 ? 1.3418 1.4371 1.4991 -0.2752 0.0081  0.3260  489 VAL   A CA  
3398 C  C   . VAL   A 469 ? 1.4004 1.4378 1.5650 -0.3121 -0.0056 0.3381  489 VAL   A C   
3399 O  O   . VAL   A 469 ? 1.4554 1.4284 1.5996 -0.3170 -0.0258 0.3168  489 VAL   A O   
3400 C  CB  . VAL   A 469 ? 1.2856 1.3350 1.3997 -0.2398 0.0066  0.3062  489 VAL   A CB  
3401 C  CG1 . VAL   A 469 ? 1.2883 1.2803 1.3764 -0.2359 0.0112  0.3253  489 VAL   A CG1 
3402 C  CG2 . VAL   A 469 ? 1.2228 1.3268 1.3328 -0.2074 0.0183  0.2975  489 VAL   A CG2 
3403 N  N   . VAL   A 470 ? 1.4014 1.4586 1.5932 -0.3379 0.0060  0.3726  490 VAL   A N   
3404 C  CA  . VAL   A 470 ? 1.5139 1.5177 1.7196 -0.3780 -0.0064 0.3892  490 VAL   A CA  
3405 C  C   . VAL   A 470 ? 1.5732 1.5354 1.7523 -0.3723 0.0106  0.4190  490 VAL   A C   
3406 O  O   . VAL   A 470 ? 1.5967 1.6054 1.7905 -0.3750 0.0346  0.4520  490 VAL   A O   
3407 C  CB  . VAL   A 470 ? 1.4967 1.5607 1.7680 -0.4190 -0.0081 0.4093  490 VAL   A CB  
3408 C  CG1 . VAL   A 470 ? 1.5781 1.5870 1.8648 -0.4584 -0.0421 0.3975  490 VAL   A CG1 
3409 C  CG2 . VAL   A 470 ? 1.4213 1.5785 1.7229 -0.4042 -0.0018 0.3982  490 VAL   A CG2 
3410 N  N   . LEU   A 471 ? 1.5398 1.4133 1.6766 -0.3615 -0.0004 0.4087  491 LEU   A N   
3411 C  CA  . LEU   A 471 ? 1.5867 1.4126 1.6926 -0.3501 0.0121  0.4349  491 LEU   A CA  
3412 C  C   . LEU   A 471 ? 1.6876 1.4283 1.7922 -0.3841 -0.0009 0.4491  491 LEU   A C   
3413 O  O   . LEU   A 471 ? 1.7422 1.4328 1.8470 -0.4026 -0.0251 0.4252  491 LEU   A O   
3414 C  CB  . LEU   A 471 ? 1.5086 1.3013 1.5683 -0.3032 0.0115  0.4146  491 LEU   A CB  
3415 C  CG  . LEU   A 471 ? 1.4628 1.3265 1.5204 -0.2688 0.0202  0.3975  491 LEU   A CG  
3416 C  CD1 . LEU   A 471 ? 1.3666 1.1926 1.3901 -0.2287 0.0153  0.3770  491 LEU   A CD1 
3417 C  CD2 . LEU   A 471 ? 1.4793 1.4066 1.5413 -0.2627 0.0421  0.4265  491 LEU   A CD2 
3418 N  N   . LYS   A 472 ? 1.7709 1.4906 1.8692 -0.3916 0.0145  0.4884  492 LYS   A N   
3419 C  CA  . LYS   A 472 ? 1.8413 1.4705 1.9337 -0.4212 0.0043  0.5064  492 LYS   A CA  
3420 C  C   . LYS   A 472 ? 1.8632 1.3979 1.9009 -0.3888 -0.0072 0.4864  492 LYS   A C   
3421 O  O   . LYS   A 472 ? 1.8772 1.4072 1.8826 -0.3505 0.0054  0.4958  492 LYS   A O   
3422 C  CB  . LYS   A 472 ? 1.9093 1.5519 2.0099 -0.4333 0.0291  0.5536  492 LYS   A CB  
3423 C  CG  . LYS   A 472 ? 2.0746 1.6232 2.1605 -0.4505 0.0238  0.5652  492 LYS   A CG  
3424 C  CD  . LYS   A 472 ? 2.2272 1.8094 2.3594 -0.4881 0.0369  0.5871  492 LYS   A CD  
