data_9COY
# 
_entry.id   9COY 
# 
_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   9COY         pdb_00009coy 10.2210/pdb9coy/pdb 
WWPDB D_1000285852 ?            ?                   
# 
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                        9COY 
_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   0000-0002-4498-6057 
# 
_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 
;N-[(2S)-1-([1,1'-biphenyl]-4-yl)-3-{[(2R)-1-oxo-3-phenyl-1-{[3-(pyridin-3-yl)propyl]amino}propan-2-yl]sulfanyl}propan-2-yl]-2,2-dimethylpropanamide
;
593.821   1  ?                                          ?                                                   ? ? 
4 water       nat water 18.015    16 ?                                          ? ? ? 
# 
_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 
;N-[(2S)-1-([1,1'-biphenyl]-4-yl)-3-{[(2R)-1-oxo-3-phenyl-1-{[3-(pyridin-3-yl)propyl]amino}propan-2-yl]sulfanyl}propan-2-yl]-2,2-dimethylpropanamide
;
A1A4T 
4 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              C41 
_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 
A1A4T non-polymer         . 
;N-[(2S)-1-([1,1'-biphenyl]-4-yl)-3-{[(2R)-1-oxo-3-phenyl-1-{[3-(pyridin-3-yl)propyl]amino}propan-2-yl]sulfanyl}propan-2-yl]-2,2-dimethylpropanamide
;
?    'C37 H43 N3 O2 S'  593.821 
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  
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 146 166 166 THR THR A . n 
A 1 147 GLY 147 167 167 GLY GLY A . n 
A 1 148 LYS 148 168 168 LYS LYS 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 184 204 204 VAL VAL A . n 
A 1 185 GLU 185 205 205 GLU GLU A . n 
A 1 186 ASN 186 206 206 ASN ASN 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 197 217 217 ASP ASP 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 220 240 240 VAL VAL A . n 
A 1 221 PHE 221 241 241 PHE PHE A . n 
A 1 222 PRO 222 242 242 PRO PRO A . n 
A 1 223 ARG 223 243 243 ARG ARG A . n 
A 1 224 GLU 224 244 244 GLU GLU A . n 
A 1 225 VAL 225 245 245 VAL VAL 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 240 260 260 ARG ARG A . n 
A 1 241 LEU 241 261 261 LEU LEU A . n 
A 1 242 GLU 242 262 262 GLU GLU A . n 
A 1 243 ASP 243 263 263 ASP ASP 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 249 269 269 VAL VAL 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 259 279 279 GLN GLN 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 ?   ?   ?   A . n 
A 1 267 HIS 267 287 ?   ?   ?   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        A1A4T 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A4T 
_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 A1A4T 1  602 700 A1A4T 564 A . 
D 4 HOH   1  701 7   HOH   HOH A . 
D 4 HOH   2  702 16  HOH   HOH A . 
D 4 HOH   3  703 11  HOH   HOH A . 
D 4 HOH   4  704 1   HOH   HOH A . 
D 4 HOH   5  705 5   HOH   HOH A . 
D 4 HOH   6  706 6   HOH   HOH A . 
D 4 HOH   7  707 4   HOH   HOH A . 
D 4 HOH   8  708 14  HOH   HOH A . 
D 4 HOH   9  709 2   HOH   HOH A . 
D 4 HOH   10 710 15  HOH   HOH A . 
D 4 HOH   11 711 13  HOH   HOH A . 
D 4 HOH   12 712 12  HOH   HOH A . 
D 4 HOH   13 713 3   HOH   HOH A . 
D 4 HOH   14 714 10  HOH   HOH A . 
D 4 HOH   15 715 8   HOH   HOH A . 
D 4 HOH   16 716 9   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                     9COY 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     77.890 
_cell.length_a_esd                 ? 
_cell.length_b                     100.690 
_cell.length_b_esd                 ? 
_cell.length_c                     130.710 
_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                         9COY 
_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                   9COY 
_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             2.30 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.50 
_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                      mirrirs 
_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         2024-02-16 
_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                                       9COY 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.65 
_reflns.d_resolution_low                               79.77 
_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                                     15204 
_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                           99.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.8 
_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                                0.031 
_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                              0.066 
_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                                    2.65 
_reflns_shell.d_res_low                                     2.79 
_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                             2185 
_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                               0.745 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.406 
_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                                  1.712 
_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                                 9COY 
_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                            2.65 
_refine.ls_d_res_low                             44.83 
_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                     15194 
_refine.ls_number_reflns_R_free                  742 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.34 
_refine.ls_percent_reflns_R_free                 4.88 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2470 
_refine.ls_R_factor_R_free                       0.2712 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2457 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               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                 31.52 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.37 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.65 
_refine_hist.d_res_low                        44.83 
_refine_hist.number_atoms_solvent             16 
_refine_hist.number_atoms_total               3683 
_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        3581 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         86 
_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' ? 0.004  ? 3775 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.763  ? 5122 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.909 ? 1426 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.046  ? 560  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 646  ? 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' 2.65 2.85  . . 163 2841 100.00 . . . . 0.3640 . . . . . . . . . . . 0.3811 
'X-RAY DIFFRACTION' 2.85 3.14  . . 158 2840 100.00 . . . . 0.3588 . . . . . . . . . . . 0.3806 
'X-RAY DIFFRACTION' 3.14 3.60  . . 154 2852 99.00  . . . . 0.2976 . . . . . . . . . . . 0.2995 
'X-RAY DIFFRACTION' 3.60 4.53  . . 135 2897 99.00  . . . . 0.2493 . . . . . . . . . . . 0.2785 
'X-RAY DIFFRACTION' 4.53 44.83 . . 132 3022 99.00  . . . . 0.2125 . . . . . . . . . . . 0.2378 
# 
_struct.entry_id                     9COY 
_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        9COY 
_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 ? 
# 
_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              9COY 
_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 9COY ?   A ?   ? UNP P08684 LEU 3  deletion         ?   1  
1 9COY ?   A ?   ? UNP P08684 ILE 4  deletion         ?   2  
1 9COY ?   A ?   ? UNP P08684 PRO 5  deletion         ?   3  
1 9COY ?   A ?   ? UNP P08684 ASP 6  deletion         ?   4  
1 9COY ?   A ?   ? UNP P08684 LEU 7  deletion         ?   5  
1 9COY ?   A ?   ? UNP P08684 ALA 8  deletion         ?   6  
1 9COY ?   A ?   ? UNP P08684 MET 9  deletion         ?   7  
1 9COY ?   A ?   ? UNP P08684 GLU 10 deletion         ?   8  
1 9COY ?   A ?   ? UNP P08684 THR 11 deletion         ?   9  
1 9COY ?   A ?   ? UNP P08684 TRP 12 deletion         ?   10 
1 9COY ?   A ?   ? UNP P08684 LEU 13 deletion         ?   11 
1 9COY ?   A ?   ? UNP P08684 LEU 14 deletion         ?   12 
1 9COY ?   A ?   ? UNP P08684 LEU 15 deletion         ?   13 
1 9COY ?   A ?   ? UNP P08684 ALA 16 deletion         ?   14 
1 9COY ?   A ?   ? UNP P08684 VAL 17 deletion         ?   15 
1 9COY ?   A ?   ? UNP P08684 SER 18 deletion         ?   16 
1 9COY ?   A ?   ? UNP P08684 LEU 19 deletion         ?   17 
1 9COY ?   A ?   ? UNP P08684 VAL 20 deletion         ?   18 
1 9COY ?   A ?   ? UNP P08684 LEU 21 deletion         ?   19 
1 9COY ?   A ?   ? UNP P08684 LEU 22 deletion         ?   20 
1 9COY HIS A 484 ? UNP P08684 ?   ?  'expression tag' 504 21 
1 9COY HIS A 485 ? UNP P08684 ?   ?  'expression tag' 505 22 
1 9COY HIS A 486 ? UNP P08684 ?   ?  'expression tag' 506 23 
1 9COY 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 
1 2 A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
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_555 x,-y,-z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 11  ? GLY A 17  ? GLY A 31  GLY A 37  1 ? 7  
HELX_P HELX_P2  AA2 ASN A 29  ? HIS A 34  ? ASN A 49  HIS A 54  5 ? 6  
HELX_P HELX_P3  AA3 LYS A 35  ? GLY A 49  ? LYS A 55  GLY A 69  1 ? 15 
HELX_P HELX_P4  AA4 ASP A 66  ? VAL A 75  ? ASP A 86  VAL A 95  1 ? 10 
HELX_P HELX_P5  AA5 VAL A 91  ? ALA A 97  ? VAL A 111 ALA A 117 5 ? 7  
HELX_P HELX_P6  AA6 GLU A 102 ? SER A 114 ? GLU A 122 SER A 134 1 ? 13 
HELX_P HELX_P7  AA7 PRO A 115 ? PHE A 117 ? PRO A 135 PHE A 137 5 ? 3  
HELX_P HELX_P8  AA8 THR A 118 ? MET A 125 ? THR A 138 MET A 145 1 ? 8  
HELX_P HELX_P9  AA9 MET A 125 ? ALA A 130 ? MET A 145 ALA A 150 1 ? 6  
HELX_P HELX_P10 AB1 GLN A 131 ? THR A 146 ? GLN A 151 THR A 166 1 ? 16 
HELX_P HELX_P11 AB2 LEU A 152 ? GLY A 170 ? LEU A 172 GLY A 190 1 ? 19 
HELX_P HELX_P12 AB3 PRO A 198 ? PHE A 206 ? PRO A 218 PHE A 226 1 ? 9  
HELX_P HELX_P13 AB4 LEU A 209 ? VAL A 215 ? LEU A 229 VAL A 235 1 ? 7  
HELX_P HELX_P14 AB5 PRO A 222 ? LEU A 241 ? PRO A 242 LEU A 261 1 ? 20 
HELX_P HELX_P15 AB6 ASP A 250 ? GLN A 259 ? ASP A 270 GLN A 279 1 ? 10 
HELX_P HELX_P16 AB7 SER A 271 ? HIS A 304 ? SER A 291 HIS A 324 1 ? 34 
HELX_P HELX_P17 AB8 HIS A 304 ? LEU A 319 ? HIS A 324 LEU A 339 1 ? 16 
HELX_P HELX_P18 AB9 PRO A 320 ? ALA A 323 ? PRO A 340 ALA A 343 5 ? 4  
HELX_P HELX_P19 AC1 THR A 326 ? LEU A 331 ? THR A 346 LEU A 351 1 ? 6  
HELX_P HELX_P20 AC2 MET A 333 ? PHE A 347 ? MET A 353 PHE A 367 1 ? 15 
HELX_P HELX_P21 AC3 PRO A 377 ? ARG A 383 ? PRO A 397 ARG A 403 1 ? 7  
HELX_P HELX_P22 AC4 LEU A 395 ? SER A 400 ? LEU A 415 SER A 420 5 ? 6  
HELX_P HELX_P23 AC5 ASN A 403 ? ILE A 407 ? ASN A 423 ILE A 427 5 ? 5  
HELX_P HELX_P24 AC6 SER A 417 ? ASN A 421 ? SER A 437 ASN A 441 5 ? 5  
HELX_P HELX_P25 AC7 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 ? ? ? ? ? ? ? 2.308 ? ? 
metalc2 metalc ? ? B HEM .   FE ? ? ? 1_555 C A1A4T . N24 ? ? A HEM 601 A A1A4T 602 1_555 ? ? ? ? ? ? ? 2.148 ? ? 
# 
_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 97.7  ? 
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 89.9  ? 
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 90.2  ? 
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 87.6  ? 
5  NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 NC  ? B HEM   . ? A HEM   601 ? 1_555 174.7 ? 
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 88.7  ? 
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 92.6  ? 
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 90.0  ? 
9  NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 ND  ? B HEM   . ? A HEM   601 ? 1_555 177.4 ? 
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 90.9  ? 
11 SG ? A CYS 422 ? A CYS 442 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N24 ? C A1A4T . ? A A1A4T 602 ? 1_555 176.8 ? 
12 NA ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N24 ? C A1A4T . ? A A1A4T 602 ? 1_555 85.1  ? 
13 NB ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N24 ? C A1A4T . ? A A1A4T 602 ? 1_555 88.4  ? 
14 NC ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N24 ? C A1A4T . ? A A1A4T 602 ? 1_555 89.7  ? 
15 ND ? B HEM .   ? A HEM 601 ? 1_555 FE ? B HEM . ? A HEM 601 ? 1_555 N24 ? C A1A4T . ? A A1A4T 602 ? 1_555 89.0  ? 
# 
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 4.12 
2 LEU 241 A . ? LEU 261 A GLU 242 A ? GLU 262 A 1 8.68 
3 ILE 453 A . ? ILE 473 A PRO 454 A ? PRO 474 A 1 3.37 
# 
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 ? PRO A 447 ? PHE A 463 PRO A 467 
AA3 1 VAL A 361 ? ILE A 363 ? VAL A 381 ILE A 383 
AA3 2 MET A 366 ? ILE A 368 ? MET A 386 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 TRP A 52  ? N TRP A 72  O ALA A 63  ? O ALA A 83  
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 LYS A 472 ? O LYS A 492 N LYS A 446 ? N LYS A 466 
AA3 1 2 N VAL A 361 ? N VAL A 381 O ILE A 368 ? O ILE A 388 
# 
_pdbx_entry_details.entry_id                   9COY 
_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 SER A 29  ? ? 67.27   -5.62   
2  1 PHE A 46  ? ? 69.86   -50.44  
3  1 VAL A 95  ? ? -122.33 -64.60  
4  1 GLU A 97  ? ? -91.41  31.61   
5  1 VAL A 101 ? ? -135.05 -37.98  
6  1 PHE A 102 ? ? -118.68 66.69   
7  1 ASP A 123 ? ? 61.21   -123.78 
8  1 PRO A 169 ? ? -45.61  152.12  
9  1 PHE A 189 ? ? -144.69 -6.32   
10 1 ASN A 198 ? ? -118.80 65.80   
11 1 PRO A 202 ? ? -109.00 52.22   
12 1 PHE A 226 ? ? -115.29 63.38   
13 1 TYR A 307 ? ? -93.95  -74.47  
14 1 ILE A 369 ? ? -59.90  -9.15   
15 1 MET A 371 ? ? 70.29   -49.27  
# 
_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         -19.0798 
_pdbx_refine_tls.origin_y         -23.8960 
_pdbx_refine_tls.origin_z         -14.0437 
_pdbx_refine_tls.T[1][1]          0.5403 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0823 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0932 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.6631 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0149 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.6272 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          2.7341 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -2.0946 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.6227 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          5.6269 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          1.1622 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.9770 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.1172 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0818 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.2222 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.3119 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.1256 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.1339 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.2966 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0544 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.2556 
_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_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 207 ? A THR 187 
9  1 Y 1 A LYS 208 ? A LYS 188 
10 1 Y 1 A LYS 209 ? A LYS 189 
11 1 Y 1 A LEU 210 ? A LEU 190 
12 1 Y 1 A LEU 211 ? A LEU 191 
13 1 Y 1 A ARG 212 ? A ARG 192 
14 1 Y 1 A PHE 213 ? A PHE 193 
15 1 Y 1 A ASP 214 ? A ASP 194 
16 1 Y 1 A PHE 215 ? A PHE 195 
17 1 Y 1 A LEU 216 ? A LEU 196 
18 1 Y 1 A THR 264 ? A THR 244 
19 1 Y 1 A GLN 265 ? A GLN 245 
20 1 Y 1 A LYS 266 ? A LYS 246 
21 1 Y 1 A HIS 267 ? A HIS 247 
22 1 Y 1 A ARG 268 ? A ARG 248 
23 1 Y 1 A ASN 280 ? A ASN 260 
24 1 Y 1 A SER 281 ? A SER 261 
25 1 Y 1 A LYS 282 ? A LYS 262 
26 1 Y 1 A GLU 283 ? A GLU 263 
27 1 Y 1 A THR 284 ? A THR 264 
28 1 Y 1 A GLU 285 ? A GLU 265 
29 1 Y 1 A SER 286 ? A SER 266 
30 1 Y 1 A HIS 287 ? A HIS 267 
31 1 Y 1 A ASP 497 ? A ASP 477 
32 1 Y 1 A GLY 498 ? A GLY 478 
33 1 Y 1 A THR 499 ? A THR 479 
34 1 Y 1 A VAL 500 ? A VAL 480 
35 1 Y 1 A SER 501 ? A SER 481 
36 1 Y 1 A GLY 502 ? A GLY 482 
37 1 Y 1 A ALA 503 ? A ALA 483 
38 1 Y 1 A HIS 504 ? A HIS 484 
39 1 Y 1 A HIS 505 ? A HIS 485 
40 1 Y 1 A HIS 506 ? A HIS 486 
41 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 
A1A4T C11  C  N N 1   
A1A4T C15  C  Y N 2   
A1A4T C16  C  Y N 3   
A1A4T C17  C  Y N 4   
A1A4T C18  C  Y N 5   
A1A4T C19  C  Y N 6   
A1A4T C20  C  Y N 7   
A1A4T C23  C  Y N 8   
A1A4T C25  C  Y N 9   
A1A4T C26  C  Y N 10  
A1A4T C13  C  N N 11  
A1A4T C14  C  N N 12  
A1A4T C22  C  N N 13  
A1A4T C01  C  N N 14  
A1A4T C02  C  N N 15  
A1A4T C03  C  N N 16  
A1A4T C05  C  N N 17  
A1A4T C06  C  N R 18  
A1A4T C08  C  N N 19  
A1A4T C09  C  N S 20  
A1A4T C27  C  Y N 21  
A1A4T C28  C  Y N 22  
A1A4T C29  C  N N 23  
A1A4T C30  C  N N 24  
A1A4T C31  C  N N 25  
A1A4T C32  C  Y N 26  
A1A4T C33  C  Y N 27  
A1A4T C34  C  Y N 28  
A1A4T C35  C  Y N 29  
A1A4T C36  C  Y N 30  
A1A4T C37  C  Y N 31  
A1A4T C38  C  Y N 32  
A1A4T C39  C  Y N 33  
A1A4T C40  C  Y N 34  
A1A4T C41  C  Y N 35  
A1A4T C42  C  Y N 36  
A1A4T C43  C  Y N 37  
A1A4T N04  N  N N 38  
A1A4T N10  N  N N 39  
A1A4T N24  N  Y N 40  
A1A4T O12  O  N N 41  
A1A4T O21  O  N N 42  
A1A4T S07  S  N N 43  
A1A4T H1   H  N N 44  
A1A4T H2   H  N N 45  
A1A4T H3   H  N N 46  
A1A4T H4   H  N N 47  
A1A4T H5   H  N N 48  
A1A4T H6   H  N N 49  
A1A4T H7   H  N N 50  
A1A4T H8   H  N N 51  
A1A4T H9   H  N N 52  
A1A4T H10  H  N N 53  
A1A4T H11  H  N N 54  
A1A4T H12  H  N N 55  
A1A4T H13  H  N N 56  
A1A4T H14  H  N N 57  
A1A4T H15  H  N N 58  
A1A4T H16  H  N N 59  
A1A4T H17  H  N N 60  
A1A4T H18  H  N N 61  
A1A4T H19  H  N N 62  
A1A4T H20  H  N N 63  
A1A4T H21  H  N N 64  
A1A4T H22  H  N N 65  
A1A4T H23  H  N N 66  
A1A4T H24  H  N N 67  
A1A4T H25  H  N N 68  
A1A4T H26  H  N N 69  
A1A4T H27  H  N N 70  
A1A4T H28  H  N N 71  
A1A4T H29  H  N N 72  
A1A4T H30  H  N N 73  
A1A4T H31  H  N N 74  
A1A4T H32  H  N N 75  
A1A4T H33  H  N N 76  
A1A4T H34  H  N N 77  
A1A4T H35  H  N N 78  
A1A4T H36  H  N N 79  
A1A4T H37  H  N N 80  
A1A4T H38  H  N N 81  
A1A4T H39  H  N N 82  
A1A4T H40  H  N N 83  
A1A4T H41  H  N N 84  
A1A4T H42  H  N N 85  
A1A4T H43  H  N N 86  
ALA   N    N  N N 87  
ALA   CA   C  N S 88  
ALA   C    C  N N 89  
ALA   O    O  N N 90  
ALA   CB   C  N N 91  
ALA   OXT  O  N N 92  
ALA   H    H  N N 93  
ALA   H2   H  N N 94  
ALA   HA   H  N N 95  
ALA   HB1  H  N N 96  
ALA   HB2  H  N N 97  
ALA   HB3  H  N N 98  
ALA   HXT  H  N N 99  
ARG   N    N  N N 100 
ARG   CA   C  N S 101 
ARG   C    C  N N 102 
ARG   O    O  N N 103 
ARG   CB   C  N N 104 
ARG   CG   C  N N 105 
ARG   CD   C  N N 106 
ARG   NE   N  N N 107 
ARG   CZ   C  N N 108 
ARG   NH1  N  N N 109 
ARG   NH2  N  N N 110 
ARG   OXT  O  N N 111 
ARG   H    H  N N 112 
ARG   H2   H  N N 113 
ARG   HA   H  N N 114 
ARG   HB2  H  N N 115 
ARG   HB3  H  N N 116 
ARG   HG2  H  N N 117 
ARG   HG3  H  N N 118 
ARG   HD2  H  N N 119 
ARG   HD3  H  N N 120 
ARG   HE   H  N N 121 
ARG   HH11 H  N N 122 
ARG   HH12 H  N N 123 
ARG   HH21 H  N N 124 
ARG   HH22 H  N N 125 
ARG   HXT  H  N N 126 
ASN   N    N  N N 127 
ASN   CA   C  N S 128 
ASN   C    C  N N 129 
ASN   O    O  N N 130 
ASN   CB   C  N N 131 
ASN   CG   C  N N 132 
ASN   OD1  O  N N 133 
ASN   ND2  N  N N 134 
ASN   OXT  O  N N 135 
ASN   H    H  N N 136 
ASN   H2   H  N N 137 
ASN   HA   H  N N 138 
ASN   HB2  H  N N 139 
ASN   HB3  H  N N 140 
ASN   HD21 H  N N 141 
ASN   HD22 H  N N 142 
ASN   HXT  H  N N 143 
ASP   N    N  N N 144 
ASP   CA   C  N S 145 
ASP   C    C  N N 146 
ASP   O    O  N N 147 
ASP   CB   C  N N 148 
ASP   CG   C  N N 149 
ASP   OD1  O  N N 150 
ASP   OD2  O  N N 151 
ASP   OXT  O  N N 152 
ASP   H    H  N N 153 
ASP   H2   H  N N 154 
ASP   HA   H  N N 155 
ASP   HB2  H  N N 156 
ASP   HB3  H  N N 157 
ASP   HD2  H  N N 158 
ASP   HXT  H  N N 159 
CYS   N    N  N N 160 
CYS   CA   C  N R 161 
CYS   C    C  N N 162 
CYS   O    O  N N 163 
CYS   CB   C  N N 164 
CYS   SG   S  N N 165 
CYS   OXT  O  N N 166 
CYS   H    H  N N 167 
CYS   H2   H  N N 168 
CYS   HA   H  N N 169 
CYS   HB2  H  N N 170 
CYS   HB3  H  N N 171 
CYS   HG   H  N N 172 
CYS   HXT  H  N N 173 
GLN   N    N  N N 174 
GLN   CA   C  N S 175 
GLN   C    C  N N 176 
GLN   O    O  N N 177 
GLN   CB   C  N N 178 
GLN   CG   C  N N 179 
GLN   CD   C  N N 180 
GLN   OE1  O  N N 181 
GLN   NE2  N  N N 182 
GLN   OXT  O  N N 183 
GLN   H    H  N N 184 
GLN   H2   H  N N 185 
GLN   HA   H  N N 186 
GLN   HB2  H  N N 187 
GLN   HB3  H  N N 188 
GLN   HG2  H  N N 189 
GLN   HG3  H  N N 190 
GLN   HE21 H  N N 191 
GLN   HE22 H  N N 192 
GLN   HXT  H  N N 193 
GLU   N    N  N N 194 
GLU   CA   C  N S 195 
GLU   C    C  N N 196 
GLU   O    O  N N 197 
GLU   CB   C  N N 198 
GLU   CG   C  N N 199 
GLU   CD   C  N N 200 
GLU   OE1  O  N N 201 
GLU   OE2  O  N N 202 
GLU   OXT  O  N N 203 
GLU   H    H  N N 204 
GLU   H2   H  N N 205 
GLU   HA   H  N N 206 
GLU   HB2  H  N N 207 
GLU   HB3  H  N N 208 
GLU   HG2  H  N N 209 
GLU   HG3  H  N N 210 
GLU   HE2  H  N N 211 
GLU   HXT  H  N N 212 
GLY   N    N  N N 213 
GLY   CA   C  N N 214 
GLY   C    C  N N 215 
GLY   O    O  N N 216 
GLY   OXT  O  N N 217 
GLY   H    H  N N 218 
GLY   H2   H  N N 219 
GLY   HA2  H  N N 220 
GLY   HA3  H  N N 221 
GLY   HXT  H  N N 222 
HEM   CHA  C  N N 223 
HEM   CHB  C  N N 224 
HEM   CHC  C  N N 225 
HEM   CHD  C  N N 226 
HEM   C1A  C  Y N 227 
HEM   C2A  C  Y N 228 
HEM   C3A  C  Y N 229 
HEM   C4A  C  Y N 230 
HEM   CMA  C  N N 231 
HEM   CAA  C  N N 232 
HEM   CBA  C  N N 233 
HEM   CGA  C  N N 234 
HEM   O1A  O  N N 235 
HEM   O2A  O  N N 236 
HEM   C1B  C  N N 237 
HEM   C2B  C  N N 238 
HEM   C3B  C  N N 239 
HEM   C4B  C  N N 240 
HEM   CMB  C  N N 241 
HEM   CAB  C  N N 242 
HEM   CBB  C  N N 243 
HEM   C1C  C  Y N 244 
HEM   C2C  C  Y N 245 
HEM   C3C  C  Y N 246 
HEM   C4C  C  Y N 247 
HEM   CMC  C  N N 248 
HEM   CAC  C  N N 249 
HEM   CBC  C  N N 250 
HEM   C1D  C  N N 251 
HEM   C2D  C  N N 252 
HEM   C3D  C  N N 253 
HEM   C4D  C  N N 254 
HEM   CMD  C  N N 255 
HEM   CAD  C  N N 256 
HEM   CBD  C  N N 257 
HEM   CGD  C  N N 258 
HEM   O1D  O  N N 259 
HEM   O2D  O  N N 260 
HEM   NA   N  Y N 261 
HEM   NB   N  N N 262 
HEM   NC   N  Y N 263 
HEM   ND   N  N N 264 
HEM   FE   FE N N 265 
HEM   HHB  H  N N 266 
HEM   HHC  H  N N 267 
HEM   HHD  H  N N 268 
HEM   HMA  H  N N 269 
HEM   HMAA H  N N 270 
HEM   HMAB H  N N 271 
HEM   HAA  H  N N 272 
HEM   HAAA H  N N 273 
HEM   HBA  H  N N 274 
HEM   HBAA H  N N 275 
HEM   HMB  H  N N 276 
HEM   HMBA H  N N 277 
HEM   HMBB H  N N 278 
HEM   HAB  H  N N 279 
HEM   HBB  H  N N 280 
HEM   HBBA H  N N 281 
HEM   HMC  H  N N 282 
HEM   HMCA H  N N 283 
HEM   HMCB H  N N 284 
HEM   HAC  H  N N 285 
HEM   HBC  H  N N 286 
HEM   HBCA H  N N 287 
HEM   HMD  H  N N 288 
HEM   HMDA H  N N 289 
HEM   HMDB H  N N 290 
HEM   HAD  H  N N 291 
HEM   HADA H  N N 292 
HEM   HBD  H  N N 293 
HEM   HBDA H  N N 294 
HEM   H2A  H  N N 295 
HEM   H2D  H  N N 296 
HEM   HHA  H  N N 297 
HIS   N    N  N N 298 
HIS   CA   C  N S 299 
HIS   C    C  N N 300 
HIS   O    O  N N 301 
HIS   CB   C  N N 302 
HIS   CG   C  Y N 303 
HIS   ND1  N  Y N 304 
HIS   CD2  C  Y N 305 
HIS   CE1  C  Y N 306 
HIS   NE2  N  Y N 307 
HIS   OXT  O  N N 308 
HIS   H    H  N N 309 
HIS   H2   H  N N 310 
HIS   HA   H  N N 311 
HIS   HB2  H  N N 312 
HIS   HB3  H  N N 313 
HIS   HD1  H  N N 314 
HIS   HD2  H  N N 315 
HIS   HE1  H  N N 316 
HIS   HE2  H  N N 317 
HIS   HXT  H  N N 318 
HOH   O    O  N N 319 
HOH   H1   H  N N 320 
HOH   H2   H  N N 321 
ILE   N    N  N N 322 
ILE   CA   C  N S 323 
ILE   C    C  N N 324 
ILE   O    O  N N 325 
ILE   CB   C  N S 326 
ILE   CG1  C  N N 327 
ILE   CG2  C  N N 328 
ILE   CD1  C  N N 329 
ILE   OXT  O  N N 330 
ILE   H    H  N N 331 
ILE   H2   H  N N 332 
ILE   HA   H  N N 333 
ILE   HB   H  N N 334 
ILE   HG12 H  N N 335 
ILE   HG13 H  N N 336 
ILE   HG21 H  N N 337 
ILE   HG22 H  N N 338 
ILE   HG23 H  N N 339 
ILE   HD11 H  N N 340 
ILE   HD12 H  N N 341 
ILE   HD13 H  N N 342 
ILE   HXT  H  N N 343 
LEU   N    N  N N 344 
LEU   CA   C  N S 345 
LEU   C    C  N N 346 
LEU   O    O  N N 347 
LEU   CB   C  N N 348 
LEU   CG   C  N N 349 
LEU   CD1  C  N N 350 
LEU   CD2  C  N N 351 
LEU   OXT  O  N N 352 
LEU   H    H  N N 353 
LEU   H2   H  N N 354 
LEU   HA   H  N N 355 
LEU   HB2  H  N N 356 
LEU   HB3  H  N N 357 
LEU   HG   H  N N 358 
LEU   HD11 H  N N 359 
LEU   HD12 H  N N 360 
LEU   HD13 H  N N 361 
LEU   HD21 H  N N 362 
LEU   HD22 H  N N 363 
LEU   HD23 H  N N 364 
LEU   HXT  H  N N 365 
LYS   N    N  N N 366 
LYS   CA   C  N S 367 
LYS   C    C  N N 368 
LYS   O    O  N N 369 
LYS   CB   C  N N 370 
LYS   CG   C  N N 371 
LYS   CD   C  N N 372 
LYS   CE   C  N N 373 
LYS   NZ   N  N N 374 
LYS   OXT  O  N N 375 
LYS   H    H  N N 376 
LYS   H2   H  N N 377 
LYS   HA   H  N N 378 
LYS   HB2  H  N N 379 
LYS   HB3  H  N N 380 
LYS   HG2  H  N N 381 
LYS   HG3  H  N N 382 
LYS   HD2  H  N N 383 
LYS   HD3  H  N N 384 
LYS   HE2  H  N N 385 
LYS   HE3  H  N N 386 
LYS   HZ1  H  N N 387 
LYS   HZ2  H  N N 388 
LYS   HZ3  H  N N 389 
LYS   HXT  H  N N 390 
MET   N    N  N N 391 
MET   CA   C  N S 392 
MET   C    C  N N 393 
MET   O    O  N N 394 
MET   CB   C  N N 395 
MET   CG   C  N N 396 
MET   SD   S  N N 397 
MET   CE   C  N N 398 
MET   OXT  O  N N 399 
MET   H    H  N N 400 
MET   H2   H  N N 401 
MET   HA   H  N N 402 
MET   HB2  H  N N 403 
MET   HB3  H  N N 404 
MET   HG2  H  N N 405 
MET   HG3  H  N N 406 
MET   HE1  H  N N 407 
MET   HE2  H  N N 408 
MET   HE3  H  N N 409 
MET   HXT  H  N N 410 
PHE   N    N  N N 411 
PHE   CA   C  N S 412 
PHE   C    C  N N 413 
PHE   O    O  N N 414 
PHE   CB   C  N N 415 
PHE   CG   C  Y N 416 
PHE   CD1  C  Y N 417 
PHE   CD2  C  Y N 418 
PHE   CE1  C  Y N 419 
PHE   CE2  C  Y N 420 
PHE   CZ   C  Y N 421 
PHE   OXT  O  N N 422 
PHE   H    H  N N 423 
PHE   H2   H  N N 424 
PHE   HA   H  N N 425 
PHE   HB2  H  N N 426 
PHE   HB3  H  N N 427 
PHE   HD1  H  N N 428 
PHE   HD2  H  N N 429 
PHE   HE1  H  N N 430 
PHE   HE2  H  N N 431 
PHE   HZ   H  N N 432 
PHE   HXT  H  N N 433 
PRO   N    N  N N 434 
PRO   CA   C  N S 435 
PRO   C    C  N N 436 
PRO   O    O  N N 437 
PRO   CB   C  N N 438 
PRO   CG   C  N N 439 
PRO   CD   C  N N 440 
PRO   OXT  O  N N 441 
PRO   H    H  N N 442 
PRO   HA   H  N N 443 
PRO   HB2  H  N N 444 
PRO   HB3  H  N N 445 
PRO   HG2  H  N N 446 
PRO   HG3  H  N N 447 
PRO   HD2  H  N N 448 
PRO   HD3  H  N N 449 
PRO   HXT  H  N N 450 
SER   N    N  N N 451 
SER   CA   C  N S 452 
SER   C    C  N N 453 
SER   O    O  N N 454 
SER   CB   C  N N 455 
SER   OG   O  N N 456 
SER   OXT  O  N N 457 
SER   H    H  N N 458 
SER   H2   H  N N 459 
SER   HA   H  N N 460 
SER   HB2  H  N N 461 
SER   HB3  H  N N 462 
SER   HG   H  N N 463 
SER   HXT  H  N N 464 
THR   N    N  N N 465 
THR   CA   C  N S 466 
THR   C    C  N N 467 
THR   O    O  N N 468 
THR   CB   C  N R 469 
THR   OG1  O  N N 470 
THR   CG2  C  N N 471 
THR   OXT  O  N N 472 
THR   H    H  N N 473 
THR   H2   H  N N 474 
THR   HA   H  N N 475 
THR   HB   H  N N 476 
THR   HG1  H  N N 477 
THR   HG21 H  N N 478 
THR   HG22 H  N N 479 
THR   HG23 H  N N 480 
THR   HXT  H  N N 481 
TRP   N    N  N N 482 
TRP   CA   C  N S 483 
TRP   C    C  N N 484 
TRP   O    O  N N 485 
TRP   CB   C  N N 486 
TRP   CG   C  Y N 487 
TRP   CD1  C  Y N 488 
TRP   CD2  C  Y N 489 
TRP   NE1  N  Y N 490 
TRP   CE2  C  Y N 491 
TRP   CE3  C  Y N 492 
TRP   CZ2  C  Y N 493 
TRP   CZ3  C  Y N 494 
TRP   CH2  C  Y N 495 
TRP   OXT  O  N N 496 
TRP   H    H  N N 497 
TRP   H2   H  N N 498 
TRP   HA   H  N N 499 
TRP   HB2  H  N N 500 
TRP   HB3  H  N N 501 
TRP   HD1  H  N N 502 
TRP   HE1  H  N N 503 
TRP   HE3  H  N N 504 
TRP   HZ2  H  N N 505 
TRP   HZ3  H  N N 506 
TRP   HH2  H  N N 507 
TRP   HXT  H  N N 508 
TYR   N    N  N N 509 
TYR   CA   C  N S 510 
TYR   C    C  N N 511 
TYR   O    O  N N 512 
TYR   CB   C  N N 513 
TYR   CG   C  Y N 514 
TYR   CD1  C  Y N 515 
TYR   CD2  C  Y N 516 
TYR   CE1  C  Y N 517 
TYR   CE2  C  Y N 518 
TYR   CZ   C  Y N 519 
TYR   OH   O  N N 520 
TYR   OXT  O  N N 521 
TYR   H    H  N N 522 
TYR   H2   H  N N 523 
TYR   HA   H  N N 524 
TYR   HB2  H  N N 525 
TYR   HB3  H  N N 526 
TYR   HD1  H  N N 527 
TYR   HD2  H  N N 528 
TYR   HE1  H  N N 529 
TYR   HE2  H  N N 530 
TYR   HH   H  N N 531 
TYR   HXT  H  N N 532 
VAL   N    N  N N 533 
VAL   CA   C  N S 534 
VAL   C    C  N N 535 
VAL   O    O  N N 536 
VAL   CB   C  N N 537 
VAL   CG1  C  N N 538 
VAL   CG2  C  N N 539 
VAL   OXT  O  N N 540 
VAL   H    H  N N 541 
VAL   H2   H  N N 542 
VAL   HA   H  N N 543 
VAL   HB   H  N N 544 
VAL   HG11 H  N N 545 
VAL   HG12 H  N N 546 
VAL   HG13 H  N N 547 
VAL   HG21 H  N N 548 
VAL   HG22 H  N N 549 
VAL   HG23 H  N N 550 
VAL   HXT  H  N N 551 
# 
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 
A1A4T C41 C42  doub Y N 1   
A1A4T C41 C40  sing Y N 2   
A1A4T C42 C43  sing Y N 3   
A1A4T C40 C39  doub Y N 4   
A1A4T C31 C22  sing N N 5   
A1A4T C43 C38  doub Y N 6   
A1A4T C39 C38  sing Y N 7   
A1A4T C38 C19  sing N N 8   
A1A4T C19 C18  doub Y N 9   
A1A4T C19 C20  sing Y N 10  
A1A4T C28 C27  doub Y N 11  
A1A4T C28 N24  sing Y N 12  
A1A4T C27 C26  sing Y N 13  
A1A4T C18 C17  sing Y N 14  
A1A4T C22 C29  sing N N 15  
A1A4T C22 C30  sing N N 16  
A1A4T C22 C11  sing N N 17  
A1A4T C20 C16  doub Y N 18  
A1A4T C17 C15  doub Y N 19  
A1A4T C16 C15  sing Y N 20  
A1A4T C11 N10  sing N N 21  
A1A4T C11 O21  doub N N 22  
A1A4T C15 C14  sing N N 23  
A1A4T N10 C09  sing N N 24  
A1A4T N24 C25  doub Y N 25  
A1A4T C26 C23  doub Y N 26  
A1A4T C14 C09  sing N N 27  
A1A4T C09 C08  sing N N 28  
A1A4T C25 C23  sing Y N 29  
A1A4T C23 C01  sing N N 30  
A1A4T C08 S07  sing N N 31  
A1A4T N04 C03  sing N N 32  
A1A4T N04 C05  sing N N 33  
A1A4T C01 C02  sing N N 34  
A1A4T C03 C02  sing N N 35  
A1A4T S07 C06  sing N N 36  
A1A4T C06 C05  sing N N 37  
A1A4T C06 C13  sing N N 38  
A1A4T C05 O12  doub N N 39  
A1A4T C34 C35  doub Y N 40  
A1A4T C34 C32  sing Y N 41  
A1A4T C13 C32  sing N N 42  
A1A4T C35 C36  sing Y N 43  
A1A4T C32 C33  doub Y N 44  
A1A4T C36 C37  doub Y N 45  
A1A4T C33 C37  sing Y N 46  
A1A4T C16 H1   sing N N 47  
A1A4T C17 H2   sing N N 48  
A1A4T C18 H3   sing N N 49  
A1A4T C20 H4   sing N N 50  
A1A4T C25 H5   sing N N 51  
A1A4T C26 H6   sing N N 52  
A1A4T C13 H7   sing N N 53  
A1A4T C13 H8   sing N N 54  
A1A4T C14 H9   sing N N 55  
A1A4T C14 H10  sing N N 56  
A1A4T C01 H11  sing N N 57  
A1A4T C01 H12  sing N N 58  
A1A4T C02 H13  sing N N 59  
A1A4T C02 H14  sing N N 60  
A1A4T C03 H15  sing N N 61  
A1A4T C03 H16  sing N N 62  
A1A4T C06 H17  sing N N 63  
A1A4T C08 H18  sing N N 64  
A1A4T C08 H19  sing N N 65  
A1A4T C09 H20  sing N N 66  
A1A4T C27 H21  sing N N 67  
A1A4T C28 H22  sing N N 68  
A1A4T C29 H23  sing N N 69  
A1A4T C29 H24  sing N N 70  
A1A4T C29 H25  sing N N 71  
A1A4T C30 H26  sing N N 72  
A1A4T C30 H27  sing N N 73  
A1A4T C30 H28  sing N N 74  
A1A4T C31 H29  sing N N 75  
A1A4T C31 H30  sing N N 76  
A1A4T C31 H31  sing N N 77  
A1A4T C33 H32  sing N N 78  
A1A4T C34 H33  sing N N 79  
A1A4T C35 H34  sing N N 80  
A1A4T C36 H35  sing N N 81  
A1A4T C37 H36  sing N N 82  
A1A4T C39 H37  sing N N 83  
A1A4T C40 H38  sing N N 84  
A1A4T C41 H39  sing N N 85  
A1A4T C42 H40  sing N N 86  
A1A4T C43 H41  sing N N 87  
A1A4T N04 H42  sing N N 88  
A1A4T N10 H43  sing N N 89  
ALA   N   CA   sing N N 90  
ALA   N   H    sing N N 91  
ALA   N   H2   sing N N 92  
ALA   CA  C    sing N N 93  
ALA   CA  CB   sing N N 94  
ALA   CA  HA   sing N N 95  
ALA   C   O    doub N N 96  
ALA   C   OXT  sing N N 97  
ALA   CB  HB1  sing N N 98  
ALA   CB  HB2  sing N N 99  
ALA   CB  HB3  sing N N 100 
ALA   OXT HXT  sing N N 101 
ARG   N   CA   sing N N 102 
ARG   N   H    sing N N 103 
ARG   N   H2   sing N N 104 
ARG   CA  C    sing N N 105 
ARG   CA  CB   sing N N 106 
ARG   CA  HA   sing N N 107 
ARG   C   O    doub N N 108 
ARG   C   OXT  sing N N 109 
ARG   CB  CG   sing N N 110 
ARG   CB  HB2  sing N N 111 
ARG   CB  HB3  sing N N 112 
ARG   CG  CD   sing N N 113 
ARG   CG  HG2  sing N N 114 
ARG   CG  HG3  sing N N 115 
ARG   CD  NE   sing N N 116 
ARG   CD  HD2  sing N N 117 
ARG   CD  HD3  sing N N 118 
ARG   NE  CZ   sing N N 119 
ARG   NE  HE   sing N N 120 
ARG   CZ  NH1  sing N N 121 
ARG   CZ  NH2  doub N N 122 
ARG   NH1 HH11 sing N N 123 
ARG   NH1 HH12 sing N N 124 
ARG   NH2 HH21 sing N N 125 
ARG   NH2 HH22 sing N N 126 
ARG   OXT HXT  sing N N 127 
ASN   N   CA   sing N N 128 
ASN   N   H    sing N N 129 
ASN   N   H2   sing N N 130 
ASN   CA  C    sing N N 131 
ASN   CA  CB   sing N N 132 
ASN   CA  HA   sing N N 133 
ASN   C   O    doub N N 134 
ASN   C   OXT  sing N N 135 
ASN   CB  CG   sing N N 136 
ASN   CB  HB2  sing N N 137 
ASN   CB  HB3  sing N N 138 
ASN   CG  OD1  doub N N 139 
ASN   CG  ND2  sing N N 140 
ASN   ND2 HD21 sing N N 141 
ASN   ND2 HD22 sing N N 142 
ASN   OXT HXT  sing N N 143 
ASP   N   CA   sing N N 144 
ASP   N   H    sing N N 145 
ASP   N   H2   sing N N 146 
ASP   CA  C    sing N N 147 
ASP   CA  CB   sing N N 148 
ASP   CA  HA   sing N N 149 
ASP   C   O    doub N N 150 
ASP   C   OXT  sing N N 151 
ASP   CB  CG   sing N N 152 
ASP   CB  HB2  sing N N 153 
ASP   CB  HB3  sing N N 154 
ASP   CG  OD1  doub N N 155 
ASP   CG  OD2  sing N N 156 
ASP   OD2 HD2  sing N N 157 
ASP   OXT HXT  sing N N 158 
CYS   N   CA   sing N N 159 
CYS   N   H    sing N N 160 
CYS   N   H2   sing N N 161 
CYS   CA  C    sing N N 162 
CYS   CA  CB   sing N N 163 
CYS   CA  HA   sing N N 164 
CYS   C   O    doub N N 165 
CYS   C   OXT  sing N N 166 
CYS   CB  SG   sing N N 167 
CYS   CB  HB2  sing N N 168 
CYS   CB  HB3  sing N N 169 
CYS   SG  HG   sing N N 170 
CYS   OXT HXT  sing N N 171 
GLN   N   CA   sing N N 172 
GLN   N   H    sing N N 173 
GLN   N   H2   sing N N 174 
GLN   CA  C    sing N N 175 
GLN   CA  CB   sing N N 176 
GLN   CA  HA   sing N N 177 
GLN   C   O    doub N N 178 
GLN   C   OXT  sing N N 179 
GLN   CB  CG   sing N N 180 
GLN   CB  HB2  sing N N 181 
GLN   CB  HB3  sing N N 182 
GLN   CG  CD   sing N N 183 
GLN   CG  HG2  sing N N 184 
GLN   CG  HG3  sing N N 185 
GLN   CD  OE1  doub N N 186 
GLN   CD  NE2  sing N N 187 
GLN   NE2 HE21 sing N N 188 
GLN   NE2 HE22 sing N N 189 
GLN   OXT HXT  sing N N 190 
GLU   N   CA   sing N N 191 
GLU   N   H    sing N N 192 
GLU   N   H2   sing N N 193 
GLU   CA  C    sing N N 194 
GLU   CA  CB   sing N N 195 
GLU   CA  HA   sing N N 196 
GLU   C   O    doub N N 197 
GLU   C   OXT  sing N N 198 
GLU   CB  CG   sing N N 199 
GLU   CB  HB2  sing N N 200 
GLU   CB  HB3  sing N N 201 
GLU   CG  CD   sing N N 202 
GLU   CG  HG2  sing N N 203 
GLU   CG  HG3  sing N N 204 
GLU   CD  OE1  doub N N 205 
GLU   CD  OE2  sing N N 206 
GLU   OE2 HE2  sing N N 207 
GLU   OXT HXT  sing N N 208 
GLY   N   CA   sing N N 209 
GLY   N   H    sing N N 210 
GLY   N   H2   sing N N 211 
GLY   CA  C    sing N N 212 
GLY   CA  HA2  sing N N 213 
GLY   CA  HA3  sing N N 214 
GLY   C   O    doub N N 215 
GLY   C   OXT  sing N N 216 
GLY   OXT HXT  sing N N 217 
HEM   CHA C1A  sing N N 218 
HEM   CHA C4D  doub N N 219 
HEM   CHA HHA  sing N N 220 
HEM   CHB C4A  sing N N 221 
HEM   CHB C1B  doub N N 222 
HEM   CHB HHB  sing N N 223 
HEM   CHC C4B  sing N N 224 
HEM   CHC C1C  doub N N 225 
HEM   CHC HHC  sing N N 226 
HEM   CHD C4C  doub N N 227 
HEM   CHD C1D  sing N N 228 
HEM   CHD HHD  sing N N 229 
HEM   C1A C2A  doub Y N 230 
HEM   C1A NA   sing Y N 231 
HEM   C2A C3A  sing Y N 232 
HEM   C2A CAA  sing N N 233 
HEM   C3A C4A  doub Y N 234 
HEM   C3A CMA  sing N N 235 
HEM   C4A NA   sing Y N 236 
HEM   CMA HMA  sing N N 237 
HEM   CMA HMAA sing N N 238 
HEM   CMA HMAB sing N N 239 
HEM   CAA CBA  sing N N 240 
HEM   CAA HAA  sing N N 241 
HEM   CAA HAAA sing N N 242 
HEM   CBA CGA  sing N N 243 
HEM   CBA HBA  sing N N 244 
HEM   CBA HBAA sing N N 245 
HEM   CGA O1A  doub N N 246 
HEM   CGA O2A  sing N N 247 
HEM   C1B C2B  sing N N 248 
HEM   C1B NB   sing N N 249 
HEM   C2B C3B  doub N N 250 
HEM   C2B CMB  sing N N 251 
HEM   C3B C4B  sing N N 252 
HEM   C3B CAB  sing N N 253 
HEM   C4B NB   doub N N 254 
HEM   CMB HMB  sing N N 255 
HEM   CMB HMBA sing N N 256 
HEM   CMB HMBB sing N N 257 
HEM   CAB CBB  doub N N 258 
HEM   CAB HAB  sing N N 259 
HEM   CBB HBB  sing N N 260 
HEM   CBB HBBA sing N N 261 
HEM   C1C C2C  sing Y N 262 
HEM   C1C NC   sing Y N 263 
HEM   C2C C3C  doub Y N 264 
HEM   C2C CMC  sing N N 265 
HEM   C3C C4C  sing Y N 266 
HEM   C3C CAC  sing N N 267 
HEM   C4C NC   sing Y N 268 
HEM   CMC HMC  sing N N 269 
HEM   CMC HMCA sing N N 270 
HEM   CMC HMCB sing N N 271 
HEM   CAC CBC  doub N N 272 
HEM   CAC HAC  sing N N 273 
HEM   CBC HBC  sing N N 274 
HEM   CBC HBCA sing N N 275 
HEM   C1D C2D  sing N N 276 
HEM   C1D ND   doub N N 277 
HEM   C2D C3D  doub N N 278 
HEM   C2D CMD  sing N N 279 
HEM   C3D C4D  sing N N 280 
HEM   C3D CAD  sing N N 281 
HEM   C4D ND   sing N N 282 
HEM   CMD HMD  sing N N 283 
HEM   CMD HMDA sing N N 284 
HEM   CMD HMDB sing N N 285 
HEM   CAD CBD  sing N N 286 
HEM   CAD HAD  sing N N 287 
HEM   CAD HADA sing N N 288 
HEM   CBD CGD  sing N N 289 
HEM   CBD HBD  sing N N 290 
HEM   CBD HBDA sing N N 291 
HEM   CGD O1D  doub N N 292 
HEM   CGD O2D  sing N N 293 
HEM   O2A H2A  sing N N 294 
HEM   O2D H2D  sing N N 295 
HEM   FE  NA   sing N N 296 
HEM   FE  NB   sing N N 297 
HEM   FE  NC   sing N N 298 
HEM   FE  ND   sing N N 299 
HIS   N   CA   sing N N 300 
HIS   N   H    sing N N 301 
HIS   N   H2   sing N N 302 
HIS   CA  C    sing N N 303 
HIS   CA  CB   sing N N 304 
HIS   CA  HA   sing N N 305 
HIS   C   O    doub N N 306 
HIS   C   OXT  sing N N 307 
HIS   CB  CG   sing N N 308 
HIS   CB  HB2  sing N N 309 
HIS   CB  HB3  sing N N 310 
HIS   CG  ND1  sing Y N 311 
HIS   CG  CD2  doub Y N 312 
HIS   ND1 CE1  doub Y N 313 
HIS   ND1 HD1  sing N N 314 
HIS   CD2 NE2  sing Y N 315 
HIS   CD2 HD2  sing N N 316 
HIS   CE1 NE2  sing Y N 317 
HIS   CE1 HE1  sing N N 318 
HIS   NE2 HE2  sing N N 319 
HIS   OXT HXT  sing N N 320 
HOH   O   H1   sing N N 321 
HOH   O   H2   sing N N 322 
ILE   N   CA   sing N N 323 
ILE   N   H    sing N N 324 
ILE   N   H2   sing N N 325 
ILE   CA  C    sing N N 326 
ILE   CA  CB   sing N N 327 
ILE   CA  HA   sing N N 328 
ILE   C   O    doub N N 329 
ILE   C   OXT  sing N N 330 
ILE   CB  CG1  sing N N 331 
ILE   CB  CG2  sing N N 332 
ILE   CB  HB   sing N N 333 
ILE   CG1 CD1  sing N N 334 
ILE   CG1 HG12 sing N N 335 
ILE   CG1 HG13 sing N N 336 
ILE   CG2 HG21 sing N N 337 
ILE   CG2 HG22 sing N N 338 
ILE   CG2 HG23 sing N N 339 
ILE   CD1 HD11 sing N N 340 
ILE   CD1 HD12 sing N N 341 
ILE   CD1 HD13 sing N N 342 
ILE   OXT HXT  sing N N 343 
LEU   N   CA   sing N N 344 
LEU   N   H    sing N N 345 
LEU   N   H2   sing N N 346 
LEU   CA  C    sing N N 347 
LEU   CA  CB   sing N N 348 
LEU   CA  HA   sing N N 349 
LEU   C   O    doub N N 350 
LEU   C   OXT  sing N N 351 
LEU   CB  CG   sing N N 352 
LEU   CB  HB2  sing N N 353 
LEU   CB  HB3  sing N N 354 
LEU   CG  CD1  sing N N 355 
LEU   CG  CD2  sing N N 356 
LEU   CG  HG   sing N N 357 
LEU   CD1 HD11 sing N N 358 
LEU   CD1 HD12 sing N N 359 
LEU   CD1 HD13 sing N N 360 
LEU   CD2 HD21 sing N N 361 
LEU   CD2 HD22 sing N N 362 
LEU   CD2 HD23 sing N N 363 
LEU   OXT HXT  sing N N 364 
LYS   N   CA   sing N N 365 
LYS   N   H    sing N N 366 
LYS   N   H2   sing N N 367 
LYS   CA  C    sing N N 368 
LYS   CA  CB   sing N N 369 
LYS   CA  HA   sing N N 370 
LYS   C   O    doub N N 371 
LYS   C   OXT  sing N N 372 
LYS   CB  CG   sing N N 373 
LYS   CB  HB2  sing N N 374 
LYS   CB  HB3  sing N N 375 
LYS   CG  CD   sing N N 376 
LYS   CG  HG2  sing N N 377 
LYS   CG  HG3  sing N N 378 
LYS   CD  CE   sing N N 379 
LYS   CD  HD2  sing N N 380 
LYS   CD  HD3  sing N N 381 
LYS   CE  NZ   sing N N 382 
LYS   CE  HE2  sing N N 383 
LYS   CE  HE3  sing N N 384 
LYS   NZ  HZ1  sing N N 385 
LYS   NZ  HZ2  sing N N 386 
LYS   NZ  HZ3  sing N N 387 
LYS   OXT HXT  sing N N 388 
MET   N   CA   sing N N 389 
MET   N   H    sing N N 390 
MET   N   H2   sing N N 391 
MET   CA  C    sing N N 392 
MET   CA  CB   sing N N 393 
MET   CA  HA   sing N N 394 
MET   C   O    doub N N 395 
MET   C   OXT  sing N N 396 
MET   CB  CG   sing N N 397 
MET   CB  HB2  sing N N 398 
MET   CB  HB3  sing N N 399 
MET   CG  SD   sing N N 400 
MET   CG  HG2  sing N N 401 
MET   CG  HG3  sing N N 402 
MET   SD  CE   sing N N 403 
MET   CE  HE1  sing N N 404 
MET   CE  HE2  sing N N 405 
MET   CE  HE3  sing N N 406 
MET   OXT HXT  sing N N 407 
PHE   N   CA   sing N N 408 
PHE   N   H    sing N N 409 
PHE   N   H2   sing N N 410 
PHE   CA  C    sing N N 411 
PHE   CA  CB   sing N N 412 
PHE   CA  HA   sing N N 413 
PHE   C   O    doub N N 414 
PHE   C   OXT  sing N N 415 
PHE   CB  CG   sing N N 416 
PHE   CB  HB2  sing N N 417 
PHE   CB  HB3  sing N N 418 
PHE   CG  CD1  doub Y N 419 
PHE   CG  CD2  sing Y N 420 
PHE   CD1 CE1  sing Y N 421 
PHE   CD1 HD1  sing N N 422 
PHE   CD2 CE2  doub Y N 423 
PHE   CD2 HD2  sing N N 424 
PHE   CE1 CZ   doub Y N 425 
PHE   CE1 HE1  sing N N 426 
PHE   CE2 CZ   sing Y N 427 
PHE   CE2 HE2  sing N N 428 
PHE   CZ  HZ   sing N N 429 
PHE   OXT HXT  sing N N 430 
PRO   N   CA   sing N N 431 
PRO   N   CD   sing N N 432 
PRO   N   H    sing N N 433 
PRO   CA  C    sing N N 434 
PRO   CA  CB   sing N N 435 
PRO   CA  HA   sing N N 436 
PRO   C   O    doub N N 437 
PRO   C   OXT  sing N N 438 
PRO   CB  CG   sing N N 439 
PRO   CB  HB2  sing N N 440 
PRO   CB  HB3  sing N N 441 
PRO   CG  CD   sing N N 442 
PRO   CG  HG2  sing N N 443 
PRO   CG  HG3  sing N N 444 
PRO   CD  HD2  sing N N 445 
PRO   CD  HD3  sing N N 446 
PRO   OXT HXT  sing N N 447 
SER   N   CA   sing N N 448 
SER   N   H    sing N N 449 
SER   N   H2   sing N N 450 
SER   CA  C    sing N N 451 
SER   CA  CB   sing N N 452 
SER   CA  HA   sing N N 453 
SER   C   O    doub N N 454 
SER   C   OXT  sing N N 455 
SER   CB  OG   sing N N 456 
SER   CB  HB2  sing N N 457 
SER   CB  HB3  sing N N 458 
SER   OG  HG   sing N N 459 
SER   OXT HXT  sing N N 460 
THR   N   CA   sing N N 461 
THR   N   H    sing N N 462 
THR   N   H2   sing N N 463 
THR   CA  C    sing N N 464 
THR   CA  CB   sing N N 465 
THR   CA  HA   sing N N 466 
THR   C   O    doub N N 467 
THR   C   OXT  sing N N 468 
THR   CB  OG1  sing N N 469 
THR   CB  CG2  sing N N 470 
THR   CB  HB   sing N N 471 
THR   OG1 HG1  sing N N 472 
THR   CG2 HG21 sing N N 473 
THR   CG2 HG22 sing N N 474 
THR   CG2 HG23 sing N N 475 
THR   OXT HXT  sing N N 476 
TRP   N   CA   sing N N 477 
TRP   N   H    sing N N 478 
TRP   N   H2   sing N N 479 
TRP   CA  C    sing N N 480 
TRP   CA  CB   sing N N 481 
TRP   CA  HA   sing N N 482 
TRP   C   O    doub N N 483 
TRP   C   OXT  sing N N 484 
TRP   CB  CG   sing N N 485 
TRP   CB  HB2  sing N N 486 
TRP   CB  HB3  sing N N 487 
TRP   CG  CD1  doub Y N 488 
TRP   CG  CD2  sing Y N 489 
TRP   CD1 NE1  sing Y N 490 
TRP   CD1 HD1  sing N N 491 
TRP   CD2 CE2  doub Y N 492 
TRP   CD2 CE3  sing Y N 493 
TRP   NE1 CE2  sing Y N 494 
TRP   NE1 HE1  sing N N 495 
TRP   CE2 CZ2  sing Y N 496 
TRP   CE3 CZ3  doub Y N 497 
TRP   CE3 HE3  sing N N 498 
TRP   CZ2 CH2  doub Y N 499 
TRP   CZ2 HZ2  sing N N 500 
TRP   CZ3 CH2  sing Y N 501 
TRP   CZ3 HZ3  sing N N 502 
TRP   CH2 HH2  sing N N 503 
TRP   OXT HXT  sing N N 504 
TYR   N   CA   sing N N 505 
TYR   N   H    sing N N 506 
TYR   N   H2   sing N N 507 
TYR   CA  C    sing N N 508 
TYR   CA  CB   sing N N 509 
TYR   CA  HA   sing N N 510 
TYR   C   O    doub N N 511 
TYR   C   OXT  sing N N 512 
TYR   CB  CG   sing N N 513 
TYR   CB  HB2  sing N N 514 
TYR   CB  HB3  sing N N 515 
TYR   CG  CD1  doub Y N 516 
TYR   CG  CD2  sing Y N 517 
TYR   CD1 CE1  sing Y N 518 
TYR   CD1 HD1  sing N N 519 
TYR   CD2 CE2  doub Y N 520 
TYR   CD2 HD2  sing N N 521 
TYR   CE1 CZ   doub Y N 522 
TYR   CE1 HE1  sing N N 523 
TYR   CE2 CZ   sing Y N 524 
TYR   CE2 HE2  sing N N 525 
TYR   CZ  OH   sing N N 526 
TYR   OH  HH   sing N N 527 
TYR   OXT HXT  sing N N 528 
VAL   N   CA   sing N N 529 
VAL   N   H    sing N N 530 
VAL   N   H2   sing N N 531 
VAL   CA  C    sing N N 532 
VAL   CA  CB   sing N N 533 
VAL   CA  HA   sing N N 534 
VAL   C   O    doub N N 535 
VAL   C   OXT  sing N N 536 
VAL   CB  CG1  sing N N 537 
VAL   CB  CG2  sing N N 538 
VAL   CB  HB   sing N N 539 
VAL   CG1 HG11 sing N N 540 
VAL   CG1 HG12 sing N N 541 
VAL   CG1 HG13 sing N N 542 
VAL   CG2 HG21 sing N N 543 
VAL   CG2 HG22 sing N N 544 
VAL   CG2 HG23 sing N N 545 
VAL   OXT HXT  sing N N 546 
# 
_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                    9COY 
_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]   0.012839 
_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]   0.009931 
_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]   0.007651 
_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   ? -30.702 8.247   -15.258 1.00 129.83 ? 28  HIS   A N   1 
ATOM   2    C  CA  . HIS   A 1 8   ? -29.399 8.808   -14.918 1.00 143.20 ? 28  HIS   A CA  1 
ATOM   3    C  C   . HIS   A 1 8   ? -28.301 7.752   -15.067 1.00 146.31 ? 28  HIS   A C   1 
ATOM   4    O  O   . HIS   A 1 8   ? -28.583 6.554   -15.043 1.00 146.57 ? 28  HIS   A O   1 
ATOM   5    C  CB  . HIS   A 1 8   ? -29.416 9.374   -13.494 1.00 147.14 ? 28  HIS   A CB  1 
ATOM   6    C  CG  . HIS   A 1 8   ? -28.097 9.922   -13.045 1.00 153.81 ? 28  HIS   A CG  1 
ATOM   7    N  ND1 . HIS   A 1 8   ? -27.509 11.023  -13.633 1.00 153.45 ? 28  HIS   A ND1 1 
ATOM   8    C  CD2 . HIS   A 1 8   ? -27.244 9.512   -12.077 1.00 153.06 ? 28  HIS   A CD2 1 
ATOM   9    C  CE1 . HIS   A 1 8   ? -26.354 11.270  -13.042 1.00 151.76 ? 28  HIS   A CE1 1 
ATOM   10   N  NE2 . HIS   A 1 8   ? -26.170 10.368  -12.094 1.00 147.60 ? 28  HIS   A NE2 1 
ATOM   11   N  N   . SER   A 1 9   ? -27.061 8.221   -15.245 1.00 126.29 ? 29  SER   A N   1 
ATOM   12   C  CA  . SER   A 1 9   ? -25.875 7.394   -15.463 1.00 121.47 ? 29  SER   A CA  1 
ATOM   13   C  C   . SER   A 1 9   ? -25.936 6.675   -16.807 1.00 102.42 ? 29  SER   A C   1 
ATOM   14   O  O   . SER   A 1 9   ? -24.968 6.025   -17.214 1.00 99.80  ? 29  SER   A O   1 
ATOM   15   C  CB  . SER   A 1 9   ? -25.688 6.376   -14.326 1.00 124.21 ? 29  SER   A CB  1 
ATOM   16   O  OG  . SER   A 1 9   ? -26.414 5.186   -14.575 1.00 117.56 ? 29  SER   A OG  1 
ATOM   17   N  N   . HIS   A 1 10  ? -27.062 6.798   -17.511 1.00 107.68 ? 30  HIS   A N   1 
ATOM   18   C  CA  . HIS   A 1 10  ? -27.215 6.176   -18.818 1.00 101.25 ? 30  HIS   A CA  1 
ATOM   19   C  C   . HIS   A 1 10  ? -26.502 6.942   -19.922 1.00 94.92  ? 30  HIS   A C   1 
ATOM   20   O  O   . HIS   A 1 10  ? -26.408 6.435   -21.044 1.00 94.16  ? 30  HIS   A O   1 
ATOM   21   C  CB  . HIS   A 1 10  ? -28.700 6.033   -19.160 1.00 97.71  ? 30  HIS   A CB  1 
ATOM   22   C  CG  . HIS   A 1 10  ? -29.372 4.898   -18.454 1.00 95.45  ? 30  HIS   A CG  1 
ATOM   23   N  ND1 . HIS   A 1 10  ? -30.599 4.407   -18.835 1.00 92.89  ? 30  HIS   A ND1 1 
ATOM   24   C  CD2 . HIS   A 1 10  ? -28.981 4.152   -17.394 1.00 96.50  ? 30  HIS   A CD2 1 
ATOM   25   C  CE1 . HIS   A 1 10  ? -30.938 3.408   -18.039 1.00 95.01  ? 30  HIS   A CE1 1 
ATOM   26   N  NE2 . HIS   A 1 10  ? -29.973 3.233   -17.156 1.00 94.50  ? 30  HIS   A NE2 1 
ATOM   27   N  N   . GLY   A 1 11  ? -26.002 8.137   -19.633 1.00 96.73  ? 31  GLY   A N   1 
ATOM   28   C  CA  . GLY   A 1 11  ? -25.145 8.877   -20.532 1.00 99.82  ? 31  GLY   A CA  1 
ATOM   29   C  C   . GLY   A 1 11  ? -23.675 8.550   -20.392 1.00 100.29 ? 31  GLY   A C   1 
ATOM   30   O  O   . GLY   A 1 11  ? -22.842 9.208   -21.024 1.00 106.62 ? 31  GLY   A O   1 
ATOM   31   N  N   . LEU   A 1 12  ? -23.331 7.543   -19.587 1.00 99.12  ? 32  LEU   A N   1 
ATOM   32   C  CA  . LEU   A 1 12  ? -21.943 7.195   -19.318 1.00 95.69  ? 32  LEU   A CA  1 
ATOM   33   C  C   . LEU   A 1 12  ? -21.201 6.851   -20.599 1.00 98.95  ? 32  LEU   A C   1 
ATOM   34   O  O   . LEU   A 1 12  ? -20.292 7.581   -21.009 1.00 103.58 ? 32  LEU   A O   1 
ATOM   35   C  CB  . LEU   A 1 12  ? -21.864 6.012   -18.348 1.00 93.15  ? 32  LEU   A CB  1 
ATOM   36   C  CG  . LEU   A 1 12  ? -20.501 5.816   -17.681 1.00 96.42  ? 32  LEU   A CG  1 
ATOM   37   C  CD1 . LEU   A 1 12  ? -20.381 6.682   -16.428 1.00 107.64 ? 32  LEU   A CD1 1 
ATOM   38   C  CD2 . LEU   A 1 12  ? -20.238 4.349   -17.362 1.00 91.59  ? 32  LEU   A CD2 1 
ATOM   39   N  N   . PHE   A 1 13  ? -21.587 5.746   -21.242 1.00 96.12  ? 33  PHE   A N   1 
ATOM   40   C  CA  . PHE   A 1 13  ? -20.883 5.307   -22.441 1.00 98.36  ? 33  PHE   A CA  1 
ATOM   41   C  C   . PHE   A 1 13  ? -21.024 6.293   -23.593 1.00 102.83 ? 33  PHE   A C   1 
ATOM   42   O  O   . PHE   A 1 13  ? -20.174 6.298   -24.491 1.00 103.26 ? 33  PHE   A O   1 
ATOM   43   C  CB  . PHE   A 1 13  ? -21.379 3.924   -22.864 1.00 91.74  ? 33  PHE   A CB  1 
ATOM   44   C  CG  . PHE   A 1 13  ? -21.150 2.860   -21.831 1.00 88.66  ? 33  PHE   A CG  1 
ATOM   45   C  CD1 . PHE   A 1 13  ? -19.872 2.585   -21.372 1.00 88.40  ? 33  PHE   A CD1 1 
ATOM   46   C  CD2 . PHE   A 1 13  ? -22.209 2.132   -21.320 1.00 83.16  ? 33  PHE   A CD2 1 
ATOM   47   C  CE1 . PHE   A 1 13  ? -19.657 1.610   -20.421 1.00 86.56  ? 33  PHE   A CE1 1 
ATOM   48   C  CE2 . PHE   A 1 13  ? -22.001 1.152   -20.368 1.00 82.49  ? 33  PHE   A CE2 1 
ATOM   49   C  CZ  . PHE   A 1 13  ? -20.722 0.890   -19.918 1.00 81.49  ? 33  PHE   A CZ  1 
ATOM   50   N  N   . LYS   A 1 14  ? -22.067 7.128   -23.591 1.00 102.78 ? 34  LYS   A N   1 
ATOM   51   C  CA  . LYS   A 1 14  ? -22.176 8.166   -24.609 1.00 104.22 ? 34  LYS   A CA  1 
ATOM   52   C  C   . LYS   A 1 14  ? -21.186 9.300   -24.376 1.00 110.99 ? 34  LYS   A C   1 
ATOM   53   O  O   . LYS   A 1 14  ? -20.833 10.006  -25.329 1.00 116.08 ? 34  LYS   A O   1 
ATOM   54   C  CB  . LYS   A 1 14  ? -23.605 8.716   -24.665 1.00 109.73 ? 34  LYS   A CB  1 
ATOM   55   C  CG  . LYS   A 1 14  ? -24.651 7.678   -25.049 1.00 116.16 ? 34  LYS   A CG  1 
ATOM   56   C  CD  . LYS   A 1 14  ? -25.833 8.296   -25.791 1.00 122.31 ? 34  LYS   A CD  1 
ATOM   57   C  CE  . LYS   A 1 14  ? -26.636 9.252   -24.918 1.00 120.68 ? 34  LYS   A CE  1 
ATOM   58   N  NZ  . LYS   A 1 14  ? -27.898 9.676   -25.596 1.00 116.24 ? 34  LYS   A NZ  1 
ATOM   59   N  N   . LYS   A 1 15  ? -20.731 9.488   -23.136 1.00 108.36 ? 35  LYS   A N   1 
ATOM   60   C  CA  . LYS   A 1 15  ? -19.717 10.486  -22.810 1.00 112.75 ? 35  LYS   A CA  1 
ATOM   61   C  C   . LYS   A 1 15  ? -18.298 9.999   -23.075 1.00 113.51 ? 35  LYS   A C   1 
ATOM   62   O  O   . LYS   A 1 15  ? -17.421 10.814  -23.384 1.00 118.82 ? 35  LYS   A O   1 
ATOM   63   C  CB  . LYS   A 1 15  ? -19.843 10.889  -21.334 1.00 116.07 ? 35  LYS   A CB  1 
ATOM   64   C  CG  . LYS   A 1 15  ? -18.886 11.986  -20.877 1.00 118.12 ? 35  LYS   A CG  1 
ATOM   65   C  CD  . LYS   A 1 15  ? -18.716 11.968  -19.366 1.00 129.83 ? 35  LYS   A CD  1 
ATOM   66   C  CE  . LYS   A 1 15  ? -17.443 11.231  -18.972 1.00 128.19 ? 35  LYS   A CE  1 
ATOM   67   N  NZ  . LYS   A 1 15  ? -17.562 10.534  -17.661 1.00 121.64 ? 35  LYS   A NZ  1 
ATOM   68   N  N   . LEU   A 1 16  ? -18.058 8.690   -22.972 1.00 111.99 ? 36  LEU   A N   1 
ATOM   69   C  CA  . LEU   A 1 16  ? -16.735 8.103   -23.153 1.00 108.43 ? 36  LEU   A CA  1 
ATOM   70   C  C   . LEU   A 1 16  ? -16.416 7.757   -24.601 1.00 106.37 ? 36  LEU   A C   1 
ATOM   71   O  O   . LEU   A 1 16  ? -15.271 7.392   -24.894 1.00 109.31 ? 36  LEU   A O   1 
ATOM   72   C  CB  . LEU   A 1 16  ? -16.604 6.837   -22.301 1.00 108.10 ? 36  LEU   A CB  1 
ATOM   73   C  CG  . LEU   A 1 16  ? -15.895 6.975   -20.956 1.00 109.12 ? 36  LEU   A CG  1 
ATOM   74   C  CD1 . LEU   A 1 16  ? -16.291 5.841   -20.030 1.00 107.44 ? 36  LEU   A CD1 1 
ATOM   75   C  CD2 . LEU   A 1 16  ? -14.390 6.991   -21.168 1.00 116.40 ? 36  LEU   A CD2 1 
ATOM   76   N  N   . GLY   A 1 17  ? -17.385 7.853   -25.507 1.00 108.19 ? 37  GLY   A N   1 
ATOM   77   C  CA  . GLY   A 1 17  ? -17.157 7.424   -26.874 1.00 101.38 ? 37  GLY   A CA  1 
ATOM   78   C  C   . GLY   A 1 17  ? -17.176 5.921   -27.049 1.00 104.86 ? 37  GLY   A C   1 
ATOM   79   O  O   . GLY   A 1 17  ? -16.546 5.406   -27.978 1.00 102.51 ? 37  GLY   A O   1 
ATOM   80   N  N   . ILE   A 1 18  ? -17.880 5.208   -26.181 1.00 105.13 ? 38  ILE   A N   1 
ATOM   81   C  CA  . ILE   A 1 18  ? -17.967 3.751   -26.228 1.00 99.00  ? 38  ILE   A CA  1 
ATOM   82   C  C   . ILE   A 1 18  ? -19.339 3.369   -26.771 1.00 95.08  ? 38  ILE   A C   1 
ATOM   83   O  O   . ILE   A 1 18  ? -20.353 3.811   -26.213 1.00 94.80  ? 38  ILE   A O   1 
ATOM   84   C  CB  . ILE   A 1 18  ? -17.737 3.130   -24.840 1.00 95.85  ? 38  ILE   A CB  1 
ATOM   85   C  CG1 . ILE   A 1 18  ? -16.278 3.297   -24.415 1.00 96.76  ? 38  ILE   A CG1 1 
ATOM   86   C  CG2 . ILE   A 1 18  ? -18.135 1.666   -24.846 1.00 94.67  ? 38  ILE   A CG2 1 
ATOM   87   C  CD1 . ILE   A 1 18  ? -16.037 3.025   -22.952 1.00 91.35  ? 38  ILE   A CD1 1 
ATOM   88   N  N   . PRO   A 1 19  ? -19.418 2.561   -27.823 1.00 93.16  ? 39  PRO   A N   1 
ATOM   89   C  CA  . PRO   A 1 19  ? -20.717 2.238   -28.417 1.00 88.13  ? 39  PRO   A CA  1 
ATOM   90   C  C   . PRO   A 1 19  ? -21.496 1.247   -27.561 1.00 91.83  ? 39  PRO   A C   1 
ATOM   91   O  O   . PRO   A 1 19  ? -20.976 0.637   -26.625 1.00 91.76  ? 39  PRO   A O   1 
ATOM   92   C  CB  . PRO   A 1 19  ? -20.339 1.625   -29.765 1.00 90.79  ? 39  PRO   A CB  1 
ATOM   93   C  CG  . PRO   A 1 19  ? -19.023 0.968   -29.495 1.00 90.50  ? 39  PRO   A CG  1 
ATOM   94   C  CD  . PRO   A 1 19  ? -18.311 1.875   -28.515 1.00 91.53  ? 39  PRO   A CD  1 
ATOM   95   N  N   . GLY   A 1 20  ? -22.772 1.093   -27.912 1.00 90.52  ? 40  GLY   A N   1 
ATOM   96   C  CA  . GLY   A 1 20  ? -23.648 0.161   -27.242 1.00 90.52  ? 40  GLY   A CA  1 
ATOM   97   C  C   . GLY   A 1 20  ? -25.105 0.405   -27.584 1.00 93.74  ? 40  GLY   A C   1 
ATOM   98   O  O   . GLY   A 1 20  ? -25.451 1.368   -28.275 1.00 97.30  ? 40  GLY   A O   1 
ATOM   99   N  N   . PRO   A 1 21  ? -25.990 -0.470  -27.110 1.00 95.33  ? 41  PRO   A N   1 
ATOM   100  C  CA  . PRO   A 1 21  ? -27.424 -0.261  -27.345 1.00 91.14  ? 41  PRO   A CA  1 
ATOM   101  C  C   . PRO   A 1 21  ? -27.963 0.861   -26.473 1.00 94.56  ? 41  PRO   A C   1 
ATOM   102  O  O   . PRO   A 1 21  ? -27.584 1.004   -25.308 1.00 97.02  ? 41  PRO   A O   1 
ATOM   103  C  CB  . PRO   A 1 21  ? -28.043 -1.612  -26.969 1.00 90.09  ? 41  PRO   A CB  1 
ATOM   104  C  CG  . PRO   A 1 21  ? -27.098 -2.177  -25.959 1.00 86.16  ? 41  PRO   A CG  1 
ATOM   105  C  CD  . PRO   A 1 21  ? -25.723 -1.710  -26.359 1.00 84.70  ? 41  PRO   A CD  1 
ATOM   106  N  N   . THR   A 1 22  ? -28.848 1.665   -27.051 1.00 100.70 ? 42  THR   A N   1 
ATOM   107  C  CA  . THR   A 1 22  ? -29.440 2.770   -26.305 1.00 103.38 ? 42  THR   A CA  1 
ATOM   108  C  C   . THR   A 1 22  ? -30.385 2.224   -25.239 1.00 98.91  ? 42  THR   A C   1 
ATOM   109  O  O   . THR   A 1 22  ? -31.299 1.456   -25.560 1.00 99.14  ? 42  THR   A O   1 
ATOM   110  C  CB  . THR   A 1 22  ? -30.184 3.725   -27.238 1.00 103.68 ? 42  THR   A CB  1 
ATOM   111  O  OG1 . THR   A 1 22  ? -30.681 3.005   -28.373 1.00 106.10 ? 42  THR   A OG1 1 
ATOM   112  C  CG2 . THR   A 1 22  ? -29.257 4.838   -27.711 1.00 105.34 ? 42  THR   A CG2 1 
ATOM   113  N  N   . PRO   A 1 23  ? -30.199 2.587   -23.973 1.00 89.61  ? 43  PRO   A N   1 
ATOM   114  C  CA  . PRO   A 1 23  ? -31.036 2.029   -22.909 1.00 87.97  ? 43  PRO   A CA  1 
ATOM   115  C  C   . PRO   A 1 23  ? -32.373 2.739   -22.782 1.00 92.82  ? 43  PRO   A C   1 
ATOM   116  O  O   . PRO   A 1 23  ? -32.527 3.913   -23.127 1.00 94.64  ? 43  PRO   A O   1 
ATOM   117  C  CB  . PRO   A 1 23  ? -30.186 2.248   -21.652 1.00 86.69  ? 43  PRO   A CB  1 
ATOM   118  C  CG  . PRO   A 1 23  ? -29.426 3.492   -21.958 1.00 86.87  ? 43  PRO   A CG  1 
ATOM   119  C  CD  . PRO   A 1 23  ? -29.122 3.439   -23.438 1.00 87.56  ? 43  PRO   A CD  1 
ATOM   120  N  N   . LEU   A 1 24  ? -33.345 1.997   -22.272 1.00 87.04  ? 44  LEU   A N   1 
ATOM   121  C  CA  . LEU   A 1 24  ? -34.621 2.571   -21.880 1.00 86.37  ? 44  LEU   A CA  1 
ATOM   122  C  C   . LEU   A 1 24  ? -34.532 3.097   -20.451 1.00 84.99  ? 44  LEU   A C   1 
ATOM   123  O  O   . LEU   A 1 24  ? -33.703 2.628   -19.664 1.00 81.71  ? 44  LEU   A O   1 
ATOM   124  C  CB  . LEU   A 1 24  ? -35.728 1.524   -21.971 1.00 89.10  ? 44  LEU   A CB  1 
ATOM   125  C  CG  . LEU   A 1 24  ? -36.004 0.904   -23.342 1.00 86.08  ? 44  LEU   A CG  1 
ATOM   126  C  CD1 . LEU   A 1 24  ? -37.011 -0.229  -23.211 1.00 82.95  ? 44  LEU   A CD1 1 
ATOM   127  C  CD2 . LEU   A 1 24  ? -36.501 1.954   -24.325 1.00 86.93  ? 44  LEU   A CD2 1 
ATOM   128  N  N   . PRO   A 1 25  ? -35.351 4.084   -20.091 1.00 85.66  ? 45  PRO   A N   1 
ATOM   129  C  CA  . PRO   A 1 25  ? -35.380 4.529   -18.693 1.00 84.86  ? 45  PRO   A CA  1 
ATOM   130  C  C   . PRO   A 1 25  ? -35.680 3.372   -17.749 1.00 86.51  ? 45  PRO   A C   1 
ATOM   131  O  O   . PRO   A 1 25  ? -36.457 2.470   -18.072 1.00 86.77  ? 45  PRO   A O   1 
ATOM   132  C  CB  . PRO   A 1 25  ? -36.499 5.576   -18.681 1.00 84.42  ? 45  PRO   A CB  1 
ATOM   133  C  CG  . PRO   A 1 25  ? -36.509 6.113   -20.074 1.00 87.10  ? 45  PRO   A CG  1 
ATOM   134  C  CD  . PRO   A 1 25  ? -36.185 4.935   -20.959 1.00 86.47  ? 45  PRO   A CD  1 
ATOM   135  N  N   . PHE   A 1 26  ? -35.008 3.384   -16.593 1.00 83.30  ? 46  PHE   A N   1 
ATOM   136  C  CA  . PHE   A 1 26  ? -35.209 2.421   -15.512 1.00 84.10  ? 46  PHE   A CA  1 
ATOM   137  C  C   . PHE   A 1 26  ? -34.693 1.042   -15.915 1.00 81.23  ? 46  PHE   A C   1 
ATOM   138  O  O   . PHE   A 1 26  ? -33.931 0.421   -15.166 1.00 87.62  ? 46  PHE   A O   1 
ATOM   139  C  CB  . PHE   A 1 26  ? -36.676 2.407   -15.067 1.00 85.01  ? 46  PHE   A CB  1 
ATOM   140  C  CG  . PHE   A 1 26  ? -37.114 3.666   -14.366 1.00 95.24  ? 46  PHE   A CG  1 
ATOM   141  C  CD1 . PHE   A 1 26  ? -36.184 4.497   -13.762 1.00 100.64 ? 46  PHE   A CD1 1 
ATOM   142  C  CD2 . PHE   A 1 26  ? -38.453 4.014   -14.310 1.00 101.51 ? 46  PHE   A CD2 1 
ATOM   143  C  CE1 . PHE   A 1 26  ? -36.584 5.656   -13.116 1.00 99.94  ? 46  PHE   A CE1 1 
ATOM   144  C  CE2 . PHE   A 1 26  ? -38.858 5.171   -13.667 1.00 102.47 ? 46  PHE   A CE2 1 
ATOM   145  C  CZ  . PHE   A 1 26  ? -37.923 5.991   -13.068 1.00 101.70 ? 46  PHE   A CZ  1 
ATOM   146  N  N   . LEU   A 1 27  ? -35.097 0.548   -17.086 1.00 82.83  ? 47  LEU   A N   1 
ATOM   147  C  CA  . LEU   A 1 27  ? -34.845 -0.847  -17.433 1.00 84.75  ? 47  LEU   A CA  1 
ATOM   148  C  C   . LEU   A 1 27  ? -33.411 -1.090  -17.886 1.00 87.10  ? 47  LEU   A C   1 
ATOM   149  O  O   . LEU   A 1 27  ? -32.876 -2.185  -17.675 1.00 85.02  ? 47  LEU   A O   1 
ATOM   150  C  CB  . LEU   A 1 27  ? -35.813 -1.300  -18.526 1.00 80.51  ? 47  LEU   A CB  1 
ATOM   151  C  CG  . LEU   A 1 27  ? -37.294 -1.329  -18.151 1.00 84.39  ? 47  LEU   A CG  1 
ATOM   152  C  CD1 . LEU   A 1 27  ? -38.133 -1.704  -19.359 1.00 82.79  ? 47  LEU   A CD1 1 
ATOM   153  C  CD2 . LEU   A 1 27  ? -37.526 -2.306  -17.013 1.00 86.50  ? 47  LEU   A CD2 1 
ATOM   154  N  N   . GLY   A 1 28  ? -32.773 -0.101  -18.498 1.00 87.54  ? 48  GLY   A N   1 
ATOM   155  C  CA  . GLY   A 1 28  ? -31.476 -0.356  -19.101 1.00 80.21  ? 48  GLY   A CA  1 
ATOM   156  C  C   . GLY   A 1 28  ? -31.676 -1.114  -20.398 1.00 78.19  ? 48  GLY   A C   1 
ATOM   157  O  O   . GLY   A 1 28  ? -32.542 -0.768  -21.208 1.00 82.14  ? 48  GLY   A O   1 
ATOM   158  N  N   . ASN   A 1 29  ? -30.890 -2.171  -20.602 1.00 79.51  ? 49  ASN   A N   1 
ATOM   159  C  CA  . ASN   A 1 29  ? -31.002 -3.000  -21.798 1.00 81.11  ? 49  ASN   A CA  1 
ATOM   160  C  C   . ASN   A 1 29  ? -31.585 -4.379  -21.526 1.00 82.99  ? 49  ASN   A C   1 
ATOM   161  O  O   . ASN   A 1 29  ? -31.610 -5.211  -22.435 1.00 84.80  ? 49  ASN   A O   1 
ATOM   162  C  CB  . ASN   A 1 29  ? -29.633 -3.152  -22.465 1.00 78.75  ? 49  ASN   A CB  1 
ATOM   163  C  CG  . ASN   A 1 29  ? -29.138 -1.862  -23.073 1.00 79.69  ? 49  ASN   A CG  1 
ATOM   164  O  OD1 . ASN   A 1 29  ? -28.169 -1.275  -22.600 1.00 75.04  ? 49  ASN   A OD1 1 
ATOM   165  N  ND2 . ASN   A 1 29  ? -29.802 -1.412  -24.132 1.00 81.88  ? 49  ASN   A ND2 1 
ATOM   166  N  N   . ILE   A 1 30  ? -32.068 -4.639  -20.308 1.00 85.67  ? 50  ILE   A N   1 
ATOM   167  C  CA  . ILE   A 1 30  ? -32.479 -5.988  -19.930 1.00 85.66  ? 50  ILE   A CA  1 
ATOM   168  C  C   . ILE   A 1 30  ? -33.585 -6.542  -20.815 1.00 84.63  ? 50  ILE   A C   1 
ATOM   169  O  O   . ILE   A 1 30  ? -33.745 -7.764  -20.898 1.00 89.98  ? 50  ILE   A O   1 
ATOM   170  C  CB  . ILE   A 1 30  ? -32.901 -6.027  -18.448 1.00 86.74  ? 50  ILE   A CB  1 
ATOM   171  C  CG1 . ILE   A 1 30  ? -34.112 -5.128  -18.204 1.00 84.20  ? 50  ILE   A CG1 1 
ATOM   172  C  CG2 . ILE   A 1 30  ? -31.741 -5.626  -17.548 1.00 86.95  ? 50  ILE   A CG2 1 
ATOM   173  C  CD1 . ILE   A 1 30  ? -34.671 -5.247  -16.813 1.00 88.28  ? 50  ILE   A CD1 1 
ATOM   174  N  N   . LEU   A 1 31  ? -34.356 -5.682  -21.486 1.00 93.55  ? 51  LEU   A N   1 
ATOM   175  C  CA  . LEU   A 1 31  ? -35.300 -6.187  -22.476 1.00 89.20  ? 51  LEU   A CA  1 
ATOM   176  C  C   . LEU   A 1 31  ? -34.599 -6.906  -23.617 1.00 93.94  ? 51  LEU   A C   1 
ATOM   177  O  O   . LEU   A 1 31  ? -35.220 -7.747  -24.274 1.00 100.93 ? 51  LEU   A O   1 
ATOM   178  C  CB  . LEU   A 1 31  ? -36.156 -5.046  -23.036 1.00 80.84  ? 51  LEU   A CB  1 
ATOM   179  C  CG  . LEU   A 1 31  ? -37.141 -4.397  -22.065 1.00 85.41  ? 51  LEU   A CG  1 
ATOM   180  C  CD1 . LEU   A 1 31  ? -38.243 -3.675  -22.824 1.00 81.19  ? 51  LEU   A CD1 1 
ATOM   181  C  CD2 . LEU   A 1 31  ? -37.724 -5.441  -21.129 1.00 77.10  ? 51  LEU   A CD2 1 
ATOM   182  N  N   . SER   A 1 32  ? -33.327 -6.599  -23.868 1.00 89.83  ? 52  SER   A N   1 
ATOM   183  C  CA  . SER   A 1 32  ? -32.560 -7.299  -24.887 1.00 96.56  ? 52  SER   A CA  1 
ATOM   184  C  C   . SER   A 1 32  ? -32.077 -8.667  -24.424 1.00 101.04 ? 52  SER   A C   1 
ATOM   185  O  O   . SER   A 1 32  ? -31.462 -9.387  -25.217 1.00 105.86 ? 52  SER   A O   1 
ATOM   186  C  CB  . SER   A 1 32  ? -31.367 -6.447  -25.325 1.00 93.60  ? 52  SER   A CB  1 
ATOM   187  O  OG  . SER   A 1 32  ? -31.789 -5.172  -25.781 1.00 89.00  ? 52  SER   A OG  1 
ATOM   188  N  N   . TYR   A 1 33  ? -32.329 -9.040  -23.169 1.00 99.20  ? 53  TYR   A N   1 
ATOM   189  C  CA  . TYR   A 1 33  ? -32.087 -10.396 -22.694 1.00 100.26 ? 53  TYR   A CA  1 
ATOM   190  C  C   . TYR   A 1 33  ? -33.197 -11.363 -23.087 1.00 109.07 ? 53  TYR   A C   1 
ATOM   191  O  O   . TYR   A 1 33  ? -33.227 -12.484 -22.570 1.00 109.70 ? 53  TYR   A O   1 
ATOM   192  C  CB  . TYR   A 1 33  ? -31.933 -10.411 -21.170 1.00 93.40  ? 53  TYR   A CB  1 
ATOM   193  C  CG  . TYR   A 1 33  ? -30.655 -9.801  -20.645 1.00 93.06  ? 53  TYR   A CG  1 
ATOM   194  C  CD1 . TYR   A 1 33  ? -29.482 -9.839  -21.388 1.00 92.82  ? 53  TYR   A CD1 1 
ATOM   195  C  CD2 . TYR   A 1 33  ? -30.621 -9.194  -19.397 1.00 90.45  ? 53  TYR   A CD2 1 
ATOM   196  C  CE1 . TYR   A 1 33  ? -28.308 -9.282  -20.901 1.00 92.01  ? 53  TYR   A CE1 1 
ATOM   197  C  CE2 . TYR   A 1 33  ? -29.458 -8.635  -18.903 1.00 92.68  ? 53  TYR   A CE2 1 
ATOM   198  C  CZ  . TYR   A 1 33  ? -28.303 -8.681  -19.657 1.00 94.32  ? 53  TYR   A CZ  1 
ATOM   199  O  OH  . TYR   A 1 33  ? -27.146 -8.123  -19.158 1.00 89.09  ? 53  TYR   A OH  1 
ATOM   200  N  N   . HIS   A 1 34  ? -34.111 -10.962 -23.974 1.00 125.29 ? 54  HIS   A N   1 
ATOM   201  C  CA  . HIS   A 1 34  ? -35.242 -11.823 -24.297 1.00 128.01 ? 54  HIS   A CA  1 
ATOM   202  C  C   . HIS   A 1 34  ? -34.831 -13.029 -25.129 1.00 125.45 ? 54  HIS   A C   1 
ATOM   203  O  O   . HIS   A 1 34  ? -35.605 -13.987 -25.232 1.00 126.25 ? 54  HIS   A O   1 
ATOM   204  C  CB  . HIS   A 1 34  ? -36.343 -11.025 -25.008 1.00 133.10 ? 54  HIS   A CB  1 
ATOM   205  C  CG  . HIS   A 1 34  ? -35.949 -10.475 -26.345 1.00 137.34 ? 54  HIS   A CG  1 
ATOM   206  N  ND1 . HIS   A 1 34  ? -34.748 -9.837  -26.571 1.00 133.52 ? 54  HIS   A ND1 1 
ATOM   207  C  CD2 . HIS   A 1 34  ? -36.617 -10.442 -27.523 1.00 137.59 ? 54  HIS   A CD2 1 
ATOM   208  C  CE1 . HIS   A 1 34  ? -34.687 -9.450  -27.832 1.00 133.78 ? 54  HIS   A CE1 1 
ATOM   209  N  NE2 . HIS   A 1 34  ? -35.810 -9.802  -28.431 1.00 136.23 ? 54  HIS   A NE2 1 
ATOM   210  N  N   . LYS   A 1 35  ? -33.635 -13.012 -25.717 1.00 119.73 ? 55  LYS   A N   1 
ATOM   211  C  CA  . LYS   A 1 35  ? -33.072 -14.186 -26.370 1.00 118.07 ? 55  LYS   A CA  1 
ATOM   212  C  C   . LYS   A 1 35  ? -31.865 -14.737 -25.618 1.00 114.01 ? 55  LYS   A C   1 
ATOM   213  O  O   . LYS   A 1 35  ? -31.109 -15.541 -26.171 1.00 116.08 ? 55  LYS   A O   1 
ATOM   214  C  CB  . LYS   A 1 35  ? -32.701 -13.874 -27.819 1.00 121.17 ? 55  LYS   A CB  1 
ATOM   215  C  CG  . LYS   A 1 35  ? -33.863 -14.006 -28.789 1.00 129.32 ? 55  LYS   A CG  1 
ATOM   216  C  CD  . LYS   A 1 35  ? -34.406 -12.647 -29.192 1.00 130.13 ? 55  LYS   A CD  1 
ATOM   217  C  CE  . LYS   A 1 35  ? -35.617 -12.784 -30.102 1.00 129.49 ? 55  LYS   A CE  1 
ATOM   218  N  NZ  . LYS   A 1 35  ? -35.954 -11.507 -30.794 1.00 133.05 ? 55  LYS   A NZ  1 
ATOM   219  N  N   . GLY   A 1 36  ? -31.668 -14.317 -24.375 1.00 112.62 ? 56  GLY   A N   1 
ATOM   220  C  CA  . GLY   A 1 36  ? -30.660 -14.901 -23.519 1.00 109.65 ? 56  GLY   A CA  1 
ATOM   221  C  C   . GLY   A 1 36  ? -29.383 -14.077 -23.466 1.00 110.84 ? 56  GLY   A C   1 
ATOM   222  O  O   . GLY   A 1 36  ? -29.098 -13.249 -24.335 1.00 109.97 ? 56  GLY   A O   1 
ATOM   223  N  N   . PHE   A 1 37  ? -28.604 -14.321 -22.407 1.00 100.24 ? 57  PHE   A N   1 
ATOM   224  C  CA  . PHE   A 1 37  ? -27.318 -13.653 -22.226 1.00 94.65  ? 57  PHE   A CA  1 
ATOM   225  C  C   . PHE   A 1 37  ? -26.416 -13.855 -23.436 1.00 95.52  ? 57  PHE   A C   1 
ATOM   226  O  O   . PHE   A 1 37  ? -25.803 -12.907 -23.941 1.00 94.11  ? 57  PHE   A O   1 
ATOM   227  C  CB  . PHE   A 1 37  ? -26.616 -14.189 -20.973 1.00 96.81  ? 57  PHE   A CB  1 
ATOM   228  C  CG  . PHE   A 1 37  ? -27.260 -13.785 -19.675 1.00 96.15  ? 57  PHE   A CG  1 
ATOM   229  C  CD1 . PHE   A 1 37  ? -28.548 -14.189 -19.361 1.00 109.19 ? 57  PHE   A CD1 1 
ATOM   230  C  CD2 . PHE   A 1 37  ? -26.554 -13.034 -18.750 1.00 94.77  ? 57  PHE   A CD2 1 
ATOM   231  C  CE1 . PHE   A 1 37  ? -29.132 -13.826 -18.161 1.00 109.63 ? 57  PHE   A CE1 1 
ATOM   232  C  CE2 . PHE   A 1 37  ? -27.130 -12.669 -17.547 1.00 100.71 ? 57  PHE   A CE2 1 
ATOM   233  C  CZ  . PHE   A 1 37  ? -28.421 -13.066 -17.251 1.00 108.34 ? 57  PHE   A CZ  1 
ATOM   234  N  N   . CYS   A 1 38  ? -26.326 -15.098 -23.911 1.00 91.78  ? 58  CYS   A N   1 
ATOM   235  C  CA  . CYS   A 1 38  ? -25.332 -15.448 -24.920 1.00 92.62  ? 58  CYS   A CA  1 
ATOM   236  C  C   . CYS   A 1 38  ? -25.640 -14.796 -26.262 1.00 89.68  ? 58  CYS   A C   1 
ATOM   237  O  O   . CYS   A 1 38  ? -24.754 -14.205 -26.891 1.00 84.98  ? 58  CYS   A O   1 
ATOM   238  C  CB  . CYS   A 1 38  ? -25.254 -16.969 -25.053 1.00 89.55  ? 58  CYS   A CB  1 
ATOM   239  S  SG  . CYS   A 1 38  ? -24.719 -17.790 -23.526 1.00 89.33  ? 58  CYS   A SG  1 
ATOM   240  N  N   . MET   A 1 39  ? -26.891 -14.894 -26.723 1.00 93.60  ? 59  MET   A N   1 
ATOM   241  C  CA  . MET   A 1 39  ? -27.247 -14.278 -27.997 1.00 94.13  ? 59  MET   A CA  1 
ATOM   242  C  C   . MET   A 1 39  ? -27.123 -12.762 -27.944 1.00 91.50  ? 59  MET   A C   1 
ATOM   243  O  O   . MET   A 1 39  ? -26.851 -12.126 -28.968 1.00 91.16  ? 59  MET   A O   1 
ATOM   244  C  CB  . MET   A 1 39  ? -28.666 -14.672 -28.406 1.00 101.65 ? 59  MET   A CB  1 
ATOM   245  C  CG  . MET   A 1 39  ? -28.754 -15.978 -29.174 1.00 106.70 ? 59  MET   A CG  1 
ATOM   246  S  SD  . MET   A 1 39  ? -29.977 -15.897 -30.498 1.00 135.66 ? 59  MET   A SD  1 
ATOM   247  C  CE  . MET   A 1 39  ? -29.284 -14.597 -31.520 1.00 115.16 ? 59  MET   A CE  1 
ATOM   248  N  N   . PHE   A 1 40  ? -27.323 -12.165 -26.768 1.00 94.04  ? 60  PHE   A N   1 
ATOM   249  C  CA  . PHE   A 1 40  ? -27.173 -10.720 -26.637 1.00 91.30  ? 60  PHE   A CA  1 
ATOM   250  C  C   . PHE   A 1 40  ? -25.716 -10.305 -26.809 1.00 90.87  ? 60  PHE   A C   1 
ATOM   251  O  O   . PHE   A 1 40  ? -25.415 -9.333  -27.513 1.00 94.28  ? 60  PHE   A O   1 
ATOM   252  C  CB  . PHE   A 1 40  ? -27.720 -10.267 -25.282 1.00 87.39  ? 60  PHE   A CB  1 
ATOM   253  C  CG  . PHE   A 1 40  ? -27.424 -8.832  -24.948 1.00 84.67  ? 60  PHE   A CG  1 
ATOM   254  C  CD1 . PHE   A 1 40  ? -27.981 -7.802  -25.687 1.00 82.22  ? 60  PHE   A CD1 1 
ATOM   255  C  CD2 . PHE   A 1 40  ? -26.609 -8.514  -23.874 1.00 85.41  ? 60  PHE   A CD2 1 
ATOM   256  C  CE1 . PHE   A 1 40  ? -27.715 -6.480  -25.370 1.00 85.51  ? 60  PHE   A CE1 1 
ATOM   257  C  CE2 . PHE   A 1 40  ? -26.339 -7.196  -23.552 1.00 86.45  ? 60  PHE   A CE2 1 
ATOM   258  C  CZ  . PHE   A 1 40  ? -26.893 -6.177  -24.301 1.00 79.85  ? 60  PHE   A CZ  1 
ATOM   259  N  N   . ASP   A 1 41  ? -24.794 -11.042 -26.186 1.00 86.73  ? 61  ASP   A N   1 
ATOM   260  C  CA  . ASP   A 1 41  ? -23.377 -10.720 -26.319 1.00 85.35  ? 61  ASP   A CA  1 
ATOM   261  C  C   . ASP   A 1 41  ? -22.876 -10.984 -27.733 1.00 86.92  ? 61  ASP   A C   1 
ATOM   262  O  O   . ASP   A 1 41  ? -22.057 -10.220 -28.260 1.00 87.56  ? 61  ASP   A O   1 
ATOM   263  C  CB  . ASP   A 1 41  ? -22.556 -11.517 -25.304 1.00 88.90  ? 61  ASP   A CB  1 
ATOM   264  C  CG  . ASP   A 1 41  ? -22.930 -11.199 -23.870 1.00 85.74  ? 61  ASP   A CG  1 
ATOM   265  O  OD1 . ASP   A 1 41  ? -23.544 -10.136 -23.635 1.00 86.46  ? 61  ASP   A OD1 1 
ATOM   266  O  OD2 . ASP   A 1 41  ? -22.602 -12.007 -22.975 1.00 86.67  ? 61  ASP   A OD2 1 
ATOM   267  N  N   . MET   A 1 42  ? -23.346 -12.065 -28.363 1.00 90.48  ? 62  MET   A N   1 
ATOM   268  C  CA  A MET   A 1 42  ? -22.931 -12.381 -29.727 0.49 88.65  ? 62  MET   A CA  1 
ATOM   269  C  CA  B MET   A 1 42  ? -22.900 -12.360 -29.719 0.51 83.77  ? 62  MET   A CA  1 
ATOM   270  C  C   . MET   A 1 42  ? -23.338 -11.274 -30.693 1.00 96.40  ? 62  MET   A C   1 
ATOM   271  O  O   . MET   A 1 42  ? -22.549 -10.848 -31.543 1.00 97.33  ? 62  MET   A O   1 
ATOM   272  C  CB  A MET   A 1 42  ? -23.535 -13.719 -30.160 0.49 89.54  ? 62  MET   A CB  1 
ATOM   273  C  CB  B MET   A 1 42  ? -23.404 -13.735 -30.162 0.51 90.76  ? 62  MET   A CB  1 
ATOM   274  C  CG  A MET   A 1 42  ? -22.956 -14.936 -29.452 0.49 93.04  ? 62  MET   A CG  1 
ATOM   275  C  CG  B MET   A 1 42  ? -22.691 -14.891 -29.470 0.51 92.69  ? 62  MET   A CG  1 
ATOM   276  S  SD  A MET   A 1 42  ? -21.434 -15.537 -30.210 0.49 92.57  ? 62  MET   A SD  1 
ATOM   277  S  SD  B MET   A 1 42  ? -22.906 -16.487 -30.285 0.51 92.55  ? 62  MET   A SD  1 
ATOM   278  C  CE  A MET   A 1 42  ? -22.051 -16.176 -31.765 0.49 90.85  ? 62  MET   A CE  1 
ATOM   279  C  CE  B MET   A 1 42  ? -21.974 -16.238 -31.796 0.51 96.37  ? 62  MET   A CE  1 
ATOM   280  N  N   . GLU   A 1 43  ? -24.581 -10.800 -30.577 1.00 101.58 ? 63  GLU   A N   1 
ATOM   281  C  CA  . GLU   A 1 43  ? -25.034 -9.718  -31.446 1.00 102.00 ? 63  GLU   A CA  1 
ATOM   282  C  C   . GLU   A 1 43  ? -24.235 -8.447  -31.193 1.00 101.63 ? 63  GLU   A C   1 
ATOM   283  O  O   . GLU   A 1 43  ? -23.770 -7.793  -32.134 1.00 105.23 ? 63  GLU   A O   1 
ATOM   284  C  CB  . GLU   A 1 43  ? -26.527 -9.453  -31.241 1.00 104.31 ? 63  GLU   A CB  1 
ATOM   285  C  CG  . GLU   A 1 43  ? -27.440 -10.589 -31.664 1.00 112.58 ? 63  GLU   A CG  1 
ATOM   286  C  CD  . GLU   A 1 43  ? -27.295 -10.949 -33.129 1.00 121.00 ? 63  GLU   A CD  1 
ATOM   287  O  OE1 . GLU   A 1 43  ? -26.961 -10.057 -33.940 1.00 124.10 ? 63  GLU   A OE1 1 
ATOM   288  O  OE2 . GLU   A 1 43  ? -27.513 -12.131 -33.469 1.00 120.84 ? 63  GLU   A OE2 1 
ATOM   289  N  N   . CYS   A 1 44  ? -24.063 -8.087  -29.918 1.00 90.45  ? 64  CYS   A N   1 
ATOM   290  C  CA  . CYS   A 1 44  ? -23.361 -6.853  -29.579 1.00 86.95  ? 64  CYS   A CA  1 
ATOM   291  C  C   . CYS   A 1 44  ? -21.932 -6.856  -30.105 1.00 87.69  ? 64  CYS   A C   1 
ATOM   292  O  O   . CYS   A 1 44  ? -21.422 -5.817  -30.538 1.00 86.92  ? 64  CYS   A O   1 
ATOM   293  C  CB  . CYS   A 1 44  ? -23.373 -6.644  -28.068 1.00 84.82  ? 64  CYS   A CB  1 
ATOM   294  S  SG  . CYS   A 1 44  ? -24.819 -5.759  -27.446 1.00 68.87  ? 64  CYS   A SG  1 
ATOM   295  N  N   . HIS   A 1 45  ? -21.266 -8.011  -30.068 1.00 88.00  ? 65  HIS   A N   1 
ATOM   296  C  CA  . HIS   A 1 45  ? -19.906 -8.081  -30.591 1.00 89.05  ? 65  HIS   A CA  1 
ATOM   297  C  C   . HIS   A 1 45  ? -19.887 -7.843  -32.096 1.00 93.87  ? 65  HIS   A C   1 
ATOM   298  O  O   . HIS   A 1 45  ? -19.020 -7.126  -32.610 1.00 92.62  ? 65  HIS   A O   1 
ATOM   299  C  CB  . HIS   A 1 45  ? -19.283 -9.435  -30.251 1.00 87.20  ? 65  HIS   A CB  1 
ATOM   300  C  CG  . HIS   A 1 45  ? -17.822 -9.528  -30.568 1.00 90.50  ? 65  HIS   A CG  1 
ATOM   301  N  ND1 . HIS   A 1 45  ? -17.041 -8.421  -30.818 1.00 90.29  ? 65  HIS   A ND1 1 
ATOM   302  C  CD2 . HIS   A 1 45  ? -17.000 -10.599 -30.672 1.00 85.70  ? 65  HIS   A CD2 1 
ATOM   303  C  CE1 . HIS   A 1 45  ? -15.801 -8.805  -31.064 1.00 90.95  ? 65  HIS   A CE1 1 
ATOM   304  N  NE2 . HIS   A 1 45  ? -15.750 -10.122 -30.982 1.00 88.39  ? 65  HIS   A NE2 1 
ATOM   305  N  N   . LYS   A 1 46  ? -20.846 -8.427  -32.816 1.00 91.22  ? 66  LYS   A N   1 
ATOM   306  C  CA  . LYS   A 1 46  ? -20.885 -8.260  -34.265 1.00 93.45  ? 66  LYS   A CA  1 
ATOM   307  C  C   . LYS   A 1 46  ? -21.158 -6.810  -34.651 1.00 99.26  ? 66  LYS   A C   1 
ATOM   308  O  O   . LYS   A 1 46  ? -20.517 -6.273  -35.561 1.00 104.14 ? 66  LYS   A O   1 
ATOM   309  C  CB  . LYS   A 1 46  ? -21.937 -9.198  -34.866 1.00 95.94  ? 66  LYS   A CB  1 
ATOM   310  C  CG  . LYS   A 1 46  ? -22.446 -8.803  -36.254 1.00 108.39 ? 66  LYS   A CG  1 
ATOM   311  C  CD  . LYS   A 1 46  ? -21.339 -8.774  -37.300 1.00 109.27 ? 66  LYS   A CD  1 
ATOM   312  C  CE  . LYS   A 1 46  ? -21.616 -7.696  -38.333 1.00 114.00 ? 66  LYS   A CE  1 
ATOM   313  N  NZ  . LYS   A 1 46  ? -20.377 -7.247  -39.023 1.00 118.56 ? 66  LYS   A NZ  1 
ATOM   314  N  N   . LYS   A 1 47  ? -22.089 -6.153  -33.963 1.00 95.56  ? 67  LYS   A N   1 
ATOM   315  C  CA  . LYS   A 1 47  ? -22.520 -4.825  -34.381 1.00 93.76  ? 67  LYS   A CA  1 
ATOM   316  C  C   . LYS   A 1 47  ? -21.654 -3.704  -33.816 1.00 93.97  ? 67  LYS   A C   1 
ATOM   317  O  O   . LYS   A 1 47  ? -21.516 -2.658  -34.461 1.00 99.83  ? 67  LYS   A O   1 
ATOM   318  C  CB  . LYS   A 1 47  ? -23.991 -4.616  -33.994 1.00 95.57  ? 67  LYS   A CB  1 
ATOM   319  C  CG  . LYS   A 1 47  ? -24.602 -3.253  -34.347 1.00 97.22  ? 67  LYS   A CG  1 
ATOM   320  C  CD  . LYS   A 1 47  ? -24.274 -2.788  -35.769 1.00 106.52 ? 67  LYS   A CD  1 
ATOM   321  C  CE  . LYS   A 1 47  ? -24.744 -3.757  -36.841 1.00 109.74 ? 67  LYS   A CE  1 
ATOM   322  N  NZ  . LYS   A 1 47  ? -23.932 -3.582  -38.079 1.00 107.78 ? 67  LYS   A NZ  1 
ATOM   323  N  N   . TYR   A 1 48  ? -21.041 -3.890  -32.649 1.00 96.63  ? 68  TYR   A N   1 
ATOM   324  C  CA  . TYR   A 1 48  ? -20.342 -2.790  -31.997 1.00 94.78  ? 68  TYR   A CA  1 
ATOM   325  C  C   . TYR   A 1 48  ? -18.826 -2.913  -32.007 1.00 96.25  ? 68  TYR   A C   1 
ATOM   326  O  O   . TYR   A 1 48  ? -18.142 -1.889  -31.962 1.00 93.47  ? 68  TYR   A O   1 
ATOM   327  C  CB  . TYR   A 1 48  ? -20.836 -2.635  -30.555 1.00 93.53  ? 68  TYR   A CB  1 
ATOM   328  C  CG  . TYR   A 1 48  ? -22.304 -2.282  -30.499 1.00 94.68  ? 68  TYR   A CG  1 
ATOM   329  C  CD1 . TYR   A 1 48  ? -22.783 -1.143  -31.135 1.00 93.27  ? 68  TYR   A CD1 1 
ATOM   330  C  CD2 . TYR   A 1 48  ? -23.213 -3.090  -29.829 1.00 87.94  ? 68  TYR   A CD2 1 
ATOM   331  C  CE1 . TYR   A 1 48  ? -24.125 -0.814  -31.101 1.00 90.75  ? 68  TYR   A CE1 1 
ATOM   332  C  CE2 . TYR   A 1 48  ? -24.558 -2.767  -29.788 1.00 88.48  ? 68  TYR   A CE2 1 
ATOM   333  C  CZ  . TYR   A 1 48  ? -25.008 -1.628  -30.425 1.00 91.76  ? 68  TYR   A CZ  1 
ATOM   334  O  OH  . TYR   A 1 48  ? -26.345 -1.304  -30.388 1.00 82.68  ? 68  TYR   A OH  1 
ATOM   335  N  N   . GLY   A 1 49  ? -18.281 -4.126  -32.064 1.00 94.88  ? 69  GLY   A N   1 
ATOM   336  C  CA  . GLY   A 1 49  ? -16.851 -4.278  -32.245 1.00 94.12  ? 69  GLY   A CA  1 
ATOM   337  C  C   . GLY   A 1 49  ? -16.086 -4.850  -31.068 1.00 94.82  ? 69  GLY   A C   1 
ATOM   338  O  O   . GLY   A 1 49  ? -16.540 -5.787  -30.405 1.00 89.93  ? 69  GLY   A O   1 
ATOM   339  N  N   . LYS   A 1 50  ? -14.908 -4.279  -30.812 1.00 98.18  ? 70  LYS   A N   1 
ATOM   340  C  CA  . LYS   A 1 50  ? -13.977 -4.810  -29.823 1.00 95.81  ? 70  LYS   A CA  1 
ATOM   341  C  C   . LYS   A 1 50  ? -14.370 -4.475  -28.392 1.00 90.57  ? 70  LYS   A C   1 
ATOM   342  O  O   . LYS   A 1 50  ? -13.998 -5.214  -27.475 1.00 86.71  ? 70  LYS   A O   1 
ATOM   343  C  CB  . LYS   A 1 50  ? -12.569 -4.285  -30.118 1.00 96.07  ? 70  LYS   A CB  1 
ATOM   344  C  CG  . LYS   A 1 50  ? -12.556 -2.935  -30.835 1.00 98.47  ? 70  LYS   A CG  1 
ATOM   345  C  CD  . LYS   A 1 50  ? -11.261 -2.707  -31.604 1.00 111.93 ? 70  LYS   A CD  1 
ATOM   346  C  CE  . LYS   A 1 50  ? -10.231 -1.954  -30.773 1.00 117.98 ? 70  LYS   A CE  1 
ATOM   347  N  NZ  . LYS   A 1 50  ? -8.998  -1.637  -31.554 1.00 116.86 ? 70  LYS   A NZ  1 
ATOM   348  N  N   . VAL   A 1 51  ? -15.103 -3.385  -28.184 1.00 99.08  ? 71  VAL   A N   1 
ATOM   349  C  CA  . VAL   A 1 51  ? -15.480 -2.913  -26.854 1.00 96.26  ? 71  VAL   A CA  1 
ATOM   350  C  C   . VAL   A 1 51  ? -16.840 -2.234  -26.959 1.00 96.28  ? 71  VAL   A C   1 
ATOM   351  O  O   . VAL   A 1 51  ? -17.070 -1.439  -27.875 1.00 99.30  ? 71  VAL   A O   1 
ATOM   352  C  CB  . VAL   A 1 51  ? -14.430 -1.935  -26.279 1.00 94.03  ? 71  VAL   A CB  1 
ATOM   353  C  CG1 . VAL   A 1 51  ? -14.978 -1.225  -25.059 1.00 92.58  ? 71  VAL   A CG1 1 
ATOM   354  C  CG2 . VAL   A 1 51  ? -13.133 -2.655  -25.926 1.00 95.42  ? 71  VAL   A CG2 1 
ATOM   355  N  N   . TRP   A 1 52  ? -17.743 -2.539  -26.028 1.00 91.90  ? 72  TRP   A N   1 
ATOM   356  C  CA  . TRP   A 1 52  ? -19.042 -1.877  -25.996 1.00 91.65  ? 72  TRP   A CA  1 
ATOM   357  C  C   . TRP   A 1 52  ? -19.582 -1.877  -24.571 1.00 84.40  ? 72  TRP   A C   1 
ATOM   358  O  O   . TRP   A 1 52  ? -19.022 -2.508  -23.672 1.00 81.02  ? 72  TRP   A O   1 
ATOM   359  C  CB  . TRP   A 1 52  ? -20.035 -2.540  -26.956 1.00 90.22  ? 72  TRP   A CB  1 
ATOM   360  C  CG  . TRP   A 1 52  ? -20.478 -3.900  -26.524 1.00 87.06  ? 72  TRP   A CG  1 
ATOM   361  C  CD1 . TRP   A 1 52  ? -21.590 -4.204  -25.797 1.00 84.19  ? 72  TRP   A CD1 1 
ATOM   362  C  CD2 . TRP   A 1 52  ? -19.823 -5.146  -26.795 1.00 88.56  ? 72  TRP   A CD2 1 
ATOM   363  N  NE1 . TRP   A 1 52  ? -21.667 -5.560  -25.593 1.00 83.59  ? 72  TRP   A NE1 1 
ATOM   364  C  CE2 . TRP   A 1 52  ? -20.595 -6.162  -26.199 1.00 86.30  ? 72  TRP   A CE2 1 
ATOM   365  C  CE3 . TRP   A 1 52  ? -18.657 -5.499  -27.483 1.00 87.40  ? 72  TRP   A CE3 1 
ATOM   366  C  CZ2 . TRP   A 1 52  ? -20.242 -7.508  -26.271 1.00 88.47  ? 72  TRP   A CZ2 1 
ATOM   367  C  CZ3 . TRP   A 1 52  ? -18.306 -6.837  -27.551 1.00 87.93  ? 72  TRP   A CZ3 1 
ATOM   368  C  CH2 . TRP   A 1 52  ? -19.097 -7.824  -26.948 1.00 88.78  ? 72  TRP   A CH2 1 
ATOM   369  N  N   . GLY   A 1 53  ? -20.687 -1.165  -24.376 1.00 84.34  ? 73  GLY   A N   1 
ATOM   370  C  CA  . GLY   A 1 53  ? -21.270 -1.023  -23.054 1.00 83.66  ? 73  GLY   A CA  1 
ATOM   371  C  C   . GLY   A 1 53  ? -22.785 -1.037  -23.089 1.00 80.38  ? 73  GLY   A C   1 
ATOM   372  O  O   . GLY   A 1 53  ? -23.412 -0.648  -24.077 1.00 85.80  ? 73  GLY   A O   1 
ATOM   373  N  N   . PHE   A 1 54  ? -23.370 -1.488  -21.978 1.00 81.33  ? 74  PHE   A N   1 
ATOM   374  C  CA  . PHE   A 1 54  ? -24.818 -1.543  -21.809 1.00 80.87  ? 74  PHE   A CA  1 
ATOM   375  C  C   . PHE   A 1 54  ? -25.138 -1.371  -20.328 1.00 76.65  ? 74  PHE   A C   1 
ATOM   376  O  O   . PHE   A 1 54  ? -24.245 -1.168  -19.499 1.00 73.95  ? 74  PHE   A O   1 
ATOM   377  C  CB  . PHE   A 1 54  ? -25.393 -2.851  -22.368 1.00 78.88  ? 74  PHE   A CB  1 
ATOM   378  C  CG  . PHE   A 1 54  ? -24.774 -4.089  -21.782 1.00 80.75  ? 74  PHE   A CG  1 
ATOM   379  C  CD1 . PHE   A 1 54  ? -23.605 -4.613  -22.312 1.00 75.20  ? 74  PHE   A CD1 1 
ATOM   380  C  CD2 . PHE   A 1 54  ? -25.363 -4.734  -20.708 1.00 77.17  ? 74  PHE   A CD2 1 
ATOM   381  C  CE1 . PHE   A 1 54  ? -23.033 -5.749  -21.778 1.00 75.63  ? 74  PHE   A CE1 1 
ATOM   382  C  CE2 . PHE   A 1 54  ? -24.795 -5.873  -20.170 1.00 81.78  ? 74  PHE   A CE2 1 
ATOM   383  C  CZ  . PHE   A 1 54  ? -23.629 -6.382  -20.707 1.00 75.32  ? 74  PHE   A CZ  1 
ATOM   384  N  N   . TYR   A 1 55  ? -26.424 -1.456  -19.990 1.00 79.70  ? 75  TYR   A N   1 
ATOM   385  C  CA  . TYR   A 1 55  ? -26.883 -1.194  -18.630 1.00 79.44  ? 75  TYR   A CA  1 
ATOM   386  C  C   . TYR   A 1 55  ? -27.817 -2.302  -18.167 1.00 75.85  ? 75  TYR   A C   1 
ATOM   387  O  O   . TYR   A 1 55  ? -28.819 -2.592  -18.831 1.00 74.61  ? 75  TYR   A O   1 
ATOM   388  C  CB  . TYR   A 1 55  ? -27.591 0.163   -18.539 1.00 79.91  ? 75  TYR   A CB  1 
ATOM   389  C  CG  . TYR   A 1 55  ? -26.790 1.318   -19.097 1.00 82.44  ? 75  TYR   A CG  1 
ATOM   390  C  CD1 . TYR   A 1 55  ? -26.832 1.624   -20.451 1.00 82.05  ? 75  TYR   A CD1 1 
ATOM   391  C  CD2 . TYR   A 1 55  ? -25.997 2.106   -18.272 1.00 82.61  ? 75  TYR   A CD2 1 
ATOM   392  C  CE1 . TYR   A 1 55  ? -26.105 2.678   -20.969 1.00 83.52  ? 75  TYR   A CE1 1 
ATOM   393  C  CE2 . TYR   A 1 55  ? -25.264 3.163   -18.782 1.00 81.11  ? 75  TYR   A CE2 1 
ATOM   394  C  CZ  . TYR   A 1 55  ? -25.322 3.443   -20.131 1.00 86.27  ? 75  TYR   A CZ  1 
ATOM   395  O  OH  . TYR   A 1 55  ? -24.596 4.495   -20.645 1.00 92.71  ? 75  TYR   A OH  1 
ATOM   396  N  N   . ASP   A 1 56  ? -27.486 -2.919  -17.031 1.00 80.44  ? 76  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 56  ? -28.407 -3.802  -16.313 1.00 78.08  ? 76  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 56  ? -29.111 -2.939  -15.276 1.00 80.21  ? 76  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 56  ? -28.667 -2.814  -14.133 1.00 83.00  ? 76  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 56  ? -27.672 -4.969  -15.665 1.00 72.91  ? 76  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 56  ? -27.063 -5.919  -16.678 1.00 77.18  ? 76  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 56  ? -27.525 -5.938  -17.838 1.00 83.69  ? 76  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 56  ? -26.126 -6.657  -16.310 1.00 77.73  ? 76  ASP   A OD2 1 
ATOM   404  N  N   . GLY   A 1 57  ? -30.224 -2.331  -15.679 1.00 79.02  ? 77  GLY   A N   1 
ATOM   405  C  CA  . GLY   A 1 57  ? -30.856 -1.321  -14.855 1.00 84.56  ? 77  GLY   A CA  1 
ATOM   406  C  C   . GLY   A 1 57  ? -30.106 -0.010  -14.962 1.00 87.38  ? 77  GLY   A C   1 
ATOM   407  O  O   . GLY   A 1 57  ? -29.963 0.539   -16.058 1.00 87.72  ? 77  GLY   A O   1 
ATOM   408  N  N   . GLN   A 1 58  ? -29.616 0.502   -13.835 1.00 86.12  ? 78  GLN   A N   1 
ATOM   409  C  CA  . GLN   A 1 58  ? -28.738 1.663   -13.827 1.00 83.15  ? 78  GLN   A CA  1 
ATOM   410  C  C   . GLN   A 1 58  ? -27.269 1.266   -13.755 1.00 82.16  ? 78  GLN   A C   1 
ATOM   411  O  O   . GLN   A 1 58  ? -26.413 2.127   -13.533 1.00 84.93  ? 78  GLN   A O   1 
ATOM   412  C  CB  . GLN   A 1 58  ? -29.088 2.589   -12.660 1.00 87.47  ? 78  GLN   A CB  1 
ATOM   413  C  CG  . GLN   A 1 58  ? -30.582 2.856   -12.477 1.00 92.05  ? 78  GLN   A CG  1 
ATOM   414  C  CD  . GLN   A 1 58  ? -31.137 3.888   -13.447 1.00 94.94  ? 78  GLN   A CD  1 
ATOM   415  O  OE1 . GLN   A 1 58  ? -30.502 4.231   -14.444 1.00 101.17 ? 78  GLN   A OE1 1 
ATOM   416  N  NE2 . GLN   A 1 58  ? -32.329 4.392   -13.151 1.00 97.66  ? 78  GLN   A NE2 1 
ATOM   417  N  N   . GLN   A 1 59  ? -26.959 -0.014  -13.945 1.00 77.88  ? 79  GLN   A N   1 
ATOM   418  C  CA  . GLN   A 1 59  ? -25.605 -0.512  -13.748 1.00 77.59  ? 79  GLN   A CA  1 
ATOM   419  C  C   . GLN   A 1 59  ? -24.848 -0.511  -15.067 1.00 76.99  ? 79  GLN   A C   1 
ATOM   420  O  O   . GLN   A 1 59  ? -25.239 -1.236  -15.990 1.00 73.29  ? 79  GLN   A O   1 
ATOM   421  C  CB  . GLN   A 1 59  ? -25.635 -1.917  -13.174 1.00 75.24  ? 79  GLN   A CB  1 
ATOM   422  C  CG  . GLN   A 1 59  ? -24.271 -2.575  -13.088 1.00 76.15  ? 79  GLN   A CG  1 
ATOM   423  C  CD  . GLN   A 1 59  ? -23.372 -1.914  -12.063 1.00 83.92  ? 79  GLN   A CD  1 
ATOM   424  O  OE1 . GLN   A 1 59  ? -22.311 -1.383  -12.397 1.00 82.42  ? 79  GLN   A OE1 1 
ATOM   425  N  NE2 . GLN   A 1 59  ? -23.791 -1.949  -10.802 1.00 83.80  ? 79  GLN   A NE2 1 
ATOM   426  N  N   . PRO   A 1 60  ? -23.771 0.264   -15.203 1.00 78.16  ? 80  PRO   A N   1 
ATOM   427  C  CA  . PRO   A 1 60  ? -22.980 0.216   -16.439 1.00 78.14  ? 80  PRO   A CA  1 
ATOM   428  C  C   . PRO   A 1 60  ? -22.109 -1.031  -16.465 1.00 80.96  ? 80  PRO   A C   1 
ATOM   429  O  O   . PRO   A 1 60  ? -21.437 -1.354  -15.483 1.00 81.72  ? 80  PRO   A O   1 
ATOM   430  C  CB  . PRO   A 1 60  ? -22.124 1.488   -16.372 1.00 79.23  ? 80  PRO   A CB  1 
ATOM   431  C  CG  . PRO   A 1 60  ? -22.643 2.276   -15.198 1.00 77.77  ? 80  PRO   A CG  1 
ATOM   432  C  CD  . PRO   A 1 60  ? -23.261 1.283   -14.273 1.00 77.22  ? 80  PRO   A CD  1 
ATOM   433  N  N   . VAL   A 1 61  ? -22.124 -1.733  -17.596 1.00 78.84  ? 81  VAL   A N   1 
ATOM   434  C  CA  . VAL   A 1 61  ? -21.287 -2.906  -17.815 1.00 77.44  ? 81  VAL   A CA  1 
ATOM   435  C  C   . VAL   A 1 61  ? -20.523 -2.700  -19.114 1.00 79.61  ? 81  VAL   A C   1 
ATOM   436  O  O   . VAL   A 1 61  ? -21.126 -2.381  -20.144 1.00 80.86  ? 81  VAL   A O   1 
ATOM   437  C  CB  . VAL   A 1 61  ? -22.117 -4.203  -17.873 1.00 77.60  ? 81  VAL   A CB  1 
ATOM   438  C  CG1 . VAL   A 1 61  ? -21.224 -5.389  -18.196 1.00 76.22  ? 81  VAL   A CG1 1 
ATOM   439  C  CG2 . VAL   A 1 61  ? -22.849 -4.431  -16.560 1.00 76.60  ? 81  VAL   A CG2 1 
ATOM   440  N  N   . LEU   A 1 62  ? -19.203 -2.877  -19.067 1.00 79.81  ? 82  LEU   A N   1 
ATOM   441  C  CA  . LEU   A 1 62  ? -18.336 -2.664  -20.224 1.00 83.55  ? 82  LEU   A CA  1 
ATOM   442  C  C   . LEU   A 1 62  ? -17.789 -4.009  -20.688 1.00 80.46  ? 82  LEU   A C   1 
ATOM   443  O  O   . LEU   A 1 62  ? -17.024 -4.658  -19.967 1.00 79.42  ? 82  LEU   A O   1 
ATOM   444  C  CB  . LEU   A 1 62  ? -17.195 -1.707  -19.889 1.00 80.26  ? 82  LEU   A CB  1 
ATOM   445  C  CG  . LEU   A 1 62  ? -16.203 -1.462  -21.028 1.00 80.64  ? 82  LEU   A CG  1 
ATOM   446  C  CD1 . LEU   A 1 62  ? -16.742 -0.434  -22.009 1.00 78.14  ? 82  LEU   A CD1 1 
ATOM   447  C  CD2 . LEU   A 1 62  ? -14.847 -1.037  -20.487 1.00 85.65  ? 82  LEU   A CD2 1 
ATOM   448  N  N   . ALA   A 1 63  ? -18.168 -4.418  -21.894 1.00 79.78  ? 83  ALA   A N   1 
ATOM   449  C  CA  . ALA   A 1 63  ? -17.682 -5.665  -22.465 1.00 83.90  ? 83  ALA   A CA  1 
ATOM   450  C  C   . ALA   A 1 63  ? -16.378 -5.416  -23.212 1.00 85.83  ? 83  ALA   A C   1 
ATOM   451  O  O   . ALA   A 1 63  ? -16.288 -4.493  -24.029 1.00 85.14  ? 83  ALA   A O   1 
ATOM   452  C  CB  . ALA   A 1 63  ? -18.725 -6.273  -23.400 1.00 77.80  ? 83  ALA   A CB  1 
ATOM   453  N  N   . ILE   A 1 64  ? -15.368 -6.236  -22.926 1.00 80.27  ? 84  ILE   A N   1 
ATOM   454  C  CA  . ILE   A 1 64  ? -14.060 -6.128  -23.561 1.00 85.97  ? 84  ILE   A CA  1 
ATOM   455  C  C   . ILE   A 1 64  ? -13.704 -7.478  -24.167 1.00 87.45  ? 84  ILE   A C   1 
ATOM   456  O  O   . ILE   A 1 64  ? -13.911 -8.521  -23.537 1.00 89.88  ? 84  ILE   A O   1 
ATOM   457  C  CB  . ILE   A 1 64  ? -12.974 -5.669  -22.567 1.00 90.29  ? 84  ILE   A CB  1 
ATOM   458  C  CG1 . ILE   A 1 64  ? -12.880 -6.629  -21.380 1.00 84.01  ? 84  ILE   A CG1 1 
ATOM   459  C  CG2 . ILE   A 1 64  ? -13.274 -4.269  -22.068 1.00 87.25  ? 84  ILE   A CG2 1 
ATOM   460  C  CD1 . ILE   A 1 64  ? -11.625 -6.456  -20.559 1.00 85.99  ? 84  ILE   A CD1 1 
ATOM   461  N  N   . THR   A 1 65  ? -13.178 -7.459  -25.390 1.00 89.31  ? 85  THR   A N   1 
ATOM   462  C  CA  . THR   A 1 65  ? -12.790 -8.679  -26.082 1.00 87.56  ? 85  THR   A CA  1 
ATOM   463  C  C   . THR   A 1 65  ? -11.318 -8.711  -26.470 1.00 90.31  ? 85  THR   A C   1 
ATOM   464  O  O   . THR   A 1 65  ? -10.853 -9.736  -26.983 1.00 92.08  ? 85  THR   A O   1 
ATOM   465  C  CB  . THR   A 1 65  ? -13.650 -8.882  -27.338 1.00 86.84  ? 85  THR   A CB  1 
ATOM   466  O  OG1 . THR   A 1 65  ? -13.515 -7.748  -28.207 1.00 88.36  ? 85  THR   A OG1 1 
ATOM   467  C  CG2 . THR   A 1 65  ? -15.111 -9.054  -26.957 1.00 81.87  ? 85  THR   A CG2 1 
ATOM   468  N  N   . ASP   A 1 66  ? -10.577 -7.635  -26.248 1.00 92.67  ? 86  ASP   A N   1 
ATOM   469  C  CA  . ASP   A 1 66  ? -9.160  -7.616  -26.589 1.00 91.14  ? 86  ASP   A CA  1 
ATOM   470  C  C   . ASP   A 1 66  ? -8.379  -8.470  -25.598 1.00 96.57  ? 86  ASP   A C   1 
ATOM   471  O  O   . ASP   A 1 66  ? -8.366  -8.157  -24.400 1.00 97.24  ? 86  ASP   A O   1 
ATOM   472  C  CB  . ASP   A 1 66  ? -8.643  -6.181  -26.601 1.00 92.97  ? 86  ASP   A CB  1 
ATOM   473  C  CG  . ASP   A 1 66  ? -7.162  -6.094  -26.907 1.00 97.68  ? 86  ASP   A CG  1 
ATOM   474  O  OD1 . ASP   A 1 66  ? -6.354  -6.367  -25.998 1.00 101.36 ? 86  ASP   A OD1 1 
ATOM   475  O  OD2 . ASP   A 1 66  ? -6.802  -5.758  -28.057 1.00 100.32 ? 86  ASP   A OD2 1 
ATOM   476  N  N   . PRO   A 1 67  ? -7.714  -9.542  -26.046 1.00 100.21 ? 87  PRO   A N   1 
ATOM   477  C  CA  . PRO   A 1 67  ? -7.057  -10.458 -25.096 1.00 97.43  ? 87  PRO   A CA  1 
ATOM   478  C  C   . PRO   A 1 67  ? -5.930  -9.826  -24.288 1.00 99.27  ? 87  PRO   A C   1 
ATOM   479  O  O   . PRO   A 1 67  ? -5.629  -10.327 -23.198 1.00 99.33  ? 87  PRO   A O   1 
ATOM   480  C  CB  . PRO   A 1 67  ? -6.538  -11.587 -26.001 1.00 95.32  ? 87  PRO   A CB  1 
ATOM   481  C  CG  . PRO   A 1 67  ? -6.452  -10.976 -27.364 1.00 97.61  ? 87  PRO   A CG  1 
ATOM   482  C  CD  . PRO   A 1 67  ? -7.573  -9.989  -27.441 1.00 97.02  ? 87  PRO   A CD  1 
ATOM   483  N  N   . ASP   A 1 68  ? -5.300  -8.752  -24.773 1.00 99.22  ? 88  ASP   A N   1 
ATOM   484  C  CA  . ASP   A 1 68  ? -4.342  -8.027  -23.940 1.00 102.95 ? 88  ASP   A CA  1 
ATOM   485  C  C   . ASP   A 1 68  ? -5.044  -7.352  -22.769 1.00 99.15  ? 88  ASP   A C   1 
ATOM   486  O  O   . ASP   A 1 68  ? -4.598  -7.455  -21.619 1.00 101.74 ? 88  ASP   A O   1 