3425 C  CE  . LYS   A 472 ? 2.4425 1.9498 2.5509 -0.4936 0.0472  0.6138  492 LYS   A CE  
3426 N  NZ  . LYS   A 472 ? 2.5807 2.1258 2.7366 -0.5298 0.0640  0.6390  492 LYS   A NZ  
3427 N  N   . VAL   A 473 ? 1.8530 1.3128 1.8796 -0.4025 -0.0317 0.4590  493 VAL   A N   
3428 C  CA  . VAL   A 473 ? 1.9199 1.2871 1.8951 -0.3696 -0.0406 0.4374  493 VAL   A CA  
3429 C  C   . VAL   A 473 ? 2.0982 1.3672 2.0554 -0.3871 -0.0439 0.4647  493 VAL   A C   
3430 O  O   . VAL   A 473 ? 2.2418 1.4760 2.2211 -0.4352 -0.0566 0.4762  493 VAL   A O   
3431 C  CB  . VAL   A 473 ? 1.9345 1.2665 1.8945 -0.3680 -0.0630 0.3901  493 VAL   A CB  
3432 C  CG1 . VAL   A 473 ? 1.9359 1.1843 1.8427 -0.3246 -0.0644 0.3679  493 VAL   A CG1 
3433 C  CG2 . VAL   A 473 ? 1.8796 1.3101 1.8631 -0.3586 -0.0606 0.3682  493 VAL   A CG2 
3434 N  N   . GLU   A 474 ? 2.0596 1.2835 1.9798 -0.3485 -0.0341 0.4763  494 GLU   A N   
3435 C  CA  . GLU   A 474 ? 2.1524 1.2749 2.0484 -0.3563 -0.0364 0.5024  494 GLU   A CA  
3436 C  C   . GLU   A 474 ? 2.2071 1.2371 2.0555 -0.3155 -0.0455 0.4744  494 GLU   A C   
3437 O  O   . GLU   A 474 ? 2.1409 1.2010 1.9773 -0.2735 -0.0422 0.4463  494 GLU   A O   
3438 C  CB  . GLU   A 474 ? 2.1791 1.3359 2.0730 -0.3418 -0.0123 0.5456  494 GLU   A CB  
3439 C  CG  . GLU   A 474 ? 2.1405 1.4129 2.0721 -0.3593 0.0055  0.5653  494 GLU   A CG  
3440 C  CD  . GLU   A 474 ? 2.1678 1.4494 2.1040 -0.3741 0.0276  0.6028  494 GLU   A CD  
3441 O  OE1 . GLU   A 474 ? 2.2152 1.4244 2.1172 -0.3588 0.0318  0.6200  494 GLU   A OE1 
3442 O  OE2 . GLU   A 474 ? 2.1837 1.5438 2.1570 -0.3995 0.0420  0.6154  494 GLU   A OE2 
3443 N  N   . SER   A 475 ? 2.2570 1.1820 2.0823 -0.3238 -0.0527 0.4788  495 SER   A N   
3444 C  CA  . SER   A 475 ? 2.2911 1.1144 2.0695 -0.2877 -0.0613 0.4527  495 SER   A CA  
3445 C  C   . SER   A 475 ? 2.3073 1.0801 2.0650 -0.2549 -0.0478 0.4800  495 SER   A C   
3446 O  O   . SER   A 475 ? 2.2434 1.0463 2.0161 -0.2656 -0.0339 0.5179  495 SER   A O   
3447 C  CB  . SER   A 475 ? 2.3291 1.0733 2.0952 -0.3161 -0.0820 0.4191  495 SER   A CB  
3448 O  OG  . SER   A 475 ? 2.3671 1.0129 2.0833 -0.2761 -0.0860 0.3923  495 SER   A OG  
3449 N  N   . ARG   A 476 ? 2.3098 1.0056 2.0307 -0.2115 -0.0503 0.4600  496 ARG   A N   
3450 C  CA  . ARG   A 476 ? 2.4038 1.0486 2.1076 -0.1742 -0.0399 0.4831  496 ARG   A CA  
3451 C  C   . ARG   A 476 ? 2.4001 0.9317 2.0795 -0.1706 -0.0476 0.4629  496 ARG   A C   
3452 O  O   . ARG   A 476 ? 2.4397 0.9341 2.1217 -0.2134 -0.0602 0.4466  496 ARG   A O   