ATOM   487  C  CB  . ASP   A 1 68  ? -3.583  -6.991  -24.773 1.00 102.89 ? 88  ASP   A CB  1 
ATOM   488  C  CG  . ASP   A 1 68  ? -2.196  -7.451  -25.158 1.00 110.07 ? 88  ASP   A CG  1 
ATOM   489  O  OD1 . ASP   A 1 68  ? -1.665  -8.361  -24.487 1.00 112.07 ? 88  ASP   A OD1 1 
ATOM   490  O  OD2 . ASP   A 1 68  ? -1.632  -6.895  -26.124 1.00 120.55 ? 88  ASP   A OD2 1 
ATOM   491  N  N   . MET   A 1 69  ? -6.151  -6.659  -23.049 1.00 101.54 ? 89  MET   A N   1 
ATOM   492  C  CA  . MET   A 1 69  ? -6.919  -5.980  -22.012 1.00 102.99 ? 89  MET   A CA  1 
ATOM   493  C  C   . MET   A 1 69  ? -7.615  -6.948  -21.066 1.00 97.34  ? 89  MET   A C   1 
ATOM   494  O  O   . MET   A 1 69  ? -7.905  -6.572  -19.925 1.00 92.41  ? 89  MET   A O   1 
ATOM   495  C  CB  . MET   A 1 69  ? -7.954  -5.058  -22.660 1.00 103.21 ? 89  MET   A CB  1 
ATOM   496  C  CG  . MET   A 1 69  ? -8.411  -3.932  -21.759 1.00 105.25 ? 89  MET   A CG  1 
ATOM   497  S  SD  . MET   A 1 69  ? -9.550  -2.790  -22.556 1.00 112.29 ? 89  MET   A SD  1 
ATOM   498  C  CE  . MET   A 1 69  ? -9.855  -3.637  -24.106 1.00 103.37 ? 89  MET   A CE  1 
ATOM   499  N  N   . ILE   A 1 70  ? -7.897  -8.172  -21.516 1.00 98.45  ? 90  ILE   A N   1 
ATOM   500  C  CA  . ILE   A 1 70  ? -8.456  -9.183  -20.627 1.00 96.19  ? 90  ILE   A CA  1 
ATOM   501  C  C   . ILE   A 1 70  ? -7.405  -9.652  -19.627 1.00 100.60 ? 90  ILE   A C   1 
ATOM   502  O  O   . ILE   A 1 70  ? -7.733  -9.982  -18.483 1.00 100.88 ? 90  ILE   A O   1 
ATOM   503  C  CB  . ILE   A 1 70  ? -9.031  -10.353 -21.451 1.00 91.30  ? 90  ILE   A CB  1 
ATOM   504  C  CG1 . ILE   A 1 70  ? -10.175 -9.860  -22.344 1.00 87.03  ? 90  ILE   A CG1 1 
ATOM   505  C  CG2 . ILE   A 1 70  ? -9.505  -11.495 -20.543 1.00 84.82  ? 90  ILE   A CG2 1 
ATOM   506  C  CD1 . ILE   A 1 70  ? -10.750 -10.924 -23.256 1.00 85.43  ? 90  ILE   A CD1 1 
ATOM   507  N  N   . LYS   A 1 71  ? -6.130  -9.684  -20.030 1.00 96.23  ? 91  LYS   A N   1 
ATOM   508  C  CA  . LYS   A 1 71  ? -5.078  -10.067 -19.092 1.00 96.75  ? 91  LYS   A CA  1 
ATOM   509  C  C   . LYS   A 1 71  ? -4.864  -8.982  -18.042 1.00 97.72  ? 91  LYS   A C   1 
ATOM   510  O  O   . LYS   A 1 71  ? -4.532  -9.278  -16.888 1.00 97.92  ? 91  LYS   A O   1 
ATOM   511  C  CB  . LYS   A 1 71  ? -3.775  -10.369 -19.835 1.00 97.51  ? 91  LYS   A CB  1 
ATOM   512  C  CG  . LYS   A 1 71  ? -2.611  -10.760 -18.920 1.00 98.16  ? 91  LYS   A CG  1 
ATOM   513  C  CD  . LYS   A 1 71  ? -1.465  -11.406 -19.695 1.00 93.90  ? 91  LYS   A CD  1 
ATOM   514  C  CE  . LYS   A 1 71  ? -0.655  -10.394 -20.485 1.00 105.02 ? 91  LYS   A CE  1 
ATOM   515  N  NZ  . LYS   A 1 71  ? 0.744   -10.321 -19.975 1.00 109.56 ? 91  LYS   A NZ  1 
ATOM   516  N  N   . THR   A 1 72  ? -5.046  -7.716  -18.424 1.00 96.50  ? 92  THR   A N   1 
ATOM   517  C  CA  . THR   A 1 72  ? -4.898  -6.634  -17.456 1.00 97.28  ? 92  THR   A CA  1 
ATOM   518  C  C   . THR   A 1 72  ? -5.962  -6.721  -16.370 1.00 99.37  ? 92  THR   A C   1 
ATOM   519  O  O   . THR   A 1 72  ? -5.687  -6.453  -15.194 1.00 100.74 ? 92  THR   A O   1 
ATOM   520  C  CB  . THR   A 1 72  ? -4.973  -5.283  -18.162 1.00 101.30 ? 92  THR   A CB  1 
ATOM   521  O  OG1 . THR   A 1 72  ? -4.222  -5.336  -19.380 1.00 101.92 ? 92  THR   A OG1 1 
ATOM   522  C  CG2 . THR   A 1 72  ? -4.398  -4.201  -17.270 1.00 104.66 ? 92  THR   A CG2 1 
ATOM   523  N  N   . VAL   A 1 73  ? -7.178  -7.113  -16.743 1.00 98.89  ? 93  VAL   A N   1 
ATOM   524  C  CA  . VAL   A 1 73  ? -8.271  -7.198  -15.782 1.00 93.79  ? 93  VAL   A CA  1 
ATOM   525  C  C   . VAL   A 1 73  ? -8.167  -8.475  -14.960 1.00 93.00  ? 93  VAL   A C   1 
ATOM   526  O  O   . VAL   A 1 73  ? -8.110  -8.439  -13.726 1.00 92.63  ? 93  VAL   A O   1 
ATOM   527  C  CB  . VAL   A 1 73  ? -9.625  -7.113  -16.507 1.00 92.64  ? 93  VAL   A CB  1 
ATOM   528  C  CG1 . VAL   A 1 73  ? -10.767 -7.164  -15.510 1.00 85.92  ? 93  VAL   A CG1 1 
ATOM   529  C  CG2 . VAL   A 1 73  ? -9.700  -5.849  -17.334 1.00 92.78  ? 93  VAL   A CG2 1 
ATOM   530  N  N   . LEU   A 1 74  ? -8.137  -9.626  -15.638 1.00 92.88  ? 94  LEU   A N   1 
ATOM   531  C  CA  . LEU   A 1 74  ? -8.225  -10.904 -14.936 1.00 90.79  ? 94  LEU   A CA  1 
ATOM   532  C  C   . LEU   A 1 74  ? -6.937  -11.243 -14.196 1.00 90.45  ? 94  LEU   A C   1 
ATOM   533  O  O   . LEU   A 1 74  ? -6.972  -11.992 -13.211 1.00 92.22  ? 94  LEU   A O   1 
ATOM   534  C  CB  . LEU   A 1 74  ? -8.571  -12.030 -15.909 1.00 83.33  ? 94  LEU   A CB  1 
ATOM   535  C  CG  . LEU   A 1 74  ? -9.942  -12.078 -16.588 1.00 85.96  ? 94  LEU   A CG  1 
ATOM   536  C  CD1 . LEU   A 1 74  ? -10.144 -13.443 -17.232 1.00 79.90  ? 94  LEU   A CD1 1 
ATOM   537  C  CD2 . LEU   A 1 74  ? -11.056 -11.790 -15.601 1.00 77.85  ? 94  LEU   A CD2 1 
ATOM   538  N  N   . VAL   A 1 75  ? -5.796  -10.716 -14.642 1.00 97.26  ? 95  VAL   A N   1 
ATOM   539  C  CA  . VAL   A 1 75  ? -4.507  -11.177 -14.132 1.00 96.70  ? 95  VAL   A CA  1 
ATOM   540  C  C   . VAL   A 1 75  ? -3.694  -10.039 -13.524 1.00 99.37  ? 95  VAL   A C   1 
ATOM   541  O  O   . VAL   A 1 75  ? -3.416  -10.039 -12.319 1.00 99.67  ? 95  VAL   A O   1 
ATOM   542  C  CB  . VAL   A 1 75  ? -3.703  -11.880 -15.241 1.00 97.27  ? 95  VAL   A CB  1 
ATOM   543  C  CG1 . VAL   A 1 75  ? -2.292  -12.156 -14.772 1.00 93.12  ? 95  VAL   A CG1 1 
ATOM   544  C  CG2 . VAL   A 1 75  ? -4.393  -13.170 -15.654 1.00 92.38  ? 95  VAL   A CG2 1 
ATOM   545  N  N   . LYS   A 1 76  ? -3.300  -9.069  -14.351 1.00 94.66  ? 96  LYS   A N   1 
ATOM   546  C  CA  . LYS   A 1 76  ? -2.365  -8.033  -13.923 1.00 100.95 ? 96  LYS   A CA  1 
ATOM   547  C  C   . LYS   A 1 76  ? -2.916  -7.188  -12.783 1.00 102.81 ? 96  LYS   A C   1 
ATOM   548  O  O   . LYS   A 1 76  ? -2.419  -7.259  -11.654 1.00 103.86 ? 96  LYS   A O   1 
ATOM   549  C  CB  . LYS   A 1 76  ? -1.991  -7.127  -15.099 1.00 99.22  ? 96  LYS   A CB  1 
ATOM   550  C  CG  . LYS   A 1 76  ? -1.125  -7.797  -16.147 1.00 105.46 ? 96  LYS   A CG  1 
ATOM   551  C  CD  . LYS   A 1 76  ? -0.853  -6.863  -17.309 1.00 115.22 ? 96  LYS   A CD  1 
ATOM   552  C  CE  . LYS   A 1 76  ? -0.031  -7.561  -18.372 1.00 120.23 ? 96  LYS   A CE  1 
ATOM   553  N  NZ  . LYS   A 1 76  ? -0.141  -6.882  -19.689 1.00 125.43 ? 96  LYS   A NZ  1 
ATOM   554  N  N   . GLU   A 1 77  ? -3.937  -6.379  -13.066 1.00 106.14 ? 97  GLU   A N   1 
ATOM   555  C  CA  . GLU   A 1 77  ? -4.512  -5.484  -12.070 1.00 103.28 ? 97  GLU   A CA  1 
ATOM   556  C  C   . GLU   A 1 77  ? -5.669  -6.118  -11.310 1.00 98.33  ? 97  GLU   A C   1 
ATOM   557  O  O   . GLU   A 1 77  ? -6.597  -5.408  -10.898 1.00 99.72  ? 97  GLU   A O   1 
ATOM   558  C  CB  . GLU   A 1 77  ? -4.952  -4.179  -12.734 1.00 102.93 ? 97  GLU   A CB  1 
ATOM   559  C  CG  . GLU   A 1 77  ? -3.873  -3.525  -13.588 1.00 106.10 ? 97  GLU   A CG  1 
ATOM   560  C  CD  . GLU   A 1 77  ? -2.667  -3.074  -12.781 1.00 110.45 ? 97  GLU   A CD  1 
ATOM   561  O  OE1 . GLU   A 1 77  ? -2.819  -2.825  -11.565 1.00 101.42 ? 97  GLU   A OE1 1 
ATOM   562  O  OE2 . GLU   A 1 77  ? -1.566  -2.967  -13.365 1.00 110.33 ? 97  GLU   A OE2 1 
ATOM   563  N  N   . CYS   A 1 78  ? -5.635  -7.438  -11.111 1.00 98.70  ? 98  CYS   A N   1 
ATOM   564  C  CA  . CYS   A 1 78  ? -6.684  -8.109  -10.347 1.00 98.60  ? 98  CYS   A CA  1 
ATOM   565  C  C   . CYS   A 1 78  ? -6.683  -7.651  -8.894  1.00 100.66 ? 98  CYS   A C   1 
ATOM   566  O  O   . CYS   A 1 78  ? -7.733  -7.321  -8.333  1.00 98.76  ? 98  CYS   A O   1 
ATOM   567  C  CB  . CYS   A 1 78  ? -6.503  -9.625  -10.430 1.00 94.18  ? 98  CYS   A CB  1 
ATOM   568  S  SG  . CYS   A 1 78  ? -7.473  -10.565 -9.222  1.00 103.75 ? 98  CYS   A SG  1 
ATOM   569  N  N   . TYR   A 1 79  ? -5.507  -7.624  -8.268  1.00 119.12 ? 99  TYR   A N   1 
ATOM   570  C  CA  . TYR   A 1 79  ? -5.410  -7.241  -6.866  1.00 117.80 ? 99  TYR   A CA  1 
ATOM   571  C  C   . TYR   A 1 79  ? -5.557  -5.744  -6.643  1.00 114.82 ? 99  TYR   A C   1 
ATOM   572  O  O   . TYR   A 1 79  ? -5.886  -5.330  -5.527  1.00 114.67 ? 99  TYR   A O   1 
ATOM   573  C  CB  . TYR   A 1 79  ? -4.076  -7.713  -6.285  1.00 123.34 ? 99  TYR   A CB  1 
ATOM   574  C  CG  . TYR   A 1 79  ? -4.047  -9.190  -5.979  1.00 126.76 ? 99  TYR   A CG  1 
ATOM   575  C  CD1 . TYR   A 1 79  ? -4.620  -9.683  -4.817  1.00 133.85 ? 99  TYR   A CD1 1 
ATOM   576  C  CD2 . TYR   A 1 79  ? -3.454  -10.092 -6.850  1.00 126.92 ? 99  TYR   A CD2 1 
ATOM   577  C  CE1 . TYR   A 1 79  ? -4.602  -11.032 -4.534  1.00 135.04 ? 99  TYR   A CE1 1 
ATOM   578  C  CE2 . TYR   A 1 79  ? -3.428  -11.446 -6.567  1.00 134.15 ? 99  TYR   A CE2 1 
ATOM   579  C  CZ  . TYR   A 1 79  ? -4.006  -11.910 -5.406  1.00 135.37 ? 99  TYR   A CZ  1 
ATOM   580  O  OH  . TYR   A 1 79  ? -3.992  -13.255 -5.111  1.00 127.79 ? 99  TYR   A OH  1 
ATOM   581  N  N   . SER   A 1 80  ? -5.334  -4.926  -7.669  1.00 104.99 ? 100 SER   A N   1 
ATOM   582  C  CA  . SER   A 1 80  ? -5.323  -3.481  -7.490  1.00 102.64 ? 100 SER   A CA  1 
ATOM   583  C  C   . SER   A 1 80  ? -6.586  -2.786  -7.979  1.00 103.78 ? 100 SER   A C   1 
ATOM   584  O  O   . SER   A 1 80  ? -6.940  -1.733  -7.438  1.00 106.70 ? 100 SER   A O   1 
ATOM   585  C  CB  . SER   A 1 80  ? -4.105  -2.872  -8.195  1.00 108.78 ? 100 SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 80  ? -3.849  -3.515  -9.432  1.00 108.39 ? 100 SER   A OG  1 
ATOM   587  N  N   . VAL   A 1 81  ? -7.279  -3.330  -8.982  1.00 104.64 ? 101 VAL   A N   1 
ATOM   588  C  CA  . VAL   A 1 81  ? -8.436  -2.641  -9.551  1.00 100.16 ? 101 VAL   A CA  1 
ATOM   589  C  C   . VAL   A 1 81  ? -9.609  -3.597  -9.751  1.00 96.29  ? 101 VAL   A C   1 
ATOM   590  O  O   . VAL   A 1 81  ? -10.768 -3.223  -9.544  1.00 92.23  ? 101 VAL   A O   1 
ATOM   591  C  CB  . VAL   A 1 81  ? -8.074  -1.948  -10.881 1.00 100.62 ? 101 VAL   A CB  1 
ATOM   592  C  CG1 . VAL   A 1 81  ? -9.286  -1.231  -11.453 1.00 98.52  ? 101 VAL   A CG1 1 
ATOM   593  C  CG2 . VAL   A 1 81  ? -6.927  -0.961  -10.690 1.00 104.75 ? 101 VAL   A CG2 1 
ATOM   594  N  N   . PHE   A 1 82  ? -9.328  -4.834  -10.160 1.00 99.52  ? 102 PHE   A N   1 
ATOM   595  C  CA  . PHE   A 1 82  ? -10.404 -5.738  -10.551 1.00 92.93  ? 102 PHE   A CA  1 
ATOM   596  C  C   . PHE   A 1 82  ? -10.460 -6.984  -9.675  1.00 96.22  ? 102 PHE   A C   1 
ATOM   597  O  O   . PHE   A 1 82  ? -10.237 -8.100  -10.155 1.00 98.36  ? 102 PHE   A O   1 
ATOM   598  C  CB  . PHE   A 1 82  ? -10.242 -6.132  -12.020 1.00 91.54  ? 102 PHE   A CB  1 
ATOM   599  C  CG  . PHE   A 1 82  ? -10.173 -4.958  -12.959 1.00 93.18  ? 102 PHE   A CG  1 
ATOM   600  C  CD1 . PHE   A 1 82  ? -11.325 -4.288  -13.332 1.00 92.27  ? 102 PHE   A CD1 1 
ATOM   601  C  CD2 . PHE   A 1 82  ? -8.959  -4.533  -13.473 1.00 98.15  ? 102 PHE   A CD2 1 
ATOM   602  C  CE1 . PHE   A 1 82  ? -11.268 -3.210  -14.196 1.00 92.37  ? 102 PHE   A CE1 1 
ATOM   603  C  CE2 . PHE   A 1 82  ? -8.896  -3.455  -14.340 1.00 97.42  ? 102 PHE   A CE2 1 
ATOM   604  C  CZ  . PHE   A 1 82  ? -10.053 -2.794  -14.702 1.00 93.80  ? 102 PHE   A CZ  1 
ATOM   605  N  N   . THR   A 1 83  ? -10.793 -6.810  -8.396  1.00 95.56  ? 103 THR   A N   1 
ATOM   606  C  CA  . THR   A 1 83  ? -10.696 -7.897  -7.427  1.00 96.18  ? 103 THR   A CA  1 
ATOM   607  C  C   . THR   A 1 83  ? -12.005 -8.654  -7.233  1.00 88.53  ? 103 THR   A C   1 
ATOM   608  O  O   . THR   A 1 83  ? -11.978 -9.839  -6.880  1.00 85.88  ? 103 THR   A O   1 
ATOM   609  C  CB  . THR   A 1 83  ? -10.210 -7.344  -6.082  1.00 97.69  ? 103 THR   A CB  1 
ATOM   610  O  OG1 . THR   A 1 83  ? -9.029  -6.560  -6.293  1.00 99.93  ? 103 THR   A OG1 1 
ATOM   611  C  CG2 . THR   A 1 83  ? -9.881  -8.467  -5.105  1.00 96.43  ? 103 THR   A CG2 1 
ATOM   612  N  N   . ASN   A 1 84  ? -13.146 -8.018  -7.471  1.00 90.08  ? 104 ASN   A N   1 
ATOM   613  C  CA  . ASN   A 1 84  ? -14.428 -8.571  -7.065  1.00 91.46  ? 104 ASN   A CA  1 
ATOM   614  C  C   . ASN   A 1 84  ? -15.357 -8.742  -8.259  1.00 86.55  ? 104 ASN   A C   1 
ATOM   615  O  O   . ASN   A 1 84  ? -15.139 -8.176  -9.333  1.00 87.77  ? 104 ASN   A O   1 
ATOM   616  C  CB  . ASN   A 1 84  ? -15.096 -7.673  -6.016  1.00 87.45  ? 104 ASN   A CB  1 
ATOM   617  C  CG  . ASN   A 1 84  ? -14.095 -7.042  -5.070  1.00 94.05  ? 104 ASN   A CG  1 
ATOM   618  O  OD1 . ASN   A 1 84  ? -13.195 -7.711  -4.558  1.00 93.55  ? 104 ASN   A OD1 1 
ATOM   619  N  ND2 . ASN   A 1 84  ? -14.239 -5.741  -4.841  1.00 97.80  ? 104 ASN   A ND2 1 
ATOM   620  N  N   . ARG   A 1 85  ? -16.397 -9.543  -8.050  1.00 86.75  ? 105 ARG   A N   1 
ATOM   621  C  CA  . ARG   A 1 85  ? -17.502 -9.688  -8.985  1.00 85.35  ? 105 ARG   A CA  1 
ATOM   622  C  C   . ARG   A 1 85  ? -18.665 -8.805  -8.538  1.00 83.70  ? 105 ARG   A C   1 
ATOM   623  O  O   . ARG   A 1 85  ? -18.688 -8.289  -7.418  1.00 89.95  ? 105 ARG   A O   1 
ATOM   624  C  CB  . ARG   A 1 85  ? -17.931 -11.155 -9.090  1.00 79.86  ? 105 ARG   A CB  1 
ATOM   625  C  CG  . ARG   A 1 85  ? -16.788 -12.101 -9.431  1.00 79.02  ? 105 ARG   A CG  1 
ATOM   626  C  CD  . ARG   A 1 85  ? -17.287 -13.497 -9.769  1.00 79.26  ? 105 ARG   A CD  1 
ATOM   627  N  NE  . ARG   A 1 85  ? -16.212 -14.338 -10.282 1.00 80.45  ? 105 ARG   A NE  1 
ATOM   628  C  CZ  . ARG   A 1 85  ? -15.480 -15.156 -9.539  1.00 80.75  ? 105 ARG   A CZ  1 
ATOM   629  N  NH1 . ARG   A 1 85  ? -15.700 -15.293 -8.242  1.00 80.01  ? 105 ARG   A NH1 1 
ATOM   630  N  NH2 . ARG   A 1 85  ? -14.504 -15.855 -10.111 1.00 78.85  ? 105 ARG   A NH2 1 
ATOM   631  N  N   . ARG   A 1 86  ? -19.637 -8.630  -9.432  1.00 84.22  ? 106 ARG   A N   1 
ATOM   632  C  CA  . ARG   A 1 86  ? -20.674 -7.632  -9.193  1.00 90.23  ? 106 ARG   A CA  1 
ATOM   633  C  C   . ARG   A 1 86  ? -21.547 -8.044  -8.008  1.00 92.43  ? 106 ARG   A C   1 
ATOM   634  O  O   . ARG   A 1 86  ? -21.785 -9.238  -7.794  1.00 90.60  ? 106 ARG   A O   1 
ATOM   635  C  CB  . ARG   A 1 86  ? -21.529 -7.414  -10.448 1.00 83.56  ? 106 ARG   A CB  1 
ATOM   636  C  CG  . ARG   A 1 86  ? -22.838 -8.182  -10.500 1.00 85.51  ? 106 ARG   A CG  1 
ATOM   637  C  CD  . ARG   A 1 86  ? -23.780 -7.580  -11.534 1.00 81.99  ? 106 ARG   A CD  1 
ATOM   638  N  NE  . ARG   A 1 86  ? -23.371 -7.880  -12.902 1.00 83.04  ? 106 ARG   A NE  1 
ATOM   639  C  CZ  . ARG   A 1 86  ? -23.949 -7.373  -13.983 1.00 83.90  ? 106 ARG   A CZ  1 
ATOM   640  N  NH1 . ARG   A 1 86  ? -24.928 -6.486  -13.894 1.00 80.64  ? 106 ARG   A NH1 1 
ATOM   641  N  NH2 . ARG   A 1 86  ? -23.537 -7.771  -15.185 1.00 80.63  ? 106 ARG   A NH2 1 
ATOM   642  N  N   . PRO   A 1 87  ? -22.009 -7.081  -7.207  1.00 90.40  ? 107 PRO   A N   1 
ATOM   643  C  CA  . PRO   A 1 87  ? -22.783 -7.421  -6.007  1.00 93.04  ? 107 PRO   A CA  1 
ATOM   644  C  C   . PRO   A 1 87  ? -24.003 -8.268  -6.333  1.00 99.72  ? 107 PRO   A C   1 
ATOM   645  O  O   . PRO   A 1 87  ? -24.624 -8.136  -7.390  1.00 101.39 ? 107 PRO   A O   1 
ATOM   646  C  CB  . PRO   A 1 87  ? -23.181 -6.052  -5.446  1.00 100.32 ? 107 PRO   A CB  1 
ATOM   647  C  CG  . PRO   A 1 87  ? -22.093 -5.139  -5.911  1.00 94.07  ? 107 PRO   A CG  1 
ATOM   648  C  CD  . PRO   A 1 87  ? -21.696 -5.643  -7.274  1.00 94.22  ? 107 PRO   A CD  1 
ATOM   649  N  N   . PHE   A 1 88  ? -24.343 -9.143  -5.393  1.00 106.87 ? 108 PHE   A N   1 
ATOM   650  C  CA  . PHE   A 1 88  ? -25.321 -10.201 -5.625  1.00 114.39 ? 108 PHE   A CA  1 
ATOM   651  C  C   . PHE   A 1 88  ? -26.027 -10.448 -4.301  1.00 124.75 ? 108 PHE   A C   1 
ATOM   652  O  O   . PHE   A 1 88  ? -25.423 -10.992 -3.373  1.00 124.88 ? 108 PHE   A O   1 
ATOM   653  C  CB  . PHE   A 1 88  ? -24.620 -11.455 -6.150  1.00 115.44 ? 108 PHE   A CB  1 
ATOM   654  C  CG  . PHE   A 1 88  ? -25.504 -12.662 -6.269  1.00 122.05 ? 108 PHE   A CG  1 
ATOM   655  C  CD1 . PHE   A 1 88  ? -26.643 -12.637 -7.055  1.00 125.96 ? 108 PHE   A CD1 1 
ATOM   656  C  CD2 . PHE   A 1 88  ? -25.165 -13.842 -5.624  1.00 123.29 ? 108 PHE   A CD2 1 
ATOM   657  C  CE1 . PHE   A 1 88  ? -27.446 -13.761 -7.172  1.00 129.79 ? 108 PHE   A CE1 1 
ATOM   658  C  CE2 . PHE   A 1 88  ? -25.960 -14.967 -5.737  1.00 128.44 ? 108 PHE   A CE2 1 
ATOM   659  C  CZ  . PHE   A 1 88  ? -27.101 -14.927 -6.512  1.00 129.20 ? 108 PHE   A CZ  1 
ATOM   660  N  N   . GLY   A 1 89  ? -27.285 -10.018 -4.202  1.00 134.70 ? 109 GLY   A N   1 
ATOM   661  C  CA  . GLY   A 1 89  ? -28.028 -10.114 -2.967  1.00 128.82 ? 109 GLY   A CA  1 
ATOM   662  C  C   . GLY   A 1 89  ? -29.526 -10.196 -3.187  1.00 120.90 ? 109 GLY   A C   1 
ATOM   663  O  O   . GLY   A 1 89  ? -30.028 -9.951  -4.288  1.00 119.90 ? 109 GLY   A O   1 
ATOM   664  N  N   . PRO   A 1 90  ? -30.279 -10.537 -2.130  1.00 120.40 ? 110 PRO   A N   1 
ATOM   665  C  CA  . PRO   A 1 90  ? -29.844 -10.766 -0.746  1.00 120.01 ? 110 PRO   A CA  1 
ATOM   666  C  C   . PRO   A 1 90  ? -29.217 -12.145 -0.532  1.00 127.61 ? 110 PRO   A C   1 
ATOM   667  O  O   . PRO   A 1 90  ? -29.687 -13.139 -1.078  1.00 128.00 ? 110 PRO   A O   1 
ATOM   668  C  CB  . PRO   A 1 90  ? -31.147 -10.596 0.046   1.00 116.99 ? 110 PRO   A CB  1 
ATOM   669  C  CG  . PRO   A 1 90  ? -32.257 -10.963 -0.920  1.00 118.55 ? 110 PRO   A CG  1 
ATOM   670  C  CD  . PRO   A 1 90  ? -31.690 -10.909 -2.323  1.00 121.30 ? 110 PRO   A CD  1 
ATOM   671  N  N   . VAL   A 1 91  ? -28.155 -12.229 0.267   1.00 123.47 ? 111 VAL   A N   1 
ATOM   672  C  CA  . VAL   A 1 91  ? -27.425 -13.478 0.442   1.00 118.51 ? 111 VAL   A CA  1 
ATOM   673  C  C   . VAL   A 1 91  ? -27.336 -13.927 1.894   1.00 118.47 ? 111 VAL   A C   1 
ATOM   674  O  O   . VAL   A 1 91  ? -27.026 -15.105 2.139   1.00 123.30 ? 111 VAL   A O   1 
ATOM   675  C  CB  . VAL   A 1 91  ? -26.011 -13.382 -0.167  1.00 116.62 ? 111 VAL   A CB  1 
ATOM   676  C  CG1 . VAL   A 1 91  ? -26.080 -13.489 -1.678  1.00 117.20 ? 111 VAL   A CG1 1 
ATOM   677  C  CG2 . VAL   A 1 91  ? -25.341 -12.081 0.251   1.00 112.95 ? 111 VAL   A CG2 1 
ATOM   678  N  N   . GLY   A 1 92  ? -27.577 -13.049 2.866   1.00 120.61 ? 112 GLY   A N   1 
ATOM   679  C  CA  . GLY   A 1 92  ? -27.515 -13.466 4.259   1.00 117.44 ? 112 GLY   A CA  1 
ATOM   680  C  C   . GLY   A 1 92  ? -26.113 -13.883 4.666   1.00 119.20 ? 112 GLY   A C   1 
ATOM   681  O  O   . GLY   A 1 92  ? -25.121 -13.214 4.355   1.00 116.95 ? 112 GLY   A O   1 
ATOM   682  N  N   . PHE   A 1 93  ? -26.029 -15.015 5.369   1.00 110.94 ? 113 PHE   A N   1 
ATOM   683  C  CA  . PHE   A 1 93  ? -24.752 -15.516 5.865   1.00 108.87 ? 113 PHE   A CA  1 
ATOM   684  C  C   . PHE   A 1 93  ? -23.841 -16.026 4.756   1.00 105.70 ? 113 PHE   A C   1 
ATOM   685  O  O   . PHE   A 1 93  ? -22.669 -16.312 5.026   1.00 106.31 ? 113 PHE   A O   1 
ATOM   686  C  CB  . PHE   A 1 93  ? -24.983 -16.633 6.883   1.00 111.89 ? 113 PHE   A CB  1 
ATOM   687  C  CG  . PHE   A 1 93  ? -25.476 -17.910 6.274   1.00 109.17 ? 113 PHE   A CG  1 
ATOM   688  C  CD1 . PHE   A 1 93  ? -26.811 -18.062 5.946   1.00 110.94 ? 113 PHE   A CD1 1 
ATOM   689  C  CD2 . PHE   A 1 93  ? -24.605 -18.958 6.023   1.00 108.82 ? 113 PHE   A CD2 1 
ATOM   690  C  CE1 . PHE   A 1 93  ? -27.267 -19.230 5.383   1.00 116.55 ? 113 PHE   A CE1 1 
ATOM   691  C  CE2 . PHE   A 1 93  ? -25.056 -20.129 5.460   1.00 113.29 ? 113 PHE   A CE2 1 
ATOM   692  C  CZ  . PHE   A 1 93  ? -26.387 -20.263 5.141   1.00 122.37 ? 113 PHE   A CZ  1 
ATOM   693  N  N   . MET   A 1 94  ? -24.345 -16.164 3.530   1.00 106.27 ? 114 MET   A N   1 
ATOM   694  C  CA  . MET   A 1 94  ? -23.513 -16.525 2.390   1.00 105.99 ? 114 MET   A CA  1 
ATOM   695  C  C   . MET   A 1 94  ? -22.693 -15.349 1.874   1.00 106.30 ? 114 MET   A C   1 
ATOM   696  O  O   . MET   A 1 94  ? -22.085 -15.450 0.801   1.00 97.91  ? 114 MET   A O   1 
ATOM   697  C  CB  . MET   A 1 94  ? -24.381 -17.108 1.269   1.00 107.96 ? 114 MET   A CB  1 
ATOM   698  C  CG  . MET   A 1 94  ? -24.962 -18.483 1.591   1.00 106.03 ? 114 MET   A CG  1 
ATOM   699  S  SD  . MET   A 1 94  ? -23.772 -19.834 1.448   1.00 111.09 ? 114 MET   A SD  1 
ATOM   700  C  CE  . MET   A 1 94  ? -23.657 -19.997 -0.332  1.00 97.94  ? 114 MET   A CE  1 
ATOM   701  N  N   . LYS   A 1 95  ? -22.672 -14.239 2.618   1.00 103.15 ? 115 LYS   A N   1 
ATOM   702  C  CA  . LYS   A 1 95  ? -21.725 -13.165 2.347   1.00 100.12 ? 115 LYS   A CA  1 
ATOM   703  C  C   . LYS   A 1 95  ? -20.287 -13.657 2.435   1.00 98.29  ? 115 LYS   A C   1 
ATOM   704  O  O   . LYS   A 1 95  ? -19.392 -13.078 1.808   1.00 96.76  ? 115 LYS   A O   1 
ATOM   705  C  CB  . LYS   A 1 95  ? -21.949 -12.021 3.335   1.00 102.03 ? 115 LYS   A CB  1 
ATOM   706  C  CG  . LYS   A 1 95  ? -22.021 -12.488 4.787   1.00 105.39 ? 115 LYS   A CG  1 
ATOM   707  C  CD  . LYS   A 1 95  ? -22.125 -11.319 5.751   1.00 104.90 ? 115 LYS   A CD  1 
ATOM   708  C  CE  . LYS   A 1 95  ? -20.834 -11.131 6.537   1.00 112.79 ? 115 LYS   A CE  1 
ATOM   709  N  NZ  . LYS   A 1 95  ? -20.609 -12.218 7.537   1.00 119.37 ? 115 LYS   A NZ  1 
ATOM   710  N  N   . SER   A 1 96  ? -20.048 -14.717 3.205   1.00 104.07 ? 116 SER   A N   1 
ATOM   711  C  CA  . SER   A 1 96  ? -18.709 -15.240 3.440   1.00 100.59 ? 116 SER   A CA  1 
ATOM   712  C  C   . SER   A 1 96  ? -18.326 -16.363 2.486   1.00 99.31  ? 116 SER   A C   1 
ATOM   713  O  O   . SER   A 1 96  ? -17.221 -16.900 2.604   1.00 100.96 ? 116 SER   A O   1 
ATOM   714  C  CB  . SER   A 1 96  ? -18.588 -15.733 4.886   1.00 111.26 ? 116 SER   A CB  1 
ATOM   715  O  OG  . SER   A 1 96  ? -18.781 -14.671 5.804   1.00 112.07 ? 116 SER   A OG  1 
ATOM   716  N  N   . ALA   A 1 97  ? -19.205 -16.738 1.559   1.00 98.23  ? 117 ALA   A N   1 
ATOM   717  C  CA  . ALA   A 1 97  ? -18.842 -17.728 0.555   1.00 96.22  ? 117 ALA   A CA  1 
ATOM   718  C  C   . ALA   A 1 97  ? -17.701 -17.196 -0.302  1.00 91.68  ? 117 ALA   A C   1 
ATOM   719  O  O   . ALA   A 1 97  ? -17.654 -16.007 -0.628  1.00 93.39  ? 117 ALA   A O   1 
ATOM   720  C  CB  . ALA   A 1 97  ? -20.050 -18.071 -0.316  1.00 96.05  ? 117 ALA   A CB  1 
ATOM   721  N  N   . ILE   A 1 98  ? -16.773 -18.086 -0.664  1.00 89.83  ? 118 ILE   A N   1 
ATOM   722  C  CA  . ILE   A 1 98  ? -15.550 -17.643 -1.330  1.00 90.04  ? 118 ILE   A CA  1 
ATOM   723  C  C   . ILE   A 1 98  ? -15.861 -16.982 -2.667  1.00 90.82  ? 118 ILE   A C   1 
ATOM   724  O  O   . ILE   A 1 98  ? -15.180 -16.031 -3.072  1.00 89.35  ? 118 ILE   A O   1 
ATOM   725  C  CB  . ILE   A 1 98  ? -14.571 -18.825 -1.490  1.00 90.82  ? 118 ILE   A CB  1 
ATOM   726  C  CG1 . ILE   A 1 98  ? -13.267 -18.354 -2.138  1.00 88.94  ? 118 ILE   A CG1 1 
ATOM   727  C  CG2 . ILE   A 1 98  ? -15.202 -19.940 -2.301  1.00 85.62  ? 118 ILE   A CG2 1 
ATOM   728  C  CD1 . ILE   A 1 98  ? -12.242 -19.450 -2.318  1.00 87.99  ? 118 ILE   A CD1 1 
ATOM   729  N  N   . SER   A 1 99  ? -16.897 -17.453 -3.366  1.00 87.10  ? 119 SER   A N   1 
ATOM   730  C  CA  . SER   A 1 99  ? -17.260 -16.874 -4.653  1.00 87.37  ? 119 SER   A CA  1 
ATOM   731  C  C   . SER   A 1 99  ? -17.979 -15.537 -4.516  1.00 89.18  ? 119 SER   A C   1 
ATOM   732  O  O   . SER   A 1 99  ? -18.100 -14.808 -5.507  1.00 86.98  ? 119 SER   A O   1 
ATOM   733  C  CB  . SER   A 1 99  ? -18.139 -17.850 -5.434  1.00 90.88  ? 119 SER   A CB  1 
ATOM   734  O  OG  . SER   A 1 99  ? -19.238 -18.270 -4.647  1.00 93.81  ? 119 SER   A OG  1 
ATOM   735  N  N   . ILE   A 1 100 ? -18.453 -15.204 -3.319  1.00 91.42  ? 120 ILE   A N   1 
ATOM   736  C  CA  . ILE   A 1 100 ? -19.189 -13.969 -3.090  1.00 87.34  ? 120 ILE   A CA  1 
ATOM   737  C  C   . ILE   A 1 100 ? -18.379 -12.955 -2.284  1.00 88.54  ? 120 ILE   A C   1 
ATOM   738  O  O   . ILE   A 1 100 ? -18.692 -11.755 -2.335  1.00 89.27  ? 120 ILE   A O   1 
ATOM   739  C  CB  . ILE   A 1 100 ? -20.542 -14.276 -2.408  1.00 92.90  ? 120 ILE   A CB  1 
ATOM   740  C  CG1 . ILE   A 1 100 ? -21.388 -15.164 -3.329  1.00 97.96  ? 120 ILE   A CG1 1 
ATOM   741  C  CG2 . ILE   A 1 100 ? -21.325 -13.012 -2.055  1.00 94.30  ? 120 ILE   A CG2 1 
ATOM   742  C  CD1 . ILE   A 1 100 ? -22.361 -16.069 -2.602  1.00 106.34 ? 120 ILE   A CD1 1 
ATOM   743  N  N   . ALA   A 1 101 ? -17.311 -13.379 -1.608  1.00 93.53  ? 121 ALA   A N   1 
ATOM   744  C  CA  . ALA   A 1 101 ? -16.492 -12.485 -0.804  1.00 92.94  ? 121 ALA   A CA  1 
ATOM   745  C  C   . ALA   A 1 101 ? -15.760 -11.472 -1.685  1.00 93.12  ? 121 ALA   A C   1 
ATOM   746  O  O   . ALA   A 1 101 ? -15.710 -11.586 -2.913  1.00 93.79  ? 121 ALA   A O   1 
ATOM   747  C  CB  . ALA   A 1 101 ? -15.489 -13.282 0.028   1.00 95.62  ? 121 ALA   A CB  1 
ATOM   748  N  N   . GLU   A 1 102 ? -15.172 -10.467 -1.032  1.00 95.95  ? 122 GLU   A N   1 
ATOM   749  C  CA  . GLU   A 1 102 ? -14.523 -9.362  -1.725  1.00 96.86  ? 122 GLU   A CA  1 
ATOM   750  C  C   . GLU   A 1 102 ? -13.244 -8.954  -1.007  1.00 101.94 ? 122 GLU   A C   1 
ATOM   751  O  O   . GLU   A 1 102 ? -13.150 -9.028  0.222   1.00 103.77 ? 122 GLU   A O   1 
ATOM   752  C  CB  . GLU   A 1 102 ? -15.440 -8.135  -1.826  1.00 94.97  ? 122 GLU   A CB  1 
ATOM   753  C  CG  . GLU   A 1 102 ? -16.679 -8.321  -2.678  1.00 94.98  ? 122 GLU   A CG  1 
ATOM   754  C  CD  . GLU   A 1 102 ? -17.674 -7.189  -2.504  1.00 92.94  ? 122 GLU   A CD  1 
ATOM   755  O  OE1 . GLU   A 1 102 ? -17.476 -6.359  -1.592  1.00 99.95  ? 122 GLU   A OE1 1 
ATOM   756  O  OE2 . GLU   A 1 102 ? -18.655 -7.131  -3.275  1.00 97.98  ? 122 GLU   A OE2 1 
ATOM   757  N  N   . ASP   A 1 103 ? -12.265 -8.513  -1.798  1.00 97.66  ? 123 ASP   A N   1 
ATOM   758  C  CA  . ASP   A 1 103 ? -11.078 -7.796  -1.320  1.00 102.01 ? 123 ASP   A CA  1 
ATOM   759  C  C   . ASP   A 1 103 ? -10.291 -8.686  -0.365  1.00 103.18 ? 123 ASP   A C   1 
ATOM   760  O  O   . ASP   A 1 103 ? -9.906  -9.799  -0.763  1.00 105.55 ? 123 ASP   A O   1 
ATOM   761  C  CB  . ASP   A 1 103 ? -11.530 -6.451  -0.750  1.00 104.48 ? 123 ASP   A CB  1 
ATOM   762  C  CG  . ASP   A 1 103 ? -11.935 -5.466  -1.833  1.00 100.30 ? 123 ASP   A CG  1 
ATOM   763  O  OD1 . ASP   A 1 103 ? -11.076 -5.102  -2.665  1.00 104.19 ? 123 ASP   A OD1 1 
ATOM   764  O  OD2 . ASP   A 1 103 ? -13.117 -5.066  -1.860  1.00 103.29 ? 123 ASP   A OD2 1 
ATOM   765  N  N   . GLU   A 1 104 ? -10.021 -8.259  0.871   1.00 102.76 ? 124 GLU   A N   1 
ATOM   766  C  CA  . GLU   A 1 104 ? -9.129  -9.019  1.739   1.00 107.99 ? 124 GLU   A CA  1 
ATOM   767  C  C   . GLU   A 1 104 ? -9.802  -10.268 2.285   1.00 107.66 ? 124 GLU   A C   1 
ATOM   768  O  O   . GLU   A 1 104 ? -9.125  -11.267 2.555   1.00 109.67 ? 124 GLU   A O   1 
ATOM   769  C  CB  . GLU   A 1 104 ? -8.642  -8.137  2.886   1.00 113.10 ? 124 GLU   A CB  1 
ATOM   770  C  CG  . GLU   A 1 104 ? -7.869  -6.918  2.428   1.00 114.83 ? 124 GLU   A CG  1 
ATOM   771  C  CD  . GLU   A 1 104 ? -6.603  -7.288  1.686   1.00 111.76 ? 124 GLU   A CD  1 
ATOM   772  O  OE1 . GLU   A 1 104 ? -5.818  -8.100  2.221   1.00 112.25 ? 124 GLU   A OE1 1 
ATOM   773  O  OE2 . GLU   A 1 104 ? -6.399  -6.777  0.564   1.00 110.05 ? 124 GLU   A OE2 1 
ATOM   774  N  N   . GLU   A 1 105 ? -11.123 -10.227 2.462   1.00 107.18 ? 125 GLU   A N   1 
ATOM   775  C  CA  . GLU   A 1 105 ? -11.840 -11.382 2.991   1.00 107.97 ? 125 GLU   A CA  1 
ATOM   776  C  C   . GLU   A 1 105 ? -11.793 -12.550 2.015   1.00 104.40 ? 125 GLU   A C   1 
ATOM   777  O  O   . GLU   A 1 105 ? -11.654 -13.706 2.429   1.00 107.71 ? 125 GLU   A O   1 
ATOM   778  C  CB  . GLU   A 1 105 ? -13.282 -10.992 3.316   1.00 109.54 ? 125 GLU   A CB  1 
ATOM   779  C  CG  . GLU   A 1 105 ? -13.440 -10.187 4.611   1.00 123.46 ? 125 GLU   A CG  1 
ATOM   780  C  CD  . GLU   A 1 105 ? -12.718 -8.845  4.584   1.00 120.07 ? 125 GLU   A CD  1 
ATOM   781  O  OE1 . GLU   A 1 105 ? -12.373 -8.371  3.480   1.00 117.43 ? 125 GLU   A OE1 1 
ATOM   782  O  OE2 . GLU   A 1 105 ? -12.494 -8.267  5.670   1.00 124.99 ? 125 GLU   A OE2 1 
ATOM   783  N  N   . TRP   A 1 106 ? -11.897 -12.264 0.715   1.00 104.69 ? 126 TRP   A N   1 
ATOM   784  C  CA  . TRP   A 1 106 ? -11.681 -13.298 -0.292  1.00 97.16  ? 126 TRP   A CA  1 
ATOM   785  C  C   . TRP   A 1 106 ? -10.252 -13.818 -0.238  1.00 96.74  ? 126 TRP   A C   1 
ATOM   786  O  O   . TRP   A 1 106 ? -10.019 -15.032 -0.233  1.00 96.71  ? 126 TRP   A O   1 
ATOM   787  C  CB  . TRP   A 1 106 ? -11.988 -12.750 -1.686  1.00 91.95  ? 126 TRP   A CB  1 
ATOM   788  C  CG  . TRP   A 1 106 ? -11.506 -13.655 -2.781  1.00 91.83  ? 126 TRP   A CG  1 
ATOM   789  C  CD1 . TRP   A 1 106 ? -12.075 -14.830 -3.177  1.00 85.84  ? 126 TRP   A CD1 1 
ATOM   790  C  CD2 . TRP   A 1 106 ? -10.354 -13.466 -3.617  1.00 92.40  ? 126 TRP   A CD2 1 
ATOM   791  N  NE1 . TRP   A 1 106 ? -11.352 -15.385 -4.206  1.00 86.22  ? 126 TRP   A NE1 1 
ATOM   792  C  CE2 . TRP   A 1 106 ? -10.291 -14.567 -4.495  1.00 90.05  ? 126 TRP   A CE2 1 
ATOM   793  C  CE3 . TRP   A 1 106 ? -9.371  -12.473 -3.708  1.00 90.44  ? 126 TRP   A CE3 1 
ATOM   794  C  CZ2 . TRP   A 1 106 ? -9.287  -14.703 -5.452  1.00 90.01  ? 126 TRP   A CZ2 1 
ATOM   795  C  CZ3 . TRP   A 1 106 ? -8.374  -12.612 -4.661  1.00 93.53  ? 126 TRP   A CZ3 1 
ATOM   796  C  CH2 . TRP   A 1 106 ? -8.340  -13.718 -5.519  1.00 91.45  ? 126 TRP   A CH2 1 
ATOM   797  N  N   . LYS   A 1 107 ? -9.283  -12.900 -0.196  1.00 97.59  ? 127 LYS   A N   1 
ATOM   798  C  CA  . LYS   A 1 107 ? -7.873  -13.272 -0.241  1.00 99.81  ? 127 LYS   A CA  1 
ATOM   799  C  C   . LYS   A 1 107 ? -7.519  -14.258 0.865   1.00 98.31  ? 127 LYS   A C   1 
ATOM   800  O  O   . LYS   A 1 107 ? -6.760  -15.209 0.641   1.00 99.79  ? 127 LYS   A O   1 
ATOM   801  C  CB  . LYS   A 1 107 ? -7.018  -12.010 -0.139  1.00 98.67  ? 127 LYS   A CB  1 
ATOM   802  C  CG  . LYS   A 1 107 ? -5.624  -12.138 -0.703  1.00 103.95 ? 127 LYS   A CG  1 
ATOM   803  C  CD  . LYS   A 1 107 ? -5.203  -10.832 -1.349  1.00 111.37 ? 127 LYS   A CD  1 
ATOM   804  C  CE  . LYS   A 1 107 ? -5.392  -9.650  -0.424  1.00 116.07 ? 127 LYS   A CE  1 
ATOM   805  N  NZ  . LYS   A 1 107 ? -5.232  -8.347  -1.133  1.00 115.93 ? 127 LYS   A NZ  1 
ATOM   806  N  N   . ARG   A 1 108 ? -8.063  -14.050 2.065   1.00 104.28 ? 128 ARG   A N   1 
ATOM   807  C  CA  . ARG   A 1 108 ? -7.829  -14.980 3.164   1.00 106.60 ? 128 ARG   A CA  1 
ATOM   808  C  C   . ARG   A 1 108 ? -8.524  -16.315 2.918   1.00 103.92 ? 128 ARG   A C   1 
ATOM   809  O  O   . ARG   A 1 108 ? -7.953  -17.377 3.189   1.00 105.08 ? 128 ARG   A O   1 
ATOM   810  C  CB  . ARG   A 1 108 ? -8.304  -14.354 4.475   1.00 115.85 ? 128 ARG   A CB  1 
ATOM   811  C  CG  . ARG   A 1 108 ? -8.689  -15.347 5.554   1.00 123.32 ? 128 ARG   A CG  1 
ATOM   812  C  CD  . ARG   A 1 108 ? -9.423  -14.644 6.686   1.00 130.57 ? 128 ARG   A CD  1 
ATOM   813  N  NE  . ARG   A 1 108 ? -10.016 -15.588 7.626   1.00 142.50 ? 128 ARG   A NE  1 
ATOM   814  C  CZ  . ARG   A 1 108 ? -11.295 -15.939 7.633   1.00 138.45 ? 128 ARG   A CZ  1 
ATOM   815  N  NH1 . ARG   A 1 108 ? -12.159 -15.424 6.772   1.00 127.58 ? 128 ARG   A NH1 1 
ATOM   816  N  NH2 . ARG   A 1 108 ? -11.719 -16.826 8.528   1.00 148.51 ? 128 ARG   A NH2 1 
ATOM   817  N  N   . LEU   A 1 109 ? -9.754  -16.279 2.402   1.00 103.70 ? 129 LEU   A N   1 
ATOM   818  C  CA  . LEU   A 1 109 ? -10.474 -17.514 2.109   1.00 99.97  ? 129 LEU   A CA  1 
ATOM   819  C  C   . LEU   A 1 109 ? -9.850  -18.253 0.932   1.00 97.48  ? 129 LEU   A C   1 
ATOM   820  O  O   . LEU   A 1 109 ? -9.737  -19.485 0.957   1.00 98.59  ? 129 LEU   A O   1 
ATOM   821  C  CB  . LEU   A 1 109 ? -11.944 -17.208 1.828   1.00 98.52  ? 129 LEU   A CB  1 
ATOM   822  C  CG  . LEU   A 1 109 ? -12.772 -16.683 2.999   1.00 102.84 ? 129 LEU   A CG  1 
ATOM   823  C  CD1 . LEU   A 1 109 ? -14.135 -16.244 2.504   1.00 97.23  ? 129 LEU   A CD1 1 
ATOM   824  C  CD2 . LEU   A 1 109 ? -12.906 -17.741 4.084   1.00 107.94 ? 129 LEU   A CD2 1 
ATOM   825  N  N   . ARG   A 1 110 ? -9.458  -17.522 -0.114  1.00 95.50  ? 130 ARG   A N   1 
ATOM   826  C  CA  . ARG   A 1 110 ? -8.733  -18.138 -1.219  1.00 93.29  ? 130 ARG   A CA  1 
ATOM   827  C  C   . ARG   A 1 110 ? -7.455  -18.798 -0.724  1.00 98.67  ? 130 ARG   A C   1 
ATOM   828  O  O   . ARG   A 1 110 ? -7.178  -19.959 -1.040  1.00 96.43  ? 130 ARG   A O   1 
ATOM   829  C  CB  . ARG   A 1 110 ? -8.412  -17.095 -2.291  1.00 90.26  ? 130 ARG   A CB  1 
ATOM   830  C  CG  . ARG   A 1 110 ? -7.748  -17.668 -3.537  1.00 89.15  ? 130 ARG   A CG  1 
ATOM   831  C  CD  . ARG   A 1 110 ? -8.783  -18.158 -4.544  1.00 91.24  ? 130 ARG   A CD  1 
ATOM   832  N  NE  . ARG   A 1 110 ? -8.171  -18.872 -5.660  1.00 91.12  ? 130 ARG   A NE  1 
ATOM   833  C  CZ  . ARG   A 1 110 ? -8.799  -19.188 -6.785  1.00 85.77  ? 130 ARG   A CZ  1 
ATOM   834  N  NH1 . ARG   A 1 110 ? -10.059 -18.842 -6.995  1.00 86.30  ? 130 ARG   A NH1 1 
ATOM   835  N  NH2 . ARG   A 1 110 ? -8.144  -19.868 -7.724  1.00 81.19  ? 130 ARG   A NH2 1 
ATOM   836  N  N   . SER   A 1 111 ? -6.668  -18.069 0.070   1.00 97.52  ? 131 SER   A N   1 
ATOM   837  C  CA  . SER   A 1 111 ? -5.435  -18.626 0.614   1.00 95.36  ? 131 SER   A CA  1 
ATOM   838  C  C   . SER   A 1 111 ? -5.714  -19.836 1.499   1.00 98.48  ? 131 SER   A C   1 
ATOM   839  O  O   . SER   A 1 111 ? -5.003  -20.844 1.426   1.00 97.86  ? 131 SER   A O   1 
ATOM   840  C  CB  . SER   A 1 111 ? -4.684  -17.549 1.397   1.00 95.98  ? 131 SER   A CB  1 
ATOM   841  O  OG  . SER   A 1 111 ? -3.428  -18.018 1.852   1.00 104.29 ? 131 SER   A OG  1 
ATOM   842  N  N   . LEU   A 1 112 ? -6.761  -19.764 2.321   1.00 102.77 ? 132 LEU   A N   1 
ATOM   843  C  CA  . LEU   A 1 112 ? -7.019  -20.810 3.305   1.00 104.93 ? 132 LEU   A CA  1 
ATOM   844  C  C   . LEU   A 1 112 ? -7.700  -22.026 2.687   1.00 104.33 ? 132 LEU   A C   1 
ATOM   845  O  O   . LEU   A 1 112 ? -7.554  -23.141 3.201   1.00 108.59 ? 132 LEU   A O   1 
ATOM   846  C  CB  . LEU   A 1 112 ? -7.844  -20.229 4.455   1.00 110.70 ? 132 LEU   A CB  1 
ATOM   847  C  CG  . LEU   A 1 112 ? -8.537  -21.071 5.525   1.00 126.52 ? 132 LEU   A CG  1 
ATOM   848  C  CD1 . LEU   A 1 112 ? -8.759  -20.225 6.771   1.00 141.59 ? 132 LEU   A CD1 1 
ATOM   849  C  CD2 . LEU   A 1 112 ? -9.863  -21.582 5.000   1.00 124.73 ? 132 LEU   A CD2 1 
ATOM   850  N  N   . LEU   A 1 113 ? -8.456  -21.837 1.608   1.00 103.26 ? 133 LEU   A N   1 
ATOM   851  C  CA  . LEU   A 1 113 ? -9.097  -22.938 0.898   1.00 101.58 ? 133 LEU   A CA  1 
ATOM   852  C  C   . LEU   A 1 113 ? -8.272  -23.456 -0.273  1.00 100.12 ? 133 LEU   A C   1 
ATOM   853  O  O   . LEU   A 1 113 ? -8.583  -24.528 -0.799  1.00 101.72 ? 133 LEU   A O   1 
ATOM   854  C  CB  . LEU   A 1 113 ? -10.481 -22.513 0.391   1.00 102.41 ? 133 LEU   A CB  1 
ATOM   855  C  CG  . LEU   A 1 113 ? -11.687 -22.700 1.313   1.00 102.96 ? 133 LEU   A CG  1 
ATOM   856  C  CD1 . LEU   A 1 113 ? -12.871 -21.921 0.773   1.00 101.46 ? 133 LEU   A CD1 1 
ATOM   857  C  CD2 . LEU   A 1 113 ? -12.038 -24.174 1.441   1.00 106.00 ? 133 LEU   A CD2 1 
ATOM   858  N  N   . SER   A 1 114 ? -7.235  -22.723 -0.690  1.00 99.61  ? 134 SER   A N   1 
ATOM   859  C  CA  . SER   A 1 114 ? -6.417  -23.152 -1.825  1.00 100.45 ? 134 SER   A CA  1 
ATOM   860  C  C   . SER   A 1 114 ? -5.783  -24.526 -1.640  1.00 102.87 ? 134 SER   A C   1 
ATOM   861  O  O   . SER   A 1 114 ? -5.843  -25.335 -2.582  1.00 102.96 ? 134 SER   A O   1 
ATOM   862  C  CB  . SER   A 1 114 ? -5.346  -22.096 -2.122  1.00 100.69 ? 134 SER   A CB  1 
ATOM   863  O  OG  . SER   A 1 114 ? -5.035  -22.060 -3.504  1.00 101.56 ? 134 SER   A OG  1 
ATOM   864  N  N   . PRO   A 1 115 ? -5.168  -24.866 -0.498  1.00 105.24 ? 135 PRO   A N   1 
ATOM   865  C  CA  . PRO   A 1 115 ? -4.479  -26.166 -0.403  1.00 107.45 ? 135 PRO   A CA  1 
ATOM   866  C  C   . PRO   A 1 115 ? -5.405  -27.367 -0.516  1.00 111.00 ? 135 PRO   A C   1 
ATOM   867  O  O   . PRO   A 1 115 ? -4.925  -28.506 -0.463  1.00 112.65 ? 135 PRO   A O   1 
ATOM   868  C  CB  . PRO   A 1 115 ? -3.821  -26.119 0.992   1.00 100.94 ? 135 PRO   A CB  1 
ATOM   869  C  CG  . PRO   A 1 115 ? -3.912  -24.698 1.440   1.00 103.22 ? 135 PRO   A CG  1 
ATOM   870  C  CD  . PRO   A 1 115 ? -5.127  -24.148 0.790   1.00 102.10 ? 135 PRO   A CD  1 
ATOM   871  N  N   . THR   A 1 116 ? -6.709  -27.146 -0.675  1.00 112.71 ? 136 THR   A N   1 
ATOM   872  C  CA  . THR   A 1 116 ? -7.668  -28.233 -0.783  1.00 113.34 ? 136 THR   A CA  1 
ATOM   873  C  C   . THR   A 1 116 ? -7.655  -28.879 -2.163  1.00 120.59 ? 136 THR   A C   1 
ATOM   874  O  O   . THR   A 1 116 ? -7.957  -30.071 -2.286  1.00 123.40 ? 136 THR   A O   1 
ATOM   875  C  CB  . THR   A 1 116 ? -9.066  -27.705 -0.459  1.00 114.59 ? 136 THR   A CB  1 
ATOM   876  O  OG1 . THR   A 1 116 ? -8.976  -26.749 0.605   1.00 114.54 ? 136 THR   A OG1 1 
ATOM   877  C  CG2 . THR   A 1 116 ? -9.966  -28.821 -0.022  1.00 122.22 ? 136 THR   A CG2 1 
ATOM   878  N  N   . PHE   A 1 117 ? -7.299  -28.119 -3.201  1.00 122.84 ? 137 PHE   A N   1 
ATOM   879  C  CA  . PHE   A 1 117 ? -7.366  -28.584 -4.581  1.00 125.96 ? 137 PHE   A CA  1 
ATOM   880  C  C   . PHE   A 1 117 ? -5.991  -28.848 -5.184  1.00 128.84 ? 137 PHE   A C   1 
ATOM   881  O  O   . PHE   A 1 117 ? -5.845  -28.806 -6.410  1.00 131.58 ? 137 PHE   A O   1 
ATOM   882  C  CB  . PHE   A 1 117 ? -8.121  -27.574 -5.447  1.00 121.14 ? 137 PHE   A CB  1 
ATOM   883  C  CG  . PHE   A 1 117 ? -9.485  -27.235 -4.935  1.00 115.36 ? 137 PHE   A CG  1 
ATOM   884  C  CD1 . PHE   A 1 117 ? -9.662  -26.193 -4.040  1.00 111.89 ? 137 PHE   A CD1 1 
ATOM   885  C  CD2 . PHE   A 1 117 ? -10.592 -27.952 -5.354  1.00 107.21 ? 137 PHE   A CD2 1 
ATOM   886  C  CE1 . PHE   A 1 117 ? -10.915 -25.878 -3.567  1.00 107.67 ? 137 PHE   A CE1 1 
ATOM   887  C  CE2 . PHE   A 1 117 ? -11.847 -27.641 -4.888  1.00 110.29 ? 137 PHE   A CE2 1 
ATOM   888  C  CZ  . PHE   A 1 117 ? -12.009 -26.602 -3.994  1.00 108.22 ? 137 PHE   A CZ  1 
ATOM   889  N  N   . THR   A 1 118 ? -4.980  -29.105 -4.361  1.00 132.64 ? 138 THR   A N   1 
ATOM   890  C  CA  . THR   A 1 118 ? -3.679  -29.461 -4.907  1.00 139.74 ? 138 THR   A CA  1 
ATOM   891  C  C   . THR   A 1 118 ? -3.746  -30.824 -5.584  1.00 145.43 ? 138 THR   A C   1 
ATOM   892  O  O   . THR   A 1 118 ? -4.577  -31.670 -5.245  1.00 142.73 ? 138 THR   A O   1 
ATOM   893  C  CB  . THR   A 1 118 ? -2.610  -29.482 -3.811  1.00 137.96 ? 138 THR   A CB  1 
ATOM   894  O  OG1 . THR   A 1 118 ? -1.452  -30.180 -4.287  1.00 142.22 ? 138 THR   A OG1 1 
ATOM   895  C  CG2 . THR   A 1 118 ? -3.132  -30.174 -2.573  1.00 130.19 ? 138 THR   A CG2 1 
ATOM   896  N  N   . SER   A 1 119 ? -2.857  -31.027 -6.560  1.00 167.59 ? 139 SER   A N   1 
ATOM   897  C  CA  . SER   A 1 119 ? -2.755  -32.335 -7.197  1.00 168.35 ? 139 SER   A CA  1 
ATOM   898  C  C   . SER   A 1 119 ? -2.441  -33.424 -6.180  1.00 165.65 ? 139 SER   A C   1 
ATOM   899  O  O   . SER   A 1 119 ? -2.865  -34.573 -6.349  1.00 165.28 ? 139 SER   A O   1 
ATOM   900  C  CB  . SER   A 1 119 ? -1.689  -32.306 -8.291  1.00 168.37 ? 139 SER   A CB  1 
ATOM   901  O  OG  . SER   A 1 119 ? -0.421  -31.975 -7.755  1.00 170.90 ? 139 SER   A OG  1 
ATOM   902  N  N   . GLY   A 1 120 ? -1.706  -33.082 -5.120  1.00 148.81 ? 140 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 120 ? -1.439  -34.056 -4.073  1.00 143.62 ? 140 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 120 ? -2.706  -34.527 -3.387  1.00 140.09 ? 140 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 120 ? -2.937  -35.728 -3.239  1.00 140.31 ? 140 GLY   A O   1 
ATOM   906  N  N   . LYS   A 1 121 ? -3.546  -33.582 -2.957  1.00 135.82 ? 141 LYS   A N   1 
ATOM   907  C  CA  . LYS   A 1 121 ? -4.839  -33.943 -2.381  1.00 134.30 ? 141 LYS   A CA  1 
ATOM   908  C  C   . LYS   A 1 121 ? -5.755  -34.546 -3.437  1.00 135.06 ? 141 LYS   A C   1 
ATOM   909  O  O   . LYS   A 1 121 ? -6.415  -35.564 -3.195  1.00 133.04 ? 141 LYS   A O   1 
ATOM   910  C  CB  . LYS   A 1 121 ? -5.498  -32.717 -1.747  1.00 126.97 ? 141 LYS   A CB  1 
ATOM   911  C  CG  . LYS   A 1 121 ? -5.281  -32.575 -0.250  1.00 123.21 ? 141 LYS   A CG  1 
ATOM   912  C  CD  . LYS   A 1 121 ? -3.809  -32.463 0.097   1.00 122.47 ? 141 LYS   A CD  1 
ATOM   913  C  CE  . LYS   A 1 121 ? -3.624  -31.948 1.512   1.00 117.56 ? 141 LYS   A CE  1 
ATOM   914  N  NZ  . LYS   A 1 121 ? -4.294  -30.630 1.690   1.00 112.86 ? 141 LYS   A NZ  1 
ATOM   915  N  N   . LEU   A 1 122 ? -5.811  -33.920 -4.616  1.00 132.92 ? 142 LEU   A N   1 
ATOM   916  C  CA  . LEU   A 1 122 ? -6.642  -34.418 -5.708  1.00 129.91 ? 142 LEU   A CA  1 
ATOM   917  C  C   . LEU   A 1 122 ? -6.295  -35.855 -6.075  1.00 127.13 ? 142 LEU   A C   1 
ATOM   918  O  O   . LEU   A 1 122 ? -7.182  -36.631 -6.448  1.00 126.88 ? 142 LEU   A O   1 
ATOM   919  C  CB  . LEU   A 1 122 ? -6.489  -33.498 -6.920  1.00 129.15 ? 142 LEU   A CB  1 
ATOM   920  C  CG  . LEU   A 1 122 ? -6.951  -33.939 -8.308  1.00 123.04 ? 142 LEU   A CG  1 
ATOM   921  C  CD1 . LEU   A 1 122 ? -8.459  -34.128 -8.360  1.00 116.83 ? 142 LEU   A CD1 1 
ATOM   922  C  CD2 . LEU   A 1 122 ? -6.499  -32.914 -9.334  1.00 119.82 ? 142 LEU   A CD2 1 
ATOM   923  N  N   . LYS   A 1 123 ? -5.017  -36.230 -5.975  1.00 129.93 ? 143 LYS   A N   1 
ATOM   924  C  CA  . LYS   A 1 123 ? -4.635  -37.612 -6.243  1.00 129.71 ? 143 LYS   A CA  1 
ATOM   925  C  C   . LYS   A 1 123 ? -5.175  -38.558 -5.177  1.00 133.72 ? 143 LYS   A C   1 
ATOM   926  O  O   . LYS   A 1 123 ? -5.474  -39.720 -5.475  1.00 132.91 ? 143 LYS   A O   1 
ATOM   927  C  CB  . LYS   A 1 123 ? -3.112  -37.724 -6.348  1.00 126.81 ? 143 LYS   A CB  1 
ATOM   928  C  CG  . LYS   A 1 123 ? -2.595  -39.137 -6.565  1.00 125.40 ? 143 LYS   A CG  1 
ATOM   929  C  CD  . LYS   A 1 123 ? -1.269  -39.135 -7.308  1.00 122.58 ? 143 LYS   A CD  1 
ATOM   930  C  CE  . LYS   A 1 123 ? -0.241  -38.253 -6.619  1.00 123.35 ? 143 LYS   A CE  1 
ATOM   931  N  NZ  . LYS   A 1 123 ? 1.091   -38.342 -7.283  1.00 119.87 ? 143 LYS   A NZ  1 
ATOM   932  N  N   . GLU   A 1 124 ? -5.317  -38.082 -3.938  1.00 129.09 ? 144 GLU   A N   1 
ATOM   933  C  CA  . GLU   A 1 124 ? -5.893  -38.915 -2.891  1.00 131.92 ? 144 GLU   A CA  1 
ATOM   934  C  C   . GLU   A 1 124 ? -7.393  -39.111 -3.067  1.00 129.60 ? 144 GLU   A C   1 
ATOM   935  O  O   . GLU   A 1 124 ? -7.937  -40.103 -2.569  1.00 128.97 ? 144 GLU   A O   1 
ATOM   936  C  CB  . GLU   A 1 124 ? -5.593  -38.310 -1.516  1.00 139.34 ? 144 GLU   A CB  1 
ATOM   937  C  CG  . GLU   A 1 124 ? -4.126  -37.953 -1.320  1.00 141.64 ? 144 GLU   A CG  1 
ATOM   938  C  CD  . GLU   A 1 124 ? -3.751  -37.752 0.135   1.00 144.33 ? 144 GLU   A CD  1 
ATOM   939  O  OE1 . GLU   A 1 124 ? -4.657  -37.717 0.994   1.00 146.99 ? 144 GLU   A OE1 1 
ATOM   940  O  OE2 . GLU   A 1 124 ? -2.540  -37.636 0.418   1.00 146.92 ? 144 GLU   A OE2 1 
ATOM   941  N  N   . MET   A 1 125 ? -8.068  -38.201 -3.773  1.00 137.95 ? 145 MET   A N   1 
ATOM   942  C  CA  . MET   A 1 125 ? -9.488  -38.369 -4.070  1.00 133.35 ? 145 MET   A CA  1 
ATOM   943  C  C   . MET   A 1 125 ? -9.752  -39.448 -5.111  1.00 132.65 ? 145 MET   A C   1 
ATOM   944  O  O   . MET   A 1 125 ? -10.911 -39.829 -5.292  1.00 133.44 ? 145 MET   A O   1 
ATOM   945  C  CB  . MET   A 1 125 ? -10.088 -37.046 -4.551  1.00 130.92 ? 145 MET   A CB  1 
ATOM   946  C  CG  . MET   A 1 125 ? -9.633  -35.815 -3.785  1.00 128.95 ? 145 MET   A CG  1 
ATOM   947  S  SD  . MET   A 1 125 ? -10.996 -34.708 -3.384  1.00 126.35 ? 145 MET   A SD  1 
ATOM   948  C  CE  . MET   A 1 125 ? -11.779 -35.631 -2.064  1.00 138.72 ? 145 MET   A CE  1 
ATOM   949  N  N   . VAL   A 1 126 ? -8.708  -39.940 -5.788  1.00 135.83 ? 146 VAL   A N   1 
ATOM   950  C  CA  . VAL   A 1 126 ? -8.906  -40.863 -6.912  1.00 135.69 ? 146 VAL   A CA  1 
ATOM   951  C  C   . VAL   A 1 126 ? -9.687  -42.110 -6.515  1.00 134.80 ? 146 VAL   A C   1 
ATOM   952  O  O   . VAL   A 1 126 ? -10.691 -42.420 -7.179  1.00 136.00 ? 146 VAL   A O   1 
ATOM   953  C  CB  . VAL   A 1 126 ? -7.550  -41.209 -7.558  1.00 136.79 ? 146 VAL   A CB  1 
ATOM   954  C  CG1 . VAL   A 1 126 ? -7.653  -42.513 -8.338  1.00 137.28 ? 146 VAL   A CG1 1 
ATOM   955  C  CG2 . VAL   A 1 126 ? -7.092  -40.086 -8.460  1.00 138.42 ? 146 VAL   A CG2 1 
ATOM   956  N  N   . PRO   A 1 127 ? -9.294  -42.874 -5.486  1.00 134.70 ? 147 PRO   A N   1 
ATOM   957  C  CA  . PRO   A 1 127 ? -10.056 -44.094 -5.171  1.00 132.83 ? 147 PRO   A CA  1 
ATOM   958  C  C   . PRO   A 1 127 ? -11.506 -43.830 -4.802  1.00 135.92 ? 147 PRO   A C   1 
ATOM   959  O  O   . PRO   A 1 127 ? -12.376 -44.648 -5.129  1.00 138.75 ? 147 PRO   A O   1 
ATOM   960  C  CB  . PRO   A 1 127 ? -9.277  -44.697 -3.995  1.00 129.26 ? 147 PRO   A CB  1 
ATOM   961  C  CG  . PRO   A 1 127 ? -7.911  -44.117 -4.104  1.00 129.04 ? 147 PRO   A CG  1 
ATOM   962  C  CD  . PRO   A 1 127 ? -8.129  -42.727 -4.595  1.00 132.57 ? 147 PRO   A CD  1 
ATOM   963  N  N   . ILE   A 1 128 ? -11.798 -42.709 -4.140  1.00 136.53 ? 148 ILE   A N   1 
ATOM   964  C  CA  . ILE   A 1 128 ? -13.168 -42.438 -3.716  1.00 136.72 ? 148 ILE   A CA  1 
ATOM   965  C  C   . ILE   A 1 128 ? -14.041 -42.108 -4.920  1.00 143.12 ? 148 ILE   A C   1 
ATOM   966  O  O   . ILE   A 1 128 ? -15.162 -42.612 -5.051  1.00 144.39 ? 148 ILE   A O   1 
ATOM   967  C  CB  . ILE   A 1 128 ? -13.201 -41.310 -2.668  1.00 128.80 ? 148 ILE   A CB  1 
ATOM   968  C  CG1 . ILE   A 1 128 ? -12.442 -41.722 -1.404  1.00 125.72 ? 148 ILE   A CG1 1 
ATOM   969  C  CG2 . ILE   A 1 128 ? -14.637 -40.951 -2.317  1.00 130.99 ? 148 ILE   A CG2 1 
ATOM   970  C  CD1 . ILE   A 1 128 ? -10.976 -41.341 -1.409  1.00 129.33 ? 148 ILE   A CD1 1 
ATOM   971  N  N   . ILE   A 1 129 ? -13.537 -41.260 -5.820  1.00 152.94 ? 149 ILE   A N   1 
ATOM   972  C  CA  . ILE   A 1 129 ? -14.246 -40.961 -7.058  1.00 148.40 ? 149 ILE   A CA  1 
ATOM   973  C  C   . ILE   A 1 129 ? -14.370 -42.203 -7.931  1.00 147.64 ? 149 ILE   A C   1 
ATOM   974  O  O   . ILE   A 1 129 ? -15.270 -42.286 -8.775  1.00 147.46 ? 149 ILE   A O   1 
ATOM   975  C  CB  . ILE   A 1 129 ? -13.532 -39.807 -7.796  1.00 146.96 ? 149 ILE   A CB  1 
ATOM   976  C  CG1 . ILE   A 1 129 ? -13.450 -38.573 -6.894  1.00 147.85 ? 149 ILE   A CG1 1 
ATOM   977  C  CG2 . ILE   A 1 129 ? -14.244 -39.452 -9.088  1.00 143.55 ? 149 ILE   A CG2 1 
ATOM   978  C  CD1 . ILE   A 1 129 ? -12.784 -37.381 -7.547  1.00 149.29 ? 149 ILE   A CD1 1 
ATOM   979  N  N   . ALA   A 1 130 ? -13.498 -43.191 -7.730  1.00 138.42 ? 150 ALA   A N   1 
ATOM   980  C  CA  . ALA   A 1 130 ? -13.554 -44.436 -8.484  1.00 139.91 ? 150 ALA   A CA  1 
ATOM   981  C  C   . ALA   A 1 130 ? -14.560 -45.433 -7.922  1.00 140.40 ? 150 ALA   A C   1 
ATOM   982  O  O   . ALA   A 1 130 ? -14.826 -46.450 -8.572  1.00 139.88 ? 150 ALA   A O   1 
ATOM   983  C  CB  . ALA   A 1 130 ? -12.167 -45.082 -8.532  1.00 140.45 ? 150 ALA   A CB  1 
ATOM   984  N  N   . GLN   A 1 131 ? -15.119 -45.176 -6.736  1.00 139.79 ? 151 GLN   A N   1 
ATOM   985  C  CA  . GLN   A 1 131 ? -16.124 -46.075 -6.179  1.00 139.02 ? 151 GLN   A CA  1 
ATOM   986  C  C   . GLN   A 1 131 ? -17.491 -45.844 -6.809  1.00 140.94 ? 151 GLN   A C   1 
ATOM   987  O  O   . GLN   A 1 131 ? -18.214 -46.803 -7.100  1.00 142.53 ? 151 GLN   A O   1 
ATOM   988  C  CB  . GLN   A 1 131 ? -16.206 -45.903 -4.661  1.00 138.87 ? 151 GLN   A CB  1 
ATOM   989  C  CG  . GLN   A 1 131 ? -17.331 -46.696 -4.010  1.00 138.50 ? 151 GLN   A CG  1 
ATOM   990  C  CD  . GLN   A 1 131 ? -17.482 -46.400 -2.530  1.00 137.75 ? 151 GLN   A CD  1 
ATOM   991  O  OE1 . GLN   A 1 131 ? -18.467 -46.791 -1.903  1.00 140.75 ? 151 GLN   A OE1 1 
ATOM   992  N  NE2 . GLN   A 1 131 ? -16.501 -45.708 -1.962  1.00 132.65 ? 151 GLN   A NE2 1 
ATOM   993  N  N   . TYR   A 1 132 ? -17.859 -44.585 -7.024  1.00 136.79 ? 152 TYR   A N   1 
ATOM   994  C  CA  . TYR   A 1 132 ? -19.141 -44.240 -7.620  1.00 137.84 ? 152 TYR   A CA  1 
ATOM   995  C  C   . TYR   A 1 132 ? -19.084 -44.185 -9.139  1.00 137.33 ? 152 TYR   A C   1 
ATOM   996  O  O   . TYR   A 1 132 ? -20.120 -43.980 -9.779  1.00 137.36 ? 152 TYR   A O   1 
ATOM   997  C  CB  . TYR   A 1 132 ? -19.635 -42.908 -7.050  1.00 135.46 ? 152 TYR   A CB  1 
ATOM   998  C  CG  . TYR   A 1 132 ? -19.527 -42.866 -5.544  1.00 136.04 ? 152 TYR   A CG  1 
ATOM   999  C  CD1 . TYR   A 1 132 ? -20.500 -43.447 -4.741  1.00 136.82 ? 152 TYR   A CD1 1 
ATOM   1000 C  CD2 . TYR   A 1 132 ? -18.435 -42.273 -4.928  1.00 134.18 ? 152 TYR   A CD2 1 
ATOM   1001 C  CE1 . TYR   A 1 132 ? -20.395 -43.422 -3.363  1.00 136.48 ? 152 TYR   A CE1 1 
ATOM   1002 C  CE2 . TYR   A 1 132 ? -18.320 -42.244 -3.555  1.00 135.13 ? 152 TYR   A CE2 1 
ATOM   1003 C  CZ  . TYR   A 1 132 ? -19.302 -42.817 -2.776  1.00 137.27 ? 152 TYR   A CZ  1 
ATOM   1004 O  OH  . TYR   A 1 132 ? -19.183 -42.784 -1.405  1.00 134.34 ? 152 TYR   A OH  1 
ATOM   1005 N  N   . GLY   A 1 133 ? -17.898 -44.354 -9.728  1.00 145.30 ? 153 GLY   A N   1 
ATOM   1006 C  CA  . GLY   A 1 133 ? -17.831 -44.676 -11.140 1.00 140.60 ? 153 GLY   A CA  1 
ATOM   1007 C  C   . GLY   A 1 133 ? -18.251 -46.104 -11.413 1.00 141.70 ? 153 GLY   A C   1 
ATOM   1008 O  O   . GLY   A 1 133 ? -18.721 -46.420 -12.509 1.00 139.17 ? 153 GLY   A O   1 
ATOM   1009 N  N   . ASP   A 1 134 ? -18.095 -46.983 -10.421 1.00 138.17 ? 154 ASP   A N   1 
ATOM   1010 C  CA  . ASP   A 1 134 ? -18.573 -48.355 -10.539 1.00 139.80 ? 154 ASP   A CA  1 
ATOM   1011 C  C   . ASP   A 1 134 ? -20.062 -48.464 -10.238 1.00 143.81 ? 154 ASP   A C   1 
ATOM   1012 O  O   . ASP   A 1 134 ? -20.740 -49.334 -10.796 1.00 145.58 ? 154 ASP   A O   1 
ATOM   1013 C  CB  . ASP   A 1 134 ? -17.776 -49.268 -9.607  1.00 139.43 ? 154 ASP   A CB  1 
ATOM   1014 C  CG  . ASP   A 1 134 ? -16.284 -49.222 -9.881  1.00 139.61 ? 154 ASP   A CG  1 
ATOM   1015 O  OD1 . ASP   A 1 134 ? -15.887 -48.674 -10.931 1.00 135.12 ? 154 ASP   A OD1 1 
ATOM   1016 O  OD2 . ASP   A 1 134 ? -15.507 -49.728 -9.044  1.00 143.86 ? 154 ASP   A OD2 1 
ATOM   1017 N  N   . VAL   A 1 135 ? -20.585 -47.603 -9.360  1.00 151.81 ? 155 VAL   A N   1 
ATOM   1018 C  CA  . VAL   A 1 135 ? -22.028 -47.552 -9.147  1.00 156.16 ? 155 VAL   A CA  1 
ATOM   1019 C  C   . VAL   A 1 135 ? -22.715 -46.935 -10.357 1.00 155.32 ? 155 VAL   A C   1 
ATOM   1020 O  O   . VAL   A 1 135 ? -23.881 -47.238 -10.644 1.00 157.40 ? 155 VAL   A O   1 
ATOM   1021 C  CB  . VAL   A 1 135 ? -22.355 -46.777 -7.856  1.00 157.79 ? 155 VAL   A CB  1 
ATOM   1022 C  CG1 . VAL   A 1 135 ? -23.830 -46.920 -7.501  1.00 158.63 ? 155 VAL   A CG1 1 
ATOM   1023 C  CG2 . VAL   A 1 135 ? -21.471 -47.249 -6.710  1.00 152.56 ? 155 VAL   A CG2 1 
ATOM   1024 N  N   . LEU   A 1 136 ? -21.960 -46.119 -11.087 1.00 146.27 ? 156 LEU   A N   1 
ATOM   1025 C  CA  . LEU   A 1 136 ? -22.514 -45.540 -12.330 1.00 140.97 ? 156 LEU   A CA  1 
ATOM   1026 C  C   . LEU   A 1 136 ? -22.734 -46.683 -13.318 1.00 144.80 ? 156 LEU   A C   1 
ATOM   1027 O  O   . LEU   A 1 136 ? -23.899 -46.979 -13.631 1.00 150.44 ? 156 LEU   A O   1 
ATOM   1028 C  CB  . LEU   A 1 136 ? -21.511 -44.523 -12.879 1.00 129.60 ? 156 LEU   A CB  1 
ATOM   1029 C  CG  . LEU   A 1 136 ? -22.037 -43.611 -13.985 1.00 122.97 ? 156 LEU   A CG  1 
ATOM   1030 C  CD1 . LEU   A 1 136 ? -23.472 -43.194 -13.706 1.00 124.17 ? 156 LEU   A CD1 1 
ATOM   1031 C  CD2 . LEU   A 1 136 ? -21.150 -42.387 -14.140 1.00 116.14 ? 156 LEU   A CD2 1 
ATOM   1032 N  N   . VAL   A 1 137 ? -21.650 -47.316 -13.762 1.00 149.84 ? 157 VAL   A N   1 
ATOM   1033 C  CA  . VAL   A 1 137 ? -21.781 -48.379 -14.796 1.00 150.03 ? 157 VAL   A CA  1 
ATOM   1034 C  C   . VAL   A 1 137 ? -22.920 -49.308 -14.387 1.00 161.47 ? 157 VAL   A C   1 
ATOM   1035 O  O   . VAL   A 1 137 ? -23.811 -49.549 -15.216 1.00 165.31 ? 157 VAL   A O   1 
ATOM   1036 C  CB  . VAL   A 1 137 ? -20.464 -49.154 -14.983 1.00 145.24 ? 157 VAL   A CB  1 
ATOM   1037 C  CG1 . VAL   A 1 137 ? -19.618 -48.554 -16.092 1.00 138.61 ? 157 VAL   A CG1 1 
ATOM   1038 C  CG2 . VAL   A 1 137 ? -19.667 -49.244 -13.694 1.00 146.05 ? 157 VAL   A CG2 1 
ATOM   1039 N  N   . ARG   A 1 138 ? -22.875 -49.813 -13.156 1.00 168.65 ? 158 ARG   A N   1 
ATOM   1040 C  CA  . ARG   A 1 138 ? -23.907 -50.780 -12.709 1.00 169.31 ? 158 ARG   A CA  1 
ATOM   1041 C  C   . ARG   A 1 138 ? -25.286 -50.239 -13.084 1.00 175.23 ? 158 ARG   A C   1 
ATOM   1042 O  O   . ARG   A 1 138 ? -25.947 -50.843 -13.946 1.00 175.53 ? 158 ARG   A O   1 
ATOM   1043 C  CB  . ARG   A 1 138 ? -23.794 -51.014 -11.203 1.00 171.82 ? 158 ARG   A CB  1 
ATOM   1044 C  CG  . ARG   A 1 138 ? -23.870 -52.480 -10.801 1.00 174.48 ? 158 ARG   A CG  1 
ATOM   1045 C  CD  . ARG   A 1 138 ? -24.403 -53.355 -11.920 1.00 179.63 ? 158 ARG   A CD  1 
ATOM   1046 N  NE  . ARG   A 1 138 ? -25.856 -53.447 -11.910 1.00 185.82 ? 158 ARG   A NE  1 
ATOM   1047 C  CZ  . ARG   A 1 138 ? -26.606 -53.595 -12.995 1.00 188.03 ? 158 ARG   A CZ  1 
ATOM   1048 N  NH1 . ARG   A 1 138 ? -26.039 -53.667 -14.186 1.00 187.70 ? 158 ARG   A NH1 1 
ATOM   1049 N  NH2 . ARG   A 1 138 ? -27.921 -53.667 -12.887 1.00 187.29 ? 158 ARG   A NH2 1 
ATOM   1050 N  N   . ASN   A 1 139 ? -25.696 -49.136 -12.462 1.00 173.53 ? 159 ASN   A N   1 
ATOM   1051 C  CA  . ASN   A 1 139 ? -27.053 -48.596 -12.721 1.00 181.37 ? 159 ASN   A CA  1 
ATOM   1052 C  C   . ASN   A 1 139 ? -27.234 -48.435 -14.229 1.00 185.17 ? 159 ASN   A C   1 
ATOM   1053 O  O   . ASN   A 1 139 ? -28.361 -48.627 -14.715 1.00 188.70 ? 159 ASN   A O   1 
ATOM   1054 C  CB  . ASN   A 1 139 ? -27.290 -47.282 -11.976 1.00 174.63 ? 159 ASN   A CB  1 
ATOM   1055 C  CG  . ASN   A 1 139 ? -27.186 -47.438 -10.475 1.00 177.50 ? 159 ASN   A CG  1 
ATOM   1056 O  OD1 . ASN   A 1 139 ? -26.672 -48.441 -9.984  1.00 179.99 ? 159 ASN   A OD1 1 
ATOM   1057 N  ND2 . ASN   A 1 139 ? -27.673 -46.453 -9.739  1.00 171.22 ? 159 ASN   A ND2 1 
ATOM   1058 N  N   . LEU   A 1 140 ? -26.158 -48.101 -14.937 1.00 167.31 ? 160 LEU   A N   1 
ATOM   1059 C  CA  . LEU   A 1 140 ? -26.279 -47.855 -16.394 1.00 159.90 ? 160 LEU   A CA  1 
ATOM   1060 C  C   . LEU   A 1 140 ? -26.711 -49.152 -17.076 1.00 159.32 ? 160 LEU   A C   1 
ATOM   1061 O  O   . LEU   A 1 140 ? -27.792 -49.163 -17.692 1.00 158.94 ? 160 LEU   A O   1 
ATOM   1062 C  CB  . LEU   A 1 140 ? -24.925 -47.377 -16.919 1.00 150.33 ? 160 LEU   A CB  1 
ATOM   1063 C  CG  . LEU   A 1 140 ? -24.546 -45.947 -16.545 1.00 140.10 ? 160 LEU   A CG  1 
ATOM   1064 C  CD1 . LEU   A 1 140 ? -23.698 -45.317 -17.636 1.00 123.19 ? 160 LEU   A CD1 1 
ATOM   1065 C  CD2 . LEU   A 1 140 ? -25.787 -45.109 -16.285 1.00 132.87 ? 160 LEU   A CD2 1 
ATOM   1066 N  N   . ARG   A 1 141 ? -25.898 -50.202 -16.953 1.00 161.32 ? 161 ARG   A N   1 
ATOM   1067 C  CA  . ARG   A 1 141 ? -26.211 -51.491 -17.624 1.00 161.95 ? 161 ARG   A CA  1 
ATOM   1068 C  C   . ARG   A 1 141 ? -27.680 -51.829 -17.376 1.00 164.60 ? 161 ARG   A C   1 
ATOM   1069 O  O   . ARG   A 1 141 ? -28.393 -52.108 -18.351 1.00 165.59 ? 161 ARG   A O   1 
ATOM   1070 C  CB  . ARG   A 1 141 ? -25.284 -52.598 -17.119 1.00 159.11 ? 161 ARG   A CB  1 
ATOM   1071 C  CG  . ARG   A 1 141 ? -24.547 -53.329 -18.231 1.00 153.89 ? 161 ARG   A CG  1 
ATOM   1072 C  CD  . ARG   A 1 141 ? -23.166 -53.794 -17.816 1.00 154.34 ? 161 ARG   A CD  1 
ATOM   1073 N  NE  . ARG   A 1 141 ? -22.517 -52.892 -16.878 1.00 147.59 ? 161 ARG   A NE  1 
ATOM   1074 C  CZ  . ARG   A 1 141 ? -22.485 -53.070 -15.563 1.00 142.78 ? 161 ARG   A CZ  1 
ATOM   1075 N  NH1 . ARG   A 1 141 ? -23.077 -54.121 -15.022 1.00 144.00 ? 161 ARG   A NH1 1 
ATOM   1076 N  NH2 . ARG   A 1 141 ? -21.864 -52.197 -14.792 1.00 130.69 ? 161 ARG   A NH2 1 
ATOM   1077 N  N   . ARG   A 1 142 ? -28.103 -51.795 -16.114 1.00 167.50 ? 162 ARG   A N   1 
ATOM   1078 C  CA  . ARG   A 1 142 ? -29.522 -52.071 -15.783 1.00 171.06 ? 162 ARG   A CA  1 
ATOM   1079 C  C   . ARG   A 1 142 ? -30.403 -51.355 -16.810 1.00 170.07 ? 162 ARG   A C   1 
ATOM   1080 O  O   . ARG   A 1 142 ? -31.114 -52.048 -17.557 1.00 169.42 ? 162 ARG   A O   1 
ATOM   1081 C  CB  . ARG   A 1 142 ? -29.816 -51.639 -14.344 1.00 172.68 ? 162 ARG   A CB  1 
ATOM   1082 C  CG  . ARG   A 1 142 ? -31.223 -51.107 -14.111 1.00 175.27 ? 162 ARG   A CG  1 
ATOM   1083 C  CD  . ARG   A 1 142 ? -31.288 -50.261 -12.854 1.00 178.56 ? 162 ARG   A CD  1 
ATOM   1084 N  NE  . ARG   A 1 142 ? -30.260 -50.632 -11.890 1.00 178.71 ? 162 ARG   A NE  1 
ATOM   1085 C  CZ  . ARG   A 1 142 ? -29.782 -49.830 -10.944 1.00 178.22 ? 162 ARG   A CZ  1 
ATOM   1086 N  NH1 . ARG   A 1 142 ? -30.241 -48.596 -10.827 1.00 176.04 ? 162 ARG   A NH1 1 
ATOM   1087 N  NH2 . ARG   A 1 142 ? -28.847 -50.265 -10.119 1.00 178.72 ? 162 ARG   A NH2 1 
ATOM   1088 N  N   . GLU   A 1 143 ? -30.322 -50.027 -16.865 1.00 166.87 ? 163 GLU   A N   1 
ATOM   1089 C  CA  . GLU   A 1 143 ? -31.185 -49.251 -17.788 1.00 166.40 ? 163 GLU   A CA  1 
ATOM   1090 C  C   . GLU   A 1 143 ? -30.907 -49.703 -19.221 1.00 166.10 ? 163 GLU   A C   1 
ATOM   1091 O  O   . GLU   A 1 143 ? -31.855 -49.803 -20.015 1.00 171.19 ? 163 GLU   A O   1 
ATOM   1092 C  CB  . GLU   A 1 143 ? -30.918 -47.756 -17.628 1.00 161.90 ? 163 GLU   A CB  1 
ATOM   1093 C  CG  . GLU   A 1 143 ? -31.319 -46.941 -18.841 1.00 161.00 ? 163 GLU   A CG  1 
ATOM   1094 C  CD  . GLU   A 1 143 ? -32.809 -46.677 -18.974 1.00 163.66 ? 163 GLU   A CD  1 
ATOM   1095 O  OE1 . GLU   A 1 143 ? -33.301 -45.738 -18.319 1.00 159.52 ? 163 GLU   A OE1 1 
ATOM   1096 O  OE2 . GLU   A 1 143 ? -33.470 -47.409 -19.734 1.00 161.84 ? 163 GLU   A OE2 1 
ATOM   1097 N  N   . ALA   A 1 144 ? -29.640 -49.955 -19.533 1.00 168.57 ? 164 ALA   A N   1 
ATOM   1098 C  CA  . ALA   A 1 144 ? -29.285 -50.376 -20.903 1.00 164.78 ? 164 ALA   A CA  1 
ATOM   1099 C  C   . ALA   A 1 144 ? -30.127 -51.597 -21.258 1.00 166.01 ? 164 ALA   A C   1 
ATOM   1100 O  O   . ALA   A 1 144 ? -30.786 -51.573 -22.309 1.00 168.38 ? 164 ALA   A O   1 
ATOM   1101 C  CB  . ALA   A 1 144 ? -27.815 -50.685 -20.981 1.00 153.08 ? 164 ALA   A CB  1 
ATOM   1102 N  N   . GLU   A 1 145 ? -30.105 -52.615 -20.396 1.00 170.86 ? 165 GLU   A N   1 
ATOM   1103 C  CA  . GLU   A 1 145 ? -30.871 -53.861 -20.651 1.00 171.32 ? 165 GLU   A CA  1 
ATOM   1104 C  C   . GLU   A 1 145 ? -32.331 -53.506 -20.932 1.00 167.06 ? 165 GLU   A C   1 
ATOM   1105 O  O   . GLU   A 1 145 ? -32.931 -54.132 -21.820 1.00 175.50 ? 165 GLU   A O   1 
ATOM   1106 C  CB  . GLU   A 1 145 ? -30.746 -54.794 -19.450 1.00 173.37 ? 165 GLU   A CB  1 
ATOM   1107 C  CG  . GLU   A 1 145 ? -29.326 -55.275 -19.218 1.00 175.74 ? 165 GLU   A CG  1 
ATOM   1108 C  CD  . GLU   A 1 145 ? -28.834 -55.134 -17.789 1.00 175.73 ? 165 GLU   A CD  1 
ATOM   1109 O  OE1 . GLU   A 1 145 ? -29.682 -55.020 -16.885 1.00 186.35 ? 165 GLU   A OE1 1 
ATOM   1110 O  OE2 . GLU   A 1 145 ? -27.605 -55.141 -17.584 1.00 171.28 ? 165 GLU   A OE2 1 
ATOM   1111 N  N   . THR   A 1 146 ? -32.866 -52.523 -20.212 1.00 170.84 ? 166 THR   A N   1 
ATOM   1112 C  CA  . THR   A 1 146 ? -34.279 -52.116 -20.401 1.00 170.80 ? 166 THR   A CA  1 
ATOM   1113 C  C   . THR   A 1 146 ? -34.482 -51.558 -21.807 1.00 172.88 ? 166 THR   A C   1 
ATOM   1114 O  O   . THR   A 1 146 ? -35.642 -51.327 -22.180 1.00 173.05 ? 166 THR   A O   1 
ATOM   1115 C  CB  . THR   A 1 146 ? -34.663 -51.058 -19.370 1.00 171.94 ? 166 THR   A CB  1 
ATOM   1116 O  OG1 . THR   A 1 146 ? -34.392 -49.782 -19.948 1.00 170.32 ? 166 THR   A OG1 1 
ATOM   1117 C  CG2 . THR   A 1 146 ? -33.887 -51.223 -18.086 1.00 171.17 ? 166 THR   A CG2 1 
ATOM   1118 N  N   . GLY   A 1 147 ? -33.395 -51.324 -22.539 1.00 172.54 ? 167 GLY   A N   1 
ATOM   1119 C  CA  . GLY   A 1 147 ? -33.504 -50.825 -23.922 1.00 177.76 ? 167 GLY   A CA  1 
ATOM   1120 C  C   . GLY   A 1 147 ? -34.410 -49.614 -24.005 1.00 175.07 ? 167 GLY   A C   1 
ATOM   1121 O  O   . GLY   A 1 147 ? -35.054 -49.433 -25.055 1.00 175.42 ? 167 GLY   A O   1 
ATOM   1122 N  N   . LYS   A 1 148 ? -34.463 -48.815 -22.938 1.00 171.13 ? 168 LYS   A N   1 
ATOM   1123 C  CA  . LYS   A 1 148 ? -35.267 -47.566 -22.967 1.00 171.06 ? 168 LYS   A CA  1 
ATOM   1124 C  C   . LYS   A 1 148 ? -34.319 -46.368 -23.059 1.00 171.19 ? 168 LYS   A C   1 
ATOM   1125 O  O   . LYS   A 1 148 ? -33.282 -46.386 -22.374 1.00 166.78 ? 168 LYS   A O   1 
ATOM   1126 C  CB  . LYS   A 1 148 ? -36.137 -47.462 -21.713 1.00 174.18 ? 168 LYS   A CB  1 
ATOM   1127 C  CG  . LYS   A 1 148 ? -37.045 -48.653 -21.444 1.00 175.47 ? 168 LYS   A CG  1 
ATOM   1128 C  CD  . LYS   A 1 148 ? -37.349 -48.842 -19.973 1.00 180.07 ? 168 LYS   A CD  1 
ATOM   1129 C  CE  . LYS   A 1 148 ? -36.805 -47.724 -19.110 1.00 178.93 ? 168 LYS   A CE  1 
ATOM   1130 N  NZ  . LYS   A 1 148 ? -35.728 -48.194 -18.207 1.00 176.38 ? 168 LYS   A NZ  1 
ATOM   1131 N  N   . PRO   A 1 149 ? -34.627 -45.337 -23.873 1.00 171.53 ? 169 PRO   A N   1 
ATOM   1132 C  CA  . PRO   A 1 149 ? -33.791 -44.137 -23.951 1.00 167.85 ? 169 PRO   A CA  1 
ATOM   1133 C  C   . PRO   A 1 149 ? -33.405 -43.657 -22.545 1.00 169.25 ? 169 PRO   A C   1 
ATOM   1134 O  O   . PRO   A 1 149 ? -34.176 -43.885 -21.632 1.00 173.37 ? 169 PRO   A O   1 
ATOM   1135 C  CB  . PRO   A 1 149 ? -34.723 -43.147 -24.650 1.00 166.21 ? 169 PRO   A CB  1 
ATOM   1136 C  CG  . PRO   A 1 149 ? -35.542 -44.027 -25.564 1.00 166.88 ? 169 PRO   A CG  1 
ATOM   1137 C  CD  . PRO   A 1 149 ? -35.788 -45.282 -24.757 1.00 168.46 ? 169 PRO   A CD  1 
ATOM   1138 N  N   . VAL   A 1 150 ? -32.257 -42.985 -22.399 1.00 156.83 ? 170 VAL   A N   1 
ATOM   1139 C  CA  . VAL   A 1 150 ? -31.777 -42.615 -21.032 1.00 151.65 ? 170 VAL   A CA  1 
ATOM   1140 C  C   . VAL   A 1 150 ? -31.617 -41.101 -20.873 1.00 146.86 ? 170 VAL   A C   1 
ATOM   1141 O  O   . VAL   A 1 150 ? -31.079 -40.467 -21.799 1.00 143.10 ? 170 VAL   A O   1 
ATOM   1142 C  CB  . VAL   A 1 150 ? -30.449 -43.327 -20.718 1.00 146.45 ? 170 VAL   A CB  1 
ATOM   1143 C  CG1 . VAL   A 1 150 ? -30.157 -43.346 -19.227 1.00 143.65 ? 170 VAL   A CG1 1 
ATOM   1144 C  CG2 . VAL   A 1 150 ? -30.425 -44.734 -21.291 1.00 150.43 ? 170 VAL   A CG2 1 
ATOM   1145 N  N   . THR   A 1 151 ? -32.072 -40.552 -19.739 1.00 145.48 ? 171 THR   A N   1 
ATOM   1146 C  CA  . THR   A 1 151 ? -31.843 -39.141 -19.454 1.00 139.90 ? 171 THR   A CA  1 
ATOM   1147 C  C   . THR   A 1 151 ? -30.503 -38.993 -18.743 1.00 133.13 ? 171 THR   A C   1 
ATOM   1148 O  O   . THR   A 1 151 ? -30.325 -39.494 -17.626 1.00 130.16 ? 171 THR   A O   1 
ATOM   1149 C  CB  . THR   A 1 151 ? -32.971 -38.557 -18.601 1.00 141.83 ? 171 THR   A CB  1 
ATOM   1150 O  OG1 . THR   A 1 151 ? -33.104 -39.312 -17.390 1.00 144.30 ? 171 THR   A OG1 1 
ATOM   1151 C  CG2 . THR   A 1 151 ? -34.289 -38.577 -19.359 1.00 144.67 ? 171 THR   A CG2 1 
ATOM   1152 N  N   . LEU   A 1 152 ? -29.564 -38.302 -19.387 1.00 119.71 ? 172 LEU   A N   1 
ATOM   1153 C  CA  . LEU   A 1 152 ? -28.216 -38.203 -18.839 1.00 118.08 ? 172 LEU   A CA  1 
ATOM   1154 C  C   . LEU   A 1 152 ? -28.178 -37.310 -17.606 1.00 117.96 ? 172 LEU   A C   1 
ATOM   1155 O  O   . LEU   A 1 152 ? -27.556 -37.663 -16.598 1.00 113.81 ? 172 LEU   A O   1 
ATOM   1156 C  CB  . LEU   A 1 152 ? -27.253 -37.685 -19.905 1.00 116.44 ? 172 LEU   A CB  1 
ATOM   1157 C  CG  . LEU   A 1 152 ? -27.091 -38.576 -21.133 1.00 110.97 ? 172 LEU   A CG  1 
ATOM   1158 C  CD1 . LEU   A 1 152 ? -26.063 -37.973 -22.061 1.00 104.91 ? 172 LEU   A CD1 1 
ATOM   1159 C  CD2 . LEU   A 1 152 ? -26.699 -39.989 -20.725 1.00 108.74 ? 172 LEU   A CD2 1 
ATOM   1160 N  N   . LYS   A 1 153 ? -28.842 -36.149 -17.663 1.00 116.01 ? 173 LYS   A N   1 
ATOM   1161 C  CA  . LYS   A 1 153 ? -28.734 -35.182 -16.573 1.00 113.19 ? 173 LYS   A CA  1 
ATOM   1162 C  C   . LYS   A 1 153 ? -29.173 -35.782 -15.243 1.00 114.03 ? 173 LYS   A C   1 
ATOM   1163 O  O   . LYS   A 1 153 ? -28.696 -35.357 -14.183 1.00 113.81 ? 173 LYS   A O   1 
ATOM   1164 C  CB  . LYS   A 1 153 ? -29.545 -33.922 -16.890 1.00 115.60 ? 173 LYS   A CB  1 
ATOM   1165 C  CG  . LYS   A 1 153 ? -31.003 -33.960 -16.444 1.00 120.09 ? 173 LYS   A CG  1 
ATOM   1166 C  CD  . LYS   A 1 153 ? -31.577 -32.553 -16.330 1.00 121.81 ? 173 LYS   A CD  1 
ATOM   1167 C  CE  . LYS   A 1 153 ? -32.934 -32.558 -15.642 1.00 123.77 ? 173 LYS   A CE  1 
ATOM   1168 N  NZ  . LYS   A 1 153 ? -33.148 -31.320 -14.838 1.00 125.05 ? 173 LYS   A NZ  1 
ATOM   1169 N  N   . ASP   A 1 154 ? -30.060 -36.777 -15.276 1.00 118.47 ? 174 ASP   A N   1 
ATOM   1170 C  CA  . ASP   A 1 154 ? -30.453 -37.481 -14.061 1.00 117.23 ? 174 ASP   A CA  1 
ATOM   1171 C  C   . ASP   A 1 154 ? -29.375 -38.465 -13.621 1.00 115.20 ? 174 ASP   A C   1 
ATOM   1172 O  O   . ASP   A 1 154 ? -28.854 -38.370 -12.506 1.00 112.26 ? 174 ASP   A O   1 
ATOM   1173 C  CB  . ASP   A 1 154 ? -31.784 -38.205 -14.284 1.00 123.85 ? 174 ASP   A CB  1 
ATOM   1174 C  CG  . ASP   A 1 154 ? -32.927 -37.247 -14.556 1.00 128.86 ? 174 ASP   A CG  1 
ATOM   1175 O  OD1 . ASP   A 1 154 ? -33.076 -36.265 -13.797 1.00 126.19 ? 174 ASP   A OD1 1 
ATOM   1176 O  OD2 . ASP   A 1 154 ? -33.671 -37.468 -15.534 1.00 139.47 ? 174 ASP   A OD2 1 
ATOM   1177 N  N   . VAL   A 1 155 ? -29.025 -39.413 -14.497 1.00 118.14 ? 175 VAL   A N   1 
ATOM   1178 C  CA  . VAL   A 1 155 ? -28.026 -40.421 -14.150 1.00 114.00 ? 175 VAL   A CA  1 
ATOM   1179 C  C   . VAL   A 1 155 ? -26.669 -39.778 -13.896 1.00 116.48 ? 175 VAL   A C   1 
ATOM   1180 O  O   . VAL   A 1 155 ? -25.863 -40.298 -13.114 1.00 116.06 ? 175 VAL   A O   1 
ATOM   1181 C  CB  . VAL   A 1 155 ? -27.949 -41.502 -15.248 1.00 114.39 ? 175 VAL   A CB  1 
ATOM   1182 C  CG1 . VAL   A 1 155 ? -29.340 -42.007 -15.589 1.00 121.86 ? 175 VAL   A CG1 1 
ATOM   1183 C  CG2 . VAL   A 1 155 ? -27.245 -40.975 -16.494 1.00 114.34 ? 175 VAL   A CG2 1 
ATOM   1184 N  N   . PHE   A 1 156 ? -26.392 -38.640 -14.538 1.00 111.73 ? 176 PHE   A N   1 
ATOM   1185 C  CA  . PHE   A 1 156 ? -25.155 -37.919 -14.257 1.00 109.60 ? 176 PHE   A CA  1 
ATOM   1186 C  C   . PHE   A 1 156 ? -25.274 -37.081 -12.992 1.00 113.53 ? 176 PHE   A C   1 
ATOM   1187 O  O   . PHE   A 1 156 ? -24.350 -37.063 -12.171 1.00 114.86 ? 176 PHE   A O   1 
ATOM   1188 C  CB  . PHE   A 1 156 ? -24.775 -37.033 -15.441 1.00 102.28 ? 176 PHE   A CB  1 
ATOM   1189 C  CG  . PHE   A 1 156 ? -23.994 -37.745 -16.502 1.00 96.79  ? 176 PHE   A CG  1 
ATOM   1190 C  CD1 . PHE   A 1 156 ? -22.953 -38.592 -16.161 1.00 96.41  ? 176 PHE   A CD1 1 
ATOM   1191 C  CD2 . PHE   A 1 156 ? -24.302 -37.571 -17.839 1.00 100.43 ? 176 PHE   A CD2 1 
ATOM   1192 C  CE1 . PHE   A 1 156 ? -22.230 -39.249 -17.138 1.00 93.39  ? 176 PHE   A CE1 1 
ATOM   1193 C  CE2 . PHE   A 1 156 ? -23.586 -38.226 -18.820 1.00 97.76  ? 176 PHE   A CE2 1 
ATOM   1194 C  CZ  . PHE   A 1 156 ? -22.548 -39.065 -18.471 1.00 88.89  ? 176 PHE   A CZ  1 
ATOM   1195 N  N   . GLY   A 1 157 ? -26.398 -36.380 -12.824 1.00 110.20 ? 177 GLY   A N   1 
ATOM   1196 C  CA  . GLY   A 1 157 ? -26.609 -35.625 -11.601 1.00 113.66 ? 177 GLY   A CA  1 
ATOM   1197 C  C   . GLY   A 1 157 ? -26.516 -36.492 -10.363 1.00 114.83 ? 177 GLY   A C   1 
ATOM   1198 O  O   . GLY   A 1 157 ? -25.917 -36.097 -9.360  1.00 116.02 ? 177 GLY   A O   1 
ATOM   1199 N  N   . ALA   A 1 158 ? -27.097 -37.692 -10.423 1.00 119.66 ? 178 ALA   A N   1 
ATOM   1200 C  CA  . ALA   A 1 158 ? -26.951 -38.646 -9.329  1.00 121.34 ? 178 ALA   A CA  1 
ATOM   1201 C  C   . ALA   A 1 158 ? -25.487 -39.006 -9.110  1.00 119.62 ? 178 ALA   A C   1 
ATOM   1202 O  O   . ALA   A 1 158 ? -25.009 -39.038 -7.970  1.00 119.58 ? 178 ALA   A O   1 
ATOM   1203 C  CB  . ALA   A 1 158 ? -27.776 -39.898 -9.617  1.00 123.06 ? 178 ALA   A CB  1 
ATOM   1204 N  N   . TYR   A 1 159 ? -24.758 -39.287 -10.195 1.00 122.13 ? 179 TYR   A N   1 
ATOM   1205 C  CA  . TYR   A 1 159 ? -23.323 -39.517 -10.067 1.00 119.64 ? 179 TYR   A CA  1 
ATOM   1206 C  C   . TYR   A 1 159 ? -22.622 -38.286 -9.515  1.00 121.68 ? 179 TYR   A C   1 
ATOM   1207 O  O   . TYR   A 1 159 ? -21.731 -38.397 -8.663  1.00 121.87 ? 179 TYR   A O   1 
ATOM   1208 C  CB  . TYR   A 1 159 ? -22.708 -39.897 -11.413 1.00 114.03 ? 179 TYR   A CB  1 
ATOM   1209 C  CG  . TYR   A 1 159 ? -21.197 -39.819 -11.390 1.00 114.88 ? 179 TYR   A CG  1 
ATOM   1210 C  CD1 . TYR   A 1 159 ? -20.448 -40.793 -10.745 1.00 119.54 ? 179 TYR   A CD1 1 
ATOM   1211 C  CD2 . TYR   A 1 159 ? -20.520 -38.762 -11.993 1.00 112.89 ? 179 TYR   A CD2 1 
ATOM   1212 C  CE1 . TYR   A 1 159 ? -19.070 -40.728 -10.708 1.00 118.80 ? 179 TYR   A CE1 1 
ATOM   1213 C  CE2 . TYR   A 1 159 ? -19.137 -38.686 -11.959 1.00 98.96  ? 179 TYR   A CE2 1 
ATOM   1214 C  CZ  . TYR   A 1 159 ? -18.419 -39.675 -11.315 1.00 113.20 ? 179 TYR   A CZ  1 
ATOM   1215 O  OH  . TYR   A 1 159 ? -17.045 -39.619 -11.274 1.00 110.45 ? 179 TYR   A OH  1 
ATOM   1216 N  N   . SER   A 1 160 ? -23.007 -37.103 -9.998  1.00 119.87 ? 180 SER   A N   1 
ATOM   1217 C  CA  . SER   A 1 160 ? -22.365 -35.877 -9.546  1.00 122.35 ? 180 SER   A CA  1 
ATOM   1218 C  C   . SER   A 1 160 ? -22.632 -35.609 -8.074  1.00 123.70 ? 180 SER   A C   1 
ATOM   1219 O  O   . SER   A 1 160 ? -21.752 -35.100 -7.375  1.00 123.53 ? 180 SER   A O   1 
ATOM   1220 C  CB  . SER   A 1 160 ? -22.834 -34.695 -10.393 1.00 117.92 ? 180 SER   A CB  1 
ATOM   1221 O  OG  . SER   A 1 160 ? -22.082 -33.542 -10.077 1.00 114.21 ? 180 SER   A OG  1 
ATOM   1222 N  N   . MET   A 1 161 ? -23.823 -35.945 -7.577  1.00 124.97 ? 181 MET   A N   1 
ATOM   1223 C  CA  . MET   A 1 161 ? -24.055 -35.792 -6.147  1.00 125.99 ? 181 MET   A CA  1 
ATOM   1224 C  C   . MET   A 1 161 ? -23.312 -36.860 -5.356  1.00 127.13 ? 181 MET   A C   1 
ATOM   1225 O  O   . MET   A 1 161 ? -22.743 -36.564 -4.301  1.00 127.89 ? 181 MET   A O   1 
ATOM   1226 C  CB  . MET   A 1 161 ? -25.551 -35.824 -5.831  1.00 128.38 ? 181 MET   A CB  1 
ATOM   1227 C  CG  . MET   A 1 161 ? -25.852 -35.254 -4.446  1.00 129.17 ? 181 MET   A CG  1 
ATOM   1228 S  SD  . MET   A 1 161 ? -24.716 -33.885 -4.124  1.00 132.22 ? 181 MET   A SD  1 
ATOM   1229 C  CE  . MET   A 1 161 ? -25.026 -33.510 -2.406  1.00 140.05 ? 181 MET   A CE  1 
ATOM   1230 N  N   . ASP   A 1 162 ? -23.286 -38.099 -5.860  1.00 127.25 ? 182 ASP   A N   1 
ATOM   1231 C  CA  . ASP   A 1 162 ? -22.551 -39.169 -5.188  1.00 130.04 ? 182 ASP   A CA  1 
ATOM   1232 C  C   . ASP   A 1 162 ? -21.102 -38.777 -4.928  1.00 131.70 ? 182 ASP   A C   1 
ATOM   1233 O  O   . ASP   A 1 162 ? -20.540 -39.104 -3.876  1.00 132.62 ? 182 ASP   A O   1 
ATOM   1234 C  CB  . ASP   A 1 162 ? -22.596 -40.456 -6.017  1.00 131.04 ? 182 ASP   A CB  1 
ATOM   1235 C  CG  . ASP   A 1 162 ? -23.840 -41.281 -5.753  1.00 134.51 ? 182 ASP   A CG  1 
ATOM   1236 O  OD1 . ASP   A 1 162 ? -24.883 -40.689 -5.416  1.00 135.00 ? 182 ASP   A OD1 1 
ATOM   1237 O  OD2 . ASP   A 1 162 ? -23.768 -42.526 -5.871  1.00 138.25 ? 182 ASP   A OD2 1 
ATOM   1238 N  N   . VAL   A 1 163 ? -20.477 -38.077 -5.877  1.00 130.89 ? 183 VAL   A N   1 
ATOM   1239 C  CA  . VAL   A 1 163 ? -19.073 -37.714 -5.716  1.00 132.29 ? 183 VAL   A CA  1 
ATOM   1240 C  C   . VAL   A 1 163 ? -18.890 -36.496 -4.813  1.00 131.96 ? 183 VAL   A C   1 
ATOM   1241 O  O   . VAL   A 1 163 ? -17.818 -36.333 -4.227  1.00 130.65 ? 183 VAL   A O   1 
ATOM   1242 C  CB  . VAL   A 1 163 ? -18.415 -37.511 -7.097  1.00 124.40 ? 183 VAL   A CB  1 
ATOM   1243 C  CG1 . VAL   A 1 163 ? -19.048 -36.357 -7.844  1.00 124.10 ? 183 VAL   A CG1 1 
ATOM   1244 C  CG2 . VAL   A 1 163 ? -16.907 -37.312 -6.970  1.00 124.37 ? 183 VAL   A CG2 1 
ATOM   1245 N  N   . ILE   A 1 164 ? -19.907 -35.652 -4.644  1.00 134.70 ? 184 ILE   A N   1 
ATOM   1246 C  CA  . ILE   A 1 164 ? -19.783 -34.516 -3.728  1.00 139.14 ? 184 ILE   A CA  1 
ATOM   1247 C  C   . ILE   A 1 164 ? -19.841 -34.975 -2.283  1.00 144.49 ? 184 ILE   A C   1 
ATOM   1248 O  O   . ILE   A 1 164 ? -18.922 -34.718 -1.497  1.00 150.00 ? 184 ILE   A O   1 
ATOM   1249 C  CB  . ILE   A 1 164 ? -20.878 -33.476 -3.990  1.00 135.32 ? 184 ILE   A CB  1 
ATOM   1250 C  CG1 . ILE   A 1 164 ? -20.701 -32.846 -5.348  1.00 130.79 ? 184 ILE   A CG1 1 
ATOM   1251 C  CG2 . ILE   A 1 164 ? -20.872 -32.414 -2.902  1.00 134.97 ? 184 ILE   A CG2 1 
ATOM   1252 C  CD1 . ILE   A 1 164 ? -21.987 -32.447 -5.847  1.00 122.80 ? 184 ILE   A CD1 1 
ATOM   1253 N  N   . THR   A 1 165 ? -20.957 -35.602 -1.909  1.00 138.77 ? 185 THR   A N   1 
ATOM   1254 C  CA  . THR   A 1 165 ? -21.152 -36.091 -0.551  1.00 143.67 ? 185 THR   A CA  1 
ATOM   1255 C  C   . THR   A 1 165 ? -19.905 -36.805 -0.054  1.00 148.08 ? 185 THR   A C   1 
ATOM   1256 O  O   . THR   A 1 165 ? -19.417 -36.549 1.052   1.00 161.70 ? 185 THR   A O   1 
ATOM   1257 C  CB  . THR   A 1 165 ? -22.350 -37.041 -0.509  1.00 146.03 ? 185 THR   A CB  1 
ATOM   1258 O  OG1 . THR   A 1 165 ? -21.979 -38.301 -1.083  1.00 143.21 ? 185 THR   A OG1 1 
ATOM   1259 C  CG2 . THR   A 1 165 ? -23.520 -36.475 -1.284  1.00 139.37 ? 185 THR   A CG2 1 
ATOM   1260 N  N   . SER   A 1 166 ? -19.362 -37.687 -0.893  1.00 155.07 ? 186 SER   A N   1 
ATOM   1261 C  CA  . SER   A 1 166 ? -18.145 -38.407 -0.542  1.00 154.79 ? 186 SER   A CA  1 
ATOM   1262 C  C   . SER   A 1 166 ? -16.953 -37.462 -0.435  1.00 158.37 ? 186 SER   A C   1 
ATOM   1263 O  O   . SER   A 1 166 ? -16.219 -37.484 0.559   1.00 160.12 ? 186 SER   A O   1 
ATOM   1264 C  CB  . SER   A 1 166 ? -17.880 -39.500 -1.575  1.00 150.91 ? 186 SER   A CB  1 
ATOM   1265 O  OG  . SER   A 1 166 ? -18.029 -39.003 -2.895  1.00 149.81 ? 186 SER   A OG  1 
ATOM   1266 N  N   . THR   A 1 167 ? -16.746 -36.618 -1.449  1.00 151.00 ? 187 THR   A N   1 
ATOM   1267 C  CA  . THR   A 1 167 ? -15.542 -35.792 -1.481  1.00 155.62 ? 187 THR   A CA  1 
ATOM   1268 C  C   . THR   A 1 167 ? -15.547 -34.683 -0.437  1.00 166.21 ? 187 THR   A C   1 
ATOM   1269 O  O   . THR   A 1 167 ? -14.476 -34.167 -0.107  1.00 163.29 ? 187 THR   A O   1 
ATOM   1270 C  CB  . THR   A 1 167 ? -15.347 -35.168 -2.865  1.00 148.77 ? 187 THR   A CB  1 
ATOM   1271 O  OG1 . THR   A 1 167 ? -16.598 -34.662 -3.346  1.00 146.68 ? 187 THR   A OG1 1 
ATOM   1272 C  CG2 . THR   A 1 167 ? -14.794 -36.192 -3.850  1.00 138.68 ? 187 THR   A CG2 1 
ATOM   1273 N  N   . SER   A 1 168 ? -16.711 -34.299 0.089   1.00 201.65 ? 188 SER   A N   1 
ATOM   1274 C  CA  . SER   A 1 168 ? -16.787 -33.150 0.980   1.00 207.27 ? 188 SER   A CA  1 
ATOM   1275 C  C   . SER   A 1 168 ? -17.297 -33.458 2.380   1.00 207.39 ? 188 SER   A C   1 
ATOM   1276 O  O   . SER   A 1 168 ? -17.142 -32.611 3.267   1.00 211.11 ? 188 SER   A O   1 
ATOM   1277 C  CB  . SER   A 1 168 ? -17.666 -32.050 0.362   1.00 204.05 ? 188 SER   A CB  1 
ATOM   1278 O  OG  . SER   A 1 168 ? -18.874 -32.578 -0.153  1.00 203.19 ? 188 SER   A OG  1 
ATOM   1279 N  N   . PHE   A 1 169 ? -17.893 -34.608 2.580   1.00 196.81 ? 189 PHE   A N   1 
ATOM   1280 C  CA  . PHE   A 1 169 ? -18.364 -34.930 3.923   1.00 205.11 ? 189 PHE   A CA  1 
ATOM   1281 C  C   . PHE   A 1 169 ? -18.244 -36.399 4.288   1.00 225.08 ? 189 PHE   A C   1 
ATOM   1282 O  O   . PHE   A 1 169 ? -18.518 -36.748 5.442   1.00 237.58 ? 189 PHE   A O   1 
ATOM   1283 C  CB  . PHE   A 1 169 ? -19.828 -34.502 4.091   1.00 200.36 ? 189 PHE   A CB  1 
ATOM   1284 C  CG  . PHE   A 1 169 ? -20.085 -33.058 3.776   1.00 197.39 ? 189 PHE   A CG  1 
ATOM   1285 C  CD1 . PHE   A 1 169 ? -19.889 -32.076 4.734   1.00 189.39 ? 189 PHE   A CD1 1 
ATOM   1286 C  CD2 . PHE   A 1 169 ? -20.522 -32.684 2.518   1.00 190.56 ? 189 PHE   A CD2 1 
ATOM   1287 C  CE1 . PHE   A 1 169 ? -20.130 -30.751 4.440   1.00 178.33 ? 189 PHE   A CE1 1 
ATOM   1288 C  CE2 . PHE   A 1 169 ? -20.758 -31.366 2.221   1.00 180.53 ? 189 PHE   A CE2 1 
ATOM   1289 C  CZ  . PHE   A 1 169 ? -20.565 -30.398 3.181   1.00 168.44 ? 189 PHE   A CZ  1 
ATOM   1290 N  N   . GLY   A 1 170 ? -17.861 -37.270 3.359   1.00 189.16 ? 190 GLY   A N   1 
ATOM   1291 C  CA  . GLY   A 1 170 ? -17.893 -38.693 3.615   1.00 176.50 ? 190 GLY   A CA  1 
ATOM   1292 C  C   . GLY   A 1 170 ? -19.272 -39.301 3.723   1.00 172.91 ? 190 GLY   A C   1 
ATOM   1293 O  O   . GLY   A 1 170 ? -19.410 -40.379 4.308   1.00 169.78 ? 190 GLY   A O   1 
ATOM   1294 N  N   . VAL   A 1 171 ? -20.295 -38.647 3.181   1.00 156.66 ? 191 VAL   A N   1 
ATOM   1295 C  CA  . VAL   A 1 171 ? -21.652 -39.180 3.158   1.00 157.00 ? 191 VAL   A CA  1 
ATOM   1296 C  C   . VAL   A 1 171 ? -21.759 -40.056 1.913   1.00 151.22 ? 191 VAL   A C   1 
ATOM   1297 O  O   . VAL   A 1 171 ? -21.665 -39.562 0.787   1.00 149.91 ? 191 VAL   A O   1 
ATOM   1298 C  CB  . VAL   A 1 171 ? -22.691 -38.050 3.157   1.00 155.49 ? 191 VAL   A CB  1 
ATOM   1299 C  CG1 . VAL   A 1 171 ? -24.098 -38.597 3.071   1.00 147.27 ? 191 VAL   A CG1 1 
ATOM   1300 C  CG2 . VAL   A 1 171 ? -22.535 -37.177 4.398   1.00 163.07 ? 191 VAL   A CG2 1 
ATOM   1301 N  N   . ASN   A 1 172 ? -21.920 -41.360 2.108   1.00 140.97 ? 192 ASN   A N   1 
ATOM   1302 C  CA  . ASN   A 1 172 ? -21.888 -42.316 1.004   1.00 145.08 ? 192 ASN   A CA  1 
ATOM   1303 C  C   . ASN   A 1 172 ? -23.317 -42.752 0.682   1.00 149.71 ? 192 ASN   A C   1 
ATOM   1304 O  O   . ASN   A 1 172 ? -23.917 -43.563 1.396   1.00 156.45 ? 192 ASN   A O   1 
ATOM   1305 C  CB  . ASN   A 1 172 ? -20.988 -43.499 1.350   1.00 144.04 ? 192 ASN   A CB  1 
ATOM   1306 C  CG  . ASN   A 1 172 ? -20.955 -44.545 0.233   1.00 147.80 ? 192 ASN   A CG  1 
ATOM   1307 O  OD1 . ASN   A 1 172 ? -21.741 -44.491 -0.713  1.00 150.12 ? 192 ASN   A OD1 1 
ATOM   1308 N  ND2 . ASN   A 1 172 ? -20.030 -45.498 0.341   1.00 150.36 ? 192 ASN   A ND2 1 
ATOM   1309 N  N   . ILE   A 1 173 ? -23.853 -42.227 -0.417  1.00 151.12 ? 193 ILE   A N   1 
ATOM   1310 C  CA  . ILE   A 1 173 ? -25.228 -42.476 -0.830  1.00 153.31 ? 193 ILE   A CA  1 
ATOM   1311 C  C   . ILE   A 1 173 ? -25.261 -42.820 -2.310  1.00 151.54 ? 193 ILE   A C   1 
ATOM   1312 O  O   . ILE   A 1 173 ? -24.521 -42.240 -3.114  1.00 150.95 ? 193 ILE   A O   1 
ATOM   1313 C  CB  . ILE   A 1 173 ? -26.129 -41.251 -0.570  1.00 154.69 ? 193 ILE   A CB  1 
ATOM   1314 C  CG1 . ILE   A 1 173 ? -26.069 -40.842 0.893   1.00 152.57 ? 193 ILE   A CG1 1 
ATOM   1315 C  CG2 . ILE   A 1 173 ? -27.582 -41.513 -0.957  1.00 163.50 ? 193 ILE   A CG2 1 
ATOM   1316 C  CD1 . ILE   A 1 173 ? -26.849 -39.581 1.159   1.00 155.20 ? 193 ILE   A CD1 1 
ATOM   1317 N  N   . ASP   A 1 174 ? -26.160 -43.737 -2.668  1.00 168.84 ? 194 ASP   A N   1 
ATOM   1318 C  CA  . ASP   A 1 174 ? -26.507 -44.007 -4.056  1.00 169.09 ? 194 ASP   A CA  1 
ATOM   1319 C  C   . ASP   A 1 174 ? -27.732 -43.149 -4.327  1.00 171.04 ? 194 ASP   A C   1 
ATOM   1320 O  O   . ASP   A 1 174 ? -28.876 -43.594 -4.241  1.00 177.50 ? 194 ASP   A O   1 
ATOM   1321 C  CB  . ASP   A 1 174 ? -26.785 -45.489 -4.266  1.00 180.52 ? 194 ASP   A CB  1 
ATOM   1322 C  CG  . ASP   A 1 174 ? -26.801 -45.872 -5.727  1.00 181.73 ? 194 ASP   A CG  1 
ATOM   1323 O  OD1 . ASP   A 1 174 ? -26.629 -44.979 -6.583  1.00 172.72 ? 194 ASP   A OD1 1 
ATOM   1324 O  OD2 . ASP   A 1 174 ? -26.972 -47.069 -6.020  1.00 185.71 ? 194 ASP   A OD2 1 
ATOM   1325 N  N   . SER   A 1 175 ? -27.468 -41.882 -4.640  1.00 163.32 ? 195 SER   A N   1 
ATOM   1326 C  CA  . SER   A 1 175 ? -28.515 -40.864 -4.607  1.00 162.53 ? 195 SER   A CA  1 
ATOM   1327 C  C   . SER   A 1 175 ? -29.666 -41.166 -5.555  1.00 168.25 ? 195 SER   A C   1 
ATOM   1328 O  O   . SER   A 1 175 ? -30.807 -40.800 -5.272  1.00 172.62 ? 195 SER   A O   1 
ATOM   1329 C  CB  . SER   A 1 175 ? -27.915 -39.498 -4.936  1.00 151.49 ? 195 SER   A CB  1 
ATOM   1330 O  OG  . SER   A 1 175 ? -26.926 -39.132 -3.998  1.00 152.77 ? 195 SER   A OG  1 
ATOM   1331 N  N   . LEU   A 1 176 ? -29.403 -41.798 -6.696  1.00 164.74 ? 196 LEU   A N   1 
ATOM   1332 C  CA  . LEU   A 1 176 ? -30.504 -42.136 -7.602  1.00 172.08 ? 196 LEU   A CA  1 
ATOM   1333 C  C   . LEU   A 1 176 ? -31.370 -43.262 -7.030  1.00 188.97 ? 196 LEU   A C   1 
ATOM   1334 O  O   . LEU   A 1 176 ? -32.606 -43.183 -7.029  1.00 179.23 ? 196 LEU   A O   1 
ATOM   1335 C  CB  . LEU   A 1 176 ? -29.936 -42.504 -8.972  1.00 171.14 ? 196 LEU   A CB  1 
ATOM   1336 C  CG  . LEU   A 1 176 ? -30.950 -42.398 -10.114 1.00 158.29 ? 196 LEU   A CG  1 
ATOM   1337 C  CD1 . LEU   A 1 176 ? -31.895 -41.214 -9.920  1.00 159.42 ? 196 LEU   A CD1 1 
ATOM   1338 C  CD2 . LEU   A 1 176 ? -30.271 -42.316 -11.466 1.00 137.16 ? 196 LEU   A CD2 1 
ATOM   1339 N  N   . ASN   A 1 177 ? -30.736 -44.321 -6.538  1.00 209.50 ? 197 ASN   A N   1 
ATOM   1340 C  CA  . ASN   A 1 177 ? -31.468 -45.406 -5.899  1.00 205.41 ? 197 ASN   A CA  1 
ATOM   1341 C  C   . ASN   A 1 177 ? -31.835 -45.096 -4.456  1.00 196.31 ? 197 ASN   A C   1 
ATOM   1342 O  O   . ASN   A 1 177 ? -32.648 -45.821 -3.872  1.00 203.72 ? 197 ASN   A O   1 
ATOM   1343 C  CB  . ASN   A 1 177 ? -30.644 -46.686 -5.958  1.00 209.10 ? 197 ASN   A CB  1 
ATOM   1344 C  CG  . ASN   A 1 177 ? -29.899 -46.827 -7.258  1.00 210.36 ? 197 ASN   A CG  1 
ATOM   1345 O  OD1 . ASN   A 1 177 ? -29.248 -45.889 -7.717  1.00 228.08 ? 197 ASN   A OD1 1 
ATOM   1346 N  ND2 . ASN   A 1 177 ? -30.004 -47.999 -7.876  1.00 195.13 ? 197 ASN   A ND2 1 
ATOM   1347 N  N   . ASN   A 1 178 ? -31.260 -44.041 -3.872  1.00 192.32 ? 198 ASN   A N   1 
ATOM   1348 C  CA  . ASN   A 1 178 ? -31.636 -43.553 -2.546  1.00 193.33 ? 198 ASN   A CA  1 
ATOM   1349 C  C   . ASN   A 1 178 ? -32.151 -42.122 -2.672  1.00 189.83 ? 198 ASN   A C   1 
ATOM   1350 O  O   . ASN   A 1 178 ? -31.529 -41.184 -2.153  1.00 186.05 ? 198 ASN   A O   1 
ATOM   1351 C  CB  . ASN   A 1 178 ? -30.464 -43.589 -1.566  1.00 197.34 ? 198 ASN   A CB  1 
ATOM   1352 C  CG  . ASN   A 1 178 ? -29.720 -44.910 -1.569  1.00 213.14 ? 198 ASN   A CG  1 
ATOM   1353 O  OD1 . ASN   A 1 178 ? -30.037 -45.818 -2.331  1.00 209.90 ? 198 ASN   A OD1 1 
ATOM   1354 N  ND2 . ASN   A 1 178 ? -28.706 -45.014 -0.715  1.00 239.98 ? 198 ASN   A ND2 1 
ATOM   1355 N  N   . PRO   A 1 179 ? -33.287 -41.914 -3.347  1.00 210.23 ? 199 PRO   A N   1 
ATOM   1356 C  CA  . PRO   A 1 179 ? -33.791 -40.540 -3.491  1.00 200.08 ? 199 PRO   A CA  1 
ATOM   1357 C  C   . PRO   A 1 179 ? -34.243 -39.944 -2.176  1.00 205.29 ? 199 PRO   A C   1 
ATOM   1358 O  O   . PRO   A 1 179 ? -34.150 -38.723 -2.000  1.00 201.08 ? 199 PRO   A O   1 
ATOM   1359 C  CB  . PRO   A 1 179 ? -34.958 -40.699 -4.472  1.00 182.71 ? 199 PRO   A CB  1 
ATOM   1360 C  CG  . PRO   A 1 179 ? -35.444 -42.088 -4.226  1.00 189.33 ? 199 PRO   A CG  1 
ATOM   1361 C  CD  . PRO   A 1 179 ? -34.222 -42.903 -3.914  1.00 200.99 ? 199 PRO   A CD  1 
ATOM   1362 N  N   . GLN   A 1 180 ? -34.709 -40.781 -1.247  1.00 234.69 ? 200 GLN   A N   1 
ATOM   1363 C  CA  . GLN   A 1 180 ? -35.213 -40.303 0.034   1.00 230.51 ? 200 GLN   A CA  1 
ATOM   1364 C  C   . GLN   A 1 180 ? -34.192 -39.416 0.734   1.00 225.67 ? 200 GLN   A C   1 
ATOM   1365 O  O   . GLN   A 1 180 ? -34.514 -38.302 1.158   1.00 224.11 ? 200 GLN   A O   1 
ATOM   1366 C  CB  . GLN   A 1 180 ? -35.592 -41.493 0.922   1.00 231.56 ? 200 GLN   A CB  1 
ATOM   1367 C  CG  . GLN   A 1 180 ? -35.760 -42.822 0.177   1.00 234.08 ? 200 GLN   A CG  1 
ATOM   1368 C  CD  . GLN   A 1 180 ? -34.427 -43.479 -0.193  1.00 230.96 ? 200 GLN   A CD  1 
ATOM   1369 O  OE1 . GLN   A 1 180 ? -33.367 -43.019 0.225   1.00 238.12 ? 200 GLN   A OE1 1 
ATOM   1370 N  NE2 . GLN   A 1 180 ? -34.481 -44.551 -0.987  1.00 232.87 ? 200 GLN   A NE2 1 
ATOM   1371 N  N   . ASP   A 1 181 ? -32.964 -39.900 0.878   1.00 199.08 ? 201 ASP   A N   1 
ATOM   1372 C  CA  . ASP   A 1 181 ? -31.894 -39.072 1.416   1.00 187.49 ? 201 ASP   A CA  1 
ATOM   1373 C  C   . ASP   A 1 181 ? -31.625 -38.028 0.343   1.00 180.85 ? 201 ASP   A C   1 
ATOM   1374 O  O   . ASP   A 1 181 ? -31.205 -38.387 -0.768  1.00 179.49 ? 201 ASP   A O   1 
ATOM   1375 C  CB  . ASP   A 1 181 ? -30.675 -39.919 1.770   1.00 179.68 ? 201 ASP   A CB  1 
ATOM   1376 C  CG  . ASP   A 1 181 ? -29.760 -39.231 2.757   1.00 170.68 ? 201 ASP   A CG  1 
ATOM   1377 O  OD1 . ASP   A 1 181 ? -29.685 -37.981 2.736   1.00 169.19 ? 201 ASP   A OD1 1 
ATOM   1378 O  OD2 . ASP   A 1 181 ? -29.115 -39.947 3.552   1.00 164.76 ? 201 ASP   A OD2 1 
ATOM   1379 N  N   . PRO   A 1 182 ? -31.968 -36.733 0.545   1.00 169.20 ? 202 PRO   A N   1 
ATOM   1380 C  CA  . PRO   A 1 182 ? -31.873 -35.747 -0.527  1.00 159.91 ? 202 PRO   A CA  1 
ATOM   1381 C  C   . PRO   A 1 182 ? -30.764 -34.698 -0.407  1.00 152.48 ? 202 PRO   A C   1 
ATOM   1382 O  O   . PRO   A 1 182 ? -31.075 -33.525 -0.511  1.00 151.40 ? 202 PRO   A O   1 
ATOM   1383 C  CB  . PRO   A 1 182 ? -33.211 -35.032 -0.299  1.00 156.80 ? 202 PRO   A CB  1 
ATOM   1384 C  CG  . PRO   A 1 182 ? -33.327 -34.953 1.216   1.00 156.37 ? 202 PRO   A CG  1 
ATOM   1385 C  CD  . PRO   A 1 182 ? -32.497 -36.100 1.760   1.00 165.66 ? 202 PRO   A CD  1 
ATOM   1386 N  N   . PHE   A 1 183 ? -29.515 -35.121 -0.199  1.00 144.68 ? 203 PHE   A N   1 
ATOM   1387 C  CA  . PHE   A 1 183 ? -28.452 -34.085 -0.212  1.00 145.60 ? 203 PHE   A CA  1 
ATOM   1388 C  C   . PHE   A 1 183 ? -28.618 -33.291 -1.511  1.00 143.88 ? 203 PHE   A C   1 
ATOM   1389 O  O   . PHE   A 1 183 ? -28.193 -32.124 -1.558  1.00 141.68 ? 203 PHE   A O   1 
ATOM   1390 C  CB  . PHE   A 1 183 ? -27.068 -34.715 -0.060  1.00 143.85 ? 203 PHE   A CB  1 
ATOM   1391 C  CG  . PHE   A 1 183 ? -26.612 -34.890 1.365   1.00 143.94 ? 203 PHE   A CG  1 
ATOM   1392 C  CD1 . PHE   A 1 183 ? -27.461 -35.424 2.321   1.00 141.50 ? 203 PHE   A CD1 1 
ATOM   1393 C  CD2 . PHE   A 1 183 ? -25.335 -34.520 1.752   1.00 144.93 ? 203 PHE   A CD2 1 
ATOM   1394 C  CE1 . PHE   A 1 183 ? -27.042 -35.583 3.631   1.00 146.34 ? 203 PHE   A CE1 1 
ATOM   1395 C  CE2 . PHE   A 1 183 ? -24.917 -34.679 3.063   1.00 142.13 ? 203 PHE   A CE2 1 
ATOM   1396 C  CZ  . PHE   A 1 183 ? -25.771 -35.210 4.000   1.00 145.70 ? 203 PHE   A CZ  1 
ATOM   1397 N  N   . VAL   A 1 184 ? -29.246 -33.902 -2.518  1.00 149.28 ? 204 VAL   A N   1 
ATOM   1398 C  CA  . VAL   A 1 184 ? -29.518 -33.186 -3.798  1.00 142.99 ? 204 VAL   A CA  1 
ATOM   1399 C  C   . VAL   A 1 184 ? -30.864 -32.488 -3.548  1.00 141.31 ? 204 VAL   A C   1 
ATOM   1400 O  O   . VAL   A 1 184 ? -31.834 -32.771 -4.277  1.00 137.99 ? 204 VAL   A O   1 
ATOM   1401 C  CB  . VAL   A 1 184 ? -29.565 -34.184 -4.973  1.00 140.62 ? 204 VAL   A CB  1 
ATOM   1402 C  CG1 . VAL   A 1 184 ? -30.219 -35.505 -4.595  1.00 139.47 ? 204 VAL   A CG1 1 
ATOM   1403 C  CG2 . VAL   A 1 184 ? -30.180 -33.593 -6.233  1.00 134.77 ? 204 VAL   A CG2 1 
ATOM   1404 N  N   . GLU   A 1 185 ? -30.922 -31.602 -2.546  1.00 139.78 ? 205 GLU   A N   1 
ATOM   1405 C  CA  . GLU   A 1 185 ? -32.166 -30.834 -2.280  1.00 134.53 ? 205 GLU   A CA  1 
ATOM   1406 C  C   . GLU   A 1 185 ? -32.094 -29.678 -3.274  1.00 132.20 ? 205 GLU   A C   1 
ATOM   1407 O  O   . GLU   A 1 185 ? -33.040 -29.533 -4.065  1.00 136.83 ? 205 GLU   A O   1 
ATOM   1408 C  CB  . GLU   A 1 185 ? -32.189 -30.289 -0.855  1.00 135.04 ? 205 GLU   A CB  1 
ATOM   1409 C  CG  . GLU   A 1 185 ? -33.537 -30.403 -0.174  1.00 137.41 ? 205 GLU   A CG  1 
ATOM   1410 C  CD  . GLU   A 1 185 ? -33.501 -31.245 1.088   1.00 141.94 ? 205 GLU   A CD  1 
ATOM   1411 O  OE1 . GLU   A 1 185 ? -32.416 -31.764 1.413   1.00 142.85 ? 205 GLU   A OE1 1 
ATOM   1412 O  OE2 . GLU   A 1 185 ? -34.553 -31.378 1.742   1.00 140.29 ? 205 GLU   A OE2 1 
ATOM   1413 N  N   . ASN   A 1 186 ? -31.010 -28.898 -3.231  1.00 133.64 ? 206 ASN   A N   1 
ATOM   1414 C  CA  . ASN   A 1 186 ? -30.805 -27.793 -4.207  1.00 134.17 ? 206 ASN   A CA  1 
ATOM   1415 C  C   . ASN   A 1 186 ? -32.149 -27.161 -4.581  1.00 129.31 ? 206 ASN   A C   1 
ATOM   1416 O  O   . ASN   A 1 186 ? -32.153 -26.369 -5.543  1.00 121.13 ? 206 ASN   A O   1 
ATOM   1417 C  CB  . ASN   A 1 186 ? -30.061 -28.277 -5.455  1.00 131.11 ? 206 ASN   A CB  1 
ATOM   1418 C  CG  . ASN   A 1 186 ? -30.990 -28.784 -6.537  1.00 132.21 ? 206 ASN   A CG  1 
ATOM   1419 O  OD1 . ASN   A 1 186 ? -31.025 -28.234 -7.635  1.00 131.38 ? 206 ASN   A OD1 1 
ATOM   1420 N  ND2 . ASN   A 1 186 ? -31.747 -29.825 -6.235  1.00 130.58 ? 206 ASN   A ND2 1 
ATOM   1421 N  N   . ASP   A 1 197 ? -34.891 -15.336 -14.077 1.00 147.74 ? 217 ASP   A N   1 
ATOM   1422 C  CA  . ASP   A 1 197 ? -36.297 -15.493 -13.725 1.00 149.70 ? 217 ASP   A CA  1 
ATOM   1423 C  C   . ASP   A 1 197 ? -36.859 -14.121 -13.318 1.00 148.62 ? 217 ASP   A C   1 
ATOM   1424 O  O   . ASP   A 1 197 ? -36.091 -13.168 -13.189 1.00 137.53 ? 217 ASP   A O   1 
ATOM   1425 C  CB  . ASP   A 1 197 ? -36.455 -16.556 -12.615 1.00 151.39 ? 217 ASP   A CB  1 
ATOM   1426 C  CG  . ASP   A 1 197 ? -35.826 -16.144 -11.290 1.00 148.25 ? 217 ASP   A CG  1 
ATOM   1427 O  OD1 . ASP   A 1 197 ? -35.484 -14.960 -11.113 1.00 141.60 ? 217 ASP   A OD1 1 
ATOM   1428 O  OD2 . ASP   A 1 197 ? -35.674 -17.020 -10.410 1.00 155.60 ? 217 ASP   A OD2 1 
ATOM   1429 N  N   . PRO   A 1 198 ? -38.180 -14.016 -13.128 1.00 151.96 ? 218 PRO   A N   1 
ATOM   1430 C  CA  . PRO   A 1 198 ? -38.759 -12.723 -12.720 1.00 149.61 ? 218 PRO   A CA  1 
ATOM   1431 C  C   . PRO   A 1 198 ? -38.115 -12.080 -11.500 1.00 147.59 ? 218 PRO   A C   1 
ATOM   1432 O  O   . PRO   A 1 198 ? -38.118 -10.846 -11.395 1.00 146.79 ? 218 PRO   A O   1 
ATOM   1433 C  CB  . PRO   A 1 198 ? -40.223 -13.082 -12.445 1.00 146.22 ? 218 PRO   A CB  1 
ATOM   1434 C  CG  . PRO   A 1 198 ? -40.503 -14.190 -13.382 1.00 150.73 ? 218 PRO   A CG  1 
ATOM   1435 C  CD  . PRO   A 1 198 ? -39.231 -14.991 -13.476 1.00 152.55 ? 218 PRO   A CD  1 
ATOM   1436 N  N   . PHE   A 1 199 ? -37.566 -12.866 -10.572 1.00 135.84 ? 219 PHE   A N   1 
ATOM   1437 C  CA  . PHE   A 1 199 ? -37.075 -12.294 -9.321  1.00 126.22 ? 219 PHE   A CA  1 
ATOM   1438 C  C   . PHE   A 1 199 ? -35.836 -11.435 -9.547  1.00 126.37 ? 219 PHE   A C   1 
ATOM   1439 O  O   . PHE   A 1 199 ? -35.827 -10.242 -9.224  1.00 122.88 ? 219 PHE   A O   1 
ATOM   1440 C  CB  . PHE   A 1 199 ? -36.782 -13.402 -8.309  1.00 122.95 ? 219 PHE   A CB  1 
ATOM   1441 C  CG  . PHE   A 1 199 ? -36.449 -12.890 -6.937  1.00 116.94 ? 219 PHE   A CG  1 
ATOM   1442 C  CD1 . PHE   A 1 199 ? -37.450 -12.441 -6.093  1.00 114.28 ? 219 PHE   A CD1 1 
ATOM   1443 C  CD2 . PHE   A 1 199 ? -35.138 -12.853 -6.491  1.00 116.65 ? 219 PHE   A CD2 1 
ATOM   1444 C  CE1 . PHE   A 1 199 ? -37.149 -11.965 -4.832  1.00 111.00 ? 219 PHE   A CE1 1 
ATOM   1445 C  CE2 . PHE   A 1 199 ? -34.834 -12.378 -5.228  1.00 112.81 ? 219 PHE   A CE2 1 
ATOM   1446 C  CZ  . PHE   A 1 199 ? -35.842 -11.934 -4.399  1.00 110.13 ? 219 PHE   A CZ  1 
ATOM   1447 N  N   . PHE   A 1 200 ? -34.776 -12.025 -10.107 1.00 121.01 ? 220 PHE   A N   1 
ATOM   1448 C  CA  . PHE   A 1 200 ? -33.500 -11.319 -10.192 1.00 118.70 ? 220 PHE   A CA  1 
ATOM   1449 C  C   . PHE   A 1 200 ? -33.566 -10.129 -11.142 1.00 111.95 ? 220 PHE   A C   1 
ATOM   1450 O  O   . PHE   A 1 200 ? -32.803 -9.170  -10.980 1.00 108.33 ? 220 PHE   A O   1 
ATOM   1451 C  CB  . PHE   A 1 200 ? -32.389 -12.278 -10.620 1.00 123.95 ? 220 PHE   A CB  1 
ATOM   1452 C  CG  . PHE   A 1 200 ? -32.162 -13.415 -9.660  1.00 126.83 ? 220 PHE   A CG  1 
ATOM   1453 C  CD1 . PHE   A 1 200 ? -32.953 -14.547 -9.715  1.00 129.03 ? 220 PHE   A CD1 1 