3453 C  CB  . ARG   A 476 ? 2.3244 0.9952 2.0165 -0.1147 -0.0333 0.4833  496 ARG   A CB  
3454 C  CG  . ARG   A 476 ? 2.2910 0.9285 1.9602 -0.0829 -0.0370 0.4390  496 ARG   A CG  
3455 C  CD  . ARG   A 476 ? 2.2348 0.9285 1.9129 -0.0236 -0.0250 0.4387  496 ARG   A CD  
3456 N  NE  . ARG   A 476 ? 2.1839 1.0087 1.9009 -0.0298 -0.0200 0.4481  496 ARG   A NE  
3457 C  CZ  . ARG   A 476 ? 2.0825 0.9815 1.8205 0.0121  -0.0129 0.4480  496 ARG   A CZ  
3458 N  NH1 . ARG   A 476 ? 2.0672 0.9338 1.7995 0.0642  -0.0079 0.4415  496 ARG   A NH1 
3459 N  NH2 . ARG   A 476 ? 1.9989 1.0067 1.7663 0.0018  -0.0112 0.4546  496 ARG   A NH2 
3460 C  CHA . HEM   B .   ? 0.9077 0.9629 1.0236 0.0919  0.1594  0.1339  601 HEM   A CHA 
3461 C  CHB . HEM   B .   ? 0.9105 1.0017 1.0575 0.0571  0.0938  0.1287  601 HEM   A CHB 
3462 C  CHC . HEM   B .   ? 1.0612 0.9755 1.0576 0.0767  0.1182  0.1115  601 HEM   A CHC 
3463 C  CHD . HEM   B .   ? 1.0910 0.9712 1.0083 0.1240  0.1826  0.1071  601 HEM   A CHD 
3464 C  C1A . HEM   B .   ? 0.9081 0.9872 1.0492 0.0794  0.1369  0.1311  601 HEM   A C1A 
3465 C  C2A . HEM   B .   ? 0.9030 1.0215 1.0872 0.0691  0.1198  0.1322  601 HEM   A C2A 
3466 C  C3A . HEM   B .   ? 0.8068 0.9355 0.9952 0.0612  0.1021  0.1299  601 HEM   A C3A 
3467 C  C4A . HEM   B .   ? 0.9063 1.0022 1.0601 0.0640  0.1068  0.1284  601 HEM   A C4A 
3468 C  CMA . HEM   B .   ? 0.7021 0.8647 0.9195 0.0520  0.0802  0.1289  601 HEM   A CMA 
3469 C  CAA . HEM   B .   ? 0.7742 0.9122 0.9887 0.0681  0.1216  0.1354  601 HEM   A CAA 
3470 C  CBA . HEM   B .   ? 0.7866 0.9427 1.0629 0.0720  0.1295  0.1471  601 HEM   A CBA 
3471 C  CGA . HEM   B .   ? 0.7466 0.9201 1.0568 0.0653  0.1229  0.1486  601 HEM   A CGA 
3472 O  O1A . HEM   B .   ? 0.7181 0.9101 1.0868 0.0636  0.1232  0.1577  601 HEM   A O1A 
3473 O  O2A . HEM   B .   ? 0.7023 0.8704 0.9834 0.0615  0.1156  0.1408  601 HEM   A O2A 
3474 C  C1B . HEM   B .   ? 0.9701 1.0222 1.0846 0.0593  0.0974  0.1273  601 HEM   A C1B 
3475 C  C2B . HEM   B .   ? 0.9564 0.9985 1.0675 0.0529  0.0858  0.1313  601 HEM   A C2B 
3476 C  C3B . HEM   B .   ? 1.0549 1.0474 1.1282 0.0570  0.0925  0.1273  601 HEM   A C3B 
3477 C  C4B . HEM   B .   ? 0.9917 0.9623 1.0386 0.0678  0.1086  0.1197  601 HEM   A C4B 
3478 C  CMB . HEM   B .   ? 0.8424 0.9199 0.9817 0.0444  0.0685  0.1387  601 HEM   A CMB 
3479 C  CAB . HEM   B .   ? 1.0058 0.9606 1.0588 0.0526  0.0852  0.1300  601 HEM   A CAB 
3480 C  CBB . HEM   B .   ? 0.9913 0.9609 1.0629 0.0448  0.0726  0.1403  601 HEM   A CBB 