ATOM   1454 C  CD2 . PHE   A 1 200 ? -31.155 -13.355 -8.712  1.00 126.76 ? 220 PHE   A CD2 1 
ATOM   1455 C  CE1 . PHE   A 1 200 ? -32.757 -15.597 -8.842  1.00 127.90 ? 220 PHE   A CE1 1 
ATOM   1456 C  CE2 . PHE   A 1 200 ? -30.950 -14.406 -7.834  1.00 125.06 ? 220 PHE   A CE2 1 
ATOM   1457 C  CZ  . PHE   A 1 200 ? -31.753 -15.528 -7.900  1.00 125.78 ? 220 PHE   A CZ  1 
ATOM   1458 N  N   . LEU   A 1 201 ? -34.457 -10.166 -12.137 1.00 114.56 ? 221 LEU   A N   1 
ATOM   1459 C  CA  . LEU   A 1 201 ? -34.609 -9.009  -13.013 1.00 114.67 ? 221 LEU   A CA  1 
ATOM   1460 C  C   . LEU   A 1 201 ? -35.301 -7.862  -12.289 1.00 113.44 ? 221 LEU   A C   1 
ATOM   1461 O  O   . LEU   A 1 201 ? -34.970 -6.690  -12.510 1.00 113.37 ? 221 LEU   A O   1 
ATOM   1462 C  CB  . LEU   A 1 201 ? -35.374 -9.393  -14.280 1.00 116.55 ? 221 LEU   A CB  1 
ATOM   1463 C  CG  . LEU   A 1 201 ? -34.542 -10.012 -15.409 1.00 112.33 ? 221 LEU   A CG  1 
ATOM   1464 C  CD1 . LEU   A 1 201 ? -33.229 -9.256  -15.586 1.00 97.07  ? 221 LEU   A CD1 1 
ATOM   1465 C  CD2 . LEU   A 1 201 ? -34.288 -11.496 -15.182 1.00 122.07 ? 221 LEU   A CD2 1 
ATOM   1466 N  N   . SER   A 1 202 ? -36.267 -8.177  -11.422 1.00 115.95 ? 222 SER   A N   1 
ATOM   1467 C  CA  . SER   A 1 202 ? -36.806 -7.159  -10.529 1.00 116.20 ? 222 SER   A CA  1 
ATOM   1468 C  C   . SER   A 1 202 ? -35.726 -6.629  -9.597  1.00 114.54 ? 222 SER   A C   1 
ATOM   1469 O  O   . SER   A 1 202 ? -35.814 -5.492  -9.122  1.00 115.69 ? 222 SER   A O   1 
ATOM   1470 C  CB  . SER   A 1 202 ? -37.971 -7.731  -9.720  1.00 118.37 ? 222 SER   A CB  1 
ATOM   1471 O  OG  . SER   A 1 202 ? -38.861 -8.458  -10.548 1.00 119.54 ? 222 SER   A OG  1 
ATOM   1472 N  N   . ILE   A 1 203 ? -34.695 -7.434  -9.339  1.00 112.34 ? 223 ILE   A N   1 
ATOM   1473 C  CA  . ILE   A 1 203 ? -33.621 -7.041  -8.437  1.00 109.27 ? 223 ILE   A CA  1 
ATOM   1474 C  C   . ILE   A 1 203 ? -32.611 -6.134  -9.140  1.00 109.69 ? 223 ILE   A C   1 
ATOM   1475 O  O   . ILE   A 1 203 ? -32.020 -5.251  -8.507  1.00 108.84 ? 223 ILE   A O   1 
ATOM   1476 C  CB  . ILE   A 1 203 ? -32.967 -8.309  -7.856  1.00 108.98 ? 223 ILE   A CB  1 
ATOM   1477 C  CG1 . ILE   A 1 203 ? -33.973 -9.082  -6.999  1.00 107.65 ? 223 ILE   A CG1 1 
ATOM   1478 C  CG2 . ILE   A 1 203 ? -31.731 -7.985  -7.057  1.00 108.60 ? 223 ILE   A CG2 1 
ATOM   1479 C  CD1 . ILE   A 1 203 ? -34.715 -8.224  -5.995  1.00 108.98 ? 223 ILE   A CD1 1 
ATOM   1480 N  N   . THR   A 1 204 ? -32.406 -6.316  -10.447 1.00 112.68 ? 224 THR   A N   1 
ATOM   1481 C  CA  . THR   A 1 204 ? -31.504 -5.437  -11.187 1.00 109.14 ? 224 THR   A CA  1 
ATOM   1482 C  C   . THR   A 1 204 ? -32.129 -4.072  -11.450 1.00 111.14 ? 224 THR   A C   1 
ATOM   1483 O  O   . THR   A 1 204 ? -31.426 -3.056  -11.440 1.00 108.86 ? 224 THR   A O   1 
ATOM   1484 C  CB  . THR   A 1 204 ? -31.091 -6.089  -12.507 1.00 104.29 ? 224 THR   A CB  1 
ATOM   1485 O  OG1 . THR   A 1 204 ? -32.207 -6.796  -13.063 1.00 107.05 ? 224 THR   A OG1 1 
ATOM   1486 C  CG2 . THR   A 1 204 ? -29.933 -7.052  -12.289 1.00 102.60 ? 224 THR   A CG2 1 
ATOM   1487 N  N   . VAL   A 1 205 ? -33.440 -4.025  -11.691 1.00 109.02 ? 225 VAL   A N   1 
ATOM   1488 C  CA  . VAL   A 1 205 ? -34.107 -2.738  -11.858 1.00 109.65 ? 225 VAL   A CA  1 
ATOM   1489 C  C   . VAL   A 1 205 ? -34.405 -2.106  -10.501 1.00 113.17 ? 225 VAL   A C   1 
ATOM   1490 O  O   . VAL   A 1 205 ? -34.456 -0.876  -10.382 1.00 113.38 ? 225 VAL   A O   1 
ATOM   1491 C  CB  . VAL   A 1 205 ? -35.373 -2.906  -12.722 1.00 114.27 ? 225 VAL   A CB  1 
ATOM   1492 C  CG1 . VAL   A 1 205 ? -36.336 -1.749  -12.537 1.00 113.81 ? 225 VAL   A CG1 1 
ATOM   1493 C  CG2 . VAL   A 1 205 ? -34.986 -2.989  -14.180 1.00 110.60 ? 225 VAL   A CG2 1 
ATOM   1494 N  N   . PHE   A 1 206 ? -34.550 -2.916  -9.452  1.00 117.68 ? 226 PHE   A N   1 
ATOM   1495 C  CA  . PHE   A 1 206 ? -34.701 -2.428  -8.081  1.00 116.61 ? 226 PHE   A CA  1 
ATOM   1496 C  C   . PHE   A 1 206 ? -33.513 -2.854  -7.219  1.00 113.73 ? 226 PHE   A C   1 
ATOM   1497 O  O   . PHE   A 1 206 ? -33.684 -3.600  -6.247  1.00 113.49 ? 226 PHE   A O   1 
ATOM   1498 C  CB  . PHE   A 1 206 ? -36.001 -2.929  -7.451  1.00 119.44 ? 226 PHE   A CB  1 
ATOM   1499 C  CG  . PHE   A 1 206 ? -37.218 -2.782  -8.328  1.00 125.41 ? 226 PHE   A CG  1 
ATOM   1500 C  CD1 . PHE   A 1 206 ? -37.391 -1.673  -9.132  1.00 124.47 ? 226 PHE   A CD1 1 
ATOM   1501 C  CD2 . PHE   A 1 206 ? -38.201 -3.762  -8.329  1.00 128.68 ? 226 PHE   A CD2 1 
ATOM   1502 C  CE1 . PHE   A 1 206 ? -38.513 -1.547  -9.928  1.00 122.98 ? 226 PHE   A CE1 1 
ATOM   1503 C  CE2 . PHE   A 1 206 ? -39.325 -3.638  -9.126  1.00 127.61 ? 226 PHE   A CE2 1 
ATOM   1504 C  CZ  . PHE   A 1 206 ? -39.480 -2.527  -9.924  1.00 124.60 ? 226 PHE   A CZ  1 
ATOM   1505 N  N   . PRO   A 1 207 ? -32.294 -2.393  -7.530  1.00 116.13 ? 227 PRO   A N   1 
ATOM   1506 C  CA  . PRO   A 1 207 ? -31.171 -2.686  -6.628  1.00 111.35 ? 227 PRO   A CA  1 
ATOM   1507 C  C   . PRO   A 1 207 ? -31.300 -1.990  -5.290  1.00 112.04 ? 227 PRO   A C   1 
ATOM   1508 O  O   . PRO   A 1 207 ? -30.637 -2.393  -4.325  1.00 109.13 ? 227 PRO   A O   1 
ATOM   1509 C  CB  . PRO   A 1 207 ? -29.950 -2.187  -7.407  1.00 108.02 ? 227 PRO   A CB  1 
ATOM   1510 C  CG  . PRO   A 1 207 ? -30.480 -1.097  -8.244  1.00 110.68 ? 227 PRO   A CG  1 
ATOM   1511 C  CD  . PRO   A 1 207 ? -31.880 -1.496  -8.623  1.00 115.37 ? 227 PRO   A CD  1 
ATOM   1512 N  N   . PHE   A 1 208 ? -32.141 -0.960  -5.205  1.00 102.33 ? 228 PHE   A N   1 
ATOM   1513 C  CA  . PHE   A 1 208 ? -32.407 -0.278  -3.950  1.00 103.12 ? 228 PHE   A CA  1 
ATOM   1514 C  C   . PHE   A 1 208 ? -33.207 -1.127  -2.973  1.00 100.29 ? 228 PHE   A C   1 
ATOM   1515 O  O   . PHE   A 1 208 ? -33.320 -0.748  -1.802  1.00 102.66 ? 228 PHE   A O   1 
ATOM   1516 C  CB  . PHE   A 1 208 ? -33.144 1.036   -4.219  1.00 104.09 ? 228 PHE   A CB  1 
ATOM   1517 C  CG  . PHE   A 1 208 ? -34.193 0.941   -5.293  1.00 108.31 ? 228 PHE   A CG  1 
ATOM   1518 C  CD1 . PHE   A 1 208 ? -35.446 0.421   -5.016  1.00 109.02 ? 228 PHE   A CD1 1 
ATOM   1519 C  CD2 . PHE   A 1 208 ? -33.928 1.387   -6.577  1.00 111.56 ? 228 PHE   A CD2 1 
ATOM   1520 C  CE1 . PHE   A 1 208 ? -36.412 0.342   -5.996  1.00 113.33 ? 228 PHE   A CE1 1 
ATOM   1521 C  CE2 . PHE   A 1 208 ? -34.889 1.309   -7.564  1.00 116.38 ? 228 PHE   A CE2 1 
ATOM   1522 C  CZ  . PHE   A 1 208 ? -36.133 0.787   -7.272  1.00 119.75 ? 228 PHE   A CZ  1 
ATOM   1523 N  N   . LEU   A 1 209 ? -33.762 -2.253  -3.415  1.00 107.51 ? 229 LEU   A N   1 
ATOM   1524 C  CA  . LEU   A 1 209 ? -34.586 -3.085  -2.552  1.00 104.14 ? 229 LEU   A CA  1 
ATOM   1525 C  C   . LEU   A 1 209 ? -33.813 -4.216  -1.887  1.00 105.48 ? 229 LEU   A C   1 
ATOM   1526 O  O   . LEU   A 1 209 ? -34.362 -4.869  -0.996  1.00 106.37 ? 229 LEU   A O   1 
ATOM   1527 C  CB  . LEU   A 1 209 ? -35.762 -3.671  -3.341  1.00 106.17 ? 229 LEU   A CB  1 
ATOM   1528 C  CG  . LEU   A 1 209 ? -36.825 -2.675  -3.814  1.00 109.34 ? 229 LEU   A CG  1 
ATOM   1529 C  CD1 . LEU   A 1 209 ? -38.016 -3.393  -4.435  1.00 113.44 ? 229 LEU   A CD1 1 
ATOM   1530 C  CD2 . LEU   A 1 209 ? -37.275 -1.782  -2.669  1.00 104.00 ? 229 LEU   A CD2 1 
ATOM   1531 N  N   . ILE   A 1 210 ? -32.569 -4.471  -2.297  1.00 103.46 ? 230 ILE   A N   1 
ATOM   1532 C  CA  . ILE   A 1 210 ? -31.773 -5.519  -1.650  1.00 103.50 ? 230 ILE   A CA  1 
ATOM   1533 C  C   . ILE   A 1 210 ? -31.672 -5.306  -0.142  1.00 102.05 ? 230 ILE   A C   1 
ATOM   1534 O  O   . ILE   A 1 210 ? -31.881 -6.269  0.608   1.00 104.31 ? 230 ILE   A O   1 
ATOM   1535 C  CB  . ILE   A 1 210 ? -30.405 -5.650  -2.328  1.00 102.86 ? 230 ILE   A CB  1 
ATOM   1536 C  CG1 . ILE   A 1 210 ? -30.521 -6.424  -3.636  1.00 103.13 ? 230 ILE   A CG1 1 
ATOM   1537 C  CG2 . ILE   A 1 210 ? -29.414 -6.343  -1.415  1.00 103.87 ? 230 ILE   A CG2 1 
ATOM   1538 C  CD1 . ILE   A 1 210 ? -30.993 -5.588  -4.766  1.00 104.88 ? 230 ILE   A CD1 1 
ATOM   1539 N  N   . PRO   A 1 211 ? -31.369 -4.106  0.365   1.00 105.18 ? 231 PRO   A N   1 
ATOM   1540 C  CA  . PRO   A 1 211 ? -31.388 -3.917  1.823   1.00 105.01 ? 231 PRO   A CA  1 
ATOM   1541 C  C   . PRO   A 1 211 ? -32.753 -4.152  2.450   1.00 107.70 ? 231 PRO   A C   1 
ATOM   1542 O  O   . PRO   A 1 211 ? -32.819 -4.458  3.648   1.00 112.94 ? 231 PRO   A O   1 
ATOM   1543 C  CB  . PRO   A 1 211 ? -30.934 -2.461  1.992   1.00 102.59 ? 231 PRO   A CB  1 
ATOM   1544 C  CG  . PRO   A 1 211 ? -30.175 -2.153  0.757   1.00 102.08 ? 231 PRO   A CG  1 
ATOM   1545 C  CD  . PRO   A 1 211 ? -30.883 -2.896  -0.326  1.00 104.82 ? 231 PRO   A CD  1 
ATOM   1546 N  N   . ILE   A 1 212 ? -33.842 -4.018  1.687   1.00 100.14 ? 232 ILE   A N   1 
ATOM   1547 C  CA  . ILE   A 1 212 ? -35.164 -4.347  2.218   1.00 101.73 ? 232 ILE   A CA  1 
ATOM   1548 C  C   . ILE   A 1 212 ? -35.224 -5.818  2.600   1.00 101.63 ? 232 ILE   A C   1 
ATOM   1549 O  O   . ILE   A 1 212 ? -35.585 -6.173  3.729   1.00 107.75 ? 232 ILE   A O   1 
ATOM   1550 C  CB  . ILE   A 1 212 ? -36.264 -3.991  1.201   1.00 101.77 ? 232 ILE   A CB  1 
ATOM   1551 C  CG1 . ILE   A 1 212 ? -36.195 -2.512  0.826   1.00 99.99  ? 232 ILE   A CG1 1 
ATOM   1552 C  CG2 . ILE   A 1 212 ? -37.640 -4.378  1.738   1.00 105.31 ? 232 ILE   A CG2 1 
ATOM   1553 C  CD1 . ILE   A 1 212 ? -36.321 -1.605  1.998   1.00 101.83 ? 232 ILE   A CD1 1 
ATOM   1554 N  N   . LEU   A 1 213 ? -34.870 -6.698  1.660   1.00 105.50 ? 233 LEU   A N   1 
ATOM   1555 C  CA  . LEU   A 1 213 ? -34.900 -8.129  1.940   1.00 108.98 ? 233 LEU   A CA  1 
ATOM   1556 C  C   . LEU   A 1 213 ? -33.873 -8.509  2.996   1.00 112.65 ? 233 LEU   A C   1 
ATOM   1557 O  O   . LEU   A 1 213 ? -34.166 -9.310  3.891   1.00 116.87 ? 233 LEU   A O   1 
ATOM   1558 C  CB  . LEU   A 1 213 ? -34.644 -8.937  0.669   1.00 106.07 ? 233 LEU   A CB  1 
ATOM   1559 C  CG  . LEU   A 1 213 ? -35.518 -8.819  -0.580  1.00 102.53 ? 233 LEU   A CG  1 
ATOM   1560 C  CD1 . LEU   A 1 213 ? -36.957 -8.443  -0.243  1.00 104.63 ? 233 LEU   A CD1 1 
ATOM   1561 C  CD2 . LEU   A 1 213 ? -34.910 -7.854  -1.584  1.00 104.80 ? 233 LEU   A CD2 1 
ATOM   1562 N  N   . GLU   A 1 214 ? -32.663 -7.954  2.903   1.00 106.20 ? 234 GLU   A N   1 
ATOM   1563 C  CA  . GLU   A 1 214 ? -31.576 -8.395  3.773   1.00 106.43 ? 234 GLU   A CA  1 
ATOM   1564 C  C   . GLU   A 1 214 ? -31.941 -8.244  5.242   1.00 106.04 ? 234 GLU   A C   1 
ATOM   1565 O  O   . GLU   A 1 214 ? -31.650 -9.129  6.058   1.00 109.36 ? 234 GLU   A O   1 
ATOM   1566 C  CB  . GLU   A 1 214 ? -30.296 -7.622  3.452   1.00 107.68 ? 234 GLU   A CB  1 
ATOM   1567 C  CG  . GLU   A 1 214 ? -29.653 -7.983  2.119   1.00 110.11 ? 234 GLU   A CG  1 
ATOM   1568 C  CD  . GLU   A 1 214 ? -28.849 -9.272  2.165   1.00 112.51 ? 234 GLU   A CD  1 
ATOM   1569 O  OE1 . GLU   A 1 214 ? -29.199 -10.179 2.950   1.00 108.82 ? 234 GLU   A OE1 1 
ATOM   1570 O  OE2 . GLU   A 1 214 ? -27.859 -9.372  1.409   1.00 113.78 ? 234 GLU   A OE2 1 
ATOM   1571 N  N   . VAL   A 1 215 ? -32.593 -7.136  5.596   1.00 109.87 ? 235 VAL   A N   1 
ATOM   1572 C  CA  . VAL   A 1 215 ? -32.873 -6.826  6.997   1.00 109.23 ? 235 VAL   A CA  1 
ATOM   1573 C  C   . VAL   A 1 215 ? -34.095 -7.631  7.422   1.00 113.04 ? 235 VAL   A C   1 
ATOM   1574 O  O   . VAL   A 1 215 ? -34.546 -7.571  8.574   1.00 118.25 ? 235 VAL   A O   1 
ATOM   1575 C  CB  . VAL   A 1 215 ? -33.080 -5.318  7.228   1.00 105.76 ? 235 VAL   A CB  1 
ATOM   1576 C  CG1 . VAL   A 1 215 ? -34.471 -4.881  6.796   1.00 109.14 ? 235 VAL   A CG1 1 
ATOM   1577 C  CG2 . VAL   A 1 215 ? -32.818 -4.950  8.681   1.00 108.14 ? 235 VAL   A CG2 1 
ATOM   1578 N  N   . LEU   A 1 216 ? -34.635 -8.394  6.474   1.00 108.61 ? 236 LEU   A N   1 
ATOM   1579 C  CA  . LEU   A 1 216 ? -35.738 -9.313  6.719   1.00 113.91 ? 236 LEU   A CA  1 
ATOM   1580 C  C   . LEU   A 1 216 ? -35.296 -10.775 6.691   1.00 119.89 ? 236 LEU   A C   1 
ATOM   1581 O  O   . LEU   A 1 216 ? -36.141 -11.669 6.799   1.00 121.58 ? 236 LEU   A O   1 
ATOM   1582 C  CB  . LEU   A 1 216 ? -36.849 -9.084  5.693   1.00 108.79 ? 236 LEU   A CB  1 
ATOM   1583 C  CG  . LEU   A 1 216 ? -37.984 -8.085  5.945   1.00 109.27 ? 236 LEU   A CG  1 
ATOM   1584 C  CD1 . LEU   A 1 216 ? -37.459 -6.708  6.281   1.00 108.28 ? 236 LEU   A CD1 1 
ATOM   1585 C  CD2 . LEU   A 1 216 ? -38.888 -8.018  4.723   1.00 105.28 ? 236 LEU   A CD2 1 
ATOM   1586 N  N   . ASN   A 1 217 ? -33.993 -11.038 6.550   1.00 119.02 ? 237 ASN   A N   1 
ATOM   1587 C  CA  . ASN   A 1 217 ? -33.418 -12.386 6.469   1.00 124.25 ? 237 ASN   A CA  1 
ATOM   1588 C  C   . ASN   A 1 217 ? -33.950 -13.188 5.280   1.00 127.36 ? 237 ASN   A C   1 
ATOM   1589 O  O   . ASN   A 1 217 ? -33.854 -14.421 5.265   1.00 128.84 ? 237 ASN   A O   1 
ATOM   1590 C  CB  . ASN   A 1 217 ? -33.614 -13.178 7.770   1.00 121.37 ? 237 ASN   A CB  1 
ATOM   1591 C  CG  . ASN   A 1 217 ? -32.601 -14.309 7.922   1.00 131.30 ? 237 ASN   A CG  1 
ATOM   1592 O  OD1 . ASN   A 1 217 ? -31.734 -14.498 7.069   1.00 135.92 ? 237 ASN   A OD1 1 
ATOM   1593 N  ND2 . ASN   A 1 217 ? -32.700 -15.055 9.019   1.00 133.39 ? 237 ASN   A ND2 1 
ATOM   1594 N  N   . ILE   A 1 218 ? -34.514 -12.521 4.272   1.00 128.84 ? 238 ILE   A N   1 
ATOM   1595 C  CA  . ILE   A 1 218 ? -34.741 -13.190 2.999   1.00 125.57 ? 238 ILE   A CA  1 
ATOM   1596 C  C   . ILE   A 1 218 ? -33.393 -13.443 2.339   1.00 127.56 ? 238 ILE   A C   1 
ATOM   1597 O  O   . ILE   A 1 218 ? -32.493 -12.594 2.377   1.00 123.72 ? 238 ILE   A O   1 
ATOM   1598 C  CB  . ILE   A 1 218 ? -35.668 -12.361 2.091   1.00 119.43 ? 238 ILE   A CB  1 
ATOM   1599 C  CG1 . ILE   A 1 218 ? -37.134 -12.566 2.473   1.00 115.88 ? 238 ILE   A CG1 1 
ATOM   1600 C  CG2 . ILE   A 1 218 ? -35.477 -12.733 0.628   1.00 119.32 ? 238 ILE   A CG2 1 
ATOM   1601 C  CD1 . ILE   A 1 218 ? -37.573 -11.775 3.663   1.00 114.65 ? 238 ILE   A CD1 1 
ATOM   1602 N  N   . CYS   A 1 219 ? -33.239 -14.625 1.748   1.00 130.10 ? 239 CYS   A N   1 
ATOM   1603 C  CA  . CYS   A 1 219 ? -31.976 -15.030 1.153   1.00 131.83 ? 239 CYS   A CA  1 
ATOM   1604 C  C   . CYS   A 1 219 ? -32.263 -15.775 -0.140  1.00 133.01 ? 239 CYS   A C   1 
ATOM   1605 O  O   . CYS   A 1 219 ? -33.169 -16.613 -0.182  1.00 138.88 ? 239 CYS   A O   1 
ATOM   1606 C  CB  . CYS   A 1 219 ? -31.179 -15.909 2.124   1.00 133.05 ? 239 CYS   A CB  1 
ATOM   1607 S  SG  . CYS   A 1 219 ? -29.666 -16.615 1.455   1.00 138.16 ? 239 CYS   A SG  1 
ATOM   1608 N  N   . VAL   A 1 220 ? -31.496 -15.469 -1.193  1.00 132.30 ? 240 VAL   A N   1 
ATOM   1609 C  CA  . VAL   A 1 220 ? -31.677 -16.159 -2.471  1.00 132.03 ? 240 VAL   A CA  1 
ATOM   1610 C  C   . VAL   A 1 220 ? -31.429 -17.652 -2.331  1.00 133.12 ? 240 VAL   A C   1 
ATOM   1611 O  O   . VAL   A 1 220 ? -31.794 -18.428 -3.219  1.00 132.41 ? 240 VAL   A O   1 
ATOM   1612 C  CB  . VAL   A 1 220 ? -30.767 -15.559 -3.561  1.00 129.65 ? 240 VAL   A CB  1 
ATOM   1613 C  CG1 . VAL   A 1 220 ? -31.202 -14.145 -3.902  1.00 129.45 ? 240 VAL   A CG1 1 
ATOM   1614 C  CG2 . VAL   A 1 220 ? -29.318 -15.591 -3.115  1.00 130.36 ? 240 VAL   A CG2 1 
ATOM   1615 N  N   . PHE   A 1 221 ? -30.803 -18.074 -1.235  1.00 132.46 ? 241 PHE   A N   1 
ATOM   1616 C  CA  . PHE   A 1 221 ? -30.623 -19.484 -0.947  1.00 136.68 ? 241 PHE   A CA  1 
ATOM   1617 C  C   . PHE   A 1 221 ? -31.662 -19.906 0.080   1.00 139.13 ? 241 PHE   A C   1 
ATOM   1618 O  O   . PHE   A 1 221 ? -31.616 -19.423 1.223   1.00 142.07 ? 241 PHE   A O   1 
ATOM   1619 C  CB  . PHE   A 1 221 ? -29.212 -19.746 -0.426  1.00 136.76 ? 241 PHE   A CB  1 
ATOM   1620 C  CG  . PHE   A 1 221 ? -28.127 -19.272 -1.358  1.00 134.29 ? 241 PHE   A CG  1 
ATOM   1621 C  CD1 . PHE   A 1 221 ? -27.710 -20.063 -2.416  1.00 132.95 ? 241 PHE   A CD1 1 
ATOM   1622 C  CD2 . PHE   A 1 221 ? -27.528 -18.035 -1.177  1.00 133.61 ? 241 PHE   A CD2 1 
ATOM   1623 C  CE1 . PHE   A 1 221 ? -26.714 -19.631 -3.274  1.00 129.87 ? 241 PHE   A CE1 1 
ATOM   1624 C  CE2 . PHE   A 1 221 ? -26.531 -17.599 -2.032  1.00 129.26 ? 241 PHE   A CE2 1 
ATOM   1625 C  CZ  . PHE   A 1 221 ? -26.125 -18.398 -3.081  1.00 127.14 ? 241 PHE   A CZ  1 
ATOM   1626 N  N   . PRO   A 1 222 ? -32.634 -20.760 -0.286  1.00 151.14 ? 242 PRO   A N   1 
ATOM   1627 C  CA  . PRO   A 1 222 ? -33.660 -21.210 0.668   1.00 157.45 ? 242 PRO   A CA  1 
ATOM   1628 C  C   . PRO   A 1 222 ? -33.114 -21.558 2.043   1.00 172.22 ? 242 PRO   A C   1 
ATOM   1629 O  O   . PRO   A 1 222 ? -32.219 -22.399 2.177   1.00 171.31 ? 242 PRO   A O   1 
ATOM   1630 C  CB  . PRO   A 1 222 ? -34.257 -22.448 -0.022  1.00 155.13 ? 242 PRO   A CB  1 
ATOM   1631 C  CG  . PRO   A 1 222 ? -33.658 -22.483 -1.434  1.00 145.40 ? 242 PRO   A CG  1 
ATOM   1632 C  CD  . PRO   A 1 222 ? -32.946 -21.190 -1.657  1.00 145.10 ? 242 PRO   A CD  1 
ATOM   1633 N  N   . ARG   A 1 223 ? -33.657 -20.907 3.074   1.00 177.23 ? 243 ARG   A N   1 
ATOM   1634 C  CA  . ARG   A 1 223 ? -33.118 -21.021 4.424   1.00 179.19 ? 243 ARG   A CA  1 
ATOM   1635 C  C   . ARG   A 1 223 ? -33.315 -22.400 5.036   1.00 191.60 ? 243 ARG   A C   1 
ATOM   1636 O  O   . ARG   A 1 223 ? -32.746 -22.668 6.099   1.00 192.87 ? 243 ARG   A O   1 
ATOM   1637 C  CB  . ARG   A 1 223 ? -33.753 -19.972 5.338   1.00 178.31 ? 243 ARG   A CB  1 
ATOM   1638 C  CG  . ARG   A 1 223 ? -35.121 -20.359 5.878   1.00 183.22 ? 243 ARG   A CG  1 
ATOM   1639 C  CD  . ARG   A 1 223 ? -35.373 -19.671 7.207   1.00 183.13 ? 243 ARG   A CD  1 
ATOM   1640 N  NE  . ARG   A 1 223 ? -34.314 -19.968 8.164   1.00 179.57 ? 243 ARG   A NE  1 
ATOM   1641 C  CZ  . ARG   A 1 223 ? -34.111 -19.302 9.292   1.00 177.16 ? 243 ARG   A CZ  1 
ATOM   1642 N  NH1 . ARG   A 1 223 ? -34.872 -18.276 9.635   1.00 170.42 ? 243 ARG   A NH1 1 
ATOM   1643 N  NH2 . ARG   A 1 223 ? -33.115 -19.670 10.093  1.00 177.83 ? 243 ARG   A NH2 1 
ATOM   1644 N  N   . GLU   A 1 224 ? -34.107 -23.273 4.411   1.00 213.08 ? 244 GLU   A N   1 
ATOM   1645 C  CA  . GLU   A 1 224 ? -34.312 -24.604 4.969   1.00 215.90 ? 244 GLU   A CA  1 
ATOM   1646 C  C   . GLU   A 1 224 ? -33.193 -25.550 4.557   1.00 211.85 ? 244 GLU   A C   1 
ATOM   1647 O  O   . GLU   A 1 224 ? -32.768 -26.401 5.349   1.00 208.04 ? 244 GLU   A O   1 
ATOM   1648 C  CB  . GLU   A 1 224 ? -35.668 -25.157 4.540   1.00 219.23 ? 244 GLU   A CB  1 
ATOM   1649 C  CG  . GLU   A 1 224 ? -35.874 -25.201 3.034   1.00 220.25 ? 244 GLU   A CG  1 
ATOM   1650 C  CD  . GLU   A 1 224 ? -37.037 -26.083 2.635   1.00 233.17 ? 244 GLU   A CD  1 
ATOM   1651 O  OE1 . GLU   A 1 224 ? -37.762 -26.557 3.537   1.00 232.72 ? 244 GLU   A OE1 1 
ATOM   1652 O  OE2 . GLU   A 1 224 ? -37.226 -26.309 1.422   1.00 235.52 ? 244 GLU   A OE2 1 
ATOM   1653 N  N   . VAL   A 1 225 ? -32.718 -25.429 3.316   1.00 192.74 ? 245 VAL   A N   1 
ATOM   1654 C  CA  . VAL   A 1 225 ? -31.555 -26.197 2.885   1.00 186.33 ? 245 VAL   A CA  1 
ATOM   1655 C  C   . VAL   A 1 225 ? -30.356 -25.853 3.757   1.00 187.48 ? 245 VAL   A C   1 
ATOM   1656 O  O   . VAL   A 1 225 ? -29.760 -26.722 4.402   1.00 186.79 ? 245 VAL   A O   1 
ATOM   1657 C  CB  . VAL   A 1 225 ? -31.265 -25.934 1.397   1.00 176.78 ? 245 VAL   A CB  1 
ATOM   1658 C  CG1 . VAL   A 1 225 ? -30.081 -26.755 0.934   1.00 167.20 ? 245 VAL   A CG1 1 
ATOM   1659 C  CG2 . VAL   A 1 225 ? -32.491 -26.245 0.556   1.00 169.78 ? 245 VAL   A CG2 1 
ATOM   1660 N  N   . THR   A 1 226 ? -30.023 -24.564 3.826   1.00 179.76 ? 246 THR   A N   1 
ATOM   1661 C  CA  . THR   A 1 226 ? -28.799 -24.141 4.496   1.00 177.55 ? 246 THR   A CA  1 
ATOM   1662 C  C   . THR   A 1 226 ? -28.847 -24.437 5.990   1.00 180.13 ? 246 THR   A C   1 
ATOM   1663 O  O   . THR   A 1 226 ? -27.823 -24.768 6.599   1.00 173.41 ? 246 THR   A O   1 
ATOM   1664 C  CB  . THR   A 1 226 ? -28.565 -22.654 4.257   1.00 169.46 ? 246 THR   A CB  1 
ATOM   1665 O  OG1 . THR   A 1 226 ? -29.327 -21.893 5.200   1.00 170.71 ? 246 THR   A OG1 1 
ATOM   1666 C  CG2 . THR   A 1 226 ? -28.992 -22.279 2.850   1.00 163.16 ? 246 THR   A CG2 1 
ATOM   1667 N  N   . ASN   A 1 227 ? -30.025 -24.308 6.606   1.00 203.17 ? 247 ASN   A N   1 
ATOM   1668 C  CA  . ASN   A 1 227 ? -30.142 -24.654 8.019   1.00 207.78 ? 247 ASN   A CA  1 
ATOM   1669 C  C   . ASN   A 1 227 ? -29.999 -26.155 8.230   1.00 208.17 ? 247 ASN   A C   1 
ATOM   1670 O  O   . ASN   A 1 227 ? -29.564 -26.594 9.301   1.00 210.37 ? 247 ASN   A O   1 
ATOM   1671 C  CB  . ASN   A 1 227 ? -31.472 -24.155 8.581   1.00 208.16 ? 247 ASN   A CB  1 
ATOM   1672 C  CG  . ASN   A 1 227 ? -31.420 -23.921 10.076  1.00 209.49 ? 247 ASN   A CG  1 
ATOM   1673 O  OD1 . ASN   A 1 227 ? -30.704 -23.038 10.552  1.00 207.54 ? 247 ASN   A OD1 1 
ATOM   1674 N  ND2 . ASN   A 1 227 ? -32.185 -24.704 10.827  1.00 213.70 ? 247 ASN   A ND2 1 
ATOM   1675 N  N   . PHE   A 1 228 ? -30.351 -26.952 7.220   1.00 194.65 ? 248 PHE   A N   1 
ATOM   1676 C  CA  . PHE   A 1 228 ? -30.123 -28.391 7.292   1.00 191.62 ? 248 PHE   A CA  1 
ATOM   1677 C  C   . PHE   A 1 228 ? -28.635 -28.706 7.200   1.00 191.08 ? 248 PHE   A C   1 
ATOM   1678 O  O   . PHE   A 1 228 ? -28.113 -29.511 7.979   1.00 194.13 ? 248 PHE   A O   1 
ATOM   1679 C  CB  . PHE   A 1 228 ? -30.926 -29.094 6.193   1.00 185.75 ? 248 PHE   A CB  1 
ATOM   1680 C  CG  . PHE   A 1 228 ? -30.258 -30.312 5.607   1.00 177.30 ? 248 PHE   A CG  1 
ATOM   1681 C  CD1 . PHE   A 1 228 ? -30.056 -31.457 6.364   1.00 177.70 ? 248 PHE   A CD1 1 
ATOM   1682 C  CD2 . PHE   A 1 228 ? -29.880 -30.325 4.273   1.00 168.95 ? 248 PHE   A CD2 1 
ATOM   1683 C  CE1 . PHE   A 1 228 ? -29.457 -32.575 5.810   1.00 169.52 ? 248 PHE   A CE1 1 
ATOM   1684 C  CE2 . PHE   A 1 228 ? -29.288 -31.442 3.713   1.00 164.63 ? 248 PHE   A CE2 1 
ATOM   1685 C  CZ  . PHE   A 1 228 ? -29.073 -32.567 4.483   1.00 162.49 ? 248 PHE   A CZ  1 
ATOM   1686 N  N   . LEU   A 1 229 ? -27.929 -28.060 6.266   1.00 181.31 ? 249 LEU   A N   1 
ATOM   1687 C  CA  . LEU   A 1 229 ? -26.489 -28.280 6.147   1.00 177.83 ? 249 LEU   A CA  1 
ATOM   1688 C  C   . LEU   A 1 229 ? -25.740 -27.738 7.356   1.00 181.16 ? 249 LEU   A C   1 
ATOM   1689 O  O   . LEU   A 1 229 ? -24.799 -28.376 7.845   1.00 179.60 ? 249 LEU   A O   1 
ATOM   1690 C  CB  . LEU   A 1 229 ? -25.949 -27.632 4.873   1.00 168.14 ? 249 LEU   A CB  1 
ATOM   1691 C  CG  . LEU   A 1 229 ? -26.138 -28.377 3.553   1.00 164.44 ? 249 LEU   A CG  1 
ATOM   1692 C  CD1 . LEU   A 1 229 ? -26.199 -29.883 3.764   1.00 163.45 ? 249 LEU   A CD1 1 
ATOM   1693 C  CD2 . LEU   A 1 229 ? -27.370 -27.881 2.846   1.00 166.44 ? 249 LEU   A CD2 1 
ATOM   1694 N  N   . ARG   A 1 230 ? -26.134 -26.556 7.837   1.00 188.51 ? 250 ARG   A N   1 
ATOM   1695 C  CA  . ARG   A 1 230 ? -25.454 -25.942 8.972   1.00 184.39 ? 250 ARG   A CA  1 
ATOM   1696 C  C   . ARG   A 1 230 ? -25.419 -26.896 10.161  1.00 192.58 ? 250 ARG   A C   1 
ATOM   1697 O  O   . ARG   A 1 230 ? -24.346 -27.213 10.680  1.00 185.95 ? 250 ARG   A O   1 
ATOM   1698 C  CB  . ARG   A 1 230 ? -26.125 -24.603 9.317   1.00 177.86 ? 250 ARG   A CB  1 
ATOM   1699 C  CG  . ARG   A 1 230 ? -26.525 -24.396 10.774  1.00 180.88 ? 250 ARG   A CG  1 
ATOM   1700 C  CD  . ARG   A 1 230 ? -26.939 -22.954 11.073  1.00 171.10 ? 250 ARG   A CD  1 
ATOM   1701 N  NE  . ARG   A 1 230 ? -28.107 -22.507 10.320  1.00 175.15 ? 250 ARG   A NE  1 
ATOM   1702 C  CZ  . ARG   A 1 230 ? -28.087 -21.542 9.410   1.00 165.25 ? 250 ARG   A CZ  1 
ATOM   1703 N  NH1 . ARG   A 1 230 ? -26.969 -20.904 9.103   1.00 148.16 ? 250 ARG   A NH1 1 
ATOM   1704 N  NH2 . ARG   A 1 230 ? -29.219 -21.202 8.798   1.00 166.37 ? 250 ARG   A NH2 1 
ATOM   1705 N  N   . LYS   A 1 231 ? -26.581 -27.424 10.559  1.00 228.52 ? 251 LYS   A N   1 
ATOM   1706 C  CA  . LYS   A 1 231 ? -26.608 -28.387 11.654  1.00 232.08 ? 251 LYS   A CA  1 
ATOM   1707 C  C   . LYS   A 1 231 ? -26.060 -29.742 11.223  1.00 234.83 ? 251 LYS   A C   1 
ATOM   1708 O  O   . LYS   A 1 231 ? -25.569 -30.504 12.065  1.00 235.85 ? 251 LYS   A O   1 
ATOM   1709 C  CB  . LYS   A 1 231 ? -28.030 -28.531 12.192  1.00 234.36 ? 251 LYS   A CB  1 
ATOM   1710 C  CG  . LYS   A 1 231 ? -29.006 -29.118 11.194  1.00 233.61 ? 251 LYS   A CG  1 
ATOM   1711 C  CD  . LYS   A 1 231 ? -30.406 -29.186 11.766  1.00 237.92 ? 251 LYS   A CD  1 
ATOM   1712 C  CE  . LYS   A 1 231 ? -31.329 -29.949 10.837  1.00 238.94 ? 251 LYS   A CE  1 
ATOM   1713 N  NZ  . LYS   A 1 231 ? -30.824 -31.328 10.587  1.00 240.10 ? 251 LYS   A NZ  1 
ATOM   1714 N  N   . SER   A 1 232 ? -26.136 -30.064 9.929   1.00 201.37 ? 252 SER   A N   1 
ATOM   1715 C  CA  . SER   A 1 232 ? -25.498 -31.282 9.437   1.00 191.93 ? 252 SER   A CA  1 
ATOM   1716 C  C   . SER   A 1 232 ? -23.986 -31.190 9.574   1.00 184.26 ? 252 SER   A C   1 
ATOM   1717 O  O   . SER   A 1 232 ? -23.337 -32.118 10.066  1.00 185.51 ? 252 SER   A O   1 
ATOM   1718 C  CB  . SER   A 1 232 ? -25.884 -31.541 7.980   1.00 183.33 ? 252 SER   A CB  1 
ATOM   1719 O  OG  . SER   A 1 232 ? -27.268 -31.808 7.856   1.00 182.89 ? 252 SER   A OG  1 
ATOM   1720 N  N   . VAL   A 1 233 ? -23.408 -30.067 9.148   1.00 197.30 ? 253 VAL   A N   1 
ATOM   1721 C  CA  . VAL   A 1 233 ? -21.963 -29.897 9.252   1.00 190.33 ? 253 VAL   A CA  1 
ATOM   1722 C  C   . VAL   A 1 233 ? -21.527 -29.904 10.712  1.00 198.30 ? 253 VAL   A C   1 
ATOM   1723 O  O   . VAL   A 1 233 ? -20.541 -30.559 11.073  1.00 198.17 ? 253 VAL   A O   1 
ATOM   1724 C  CB  . VAL   A 1 233 ? -21.524 -28.613 8.529   1.00 176.74 ? 253 VAL   A CB  1 
ATOM   1725 C  CG1 . VAL   A 1 233 ? -20.087 -28.313 8.847   1.00 170.17 ? 253 VAL   A CG1 1 
ATOM   1726 C  CG2 . VAL   A 1 233 ? -21.709 -28.766 7.029   1.00 169.30 ? 253 VAL   A CG2 1 
ATOM   1727 N  N   . LYS   A 1 234 ? -22.258 -29.193 11.579  1.00 186.17 ? 254 LYS   A N   1 
ATOM   1728 C  CA  . LYS   A 1 234 ? -21.935 -29.210 13.003  1.00 185.06 ? 254 LYS   A CA  1 
ATOM   1729 C  C   . LYS   A 1 234 ? -22.056 -30.606 13.602  1.00 193.04 ? 254 LYS   A C   1 
ATOM   1730 O  O   . LYS   A 1 234 ? -21.437 -30.877 14.637  1.00 197.86 ? 254 LYS   A O   1 
ATOM   1731 C  CB  . LYS   A 1 234 ? -22.837 -28.250 13.788  1.00 186.64 ? 254 LYS   A CB  1 
ATOM   1732 C  CG  . LYS   A 1 234 ? -22.949 -26.828 13.247  1.00 185.41 ? 254 LYS   A CG  1 
ATOM   1733 C  CD  . LYS   A 1 234 ? -21.727 -25.969 13.512  1.00 172.20 ? 254 LYS   A CD  1 
ATOM   1734 C  CE  . LYS   A 1 234 ? -20.956 -25.719 12.230  1.00 161.22 ? 254 LYS   A CE  1 
ATOM   1735 N  NZ  . LYS   A 1 234 ? -20.325 -24.376 12.214  1.00 154.67 ? 254 LYS   A NZ  1 
ATOM   1736 N  N   . ARG   A 1 235 ? -22.846 -31.493 12.990  1.00 193.38 ? 255 ARG   A N   1 
ATOM   1737 C  CA  . ARG   A 1 235 ? -22.891 -32.873 13.463  1.00 196.42 ? 255 ARG   A CA  1 
ATOM   1738 C  C   . ARG   A 1 235 ? -21.677 -33.658 12.981  1.00 198.94 ? 255 ARG   A C   1 
ATOM   1739 O  O   . ARG   A 1 235 ? -21.144 -34.495 13.717  1.00 197.97 ? 255 ARG   A O   1 
ATOM   1740 C  CB  . ARG   A 1 235 ? -24.195 -33.555 13.023  1.00 197.90 ? 255 ARG   A CB  1 
ATOM   1741 C  CG  . ARG   A 1 235 ? -24.065 -34.511 11.832  1.00 196.09 ? 255 ARG   A CG  1 
ATOM   1742 C  CD  . ARG   A 1 235 ? -25.048 -35.672 11.899  1.00 194.73 ? 255 ARG   A CD  1 
ATOM   1743 N  NE  . ARG   A 1 235 ? -26.437 -35.247 11.766  1.00 195.35 ? 255 ARG   A NE  1 
ATOM   1744 C  CZ  . ARG   A 1 235 ? -27.119 -35.253 10.629  1.00 191.32 ? 255 ARG   A CZ  1 
ATOM   1745 N  NH1 . ARG   A 1 235 ? -26.566 -35.644 9.492   1.00 185.57 ? 255 ARG   A NH1 1 
ATOM   1746 N  NH2 . ARG   A 1 235 ? -28.390 -34.861 10.633  1.00 193.61 ? 255 ARG   A NH2 1 
ATOM   1747 N  N   . MET   A 1 236 ? -21.210 -33.382 11.759  1.00 194.17 ? 256 MET   A N   1 
ATOM   1748 C  CA  . MET   A 1 236 ? -20.041 -34.074 11.229  1.00 195.87 ? 256 MET   A CA  1 
ATOM   1749 C  C   . MET   A 1 236 ? -18.755 -33.526 11.831  1.00 197.08 ? 256 MET   A C   1 
ATOM   1750 O  O   . MET   A 1 236 ? -17.810 -34.285 12.074  1.00 202.34 ? 256 MET   A O   1 
ATOM   1751 C  CB  . MET   A 1 236 ? -20.003 -33.951 9.707   1.00 186.23 ? 256 MET   A CB  1 
ATOM   1752 C  CG  . MET   A 1 236 ? -21.328 -34.241 9.030   1.00 186.49 ? 256 MET   A CG  1 
ATOM   1753 S  SD  . MET   A 1 236 ? -21.415 -33.481 7.402   1.00 191.66 ? 256 MET   A SD  1 
ATOM   1754 C  CE  . MET   A 1 236 ? -23.153 -33.664 7.021   1.00 187.56 ? 256 MET   A CE  1 
ATOM   1755 N  N   . LYS   A 1 237 ? -18.704 -32.212 12.066  1.00 197.34 ? 257 LYS   A N   1 
ATOM   1756 C  CA  . LYS   A 1 237 ? -17.563 -31.619 12.755  1.00 196.73 ? 257 LYS   A CA  1 
ATOM   1757 C  C   . LYS   A 1 237 ? -17.333 -32.291 14.101  1.00 208.13 ? 257 LYS   A C   1 
ATOM   1758 O  O   . LYS   A 1 237 ? -16.210 -32.688 14.428  1.00 209.89 ? 257 LYS   A O   1 
ATOM   1759 C  CB  . LYS   A 1 237 ? -17.779 -30.114 12.943  1.00 187.85 ? 257 LYS   A CB  1 
ATOM   1760 C  CG  . LYS   A 1 237 ? -17.698 -29.286 11.672  1.00 174.48 ? 257 LYS   A CG  1 
ATOM   1761 C  CD  . LYS   A 1 237 ? -17.933 -27.804 11.955  1.00 164.23 ? 257 LYS   A CD  1 
ATOM   1762 C  CE  . LYS   A 1 237 ? -16.840 -27.213 12.834  1.00 161.97 ? 257 LYS   A CE  1 
ATOM   1763 N  NZ  . LYS   A 1 237 ? -16.915 -25.727 12.887  1.00 153.98 ? 257 LYS   A NZ  1 
ATOM   1764 N  N   . GLU   A 1 238 ? -18.395 -32.439 14.893  1.00 220.37 ? 258 GLU   A N   1 
ATOM   1765 C  CA  . GLU   A 1 238 ? -18.269 -32.981 16.238  1.00 225.75 ? 258 GLU   A CA  1 
ATOM   1766 C  C   . GLU   A 1 238 ? -18.401 -34.497 16.296  1.00 229.17 ? 258 GLU   A C   1 
ATOM   1767 O  O   . GLU   A 1 238 ? -18.231 -35.073 17.376  1.00 237.35 ? 258 GLU   A O   1 
ATOM   1768 C  CB  . GLU   A 1 238 ? -19.311 -32.343 17.164  1.00 233.78 ? 258 GLU   A CB  1 
ATOM   1769 C  CG  . GLU   A 1 238 ? -18.710 -31.745 18.426  1.00 243.74 ? 258 GLU   A CG  1 
ATOM   1770 C  CD  . GLU   A 1 238 ? -19.727 -30.999 19.266  1.00 250.69 ? 258 GLU   A CD  1 
ATOM   1771 O  OE1 . GLU   A 1 238 ? -20.876 -30.836 18.806  1.00 254.30 ? 258 GLU   A OE1 1 
ATOM   1772 O  OE2 . GLU   A 1 238 ? -19.375 -30.577 20.387  1.00 255.43 ? 258 GLU   A OE2 1 
ATOM   1773 N  N   . SER   A 1 239 ? -18.708 -35.156 15.178  1.00 211.31 ? 259 SER   A N   1 
ATOM   1774 C  CA  . SER   A 1 239 ? -18.620 -36.610 15.137  1.00 208.20 ? 259 SER   A CA  1 
ATOM   1775 C  C   . SER   A 1 239 ? -17.215 -37.064 14.775  1.00 204.95 ? 259 SER   A C   1 
ATOM   1776 O  O   . SER   A 1 239 ? -16.692 -38.010 15.376  1.00 199.66 ? 259 SER   A O   1 
ATOM   1777 C  CB  . SER   A 1 239 ? -19.625 -37.189 14.136  1.00 204.60 ? 259 SER   A CB  1 
ATOM   1778 O  OG  . SER   A 1 239 ? -19.159 -37.049 12.805  1.00 196.32 ? 259 SER   A OG  1 
ATOM   1779 N  N   . ARG   A 1 240 ? -16.593 -36.400 13.798  1.00 198.74 ? 260 ARG   A N   1 
ATOM   1780 C  CA  . ARG   A 1 240 ? -15.222 -36.734 13.441  1.00 196.31 ? 260 ARG   A CA  1 
ATOM   1781 C  C   . ARG   A 1 240 ? -14.226 -36.201 14.457  1.00 199.81 ? 260 ARG   A C   1 
ATOM   1782 O  O   . ARG   A 1 240 ? -13.056 -36.595 14.427  1.00 202.19 ? 260 ARG   A O   1 
ATOM   1783 C  CB  . ARG   A 1 240 ? -14.875 -36.187 12.055  1.00 187.85 ? 260 ARG   A CB  1 
ATOM   1784 C  CG  . ARG   A 1 240 ? -14.542 -34.706 12.072  1.00 188.68 ? 260 ARG   A CG  1 
ATOM   1785 C  CD  . ARG   A 1 240 ? -13.438 -34.338 11.085  1.00 180.18 ? 260 ARG   A CD  1 
ATOM   1786 N  NE  . ARG   A 1 240 ? -13.761 -34.726 9.718   1.00 176.47 ? 260 ARG   A NE  1 
ATOM   1787 C  CZ  . ARG   A 1 240 ? -13.010 -35.521 8.968   1.00 171.80 ? 260 ARG   A CZ  1 
ATOM   1788 N  NH1 . ARG   A 1 240 ? -11.843 -35.974 9.396   1.00 172.19 ? 260 ARG   A NH1 1 
ATOM   1789 N  NH2 . ARG   A 1 240 ? -13.439 -35.867 7.758   1.00 168.65 ? 260 ARG   A NH2 1 
ATOM   1790 N  N   . LEU   A 1 241 ? -14.653 -35.300 15.332  1.00 206.86 ? 261 LEU   A N   1 
ATOM   1791 C  CA  . LEU   A 1 241 ? -13.850 -34.840 16.462  1.00 206.11 ? 261 LEU   A CA  1 
ATOM   1792 C  C   . LEU   A 1 241 ? -14.520 -35.418 17.705  1.00 204.73 ? 261 LEU   A C   1 
ATOM   1793 O  O   . LEU   A 1 241 ? -15.360 -34.767 18.327  1.00 210.87 ? 261 LEU   A O   1 
ATOM   1794 C  CB  . LEU   A 1 241 ? -13.764 -33.308 16.516  1.00 208.01 ? 261 LEU   A CB  1 
ATOM   1795 C  CG  . LEU   A 1 241 ? -13.210 -32.545 15.310  1.00 208.08 ? 261 LEU   A CG  1 
ATOM   1796 C  CD1 . LEU   A 1 241 ? -13.253 -31.045 15.567  1.00 199.60 ? 261 LEU   A CD1 1 
ATOM   1797 C  CD2 . LEU   A 1 241 ? -11.798 -32.996 14.979  1.00 208.13 ? 261 LEU   A CD2 1 
ATOM   1798 N  N   . GLU   A 1 242 ? -14.143 -36.641 18.074  1.00 202.93 ? 262 GLU   A N   1 
ATOM   1799 C  CA  . GLU   A 1 242 ? -13.051 -37.475 17.571  1.00 198.38 ? 262 GLU   A CA  1 
ATOM   1800 C  C   . GLU   A 1 242 ? -13.557 -38.770 16.914  1.00 193.72 ? 262 GLU   A C   1 
ATOM   1801 O  O   . GLU   A 1 242 ? -14.660 -39.231 17.208  1.00 198.17 ? 262 GLU   A O   1 
ATOM   1802 C  CB  . GLU   A 1 242 ? -12.101 -37.799 18.734  1.00 198.75 ? 262 GLU   A CB  1 
ATOM   1803 C  CG  . GLU   A 1 242 ? -10.911 -38.683 18.411  1.00 197.31 ? 262 GLU   A CG  1 
ATOM   1804 C  CD  . GLU   A 1 242 ? -10.063 -38.971 19.636  1.00 200.34 ? 262 GLU   A CD  1 
ATOM   1805 O  OE1 . GLU   A 1 242 ? -10.516 -38.662 20.759  1.00 200.05 ? 262 GLU   A OE1 1 
ATOM   1806 O  OE2 . GLU   A 1 242 ? -8.943  -39.500 19.478  1.00 196.41 ? 262 GLU   A OE2 1 
ATOM   1807 N  N   . ASP   A 1 243 ? -12.753 -39.346 16.021  1.00 193.33 ? 263 ASP   A N   1 
ATOM   1808 C  CA  . ASP   A 1 243 ? -13.082 -40.627 15.399  1.00 187.41 ? 263 ASP   A CA  1 
ATOM   1809 C  C   . ASP   A 1 243 ? -11.827 -41.452 15.111  1.00 183.24 ? 263 ASP   A C   1 
ATOM   1810 O  O   . ASP   A 1 243 ? -10.826 -41.351 15.821  1.00 183.70 ? 263 ASP   A O   1 
ATOM   1811 C  CB  . ASP   A 1 243 ? -13.871 -40.410 14.105  1.00 185.61 ? 263 ASP   A CB  1 
ATOM   1812 C  CG  . ASP   A 1 243 ? -13.066 -39.681 13.046  1.00 185.91 ? 263 ASP   A CG  1 
ATOM   1813 O  OD1 . ASP   A 1 243 ? -12.115 -38.958 13.411  1.00 188.53 ? 263 ASP   A OD1 1 
ATOM   1814 O  OD2 . ASP   A 1 243 ? -13.386 -39.829 11.848  1.00 178.09 ? 263 ASP   A OD2 1 
ATOM   1815 N  N   . VAL   A 1 249 ? -10.320 -37.347 4.649   1.00 168.86 ? 269 VAL   A N   1 
ATOM   1816 C  CA  . VAL   A 1 249 ? -9.915  -37.417 3.253   1.00 170.00 ? 269 VAL   A CA  1 
ATOM   1817 C  C   . VAL   A 1 249 ? -10.858 -36.561 2.402   1.00 167.31 ? 269 VAL   A C   1 
ATOM   1818 O  O   . VAL   A 1 249 ? -10.750 -36.524 1.175   1.00 164.70 ? 269 VAL   A O   1 
ATOM   1819 C  CB  . VAL   A 1 249 ? -9.876  -38.888 2.767   1.00 166.76 ? 269 VAL   A CB  1 
ATOM   1820 C  CG1 . VAL   A 1 249 ? -11.286 -39.430 2.568   1.00 164.98 ? 269 VAL   A CG1 1 
ATOM   1821 C  CG2 . VAL   A 1 249 ? -9.033  -39.034 1.500   1.00 157.36 ? 269 VAL   A CG2 1 
ATOM   1822 N  N   . ASP   A 1 250 ? -11.771 -35.853 3.062   1.00 169.20 ? 270 ASP   A N   1 
ATOM   1823 C  CA  . ASP   A 1 250 ? -12.792 -35.065 2.386   1.00 166.92 ? 270 ASP   A CA  1 
ATOM   1824 C  C   . ASP   A 1 250 ? -12.547 -33.571 2.572   1.00 160.21 ? 270 ASP   A C   1 
ATOM   1825 O  O   . ASP   A 1 250 ? -11.722 -33.146 3.387   1.00 153.99 ? 270 ASP   A O   1 
ATOM   1826 C  CB  . ASP   A 1 250 ? -14.194 -35.442 2.887   1.00 170.00 ? 270 ASP   A CB  1 
ATOM   1827 C  CG  . ASP   A 1 250 ? -14.281 -35.509 4.402   1.00 167.55 ? 270 ASP   A CG  1 
ATOM   1828 O  OD1 . ASP   A 1 250 ? -13.784 -34.582 5.076   1.00 166.21 ? 270 ASP   A OD1 1 
ATOM   1829 O  OD2 . ASP   A 1 250 ? -14.863 -36.484 4.922   1.00 171.38 ? 270 ASP   A OD2 1 
ATOM   1830 N  N   . PHE   A 1 251 ? -13.294 -32.776 1.794   1.00 161.17 ? 271 PHE   A N   1 
ATOM   1831 C  CA  . PHE   A 1 251 ? -13.171 -31.320 1.851   1.00 156.94 ? 271 PHE   A CA  1 
ATOM   1832 C  C   . PHE   A 1 251 ? -13.333 -30.789 3.271   1.00 156.82 ? 271 PHE   A C   1 
ATOM   1833 O  O   . PHE   A 1 251 ? -12.658 -29.831 3.661   1.00 151.79 ? 271 PHE   A O   1 
ATOM   1834 C  CB  . PHE   A 1 251 ? -14.207 -30.660 0.932   1.00 152.56 ? 271 PHE   A CB  1 
ATOM   1835 C  CG  . PHE   A 1 251 ? -13.894 -30.768 -0.540  1.00 146.06 ? 271 PHE   A CG  1 
ATOM   1836 C  CD1 . PHE   A 1 251 ? -12.765 -30.173 -1.065  1.00 136.67 ? 271 PHE   A CD1 1 
ATOM   1837 C  CD2 . PHE   A 1 251 ? -14.751 -31.428 -1.403  1.00 148.16 ? 271 PHE   A CD2 1 
ATOM   1838 C  CE1 . PHE   A 1 251 ? -12.474 -30.256 -2.414  1.00 127.17 ? 271 PHE   A CE1 1 
ATOM   1839 C  CE2 . PHE   A 1 251 ? -14.470 -31.515 -2.755  1.00 136.25 ? 271 PHE   A CE2 1 
ATOM   1840 C  CZ  . PHE   A 1 251 ? -13.329 -30.927 -3.261  1.00 122.63 ? 271 PHE   A CZ  1 
ATOM   1841 N  N   . LEU   A 1 252 ? -14.225 -31.400 4.058   1.00 171.38 ? 272 LEU   A N   1 
ATOM   1842 C  CA  . LEU   A 1 252 ? -14.463 -30.932 5.422   1.00 164.35 ? 272 LEU   A CA  1 
ATOM   1843 C  C   . LEU   A 1 252 ? -13.266 -31.197 6.326   1.00 166.32 ? 272 LEU   A C   1 
ATOM   1844 O  O   . LEU   A 1 252 ? -12.880 -30.325 7.114   1.00 162.90 ? 272 LEU   A O   1 
ATOM   1845 C  CB  . LEU   A 1 252 ? -15.721 -31.589 5.990   1.00 162.19 ? 272 LEU   A CB  1 
ATOM   1846 C  CG  . LEU   A 1 252 ? -16.005 -31.497 7.492   1.00 157.17 ? 272 LEU   A CG  1 
ATOM   1847 C  CD1 . LEU   A 1 252 ? -15.971 -30.060 7.993   1.00 153.59 ? 272 LEU   A CD1 1 
ATOM   1848 C  CD2 . LEU   A 1 252 ? -17.352 -32.125 7.798   1.00 168.41 ? 272 LEU   A CD2 1 
ATOM   1849 N  N   . GLN   A 1 253 ? -12.673 -32.391 6.238   1.00 171.38 ? 273 GLN   A N   1 
ATOM   1850 C  CA  . GLN   A 1 253 ? -11.458 -32.670 6.998   1.00 172.78 ? 273 GLN   A CA  1 
ATOM   1851 C  C   . GLN   A 1 253 ? -10.382 -31.639 6.697   1.00 174.25 ? 273 GLN   A C   1 
ATOM   1852 O  O   . GLN   A 1 253 ? -9.616  -31.247 7.583   1.00 176.72 ? 273 GLN   A O   1 
ATOM   1853 C  CB  . GLN   A 1 253 ? -10.940 -34.074 6.680   1.00 172.08 ? 273 GLN   A CB  1 
ATOM   1854 C  CG  . GLN   A 1 253 ? -9.642  -34.433 7.402   1.00 172.93 ? 273 GLN   A CG  1 
ATOM   1855 C  CD  . GLN   A 1 253 ? -9.046  -35.743 6.924   1.00 175.53 ? 273 GLN   A CD  1 
ATOM   1856 O  OE1 . GLN   A 1 253 ? -9.717  -36.774 6.918   1.00 175.96 ? 273 GLN   A OE1 1 
ATOM   1857 N  NE2 . GLN   A 1 253 ? -7.783  -35.708 6.508   1.00 172.43 ? 273 GLN   A NE2 1 
ATOM   1858 N  N   . LEU   A 1 254 ? -10.320 -31.178 5.449   1.00 164.72 ? 274 LEU   A N   1 
ATOM   1859 C  CA  . LEU   A 1 254 ? -9.285  -30.230 5.066   1.00 162.35 ? 274 LEU   A CA  1 
ATOM   1860 C  C   . LEU   A 1 254 ? -9.604  -28.822 5.556   1.00 163.52 ? 274 LEU   A C   1 
ATOM   1861 O  O   . LEU   A 1 254 ? -8.685  -28.059 5.878   1.00 161.72 ? 274 LEU   A O   1 
ATOM   1862 C  CB  . LEU   A 1 254 ? -9.091  -30.260 3.547   1.00 152.34 ? 274 LEU   A CB  1 
ATOM   1863 C  CG  . LEU   A 1 254 ? -8.981  -31.664 2.928   1.00 147.63 ? 274 LEU   A CG  1 
ATOM   1864 C  CD1 . LEU   A 1 254 ? -8.560  -31.622 1.465   1.00 132.94 ? 274 LEU   A CD1 1 
ATOM   1865 C  CD2 . LEU   A 1 254 ? -8.039  -32.565 3.721   1.00 148.09 ? 274 LEU   A CD2 1 
ATOM   1866 N  N   . MET   A 1 255 ? -10.889 -28.464 5.629   1.00 158.23 ? 275 MET   A N   1 
ATOM   1867 C  CA  . MET   A 1 255 ? -11.281 -27.208 6.257   1.00 156.92 ? 275 MET   A CA  1 
ATOM   1868 C  C   . MET   A 1 255 ? -11.308 -27.303 7.777   1.00 156.46 ? 275 MET   A C   1 
ATOM   1869 O  O   . MET   A 1 255 ? -11.233 -26.268 8.449   1.00 158.95 ? 275 MET   A O   1 
ATOM   1870 C  CB  . MET   A 1 255 ? -12.659 -26.755 5.769   1.00 151.41 ? 275 MET   A CB  1 
ATOM   1871 C  CG  . MET   A 1 255 ? -12.866 -26.758 4.270   1.00 148.47 ? 275 MET   A CG  1 
ATOM   1872 S  SD  . MET   A 1 255 ? -14.574 -26.322 3.886   1.00 132.44 ? 275 MET   A SD  1 
ATOM   1873 C  CE  . MET   A 1 255 ? -14.739 -26.979 2.227   1.00 118.12 ? 275 MET   A CE  1 
ATOM   1874 N  N   . ILE   A 1 256 ? -11.428 -28.511 8.331   1.00 165.14 ? 276 ILE   A N   1 
ATOM   1875 C  CA  . ILE   A 1 256 ? -11.420 -28.654 9.783   1.00 168.17 ? 276 ILE   A CA  1 
ATOM   1876 C  C   . ILE   A 1 256 ? -9.998  -28.553 10.325  1.00 172.59 ? 276 ILE   A C   1 
ATOM   1877 O  O   . ILE   A 1 256 ? -9.787  -28.035 11.428  1.00 171.53 ? 276 ILE   A O   1 
ATOM   1878 C  CB  . ILE   A 1 256 ? -12.105 -29.971 10.196  1.00 166.71 ? 276 ILE   A CB  1 
ATOM   1879 C  CG1 . ILE   A 1 256 ? -12.976 -29.755 11.431  1.00 164.97 ? 276 ILE   A CG1 1 
ATOM   1880 C  CG2 . ILE   A 1 256 ? -11.093 -31.078 10.464  1.00 167.47 ? 276 ILE   A CG2 1 
ATOM   1881 C  CD1 . ILE   A 1 256 ? -14.163 -28.868 11.175  1.00 159.96 ? 276 ILE   A CD1 1 
ATOM   1882 N  N   . ASP   A 1 257 ? -9.005  -29.015 9.561   1.00 171.00 ? 277 ASP   A N   1 
ATOM   1883 C  CA  . ASP   A 1 257 ? -7.614  -28.903 9.975   1.00 173.19 ? 277 ASP   A CA  1 
ATOM   1884 C  C   . ASP   A 1 257 ? -7.039  -27.527 9.678   1.00 173.53 ? 277 ASP   A C   1 
ATOM   1885 O  O   . ASP   A 1 257 ? -6.002  -27.167 10.244  1.00 174.85 ? 277 ASP   A O   1 
ATOM   1886 C  CB  . ASP   A 1 257 ? -6.768  -29.979 9.285   1.00 178.46 ? 277 ASP   A CB  1 
ATOM   1887 C  CG  . ASP   A 1 257 ? -7.299  -31.383 9.522   1.00 176.93 ? 277 ASP   A CG  1 
ATOM   1888 O  OD1 . ASP   A 1 257 ? -7.897  -31.622 10.592  1.00 172.00 ? 277 ASP   A OD1 1 
ATOM   1889 O  OD2 . ASP   A 1 257 ? -7.124  -32.248 8.636   1.00 174.11 ? 277 ASP   A OD2 1 
ATOM   1890 N  N   . SER   A 1 258 ? -7.691  -26.753 8.809   1.00 171.35 ? 278 SER   A N   1 
ATOM   1891 C  CA  . SER   A 1 258 ? -7.191  -25.420 8.491   1.00 172.22 ? 278 SER   A CA  1 
ATOM   1892 C  C   . SER   A 1 258 ? -7.462  -24.448 9.632   1.00 174.72 ? 278 SER   A C   1 
ATOM   1893 O  O   . SER   A 1 258 ? -6.593  -23.647 9.996   1.00 175.78 ? 278 SER   A O   1 
ATOM   1894 C  CB  . SER   A 1 258 ? -7.820  -24.922 7.190   1.00 162.83 ? 278 SER   A CB  1 
ATOM   1895 O  OG  . SER   A 1 258 ? -9.233  -24.884 7.291   1.00 161.26 ? 278 SER   A OG  1 
ATOM   1896 N  N   . GLN   A 1 259 ? -8.659  -24.500 10.205  1.00 175.37 ? 279 GLN   A N   1 
ATOM   1897 C  CA  . GLN   A 1 259 ? -9.004  -23.638 11.324  1.00 174.74 ? 279 GLN   A CA  1 
ATOM   1898 C  C   . GLN   A 1 259 ? -8.310  -24.111 12.594  1.00 180.35 ? 279 GLN   A C   1 
ATOM   1899 O  O   . GLN   A 1 259 ? -8.266  -23.393 13.591  1.00 182.78 ? 279 GLN   A O   1 
ATOM   1900 C  CB  . GLN   A 1 259 ? -10.520 -23.599 11.529  1.00 172.29 ? 279 GLN   A CB  1 
ATOM   1901 C  CG  . GLN   A 1 259 ? -11.186 -24.963 11.576  1.00 168.33 ? 279 GLN   A CG  1 
ATOM   1902 C  CD  . GLN   A 1 259 ? -12.682 -24.867 11.810  1.00 164.18 ? 279 GLN   A CD  1 
ATOM   1903 O  OE1 . GLN   A 1 259 ? -13.431 -25.792 11.500  1.00 158.83 ? 279 GLN   A OE1 1 
ATOM   1904 N  NE2 . GLN   A 1 259 ? -13.124 -23.742 12.362  1.00 159.01 ? 279 GLN   A NE2 1 
ATOM   1905 N  N   . LYS   A 1 268 ? -7.897  -15.193 11.885  1.00 167.12 ? 288 LYS   A N   1 
ATOM   1906 C  CA  . LYS   A 1 268 ? -7.342  -15.418 10.555  1.00 162.84 ? 288 LYS   A CA  1 
ATOM   1907 C  C   . LYS   A 1 268 ? -7.709  -16.809 10.042  1.00 167.54 ? 288 LYS   A C   1 
ATOM   1908 O  O   . LYS   A 1 268 ? -7.976  -16.992 8.853   1.00 164.11 ? 288 LYS   A O   1 
ATOM   1909 C  CB  . LYS   A 1 268 ? -5.823  -15.233 10.576  1.00 162.03 ? 288 LYS   A CB  1 
ATOM   1910 C  CG  . LYS   A 1 268 ? -5.097  -15.716 9.329   1.00 159.44 ? 288 LYS   A CG  1 
ATOM   1911 C  CD  . LYS   A 1 268 ? -5.412  -14.864 8.113   1.00 150.16 ? 288 LYS   A CD  1 
ATOM   1912 C  CE  . LYS   A 1 268 ? -4.354  -15.061 7.041   1.00 145.57 ? 288 LYS   A CE  1 
ATOM   1913 N  NZ  . LYS   A 1 268 ? -2.989  -14.809 7.592   1.00 150.84 ? 288 LYS   A NZ  1 
ATOM   1914 N  N   . ALA   A 1 269 ? -7.727  -17.786 10.946  1.00 196.72 ? 289 ALA   A N   1 
ATOM   1915 C  CA  . ALA   A 1 269 ? -8.146  -19.130 10.581  1.00 195.70 ? 289 ALA   A CA  1 
ATOM   1916 C  C   . ALA   A 1 269 ? -9.658  -19.172 10.369  1.00 195.75 ? 289 ALA   A C   1 
ATOM   1917 O  O   . ALA   A 1 269 ? -10.382 -18.205 10.627  1.00 193.38 ? 289 ALA   A O   1 
ATOM   1918 C  CB  . ALA   A 1 269 ? -7.724  -20.136 11.651  1.00 198.06 ? 289 ALA   A CB  1 
ATOM   1919 N  N   . LEU   A 1 270 ? -10.136 -20.319 9.896   1.00 175.87 ? 290 LEU   A N   1 
ATOM   1920 C  CA  . LEU   A 1 270 ? -11.533 -20.439 9.505   1.00 164.40 ? 290 LEU   A CA  1 
ATOM   1921 C  C   . LEU   A 1 270 ? -12.456 -20.334 10.712  1.00 160.75 ? 290 LEU   A C   1 
ATOM   1922 O  O   . LEU   A 1 270 ? -12.137 -20.806 11.807  1.00 165.95 ? 290 LEU   A O   1 
ATOM   1923 C  CB  . LEU   A 1 270 ? -11.775 -21.765 8.785   1.00 161.15 ? 290 LEU   A CB  1 
ATOM   1924 C  CG  . LEU   A 1 270 ? -12.271 -21.680 7.341   1.00 158.91 ? 290 LEU   A CG  1 
ATOM   1925 C  CD1 . LEU   A 1 270 ? -12.943 -22.977 6.902   1.00 158.53 ? 290 LEU   A CD1 1 
ATOM   1926 C  CD2 . LEU   A 1 270 ? -13.177 -20.482 7.121   1.00 149.33 ? 290 LEU   A CD2 1 
ATOM   1927 N  N   . SER   A 1 271 ? -13.605 -19.698 10.506  1.00 165.63 ? 291 SER   A N   1 
ATOM   1928 C  CA  . SER   A 1 271 ? -14.681 -19.692 11.482  1.00 161.83 ? 291 SER   A CA  1 
ATOM   1929 C  C   . SER   A 1 271 ? -15.644 -20.843 11.198  1.00 161.13 ? 291 SER   A C   1 
ATOM   1930 O  O   . SER   A 1 271 ? -15.622 -21.454 10.128  1.00 160.57 ? 291 SER   A O   1 
ATOM   1931 C  CB  . SER   A 1 271 ? -15.414 -18.352 11.465  1.00 156.88 ? 291 SER   A CB  1 
ATOM   1932 O  OG  . SER   A 1 271 ? -16.759 -18.500 11.884  1.00 155.18 ? 291 SER   A OG  1 
ATOM   1933 N  N   . ASP   A 1 272 ? -16.505 -21.136 12.176  1.00 156.21 ? 292 ASP   A N   1 
ATOM   1934 C  CA  . ASP   A 1 272 ? -17.383 -22.298 12.060  1.00 152.63 ? 292 ASP   A CA  1 
ATOM   1935 C  C   . ASP   A 1 272 ? -18.513 -22.070 11.058  1.00 143.89 ? 292 ASP   A C   1 
ATOM   1936 O  O   . ASP   A 1 272 ? -18.821 -22.961 10.259  1.00 142.36 ? 292 ASP   A O   1 