3481 C  C1C . HEM   B .   ? 1.0822 0.9706 1.0447 0.0915  0.1361  0.1056  601 HEM   A C1C 
3482 C  C2C . HEM   B .   ? 1.2602 1.0821 1.1605 0.1057  0.1472  0.0955  601 HEM   A C2C 
3483 C  C3C . HEM   B .   ? 1.1663 0.9783 1.0400 0.1203  0.1654  0.0934  601 HEM   A C3C 
3484 C  C4C . HEM   B .   ? 1.1336 1.0056 1.0572 0.1141  0.1661  0.1032  601 HEM   A C4C 
3485 C  CMC . HEM   B .   ? 1.1601 0.9249 1.0251 0.1050  0.1393  0.0885  601 HEM   A CMC 
3486 C  CAC . HEM   B .   ? 1.2677 1.0084 1.0631 0.1413  0.1820  0.0819  601 HEM   A CAC 
3487 C  CBC . HEM   B .   ? 1.3652 1.0941 1.1259 0.1568  0.2008  0.0818  601 HEM   A CBC 
3488 C  C1D . HEM   B .   ? 1.0396 0.9695 1.0066 0.1185  0.1836  0.1170  601 HEM   A C1D 
3489 C  C2D . HEM   B .   ? 1.0237 0.9566 0.9814 0.1270  0.1995  0.1229  601 HEM   A C2D 
3490 C  C3D . HEM   B .   ? 1.0335 1.0142 1.0498 0.1169  0.1933  0.1310  601 HEM   A C3D 
3491 C  C4D . HEM   B .   ? 0.8976 0.9080 0.9577 0.1033  0.1730  0.1296  601 HEM   A C4D 
3492 C  CMD . HEM   B .   ? 1.0259 0.9089 0.9108 0.1456  0.2193  0.1203  601 HEM   A CMD 
3493 C  CAD . HEM   B .   ? 0.8709 0.8660 0.9008 0.1200  0.2052  0.1408  601 HEM   A CAD 
3494 C  CBD . HEM   B .   ? 0.9603 0.9605 1.0307 0.1356  0.2410  0.1588  601 HEM   A CBD 
3495 C  CGD . HEM   B .   ? 1.0349 1.0414 1.1156 0.1378  0.2557  0.1714  601 HEM   A CGD 
3496 O  O1D . HEM   B .   ? 1.0292 1.0388 1.1410 0.1499  0.2891  0.1897  601 HEM   A O1D 
3497 O  O2D . HEM   B .   ? 0.9938 1.0026 1.0543 0.1281  0.2354  0.1651  601 HEM   A O2D 
3498 N  NA  . HEM   B .   ? 0.9842 1.0486 1.1080 0.0755  0.1271  0.1274  601 HEM   A NA  
3499 N  NB  . HEM   B .   ? 1.0908 1.1001 1.1651 0.0687  0.1122  0.1217  601 HEM   A NB  
3500 N  NC  . HEM   B .   ? 1.1538 1.0695 1.1292 0.0969  0.1470  0.1086  601 HEM   A NC  
3501 N  ND  . HEM   B .   ? 1.0785 1.0580 1.1080 0.1046  0.1686  0.1227  601 HEM   A ND  
3502 FE FE  . HEM   B .   ? 0.8786 0.8747 0.9318 0.0853  0.1381  0.1196  601 HEM   A FE  
3503 C  C1  . GOL   C .   ? 1.3286 1.4784 1.0166 0.0533  0.0157  0.3968  602 GOL   A C1  
3504 O  O1  . GOL   C .   ? 1.3828 1.5599 1.1243 0.0385  0.0239  0.3735  602 GOL   A O1  
3505 C  C2  . GOL   C .   ? 1.3472 1.4571 1.0617 0.0484  -0.0007 0.4082  602 GOL   A C2  
3506 O  O2  . GOL   C .   ? 1.2627 1.3738 1.0399 0.0340  -0.0033 0.3886  602 GOL   A O2  
3507 C  C3  . GOL   C .   ? 1.3858 1.4804 1.0678 0.0763  -0.0357 0.4025  602 GOL   A C3  
3508 O  O3  . GOL   C .   ? 1.3706 1.4521 1.1038 0.0770  -0.0561 0.3904  602 GOL   A O3  
3509 C  C12 . A1A4V D .   ? 1.0848 1.0427 1.0333 0.0680  0.1034  0.0928  603 A1A4V A C12 
3510 C  C14 . A1A4V D .   ? 1.1978 1.2298 1.0567 0.0615  0.0076  0.0775  603 A1A4V A C14 
3511 C  C15 . A1A4V D .   ? 1.1450 1.1598 0.9874 0.0447  -0.0102 0.0678  603 A1A4V A C15 
3512 C  C16 . A1A4V D .   ? 1.2123 1.1680 0.9899 0.0498  -0.0139 0.0592  603 A1A4V A C16 
3513 C  C19 . A1A4V D .   ? 1.2433 1.2757 1.1205 0.0060  -0.0373 0.0610  603 A1A4V A C19 
3514 C  C20 . A1A4V D .   ? 1.1769 1.2288 1.0650 0.0240  -0.0217 0.0676  603 A1A4V A C20 
3515 C  C22 . A1A4V D .   ? 1.1748 1.2303 1.1390 0.0842  0.0845  0.1060  603 A1A4V A C22 
3516 C  C23 . A1A4V D .   ? 1.0403 1.1399 1.0538 0.0706  0.0706  0.1012  603 A1A4V A C23 
3517 C  C10 . A1A4V D .   ? 0.9558 0.9796 0.9797 0.0475  0.0846  0.1014  603 A1A4V A C10 
3518 C  C13 . A1A4V D .   ? 1.1349 1.1770 1.0341 0.0652  0.0365  0.0853  603 A1A4V A C13 
3519 C  C17 . A1A4V D .   ? 1.2927 1.2247 1.0549 0.0329  -0.0320 0.0489  603 A1A4V A C17 
3520 C  C18 . A1A4V D .   ? 1.2488 1.2194 1.0642 0.0093  -0.0442 0.0507  603 A1A4V A C18 
3521 C  C02 . A1A4V D .   ? 1.0268 1.0320 0.9105 0.0689  0.0572  0.0855  603 A1A4V A C02 
3522 C  C04 . A1A4V D .   ? 1.0257 1.0163 0.9414 0.0651  0.0807  0.0878  603 A1A4V A C04 
3523 C  C05 . A1A4V D .   ? 1.1703 1.1101 1.0279 0.0652  0.0730  0.0775  603 A1A4V A C05 
3524 C  C06 . A1A4V D .   ? 1.0833 1.0087 0.9496 0.0569  0.0711  0.0750  603 A1A4V A C06 
3525 C  C07 . A1A4V D .   ? 1.0370 1.0002 0.9640 0.0524  0.0783  0.0847  603 A1A4V A C07 
3526 C  C08 . A1A4V D .   ? 1.0220 1.0277 0.9856 0.0337  0.0598  0.0869  603 A1A4V A C08 
3527 C  C09 . A1A4V D .   ? 0.9560 0.9899 0.9636 0.0320  0.0644  0.0951  603 A1A4V A C09 
3528 C  C24 . A1A4V D .   ? 0.9407 1.0480 0.9966 0.0683  0.0854  0.1061  603 A1A4V A C24 
3529 C  C25 . A1A4V D .   ? 0.9100 1.0103 0.9688 0.0632  0.0895  0.1056  603 A1A4V A C25 
3530 C  C26 . A1A4V D .   ? 0.9038 1.0275 0.9781 0.0509  0.0735  0.1011  603 A1A4V A C26 
3531 C  C27 . A1A4V D .   ? 0.8631 1.0203 0.9505 0.0438  0.0568  0.0969  603 A1A4V A C27 
3532 C  C28 . A1A4V D .   ? 0.9118 1.0911 1.0110 0.0331  0.0460  0.0959  603 A1A4V A C28 
3533 C  C29 . A1A4V D .   ? 0.9142 1.0796 1.0126 0.0275  0.0483  0.0991  603 A1A4V A C29 
3534 C  C30 . A1A4V D .   ? 0.9424 1.0742 1.0296 0.0352  0.0622  0.1014  603 A1A4V A C30 
3535 C  C31 . A1A4V D .   ? 0.9418 1.0539 1.0170 0.0474  0.0764  0.1024  603 A1A4V A C31 