ATOM   1937 C  CB  . ASP   A 1 272 ? -17.943 -22.676 13.435  1.00 156.49 ? 292 ASP   A CB  1 
ATOM   1938 C  CG  . ASP   A 1 272 ? -18.846 -21.607 14.028  1.00 157.11 ? 292 ASP   A CG  1 
ATOM   1939 O  OD1 . ASP   A 1 272 ? -18.902 -20.486 13.480  1.00 155.74 ? 292 ASP   A OD1 1 
ATOM   1940 O  OD2 . ASP   A 1 272 ? -19.509 -21.896 15.049  1.00 158.43 ? 292 ASP   A OD2 1 
ATOM   1941 N  N   . LEU   A 1 273 ? -19.142 -20.891 11.085  1.00 142.15 ? 293 LEU   A N   1 
ATOM   1942 C  CA  . LEU   A 1 273 ? -20.178 -20.587 10.102  1.00 140.13 ? 293 LEU   A CA  1 
ATOM   1943 C  C   . LEU   A 1 273 ? -19.568 -20.358 8.725   1.00 138.69 ? 293 LEU   A C   1 
ATOM   1944 O  O   . LEU   A 1 273 ? -20.168 -20.726 7.708   1.00 132.58 ? 293 LEU   A O   1 
ATOM   1945 C  CB  . LEU   A 1 273 ? -20.988 -19.369 10.548  1.00 142.51 ? 293 LEU   A CB  1 
ATOM   1946 C  CG  . LEU   A 1 273 ? -22.369 -19.079 9.938   1.00 134.22 ? 293 LEU   A CG  1 
ATOM   1947 C  CD1 . LEU   A 1 273 ? -22.277 -18.475 8.538   1.00 128.76 ? 293 LEU   A CD1 1 
ATOM   1948 C  CD2 . LEU   A 1 273 ? -23.243 -20.331 9.928   1.00 128.99 ? 293 LEU   A CD2 1 
ATOM   1949 N  N   . GLU   A 1 274 ? -18.387 -19.735 8.677   1.00 146.87 ? 294 GLU   A N   1 
ATOM   1950 C  CA  . GLU   A 1 274 ? -17.648 -19.611 7.425   1.00 145.08 ? 294 GLU   A CA  1 
ATOM   1951 C  C   . GLU   A 1 274 ? -17.495 -20.966 6.750   1.00 140.45 ? 294 GLU   A C   1 
ATOM   1952 O  O   . GLU   A 1 274 ? -17.731 -21.109 5.546   1.00 138.23 ? 294 GLU   A O   1 
ATOM   1953 C  CB  . GLU   A 1 274 ? -16.273 -18.994 7.693   1.00 149.28 ? 294 GLU   A CB  1 
ATOM   1954 C  CG  . GLU   A 1 274 ? -16.164 -17.503 7.425   1.00 152.31 ? 294 GLU   A CG  1 
ATOM   1955 C  CD  . GLU   A 1 274 ? -16.735 -16.651 8.542   1.00 158.64 ? 294 GLU   A CD  1 
ATOM   1956 O  OE1 . GLU   A 1 274 ? -17.447 -17.194 9.414   1.00 161.26 ? 294 GLU   A OE1 1 
ATOM   1957 O  OE2 . GLU   A 1 274 ? -16.468 -15.431 8.548   1.00 161.11 ? 294 GLU   A OE2 1 
ATOM   1958 N  N   . LEU   A 1 275 ? -17.108 -21.978 7.528   1.00 139.53 ? 295 LEU   A N   1 
ATOM   1959 C  CA  . LEU   A 1 275 ? -16.922 -23.319 6.987   1.00 134.68 ? 295 LEU   A CA  1 
ATOM   1960 C  C   . LEU   A 1 275 ? -18.231 -23.905 6.469   1.00 125.62 ? 295 LEU   A C   1 
ATOM   1961 O  O   . LEU   A 1 275 ? -18.224 -24.690 5.513   1.00 119.21 ? 295 LEU   A O   1 
ATOM   1962 C  CB  . LEU   A 1 275 ? -16.299 -24.205 8.066   1.00 137.78 ? 295 LEU   A CB  1 
ATOM   1963 C  CG  . LEU   A 1 275 ? -16.212 -25.717 7.907   1.00 134.38 ? 295 LEU   A CG  1 
ATOM   1964 C  CD1 . LEU   A 1 275 ? -14.872 -26.207 8.402   1.00 146.11 ? 295 LEU   A CD1 1 
ATOM   1965 C  CD2 . LEU   A 1 275 ? -17.303 -26.335 8.725   1.00 135.42 ? 295 LEU   A CD2 1 
ATOM   1966 N  N   . VAL   A 1 276 ? -19.361 -23.532 7.074   1.00 131.10 ? 296 VAL   A N   1 
ATOM   1967 C  CA  . VAL   A 1 276 ? -20.654 -23.969 6.560   1.00 125.67 ? 296 VAL   A CA  1 
ATOM   1968 C  C   . VAL   A 1 276 ? -20.947 -23.315 5.216   1.00 121.36 ? 296 VAL   A C   1 
ATOM   1969 O  O   . VAL   A 1 276 ? -21.588 -23.919 4.347   1.00 115.85 ? 296 VAL   A O   1 
ATOM   1970 C  CB  . VAL   A 1 276 ? -21.761 -23.666 7.586   1.00 128.79 ? 296 VAL   A CB  1 
ATOM   1971 C  CG1 . VAL   A 1 276 ? -23.123 -24.075 7.046   1.00 132.93 ? 296 VAL   A CG1 1 
ATOM   1972 C  CG2 . VAL   A 1 276 ? -21.469 -24.370 8.897   1.00 138.41 ? 296 VAL   A CG2 1 
ATOM   1973 N  N   . ALA   A 1 277 ? -20.476 -22.084 5.014   1.00 115.95 ? 297 ALA   A N   1 
ATOM   1974 C  CA  . ALA   A 1 277 ? -20.773 -21.377 3.774   1.00 108.48 ? 297 ALA   A CA  1 
ATOM   1975 C  C   . ALA   A 1 277 ? -19.949 -21.909 2.608   1.00 103.50 ? 297 ALA   A C   1 
ATOM   1976 O  O   . ALA   A 1 277 ? -20.421 -21.899 1.465   1.00 100.25 ? 297 ALA   A O   1 
ATOM   1977 C  CB  . ALA   A 1 277 ? -20.539 -19.879 3.952   1.00 109.04 ? 297 ALA   A CB  1 
ATOM   1978 N  N   . GLN   A 1 278 ? -18.720 -22.364 2.865   1.00 113.46 ? 298 GLN   A N   1 
ATOM   1979 C  CA  . GLN   A 1 278 ? -17.909 -22.920 1.786   1.00 107.26 ? 298 GLN   A CA  1 
ATOM   1980 C  C   . GLN   A 1 278 ? -18.436 -24.279 1.353   1.00 105.49 ? 298 GLN   A C   1 
ATOM   1981 O  O   . GLN   A 1 278 ? -18.362 -24.635 0.170   1.00 103.33 ? 298 GLN   A O   1 
ATOM   1982 C  CB  . GLN   A 1 278 ? -16.448 -23.032 2.218   1.00 106.70 ? 298 GLN   A CB  1 
ATOM   1983 C  CG  . GLN   A 1 278 ? -15.923 -21.826 2.971   1.00 109.69 ? 298 GLN   A CG  1 
ATOM   1984 C  CD  . GLN   A 1 278 ? -16.257 -20.515 2.289   1.00 107.26 ? 298 GLN   A CD  1 
ATOM   1985 O  OE1 . GLN   A 1 278 ? -16.173 -20.391 1.065   1.00 104.48 ? 298 GLN   A OE1 1 
ATOM   1986 N  NE2 . GLN   A 1 278 ? -16.649 -19.526 3.083   1.00 108.06 ? 298 GLN   A NE2 1 
ATOM   1987 N  N   . SER   A 1 279 ? -18.968 -25.051 2.302   1.00 108.83 ? 299 SER   A N   1 
ATOM   1988 C  CA  . SER   A 1 279 ? -19.532 -26.355 1.980   1.00 104.39 ? 299 SER   A CA  1 
ATOM   1989 C  C   . SER   A 1 279 ? -20.638 -26.234 0.940   1.00 105.92 ? 299 SER   A C   1 
ATOM   1990 O  O   . SER   A 1 279 ? -20.743 -27.067 0.034   1.00 106.41 ? 299 SER   A O   1 
ATOM   1991 C  CB  . SER   A 1 279 ? -20.063 -27.014 3.251   1.00 114.92 ? 299 SER   A CB  1 
ATOM   1992 O  OG  . SER   A 1 279 ? -19.135 -26.897 4.316   1.00 120.31 ? 299 SER   A OG  1 
ATOM   1993 N  N   . ILE   A 1 280 ? -21.461 -25.189 1.046   1.00 107.11 ? 300 ILE   A N   1 
ATOM   1994 C  CA  . ILE   A 1 280 ? -22.595 -25.037 0.141   1.00 101.86 ? 300 ILE   A CA  1 
ATOM   1995 C  C   . ILE   A 1 280 ? -22.122 -24.670 -1.261  1.00 96.22  ? 300 ILE   A C   1 
ATOM   1996 O  O   . ILE   A 1 280 ? -22.678 -25.141 -2.261  1.00 97.45  ? 300 ILE   A O   1 
ATOM   1997 C  CB  . ILE   A 1 280 ? -23.580 -23.999 0.707   1.00 100.53 ? 300 ILE   A CB  1 
ATOM   1998 C  CG1 . ILE   A 1 280 ? -24.032 -24.422 2.106   1.00 103.11 ? 300 ILE   A CG1 1 
ATOM   1999 C  CG2 . ILE   A 1 280 ? -24.780 -23.836 -0.210  1.00 104.38 ? 300 ILE   A CG2 1 
ATOM   2000 C  CD1 . ILE   A 1 280 ? -24.964 -23.440 2.768   1.00 108.82 ? 300 ILE   A CD1 1 
ATOM   2001 N  N   . ILE   A 1 281 ? -21.088 -23.831 -1.362  1.00 105.66 ? 301 ILE   A N   1 
ATOM   2002 C  CA  . ILE   A 1 281 ? -20.511 -23.519 -2.668  1.00 105.26 ? 301 ILE   A CA  1 
ATOM   2003 C  C   . ILE   A 1 281 ? -19.945 -24.778 -3.308  1.00 107.06 ? 301 ILE   A C   1 
ATOM   2004 O  O   . ILE   A 1 281 ? -20.218 -25.083 -4.475  1.00 113.72 ? 301 ILE   A O   1 
ATOM   2005 C  CB  . ILE   A 1 281 ? -19.434 -22.429 -2.535  1.00 98.36  ? 301 ILE   A CB  1 
ATOM   2006 C  CG1 . ILE   A 1 281 ? -20.070 -21.104 -2.122  1.00 98.84  ? 301 ILE   A CG1 1 
ATOM   2007 C  CG2 . ILE   A 1 281 ? -18.661 -22.281 -3.840  1.00 99.99  ? 301 ILE   A CG2 1 
ATOM   2008 C  CD1 . ILE   A 1 281 ? -21.009 -20.534 -3.152  1.00 103.15 ? 301 ILE   A CD1 1 
ATOM   2009 N  N   . PHE   A 1 282 ? -19.148 -25.530 -2.549  1.00 94.15  ? 302 PHE   A N   1 
ATOM   2010 C  CA  . PHE   A 1 282 ? -18.528 -26.735 -3.087  1.00 100.45 ? 302 PHE   A CA  1 
ATOM   2011 C  C   . PHE   A 1 282 ? -19.581 -27.746 -3.525  1.00 103.83 ? 302 PHE   A C   1 
ATOM   2012 O  O   . PHE   A 1 282 ? -19.477 -28.337 -4.606  1.00 104.58 ? 302 PHE   A O   1 
ATOM   2013 C  CB  . PHE   A 1 282 ? -17.597 -27.363 -2.049  1.00 103.20 ? 302 PHE   A CB  1 
ATOM   2014 C  CG  . PHE   A 1 282 ? -16.296 -26.632 -1.858  1.00 100.13 ? 302 PHE   A CG  1 
ATOM   2015 C  CD1 . PHE   A 1 282 ? -16.202 -25.259 -2.033  1.00 100.38 ? 302 PHE   A CD1 1 
ATOM   2016 C  CD2 . PHE   A 1 282 ? -15.161 -27.334 -1.497  1.00 107.52 ? 302 PHE   A CD2 1 
ATOM   2017 C  CE1 . PHE   A 1 282 ? -15.002 -24.604 -1.848  1.00 98.48  ? 302 PHE   A CE1 1 
ATOM   2018 C  CE2 . PHE   A 1 282 ? -13.960 -26.686 -1.311  1.00 110.23 ? 302 PHE   A CE2 1 
ATOM   2019 C  CZ  . PHE   A 1 282 ? -13.879 -25.318 -1.487  1.00 109.74 ? 302 PHE   A CZ  1 
ATOM   2020 N  N   . ILE   A 1 283 ? -20.604 -27.957 -2.691  1.00 106.41 ? 303 ILE   A N   1 
ATOM   2021 C  CA  . ILE   A 1 283 ? -21.644 -28.936 -3.007  1.00 103.54 ? 303 ILE   A CA  1 
ATOM   2022 C  C   . ILE   A 1 283 ? -22.288 -28.615 -4.348  1.00 103.23 ? 303 ILE   A C   1 
ATOM   2023 O  O   . ILE   A 1 283 ? -22.423 -29.485 -5.215  1.00 108.50 ? 303 ILE   A O   1 
ATOM   2024 C  CB  . ILE   A 1 283 ? -22.696 -28.996 -1.885  1.00 103.13 ? 303 ILE   A CB  1 
ATOM   2025 C  CG1 . ILE   A 1 283 ? -22.149 -29.708 -0.651  1.00 111.54 ? 303 ILE   A CG1 1 
ATOM   2026 C  CG2 . ILE   A 1 283 ? -23.945 -29.715 -2.366  1.00 107.77 ? 303 ILE   A CG2 1 
ATOM   2027 C  CD1 . ILE   A 1 283 ? -23.090 -29.620 0.528   1.00 119.21 ? 303 ILE   A CD1 1 
ATOM   2028 N  N   . PHE   A 1 284 ? -22.689 -27.360 -4.544  1.00 106.89 ? 304 PHE   A N   1 
ATOM   2029 C  CA  . PHE   A 1 284 ? -23.330 -26.999 -5.803  1.00 104.43 ? 304 PHE   A CA  1 
ATOM   2030 C  C   . PHE   A 1 284 ? -22.368 -27.147 -6.971  1.00 111.25 ? 304 PHE   A C   1 
ATOM   2031 O  O   . PHE   A 1 284 ? -22.670 -27.824 -7.960  1.00 114.01 ? 304 PHE   A O   1 
ATOM   2032 C  CB  . PHE   A 1 284 ? -23.868 -25.574 -5.756  1.00 102.77 ? 304 PHE   A CB  1 
ATOM   2033 C  CG  . PHE   A 1 284 ? -24.444 -25.119 -7.067  1.00 108.36 ? 304 PHE   A CG  1 
ATOM   2034 C  CD1 . PHE   A 1 284 ? -25.771 -25.365 -7.374  1.00 109.04 ? 304 PHE   A CD1 1 
ATOM   2035 C  CD2 . PHE   A 1 284 ? -23.653 -24.463 -8.001  1.00 109.70 ? 304 PHE   A CD2 1 
ATOM   2036 C  CE1 . PHE   A 1 284 ? -26.304 -24.960 -8.583  1.00 112.30 ? 304 PHE   A CE1 1 
ATOM   2037 C  CE2 . PHE   A 1 284 ? -24.178 -24.058 -9.212  1.00 113.37 ? 304 PHE   A CE2 1 
ATOM   2038 C  CZ  . PHE   A 1 284 ? -25.506 -24.305 -9.504  1.00 115.97 ? 304 PHE   A CZ  1 
ATOM   2039 N  N   . ALA   A 1 285 ? -21.214 -26.479 -6.886  1.00 102.29 ? 305 ALA   A N   1 
ATOM   2040 C  CA  . ALA   A 1 285 ? -20.216 -26.506 -7.948  1.00 97.22  ? 305 ALA   A CA  1 
ATOM   2041 C  C   . ALA   A 1 285 ? -19.977 -27.926 -8.443  1.00 99.01  ? 305 ALA   A C   1 
ATOM   2042 O  O   . ALA   A 1 285 ? -20.172 -28.227 -9.625  1.00 103.46 ? 305 ALA   A O   1 
ATOM   2043 C  CB  . ALA   A 1 285 ? -18.911 -25.884 -7.452  1.00 95.23  ? 305 ALA   A CB  1 
ATOM   2044 N  N   . GLY   A 1 286 ? -19.585 -28.821 -7.537  1.00 99.76  ? 306 GLY   A N   1 
ATOM   2045 C  CA  . GLY   A 1 286 ? -19.393 -30.208 -7.905  1.00 102.18 ? 306 GLY   A CA  1 
ATOM   2046 C  C   . GLY   A 1 286 ? -20.643 -30.907 -8.407  1.00 108.48 ? 306 GLY   A C   1 
ATOM   2047 O  O   . GLY   A 1 286 ? -20.532 -32.011 -8.954  1.00 108.52 ? 306 GLY   A O   1 
ATOM   2048 N  N   . TYR   A 1 287 ? -21.824 -30.312 -8.227  1.00 108.71 ? 307 TYR   A N   1 
ATOM   2049 C  CA  . TYR   A 1 287 ? -23.070 -30.959 -8.663  1.00 107.71 ? 307 TYR   A CA  1 
ATOM   2050 C  C   . TYR   A 1 287 ? -23.467 -30.503 -10.059 1.00 106.40 ? 307 TYR   A C   1 
ATOM   2051 O  O   . TYR   A 1 287 ? -23.345 -31.256 -11.028 1.00 107.43 ? 307 TYR   A O   1 
ATOM   2052 C  CB  . TYR   A 1 287 ? -24.214 -30.683 -7.688  1.00 109.43 ? 307 TYR   A CB  1 
ATOM   2053 C  CG  . TYR   A 1 287 ? -25.543 -31.173 -8.216  1.00 110.29 ? 307 TYR   A CG  1 
ATOM   2054 C  CD1 . TYR   A 1 287 ? -25.806 -32.532 -8.325  1.00 113.19 ? 307 TYR   A CD1 1 
ATOM   2055 C  CD2 . TYR   A 1 287 ? -26.524 -30.279 -8.623  1.00 108.12 ? 307 TYR   A CD2 1 
ATOM   2056 C  CE1 . TYR   A 1 287 ? -27.014 -32.988 -8.815  1.00 110.58 ? 307 TYR   A CE1 1 
ATOM   2057 C  CE2 . TYR   A 1 287 ? -27.734 -30.725 -9.114  1.00 110.61 ? 307 TYR   A CE2 1 
ATOM   2058 C  CZ  . TYR   A 1 287 ? -27.973 -32.080 -9.208  1.00 112.12 ? 307 TYR   A CZ  1 
ATOM   2059 O  OH  . TYR   A 1 287 ? -29.176 -32.527 -9.697  1.00 113.29 ? 307 TYR   A OH  1 
ATOM   2060 N  N   . GLU   A 1 288 ? -23.970 -29.275 -10.156 1.00 105.22 ? 308 GLU   A N   1 
ATOM   2061 C  CA  . GLU   A 1 288 ? -24.514 -28.799 -11.418 1.00 103.79 ? 308 GLU   A CA  1 
ATOM   2062 C  C   . GLU   A 1 288 ? -23.440 -28.765 -12.494 1.00 104.00 ? 308 GLU   A C   1 
ATOM   2063 O  O   . GLU   A 1 288 ? -23.631 -29.299 -13.592 1.00 105.39 ? 308 GLU   A O   1 
ATOM   2064 C  CB  . GLU   A 1 288 ? -25.142 -27.417 -11.233 1.00 105.65 ? 308 GLU   A CB  1 
ATOM   2065 C  CG  . GLU   A 1 288 ? -26.259 -27.112 -12.218 1.00 110.71 ? 308 GLU   A CG  1 
ATOM   2066 C  CD  . GLU   A 1 288 ? -25.775 -26.995 -13.654 1.00 113.59 ? 308 GLU   A CD  1 
ATOM   2067 O  OE1 . GLU   A 1 288 ? -24.668 -26.456 -13.876 1.00 108.96 ? 308 GLU   A OE1 1 
ATOM   2068 O  OE2 . GLU   A 1 288 ? -26.506 -27.446 -14.562 1.00 117.08 ? 308 GLU   A OE2 1 
ATOM   2069 N  N   . THR   A 1 289 ? -22.295 -28.150 -12.192 1.00 104.02 ? 309 THR   A N   1 
ATOM   2070 C  CA  . THR   A 1 289 ? -21.270 -27.964 -13.213 1.00 99.97  ? 309 THR   A CA  1 
ATOM   2071 C  C   . THR   A 1 289 ? -20.786 -29.303 -13.753 1.00 100.33 ? 309 THR   A C   1 
ATOM   2072 O  O   . THR   A 1 289 ? -20.666 -29.487 -14.969 1.00 99.01  ? 309 THR   A O   1 
ATOM   2073 C  CB  . THR   A 1 289 ? -20.096 -27.160 -12.653 1.00 94.44  ? 309 THR   A CB  1 
ATOM   2074 O  OG1 . THR   A 1 289 ? -19.283 -28.007 -11.832 1.00 91.29  ? 309 THR   A OG1 1 
ATOM   2075 C  CG2 . THR   A 1 289 ? -20.602 -25.984 -11.828 1.00 93.79  ? 309 THR   A CG2 1 
ATOM   2076 N  N   . THR   A 1 290 ? -20.516 -30.259 -12.860 1.00 104.44 ? 310 THR   A N   1 
ATOM   2077 C  CA  . THR   A 1 290 ? -20.012 -31.557 -13.299 1.00 100.79 ? 310 THR   A CA  1 
ATOM   2078 C  C   . THR   A 1 290 ? -21.046 -32.290 -14.144 1.00 96.66  ? 310 THR   A C   1 
ATOM   2079 O  O   . THR   A 1 290 ? -20.736 -32.788 -15.232 1.00 92.50  ? 310 THR   A O   1 
ATOM   2080 C  CB  . THR   A 1 290 ? -19.611 -32.408 -12.094 1.00 98.27  ? 310 THR   A CB  1 
ATOM   2081 O  OG1 . THR   A 1 290 ? -18.819 -31.629 -11.191 1.00 100.68 ? 310 THR   A OG1 1 
ATOM   2082 C  CG2 . THR   A 1 290 ? -18.803 -33.613 -12.551 1.00 100.53 ? 310 THR   A CG2 1 
ATOM   2083 N  N   . SER   A 1 291 ? -22.287 -32.359 -13.662 1.00 99.71  ? 311 SER   A N   1 
ATOM   2084 C  CA  . SER   A 1 291 ? -23.305 -33.130 -14.368 1.00 99.14  ? 311 SER   A CA  1 
ATOM   2085 C  C   . SER   A 1 291 ? -23.736 -32.441 -15.657 1.00 96.31  ? 311 SER   A C   1 
ATOM   2086 O  O   . SER   A 1 291 ? -24.015 -33.109 -16.659 1.00 98.58  ? 311 SER   A O   1 
ATOM   2087 C  CB  . SER   A 1 291 ? -24.510 -33.367 -13.461 1.00 105.20 ? 311 SER   A CB  1 
ATOM   2088 O  OG  . SER   A 1 291 ? -25.162 -32.147 -13.156 1.00 108.98 ? 311 SER   A OG  1 
ATOM   2089 N  N   . SER   A 1 292 ? -23.802 -31.107 -15.654 1.00 93.72  ? 312 SER   A N   1 
ATOM   2090 C  CA  . SER   A 1 292 ? -24.236 -30.398 -16.855 1.00 94.85  ? 312 SER   A CA  1 
ATOM   2091 C  C   . SER   A 1 292 ? -23.218 -30.543 -17.981 1.00 91.41  ? 312 SER   A C   1 
ATOM   2092 O  O   . SER   A 1 292 ? -23.595 -30.721 -19.145 1.00 91.70  ? 312 SER   A O   1 
ATOM   2093 C  CB  . SER   A 1 292 ? -24.483 -28.923 -16.536 1.00 97.12  ? 312 SER   A CB  1 
ATOM   2094 O  OG  . SER   A 1 292 ? -25.204 -28.283 -17.577 1.00 101.00 ? 312 SER   A OG  1 
ATOM   2095 N  N   . VAL   A 1 293 ? -21.925 -30.485 -17.655 1.00 90.53  ? 313 VAL   A N   1 
ATOM   2096 C  CA  . VAL   A 1 293 ? -20.896 -30.625 -18.681 1.00 89.02  ? 313 VAL   A CA  1 
ATOM   2097 C  C   . VAL   A 1 293 ? -20.808 -32.068 -19.164 1.00 88.61  ? 313 VAL   A C   1 
ATOM   2098 O  O   . VAL   A 1 293 ? -20.670 -32.323 -20.366 1.00 89.56  ? 313 VAL   A O   1 
ATOM   2099 C  CB  . VAL   A 1 293 ? -19.541 -30.119 -18.156 1.00 88.99  ? 313 VAL   A CB  1 
ATOM   2100 C  CG1 . VAL   A 1 293 ? -18.442 -30.415 -19.161 1.00 86.00  ? 313 VAL   A CG1 1 
ATOM   2101 C  CG2 . VAL   A 1 293 ? -19.607 -28.630 -17.887 1.00 77.11  ? 313 VAL   A CG2 1 
ATOM   2102 N  N   . LEU   A 1 294 ? -20.884 -33.033 -18.242 1.00 95.31  ? 314 LEU   A N   1 
ATOM   2103 C  CA  . LEU   A 1 294 ? -20.840 -34.439 -18.635 1.00 94.89  ? 314 LEU   A CA  1 
ATOM   2104 C  C   . LEU   A 1 294 ? -21.992 -34.799 -19.564 1.00 95.00  ? 314 LEU   A C   1 
ATOM   2105 O  O   . LEU   A 1 294 ? -21.879 -35.741 -20.357 1.00 93.47  ? 314 LEU   A O   1 
ATOM   2106 C  CB  . LEU   A 1 294 ? -20.860 -35.335 -17.397 1.00 87.68  ? 314 LEU   A CB  1 
ATOM   2107 C  CG  . LEU   A 1 294 ? -19.532 -35.542 -16.670 1.00 85.41  ? 314 LEU   A CG  1 
ATOM   2108 C  CD1 . LEU   A 1 294 ? -19.751 -36.163 -15.300 1.00 89.14  ? 314 LEU   A CD1 1 
ATOM   2109 C  CD2 . LEU   A 1 294 ? -18.624 -36.416 -17.509 1.00 84.44  ? 314 LEU   A CD2 1 
ATOM   2110 N  N   . SER   A 1 295 ? -23.106 -34.069 -19.479 1.00 86.54  ? 315 SER   A N   1 
ATOM   2111 C  CA  . SER   A 1 295 ? -24.226 -34.316 -20.380 1.00 87.92  ? 315 SER   A CA  1 
ATOM   2112 C  C   . SER   A 1 295 ? -23.968 -33.723 -21.761 1.00 87.76  ? 315 SER   A C   1 
ATOM   2113 O  O   . SER   A 1 295 ? -24.261 -34.365 -22.776 1.00 86.90  ? 315 SER   A O   1 
ATOM   2114 C  CB  . SER   A 1 295 ? -25.517 -33.747 -19.787 1.00 96.17  ? 315 SER   A CB  1 
ATOM   2115 O  OG  . SER   A 1 295 ? -25.710 -34.176 -18.448 1.00 102.09 ? 315 SER   A OG  1 
ATOM   2116 N  N   . PHE   A 1 296 ? -23.428 -32.500 -21.814 1.00 87.33  ? 316 PHE   A N   1 
ATOM   2117 C  CA  . PHE   A 1 296 ? -23.041 -31.906 -23.092 1.00 89.42  ? 316 PHE   A CA  1 
ATOM   2118 C  C   . PHE   A 1 296 ? -22.042 -32.790 -23.831 1.00 87.84  ? 316 PHE   A C   1 
ATOM   2119 O  O   . PHE   A 1 296 ? -22.152 -32.980 -25.050 1.00 81.93  ? 316 PHE   A O   1 
ATOM   2120 C  CB  . PHE   A 1 296 ? -22.445 -30.515 -22.869 1.00 93.22  ? 316 PHE   A CB  1 
ATOM   2121 C  CG  . PHE   A 1 296 ? -23.455 -29.464 -22.505 1.00 90.08  ? 316 PHE   A CG  1 
ATOM   2122 C  CD1 . PHE   A 1 296 ? -24.615 -29.305 -23.245 1.00 91.28  ? 316 PHE   A CD1 1 
ATOM   2123 C  CD2 . PHE   A 1 296 ? -23.238 -28.625 -21.425 1.00 88.97  ? 316 PHE   A CD2 1 
ATOM   2124 C  CE1 . PHE   A 1 296 ? -25.542 -28.332 -22.912 1.00 95.18  ? 316 PHE   A CE1 1 
ATOM   2125 C  CE2 . PHE   A 1 296 ? -24.158 -27.652 -21.084 1.00 92.01  ? 316 PHE   A CE2 1 
ATOM   2126 C  CZ  . PHE   A 1 296 ? -25.312 -27.505 -21.829 1.00 94.62  ? 316 PHE   A CZ  1 
ATOM   2127 N  N   . ILE   A 1 297 ? -21.063 -33.340 -23.107 1.00 85.52  ? 317 ILE   A N   1 
ATOM   2128 C  CA  . ILE   A 1 297 ? -20.030 -34.169 -23.727 1.00 86.56  ? 317 ILE   A CA  1 
ATOM   2129 C  C   . ILE   A 1 297 ? -20.649 -35.387 -24.399 1.00 86.63  ? 317 ILE   A C   1 
ATOM   2130 O  O   . ILE   A 1 297 ? -20.341 -35.708 -25.553 1.00 86.52  ? 317 ILE   A O   1 
ATOM   2131 C  CB  . ILE   A 1 297 ? -18.977 -34.588 -22.685 1.00 86.33  ? 317 ILE   A CB  1 
ATOM   2132 C  CG1 . ILE   A 1 297 ? -18.145 -33.384 -22.235 1.00 82.93  ? 317 ILE   A CG1 1 
ATOM   2133 C  CG2 . ILE   A 1 297 ? -18.090 -35.704 -23.238 1.00 87.95  ? 317 ILE   A CG2 1 
ATOM   2134 C  CD1 . ILE   A 1 297 ? -16.986 -33.745 -21.328 1.00 83.50  ? 317 ILE   A CD1 1 
ATOM   2135 N  N   . MET   A 1 298 ? -21.523 -36.095 -23.682 1.00 84.42  ? 318 MET   A N   1 
ATOM   2136 C  CA  . MET   A 1 298 ? -22.088 -37.323 -24.229 1.00 86.68  ? 318 MET   A CA  1 
ATOM   2137 C  C   . MET   A 1 298 ? -23.115 -37.058 -25.323 1.00 88.77  ? 318 MET   A C   1 
ATOM   2138 O  O   . MET   A 1 298 ? -23.399 -37.962 -26.115 1.00 87.21  ? 318 MET   A O   1 
ATOM   2139 C  CB  . MET   A 1 298 ? -22.696 -38.164 -23.107 1.00 89.34  ? 318 MET   A CB  1 
ATOM   2140 C  CG  . MET   A 1 298 ? -21.652 -38.818 -22.210 1.00 92.72  ? 318 MET   A CG  1 
ATOM   2141 S  SD  . MET   A 1 298 ? -20.820 -40.197 -23.030 1.00 100.79 ? 318 MET   A SD  1 
ATOM   2142 C  CE  . MET   A 1 298 ? -19.226 -40.184 -22.221 1.00 95.29  ? 318 MET   A CE  1 
ATOM   2143 N  N   . TYR   A 1 299 ? -23.680 -35.850 -25.389 1.00 90.16  ? 319 TYR   A N   1 
ATOM   2144 C  CA  . TYR   A 1 299 ? -24.408 -35.455 -26.590 1.00 91.23  ? 319 TYR   A CA  1 
ATOM   2145 C  C   . TYR   A 1 299 ? -23.469 -35.407 -27.785 1.00 93.23  ? 319 TYR   A C   1 
ATOM   2146 O  O   . TYR   A 1 299 ? -23.734 -36.022 -28.824 1.00 96.00  ? 319 TYR   A O   1 
ATOM   2147 C  CB  . TYR   A 1 299 ? -25.083 -34.094 -26.387 1.00 95.43  ? 319 TYR   A CB  1 
ATOM   2148 C  CG  . TYR   A 1 299 ? -25.585 -33.445 -27.669 1.00 99.17  ? 319 TYR   A CG  1 
ATOM   2149 C  CD1 . TYR   A 1 299 ? -26.858 -33.718 -28.160 1.00 101.06 ? 319 TYR   A CD1 1 
ATOM   2150 C  CD2 . TYR   A 1 299 ? -24.789 -32.551 -28.381 1.00 100.04 ? 319 TYR   A CD2 1 
ATOM   2151 C  CE1 . TYR   A 1 299 ? -27.321 -33.124 -29.329 1.00 104.72 ? 319 TYR   A CE1 1 
ATOM   2152 C  CE2 . TYR   A 1 299 ? -25.240 -31.957 -29.547 1.00 102.44 ? 319 TYR   A CE2 1 
ATOM   2153 C  CZ  . TYR   A 1 299 ? -26.505 -32.245 -30.016 1.00 106.86 ? 319 TYR   A CZ  1 
ATOM   2154 O  OH  . TYR   A 1 299 ? -26.943 -31.646 -31.175 1.00 117.54 ? 319 TYR   A OH  1 
ATOM   2155 N  N   . GLU   A 1 300 ? -22.353 -34.684 -27.645 1.00 93.70  ? 320 GLU   A N   1 
ATOM   2156 C  CA  . GLU   A 1 300 ? -21.414 -34.529 -28.750 1.00 93.62  ? 320 GLU   A CA  1 
ATOM   2157 C  C   . GLU   A 1 300 ? -20.826 -35.869 -29.173 1.00 94.76  ? 320 GLU   A C   1 
ATOM   2158 O  O   . GLU   A 1 300 ? -20.688 -36.144 -30.371 1.00 95.77  ? 320 GLU   A O   1 
ATOM   2159 C  CB  . GLU   A 1 300 ? -20.302 -33.552 -28.360 1.00 84.03  ? 320 GLU   A CB  1 
ATOM   2160 C  CG  . GLU   A 1 300 ? -20.772 -32.121 -28.122 1.00 88.32  ? 320 GLU   A CG  1 
ATOM   2161 C  CD  . GLU   A 1 300 ? -21.392 -31.485 -29.355 1.00 89.13  ? 320 GLU   A CD  1 
ATOM   2162 O  OE1 . GLU   A 1 300 ? -21.125 -31.956 -30.481 1.00 90.23  ? 320 GLU   A OE1 1 
ATOM   2163 O  OE2 . GLU   A 1 300 ? -22.153 -30.508 -29.196 1.00 92.28  ? 320 GLU   A OE2 1 
ATOM   2164 N  N   . LEU   A 1 301 ? -20.472 -36.717 -28.205 1.00 92.25  ? 321 LEU   A N   1 
ATOM   2165 C  CA  . LEU   A 1 301 ? -19.928 -38.025 -28.549 1.00 93.39  ? 321 LEU   A CA  1 
ATOM   2166 C  C   . LEU   A 1 301 ? -20.959 -38.902 -29.249 1.00 101.29 ? 321 LEU   A C   1 
ATOM   2167 O  O   . LEU   A 1 301 ? -20.593 -39.738 -30.083 1.00 102.45 ? 321 LEU   A O   1 
ATOM   2168 C  CB  . LEU   A 1 301 ? -19.400 -38.723 -27.296 1.00 91.84  ? 321 LEU   A CB  1 
ATOM   2169 C  CG  . LEU   A 1 301 ? -18.095 -38.165 -26.726 1.00 93.20  ? 321 LEU   A CG  1 
ATOM   2170 C  CD1 . LEU   A 1 301 ? -17.528 -39.097 -25.667 1.00 97.49  ? 321 LEU   A CD1 1 
ATOM   2171 C  CD2 . LEU   A 1 301 ? -17.083 -37.930 -27.838 1.00 90.05  ? 321 LEU   A CD2 1 
ATOM   2172 N  N   . ALA   A 1 302 ? -22.244 -38.724 -28.937 1.00 101.37 ? 322 ALA   A N   1 
ATOM   2173 C  CA  . ALA   A 1 302 ? -23.276 -39.533 -29.575 1.00 103.35 ? 322 ALA   A CA  1 
ATOM   2174 C  C   . ALA   A 1 302 ? -23.609 -39.039 -30.977 1.00 102.36 ? 322 ALA   A C   1 
ATOM   2175 O  O   . ALA   A 1 302 ? -23.950 -39.849 -31.844 1.00 110.46 ? 322 ALA   A O   1 
ATOM   2176 C  CB  . ALA   A 1 302 ? -24.537 -39.562 -28.712 1.00 104.32 ? 322 ALA   A CB  1 
ATOM   2177 N  N   . THR   A 1 303 ? -23.524 -37.732 -31.221 1.00 116.54 ? 323 THR   A N   1 
ATOM   2178 C  CA  . THR   A 1 303 ? -23.758 -37.189 -32.554 1.00 117.67 ? 323 THR   A CA  1 
ATOM   2179 C  C   . THR   A 1 303 ? -22.498 -37.164 -33.410 1.00 119.15 ? 323 THR   A C   1 
ATOM   2180 O  O   . THR   A 1 303 ? -22.566 -36.749 -34.573 1.00 128.31 ? 323 THR   A O   1 
ATOM   2181 C  CB  . THR   A 1 303 ? -24.349 -35.775 -32.466 1.00 115.22 ? 323 THR   A CB  1 
ATOM   2182 O  OG1 . THR   A 1 303 ? -24.514 -35.244 -33.786 1.00 125.42 ? 323 THR   A OG1 1 
ATOM   2183 C  CG2 . THR   A 1 303 ? -23.436 -34.858 -31.681 1.00 110.98 ? 323 THR   A CG2 1 
ATOM   2184 N  N   . HIS   A 1 304 ? -21.359 -37.593 -32.867 1.00 106.86 ? 324 HIS   A N   1 
ATOM   2185 C  CA  . HIS   A 1 304 ? -20.104 -37.710 -33.610 1.00 107.93 ? 324 HIS   A CA  1 
ATOM   2186 C  C   . HIS   A 1 304 ? -19.480 -39.050 -33.240 1.00 106.46 ? 324 HIS   A C   1 
ATOM   2187 O  O   . HIS   A 1 304 ? -18.503 -39.106 -32.477 1.00 106.56 ? 324 HIS   A O   1 
ATOM   2188 C  CB  . HIS   A 1 304 ? -19.166 -36.538 -33.310 1.00 102.96 ? 324 HIS   A CB  1 
ATOM   2189 C  CG  . HIS   A 1 304 ? -19.692 -35.213 -33.767 1.00 101.22 ? 324 HIS   A CG  1 
ATOM   2190 N  ND1 . HIS   A 1 304 ? -20.525 -34.434 -32.993 1.00 101.48 ? 324 HIS   A ND1 1 
ATOM   2191 C  CD2 . HIS   A 1 304 ? -19.501 -34.529 -34.920 1.00 101.02 ? 324 HIS   A CD2 1 
ATOM   2192 C  CE1 . HIS   A 1 304 ? -20.826 -33.328 -33.650 1.00 102.19 ? 324 HIS   A CE1 1 
ATOM   2193 N  NE2 . HIS   A 1 304 ? -20.218 -33.361 -34.822 1.00 102.94 ? 324 HIS   A NE2 1 
ATOM   2194 N  N   . PRO   A 1 305 ? -20.015 -40.151 -33.776 1.00 103.70 ? 325 PRO   A N   1 
ATOM   2195 C  CA  . PRO   A 1 305 ? -19.574 -41.482 -33.324 1.00 104.45 ? 325 PRO   A CA  1 
ATOM   2196 C  C   . PRO   A 1 305 ? -18.110 -41.760 -33.599 1.00 103.96 ? 325 PRO   A C   1 
ATOM   2197 O  O   . PRO   A 1 305 ? -17.500 -42.579 -32.899 1.00 101.24 ? 325 PRO   A O   1 
ATOM   2198 C  CB  . PRO   A 1 305 ? -20.485 -42.439 -34.106 1.00 107.26 ? 325 PRO   A CB  1 
ATOM   2199 C  CG  . PRO   A 1 305 ? -21.633 -41.582 -34.592 1.00 107.48 ? 325 PRO   A CG  1 
ATOM   2200 C  CD  . PRO   A 1 305 ? -21.030 -40.238 -34.835 1.00 105.80 ? 325 PRO   A CD  1 
ATOM   2201 N  N   . ASP   A 1 306 ? -17.531 -41.112 -34.612 1.00 101.55 ? 326 ASP   A N   1 
ATOM   2202 C  CA  . ASP   A 1 306 ? -16.111 -41.284 -34.898 1.00 101.37 ? 326 ASP   A CA  1 
ATOM   2203 C  C   . ASP   A 1 306 ? -15.255 -40.848 -33.716 1.00 99.93  ? 326 ASP   A C   1 
ATOM   2204 O  O   . ASP   A 1 306 ? -14.281 -41.522 -33.359 1.00 98.86  ? 326 ASP   A O   1 
ATOM   2205 C  CB  . ASP   A 1 306 ? -15.745 -40.486 -36.146 1.00 103.34 ? 326 ASP   A CB  1 
ATOM   2206 C  CG  . ASP   A 1 306 ? -16.348 -39.097 -36.131 1.00 108.28 ? 326 ASP   A CG  1 
ATOM   2207 O  OD1 . ASP   A 1 306 ? -17.567 -38.984 -35.875 1.00 111.88 ? 326 ASP   A OD1 1 
ATOM   2208 O  OD2 . ASP   A 1 306 ? -15.604 -38.118 -36.345 1.00 114.50 ? 326 ASP   A OD2 1 
ATOM   2209 N  N   . VAL   A 1 307 ? -15.605 -39.720 -33.096 1.00 102.40 ? 327 VAL   A N   1 
ATOM   2210 C  CA  . VAL   A 1 307 ? -14.861 -39.234 -31.940 1.00 95.33  ? 327 VAL   A CA  1 
ATOM   2211 C  C   . VAL   A 1 307 ? -15.044 -40.170 -30.753 1.00 93.27  ? 327 VAL   A C   1 
ATOM   2212 O  O   . VAL   A 1 307 ? -14.131 -40.336 -29.934 1.00 90.37  ? 327 VAL   A O   1 
ATOM   2213 C  CB  . VAL   A 1 307 ? -15.302 -37.795 -31.608 1.00 94.64  ? 327 VAL   A CB  1 
ATOM   2214 C  CG1 . VAL   A 1 307 ? -14.440 -37.203 -30.509 1.00 92.27  ? 327 VAL   A CG1 1 
ATOM   2215 C  CG2 . VAL   A 1 307 ? -15.255 -36.928 -32.858 1.00 95.45  ? 327 VAL   A CG2 1 
ATOM   2216 N  N   . GLN   A 1 308 ? -16.213 -40.801 -30.641 1.00 94.00  ? 328 GLN   A N   1 
ATOM   2217 C  CA  . GLN   A 1 308 ? -16.454 -41.729 -29.542 1.00 91.80  ? 328 GLN   A CA  1 
ATOM   2218 C  C   . GLN   A 1 308 ? -15.621 -42.992 -29.706 1.00 91.80  ? 328 GLN   A C   1 
ATOM   2219 O  O   . GLN   A 1 308 ? -14.980 -43.453 -28.754 1.00 95.02  ? 328 GLN   A O   1 
ATOM   2220 C  CB  . GLN   A 1 308 ? -17.942 -42.067 -29.460 1.00 92.61  ? 328 GLN   A CB  1 
ATOM   2221 C  CG  . GLN   A 1 308 ? -18.335 -42.848 -28.219 1.00 91.82  ? 328 GLN   A CG  1 
ATOM   2222 C  CD  . GLN   A 1 308 ? -19.812 -43.179 -28.184 1.00 95.69  ? 328 GLN   A CD  1 
ATOM   2223 O  OE1 . GLN   A 1 308 ? -20.221 -44.173 -27.586 1.00 99.96  ? 328 GLN   A OE1 1 
ATOM   2224 N  NE2 . GLN   A 1 308 ? -20.623 -42.346 -28.825 1.00 95.77  ? 328 GLN   A NE2 1 
ATOM   2225 N  N   . GLN   A 1 309 ? -15.617 -43.565 -30.911 1.00 93.98  ? 329 GLN   A N   1 
ATOM   2226 C  CA  . GLN   A 1 309 ? -14.778 -44.731 -31.160 1.00 91.77  ? 329 GLN   A CA  1 
ATOM   2227 C  C   . GLN   A 1 309 ? -13.304 -44.391 -30.982 1.00 93.74  ? 329 GLN   A C   1 
ATOM   2228 O  O   . GLN   A 1 309 ? -12.539 -45.192 -30.435 1.00 95.64  ? 329 GLN   A O   1 
ATOM   2229 C  CB  . GLN   A 1 309 ? -15.038 -45.285 -32.561 1.00 92.58  ? 329 GLN   A CB  1 
ATOM   2230 C  CG  . GLN   A 1 309 ? -14.258 -46.553 -32.872 1.00 92.20  ? 329 GLN   A CG  1 
ATOM   2231 C  CD  . GLN   A 1 309 ? -14.476 -47.039 -34.291 1.00 95.34  ? 329 GLN   A CD  1 
ATOM   2232 O  OE1 . GLN   A 1 309 ? -15.335 -46.526 -35.009 1.00 97.92  ? 329 GLN   A OE1 1 
ATOM   2233 N  NE2 . GLN   A 1 309 ? -13.694 -48.031 -34.706 1.00 96.90  ? 329 GLN   A NE2 1 
ATOM   2234 N  N   . LYS   A 1 310 ? -12.886 -43.201 -31.426 1.00 93.88  ? 330 LYS   A N   1 
ATOM   2235 C  CA  . LYS   A 1 310 ? -11.488 -42.817 -31.259 1.00 93.58  ? 330 LYS   A CA  1 
ATOM   2236 C  C   . LYS   A 1 310 ? -11.141 -42.645 -29.786 1.00 92.21  ? 330 LYS   A C   1 
ATOM   2237 O  O   . LYS   A 1 310 ? -10.068 -43.069 -29.342 1.00 92.45  ? 330 LYS   A O   1 
ATOM   2238 C  CB  . LYS   A 1 310 ? -11.186 -41.538 -32.039 1.00 88.47  ? 330 LYS   A CB  1 
ATOM   2239 C  CG  . LYS   A 1 310 ? -9.710  -41.159 -32.030 1.00 88.44  ? 330 LYS   A CG  1 
ATOM   2240 C  CD  . LYS   A 1 310 ? -9.400  -40.005 -32.970 1.00 97.66  ? 330 LYS   A CD  1 
ATOM   2241 C  CE  . LYS   A 1 310 ? -7.895  -39.778 -33.061 1.00 95.49  ? 330 LYS   A CE  1 
ATOM   2242 N  NZ  . LYS   A 1 310 ? -7.542  -38.603 -33.905 1.00 93.74  ? 330 LYS   A NZ  1 
ATOM   2243 N  N   . LEU   A 1 311 ? -12.041 -42.038 -29.013 1.00 90.86  ? 331 LEU   A N   1 
ATOM   2244 C  CA  . LEU   A 1 311 ? -11.815 -41.921 -27.577 1.00 89.69  ? 331 LEU   A CA  1 
ATOM   2245 C  C   . LEU   A 1 311 ? -11.803 -43.293 -26.911 1.00 89.37  ? 331 LEU   A C   1 
ATOM   2246 O  O   . LEU   A 1 311 ? -10.939 -43.570 -26.072 1.00 88.28  ? 331 LEU   A O   1 
ATOM   2247 C  CB  . LEU   A 1 311 ? -12.878 -41.014 -26.956 1.00 91.88  ? 331 LEU   A CB  1 
ATOM   2248 C  CG  . LEU   A 1 311 ? -12.732 -40.632 -25.484 1.00 89.84  ? 331 LEU   A CG  1 
ATOM   2249 C  CD1 . LEU   A 1 311 ? -13.008 -39.152 -25.278 1.00 85.81  ? 331 LEU   A CD1 1 
ATOM   2250 C  CD2 . LEU   A 1 311 ? -13.687 -41.450 -24.654 1.00 91.75  ? 331 LEU   A CD2 1 
ATOM   2251 N  N   . GLN   A 1 312 ? -12.739 -44.170 -27.287 1.00 92.64  ? 332 GLN   A N   1 
ATOM   2252 C  CA  . GLN   A 1 312 ? -12.773 -45.509 -26.706 1.00 94.06  ? 332 GLN   A CA  1 
ATOM   2253 C  C   . GLN   A 1 312 ? -11.529 -46.304 -27.078 1.00 89.85  ? 332 GLN   A C   1 
ATOM   2254 O  O   . GLN   A 1 312 ? -11.024 -47.093 -26.271 1.00 90.40  ? 332 GLN   A O   1 
ATOM   2255 C  CB  . GLN   A 1 312 ? -14.038 -46.245 -27.150 1.00 94.82  ? 332 GLN   A CB  1 
ATOM   2256 C  CG  . GLN   A 1 312 ? -15.314 -45.740 -26.491 1.00 91.54  ? 332 GLN   A CG  1 
ATOM   2257 C  CD  . GLN   A 1 312 ? -16.555 -46.455 -26.992 1.00 98.24  ? 332 GLN   A CD  1 
ATOM   2258 O  OE1 . GLN   A 1 312 ? -16.646 -46.821 -28.164 1.00 99.14  ? 332 GLN   A OE1 1 
ATOM   2259 N  NE2 . GLN   A 1 312 ? -17.517 -46.663 -26.101 1.00 101.73 ? 332 GLN   A NE2 1 
ATOM   2260 N  N   . GLU   A 1 313 ? -11.027 -46.118 -28.303 1.00 88.66  ? 333 GLU   A N   1 
ATOM   2261 C  CA  . GLU   A 1 313 ? -9.771  -46.751 -28.695 1.00 86.89  ? 333 GLU   A CA  1 
ATOM   2262 C  C   . GLU   A 1 313 ? -8.625  -46.294 -27.804 1.00 87.82  ? 333 GLU   A C   1 
ATOM   2263 O  O   . GLU   A 1 313 ? -7.784  -47.104 -27.394 1.00 91.55  ? 333 GLU   A O   1 
ATOM   2264 C  CB  . GLU   A 1 313 ? -9.457  -46.438 -30.157 1.00 91.55  ? 333 GLU   A CB  1 
ATOM   2265 C  CG  . GLU   A 1 313 ? -10.293 -47.202 -31.167 1.00 97.06  ? 333 GLU   A CG  1 
ATOM   2266 C  CD  . GLU   A 1 313 ? -10.186 -46.615 -32.562 1.00 98.58  ? 333 GLU   A CD  1 
ATOM   2267 O  OE1 . GLU   A 1 313 ? -9.196  -45.903 -32.835 1.00 100.69 ? 333 GLU   A OE1 1 
ATOM   2268 O  OE2 . GLU   A 1 313 ? -11.096 -46.858 -33.381 1.00 106.08 ? 333 GLU   A OE2 1 
ATOM   2269 N  N   . GLU   A 1 314 ? -8.572  -44.996 -27.498 1.00 89.80  ? 334 GLU   A N   1 
ATOM   2270 C  CA  . GLU   A 1 314 ? -7.512  -44.484 -26.637 1.00 90.57  ? 334 GLU   A CA  1 
ATOM   2271 C  C   . GLU   A 1 314 ? -7.635  -45.032 -25.221 1.00 95.46  ? 334 GLU   A C   1 
ATOM   2272 O  O   . GLU   A 1 314 ? -6.625  -45.376 -24.595 1.00 95.79  ? 334 GLU   A O   1 
ATOM   2273 C  CB  . GLU   A 1 314 ? -7.534  -42.955 -26.623 1.00 92.28  ? 334 GLU   A CB  1 
ATOM   2274 C  CG  . GLU   A 1 314 ? -6.637  -42.347 -25.555 1.00 95.78  ? 334 GLU   A CG  1 
ATOM   2275 C  CD  . GLU   A 1 314 ? -6.666  -40.832 -25.545 1.00 91.85  ? 334 GLU   A CD  1 
ATOM   2276 O  OE1 . GLU   A 1 314 ? -6.104  -40.220 -26.474 1.00 96.56  ? 334 GLU   A OE1 1 
ATOM   2277 O  OE2 . GLU   A 1 314 ? -7.249  -40.255 -24.605 1.00 91.42  ? 334 GLU   A OE2 1 
ATOM   2278 N  N   . ILE   A 1 315 ? -8.862  -45.126 -24.701 1.00 95.26  ? 335 ILE   A N   1 
ATOM   2279 C  CA  . ILE   A 1 315 ? -9.062  -45.620 -23.339 1.00 92.79  ? 335 ILE   A CA  1 
ATOM   2280 C  C   . ILE   A 1 315 ? -8.512  -47.034 -23.199 1.00 96.40  ? 335 ILE   A C   1 
ATOM   2281 O  O   . ILE   A 1 315 ? -7.814  -47.359 -22.231 1.00 101.04 ? 335 ILE   A O   1 
ATOM   2282 C  CB  . ILE   A 1 315 ? -10.550 -45.569 -22.952 1.00 91.76  ? 335 ILE   A CB  1 
ATOM   2283 C  CG1 . ILE   A 1 315 ? -11.101 -44.148 -23.047 1.00 89.88  ? 335 ILE   A CG1 1 
ATOM   2284 C  CG2 . ILE   A 1 315 ? -10.732 -46.089 -21.546 1.00 97.55  ? 335 ILE   A CG2 1 
ATOM   2285 C  CD1 . ILE   A 1 315 ? -12.516 -44.024 -22.538 1.00 90.54  ? 335 ILE   A CD1 1 
ATOM   2286 N  N   . ASP   A 1 316 ? -8.828  -47.899 -24.162 1.00 97.31  ? 336 ASP   A N   1 
ATOM   2287 C  CA  . ASP   A 1 316 ? -8.406  -49.292 -24.102 1.00 99.31  ? 336 ASP   A CA  1 
ATOM   2288 C  C   . ASP   A 1 316 ? -6.931  -49.483 -24.433 1.00 101.76 ? 336 ASP   A C   1 
ATOM   2289 O  O   . ASP   A 1 316 ? -6.391  -50.564 -24.173 1.00 96.23  ? 336 ASP   A O   1 
ATOM   2290 C  CB  . ASP   A 1 316 ? -9.275  -50.130 -25.042 1.00 94.15  ? 336 ASP   A CB  1 
ATOM   2291 C  CG  . ASP   A 1 316 ? -10.757 -50.002 -24.730 1.00 99.13  ? 336 ASP   A CG  1 
ATOM   2292 O  OD1 . ASP   A 1 316 ? -11.098 -49.404 -23.684 1.00 100.90 ? 336 ASP   A OD1 1 
ATOM   2293 O  OD2 . ASP   A 1 316 ? -11.581 -50.492 -25.530 1.00 100.79 ? 336 ASP   A OD2 1 
ATOM   2294 N  N   . ALA   A 1 317 ? -6.268  -48.469 -24.996 1.00 96.23  ? 337 ALA   A N   1 
ATOM   2295 C  CA  . ALA   A 1 317 ? -4.822  -48.539 -25.174 1.00 93.38  ? 337 ALA   A CA  1 
ATOM   2296 C  C   . ALA   A 1 317 ? -4.081  -48.112 -23.915 1.00 98.17  ? 337 ALA   A C   1 
ATOM   2297 O  O   . ALA   A 1 317 ? -2.942  -48.540 -23.695 1.00 99.49  ? 337 ALA   A O   1 
ATOM   2298 C  CB  . ALA   A 1 317 ? -4.389  -47.672 -26.357 1.00 92.94  ? 337 ALA   A CB  1 
ATOM   2299 N  N   . VAL   A 1 318 ? -4.704  -47.276 -23.088 1.00 93.98  ? 338 VAL   A N   1 
ATOM   2300 C  CA  . VAL   A 1 318 ? -4.108  -46.858 -21.823 1.00 101.06 ? 338 VAL   A CA  1 
ATOM   2301 C  C   . VAL   A 1 318 ? -4.543  -47.768 -20.682 1.00 101.09 ? 338 VAL   A C   1 
ATOM   2302 O  O   . VAL   A 1 318 ? -3.743  -48.094 -19.802 1.00 102.43 ? 338 VAL   A O   1 
ATOM   2303 C  CB  . VAL   A 1 318 ? -4.466  -45.385 -21.532 1.00 103.56 ? 338 VAL   A CB  1 
ATOM   2304 C  CG1 . VAL   A 1 318 ? -3.716  -44.884 -20.304 1.00 103.31 ? 338 VAL   A CG1 1 
ATOM   2305 C  CG2 . VAL   A 1 318 ? -4.174  -44.508 -22.745 1.00 101.90 ? 338 VAL   A CG2 1 
ATOM   2306 N  N   . LEU   A 1 319 ? -5.810  -48.190 -20.683 1.00 100.64 ? 339 LEU   A N   1 
ATOM   2307 C  CA  . LEU   A 1 319 ? -6.389  -49.022 -19.629 1.00 104.89 ? 339 LEU   A CA  1 
ATOM   2308 C  C   . LEU   A 1 319 ? -6.968  -50.282 -20.261 1.00 107.71 ? 339 LEU   A C   1 
ATOM   2309 O  O   . LEU   A 1 319 ? -8.186  -50.381 -20.473 1.00 109.46 ? 339 LEU   A O   1 
ATOM   2310 C  CB  . LEU   A 1 319 ? -7.450  -48.252 -18.845 1.00 107.50 ? 339 LEU   A CB  1 
ATOM   2311 C  CG  . LEU   A 1 319 ? -6.911  -47.116 -17.976 1.00 106.52 ? 339 LEU   A CG  1 
ATOM   2312 C  CD1 . LEU   A 1 319 ? -7.956  -46.043 -17.768 1.00 103.66 ? 339 LEU   A CD1 1 
ATOM   2313 C  CD2 . LEU   A 1 319 ? -6.452  -47.667 -16.643 1.00 108.83 ? 339 LEU   A CD2 1 
ATOM   2314 N  N   . PRO   A 1 320 ? -6.127  -51.265 -20.570 1.00 117.77 ? 340 PRO   A N   1 
ATOM   2315 C  CA  . PRO   A 1 320 ? -6.613  -52.494 -21.203 1.00 120.61 ? 340 PRO   A CA  1 
ATOM   2316 C  C   . PRO   A 1 320 ? -7.254  -53.438 -20.195 1.00 132.81 ? 340 PRO   A C   1 
ATOM   2317 O  O   . PRO   A 1 320 ? -7.064  -53.327 -18.983 1.00 136.23 ? 340 PRO   A O   1 
ATOM   2318 C  CB  . PRO   A 1 320 ? -5.341  -53.105 -21.798 1.00 116.21 ? 340 PRO   A CB  1 
ATOM   2319 C  CG  . PRO   A 1 320 ? -4.255  -52.629 -20.892 1.00 112.50 ? 340 PRO   A CG  1 
ATOM   2320 C  CD  . PRO   A 1 320 ? -4.662  -51.259 -20.415 1.00 114.51 ? 340 PRO   A CD  1 
ATOM   2321 N  N   . ASN   A 1 321 ? -8.019  -54.394 -20.733 1.00 156.17 ? 341 ASN   A N   1 
ATOM   2322 C  CA  . ASN   A 1 321 ? -8.835  -55.310 -19.933 1.00 156.30 ? 341 ASN   A CA  1 
ATOM   2323 C  C   . ASN   A 1 321 ? -9.783  -54.550 -19.010 1.00 152.68 ? 341 ASN   A C   1 
ATOM   2324 O  O   . ASN   A 1 321 ? -10.097 -55.010 -17.908 1.00 154.09 ? 341 ASN   A O   1 
ATOM   2325 C  CB  . ASN   A 1 321 ? -7.966  -56.282 -19.125 1.00 157.80 ? 341 ASN   A CB  1 
ATOM   2326 C  CG  . ASN   A 1 321 ? -7.146  -57.206 -20.008 1.00 162.34 ? 341 ASN   A CG  1 
ATOM   2327 O  OD1 . ASN   A 1 321 ? -7.592  -57.616 -21.080 1.00 163.84 ? 341 ASN   A OD1 1 
ATOM   2328 N  ND2 . ASN   A 1 321 ? -5.942  -57.539 -19.558 1.00 170.97 ? 341 ASN   A ND2 1 
ATOM   2329 N  N   . LYS   A 1 322 ? -10.250 -53.385 -19.465 1.00 132.98 ? 342 LYS   A N   1 
ATOM   2330 C  CA  . LYS   A 1 322 ? -11.057 -52.473 -18.653 1.00 126.76 ? 342 LYS   A CA  1 
ATOM   2331 C  C   . LYS   A 1 322 ? -10.375 -52.170 -17.320 1.00 123.36 ? 342 LYS   A C   1 
ATOM   2332 O  O   . LYS   A 1 322 ? -11.007 -52.169 -16.260 1.00 120.36 ? 342 LYS   A O   1 
ATOM   2333 C  CB  . LYS   A 1 322 ? -12.469 -53.021 -18.438 1.00 123.95 ? 342 LYS   A CB  1 
ATOM   2334 C  CG  . LYS   A 1 322 ? -13.325 -53.049 -19.699 1.00 121.64 ? 342 LYS   A CG  1 
ATOM   2335 C  CD  . LYS   A 1 322 ? -14.756 -53.478 -19.397 1.00 122.02 ? 342 LYS   A CD  1 
ATOM   2336 C  CE  . LYS   A 1 322 ? -15.551 -53.722 -20.672 1.00 119.47 ? 342 LYS   A CE  1 
ATOM   2337 N  NZ  . LYS   A 1 322 ? -16.947 -54.156 -20.381 1.00 116.11 ? 342 LYS   A NZ  1 
ATOM   2338 N  N   . ALA   A 1 323 ? -9.069  -51.910 -17.382 1.00 115.95 ? 343 ALA   A N   1 
ATOM   2339 C  CA  . ALA   A 1 323 ? -8.313  -51.570 -16.189 1.00 113.05 ? 343 ALA   A CA  1 
ATOM   2340 C  C   . ALA   A 1 323 ? -8.895  -50.316 -15.539 1.00 109.56 ? 343 ALA   A C   1 
ATOM   2341 O  O   . ALA   A 1 323 ? -9.442  -49.448 -16.226 1.00 110.84 ? 343 ALA   A O   1 
ATOM   2342 C  CB  . ALA   A 1 323 ? -6.838  -51.338 -16.541 1.00 109.11 ? 343 ALA   A CB  1 
ATOM   2343 N  N   . PRO   A 1 324 ? -8.802  -50.202 -14.217 1.00 112.28 ? 344 PRO   A N   1 
ATOM   2344 C  CA  . PRO   A 1 324 ? -9.396  -49.058 -13.533 1.00 107.91 ? 344 PRO   A CA  1 
ATOM   2345 C  C   . PRO   A 1 324 ? -8.540  -47.819 -13.706 1.00 108.12 ? 344 PRO   A C   1 
ATOM   2346 O  O   . PRO   A 1 324 ? -7.307  -47.884 -13.591 1.00 111.18 ? 344 PRO   A O   1 
ATOM   2347 C  CB  . PRO   A 1 324 ? -9.442  -49.507 -12.064 1.00 108.78 ? 344 PRO   A CB  1 
ATOM   2348 C  CG  . PRO   A 1 324 ? -8.394  -50.578 -11.943 1.00 109.79 ? 344 PRO   A CG  1 
ATOM   2349 C  CD  . PRO   A 1 324 ? -7.964  -51.014 -13.314 1.00 111.10 ? 344 PRO   A CD  1 
ATOM   2350 N  N   . PRO   A 1 325 ? -9.156  -46.677 -13.990 1.00 117.65 ? 345 PRO   A N   1 
ATOM   2351 C  CA  . PRO   A 1 325 ? -8.376  -45.450 -14.166 1.00 116.54 ? 345 PRO   A CA  1 
ATOM   2352 C  C   . PRO   A 1 325 ? -7.682  -45.069 -12.870 1.00 122.53 ? 345 PRO   A C   1 
ATOM   2353 O  O   . PRO   A 1 325 ? -8.259  -45.157 -11.784 1.00 121.84 ? 345 PRO   A O   1 
ATOM   2354 C  CB  . PRO   A 1 325 ? -9.426  -44.406 -14.571 1.00 110.26 ? 345 PRO   A CB  1 
ATOM   2355 C  CG  . PRO   A 1 325 ? -10.677 -45.171 -14.867 1.00 108.21 ? 345 PRO   A CG  1 
ATOM   2356 C  CD  . PRO   A 1 325 ? -10.604 -46.436 -14.086 1.00 116.41 ? 345 PRO   A CD  1 
ATOM   2357 N  N   . THR   A 1 326 ? -6.421  -44.672 -12.987 1.00 133.61 ? 346 THR   A N   1 
ATOM   2358 C  CA  . THR   A 1 326 ? -5.677  -44.121 -11.868 1.00 136.66 ? 346 THR   A CA  1 
ATOM   2359 C  C   . THR   A 1 326 ? -5.328  -42.673 -12.181 1.00 135.69 ? 346 THR   A C   1 
ATOM   2360 O  O   . THR   A 1 326 ? -5.538  -42.191 -13.297 1.00 132.59 ? 346 THR   A O   1 
ATOM   2361 C  CB  . THR   A 1 326 ? -4.409  -44.935 -11.576 1.00 136.63 ? 346 THR   A CB  1 
ATOM   2362 O  OG1 . THR   A 1 326 ? -3.926  -44.609 -10.267 1.00 139.11 ? 346 THR   A OG1 1 
ATOM   2363 C  CG2 . THR   A 1 326 ? -3.323  -44.623 -12.589 1.00 136.96 ? 346 THR   A CG2 1 
ATOM   2364 N  N   . TYR   A 1 327 ? -4.801  -41.975 -11.173 1.00 134.98 ? 347 TYR   A N   1 
ATOM   2365 C  CA  . TYR   A 1 327 ? -4.463  -40.566 -11.353 1.00 128.48 ? 347 TYR   A CA  1 
ATOM   2366 C  C   . TYR   A 1 327 ? -3.490  -40.374 -12.508 1.00 127.35 ? 347 TYR   A C   1 
ATOM   2367 O  O   . TYR   A 1 327 ? -3.625  -39.430 -13.294 1.00 124.81 ? 347 TYR   A O   1 
ATOM   2368 C  CB  . TYR   A 1 327 ? -3.872  -39.994 -10.066 1.00 127.60 ? 347 TYR   A CB  1 
ATOM   2369 C  CG  . TYR   A 1 327 ? -3.589  -38.510 -10.137 1.00 121.72 ? 347 TYR   A CG  1 
ATOM   2370 C  CD1 . TYR   A 1 327 ? -2.368  -38.035 -10.600 1.00 121.54 ? 347 TYR   A CD1 1 
ATOM   2371 C  CD2 . TYR   A 1 327 ? -4.545  -37.584 -9.744  1.00 121.73 ? 347 TYR   A CD2 1 
ATOM   2372 C  CE1 . TYR   A 1 327 ? -2.110  -36.681 -10.669 1.00 120.45 ? 347 TYR   A CE1 1 
ATOM   2373 C  CE2 . TYR   A 1 327 ? -4.294  -36.228 -9.806  1.00 123.10 ? 347 TYR   A CE2 1 
ATOM   2374 C  CZ  . TYR   A 1 327 ? -3.076  -35.782 -10.270 1.00 123.01 ? 347 TYR   A CZ  1 
ATOM   2375 O  OH  . TYR   A 1 327 ? -2.822  -34.433 -10.336 1.00 126.29 ? 347 TYR   A OH  1 
ATOM   2376 N  N   . ASP   A 1 328 ? -2.501  -41.257 -12.629 1.00 122.86 ? 348 ASP   A N   1 
ATOM   2377 C  CA  . ASP   A 1 328 ? -1.483  -41.075 -13.654 1.00 122.25 ? 348 ASP   A CA  1 
ATOM   2378 C  C   . ASP   A 1 328 ? -1.956  -41.525 -15.030 1.00 116.34 ? 348 ASP   A C   1 
ATOM   2379 O  O   . ASP   A 1 328 ? -1.466  -41.013 -16.042 1.00 110.18 ? 348 ASP   A O   1 
ATOM   2380 C  CB  . ASP   A 1 328 ? -0.206  -41.813 -13.250 1.00 131.36 ? 348 ASP   A CB  1 
ATOM   2381 C  CG  . ASP   A 1 328 ? 0.534   -41.116 -12.123 1.00 132.62 ? 348 ASP   A CG  1 
ATOM   2382 O  OD1 . ASP   A 1 328 ? 0.905   -39.935 -12.299 1.00 132.69 ? 348 ASP   A OD1 1 
ATOM   2383 O  OD2 . ASP   A 1 328 ? 0.729   -41.739 -11.057 1.00 136.24 ? 348 ASP   A OD2 1 
ATOM   2384 N  N   . THR   A 1 329 ? -2.903  -42.462 -15.100 1.00 124.20 ? 349 THR   A N   1 
ATOM   2385 C  CA  . THR   A 1 329 ? -3.406  -42.882 -16.403 1.00 118.67 ? 349 THR   A CA  1 
ATOM   2386 C  C   . THR   A 1 329 ? -4.362  -41.865 -17.012 1.00 113.66 ? 349 THR   A C   1 
ATOM   2387 O  O   . THR   A 1 329 ? -4.406  -41.731 -18.238 1.00 111.82 ? 349 THR   A O   1 
ATOM   2388 C  CB  . THR   A 1 329 ? -4.109  -44.239 -16.306 1.00 118.76 ? 349 THR   A CB  1 
ATOM   2389 O  OG1 . THR   A 1 329 ? -5.037  -44.228 -15.215 1.00 122.51 ? 349 THR   A OG1 1 
ATOM   2390 C  CG2 . THR   A 1 329 ? -3.098  -45.360 -16.115 1.00 118.22 ? 349 THR   A CG2 1 
ATOM   2391 N  N   . VAL   A 1 330 ? -5.130  -41.146 -16.192 1.00 108.67 ? 350 VAL   A N   1 
ATOM   2392 C  CA  . VAL   A 1 330 ? -6.114  -40.219 -16.742 1.00 107.42 ? 350 VAL   A CA  1 
ATOM   2393 C  C   . VAL   A 1 330 ? -5.438  -38.966 -17.293 1.00 106.66 ? 350 VAL   A C   1 
ATOM   2394 O  O   . VAL   A 1 330 ? -5.832  -38.450 -18.345 1.00 106.85 ? 350 VAL   A O   1 
ATOM   2395 C  CB  . VAL   A 1 330 ? -7.188  -39.881 -15.689 1.00 105.56 ? 350 VAL   A CB  1 
ATOM   2396 C  CG1 . VAL   A 1 330 ? -6.555  -39.434 -14.391 1.00 110.63 ? 350 VAL   A CG1 1 
ATOM   2397 C  CG2 . VAL   A 1 330 ? -8.133  -38.811 -16.215 1.00 99.06  ? 350 VAL   A CG2 1 
ATOM   2398 N  N   . LEU   A 1 331 ? -4.409  -38.458 -16.608 1.00 108.80 ? 351 LEU   A N   1 
ATOM   2399 C  CA  . LEU   A 1 331 ? -3.612  -37.379 -17.182 1.00 107.95 ? 351 LEU   A CA  1 
ATOM   2400 C  C   . LEU   A 1 331 ? -2.831  -37.843 -18.403 1.00 109.17 ? 351 LEU   A C   1 
ATOM   2401 O  O   . LEU   A 1 331 ? -2.363  -37.007 -19.183 1.00 108.93 ? 351 LEU   A O   1 
ATOM   2402 C  CB  . LEU   A 1 331 ? -2.644  -36.807 -16.141 1.00 105.76 ? 351 LEU   A CB  1 
ATOM   2403 C  CG  . LEU   A 1 331 ? -3.161  -35.773 -15.137 1.00 106.00 ? 351 LEU   A CG  1 
ATOM   2404 C  CD1 . LEU   A 1 331 ? -4.017  -36.418 -14.061 1.00 108.49 ? 351 LEU   A CD1 1 
ATOM   2405 C  CD2 . LEU   A 1 331 ? -2.002  -35.012 -14.512 1.00 110.20 ? 351 LEU   A CD2 1 
ATOM   2406 N  N   . GLN   A 1 332 ? -2.688  -39.155 -18.582 1.00 107.65 ? 352 GLN   A N   1 
ATOM   2407 C  CA  . GLN   A 1 332 ? -1.968  -39.738 -19.703 1.00 105.60 ? 352 GLN   A CA  1 
ATOM   2408 C  C   . GLN   A 1 332 ? -2.787  -39.763 -20.989 1.00 106.31 ? 352 GLN   A C   1 
ATOM   2409 O  O   . GLN   A 1 332 ? -2.244  -40.126 -22.039 1.00 104.37 ? 352 GLN   A O   1 
ATOM   2410 C  CB  . GLN   A 1 332 ? -1.539  -41.164 -19.336 1.00 109.50 ? 352 GLN   A CB  1 
ATOM   2411 C  CG  . GLN   A 1 332 ? -0.273  -41.663 -20.006 1.00 116.93 ? 352 GLN   A CG  1 
ATOM   2412 C  CD  . GLN   A 1 332 ? -0.127  -43.172 -19.907 1.00 120.36 ? 352 GLN   A CD  1 
ATOM   2413 O  OE1 . GLN   A 1 332 ? -0.586  -43.909 -20.782 1.00 117.29 ? 352 GLN   A OE1 1 
ATOM   2414 N  NE2 . GLN   A 1 332 ? 0.510   -43.640 -18.838 1.00 115.84 ? 352 GLN   A NE2 1 
ATOM   2415 N  N   . MET   A 1 333 ? -4.064  -39.376 -20.938 1.00 100.59 ? 353 MET   A N   1 
ATOM   2416 C  CA  . MET   A 1 333 ? -5.003  -39.548 -22.047 1.00 100.83 ? 353 MET   A CA  1 
ATOM   2417 C  C   . MET   A 1 333 ? -5.303  -38.193 -22.683 1.00 101.06 ? 353 MET   A C   1 
ATOM   2418 O  O   . MET   A 1 333 ? -5.977  -37.350 -22.079 1.00 97.42  ? 353 MET   A O   1 
ATOM   2419 C  CB  . MET   A 1 333 ? -6.281  -40.223 -21.558 1.00 97.60  ? 353 MET   A CB  1 