3536 C  C32 . A1A4V D .   ? 0.9641 1.0429 1.0260 0.0587  0.0961  0.1063  603 A1A4V A C32 
3537 C  C33 . A1A4V D .   ? 0.9885 1.0484 1.0359 0.0713  0.1140  0.1104  603 A1A4V A C33 
3538 C  C34 . A1A4V D .   ? 0.9778 1.0477 1.0228 0.0725  0.1104  0.1109  603 A1A4V A C34 
3539 C  C36 . A1A4V D .   ? 1.1182 1.2793 1.1582 0.0662  0.0384  0.0934  603 A1A4V A C36 
3540 C  C38 . A1A4V D .   ? 1.1191 1.3040 1.1710 0.0750  0.0294  0.0921  603 A1A4V A C38 
3541 C  C39 . A1A4V D .   ? 1.0867 1.2521 1.1310 0.0892  0.0360  0.0965  603 A1A4V A C39 
3542 C  C41 . A1A4V D .   ? 1.0840 1.3043 1.1544 0.0996  0.0160  0.0894  603 A1A4V A C41 
3543 C  C42 . A1A4V D .   ? 1.1123 1.3595 1.1942 0.0844  0.0107  0.0865  603 A1A4V A C42 
3544 C  C43 . A1A4V D .   ? 1.1127 1.3395 1.1844 0.0712  0.0161  0.0879  603 A1A4V A C43 
3545 N  N03 . A1A4V D .   ? 1.0713 1.0921 0.9937 0.0589  0.0618  0.0864  603 A1A4V A N03 
3546 N  N11 . A1A4V D .   ? 1.0133 1.0025 1.0127 0.0651  0.1051  0.1010  603 A1A4V A N11 
3547 N  N35 . A1A4V D .   ? 1.0892 1.2140 1.1152 0.0731  0.0577  0.0995  603 A1A4V A N35 
3548 N  N40 . A1A4V D .   ? 1.1056 1.2849 1.1576 0.1005  0.0286  0.0953  603 A1A4V A N40 
3549 O  O01 . A1A4V D .   ? 1.0684 1.0302 0.9038 0.0828  0.0701  0.0857  603 A1A4V A O01 
3550 O  O37 . A1A4V D .   ? 1.0696 1.2419 1.1128 0.0541  0.0310  0.0904  603 A1A4V A O37 
3551 S  S21 . A1A4V D .   ? 1.0796 1.1183 0.9849 0.0847  0.0590  0.0973  603 A1A4V A S21 
3552 O  O   . HOH   E .   ? 0.8802 1.1490 1.0198 0.0309  0.0268  0.0950  701 HOH   A O   
3553 O  O   . HOH   E .   ? 1.1475 1.1936 1.1923 0.1019  0.1630  0.1480  702 HOH   A O   
3554 O  O   . HOH   E .   ? 1.6703 1.7623 1.7945 0.2812  -0.3514 0.4427  703 HOH   A O   
3555 O  O   . HOH   E .   ? 1.4584 1.6867 1.5473 0.3572  0.0171  0.0659  704 HOH   A O   
3556 O  O   . HOH   E .   ? 0.7355 0.9615 1.2881 0.0581  0.1724  0.2086  705 HOH   A O   
3557 O  O   . HOH   E .   ? 1.8715 1.9320 1.4034 0.1994  -0.2646 0.3592  706 HOH   A O   
3558 O  O   . HOH   E .   ? 2.2866 2.0390 1.5428 0.3260  -0.0618 0.2348  707 HOH   A O   
3559 O  O   . HOH   E .   ? 1.7931 1.7950 2.2101 0.4452  0.5745  0.3073  708 HOH   A O   
3560 O  O   . HOH   E .   ? 1.2744 1.4929 1.2924 0.1351  -0.3281 0.2059  709 HOH   A O   
3561 O  O   . HOH   E .   ? 0.7355 1.0234 0.8377 0.0633  -0.0253 0.0655  710 HOH   A O   
3562 O  O   . HOH   E .   ? 0.8436 1.1093 0.9871 0.0745  0.0234  0.0741  711 HOH   A O   
3563 O  O   . HOH   E .   ? 1.3514 1.3908 1.3503 0.4758  0.0314  0.0020  712 HOH   A O   