ATOM   2420 C  CG  . MET   A 1 333 ? -6.037  -41.542 -20.850 1.00 99.49  ? 353 MET   A CG  1 
ATOM   2421 S  SD  . MET   A 1 333 ? -7.576  -42.371 -20.432 1.00 98.86  ? 353 MET   A SD  1 
ATOM   2422 C  CE  . MET   A 1 333 ? -8.350  -42.344 -22.038 1.00 90.20  ? 353 MET   A CE  1 
ATOM   2423 N  N   . GLU   A 1 334 ? -4.841  -38.008 -23.922 1.00 91.96  ? 354 GLU   A N   1 
ATOM   2424 C  CA  . GLU   A 1 334 ? -4.823  -36.710 -24.591 1.00 90.97  ? 354 GLU   A CA  1 
ATOM   2425 C  C   . GLU   A 1 334 ? -6.101  -36.419 -25.378 1.00 89.05  ? 354 GLU   A C   1 
ATOM   2426 O  O   . GLU   A 1 334 ? -6.635  -35.309 -25.296 1.00 81.39  ? 354 GLU   A O   1 
ATOM   2427 C  CB  . GLU   A 1 334 ? -3.601  -36.613 -25.513 1.00 92.44  ? 354 GLU   A CB  1 
ATOM   2428 C  CG  . GLU   A 1 334 ? -3.384  -37.812 -26.433 1.00 101.52 ? 354 GLU   A CG  1 
ATOM   2429 C  CD  . GLU   A 1 334 ? -2.771  -39.011 -25.721 1.00 107.52 ? 354 GLU   A CD  1 
ATOM   2430 O  OE1 . GLU   A 1 334 ? -2.520  -38.912 -24.501 1.00 107.15 ? 354 GLU   A OE1 1 
ATOM   2431 O  OE2 . GLU   A 1 334 ? -2.546  -40.050 -26.381 1.00 109.99 ? 354 GLU   A OE2 1 
ATOM   2432 N  N   . TYR   A 1 335 ? -6.590  -37.385 -26.164 1.00 92.50  ? 355 TYR   A N   1 
ATOM   2433 C  CA  . TYR   A 1 335 ? -7.859  -37.178 -26.862 1.00 85.60  ? 355 TYR   A CA  1 
ATOM   2434 C  C   . TYR   A 1 335 ? -8.992  -36.981 -25.863 1.00 83.29  ? 355 TYR   A C   1 
ATOM   2435 O  O   . TYR   A 1 335 ? -10.004 -36.341 -26.174 1.00 84.61  ? 355 TYR   A O   1 
ATOM   2436 C  CB  . TYR   A 1 335 ? -8.147  -38.349 -27.800 1.00 87.01  ? 355 TYR   A CB  1 
ATOM   2437 C  CG  . TYR   A 1 335 ? -9.100  -38.043 -28.936 1.00 87.94  ? 355 TYR   A CG  1 
ATOM   2438 C  CD1 . TYR   A 1 335 ? -8.751  -37.146 -29.940 1.00 85.45  ? 355 TYR   A CD1 1 
ATOM   2439 C  CD2 . TYR   A 1 335 ? -10.332 -38.685 -29.028 1.00 86.88  ? 355 TYR   A CD2 1 
ATOM   2440 C  CE1 . TYR   A 1 335 ? -9.612  -36.876 -30.988 1.00 88.68  ? 355 TYR   A CE1 1 
ATOM   2441 C  CE2 . TYR   A 1 335 ? -11.198 -38.424 -30.076 1.00 87.58  ? 355 TYR   A CE2 1 
ATOM   2442 C  CZ  . TYR   A 1 335 ? -10.833 -37.516 -31.053 1.00 89.90  ? 355 TYR   A CZ  1 
ATOM   2443 O  OH  . TYR   A 1 335 ? -11.677 -37.238 -32.105 1.00 84.88  ? 355 TYR   A OH  1 
ATOM   2444 N  N   . LEU   A 1 336 ? -8.833  -37.520 -24.653 1.00 83.62  ? 356 LEU   A N   1 
ATOM   2445 C  CA  . LEU   A 1 336 ? -9.780  -37.241 -23.579 1.00 90.69  ? 356 LEU   A CA  1 
ATOM   2446 C  C   . LEU   A 1 336 ? -9.754  -35.764 -23.197 1.00 81.11  ? 356 LEU   A C   1 
ATOM   2447 O  O   . LEU   A 1 336 ? -10.800 -35.167 -22.909 1.00 79.51  ? 356 LEU   A O   1 
ATOM   2448 C  CB  . LEU   A 1 336 ? -9.464  -38.129 -22.375 1.00 88.00  ? 356 LEU   A CB  1 
ATOM   2449 C  CG  . LEU   A 1 336 ? -10.319 -37.983 -21.114 1.00 82.25  ? 356 LEU   A CG  1 
ATOM   2450 C  CD1 . LEU   A 1 336 ? -11.787 -38.235 -21.414 1.00 83.77  ? 356 LEU   A CD1 1 
ATOM   2451 C  CD2 . LEU   A 1 336 ? -9.816  -38.925 -20.032 1.00 86.36  ? 356 LEU   A CD2 1 
ATOM   2452 N  N   . ASP   A 1 337 ? -8.569  -35.151 -23.209 1.00 82.33  ? 357 ASP   A N   1 
ATOM   2453 C  CA  . ASP   A 1 337 ? -8.471  -33.725 -22.911 1.00 81.09  ? 357 ASP   A CA  1 
ATOM   2454 C  C   . ASP   A 1 337 ? -9.005  -32.884 -24.066 1.00 80.52  ? 357 ASP   A C   1 
ATOM   2455 O  O   . ASP   A 1 337 ? -9.700  -31.885 -23.844 1.00 78.12  ? 357 ASP   A O   1 
ATOM   2456 C  CB  . ASP   A 1 337 ? -7.018  -33.358 -22.594 1.00 81.47  ? 357 ASP   A CB  1 
ATOM   2457 C  CG  . ASP   A 1 337 ? -6.885  -31.997 -21.932 1.00 82.00  ? 357 ASP   A CG  1 
ATOM   2458 O  OD1 . ASP   A 1 337 ? -7.575  -31.756 -20.918 1.00 78.10  ? 357 ASP   A OD1 1 
ATOM   2459 O  OD2 . ASP   A 1 337 ? -6.078  -31.174 -22.417 1.00 83.79  ? 357 ASP   A OD2 1 
ATOM   2460 N  N   . MET   A 1 338 ? -8.696  -33.277 -25.305 1.00 81.71  ? 358 MET   A N   1 
ATOM   2461 C  CA  . MET   A 1 338 ? -9.204  -32.553 -26.467 1.00 75.23  ? 358 MET   A CA  1 
ATOM   2462 C  C   . MET   A 1 338 ? -10.725 -32.597 -26.521 1.00 81.98  ? 358 MET   A C   1 
ATOM   2463 O  O   . MET   A 1 338 ? -11.375 -31.583 -26.807 1.00 76.59  ? 358 MET   A O   1 
ATOM   2464 C  CB  . MET   A 1 338 ? -8.608  -33.138 -27.748 1.00 78.18  ? 358 MET   A CB  1 
ATOM   2465 C  CG  . MET   A 1 338 ? -7.085  -33.129 -27.797 1.00 80.90  ? 358 MET   A CG  1 
ATOM   2466 S  SD  . MET   A 1 338 ? -6.417  -34.192 -29.092 1.00 74.47  ? 358 MET   A SD  1 
ATOM   2467 C  CE  . MET   A 1 338 ? -7.528  -33.813 -30.445 1.00 83.49  ? 358 MET   A CE  1 
ATOM   2468 N  N   . VAL   A 1 339 ? -11.311 -33.765 -26.253 1.00 79.93  ? 359 VAL   A N   1 
ATOM   2469 C  CA  . VAL   A 1 339 ? -12.767 -33.879 -26.236 1.00 74.81  ? 359 VAL   A CA  1 
ATOM   2470 C  C   . VAL   A 1 339 ? -13.347 -33.042 -25.104 1.00 75.27  ? 359 VAL   A C   1 
ATOM   2471 O  O   . VAL   A 1 339 ? -14.326 -32.309 -25.290 1.00 80.57  ? 359 VAL   A O   1 
ATOM   2472 C  CB  . VAL   A 1 339 ? -13.190 -35.355 -26.128 1.00 84.05  ? 359 VAL   A CB  1 
ATOM   2473 C  CG1 . VAL   A 1 339 ? -14.666 -35.468 -25.765 1.00 78.58  ? 359 VAL   A CG1 1 
ATOM   2474 C  CG2 . VAL   A 1 339 ? -12.918 -36.065 -27.440 1.00 80.47  ? 359 VAL   A CG2 1 
ATOM   2475 N  N   . VAL   A 1 340 ? -12.744 -33.129 -23.916 1.00 77.47  ? 360 VAL   A N   1 
ATOM   2476 C  CA  . VAL   A 1 340 ? -13.202 -32.318 -22.789 1.00 79.05  ? 360 VAL   A CA  1 
ATOM   2477 C  C   . VAL   A 1 340 ? -13.092 -30.836 -23.121 1.00 74.07  ? 360 VAL   A C   1 
ATOM   2478 O  O   . VAL   A 1 340 ? -14.069 -30.086 -23.010 1.00 71.70  ? 360 VAL   A O   1 
ATOM   2479 C  CB  . VAL   A 1 340 ? -12.412 -32.671 -21.515 1.00 81.80  ? 360 VAL   A CB  1 
ATOM   2480 C  CG1 . VAL   A 1 340 ? -12.482 -31.528 -20.514 1.00 78.69  ? 360 VAL   A CG1 1 
ATOM   2481 C  CG2 . VAL   A 1 340 ? -12.957 -33.947 -20.896 1.00 75.54  ? 360 VAL   A CG2 1 
ATOM   2482 N  N   . ASN   A 1 341 ? -11.903 -30.400 -23.551 1.00 79.38  ? 361 ASN   A N   1 
ATOM   2483 C  CA  . ASN   A 1 341 ? -11.678 -28.986 -23.836 1.00 76.36  ? 361 ASN   A CA  1 
ATOM   2484 C  C   . ASN   A 1 341 ? -12.645 -28.460 -24.888 1.00 76.06  ? 361 ASN   A C   1 
ATOM   2485 O  O   . ASN   A 1 341 ? -13.188 -27.359 -24.741 1.00 71.56  ? 361 ASN   A O   1 
ATOM   2486 C  CB  . ASN   A 1 341 ? -10.240 -28.767 -24.300 1.00 74.24  ? 361 ASN   A CB  1 
ATOM   2487 C  CG  . ASN   A 1 341 ? -9.237  -28.902 -23.176 1.00 76.00  ? 361 ASN   A CG  1 
ATOM   2488 O  OD1 . ASN   A 1 341 ? -9.589  -29.259 -22.052 1.00 82.52  ? 361 ASN   A OD1 1 
ATOM   2489 N  ND2 . ASN   A 1 341 ? -7.976  -28.626 -23.476 1.00 83.46  ? 361 ASN   A ND2 1 
ATOM   2490 N  N   . GLU   A 1 342 ? -12.869 -29.227 -25.957 1.00 77.31  ? 362 GLU   A N   1 
ATOM   2491 C  CA  . GLU   A 1 342 ? -13.692 -28.727 -27.052 1.00 73.15  ? 362 GLU   A CA  1 
ATOM   2492 C  C   . GLU   A 1 342 ? -15.145 -28.561 -26.626 1.00 75.64  ? 362 GLU   A C   1 
ATOM   2493 O  O   . GLU   A 1 342 ? -15.798 -27.582 -27.006 1.00 79.49  ? 362 GLU   A O   1 
ATOM   2494 C  CB  . GLU   A 1 342 ? -13.582 -29.654 -28.264 1.00 80.59  ? 362 GLU   A CB  1 
ATOM   2495 C  CG  . GLU   A 1 342 ? -14.611 -29.398 -29.368 1.00 79.35  ? 362 GLU   A CG  1 
ATOM   2496 C  CD  . GLU   A 1 342 ? -14.309 -28.172 -30.221 1.00 79.04  ? 362 GLU   A CD  1 
ATOM   2497 O  OE1 . GLU   A 1 342 ? -13.617 -27.249 -29.740 1.00 75.24  ? 362 GLU   A OE1 1 
ATOM   2498 O  OE2 . GLU   A 1 342 ? -14.769 -28.137 -31.384 1.00 77.13  ? 362 GLU   A OE2 1 
ATOM   2499 N  N   . THR   A 1 343 ? -15.672 -29.502 -25.838 1.00 70.69  ? 363 THR   A N   1 
ATOM   2500 C  CA  . THR   A 1 343 ? -17.021 -29.328 -25.310 1.00 77.31  ? 363 THR   A CA  1 
ATOM   2501 C  C   . THR   A 1 343 ? -17.127 -28.035 -24.513 1.00 77.80  ? 363 THR   A C   1 
ATOM   2502 O  O   . THR   A 1 343 ? -18.089 -27.274 -24.671 1.00 72.34  ? 363 THR   A O   1 
ATOM   2503 C  CB  . THR   A 1 343 ? -17.413 -30.520 -24.437 1.00 80.39  ? 363 THR   A CB  1 
ATOM   2504 O  OG1 . THR   A 1 343 ? -17.316 -31.731 -25.195 1.00 81.64  ? 363 THR   A OG1 1 
ATOM   2505 C  CG2 . THR   A 1 343 ? -18.836 -30.351 -23.935 1.00 79.32  ? 363 THR   A CG2 1 
ATOM   2506 N  N   . LEU   A 1 344 ? -16.129 -27.761 -23.671 1.00 78.66  ? 364 LEU   A N   1 
ATOM   2507 C  CA  . LEU   A 1 344 ? -16.127 -26.530 -22.892 1.00 74.75  ? 364 LEU   A CA  1 
ATOM   2508 C  C   . LEU   A 1 344 ? -16.035 -25.295 -23.779 1.00 70.24  ? 364 LEU   A C   1 
ATOM   2509 O  O   . LEU   A 1 344 ? -16.495 -24.217 -23.385 1.00 68.43  ? 364 LEU   A O   1 
ATOM   2510 C  CB  . LEU   A 1 344 ? -14.980 -26.561 -21.884 1.00 70.27  ? 364 LEU   A CB  1 
ATOM   2511 C  CG  . LEU   A 1 344 ? -15.229 -27.510 -20.713 1.00 72.89  ? 364 LEU   A CG  1 
ATOM   2512 C  CD1 . LEU   A 1 344 ? -14.010 -27.594 -19.819 1.00 71.70  ? 364 LEU   A CD1 1 
ATOM   2513 C  CD2 . LEU   A 1 344 ? -16.439 -27.037 -19.923 1.00 75.04  ? 364 LEU   A CD2 1 
ATOM   2514 N  N   . ARG   A 1 345 ? -15.449 -25.419 -24.971 1.00 76.58  ? 365 ARG   A N   1 
ATOM   2515 C  CA  . ARG   A 1 345 ? -15.480 -24.298 -25.905 1.00 77.59  ? 365 ARG   A CA  1 
ATOM   2516 C  C   . ARG   A 1 345 ? -16.898 -24.045 -26.394 1.00 76.87  ? 365 ARG   A C   1 
ATOM   2517 O  O   . ARG   A 1 345 ? -17.366 -22.902 -26.408 1.00 78.23  ? 365 ARG   A O   1 
ATOM   2518 C  CB  . ARG   A 1 345 ? -14.549 -24.548 -27.092 1.00 74.27  ? 365 ARG   A CB  1 
ATOM   2519 C  CG  . ARG   A 1 345 ? -14.372 -23.316 -27.973 1.00 77.99  ? 365 ARG   A CG  1 
ATOM   2520 C  CD  . ARG   A 1 345 ? -13.641 -23.633 -29.261 1.00 78.31  ? 365 ARG   A CD  1 
ATOM   2521 N  NE  . ARG   A 1 345 ? -14.319 -24.673 -30.025 1.00 81.97  ? 365 ARG   A NE  1 
ATOM   2522 C  CZ  . ARG   A 1 345 ? -15.352 -24.458 -30.828 1.00 85.62  ? 365 ARG   A CZ  1 
ATOM   2523 N  NH1 . ARG   A 1 345 ? -15.853 -23.245 -31.000 1.00 92.08  ? 365 ARG   A NH1 1 
ATOM   2524 N  NH2 . ARG   A 1 345 ? -15.900 -25.487 -31.469 1.00 89.06  ? 365 ARG   A NH2 1 
ATOM   2525 N  N   . LEU   A 1 346 ? -17.602 -25.105 -26.791 1.00 75.30  ? 366 LEU   A N   1 
ATOM   2526 C  CA  . LEU   A 1 346 ? -18.953 -24.934 -27.311 1.00 75.71  ? 366 LEU   A CA  1 
ATOM   2527 C  C   . LEU   A 1 346 ? -19.951 -24.624 -26.203 1.00 80.60  ? 366 LEU   A C   1 
ATOM   2528 O  O   . LEU   A 1 346 ? -20.956 -23.949 -26.453 1.00 83.15  ? 366 LEU   A O   1 
ATOM   2529 C  CB  . LEU   A 1 346 ? -19.386 -26.178 -28.087 1.00 83.91  ? 366 LEU   A CB  1 
ATOM   2530 C  CG  . LEU   A 1 346 ? -18.898 -26.298 -29.534 1.00 85.83  ? 366 LEU   A CG  1 
ATOM   2531 C  CD1 . LEU   A 1 346 ? -19.345 -27.617 -30.138 1.00 89.35  ? 366 LEU   A CD1 1 
ATOM   2532 C  CD2 . LEU   A 1 346 ? -19.407 -25.131 -30.367 1.00 86.51  ? 366 LEU   A CD2 1 
ATOM   2533 N  N   . PHE   A 1 347 ? -19.698 -25.089 -24.979 1.00 78.61  ? 367 PHE   A N   1 
ATOM   2534 C  CA  . PHE   A 1 347 ? -20.615 -24.881 -23.857 1.00 77.98  ? 367 PHE   A CA  1 
ATOM   2535 C  C   . PHE   A 1 347 ? -19.848 -24.478 -22.602 1.00 75.25  ? 367 PHE   A C   1 
ATOM   2536 O  O   . PHE   A 1 347 ? -19.765 -25.240 -21.631 1.00 74.75  ? 367 PHE   A O   1 
ATOM   2537 C  CB  . PHE   A 1 347 ? -21.450 -26.137 -23.598 1.00 79.24  ? 367 PHE   A CB  1 
ATOM   2538 C  CG  . PHE   A 1 347 ? -22.124 -26.684 -24.821 1.00 81.87  ? 367 PHE   A CG  1 
ATOM   2539 C  CD1 . PHE   A 1 347 ? -23.132 -25.975 -25.450 1.00 84.15  ? 367 PHE   A CD1 1 
ATOM   2540 C  CD2 . PHE   A 1 347 ? -21.755 -27.918 -25.333 1.00 86.03  ? 367 PHE   A CD2 1 
ATOM   2541 C  CE1 . PHE   A 1 347 ? -23.756 -26.482 -26.576 1.00 86.48  ? 367 PHE   A CE1 1 
ATOM   2542 C  CE2 . PHE   A 1 347 ? -22.376 -28.432 -26.455 1.00 84.30  ? 367 PHE   A CE2 1 
ATOM   2543 C  CZ  . PHE   A 1 347 ? -23.378 -27.714 -27.078 1.00 84.68  ? 367 PHE   A CZ  1 
ATOM   2544 N  N   . PRO   A 1 348 ? -19.294 -23.262 -22.575 1.00 73.74  ? 368 PRO   A N   1 
ATOM   2545 C  CA  . PRO   A 1 348 ? -18.680 -22.769 -21.333 1.00 75.60  ? 368 PRO   A CA  1 
ATOM   2546 C  C   . PRO   A 1 348 ? -19.737 -22.378 -20.315 1.00 78.90  ? 368 PRO   A C   1 
ATOM   2547 O  O   . PRO   A 1 348 ? -20.314 -21.290 -20.406 1.00 81.40  ? 368 PRO   A O   1 
ATOM   2548 C  CB  . PRO   A 1 348 ? -17.867 -21.557 -21.802 1.00 72.55  ? 368 PRO   A CB  1 
ATOM   2549 C  CG  . PRO   A 1 348 ? -18.605 -21.066 -23.003 1.00 74.77  ? 368 PRO   A CG  1 
ATOM   2550 C  CD  . PRO   A 1 348 ? -19.197 -22.281 -23.672 1.00 71.43  ? 368 PRO   A CD  1 
ATOM   2551 N  N   . ILE   A 1 349 ? -19.988 -23.246 -19.331 1.00 76.84  ? 369 ILE   A N   1 
ATOM   2552 C  CA  . ILE   A 1 349 ? -21.155 -23.118 -18.467 1.00 79.96  ? 369 ILE   A CA  1 
ATOM   2553 C  C   . ILE   A 1 349 ? -21.203 -21.811 -17.688 1.00 79.14  ? 369 ILE   A C   1 
ATOM   2554 O  O   . ILE   A 1 349 ? -22.225 -21.519 -17.057 1.00 81.19  ? 369 ILE   A O   1 
ATOM   2555 C  CB  . ILE   A 1 349 ? -21.230 -24.311 -17.492 1.00 82.95  ? 369 ILE   A CB  1 
ATOM   2556 C  CG1 . ILE   A 1 349 ? -19.876 -24.526 -16.821 1.00 77.78  ? 369 ILE   A CG1 1 
ATOM   2557 C  CG2 . ILE   A 1 349 ? -21.679 -25.565 -18.219 1.00 81.71  ? 369 ILE   A CG2 1 
ATOM   2558 C  CD1 . ILE   A 1 349 ? -19.974 -24.750 -15.335 1.00 82.50  ? 369 ILE   A CD1 1 
ATOM   2559 N  N   . ALA   A 1 350 ? -20.135 -21.017 -17.710 1.00 79.94  ? 370 ALA   A N   1 
ATOM   2560 C  CA  . ALA   A 1 350 ? -20.146 -19.727 -17.031 1.00 78.86  ? 370 ALA   A CA  1 
ATOM   2561 C  C   . ALA   A 1 350 ? -20.645 -18.595 -17.919 1.00 80.05  ? 370 ALA   A C   1 
ATOM   2562 O  O   . ALA   A 1 350 ? -21.192 -17.612 -17.402 1.00 82.12  ? 370 ALA   A O   1 
ATOM   2563 C  CB  . ALA   A 1 350 ? -18.746 -19.389 -16.515 1.00 72.52  ? 370 ALA   A CB  1 
ATOM   2564 N  N   . MET   A 1 351 ? -20.448 -18.710 -19.237 1.00 78.39  ? 371 MET   A N   1 
ATOM   2565 C  CA  . MET   A 1 351 ? -20.956 -17.779 -20.245 1.00 78.09  ? 371 MET   A CA  1 
ATOM   2566 C  C   . MET   A 1 351 ? -20.252 -16.426 -20.206 1.00 77.02  ? 371 MET   A C   1 
ATOM   2567 O  O   . MET   A 1 351 ? -19.821 -15.922 -21.249 1.00 71.62  ? 371 MET   A O   1 
ATOM   2568 C  CB  . MET   A 1 351 ? -22.472 -17.596 -20.100 1.00 73.02  ? 371 MET   A CB  1 
ATOM   2569 C  CG  . MET   A 1 351 ? -23.269 -18.874 -20.311 1.00 83.94  ? 371 MET   A CG  1 
ATOM   2570 S  SD  . MET   A 1 351 ? -25.039 -18.656 -20.054 1.00 89.23  ? 371 MET   A SD  1 
ATOM   2571 C  CE  . MET   A 1 351 ? -25.103 -18.404 -18.280 1.00 94.73  ? 371 MET   A CE  1 
ATOM   2572 N  N   . ARG   A 1 352 ? -20.138 -15.826 -19.021 1.00 77.30  ? 372 ARG   A N   1 
ATOM   2573 C  CA  . ARG   A 1 352 ? -19.444 -14.558 -18.851 1.00 72.61  ? 372 ARG   A CA  1 
ATOM   2574 C  C   . ARG   A 1 352 ? -18.539 -14.619 -17.630 1.00 72.36  ? 372 ARG   A C   1 
ATOM   2575 O  O   . ARG   A 1 352 ? -18.834 -15.309 -16.650 1.00 76.15  ? 372 ARG   A O   1 
ATOM   2576 C  CB  . ARG   A 1 352 ? -20.414 -13.387 -18.664 1.00 76.42  ? 372 ARG   A CB  1 
ATOM   2577 C  CG  . ARG   A 1 352 ? -21.515 -13.240 -19.688 1.00 78.36  ? 372 ARG   A CG  1 
ATOM   2578 C  CD  . ARG   A 1 352 ? -22.577 -12.320 -19.107 1.00 82.87  ? 372 ARG   A CD  1 
ATOM   2579 N  NE  . ARG   A 1 352 ? -23.416 -11.689 -20.116 1.00 83.36  ? 372 ARG   A NE  1 
ATOM   2580 C  CZ  . ARG   A 1 352 ? -24.199 -10.645 -19.879 1.00 84.50  ? 372 ARG   A CZ  1 
ATOM   2581 N  NH1 . ARG   A 1 352 ? -24.272 -10.095 -18.678 1.00 88.92  ? 372 ARG   A NH1 1 
ATOM   2582 N  NH2 . ARG   A 1 352 ? -24.919 -10.135 -20.873 1.00 90.78  ? 372 ARG   A NH2 1 
ATOM   2583 N  N   . LEU   A 1 353 ? -17.437 -13.879 -17.696 1.00 72.74  ? 373 LEU   A N   1 
ATOM   2584 C  CA  . LEU   A 1 353 ? -16.629 -13.548 -16.534 1.00 75.17  ? 373 LEU   A CA  1 
ATOM   2585 C  C   . LEU   A 1 353 ? -16.779 -12.057 -16.266 1.00 70.38  ? 373 LEU   A C   1 
ATOM   2586 O  O   . LEU   A 1 353 ? -16.950 -11.267 -17.197 1.00 74.49  ? 373 LEU   A O   1 
ATOM   2587 C  CB  . LEU   A 1 353 ? -15.153 -13.890 -16.754 1.00 73.64  ? 373 LEU   A CB  1 
ATOM   2588 C  CG  . LEU   A 1 353 ? -14.823 -15.174 -17.516 1.00 77.69  ? 373 LEU   A CG  1 
ATOM   2589 C  CD1 . LEU   A 1 353 ? -13.341 -15.225 -17.825 1.00 70.86  ? 373 LEU   A CD1 1 
ATOM   2590 C  CD2 . LEU   A 1 353 ? -15.248 -16.392 -16.714 1.00 76.20  ? 373 LEU   A CD2 1 
ATOM   2591 N  N   . GLU   A 1 354 ? -16.723 -11.668 -14.993 1.00 75.63  ? 374 GLU   A N   1 
ATOM   2592 C  CA  . GLU   A 1 354 ? -16.966 -10.279 -14.628 1.00 73.76  ? 374 GLU   A CA  1 
ATOM   2593 C  C   . GLU   A 1 354 ? -16.059 -9.853  -13.483 1.00 74.35  ? 374 GLU   A C   1 
ATOM   2594 O  O   . GLU   A 1 354 ? -15.699 -10.656 -12.618 1.00 75.38  ? 374 GLU   A O   1 
ATOM   2595 C  CB  . GLU   A 1 354 ? -18.430 -10.047 -14.227 1.00 79.00  ? 374 GLU   A CB  1 
ATOM   2596 C  CG  . GLU   A 1 354 ? -19.431 -10.215 -15.360 1.00 77.06  ? 374 GLU   A CG  1 
ATOM   2597 C  CD  . GLU   A 1 354 ? -20.847 -9.868  -14.946 1.00 81.42  ? 374 GLU   A CD  1 
ATOM   2598 O  OE1 . GLU   A 1 354 ? -21.068 -9.587  -13.747 1.00 82.16  ? 374 GLU   A OE1 1 
ATOM   2599 O  OE2 . GLU   A 1 354 ? -21.738 -9.876  -15.823 1.00 84.49  ? 374 GLU   A OE2 1 
ATOM   2600 N  N   . ARG   A 1 355 ? -15.700 -8.568  -13.490 1.00 81.66  ? 375 ARG   A N   1 
ATOM   2601 C  CA  . ARG   A 1 355 ? -14.961 -7.926  -12.412 1.00 82.15  ? 375 ARG   A CA  1 
ATOM   2602 C  C   . ARG   A 1 355 ? -15.483 -6.508  -12.236 1.00 85.14  ? 375 ARG   A C   1 
ATOM   2603 O  O   . ARG   A 1 355 ? -15.750 -5.817  -13.223 1.00 81.44  ? 375 ARG   A O   1 
ATOM   2604 C  CB  . ARG   A 1 355 ? -13.452 -7.870  -12.692 1.00 81.53  ? 375 ARG   A CB  1 
ATOM   2605 C  CG  . ARG   A 1 355 ? -12.785 -9.212  -12.913 1.00 83.67  ? 375 ARG   A CG  1 
ATOM   2606 C  CD  . ARG   A 1 355 ? -12.631 -9.994  -11.620 1.00 82.42  ? 375 ARG   A CD  1 
ATOM   2607 N  NE  . ARG   A 1 355 ? -11.994 -11.279 -11.874 1.00 73.58  ? 375 ARG   A NE  1 
ATOM   2608 C  CZ  . ARG   A 1 355 ? -12.650 -12.387 -12.187 1.00 70.89  ? 375 ARG   A CZ  1 
ATOM   2609 N  NH1 . ARG   A 1 355 ? -13.971 -12.418 -12.232 1.00 75.86  ? 375 ARG   A NH1 1 
ATOM   2610 N  NH2 . ARG   A 1 355 ? -11.963 -13.489 -12.469 1.00 78.51  ? 375 ARG   A NH2 1 
ATOM   2611 N  N   . VAL   A 1 356 ? -15.621 -6.072  -10.984 1.00 86.78  ? 376 VAL   A N   1 
ATOM   2612 C  CA  . VAL   A 1 356 ? -15.982 -4.684  -10.721 1.00 86.27  ? 376 VAL   A CA  1 
ATOM   2613 C  C   . VAL   A 1 356 ? -14.723 -3.831  -10.767 1.00 88.59  ? 376 VAL   A C   1 
ATOM   2614 O  O   . VAL   A 1 356 ? -13.642 -4.251  -10.334 1.00 88.66  ? 376 VAL   A O   1 
ATOM   2615 C  CB  . VAL   A 1 356 ? -16.715 -4.535  -9.372  1.00 89.93  ? 376 VAL   A CB  1 
ATOM   2616 C  CG1 . VAL   A 1 356 ? -17.790 -5.588  -9.233  1.00 84.80  ? 376 VAL   A CG1 1 
ATOM   2617 C  CG2 . VAL   A 1 356 ? -15.746 -4.584  -8.190  1.00 93.93  ? 376 VAL   A CG2 1 
ATOM   2618 N  N   . CYS   A 1 357 ? -14.857 -2.636  -11.326 1.00 94.81  ? 377 CYS   A N   1 
ATOM   2619 C  CA  . CYS   A 1 357 ? -13.771 -1.668  -11.360 1.00 89.60  ? 377 CYS   A CA  1 
ATOM   2620 C  C   . CYS   A 1 357 ? -13.922 -0.769  -10.140 1.00 91.94  ? 377 CYS   A C   1 
ATOM   2621 O  O   . CYS   A 1 357 ? -14.875 0.009   -10.051 1.00 95.32  ? 377 CYS   A O   1 
ATOM   2622 C  CB  . CYS   A 1 357 ? -13.809 -0.869  -12.658 1.00 90.65  ? 377 CYS   A CB  1 
ATOM   2623 S  SG  . CYS   A 1 357 ? -12.449 0.286   -12.842 1.00 105.97 ? 377 CYS   A SG  1 
ATOM   2624 N  N   . LYS   A 1 358 ? -12.999 -0.891  -9.188  1.00 96.13  ? 378 LYS   A N   1 
ATOM   2625 C  CA  . LYS   A 1 358 ? -13.109 -0.192  -7.913  1.00 96.72  ? 378 LYS   A CA  1 
ATOM   2626 C  C   . LYS   A 1 358 ? -12.337 1.121   -7.878  1.00 99.11  ? 378 LYS   A C   1 
ATOM   2627 O  O   . LYS   A 1 358 ? -12.321 1.783   -6.835  1.00 101.10 ? 378 LYS   A O   1 
ATOM   2628 C  CB  . LYS   A 1 358 ? -12.649 -1.100  -6.769  1.00 99.14  ? 378 LYS   A CB  1 
ATOM   2629 C  CG  . LYS   A 1 358 ? -11.234 -1.641  -6.907  1.00 100.25 ? 378 LYS   A CG  1 
ATOM   2630 C  CD  . LYS   A 1 358 ? -10.926 -2.650  -5.807  1.00 97.60  ? 378 LYS   A CD  1 
ATOM   2631 C  CE  . LYS   A 1 358 ? -9.641  -3.411  -6.090  1.00 102.21 ? 378 LYS   A CE  1 
ATOM   2632 N  NZ  . LYS   A 1 358 ? -8.517  -2.992  -5.207  1.00 106.95 ? 378 LYS   A NZ  1 
ATOM   2633 N  N   . LYS   A 1 359 ? -11.703 1.512   -8.982  1.00 98.76  ? 379 LYS   A N   1 
ATOM   2634 C  CA  . LYS   A 1 359 ? -10.963 2.765   -9.063  1.00 104.66 ? 379 LYS   A CA  1 
ATOM   2635 C  C   . LYS   A 1 359 ? -11.008 3.276   -10.494 1.00 106.43 ? 379 LYS   A C   1 
ATOM   2636 O  O   . LYS   A 1 359 ? -11.152 2.495   -11.436 1.00 108.69 ? 379 LYS   A O   1 
ATOM   2637 C  CB  . LYS   A 1 359 ? -9.492  2.604   -8.661  1.00 105.25 ? 379 LYS   A CB  1 
ATOM   2638 C  CG  . LYS   A 1 359 ? -9.218  2.111   -7.254  1.00 108.35 ? 379 LYS   A CG  1 
ATOM   2639 C  CD  . LYS   A 1 359 ? -7.725  1.885   -7.061  1.00 109.77 ? 379 LYS   A CD  1 
ATOM   2640 C  CE  . LYS   A 1 359 ? -6.915  2.918   -7.840  1.00 108.09 ? 379 LYS   A CE  1 
ATOM   2641 N  NZ  . LYS   A 1 359 ? -5.677  3.342   -7.133  1.00 109.86 ? 379 LYS   A NZ  1 
ATOM   2642 N  N   . ASP   A 1 360 ? -10.862 4.588   -10.655 1.00 104.65 ? 380 ASP   A N   1 
ATOM   2643 C  CA  . ASP   A 1 360 ? -10.537 5.122   -11.970 1.00 108.78 ? 380 ASP   A CA  1 
ATOM   2644 C  C   . ASP   A 1 360 ? -9.249  4.471   -12.461 1.00 109.03 ? 380 ASP   A C   1 
ATOM   2645 O  O   . ASP   A 1 360 ? -8.309  4.262   -11.691 1.00 110.73 ? 380 ASP   A O   1 
ATOM   2646 C  CB  . ASP   A 1 360 ? -10.377 6.642   -11.915 1.00 114.21 ? 380 ASP   A CB  1 
ATOM   2647 C  CG  . ASP   A 1 360 ? -11.693 7.366   -11.689 1.00 116.03 ? 380 ASP   A CG  1 
ATOM   2648 O  OD1 . ASP   A 1 360 ? -12.669 7.082   -12.416 1.00 111.27 ? 380 ASP   A OD1 1 
ATOM   2649 O  OD2 . ASP   A 1 360 ? -11.749 8.221   -10.779 1.00 123.53 ? 380 ASP   A OD2 1 
ATOM   2650 N  N   . VAL   A 1 361 ? -9.213  4.128   -13.748 1.00 110.35 ? 381 VAL   A N   1 
ATOM   2651 C  CA  . VAL   A 1 361 ? -8.084  3.386   -14.295 1.00 111.98 ? 381 VAL   A CA  1 
ATOM   2652 C  C   . VAL   A 1 361 ? -8.061  3.575   -15.802 1.00 116.90 ? 381 VAL   A C   1 
ATOM   2653 O  O   . VAL   A 1 361 ? -9.090  3.852   -16.423 1.00 118.37 ? 381 VAL   A O   1 
ATOM   2654 C  CB  . VAL   A 1 361 ? -8.162  1.889   -13.897 1.00 110.51 ? 381 VAL   A CB  1 
ATOM   2655 C  CG1 . VAL   A 1 361 ? -9.333  1.208   -14.592 1.00 106.32 ? 381 VAL   A CG1 1 
ATOM   2656 C  CG2 . VAL   A 1 361 ? -6.851  1.177   -14.196 1.00 112.24 ? 381 VAL   A CG2 1 
ATOM   2657 N  N   . GLU   A 1 362 ? -6.872  3.438   -16.386 1.00 113.67 ? 382 GLU   A N   1 
ATOM   2658 C  CA  . GLU   A 1 362 ? -6.671  3.460   -17.832 1.00 116.20 ? 382 GLU   A CA  1 
ATOM   2659 C  C   . GLU   A 1 362 ? -5.845  2.231   -18.201 1.00 116.78 ? 382 GLU   A C   1 
ATOM   2660 O  O   . GLU   A 1 362 ? -4.613  2.255   -18.108 1.00 121.21 ? 382 GLU   A O   1 
ATOM   2661 C  CB  . GLU   A 1 362 ? -5.982  4.745   -18.280 1.00 123.87 ? 382 GLU   A CB  1 
ATOM   2662 C  CG  . GLU   A 1 362 ? -6.928  5.916   -18.460 1.00 131.12 ? 382 GLU   A CG  1 
ATOM   2663 C  CD  . GLU   A 1 362 ? -6.355  7.221   -17.952 1.00 138.22 ? 382 GLU   A CD  1 
ATOM   2664 O  OE1 . GLU   A 1 362 ? -5.199  7.222   -17.478 1.00 144.44 ? 382 GLU   A OE1 1 
ATOM   2665 O  OE2 . GLU   A 1 362 ? -7.066  8.246   -18.020 1.00 138.83 ? 382 GLU   A OE2 1 
ATOM   2666 N  N   . ILE   A 1 363 ? -6.516  1.159   -18.613 1.00 123.41 ? 383 ILE   A N   1 
ATOM   2667 C  CA  . ILE   A 1 363 ? -5.847  -0.060  -19.050 1.00 123.47 ? 383 ILE   A CA  1 
ATOM   2668 C  C   . ILE   A 1 363 ? -5.845  -0.094  -20.573 1.00 127.26 ? 383 ILE   A C   1 
ATOM   2669 O  O   . ILE   A 1 363 ? -6.864  0.206   -21.212 1.00 125.76 ? 383 ILE   A O   1 
ATOM   2670 C  CB  . ILE   A 1 363 ? -6.514  -1.317  -18.459 1.00 118.47 ? 383 ILE   A CB  1 
ATOM   2671 C  CG1 . ILE   A 1 363 ? -7.899  -1.553  -19.057 1.00 111.52 ? 383 ILE   A CG1 1 
ATOM   2672 C  CG2 . ILE   A 1 363 ? -6.632  -1.197  -16.952 1.00 114.50 ? 383 ILE   A CG2 1 
ATOM   2673 C  CD1 . ILE   A 1 363 ? -8.628  -2.712  -18.437 1.00 110.29 ? 383 ILE   A CD1 1 
ATOM   2674 N  N   . ASN   A 1 364 ? -4.691  -0.427  -21.147 1.00 133.01 ? 384 ASN   A N   1 
ATOM   2675 C  CA  . ASN   A 1 364 ? -4.518  -0.593  -22.589 1.00 134.38 ? 384 ASN   A CA  1 
ATOM   2676 C  C   . ASN   A 1 364 ? -5.175  0.539   -23.375 1.00 131.70 ? 384 ASN   A C   1 
ATOM   2677 O  O   . ASN   A 1 364 ? -5.930  0.324   -24.325 1.00 132.18 ? 384 ASN   A O   1 
ATOM   2678 C  CB  . ASN   A 1 364 ? -5.041  -1.955  -23.037 1.00 132.27 ? 384 ASN   A CB  1 
ATOM   2679 C  CG  . ASN   A 1 364 ? -4.305  -3.104  -22.371 1.00 129.64 ? 384 ASN   A CG  1 
ATOM   2680 O  OD1 . ASN   A 1 364 ? -4.734  -3.615  -21.336 1.00 125.54 ? 384 ASN   A OD1 1 
ATOM   2681 N  ND2 . ASN   A 1 364 ? -3.183  -3.508  -22.958 1.00 130.78 ? 384 ASN   A ND2 1 
ATOM   2682 N  N   . GLY   A 1 365 ? -4.882  1.768   -22.954 1.00 124.63 ? 385 GLY   A N   1 
ATOM   2683 C  CA  . GLY   A 1 365 ? -5.336  2.933   -23.687 1.00 124.72 ? 385 GLY   A CA  1 
ATOM   2684 C  C   . GLY   A 1 365 ? -6.800  3.280   -23.526 1.00 126.37 ? 385 GLY   A C   1 
ATOM   2685 O  O   . GLY   A 1 365 ? -7.321  4.079   -24.307 1.00 127.18 ? 385 GLY   A O   1 
ATOM   2686 N  N   . MET   A 1 366 ? -7.481  2.718   -22.530 1.00 120.05 ? 386 MET   A N   1 
ATOM   2687 C  CA  . MET   A 1 366 ? -8.902  2.968   -22.324 1.00 117.32 ? 386 MET   A CA  1 
ATOM   2688 C  C   . MET   A 1 366 ? -9.174  3.305   -20.866 1.00 116.99 ? 386 MET   A C   1 
ATOM   2689 O  O   . MET   A 1 366 ? -8.767  2.561   -19.969 1.00 115.91 ? 386 MET   A O   1 
ATOM   2690 C  CB  . MET   A 1 366 ? -9.743  1.761   -22.741 1.00 118.58 ? 386 MET   A CB  1 
ATOM   2691 C  CG  . MET   A 1 366 ? -11.186 1.834   -22.275 1.00 118.47 ? 386 MET   A CG  1 
ATOM   2692 S  SD  . MET   A 1 366 ? -12.219 0.611   -23.093 1.00 106.67 ? 386 MET   A SD  1 
ATOM   2693 C  CE  . MET   A 1 366 ? -11.887 1.012   -24.807 1.00 116.16 ? 386 MET   A CE  1 
ATOM   2694 N  N   . PHE   A 1 367 ? -9.883  4.409   -20.640 1.00 116.65 ? 387 PHE   A N   1 
ATOM   2695 C  CA  . PHE   A 1 367 ? -10.239 4.843   -19.294 1.00 113.35 ? 387 PHE   A CA  1 
ATOM   2696 C  C   . PHE   A 1 367 ? -11.510 4.137   -18.840 1.00 112.59 ? 387 PHE   A C   1 
ATOM   2697 O  O   . PHE   A 1 367 ? -12.557 4.250   -19.489 1.00 114.76 ? 387 PHE   A O   1 
ATOM   2698 C  CB  . PHE   A 1 367 ? -10.426 6.359   -19.264 1.00 116.19 ? 387 PHE   A CB  1 
ATOM   2699 C  CG  . PHE   A 1 367 ? -11.059 6.876   -18.000 1.00 117.82 ? 387 PHE   A CG  1 
ATOM   2700 C  CD1 . PHE   A 1 367 ? -10.300 7.081   -16.859 1.00 118.86 ? 387 PHE   A CD1 1 
ATOM   2701 C  CD2 . PHE   A 1 367 ? -12.412 7.175   -17.960 1.00 114.93 ? 387 PHE   A CD2 1 
ATOM   2702 C  CE1 . PHE   A 1 367 ? -10.881 7.564   -15.700 1.00 116.09 ? 387 PHE   A CE1 1 
ATOM   2703 C  CE2 . PHE   A 1 367 ? -12.999 7.657   -16.805 1.00 110.48 ? 387 PHE   A CE2 1 
ATOM   2704 C  CZ  . PHE   A 1 367 ? -12.233 7.852   -15.674 1.00 114.09 ? 387 PHE   A CZ  1 
ATOM   2705 N  N   . ILE   A 1 368 ? -11.424 3.414   -17.733 1.00 114.69 ? 388 ILE   A N   1 
ATOM   2706 C  CA  . ILE   A 1 368 ? -12.575 2.756   -17.122 1.00 109.12 ? 388 ILE   A CA  1 
ATOM   2707 C  C   . ILE   A 1 368 ? -12.823 3.412   -15.769 1.00 112.24 ? 388 ILE   A C   1 
ATOM   2708 O  O   . ILE   A 1 368 ? -11.920 3.438   -14.923 1.00 114.69 ? 388 ILE   A O   1 
ATOM   2709 C  CB  . ILE   A 1 368 ? -12.361 1.243   -16.976 1.00 107.33 ? 388 ILE   A CB  1 
ATOM   2710 C  CG1 . ILE   A 1 368 ? -12.350 0.591   -18.356 1.00 109.34 ? 388 ILE   A CG1 1 
ATOM   2711 C  CG2 . ILE   A 1 368 ? -13.463 0.632   -16.133 1.00 104.21 ? 388 ILE   A CG2 1 
ATOM   2712 C  CD1 . ILE   A 1 368 ? -11.128 -0.216  -18.632 1.00 109.89 ? 388 ILE   A CD1 1 
ATOM   2713 N  N   . PRO   A 1 369 ? -14.009 3.957   -15.526 1.00 108.02 ? 389 PRO   A N   1 
ATOM   2714 C  CA  . PRO   A 1 369 ? -14.259 4.655   -14.265 1.00 105.63 ? 389 PRO   A CA  1 
ATOM   2715 C  C   . PRO   A 1 369 ? -14.603 3.691   -13.144 1.00 104.56 ? 389 PRO   A C   1 
ATOM   2716 O  O   . PRO   A 1 369 ? -15.068 2.571   -13.367 1.00 99.40  ? 389 PRO   A O   1 
ATOM   2717 C  CB  . PRO   A 1 369 ? -15.457 5.561   -14.589 1.00 104.11 ? 389 PRO   A CB  1 
ATOM   2718 C  CG  . PRO   A 1 369 ? -15.753 5.360   -16.069 1.00 104.08 ? 389 PRO   A CG  1 
ATOM   2719 C  CD  . PRO   A 1 369 ? -15.154 4.050   -16.443 1.00 104.55 ? 389 PRO   A CD  1 
ATOM   2720 N  N   . LYS   A 1 370 ? -14.355 4.151   -11.921 1.00 104.98 ? 390 LYS   A N   1 
ATOM   2721 C  CA  . LYS   A 1 370 ? -14.768 3.423   -10.732 1.00 100.82 ? 390 LYS   A CA  1 
ATOM   2722 C  C   . LYS   A 1 370 ? -16.261 3.128   -10.782 1.00 95.05  ? 390 LYS   A C   1 
ATOM   2723 O  O   . LYS   A 1 370 ? -17.077 4.030   -10.981 1.00 101.20 ? 390 LYS   A O   1 
ATOM   2724 C  CB  . LYS   A 1 370 ? -14.434 4.238   -9.482  1.00 100.19 ? 390 LYS   A CB  1 
ATOM   2725 C  CG  . LYS   A 1 370 ? -15.120 3.746   -8.222  1.00 99.60  ? 390 LYS   A CG  1 
ATOM   2726 C  CD  . LYS   A 1 370 ? -14.837 4.649   -7.035  1.00 97.63  ? 390 LYS   A CD  1 
ATOM   2727 C  CE  . LYS   A 1 370 ? -14.620 3.819   -5.783  1.00 100.25 ? 390 LYS   A CE  1 
ATOM   2728 N  NZ  . LYS   A 1 370 ? -14.886 4.592   -4.541  1.00 103.31 ? 390 LYS   A NZ  1 
ATOM   2729 N  N   . GLY   A 1 371 ? -16.613 1.853   -10.616 1.00 94.26  ? 391 GLY   A N   1 
ATOM   2730 C  CA  . GLY   A 1 371 ? -17.995 1.423   -10.528 1.00 92.46  ? 391 GLY   A CA  1 
ATOM   2731 C  C   . GLY   A 1 371 ? -18.466 0.547   -11.670 1.00 94.35  ? 391 GLY   A C   1 
ATOM   2732 O  O   . GLY   A 1 371 ? -19.482 -0.145  -11.521 1.00 89.82  ? 391 GLY   A O   1 
ATOM   2733 N  N   . VAL   A 1 372 ? -17.766 0.548   -12.799 1.00 86.70  ? 392 VAL   A N   1 
ATOM   2734 C  CA  . VAL   A 1 372 ? -18.218 -0.187  -13.975 1.00 84.65  ? 392 VAL   A CA  1 
ATOM   2735 C  C   . VAL   A 1 372 ? -17.899 -1.667  -13.815 1.00 84.70  ? 392 VAL   A C   1 
ATOM   2736 O  O   . VAL   A 1 372 ? -16.813 -2.045  -13.356 1.00 87.36  ? 392 VAL   A O   1 
ATOM   2737 C  CB  . VAL   A 1 372 ? -17.574 0.390   -15.247 1.00 86.50  ? 392 VAL   A CB  1 
ATOM   2738 C  CG1 . VAL   A 1 372 ? -18.163 -0.267  -16.488 1.00 85.37  ? 392 VAL   A CG1 1 
ATOM   2739 C  CG2 . VAL   A 1 372 ? -17.767 1.893   -15.294 1.00 89.72  ? 392 VAL   A CG2 1 
ATOM   2740 N  N   . VAL   A 1 373 ? -18.853 -2.514  -14.195 1.00 78.85  ? 393 VAL   A N   1 
ATOM   2741 C  CA  . VAL   A 1 373 ? -18.648 -3.959  -14.215 1.00 81.10  ? 393 VAL   A CA  1 
ATOM   2742 C  C   . VAL   A 1 373 ? -17.974 -4.321  -15.534 1.00 83.73  ? 393 VAL   A C   1 
ATOM   2743 O  O   . VAL   A 1 373 ? -18.600 -4.271  -16.595 1.00 83.47  ? 393 VAL   A O   1 
ATOM   2744 C  CB  . VAL   A 1 373 ? -19.967 -4.720  -14.040 1.00 73.40  ? 393 VAL   A CB  1 
ATOM   2745 C  CG1 . VAL   A 1 373 ? -19.749 -6.211  -14.253 1.00 73.83  ? 393 VAL   A CG1 1 
ATOM   2746 C  CG2 . VAL   A 1 373 ? -20.551 -4.459  -12.663 1.00 76.42  ? 393 VAL   A CG2 1 
ATOM   2747 N  N   . VAL   A 1 374 ? -16.695 -4.675  -15.474 1.00 78.93  ? 394 VAL   A N   1 
ATOM   2748 C  CA  . VAL   A 1 374 ? -15.990 -5.151  -16.657 1.00 78.59  ? 394 VAL   A CA  1 
ATOM   2749 C  C   . VAL   A 1 374 ? -16.338 -6.615  -16.874 1.00 80.45  ? 394 VAL   A C   1 
ATOM   2750 O  O   . VAL   A 1 374 ? -16.178 -7.446  -15.972 1.00 79.47  ? 394 VAL   A O   1 
ATOM   2751 C  CB  . VAL   A 1 374 ? -14.476 -4.948  -16.514 1.00 81.08  ? 394 VAL   A CB  1 
ATOM   2752 C  CG1 . VAL   A 1 374 ? -13.769 -5.402  -17.779 1.00 79.23  ? 394 VAL   A CG1 1 
ATOM   2753 C  CG2 . VAL   A 1 374 ? -14.174 -3.487  -16.228 1.00 76.27  ? 394 VAL   A CG2 1 
ATOM   2754 N  N   . MET   A 1 375 ? -16.822 -6.933  -18.071 1.00 77.48  ? 395 MET   A N   1 
ATOM   2755 C  CA  . MET   A 1 375 ? -17.360 -8.249  -18.381 1.00 74.07  ? 395 MET   A CA  1 
ATOM   2756 C  C   . MET   A 1 375 ? -16.652 -8.814  -19.603 1.00 72.13  ? 395 MET   A C   1 
ATOM   2757 O  O   . MET   A 1 375 ? -16.537 -8.134  -20.626 1.00 70.65  ? 395 MET   A O   1 
ATOM   2758 C  CB  . MET   A 1 375 ? -18.873 -8.166  -18.618 1.00 74.69  ? 395 MET   A CB  1 
ATOM   2759 C  CG  . MET   A 1 375 ? -19.545 -9.483  -18.952 1.00 74.10  ? 395 MET   A CG  1 
ATOM   2760 S  SD  . MET   A 1 375 ? -19.514 -9.865  -20.715 1.00 74.75  ? 395 MET   A SD  1 
ATOM   2761 C  CE  . MET   A 1 375 ? -21.196 -9.491  -21.196 1.00 83.83  ? 395 MET   A CE  1 
ATOM   2762 N  N   . ILE   A 1 376 ? -16.182 -10.050 -19.493 1.00 72.34  ? 396 ILE   A N   1 
ATOM   2763 C  CA  . ILE   A 1 376 ? -15.565 -10.774 -20.601 1.00 74.69  ? 396 ILE   A CA  1 
ATOM   2764 C  C   . ILE   A 1 376 ? -16.601 -11.747 -21.153 1.00 76.52  ? 396 ILE   A C   1 
ATOM   2765 O  O   . ILE   A 1 376 ? -17.046 -12.637 -20.414 1.00 71.36  ? 396 ILE   A O   1 
ATOM   2766 C  CB  . ILE   A 1 376 ? -14.292 -11.516 -20.161 1.00 76.96  ? 396 ILE   A CB  1 
ATOM   2767 C  CG1 . ILE   A 1 376 ? -13.208 -10.534 -19.705 1.00 76.11  ? 396 ILE   A CG1 1 
ATOM   2768 C  CG2 . ILE   A 1 376 ? -13.766 -12.382 -21.295 1.00 73.11  ? 396 ILE   A CG2 1 
ATOM   2769 C  CD1 . ILE   A 1 376 ? -13.266 -10.181 -18.235 1.00 71.65  ? 396 ILE   A CD1 1 
ATOM   2770 N  N   . PRO   A 1 377 ? -17.021 -11.611 -22.421 1.00 79.68  ? 397 PRO   A N   1 
ATOM   2771 C  CA  . PRO   A 1 377 ? -18.053 -12.503 -22.972 1.00 78.42  ? 397 PRO   A CA  1 
ATOM   2772 C  C   . PRO   A 1 377 ? -17.504 -13.851 -23.419 1.00 76.55  ? 397 PRO   A C   1 
ATOM   2773 O  O   . PRO   A 1 377 ? -17.151 -14.037 -24.591 1.00 73.36  ? 397 PRO   A O   1 
ATOM   2774 C  CB  . PRO   A 1 377 ? -18.600 -11.700 -24.161 1.00 77.94  ? 397 PRO   A CB  1 
ATOM   2775 C  CG  . PRO   A 1 377 ? -17.447 -10.863 -24.596 1.00 75.40  ? 397 PRO   A CG  1 
ATOM   2776 C  CD  . PRO   A 1 377 ? -16.658 -10.531 -23.356 1.00 76.21  ? 397 PRO   A CD  1 
ATOM   2777 N  N   . SER   A 1 378 ? -17.459 -14.808 -22.495 1.00 77.23  ? 398 SER   A N   1 
ATOM   2778 C  CA  . SER   A 1 378 ? -16.775 -16.067 -22.765 1.00 75.67  ? 398 SER   A CA  1 
ATOM   2779 C  C   . SER   A 1 378 ? -17.483 -16.878 -23.844 1.00 79.89  ? 398 SER   A C   1 
ATOM   2780 O  O   . SER   A 1 378 ? -16.841 -17.365 -24.783 1.00 82.77  ? 398 SER   A O   1 
ATOM   2781 C  CB  . SER   A 1 378 ? -16.646 -16.879 -21.473 1.00 72.76  ? 398 SER   A CB  1 
ATOM   2782 O  OG  . SER   A 1 378 ? -15.669 -16.303 -20.624 1.00 68.10  ? 398 SER   A OG  1 
ATOM   2783 N  N   . TYR   A 1 379 ? -18.804 -17.046 -23.726 1.00 76.44  ? 399 TYR   A N   1 
ATOM   2784 C  CA  . TYR   A 1 379 ? -19.534 -17.815 -24.731 1.00 82.01  ? 399 TYR   A CA  1 
ATOM   2785 C  C   . TYR   A 1 379 ? -19.310 -17.246 -26.123 1.00 83.13  ? 399 TYR   A C   1 
ATOM   2786 O  O   . TYR   A 1 379 ? -19.105 -17.994 -27.086 1.00 82.98  ? 399 TYR   A O   1 
ATOM   2787 C  CB  . TYR   A 1 379 ? -21.032 -17.839 -24.409 1.00 81.09  ? 399 TYR   A CB  1 
ATOM   2788 C  CG  . TYR   A 1 379 ? -21.874 -18.568 -25.444 1.00 81.98  ? 399 TYR   A CG  1 
ATOM   2789 C  CD1 . TYR   A 1 379 ? -22.345 -17.912 -26.580 1.00 87.05  ? 399 TYR   A CD1 1 
ATOM   2790 C  CD2 . TYR   A 1 379 ? -22.205 -19.908 -25.281 1.00 84.32  ? 399 TYR   A CD2 1 
ATOM   2791 C  CE1 . TYR   A 1 379 ? -23.115 -18.573 -27.525 1.00 84.03  ? 399 TYR   A CE1 1 
ATOM   2792 C  CE2 . TYR   A 1 379 ? -22.975 -20.577 -26.224 1.00 86.60  ? 399 TYR   A CE2 1 
ATOM   2793 C  CZ  . TYR   A 1 379 ? -23.427 -19.903 -27.343 1.00 85.70  ? 399 TYR   A CZ  1 
ATOM   2794 O  OH  . TYR   A 1 379 ? -24.191 -20.562 -28.282 1.00 86.87  ? 399 TYR   A OH  1 
ATOM   2795 N  N   . ALA   A 1 380 ? -19.342 -15.918 -26.245 1.00 84.06  ? 400 ALA   A N   1 
ATOM   2796 C  CA  . ALA   A 1 380 ? -19.178 -15.290 -27.550 1.00 86.35  ? 400 ALA   A CA  1 
ATOM   2797 C  C   . ALA   A 1 380 ? -17.760 -15.473 -28.076 1.00 85.23  ? 400 ALA   A C   1 
ATOM   2798 O  O   . ALA   A 1 380 ? -17.563 -15.846 -29.238 1.00 90.01  ? 400 ALA   A O   1 
ATOM   2799 C  CB  . ALA   A 1 380 ? -19.542 -13.807 -27.467 1.00 89.54  ? 400 ALA   A CB  1 
ATOM   2800 N  N   . LEU   A 1 381 ? -16.756 -15.223 -27.229 1.00 86.72  ? 401 LEU   A N   1 
ATOM   2801 C  CA  . LEU   A 1 381 ? -15.367 -15.336 -27.669 1.00 81.63  ? 401 LEU   A CA  1 
ATOM   2802 C  C   . LEU   A 1 381 ? -15.033 -16.758 -28.103 1.00 84.72  ? 401 LEU   A C   1 
ATOM   2803 O  O   . LEU   A 1 381 ? -14.240 -16.961 -29.030 1.00 86.36  ? 401 LEU   A O   1 
ATOM   2804 C  CB  . LEU   A 1 381 ? -14.425 -14.879 -26.555 1.00 77.03  ? 401 LEU   A CB  1 
ATOM   2805 C  CG  . LEU   A 1 381 ? -14.491 -13.391 -26.211 1.00 74.72  ? 401 LEU   A CG  1 
ATOM   2806 C  CD1 . LEU   A 1 381 ? -13.606 -13.066 -25.016 1.00 77.18  ? 401 LEU   A CD1 1 
ATOM   2807 C  CD2 . LEU   A 1 381 ? -14.101 -12.555 -27.419 1.00 83.37  ? 401 LEU   A CD2 1 
ATOM   2808 N  N   . HIS   A 1 382 ? -15.628 -17.757 -27.446 1.00 81.15  ? 402 HIS   A N   1 
ATOM   2809 C  CA  . HIS   A 1 382 ? -15.418 -19.140 -27.854 1.00 82.07  ? 402 HIS   A CA  1 
ATOM   2810 C  C   . HIS   A 1 382 ? -15.964 -19.421 -29.249 1.00 85.49  ? 402 HIS   A C   1 
ATOM   2811 O  O   . HIS   A 1 382 ? -15.532 -20.386 -29.888 1.00 90.25  ? 402 HIS   A O   1 
ATOM   2812 C  CB  . HIS   A 1 382 ? -16.066 -20.090 -26.848 1.00 80.45  ? 402 HIS   A CB  1 
ATOM   2813 C  CG  . HIS   A 1 382 ? -15.381 -20.128 -25.517 1.00 79.91  ? 402 HIS   A CG  1 
ATOM   2814 N  ND1 . HIS   A 1 382 ? -15.674 -21.075 -24.559 1.00 80.09  ? 402 HIS   A ND1 1 
ATOM   2815 C  CD2 . HIS   A 1 382 ? -14.417 -19.341 -24.984 1.00 82.02  ? 402 HIS   A CD2 1 
ATOM   2816 C  CE1 . HIS   A 1 382 ? -14.919 -20.871 -23.494 1.00 82.35  ? 402 HIS   A CE1 1 
ATOM   2817 N  NE2 . HIS   A 1 382 ? -14.146 -19.826 -23.727 1.00 80.02  ? 402 HIS   A NE2 1 
ATOM   2818 N  N   . ARG   A 1 383 ? -16.895 -18.604 -29.735 1.00 86.25  ? 403 ARG   A N   1 
ATOM   2819 C  CA  . ARG   A 1 383 ? -17.530 -18.802 -31.032 1.00 89.28  ? 403 ARG   A CA  1 
ATOM   2820 C  C   . ARG   A 1 383 ? -17.250 -17.632 -31.971 1.00 95.81  ? 403 ARG   A C   1 
ATOM   2821 O  O   . ARG   A 1 383 ? -18.103 -17.236 -32.768 1.00 101.30 ? 403 ARG   A O   1 
ATOM   2822 C  CB  . ARG   A 1 383 ? -19.033 -19.013 -30.867 1.00 88.15  ? 403 ARG   A CB  1 
ATOM   2823 C  CG  . ARG   A 1 383 ? -19.394 -20.277 -30.112 1.00 88.19  ? 403 ARG   A CG  1 
ATOM   2824 C  CD  . ARG   A 1 383 ? -20.835 -20.243 -29.652 1.00 90.08  ? 403 ARG   A CD  1 
ATOM   2825 N  NE  . ARG   A 1 383 ? -21.211 -21.462 -28.948 1.00 87.11  ? 403 ARG   A NE  1 
ATOM   2826 C  CZ  . ARG   A 1 383 ? -21.918 -22.446 -29.485 1.00 92.15  ? 403 ARG   A CZ  1 
ATOM   2827 N  NH1 . ARG   A 1 383 ? -22.352 -22.384 -30.733 1.00 99.61  ? 403 ARG   A NH1 1 
ATOM   2828 N  NH2 . ARG   A 1 383 ? -22.202 -23.518 -28.750 1.00 89.25  ? 403 ARG   A NH2 1 
ATOM   2829 N  N   . ASP   A 1 384 ? -16.045 -17.069 -31.890 1.00 105.66 ? 404 ASP   A N   1 
ATOM   2830 C  CA  . ASP   A 1 384 ? -15.661 -15.959 -32.751 1.00 113.44 ? 404 ASP   A CA  1 
ATOM   2831 C  C   . ASP   A 1 384 ? -14.977 -16.498 -34.000 1.00 120.65 ? 404 ASP   A C   1 
ATOM   2832 O  O   . ASP   A 1 384 ? -13.970 -17.209 -33.880 1.00 117.81 ? 404 ASP   A O   1 
ATOM   2833 C  CB  . ASP   A 1 384 ? -14.732 -15.003 -32.017 1.00 112.20 ? 404 ASP   A CB  1 
ATOM   2834 C  CG  . ASP   A 1 384 ? -14.570 -13.669 -32.732 1.00 116.47 ? 404 ASP   A CG  1 
ATOM   2835 O  OD1 . ASP   A 1 384 ? -14.523 -13.647 -33.980 1.00 118.54 ? 404 ASP   A OD1 1 
ATOM   2836 O  OD2 . ASP   A 1 384 ? -14.492 -12.632 -32.041 1.00 113.33 ? 404 ASP   A OD2 1 
ATOM   2837 N  N   . PRO   A 1 385 ? -15.482 -16.198 -35.202 1.00 134.38 ? 405 PRO   A N   1 
ATOM   2838 C  CA  . PRO   A 1 385 ? -14.835 -16.692 -36.426 1.00 136.33 ? 405 PRO   A CA  1 
ATOM   2839 C  C   . PRO   A 1 385 ? -13.453 -16.105 -36.680 1.00 135.63 ? 405 PRO   A C   1 
ATOM   2840 O  O   . PRO   A 1 385 ? -12.782 -16.487 -37.646 1.00 139.36 ? 405 PRO   A O   1 
ATOM   2841 C  CB  . PRO   A 1 385 ? -15.821 -16.286 -37.525 1.00 134.11 ? 405 PRO   A CB  1 
ATOM   2842 C  CG  . PRO   A 1 385 ? -17.142 -16.226 -36.831 1.00 134.26 ? 405 PRO   A CG  1 
ATOM   2843 C  CD  . PRO   A 1 385 ? -16.839 -15.691 -35.461 1.00 132.12 ? 405 PRO   A CD  1 
ATOM   2844 N  N   . LYS   A 1 386 ? -13.014 -15.175 -35.831 1.00 122.25 ? 406 LYS   A N   1 
ATOM   2845 C  CA  . LYS   A 1 386 ? -11.651 -14.665 -35.954 1.00 119.41 ? 406 LYS   A CA  1 
ATOM   2846 C  C   . LYS   A 1 386 ? -10.646 -15.623 -35.323 1.00 118.85 ? 406 LYS   A C   1 
ATOM   2847 O  O   . LYS   A 1 386 ? -9.588  -15.890 -35.904 1.00 124.61 ? 406 LYS   A O   1 
ATOM   2848 C  CB  . LYS   A 1 386 ? -11.547 -13.267 -35.336 1.00 120.37 ? 406 LYS   A CB  1 
ATOM   2849 C  CG  . LYS   A 1 386 ? -10.266 -12.980 -34.534 1.00 120.09 ? 406 LYS   A CG  1 
ATOM   2850 C  CD  . LYS   A 1 386 ? -9.013  -12.799 -35.400 1.00 123.38 ? 406 LYS   A CD  1 
ATOM   2851 C  CE  . LYS   A 1 386 ? -7.760  -12.712 -34.528 1.00 125.13 ? 406 LYS   A CE  1 
ATOM   2852 N  NZ  . LYS   A 1 386 ? -6.528  -13.195 -35.216 1.00 136.41 ? 406 LYS   A NZ  1 
ATOM   2853 N  N   . TYR   A 1 387 ? -10.964 -16.158 -34.146 1.00 115.71 ? 407 TYR   A N   1 
ATOM   2854 C  CA  . TYR   A 1 387 ? -10.053 -17.036 -33.428 1.00 109.94 ? 407 TYR   A CA  1 
ATOM   2855 C  C   . TYR   A 1 387 ? -10.338 -18.516 -33.651 1.00 107.59 ? 407 TYR   A C   1 
ATOM   2856 O  O   . TYR   A 1 387 ? -9.520  -19.351 -33.249 1.00 108.14 ? 407 TYR   A O   1 
ATOM   2857 C  CB  . TYR   A 1 387 ? -10.100 -16.730 -31.926 1.00 110.47 ? 407 TYR   A CB  1 
ATOM   2858 C  CG  . TYR   A 1 387 ? -9.676  -15.320 -31.576 1.00 117.80 ? 407 TYR   A CG  1 
ATOM   2859 C  CD1 . TYR   A 1 387 ? -8.331  -14.975 -31.513 1.00 119.32 ? 407 TYR   A CD1 1 
ATOM   2860 C  CD2 . TYR   A 1 387 ? -10.619 -14.335 -31.305 1.00 114.26 ? 407 TYR   A CD2 1 
ATOM   2861 C  CE1 . TYR   A 1 387 ? -7.937  -13.689 -31.193 1.00 121.83 ? 407 TYR   A CE1 1 
ATOM   2862 C  CE2 . TYR   A 1 387 ? -10.234 -13.043 -30.984 1.00 111.08 ? 407 TYR   A CE2 1 
ATOM   2863 C  CZ  . TYR   A 1 387 ? -8.892  -12.728 -30.930 1.00 119.00 ? 407 TYR   A CZ  1 
ATOM   2864 O  OH  . TYR   A 1 387 ? -8.501  -11.447 -30.613 1.00 121.95 ? 407 TYR   A OH  1 
ATOM   2865 N  N   . TRP   A 1 388 ? -11.459 -18.862 -34.282 1.00 108.98 ? 408 TRP   A N   1 
ATOM   2866 C  CA  . TRP   A 1 388 ? -11.838 -20.253 -34.473 1.00 106.89 ? 408 TRP   A CA  1 
ATOM   2867 C  C   . TRP   A 1 388 ? -12.387 -20.453 -35.877 1.00 111.31 ? 408 TRP   A C   1 
ATOM   2868 O  O   . TRP   A 1 388 ? -13.160 -19.630 -36.372 1.00 114.01 ? 408 TRP   A O   1 
ATOM   2869 C  CB  . TRP   A 1 388 ? -12.891 -20.691 -33.446 1.00 101.78 ? 408 TRP   A CB  1 
ATOM   2870 C  CG  . TRP   A 1 388 ? -12.583 -20.295 -32.036 1.00 98.07  ? 408 TRP   A CG  1 
ATOM   2871 C  CD1 . TRP   A 1 388 ? -13.028 -19.184 -31.382 1.00 94.71  ? 408 TRP   A CD1 1 
ATOM   2872 C  CD2 . TRP   A 1 388 ? -11.774 -21.016 -31.100 1.00 93.77  ? 408 TRP   A CD2 1 
ATOM   2873 N  NE1 . TRP   A 1 388 ? -12.543 -19.165 -30.097 1.00 93.68  ? 408 TRP   A NE1 1 
ATOM   2874 C  CE2 . TRP   A 1 388 ? -11.771 -20.280 -29.898 1.00 93.26  ? 408 TRP   A CE2 1 
ATOM   2875 C  CE3 . TRP   A 1 388 ? -11.050 -22.211 -31.162 1.00 92.75  ? 408 TRP   A CE3 1 
ATOM   2876 C  CZ2 . TRP   A 1 388 ? -11.074 -20.700 -28.768 1.00 91.88  ? 408 TRP   A CZ2 1 
ATOM   2877 C  CZ3 . TRP   A 1 388 ? -10.358 -22.627 -30.040 1.00 89.39  ? 408 TRP   A CZ3 1 
ATOM   2878 C  CH2 . TRP   A 1 388 ? -10.375 -21.873 -28.858 1.00 90.62  ? 408 TRP   A CH2 1 
ATOM   2879 N  N   . THR   A 1 389 ? -11.986 -21.553 -36.512 1.00 104.74 ? 409 THR   A N   1 
ATOM   2880 C  CA  . THR   A 1 389 ? -12.507 -21.939 -37.817 1.00 106.50 ? 409 THR   A CA  1 
ATOM   2881 C  C   . THR   A 1 389 ? -13.735 -22.815 -37.618 1.00 108.33 ? 409 THR   A C   1 
ATOM   2882 O  O   . THR   A 1 389 ? -13.708 -23.733 -36.790 1.00 107.00 ? 409 THR   A O   1 
ATOM   2883 C  CB  . THR   A 1 389 ? -11.442 -22.687 -38.625 1.00 109.56 ? 409 THR   A CB  1 
ATOM   2884 O  OG1 . THR   A 1 389 ? -11.078 -23.887 -37.927 1.00 112.45 ? 409 THR   A OG1 1 
ATOM   2885 C  CG2 . THR   A 1 389 ? -10.203 -21.826 -38.813 1.00 105.01 ? 409 THR   A CG2 1 
ATOM   2886 N  N   . GLU   A 1 390 ? -14.795 -22.534 -38.374 1.00 114.00 ? 410 GLU   A N   1 
ATOM   2887 C  CA  . GLU   A 1 390 ? -16.070 -23.229 -38.229 1.00 115.28 ? 410 GLU   A CA  1 
ATOM   2888 C  C   . GLU   A 1 390 ? -16.479 -23.317 -36.757 1.00 113.23 ? 410 GLU   A C   1 
ATOM   2889 O  O   . GLU   A 1 390 ? -16.612 -24.420 -36.209 1.00 112.54 ? 410 GLU   A O   1 
ATOM   2890 C  CB  . GLU   A 1 390 ? -16.016 -24.617 -38.851 1.00 117.97 ? 410 GLU   A CB  1 
ATOM   2891 C  CG  . GLU   A 1 390 ? -15.679 -24.640 -40.332 1.00 119.38 ? 410 GLU   A CG  1 
ATOM   2892 C  CD  . GLU   A 1 390 ? -15.666 -26.045 -40.897 1.00 127.67 ? 410 GLU   A CD  1 
ATOM   2893 O  OE1 . GLU   A 1 390 ? -16.335 -26.928 -40.320 1.00 130.06 ? 410 GLU   A OE1 1 
ATOM   2894 O  OE2 . GLU   A 1 390 ? -14.980 -26.267 -41.916 1.00 135.01 ? 410 GLU   A OE2 1 
ATOM   2895 N  N   . PRO   A 1 391 ? -16.676 -22.180 -36.085 1.00 111.11 ? 411 PRO   A N   1 
ATOM   2896 C  CA  . PRO   A 1 391 ? -16.826 -22.208 -34.619 1.00 108.36 ? 411 PRO   A CA  1 
ATOM   2897 C  C   . PRO   A 1 391 ? -18.031 -22.997 -34.130 1.00 108.00 ? 411 PRO   A C   1 
ATOM   2898 O  O   . PRO   A 1 391 ? -18.044 -23.420 -32.967 1.00 104.50 ? 411 PRO   A O   1 
ATOM   2899 C  CB  . PRO   A 1 391 ? -16.944 -20.721 -34.251 1.00 105.93 ? 411 PRO   A CB  1 
ATOM   2900 C  CG  . PRO   A 1 391 ? -17.503 -20.083 -35.475 1.00 110.40 ? 411 PRO   A CG  1 
ATOM   2901 C  CD  . PRO   A 1 391 ? -16.911 -20.832 -36.638 1.00 111.54 ? 411 PRO   A CD  1 
ATOM   2902 N  N   . GLU   A 1 392 ? -19.037 -23.214 -34.974 1.00 108.70 ? 412 GLU   A N   1 
ATOM   2903 C  CA  . GLU   A 1 392 ? -20.237 -23.947 -34.598 1.00 108.66 ? 412 GLU   A CA  1 