3564 O  O   . HOH   E .   ? 2.6299 2.0801 2.8256 -0.6062 -0.1333 0.4240  713 HOH   A O   
3565 O  O   . HOH   E .   ? 0.8390 1.0085 0.9958 0.0712  0.0645  0.1040  714 HOH   A O   
3566 O  O   . HOH   E .   ? 3.1029 1.8129 1.2582 0.4279  0.1169  -0.1173 715 HOH   A O   
3567 O  O   . HOH   E .   ? 1.8790 1.2645 1.3253 0.2622  0.2641  0.0262  716 HOH   A O   
3568 O  O   . HOH   E .   ? 0.8872 1.1168 1.1276 0.0368  0.0109  0.1259  717 HOH   A O   
3569 O  O   . HOH   E .   ? 1.1223 1.1930 1.4591 0.2045  0.2987  0.2098  718 HOH   A O   
3570 O  O   . HOH   E .   ? 1.1109 1.5800 1.2448 0.0201  0.0508  0.1392  719 HOH   A O   
3571 O  O   . HOH   E .   ? 0.9126 1.1167 0.9147 0.1403  -0.0479 -0.0170 720 HOH   A O   
3572 O  O   . HOH   E .   ? 1.7943 1.5890 1.0965 0.3183  -0.2442 -0.2396 721 HOH   A O   
3573 O  O   . HOH   E .   ? 0.6825 0.8658 0.9116 0.0509  0.0764  0.1167  722 HOH   A O   
3574 O  O   . HOH   E .   ? 1.1307 1.5047 1.1116 0.0062  0.0607  0.2253  723 HOH   A O   
3575 O  O   . HOH   E .   ? 1.0971 1.0906 1.5591 0.0524  0.3144  0.3301  724 HOH   A O   
3576 O  O   . HOH   E .   ? 0.9979 1.4438 1.0879 0.0515  0.0503  0.1216  725 HOH   A O   
3577 O  O   . HOH   E .   ? 1.6470 1.6740 1.1640 0.1413  -0.1003 0.4510  726 HOH   A O   
3578 O  O   . HOH   E .   ? 0.9342 1.2395 1.8847 0.0302  0.3074  0.3559  727 HOH   A O   
3579 O  O   . HOH   E .   ? 2.3067 1.2610 1.7984 -0.1659 -0.1500 0.0028  728 HOH   A O   
3580 O  O   . HOH   E .   ? 1.0221 1.2701 1.1839 0.1281  -0.3018 0.2196  729 HOH   A O   
3581 O  O   . HOH   E .   ? 1.0454 1.3581 1.0027 -0.0068 0.0489  0.2584  730 HOH   A O   
3582 O  O   . HOH   E .   ? 1.5031 1.4570 2.1227 0.5690  0.3514  0.3350  731 HOH   A O   
3583 O  O   . HOH   E .   ? 1.1676 0.9618 1.3434 0.1477  0.0078  0.0807  732 HOH   A O   
3584 O  O   . HOH   E .   ? 0.7908 0.9781 0.9556 0.0557  0.0626  0.1031  733 HOH   A O   
3585 O  O   . HOH   E .   ? 1.4825 1.4709 1.0832 0.1390  -0.1214 0.4659  734 HOH   A O   
3586 O  O   . HOH   E .   ? 0.8918 1.1632 1.0299 0.0494  0.0274  0.0869  735 HOH   A O   
3587 O  O   . HOH   E .   ? 1.1186 1.5890 1.2981 0.0583  0.0112  0.1061  736 HOH   A O   
3588 O  O   . HOH   E .   ? 1.0194 1.5917 1.2538 0.0556  0.0167  0.1257  737 HOH   A O   
3589 O  O   . HOH   E .   ? 1.6029 1.2269 1.1328 0.2536  -0.3126 -0.2949 738 HOH   A O   
3590 O  O   . HOH   E .   ? 1.5890 1.5709 1.2225 0.1746  -0.1893 0.4582  739 HOH   A O   
3591 O  O   . HOH   E .   ? 1.6442 2.1245 1.8500 0.4215  0.0000  0.0000  740 HOH   A O   
# 