ATOM   2904 C  C   . GLU   A 1 392 ? -20.074 -25.456 -34.714 1.00 106.88 ? 412 GLU   A C   1 
ATOM   2905 O  O   . GLU   A 1 392 ? -21.077 -26.179 -34.691 1.00 110.11 ? 412 GLU   A O   1 
ATOM   2906 C  CB  . GLU   A 1 392 ? -21.420 -23.484 -35.454 1.00 111.86 ? 412 GLU   A CB  1 
ATOM   2907 C  CG  . GLU   A 1 392 ? -21.714 -21.994 -35.355 1.00 115.20 ? 412 GLU   A CG  1 
ATOM   2908 C  CD  . GLU   A 1 392 ? -22.290 -21.604 -34.009 1.00 121.48 ? 412 GLU   A CD  1 
ATOM   2909 O  OE1 . GLU   A 1 392 ? -23.184 -22.324 -33.514 1.00 117.96 ? 412 GLU   A OE1 1 
ATOM   2910 O  OE2 . GLU   A 1 392 ? -21.847 -20.581 -33.443 1.00 118.78 ? 412 GLU   A OE2 1 
ATOM   2911 N  N   . LYS   A 1 393 ? -18.848 -25.954 -34.833 1.00 104.28 ? 413 LYS   A N   1 
ATOM   2912 C  CA  . LYS   A 1 393 ? -18.608 -27.361 -35.113 1.00 101.59 ? 413 LYS   A CA  1 
ATOM   2913 C  C   . LYS   A 1 393 ? -17.770 -27.990 -34.008 1.00 100.80 ? 413 LYS   A C   1 
ATOM   2914 O  O   . LYS   A 1 393 ? -16.824 -27.376 -33.503 1.00 102.17 ? 413 LYS   A O   1 
ATOM   2915 C  CB  . LYS   A 1 393 ? -17.920 -27.535 -36.472 1.00 106.03 ? 413 LYS   A CB  1 
ATOM   2916 C  CG  . LYS   A 1 393 ? -18.334 -28.794 -37.213 1.00 108.10 ? 413 LYS   A CG  1 
ATOM   2917 C  CD  . LYS   A 1 393 ? -19.816 -29.076 -37.018 1.00 111.47 ? 413 LYS   A CD  1 
ATOM   2918 C  CE  . LYS   A 1 393 ? -20.017 -30.414 -36.326 1.00 108.90 ? 413 LYS   A CE  1 
ATOM   2919 N  NZ  . LYS   A 1 393 ? -21.386 -30.570 -35.766 1.00 102.64 ? 413 LYS   A NZ  1 
ATOM   2920 N  N   . PHE   A 1 394 ? -18.131 -29.221 -33.642 1.00 94.86  ? 414 PHE   A N   1 
ATOM   2921 C  CA  . PHE   A 1 394 ? -17.431 -30.002 -32.623 1.00 92.17  ? 414 PHE   A CA  1 
ATOM   2922 C  C   . PHE   A 1 394 ? -16.237 -30.681 -33.285 1.00 87.87  ? 414 PHE   A C   1 
ATOM   2923 O  O   . PHE   A 1 394 ? -16.343 -31.769 -33.854 1.00 88.90  ? 414 PHE   A O   1 
ATOM   2924 C  CB  . PHE   A 1 394 ? -18.377 -31.015 -31.987 1.00 91.46  ? 414 PHE   A CB  1 
ATOM   2925 C  CG  . PHE   A 1 394 ? -17.755 -31.824 -30.884 1.00 89.76  ? 414 PHE   A CG  1 
ATOM   2926 C  CD1 . PHE   A 1 394 ? -17.570 -31.278 -29.626 1.00 83.33  ? 414 PHE   A CD1 1 
ATOM   2927 C  CD2 . PHE   A 1 394 ? -17.372 -33.139 -31.103 1.00 87.90  ? 414 PHE   A CD2 1 
ATOM   2928 C  CE1 . PHE   A 1 394 ? -17.000 -32.020 -28.605 1.00 83.76  ? 414 PHE   A CE1 1 
ATOM   2929 C  CE2 . PHE   A 1 394 ? -16.805 -33.890 -30.088 1.00 90.30  ? 414 PHE   A CE2 1 
ATOM   2930 C  CZ  . PHE   A 1 394 ? -16.618 -33.329 -28.836 1.00 87.44  ? 414 PHE   A CZ  1 
ATOM   2931 N  N   . LEU   A 1 395 ? -15.081 -30.021 -33.214 1.00 85.56  ? 415 LEU   A N   1 
ATOM   2932 C  CA  . LEU   A 1 395 ? -13.858 -30.465 -33.882 1.00 86.10  ? 415 LEU   A CA  1 
ATOM   2933 C  C   . LEU   A 1 395 ? -12.739 -30.578 -32.854 1.00 85.91  ? 415 LEU   A C   1 
ATOM   2934 O  O   . LEU   A 1 395 ? -11.911 -29.667 -32.723 1.00 82.56  ? 415 LEU   A O   1 
ATOM   2935 C  CB  . LEU   A 1 395 ? -13.478 -29.505 -35.010 1.00 83.23  ? 415 LEU   A CB  1 
ATOM   2936 C  CG  . LEU   A 1 395 ? -14.492 -29.402 -36.148 1.00 88.46  ? 415 LEU   A CG  1 
ATOM   2937 C  CD1 . LEU   A 1 395 ? -14.148 -28.242 -37.061 1.00 98.06  ? 415 LEU   A CD1 1 
ATOM   2938 C  CD2 . LEU   A 1 395 ? -14.535 -30.706 -36.932 1.00 85.72  ? 415 LEU   A CD2 1 
ATOM   2939 N  N   . PRO   A 1 396 ? -12.675 -31.693 -32.120 1.00 86.53  ? 416 PRO   A N   1 
ATOM   2940 C  CA  . PRO   A 1 396 ? -11.665 -31.821 -31.052 1.00 83.94  ? 416 PRO   A CA  1 
ATOM   2941 C  C   . PRO   A 1 396 ? -10.232 -31.591 -31.509 1.00 89.73  ? 416 PRO   A C   1 
ATOM   2942 O  O   . PRO   A 1 396 ? -9.392  -31.217 -30.681 1.00 88.70  ? 416 PRO   A O   1 
ATOM   2943 C  CB  . PRO   A 1 396 ? -11.866 -33.259 -30.553 1.00 81.93  ? 416 PRO   A CB  1 
ATOM   2944 C  CG  . PRO   A 1 396 ? -13.285 -33.571 -30.886 1.00 84.10  ? 416 PRO   A CG  1 
ATOM   2945 C  CD  . PRO   A 1 396 ? -13.565 -32.865 -32.182 1.00 85.19  ? 416 PRO   A CD  1 
ATOM   2946 N  N   . GLU   A 1 397 ? -9.921  -31.784 -32.792 1.00 87.99  ? 417 GLU   A N   1 
ATOM   2947 C  CA  . GLU   A 1 397 ? -8.572  -31.526 -33.278 1.00 87.27  ? 417 GLU   A CA  1 
ATOM   2948 C  C   . GLU   A 1 397 ? -8.148  -30.072 -33.103 1.00 89.38  ? 417 GLU   A C   1 
ATOM   2949 O  O   . GLU   A 1 397 ? -6.953  -29.780 -33.239 1.00 90.93  ? 417 GLU   A O   1 
ATOM   2950 C  CB  . GLU   A 1 397 ? -8.461  -31.936 -34.749 1.00 90.28  ? 417 GLU   A CB  1 
ATOM   2951 C  CG  . GLU   A 1 397 ? -8.731  -33.414 -34.991 1.00 93.65  ? 417 GLU   A CG  1 
ATOM   2952 C  CD  . GLU   A 1 397 ? -7.674  -34.311 -34.372 1.00 94.64  ? 417 GLU   A CD  1 
ATOM   2953 O  OE1 . GLU   A 1 397 ? -6.525  -33.850 -34.204 1.00 97.19  ? 417 GLU   A OE1 1 
ATOM   2954 O  OE2 . GLU   A 1 397 ? -7.990  -35.479 -34.058 1.00 95.98  ? 417 GLU   A OE2 1 
ATOM   2955 N  N   . ARG   A 1 398 ? -9.085  -29.161 -32.808 1.00 92.12  ? 418 ARG   A N   1 
ATOM   2956 C  CA  . ARG   A 1 398 ? -8.702  -27.810 -32.403 1.00 87.36  ? 418 ARG   A CA  1 
ATOM   2957 C  C   . ARG   A 1 398 ? -7.643  -27.836 -31.316 1.00 92.93  ? 418 ARG   A C   1 
ATOM   2958 O  O   . ARG   A 1 398 ? -6.732  -27.003 -31.306 1.00 97.17  ? 418 ARG   A O   1 
ATOM   2959 C  CB  . ARG   A 1 398 ? -9.922  -27.035 -31.890 1.00 87.21  ? 418 ARG   A CB  1 
ATOM   2960 C  CG  . ARG   A 1 398 ? -10.991 -26.738 -32.906 1.00 88.05  ? 418 ARG   A CG  1 
ATOM   2961 C  CD  . ARG   A 1 398 ? -12.077 -25.899 -32.261 1.00 81.44  ? 418 ARG   A CD  1 
ATOM   2962 N  NE  . ARG   A 1 398 ? -13.335 -25.957 -32.993 1.00 85.15  ? 418 ARG   A NE  1 
ATOM   2963 C  CZ  . ARG   A 1 398 ? -13.603 -25.241 -34.076 1.00 94.80  ? 418 ARG   A CZ  1 
ATOM   2964 N  NH1 . ARG   A 1 398 ? -12.708 -24.420 -34.599 1.00 98.64  ? 418 ARG   A NH1 1 
ATOM   2965 N  NH2 . ARG   A 1 398 ? -14.798 -25.355 -34.649 1.00 100.96 ? 418 ARG   A NH2 1 
ATOM   2966 N  N   . PHE   A 1 399 ? -7.746  -28.785 -30.387 1.00 94.55  ? 419 PHE   A N   1 
ATOM   2967 C  CA  . PHE   A 1 399 ? -6.889  -28.831 -29.215 1.00 91.93  ? 419 PHE   A CA  1 
ATOM   2968 C  C   . PHE   A 1 399 ? -5.814  -29.904 -29.304 1.00 95.14  ? 419 PHE   A C   1 
ATOM   2969 O  O   . PHE   A 1 399 ? -5.211  -30.246 -28.282 1.00 96.40  ? 419 PHE   A O   1 
ATOM   2970 C  CB  . PHE   A 1 399 ? -7.734  -29.037 -27.961 1.00 78.42  ? 419 PHE   A CB  1 
ATOM   2971 C  CG  . PHE   A 1 399 ? -8.673  -27.901 -27.676 1.00 82.79  ? 419 PHE   A CG  1 
ATOM   2972 C  CD1 . PHE   A 1 399 ? -9.952  -27.888 -28.205 1.00 82.18  ? 419 PHE   A CD1 1 
ATOM   2973 C  CD2 . PHE   A 1 399 ? -8.268  -26.840 -26.885 1.00 82.40  ? 419 PHE   A CD2 1 
ATOM   2974 C  CE1 . PHE   A 1 399 ? -10.811 -26.837 -27.948 1.00 77.92  ? 419 PHE   A CE1 1 
ATOM   2975 C  CE2 . PHE   A 1 399 ? -9.119  -25.789 -26.625 1.00 76.06  ? 419 PHE   A CE2 1 
ATOM   2976 C  CZ  . PHE   A 1 399 ? -10.394 -25.787 -27.156 1.00 74.76  ? 419 PHE   A CZ  1 
ATOM   2977 N  N   . SER   A 1 400 ? -5.559  -30.438 -30.495 1.00 97.73  ? 420 SER   A N   1 
ATOM   2978 C  CA  . SER   A 1 400 ? -4.454  -31.367 -30.653 1.00 102.20 ? 420 SER   A CA  1 
ATOM   2979 C  C   . SER   A 1 400 ? -3.141  -30.654 -30.351 1.00 109.24 ? 420 SER   A C   1 
ATOM   2980 O  O   . SER   A 1 400 ? -3.030  -29.429 -30.453 1.00 108.53 ? 420 SER   A O   1 
ATOM   2981 C  CB  . SER   A 1 400 ? -4.437  -31.956 -32.064 1.00 98.56  ? 420 SER   A CB  1 
ATOM   2982 O  OG  . SER   A 1 400 ? -4.079  -30.980 -33.025 1.00 103.54 ? 420 SER   A OG  1 
ATOM   2983 N  N   . LYS   A 1 401 ? -2.136  -31.444 -29.965 1.00 108.80 ? 421 LYS   A N   1 
ATOM   2984 C  CA  . LYS   A 1 401 ? -0.874  -30.876 -29.503 1.00 112.49 ? 421 LYS   A CA  1 
ATOM   2985 C  C   . LYS   A 1 401 ? -0.209  -29.996 -30.554 1.00 112.41 ? 421 LYS   A C   1 
ATOM   2986 O  O   . LYS   A 1 401 ? 0.584   -29.119 -30.198 1.00 117.56 ? 421 LYS   A O   1 
ATOM   2987 C  CB  . LYS   A 1 401 ? 0.070   -31.998 -29.071 1.00 119.20 ? 421 LYS   A CB  1 
ATOM   2988 C  CG  . LYS   A 1 401 ? 0.729   -31.764 -27.719 1.00 121.67 ? 421 LYS   A CG  1 
ATOM   2989 C  CD  . LYS   A 1 401 ? 0.910   -33.070 -26.957 1.00 123.25 ? 421 LYS   A CD  1 
ATOM   2990 C  CE  . LYS   A 1 401 ? 1.706   -34.084 -27.764 1.00 126.81 ? 421 LYS   A CE  1 
ATOM   2991 N  NZ  . LYS   A 1 401 ? 1.861   -35.373 -27.033 1.00 129.77 ? 421 LYS   A NZ  1 
ATOM   2992 N  N   . LYS   A 1 402 ? -0.523  -30.199 -31.834 1.00 111.21 ? 422 LYS   A N   1 
ATOM   2993 C  CA  . LYS   A 1 402 ? 0.031   -29.369 -32.895 1.00 111.10 ? 422 LYS   A CA  1 
ATOM   2994 C  C   . LYS   A 1 402 ? -0.758  -28.086 -33.123 1.00 108.18 ? 422 LYS   A C   1 
ATOM   2995 O  O   . LYS   A 1 402 ? -0.269  -27.195 -33.826 1.00 108.17 ? 422 LYS   A O   1 
ATOM   2996 C  CB  . LYS   A 1 402 ? 0.092   -30.166 -34.201 1.00 109.38 ? 422 LYS   A CB  1 
ATOM   2997 C  CG  . LYS   A 1 402 ? -1.265  -30.363 -34.857 1.00 105.11 ? 422 LYS   A CG  1 
ATOM   2998 C  CD  . LYS   A 1 402 ? -1.203  -31.340 -36.020 1.00 106.47 ? 422 LYS   A CD  1 
ATOM   2999 C  CE  . LYS   A 1 402 ? -0.069  -31.000 -36.975 1.00 115.04 ? 422 LYS   A CE  1 
ATOM   3000 N  NZ  . LYS   A 1 402 ? -0.174  -29.603 -37.478 1.00 119.40 ? 422 LYS   A NZ  1 
ATOM   3001 N  N   . ASN   A 1 403 ? -1.960  -27.967 -32.552 1.00 113.48 ? 423 ASN   A N   1 
ATOM   3002 C  CA  . ASN   A 1 403 ? -2.814  -26.809 -32.769 1.00 109.42 ? 423 ASN   A CA  1 
ATOM   3003 C  C   . ASN   A 1 403 ? -3.149  -26.034 -31.502 1.00 112.34 ? 423 ASN   A C   1 
ATOM   3004 O  O   . ASN   A 1 403 ? -3.646  -24.907 -31.609 1.00 116.99 ? 423 ASN   A O   1 
ATOM   3005 C  CB  . ASN   A 1 403 ? -4.126  -27.231 -33.452 1.00 104.64 ? 423 ASN   A CB  1 
ATOM   3006 C  CG  . ASN   A 1 403 ? -3.921  -27.683 -34.886 1.00 106.61 ? 423 ASN   A CG  1 
ATOM   3007 O  OD1 . ASN   A 1 403 ? -2.813  -27.609 -35.418 1.00 111.43 ? 423 ASN   A OD1 1 
ATOM   3008 N  ND2 . ASN   A 1 403 ? -4.987  -28.159 -35.516 1.00 103.71 ? 423 ASN   A ND2 1 
ATOM   3009 N  N   . LYS   A 1 404 ? -2.894  -26.591 -30.315 1.00 110.62 ? 424 LYS   A N   1 
ATOM   3010 C  CA  . LYS   A 1 404 ? -3.212  -25.894 -29.073 1.00 115.65 ? 424 LYS   A CA  1 
ATOM   3011 C  C   . LYS   A 1 404 ? -2.314  -24.686 -28.823 1.00 122.99 ? 424 LYS   A C   1 
ATOM   3012 O  O   . LYS   A 1 404 ? -2.736  -23.758 -28.123 1.00 117.14 ? 424 LYS   A O   1 
ATOM   3013 C  CB  . LYS   A 1 404 ? -3.122  -26.867 -27.892 1.00 115.00 ? 424 LYS   A CB  1 
ATOM   3014 C  CG  . LYS   A 1 404 ? -1.933  -27.810 -27.947 1.00 110.42 ? 424 LYS   A CG  1 
ATOM   3015 C  CD  . LYS   A 1 404 ? -1.933  -28.759 -26.764 1.00 117.89 ? 424 LYS   A CD  1 
ATOM   3016 C  CE  . LYS   A 1 404 ? -1.367  -28.084 -25.529 1.00 122.39 ? 424 LYS   A CE  1 
ATOM   3017 N  NZ  . LYS   A 1 404 ? -1.498  -28.936 -24.316 1.00 121.57 ? 424 LYS   A NZ  1 
ATOM   3018 N  N   . ASP   A 1 405 ? -1.096  -24.674 -29.376 1.00 136.19 ? 425 ASP   A N   1 
ATOM   3019 C  CA  . ASP   A 1 405 ? -0.208  -23.522 -29.241 1.00 135.43 ? 425 ASP   A CA  1 
ATOM   3020 C  C   . ASP   A 1 405 ? -0.767  -22.279 -29.918 1.00 135.84 ? 425 ASP   A C   1 
ATOM   3021 O  O   . ASP   A 1 405 ? -0.308  -21.167 -29.635 1.00 132.08 ? 425 ASP   A O   1 
ATOM   3022 C  CB  . ASP   A 1 405 ? 1.166   -23.853 -29.827 1.00 135.72 ? 425 ASP   A CB  1 
ATOM   3023 C  CG  . ASP   A 1 405 ? 1.077   -24.457 -31.220 1.00 136.54 ? 425 ASP   A CG  1 
ATOM   3024 O  OD1 . ASP   A 1 405 ? 0.480   -23.822 -32.116 1.00 137.98 ? 425 ASP   A OD1 1 
ATOM   3025 O  OD2 . ASP   A 1 405 ? 1.607   -25.570 -31.421 1.00 139.71 ? 425 ASP   A OD2 1 
ATOM   3026 N  N   . ASN   A 1 406 ? -1.728  -22.455 -30.822 1.00 126.85 ? 426 ASN   A N   1 
ATOM   3027 C  CA  . ASN   A 1 406 ? -2.388  -21.364 -31.525 1.00 124.85 ? 426 ASN   A CA  1 
ATOM   3028 C  C   . ASN   A 1 406 ? -3.474  -20.708 -30.672 1.00 122.50 ? 426 ASN   A C   1 
ATOM   3029 O  O   . ASN   A 1 406 ? -3.755  -19.518 -30.849 1.00 124.54 ? 426 ASN   A O   1 
ATOM   3030 C  CB  . ASN   A 1 406 ? -2.922  -21.942 -32.849 1.00 127.40 ? 426 ASN   A CB  1 
ATOM   3031 C  CG  . ASN   A 1 406 ? -4.024  -21.114 -33.501 1.00 142.22 ? 426 ASN   A CG  1 
ATOM   3032 O  OD1 . ASN   A 1 406 ? -4.109  -19.897 -33.350 1.00 153.65 ? 426 ASN   A OD1 1 
ATOM   3033 N  ND2 . ASN   A 1 406 ? -4.864  -21.794 -34.277 1.00 143.05 ? 426 ASN   A ND2 1 
ATOM   3034 N  N   . ILE   A 1 407 ? -4.033  -21.436 -29.706 1.00 122.06 ? 427 ILE   A N   1 
ATOM   3035 C  CA  . ILE   A 1 407 ? -5.162  -20.942 -28.925 1.00 109.45 ? 427 ILE   A CA  1 
ATOM   3036 C  C   . ILE   A 1 407 ? -4.683  -19.898 -27.923 1.00 104.54 ? 427 ILE   A C   1 
ATOM   3037 O  O   . ILE   A 1 407 ? -3.784  -20.153 -27.113 1.00 104.30 ? 427 ILE   A O   1 
ATOM   3038 C  CB  . ILE   A 1 407 ? -5.875  -22.103 -28.220 1.00 102.95 ? 427 ILE   A CB  1 
ATOM   3039 C  CG1 . ILE   A 1 407 ? -6.665  -22.926 -29.241 1.00 101.55 ? 427 ILE   A CG1 1 
ATOM   3040 C  CG2 . ILE   A 1 407 ? -6.770  -21.587 -27.100 1.00 96.39  ? 427 ILE   A CG2 1 
ATOM   3041 C  CD1 . ILE   A 1 407 ? -6.656  -24.412 -28.972 1.00 98.86  ? 427 ILE   A CD1 1 
ATOM   3042 N  N   . ASP   A 1 408 ? -5.295  -18.716 -27.969 1.00 94.91  ? 428 ASP   A N   1 
ATOM   3043 C  CA  . ASP   A 1 408 ? -4.986  -17.658 -27.008 1.00 90.55  ? 428 ASP   A CA  1 
ATOM   3044 C  C   . ASP   A 1 408 ? -5.624  -17.989 -25.664 1.00 92.84  ? 428 ASP   A C   1 
ATOM   3045 O  O   . ASP   A 1 408 ? -6.829  -18.261 -25.606 1.00 84.13  ? 428 ASP   A O   1 
ATOM   3046 C  CB  . ASP   A 1 408 ? -5.495  -16.311 -27.523 1.00 86.49  ? 428 ASP   A CB  1 
ATOM   3047 C  CG  . ASP   A 1 408 ? -4.989  -15.131 -26.703 1.00 90.26  ? 428 ASP   A CG  1 
ATOM   3048 O  OD1 . ASP   A 1 408 ? -5.238  -15.083 -25.480 1.00 87.05  ? 428 ASP   A OD1 1 
ATOM   3049 O  OD2 . ASP   A 1 408 ? -4.334  -14.245 -27.290 1.00 95.88  ? 428 ASP   A OD2 1 
ATOM   3050 N  N   . PRO   A 1 409 ? -4.865  -17.964 -24.564 1.00 97.68  ? 429 PRO   A N   1 
ATOM   3051 C  CA  . PRO   A 1 409 ? -5.432  -18.355 -23.265 1.00 89.59  ? 429 PRO   A CA  1 
ATOM   3052 C  C   . PRO   A 1 409 ? -6.434  -17.361 -22.705 1.00 87.46  ? 429 PRO   A C   1 
ATOM   3053 O  O   . PRO   A 1 409 ? -7.002  -17.610 -21.635 1.00 88.37  ? 429 PRO   A O   1 
ATOM   3054 C  CB  . PRO   A 1 409 ? -4.193  -18.452 -22.366 1.00 83.15  ? 429 PRO   A CB  1 
ATOM   3055 C  CG  . PRO   A 1 409 ? -3.237  -17.494 -22.964 1.00 89.12  ? 429 PRO   A CG  1 
ATOM   3056 C  CD  . PRO   A 1 409 ? -3.451  -17.572 -24.453 1.00 90.16  ? 429 PRO   A CD  1 
ATOM   3057 N  N   . TYR   A 1 410 ? -6.669  -16.248 -23.393 1.00 84.59  ? 430 TYR   A N   1 
ATOM   3058 C  CA  . TYR   A 1 410 ? -7.619  -15.246 -22.941 1.00 86.63  ? 430 TYR   A CA  1 
ATOM   3059 C  C   . TYR   A 1 410 ? -8.824  -15.130 -23.861 1.00 83.84  ? 430 TYR   A C   1 
ATOM   3060 O  O   . TYR   A 1 410 ? -9.736  -14.347 -23.573 1.00 84.02  ? 430 TYR   A O   1 
ATOM   3061 C  CB  . TYR   A 1 410 ? -6.911  -13.899 -22.790 1.00 85.82  ? 430 TYR   A CB  1 
ATOM   3062 C  CG  . TYR   A 1 410 ? -5.791  -13.973 -21.780 1.00 90.47  ? 430 TYR   A CG  1 
ATOM   3063 C  CD1 . TYR   A 1 410 ? -6.043  -13.808 -20.425 1.00 93.92  ? 430 TYR   A CD1 1 
ATOM   3064 C  CD2 . TYR   A 1 410 ? -4.487  -14.244 -22.179 1.00 93.92  ? 430 TYR   A CD2 1 
ATOM   3065 C  CE1 . TYR   A 1 410 ? -5.023  -13.890 -19.496 1.00 95.11  ? 430 TYR   A CE1 1 
ATOM   3066 C  CE2 . TYR   A 1 410 ? -3.462  -14.328 -21.258 1.00 92.19  ? 430 TYR   A CE2 1 
ATOM   3067 C  CZ  . TYR   A 1 410 ? -3.735  -14.150 -19.920 1.00 94.53  ? 430 TYR   A CZ  1 
ATOM   3068 O  OH  . TYR   A 1 410 ? -2.711  -14.236 -19.007 1.00 92.35  ? 430 TYR   A OH  1 
ATOM   3069 N  N   . ILE   A 1 411 ? -8.851  -15.885 -24.956 1.00 86.32  ? 431 ILE   A N   1 
ATOM   3070 C  CA  . ILE   A 1 411 ? -10.083 -16.079 -25.707 1.00 86.87  ? 431 ILE   A CA  1 
ATOM   3071 C  C   . ILE   A 1 411 ? -10.824 -17.315 -25.204 1.00 84.50  ? 431 ILE   A C   1 
ATOM   3072 O  O   . ILE   A 1 411 ? -12.059 -17.327 -25.169 1.00 83.22  ? 431 ILE   A O   1 
ATOM   3073 C  CB  . ILE   A 1 411 ? -9.791  -16.188 -27.213 1.00 90.59  ? 431 ILE   A CB  1 
ATOM   3074 C  CG1 . ILE   A 1 411 ? -8.896  -15.037 -27.680 1.00 94.23  ? 431 ILE   A CG1 1 
ATOM   3075 C  CG2 . ILE   A 1 411 ? -11.087 -16.205 -28.011 1.00 87.39  ? 431 ILE   A CG2 1 
ATOM   3076 C  CD1 . ILE   A 1 411 ? -9.502  -13.664 -27.485 1.00 96.13  ? 431 ILE   A CD1 1 
ATOM   3077 N  N   . TYR   A 1 412 ? -10.086 -18.344 -24.790 1.00 84.26  ? 432 TYR   A N   1 
ATOM   3078 C  CA  . TYR   A 1 412 ? -10.640 -19.607 -24.313 1.00 83.00  ? 432 TYR   A CA  1 
ATOM   3079 C  C   . TYR   A 1 412 ? -10.444 -19.667 -22.800 1.00 82.27  ? 432 TYR   A C   1 
ATOM   3080 O  O   . TYR   A 1 412 ? -9.379  -20.064 -22.317 1.00 82.99  ? 432 TYR   A O   1 
ATOM   3081 C  CB  . TYR   A 1 412 ? -9.967  -20.788 -25.016 1.00 80.65  ? 432 TYR   A CB  1 
ATOM   3082 C  CG  . TYR   A 1 412 ? -10.511 -22.129 -24.589 1.00 80.78  ? 432 TYR   A CG  1 
ATOM   3083 C  CD1 . TYR   A 1 412 ? -11.824 -22.478 -24.862 1.00 74.22  ? 432 TYR   A CD1 1 
ATOM   3084 C  CD2 . TYR   A 1 412 ? -9.716  -23.045 -23.913 1.00 76.26  ? 432 TYR   A CD2 1 
ATOM   3085 C  CE1 . TYR   A 1 412 ? -12.332 -23.694 -24.473 1.00 74.55  ? 432 TYR   A CE1 1 
ATOM   3086 C  CE2 . TYR   A 1 412 ? -10.218 -24.271 -23.521 1.00 72.98  ? 432 TYR   A CE2 1 
ATOM   3087 C  CZ  . TYR   A 1 412 ? -11.528 -24.586 -23.805 1.00 69.19  ? 432 TYR   A CZ  1 
ATOM   3088 O  OH  . TYR   A 1 412 ? -12.046 -25.799 -23.422 1.00 69.05  ? 432 TYR   A OH  1 
ATOM   3089 N  N   . THR   A 1 413 ? -11.473 -19.271 -22.052 1.00 85.85  ? 433 THR   A N   1 
ATOM   3090 C  CA  . THR   A 1 413 ? -11.412 -19.191 -20.592 1.00 87.11  ? 433 THR   A CA  1 
ATOM   3091 C  C   . THR   A 1 413 ? -12.620 -19.889 -19.975 1.00 85.57  ? 433 THR   A C   1 
ATOM   3092 O  O   . THR   A 1 413 ? -13.475 -19.241 -19.359 1.00 82.19  ? 433 THR   A O   1 
ATOM   3093 C  CB  . THR   A 1 413 ? -11.347 -17.736 -20.122 1.00 84.75  ? 433 THR   A CB  1 
ATOM   3094 O  OG1 . THR   A 1 413 ? -12.537 -17.049 -20.530 1.00 80.55  ? 433 THR   A OG1 1 
ATOM   3095 C  CG2 . THR   A 1 413 ? -10.120 -17.026 -20.700 1.00 80.40  ? 433 THR   A CG2 1 
ATOM   3096 N  N   . PRO   A 1 414 ? -12.712 -21.218 -20.100 1.00 83.45  ? 434 PRO   A N   1 
ATOM   3097 C  CA  . PRO   A 1 414 ? -13.816 -21.934 -19.442 1.00 82.11  ? 434 PRO   A CA  1 
ATOM   3098 C  C   . PRO   A 1 414 ? -13.686 -21.979 -17.928 1.00 77.81  ? 434 PRO   A C   1 
ATOM   3099 O  O   . PRO   A 1 414 ? -14.666 -22.315 -17.247 1.00 75.13  ? 434 PRO   A O   1 
ATOM   3100 C  CB  . PRO   A 1 414 ? -13.739 -23.336 -20.050 1.00 75.28  ? 434 PRO   A CB  1 
ATOM   3101 C  CG  . PRO   A 1 414 ? -12.294 -23.500 -20.382 1.00 78.12  ? 434 PRO   A CG  1 
ATOM   3102 C  CD  . PRO   A 1 414 ? -11.798 -22.138 -20.797 1.00 75.47  ? 434 PRO   A CD  1 
ATOM   3103 N  N   . PHE   A 1 415 ? -12.511 -21.661 -17.381 1.00 80.36  ? 435 PHE   A N   1 
ATOM   3104 C  CA  . PHE   A 1 415 ? -12.288 -21.629 -15.941 1.00 80.65  ? 435 PHE   A CA  1 
ATOM   3105 C  C   . PHE   A 1 415 ? -11.836 -20.251 -15.472 1.00 77.64  ? 435 PHE   A C   1 
ATOM   3106 O  O   . PHE   A 1 415 ? -11.291 -20.119 -14.370 1.00 73.98  ? 435 PHE   A O   1 
ATOM   3107 C  CB  . PHE   A 1 415 ? -11.264 -22.691 -15.533 1.00 74.43  ? 435 PHE   A CB  1 
ATOM   3108 C  CG  . PHE   A 1 415 ? -11.715 -24.103 -15.793 1.00 81.09  ? 435 PHE   A CG  1 
ATOM   3109 C  CD1 . PHE   A 1 415 ? -12.511 -24.769 -14.872 1.00 77.72  ? 435 PHE   A CD1 1 
ATOM   3110 C  CD2 . PHE   A 1 415 ? -11.342 -24.764 -16.955 1.00 76.96  ? 435 PHE   A CD2 1 
ATOM   3111 C  CE1 . PHE   A 1 415 ? -12.927 -26.069 -15.107 1.00 81.06  ? 435 PHE   A CE1 1 
ATOM   3112 C  CE2 . PHE   A 1 415 ? -11.755 -26.065 -17.196 1.00 72.76  ? 435 PHE   A CE2 1 
ATOM   3113 C  CZ  . PHE   A 1 415 ? -12.547 -26.718 -16.270 1.00 81.43  ? 435 PHE   A CZ  1 
ATOM   3114 N  N   . GLY   A 1 416 ? -12.060 -19.221 -16.287 1.00 79.27  ? 436 GLY   A N   1 
ATOM   3115 C  CA  . GLY   A 1 416 ? -11.536 -17.916 -15.973 1.00 73.27  ? 436 GLY   A CA  1 
ATOM   3116 C  C   . GLY   A 1 416 ? -10.024 -17.920 -16.099 1.00 75.31  ? 436 GLY   A C   1 
ATOM   3117 O  O   . GLY   A 1 416 ? -9.420  -18.768 -16.767 1.00 72.69  ? 436 GLY   A O   1 
ATOM   3118 N  N   . SER   A 1 417 ? -9.409  -16.946 -15.436 1.00 73.46  ? 437 SER   A N   1 
ATOM   3119 C  CA  . SER   A 1 417 ? -7.958  -16.848 -15.406 1.00 74.23  ? 437 SER   A CA  1 
ATOM   3120 C  C   . SER   A 1 417 ? -7.577  -15.915 -14.268 1.00 79.20  ? 437 SER   A C   1 
ATOM   3121 O  O   . SER   A 1 417 ? -8.423  -15.220 -13.698 1.00 80.48  ? 437 SER   A O   1 
ATOM   3122 C  CB  . SER   A 1 417 ? -7.401  -16.356 -16.747 1.00 77.56  ? 437 SER   A CB  1 
ATOM   3123 O  OG  . SER   A 1 417 ? -6.033  -16.704 -16.894 1.00 86.32  ? 437 SER   A OG  1 
ATOM   3124 N  N   . GLY   A 1 418 ? -6.293  -15.916 -13.936 1.00 80.53  ? 438 GLY   A N   1 
ATOM   3125 C  CA  . GLY   A 1 418 ? -5.786  -15.047 -12.906 1.00 83.33  ? 438 GLY   A CA  1 
ATOM   3126 C  C   . GLY   A 1 418 ? -6.098  -15.548 -11.511 1.00 83.97  ? 438 GLY   A C   1 
ATOM   3127 O  O   . GLY   A 1 418 ? -6.677  -16.625 -11.322 1.00 77.99  ? 438 GLY   A O   1 
ATOM   3128 N  N   . PRO   A 1 419 ? -5.726  -14.755 -10.504 1.00 86.40  ? 439 PRO   A N   1 
ATOM   3129 C  CA  . PRO   A 1 419 ? -5.862  -15.212 -9.109  1.00 87.74  ? 439 PRO   A CA  1 
ATOM   3130 C  C   . PRO   A 1 419 ? -7.279  -15.608 -8.709  1.00 82.74  ? 439 PRO   A C   1 
ATOM   3131 O  O   . PRO   A 1 419 ? -7.446  -16.287 -7.688  1.00 84.20  ? 439 PRO   A O   1 
ATOM   3132 C  CB  . PRO   A 1 419 ? -5.368  -14.004 -8.296  1.00 89.04  ? 439 PRO   A CB  1 
ATOM   3133 C  CG  . PRO   A 1 419 ? -4.504  -13.237 -9.238  1.00 89.74  ? 439 PRO   A CG  1 
ATOM   3134 C  CD  . PRO   A 1 419 ? -5.093  -13.428 -10.600 1.00 88.12  ? 439 PRO   A CD  1 
ATOM   3135 N  N   . ARG   A 1 420 ? -8.304  -15.223 -9.472  1.00 77.78  ? 440 ARG   A N   1 
ATOM   3136 C  CA  . ARG   A 1 420 ? -9.685  -15.526 -9.119  1.00 82.99  ? 440 ARG   A CA  1 
ATOM   3137 C  C   . ARG   A 1 420 ? -10.337 -16.483 -10.114 1.00 80.17  ? 440 ARG   A C   1 
ATOM   3138 O  O   . ARG   A 1 420 ? -11.557 -16.461 -10.304 1.00 74.72  ? 440 ARG   A O   1 
ATOM   3139 C  CB  . ARG   A 1 420 ? -10.498 -14.238 -8.992  1.00 80.87  ? 440 ARG   A CB  1 
ATOM   3140 C  CG  . ARG   A 1 420 ? -11.733 -14.397 -8.116  1.00 85.50  ? 440 ARG   A CG  1 
ATOM   3141 C  CD  . ARG   A 1 420 ? -12.027 -13.168 -7.286  1.00 84.27  ? 440 ARG   A CD  1 
ATOM   3142 N  NE  . ARG   A 1 420 ? -13.015 -13.490 -6.265  1.00 86.11  ? 440 ARG   A NE  1 
ATOM   3143 C  CZ  . ARG   A 1 420 ? -13.604 -12.605 -5.473  1.00 84.86  ? 440 ARG   A CZ  1 
ATOM   3144 N  NH1 . ARG   A 1 420 ? -13.327 -11.315 -5.551  1.00 86.57  ? 440 ARG   A NH1 1 
ATOM   3145 N  NH2 . ARG   A 1 420 ? -14.496 -13.027 -4.583  1.00 87.37  ? 440 ARG   A NH2 1 
ATOM   3146 N  N   . ASN   A 1 421 ? -9.543  -17.351 -10.732 1.00 78.95  ? 441 ASN   A N   1 
ATOM   3147 C  CA  . ASN   A 1 421 ? -10.075 -18.346 -11.651 1.00 74.41  ? 441 ASN   A CA  1 
ATOM   3148 C  C   . ASN   A 1 421 ? -10.860 -19.387 -10.856 1.00 80.14  ? 441 ASN   A C   1 
ATOM   3149 O  O   . ASN   A 1 421 ? -11.066 -19.267 -9.644  1.00 83.21  ? 441 ASN   A O   1 
ATOM   3150 C  CB  . ASN   A 1 421 ? -8.946  -18.967 -12.470 1.00 75.76  ? 441 ASN   A CB  1 
ATOM   3151 C  CG  . ASN   A 1 421 ? -7.993  -19.800 -11.627 1.00 77.03  ? 441 ASN   A CG  1 
ATOM   3152 O  OD1 . ASN   A 1 421 ? -7.967  -19.694 -10.398 1.00 79.51  ? 441 ASN   A OD1 1 
ATOM   3153 N  ND2 . ASN   A 1 421 ? -7.192  -20.629 -12.290 1.00 70.80  ? 441 ASN   A ND2 1 
ATOM   3154 N  N   . CYS   A 1 422 ? -11.314 -20.431 -11.540 1.00 74.73  ? 442 CYS   A N   1 
ATOM   3155 C  CA  . CYS   A 1 422 ? -12.006 -21.515 -10.860 1.00 76.47  ? 442 CYS   A CA  1 
ATOM   3156 C  C   . CYS   A 1 422 ? -11.027 -22.265 -9.970  1.00 75.37  ? 442 CYS   A C   1 
ATOM   3157 O  O   . CYS   A 1 422 ? -10.068 -22.868 -10.462 1.00 77.47  ? 442 CYS   A O   1 
ATOM   3158 C  CB  . CYS   A 1 422 ? -12.637 -22.466 -11.870 1.00 81.69  ? 442 CYS   A CB  1 
ATOM   3159 S  SG  . CYS   A 1 422 ? -13.465 -23.873 -11.087 1.00 71.75  ? 442 CYS   A SG  1 
ATOM   3160 N  N   . ILE   A 1 423 ? -11.267 -22.227 -8.658  1.00 79.19  ? 443 ILE   A N   1 
ATOM   3161 C  CA  . ILE   A 1 423 ? -10.382 -22.924 -7.735  1.00 86.93  ? 443 ILE   A CA  1 
ATOM   3162 C  C   . ILE   A 1 423 ? -10.568 -24.435 -7.821  1.00 92.55  ? 443 ILE   A C   1 
ATOM   3163 O  O   . ILE   A 1 423 ? -9.699  -25.190 -7.370  1.00 100.93 ? 443 ILE   A O   1 
ATOM   3164 C  CB  . ILE   A 1 423 ? -10.604 -22.409 -6.298  1.00 91.08  ? 443 ILE   A CB  1 
ATOM   3165 C  CG1 . ILE   A 1 423 ? -9.454  -22.839 -5.383  1.00 91.96  ? 443 ILE   A CG1 1 
ATOM   3166 C  CG2 . ILE   A 1 423 ? -11.937 -22.890 -5.753  1.00 92.65  ? 443 ILE   A CG2 1 
ATOM   3167 C  CD1 . ILE   A 1 423 ? -9.519  -22.236 -3.995  1.00 92.36  ? 443 ILE   A CD1 1 
ATOM   3168 N  N   . GLY   A 1 424 ? -11.668 -24.900 -8.410  1.00 89.65  ? 444 GLY   A N   1 
ATOM   3169 C  CA  . GLY   A 1 424 ? -11.903 -26.322 -8.540  1.00 89.26  ? 444 GLY   A CA  1 
ATOM   3170 C  C   . GLY   A 1 424 ? -11.691 -26.841 -9.947  1.00 89.93  ? 444 GLY   A C   1 
ATOM   3171 O  O   . GLY   A 1 424 ? -12.291 -27.848 -10.336 1.00 94.02  ? 444 GLY   A O   1 
ATOM   3172 N  N   . MET   A 1 425 ? -10.840 -26.165 -10.722 1.00 81.58  ? 445 MET   A N   1 
ATOM   3173 C  CA  . MET   A 1 425 ? -10.604 -26.578 -12.103 1.00 83.63  ? 445 MET   A CA  1 
ATOM   3174 C  C   . MET   A 1 425 ? -9.959  -27.957 -12.161 1.00 88.69  ? 445 MET   A C   1 
ATOM   3175 O  O   . MET   A 1 425 ? -10.390 -28.826 -12.929 1.00 87.56  ? 445 MET   A O   1 
ATOM   3176 C  CB  . MET   A 1 425 ? -9.731  -25.545 -12.820 1.00 81.43  ? 445 MET   A CB  1 
ATOM   3177 C  CG  . MET   A 1 425 ? -9.252  -25.991 -14.196 1.00 77.36  ? 445 MET   A CG  1 
ATOM   3178 S  SD  . MET   A 1 425 ? -8.295  -24.736 -15.073 1.00 72.64  ? 445 MET   A SD  1 
ATOM   3179 C  CE  . MET   A 1 425 ? -6.851  -24.604 -14.019 1.00 90.43  ? 445 MET   A CE  1 
ATOM   3180 N  N   . ARG   A 1 426 ? -8.922  -28.177 -11.349 1.00 94.13  ? 446 ARG   A N   1 
ATOM   3181 C  CA  . ARG   A 1 426 ? -8.232  -29.463 -11.355 1.00 97.03  ? 446 ARG   A CA  1 
ATOM   3182 C  C   . ARG   A 1 426 ? -9.152  -30.589 -10.902 1.00 93.15  ? 446 ARG   A C   1 
ATOM   3183 O  O   . ARG   A 1 426 ? -9.163  -31.672 -11.501 1.00 91.26  ? 446 ARG   A O   1 
ATOM   3184 C  CB  . ARG   A 1 426 ? -6.994  -29.392 -10.462 1.00 102.68 ? 446 ARG   A CB  1 
ATOM   3185 C  CG  . ARG   A 1 426 ? -6.019  -28.291 -10.834 1.00 111.80 ? 446 ARG   A CG  1 
ATOM   3186 C  CD  . ARG   A 1 426 ? -4.804  -28.324 -9.925  1.00 122.23 ? 446 ARG   A CD  1 
ATOM   3187 N  NE  . ARG   A 1 426 ? -3.560  -28.301 -10.684 1.00 132.81 ? 446 ARG   A NE  1 
ATOM   3188 C  CZ  . ARG   A 1 426 ? -3.039  -29.356 -11.297 1.00 140.54 ? 446 ARG   A CZ  1 
ATOM   3189 N  NH1 . ARG   A 1 426 ? -3.640  -30.534 -11.277 1.00 141.05 ? 446 ARG   A NH1 1 
ATOM   3190 N  NH2 . ARG   A 1 426 ? -1.887  -29.223 -11.949 1.00 143.51 ? 446 ARG   A NH2 1 
ATOM   3191 N  N   . PHE   A 1 427 ? -9.929  -30.354 -9.843  1.00 98.65  ? 447 PHE   A N   1 
ATOM   3192 C  CA  . PHE   A 1 427 ? -10.851 -31.375 -9.357  1.00 95.55  ? 447 PHE   A CA  1 
ATOM   3193 C  C   . PHE   A 1 427 ? -11.960 -31.650 -10.365 1.00 96.71  ? 447 PHE   A C   1 
ATOM   3194 O  O   . PHE   A 1 427 ? -12.390 -32.799 -10.523 1.00 93.24  ? 447 PHE   A O   1 
ATOM   3195 C  CB  . PHE   A 1 427 ? -11.438 -30.947 -8.012  1.00 95.06  ? 447 PHE   A CB  1 
ATOM   3196 C  CG  . PHE   A 1 427 ? -12.581 -31.802 -7.551  1.00 94.85  ? 447 PHE   A CG  1 
ATOM   3197 C  CD1 . PHE   A 1 427 ? -12.347 -32.994 -6.887  1.00 96.60  ? 447 PHE   A CD1 1 
ATOM   3198 C  CD2 . PHE   A 1 427 ? -13.891 -31.412 -7.777  1.00 92.40  ? 447 PHE   A CD2 1 
ATOM   3199 C  CE1 . PHE   A 1 427 ? -13.397 -33.782 -6.461  1.00 101.80 ? 447 PHE   A CE1 1 
ATOM   3200 C  CE2 . PHE   A 1 427 ? -14.944 -32.195 -7.355  1.00 97.13  ? 447 PHE   A CE2 1 
ATOM   3201 C  CZ  . PHE   A 1 427 ? -14.698 -33.381 -6.695  1.00 102.97 ? 447 PHE   A CZ  1 
ATOM   3202 N  N   . ALA   A 1 428 ? -12.441 -30.612 -11.052 1.00 93.92  ? 448 ALA   A N   1 
ATOM   3203 C  CA  . ALA   A 1 428 ? -13.510 -30.807 -12.027 1.00 90.03  ? 448 ALA   A CA  1 
ATOM   3204 C  C   . ALA   A 1 428 ? -13.013 -31.582 -13.240 1.00 88.65  ? 448 ALA   A C   1 
ATOM   3205 O  O   . ALA   A 1 428 ? -13.682 -32.507 -13.713 1.00 91.45  ? 448 ALA   A O   1 
ATOM   3206 C  CB  . ALA   A 1 428 ? -14.092 -29.460 -12.453 1.00 87.57  ? 448 ALA   A CB  1 
ATOM   3207 N  N   . LEU   A 1 429 ? -11.839 -31.217 -13.761 1.00 89.27  ? 449 LEU   A N   1 
ATOM   3208 C  CA  . LEU   A 1 429 ? -11.316 -31.901 -14.938 1.00 89.66  ? 449 LEU   A CA  1 
ATOM   3209 C  C   . LEU   A 1 429 ? -10.996 -33.358 -14.641 1.00 91.65  ? 449 LEU   A C   1 
ATOM   3210 O  O   . LEU   A 1 429 ? -11.038 -34.200 -15.542 1.00 93.15  ? 449 LEU   A O   1 
ATOM   3211 C  CB  . LEU   A 1 429 ? -10.075 -31.179 -15.462 1.00 83.13  ? 449 LEU   A CB  1 
ATOM   3212 C  CG  . LEU   A 1 429 ? -10.299 -29.838 -16.165 1.00 84.05  ? 449 LEU   A CG  1 
ATOM   3213 C  CD1 . LEU   A 1 429 ? -8.967  -29.185 -16.487 1.00 79.65  ? 449 LEU   A CD1 1 
ATOM   3214 C  CD2 . LEU   A 1 429 ? -11.116 -30.033 -17.429 1.00 80.28  ? 449 LEU   A CD2 1 
ATOM   3215 N  N   . MET   A 1 430 ? -10.686 -33.679 -13.387 1.00 92.98  ? 450 MET   A N   1 
ATOM   3216 C  CA  . MET   A 1 430 ? -10.362 -35.056 -13.042 1.00 93.46  ? 450 MET   A CA  1 
ATOM   3217 C  C   . MET   A 1 430 ? -11.615 -35.868 -12.743 1.00 93.54  ? 450 MET   A C   1 
ATOM   3218 O  O   . MET   A 1 430 ? -11.682 -37.058 -13.073 1.00 95.48  ? 450 MET   A O   1 
ATOM   3219 C  CB  . MET   A 1 430 ? -9.406  -35.081 -11.855 1.00 97.78  ? 450 MET   A CB  1 
ATOM   3220 C  CG  . MET   A 1 430 ? -7.966  -35.300 -12.247 1.00 105.58 ? 450 MET   A CG  1 
ATOM   3221 S  SD  . MET   A 1 430 ? -7.533  -37.026 -12.017 1.00 114.34 ? 450 MET   A SD  1 
ATOM   3222 C  CE  . MET   A 1 430 ? -8.018  -37.226 -10.308 1.00 108.82 ? 450 MET   A CE  1 
ATOM   3223 N  N   . ASN   A 1 431 ? -12.612 -35.243 -12.113 1.00 92.57  ? 451 ASN   A N   1 
ATOM   3224 C  CA  . ASN   A 1 431 ? -13.843 -35.953 -11.781 1.00 94.52  ? 451 ASN   A CA  1 
ATOM   3225 C  C   . ASN   A 1 431 ? -14.601 -36.367 -13.036 1.00 92.79  ? 451 ASN   A C   1 
ATOM   3226 O  O   . ASN   A 1 431 ? -15.092 -37.498 -13.123 1.00 95.22  ? 451 ASN   A O   1 
ATOM   3227 C  CB  . ASN   A 1 431 ? -14.714 -35.078 -10.880 1.00 93.90  ? 451 ASN   A CB  1 
ATOM   3228 C  CG  . ASN   A 1 431 ? -16.024 -35.739 -10.512 1.00 102.14 ? 451 ASN   A CG  1 
ATOM   3229 O  OD1 . ASN   A 1 431 ? -17.053 -35.076 -10.387 1.00 104.38 ? 451 ASN   A OD1 1 
ATOM   3230 N  ND2 . ASN   A 1 431 ? -15.996 -37.055 -10.345 1.00 104.33 ? 451 ASN   A ND2 1 
ATOM   3231 N  N   . MET   A 1 432 ? -14.699 -35.473 -14.020 1.00 91.24  ? 452 MET   A N   1 
ATOM   3232 C  CA  . MET   A 1 432 ? -15.397 -35.816 -15.255 1.00 90.45  ? 452 MET   A CA  1 
ATOM   3233 C  C   . MET   A 1 432 ? -14.643 -36.885 -16.028 1.00 89.29  ? 452 MET   A C   1 
ATOM   3234 O  O   . MET   A 1 432 ? -15.233 -37.873 -16.478 1.00 91.97  ? 452 MET   A O   1 
ATOM   3235 C  CB  . MET   A 1 432 ? -15.583 -34.572 -16.121 1.00 92.05  ? 452 MET   A CB  1 
ATOM   3236 C  CG  . MET   A 1 432 ? -16.247 -33.417 -15.410 1.00 82.25  ? 452 MET   A CG  1 
ATOM   3237 S  SD  . MET   A 1 432 ? -16.803 -32.150 -16.564 1.00 83.23  ? 452 MET   A SD  1 
ATOM   3238 C  CE  . MET   A 1 432 ? -15.332 -31.902 -17.555 1.00 91.03  ? 452 MET   A CE  1 
ATOM   3239 N  N   . LYS   A 1 433 ? -13.333 -36.696 -16.201 1.00 92.99  ? 453 LYS   A N   1 
ATOM   3240 C  CA  . LYS   A 1 433 ? -12.543 -37.655 -16.965 1.00 89.74  ? 453 LYS   A CA  1 
ATOM   3241 C  C   . LYS   A 1 433 ? -12.552 -39.028 -16.307 1.00 93.28  ? 453 LYS   A C   1 
ATOM   3242 O  O   . LYS   A 1 433 ? -12.640 -40.050 -16.995 1.00 96.77  ? 453 LYS   A O   1 
ATOM   3243 C  CB  . LYS   A 1 433 ? -11.116 -37.137 -17.136 1.00 88.83  ? 453 LYS   A CB  1 
ATOM   3244 C  CG  . LYS   A 1 433 ? -11.012 -35.936 -18.060 1.00 82.05  ? 453 LYS   A CG  1 
ATOM   3245 C  CD  . LYS   A 1 433 ? -9.581  -35.450 -18.184 1.00 81.94  ? 453 LYS   A CD  1 
ATOM   3246 C  CE  . LYS   A 1 433 ? -9.509  -34.173 -19.004 1.00 79.00  ? 453 LYS   A CE  1 
ATOM   3247 N  NZ  . LYS   A 1 433 ? -8.105  -33.795 -19.325 1.00 82.20  ? 453 LYS   A NZ  1 
ATOM   3248 N  N   . LEU   A 1 434 ? -12.474 -39.074 -14.973 1.00 94.77  ? 454 LEU   A N   1 
ATOM   3249 C  CA  . LEU   A 1 434 ? -12.629 -40.349 -14.277 1.00 96.01  ? 454 LEU   A CA  1 
ATOM   3250 C  C   . LEU   A 1 434 ? -13.974 -40.988 -14.599 1.00 95.38  ? 454 LEU   A C   1 
ATOM   3251 O  O   . LEU   A 1 434 ? -14.067 -42.211 -14.755 1.00 93.72  ? 454 LEU   A O   1 
ATOM   3252 C  CB  . LEU   A 1 434 ? -12.477 -40.157 -12.768 1.00 98.18  ? 454 LEU   A CB  1 
ATOM   3253 C  CG  . LEU   A 1 434 ? -11.067 -40.335 -12.203 1.00 98.68  ? 454 LEU   A CG  1 
ATOM   3254 C  CD1 . LEU   A 1 434 ? -11.078 -40.299 -10.684 1.00 110.42 ? 454 LEU   A CD1 1 
ATOM   3255 C  CD2 . LEU   A 1 434 ? -10.463 -41.631 -12.701 1.00 97.06  ? 454 LEU   A CD2 1 
ATOM   3256 N  N   . ALA   A 1 435 ? -15.026 -40.174 -14.708 1.00 100.34 ? 455 ALA   A N   1 
ATOM   3257 C  CA  . ALA   A 1 435 ? -16.335 -40.700 -15.078 1.00 96.26  ? 455 ALA   A CA  1 
ATOM   3258 C  C   . ALA   A 1 435 ? -16.341 -41.187 -16.522 1.00 106.22 ? 455 ALA   A C   1 
ATOM   3259 O  O   . ALA   A 1 435 ? -16.777 -42.309 -16.807 1.00 104.47 ? 455 ALA   A O   1 
ATOM   3260 C  CB  . ALA   A 1 435 ? -17.408 -39.633 -14.869 1.00 94.05  ? 455 ALA   A CB  1 
ATOM   3261 N  N   . LEU   A 1 436 ? -15.845 -40.354 -17.443 1.00 95.32  ? 456 LEU   A N   1 
ATOM   3262 C  CA  . LEU   A 1 436 ? -15.891 -40.678 -18.867 1.00 92.48  ? 456 LEU   A CA  1 
ATOM   3263 C  C   . LEU   A 1 436 ? -15.182 -41.995 -19.163 1.00 93.46  ? 456 LEU   A C   1 
ATOM   3264 O  O   . LEU   A 1 436 ? -15.699 -42.839 -19.904 1.00 95.59  ? 456 LEU   A O   1 
ATOM   3265 C  CB  . LEU   A 1 436 ? -15.270 -39.541 -19.679 1.00 92.55  ? 456 LEU   A CB  1 
ATOM   3266 C  CG  . LEU   A 1 436 ? -15.899 -38.153 -19.534 1.00 92.06  ? 456 LEU   A CG  1 
ATOM   3267 C  CD1 . LEU   A 1 436 ? -14.865 -37.078 -19.815 1.00 84.22  ? 456 LEU   A CD1 1 
ATOM   3268 C  CD2 . LEU   A 1 436 ? -17.092 -37.987 -20.454 1.00 91.58  ? 456 LEU   A CD2 1 
ATOM   3269 N  N   . ILE   A 1 437 ? -13.991 -42.184 -18.590 1.00 99.44  ? 457 ILE   A N   1 
ATOM   3270 C  CA  . ILE   A 1 437 ? -13.225 -43.403 -18.835 1.00 97.20  ? 457 ILE   A CA  1 
ATOM   3271 C  C   . ILE   A 1 437 ? -14.030 -44.633 -18.438 1.00 97.97  ? 457 ILE   A C   1 
ATOM   3272 O  O   . ILE   A 1 437 ? -14.083 -45.623 -19.177 1.00 103.20 ? 457 ILE   A O   1 
ATOM   3273 C  CB  . ILE   A 1 437 ? -11.881 -43.346 -18.088 1.00 93.10  ? 457 ILE   A CB  1 
ATOM   3274 C  CG1 . ILE   A 1 437 ? -11.052 -42.150 -18.551 1.00 90.09  ? 457 ILE   A CG1 1 
ATOM   3275 C  CG2 . ILE   A 1 437 ? -11.114 -44.619 -18.309 1.00 99.34  ? 457 ILE   A CG2 1 
ATOM   3276 C  CD1 . ILE   A 1 437 ? -9.864  -41.859 -17.662 1.00 92.86  ? 457 ILE   A CD1 1 
ATOM   3277 N  N   . ARG   A 1 438 ? -14.680 -44.586 -17.275 1.00 99.02  ? 458 ARG   A N   1 
ATOM   3278 C  CA  . ARG   A 1 438 ? -15.392 -45.761 -16.782 1.00 101.42 ? 458 ARG   A CA  1 
ATOM   3279 C  C   . ARG   A 1 438 ? -16.686 -46.000 -17.553 1.00 99.28  ? 458 ARG   A C   1 
ATOM   3280 O  O   . ARG   A 1 438 ? -17.056 -47.152 -17.804 1.00 99.58  ? 458 ARG   A O   1 
ATOM   3281 C  CB  . ARG   A 1 438 ? -15.666 -45.612 -15.285 1.00 100.55 ? 458 ARG   A CB  1 
ATOM   3282 C  CG  . ARG   A 1 438 ? -14.709 -46.406 -14.404 1.00 106.15 ? 458 ARG   A CG  1 
ATOM   3283 C  CD  . ARG   A 1 438 ? -15.006 -47.893 -14.514 1.00 113.26 ? 458 ARG   A CD  1 
ATOM   3284 N  NE  . ARG   A 1 438 ? -14.086 -48.723 -13.746 1.00 112.79 ? 458 ARG   A NE  1 
ATOM   3285 C  CZ  . ARG   A 1 438 ? -13.164 -49.511 -14.282 1.00 111.97 ? 458 ARG   A CZ  1 
ATOM   3286 N  NH1 . ARG   A 1 438 ? -12.996 -49.588 -15.592 1.00 113.67 ? 458 ARG   A NH1 1 
ATOM   3287 N  NH2 . ARG   A 1 438 ? -12.398 -50.250 -13.484 1.00 110.99 ? 458 ARG   A NH2 1 
ATOM   3288 N  N   . VAL   A 1 439 ? -17.384 -44.930 -17.946 1.00 106.93 ? 459 VAL   A N   1 
ATOM   3289 C  CA  . VAL   A 1 439 ? -18.666 -45.107 -18.625 1.00 101.95 ? 459 VAL   A CA  1 
ATOM   3290 C  C   . VAL   A 1 439 ? -18.465 -45.564 -20.065 1.00 107.51 ? 459 VAL   A C   1 
ATOM   3291 O  O   . VAL   A 1 439 ? -19.278 -46.331 -20.598 1.00 114.08 ? 459 VAL   A O   1 
ATOM   3292 C  CB  . VAL   A 1 439 ? -19.506 -43.815 -18.551 1.00 100.48 ? 459 VAL   A CB  1 
ATOM   3293 C  CG1 . VAL   A 1 439 ? -18.782 -42.655 -19.197 1.00 99.43  ? 459 VAL   A CG1 1 
ATOM   3294 C  CG2 . VAL   A 1 439 ? -20.845 -44.014 -19.220 1.00 96.82  ? 459 VAL   A CG2 1 
ATOM   3295 N  N   . LEU   A 1 440 ? -17.388 -45.129 -20.717 1.00 102.21 ? 460 LEU   A N   1 
ATOM   3296 C  CA  . LEU   A 1 440 ? -17.153 -45.514 -22.101 1.00 100.05 ? 460 LEU   A CA  1 
ATOM   3297 C  C   . LEU   A 1 440 ? -16.319 -46.780 -22.241 1.00 102.48 ? 460 LEU   A C   1 
ATOM   3298 O  O   . LEU   A 1 440 ? -16.251 -47.337 -23.342 1.00 104.32 ? 460 LEU   A O   1 
ATOM   3299 C  CB  . LEU   A 1 440 ? -16.501 -44.362 -22.872 1.00 96.42  ? 460 LEU   A CB  1 
ATOM   3300 C  CG  . LEU   A 1 440 ? -17.501 -43.270 -23.263 1.00 96.69  ? 460 LEU   A CG  1 
ATOM   3301 C  CD1 . LEU   A 1 440 ? -17.016 -42.503 -24.470 1.00 93.74  ? 460 LEU   A CD1 1 
ATOM   3302 C  CD2 . LEU   A 1 440 ? -18.872 -43.866 -23.539 1.00 100.32 ? 460 LEU   A CD2 1 
ATOM   3303 N  N   . GLN   A 1 441 ? -15.696 -47.255 -21.161 1.00 101.91 ? 461 GLN   A N   1 
ATOM   3304 C  CA  . GLN   A 1 441 ? -15.102 -48.585 -21.187 1.00 101.49 ? 461 GLN   A CA  1 
ATOM   3305 C  C   . GLN   A 1 441 ? -16.154 -49.678 -21.297 1.00 109.15 ? 461 GLN   A C   1 
ATOM   3306 O  O   . GLN   A 1 441 ? -15.838 -50.779 -21.758 1.00 111.37 ? 461 GLN   A O   1 
ATOM   3307 C  CB  . GLN   A 1 441 ? -14.257 -48.819 -19.932 1.00 103.68 ? 461 GLN   A CB  1 
ATOM   3308 C  CG  . GLN   A 1 441 ? -12.800 -48.447 -20.088 1.00 103.36 ? 461 GLN   A CG  1 
ATOM   3309 C  CD  . GLN   A 1 441 ? -12.004 -48.642 -18.813 1.00 108.51 ? 461 GLN   A CD  1 
ATOM   3310 O  OE1 . GLN   A 1 441 ? -12.476 -48.330 -17.719 1.00 108.39 ? 461 GLN   A OE1 1 
ATOM   3311 N  NE2 . GLN   A 1 441 ? -10.790 -49.164 -18.948 1.00 111.00 ? 461 GLN   A NE2 1 
ATOM   3312 N  N   . ASN   A 1 442 ? -17.397 -49.396 -20.897 1.00 111.06 ? 462 ASN   A N   1 
ATOM   3313 C  CA  . ASN   A 1 442 ? -18.439 -50.409 -20.826 1.00 113.41 ? 462 ASN   A CA  1 
ATOM   3314 C  C   . ASN   A 1 442 ? -19.628 -50.166 -21.745 1.00 113.47 ? 462 ASN   A C   1 
ATOM   3315 O  O   . ASN   A 1 442 ? -20.353 -51.123 -22.038 1.00 120.39 ? 462 ASN   A O   1 
ATOM   3316 C  CB  . ASN   A 1 442 ? -18.960 -50.539 -19.384 1.00 113.76 ? 462 ASN   A CB  1 
ATOM   3317 C  CG  . ASN   A 1 442 ? -17.982 -51.251 -18.471 1.00 116.43 ? 462 ASN   A CG  1 
ATOM   3318 O  OD1 . ASN   A 1 442 ? -17.923 -52.482 -18.447 1.00 118.05 ? 462 ASN   A OD1 1 
ATOM   3319 N  ND2 . ASN   A 1 442 ? -17.213 -50.481 -17.709 1.00 116.95 ? 462 ASN   A ND2 1 
ATOM   3320 N  N   . PHE   A 1 443 ? -19.856 -48.936 -22.203 1.00 111.17 ? 463 PHE   A N   1 
ATOM   3321 C  CA  . PHE   A 1 443 ? -21.044 -48.618 -22.982 1.00 111.35 ? 463 PHE   A CA  1 
ATOM   3322 C  C   . PHE   A 1 443 ? -20.667 -47.774 -24.192 1.00 110.70 ? 463 PHE   A C   1 
ATOM   3323 O  O   . PHE   A 1 443 ? -19.586 -47.181 -24.255 1.00 106.13 ? 463 PHE   A O   1 
ATOM   3324 C  CB  . PHE   A 1 443 ? -22.092 -47.859 -22.147 1.00 116.74 ? 463 PHE   A CB  1 
ATOM   3325 C  CG  . PHE   A 1 443 ? -22.548 -48.591 -20.913 1.00 123.85 ? 463 PHE   A CG  1 
ATOM   3326 C  CD1 . PHE   A 1 443 ? -21.771 -48.593 -19.765 1.00 122.63 ? 463 PHE   A CD1 1 
ATOM   3327 C  CD2 . PHE   A 1 443 ? -23.766 -49.251 -20.892 1.00 129.05 ? 463 PHE   A CD2 1 
ATOM   3328 C  CE1 . PHE   A 1 443 ? -22.189 -49.259 -18.629 1.00 130.50 ? 463 PHE   A CE1 1 
ATOM   3329 C  CE2 . PHE   A 1 443 ? -24.194 -49.912 -19.758 1.00 134.07 ? 463 PHE   A CE2 1 
ATOM   3330 C  CZ  . PHE   A 1 443 ? -23.404 -49.916 -18.624 1.00 137.37 ? 463 PHE   A CZ  1 
ATOM   3331 N  N   . SER   A 1 444 ? -21.586 -47.730 -25.157 1.00 114.24 ? 464 SER   A N   1 
ATOM   3332 C  CA  . SER   A 1 444 ? -21.540 -46.786 -26.264 1.00 109.54 ? 464 SER   A CA  1 
ATOM   3333 C  C   . SER   A 1 444 ? -22.921 -46.165 -26.420 1.00 109.82 ? 464 SER   A C   1 
ATOM   3334 O  O   . SER   A 1 444 ? -23.941 -46.819 -26.189 1.00 115.86 ? 464 SER   A O   1 
ATOM   3335 C  CB  . SER   A 1 444 ? -21.096 -47.451 -27.580 1.00 110.31 ? 464 SER   A CB  1 
ATOM   3336 O  OG  . SER   A 1 444 ? -22.195 -47.661 -28.451 1.00 115.19 ? 464 SER   A OG  1 
ATOM   3337 N  N   . PHE   A 1 445 ? -22.945 -44.893 -26.806 1.00 112.42 ? 465 PHE   A N   1 
ATOM   3338 C  CA  . PHE   A 1 445 ? -24.155 -44.082 -26.766 1.00 112.84 ? 465 PHE   A CA  1 
ATOM   3339 C  C   . PHE   A 1 445 ? -24.550 -43.675 -28.178 1.00 117.47 ? 465 PHE   A C   1 
ATOM   3340 O  O   . PHE   A 1 445 ? -23.731 -43.133 -28.927 1.00 116.67 ? 465 PHE   A O   1 
ATOM   3341 C  CB  . PHE   A 1 445 ? -23.955 -42.844 -25.893 1.00 110.95 ? 465 PHE   A CB  1 
ATOM   3342 C  CG  . PHE   A 1 445 ? -23.709 -43.156 -24.440 1.00 109.22 ? 465 PHE   A CG  1 
ATOM   3343 C  CD1 . PHE   A 1 445 ? -22.528 -43.757 -24.034 1.00 108.70 ? 465 PHE   A CD1 1 
ATOM   3344 C  CD2 . PHE   A 1 445 ? -24.652 -42.836 -23.479 1.00 105.96 ? 465 PHE   A CD2 1 
ATOM   3345 C  CE1 . PHE   A 1 445 ? -22.300 -44.045 -22.706 1.00 110.23 ? 465 PHE   A CE1 1 
ATOM   3346 C  CE2 . PHE   A 1 445 ? -24.425 -43.119 -22.145 1.00 108.00 ? 465 PHE   A CE2 1 
ATOM   3347 C  CZ  . PHE   A 1 445 ? -23.248 -43.725 -21.760 1.00 107.51 ? 465 PHE   A CZ  1 
ATOM   3348 N  N   . LYS   A 1 446 ? -25.809 -43.929 -28.530 1.00 122.44 ? 466 LYS   A N   1 
ATOM   3349 C  CA  . LYS   A 1 446 ? -26.378 -43.619 -29.821 1.00 127.62 ? 466 LYS   A CA  1 
ATOM   3350 C  C   . LYS   A 1 446 ? -27.613 -42.746 -29.646 1.00 129.68 ? 466 LYS   A C   1 
ATOM   3351 O  O   . LYS   A 1 446 ? -28.348 -42.910 -28.669 1.00 131.03 ? 466 LYS   A O   1 
ATOM   3352 C  CB  . LYS   A 1 446 ? -26.763 -44.904 -30.571 1.00 125.72 ? 466 LYS   A CB  1 
ATOM   3353 C  CG  . LYS   A 1 446 ? -25.644 -45.930 -30.638 1.00 128.70 ? 466 LYS   A CG  1 
ATOM   3354 C  CD  . LYS   A 1 446 ? -26.191 -47.346 -30.690 1.00 138.53 ? 466 LYS   A CD  1 
ATOM   3355 C  CE  . LYS   A 1 446 ? -27.216 -47.509 -31.803 1.00 143.36 ? 466 LYS   A CE  1 
ATOM   3356 N  NZ  . LYS   A 1 446 ? -27.668 -48.923 -31.958 1.00 146.85 ? 466 LYS   A NZ  1 
ATOM   3357 N  N   . PRO   A 1 447 ? -27.857 -41.800 -30.548 1.00 131.55 ? 467 PRO   A N   1 
ATOM   3358 C  CA  . PRO   A 1 447 ? -29.022 -40.920 -30.395 1.00 135.17 ? 467 PRO   A CA  1 
ATOM   3359 C  C   . PRO   A 1 447 ? -30.332 -41.682 -30.547 1.00 143.80 ? 467 PRO   A C   1 
ATOM   3360 O  O   . PRO   A 1 447 ? -30.387 -42.795 -31.077 1.00 143.37 ? 467 PRO   A O   1 
ATOM   3361 C  CB  . PRO   A 1 447 ? -28.845 -39.892 -31.520 1.00 130.75 ? 467 PRO   A CB  1 
ATOM   3362 C  CG  . PRO   A 1 447 ? -27.391 -39.948 -31.868 1.00 122.10 ? 467 PRO   A CG  1 
ATOM   3363 C  CD  . PRO   A 1 447 ? -26.982 -41.372 -31.653 1.00 124.66 ? 467 PRO   A CD  1 
ATOM   3364 N  N   . CYS   A 1 448 ? -31.397 -41.060 -30.055 1.00 142.80 ? 468 CYS   A N   1 
ATOM   3365 C  CA  . CYS   A 1 448 ? -32.756 -41.569 -30.182 1.00 153.72 ? 468 CYS   A CA  1 
ATOM   3366 C  C   . CYS   A 1 448 ? -33.564 -40.668 -31.106 1.00 159.69 ? 468 CYS   A C   1 
ATOM   3367 O  O   . CYS   A 1 448 ? -33.136 -39.571 -31.473 1.00 154.52 ? 468 CYS   A O   1 
ATOM   3368 C  CB  . CYS   A 1 448 ? -33.435 -41.668 -28.811 1.00 151.23 ? 468 CYS   A CB  1 
ATOM   3369 S  SG  . CYS   A 1 448 ? -32.913 -43.071 -27.799 1.00 151.74 ? 468 CYS   A SG  1 
ATOM   3370 N  N   . LYS   A 1 449 ? -34.753 -41.142 -31.486 1.00 182.05 ? 469 LYS   A N   1 
ATOM   3371 C  CA  . LYS   A 1 449 ? -35.604 -40.324 -32.341 1.00 181.44 ? 469 LYS   A CA  1 
ATOM   3372 C  C   . LYS   A 1 449 ? -36.122 -39.098 -31.599 1.00 180.32 ? 469 LYS   A C   1 
ATOM   3373 O  O   . LYS   A 1 449 ? -36.311 -38.042 -32.213 1.00 184.71 ? 469 LYS   A O   1 
ATOM   3374 C  CB  . LYS   A 1 449 ? -36.759 -41.165 -32.902 1.00 180.11 ? 469 LYS   A CB  1 
ATOM   3375 C  CG  . LYS   A 1 449 ? -37.995 -41.293 -32.015 1.00 182.21 ? 469 LYS   A CG  1 
ATOM   3376 C  CD  . LYS   A 1 449 ? -39.086 -40.310 -32.434 1.00 191.63 ? 469 LYS   A CD  1 
ATOM   3377 C  CE  . LYS   A 1 449 ? -40.448 -40.715 -31.889 1.00 191.17 ? 469 LYS   A CE  1 
ATOM   3378 N  NZ  . LYS   A 1 449 ? -41.478 -39.667 -32.143 1.00 201.85 ? 469 LYS   A NZ  1 
ATOM   3379 N  N   . GLU   A 1 450 ? -36.334 -39.205 -30.286 1.00 168.93 ? 470 GLU   A N   1 
ATOM   3380 C  CA  . GLU   A 1 450 ? -36.713 -38.052 -29.481 1.00 163.48 ? 470 GLU   A CA  1 
ATOM   3381 C  C   . GLU   A 1 450 ? -35.512 -37.233 -29.035 1.00 156.57 ? 470 GLU   A C   1 
ATOM   3382 O  O   . GLU   A 1 450 ? -35.687 -36.261 -28.292 1.00 148.48 ? 470 GLU   A O   1 
ATOM   3383 C  CB  . GLU   A 1 450 ? -37.525 -38.493 -28.258 1.00 158.94 ? 470 GLU   A CB  1 
ATOM   3384 C  CG  . GLU   A 1 450 ? -36.735 -39.251 -27.205 1.00 155.69 ? 470 GLU   A CG  1 
ATOM   3385 C  CD  . GLU   A 1 450 ? -36.530 -40.712 -27.556 1.00 163.17 ? 470 GLU   A CD  1 
ATOM   3386 O  OE1 . GLU   A 1 450 ? -37.003 -41.154 -28.625 1.00 168.25 ? 470 GLU   A OE1 1 
ATOM   3387 O  OE2 . GLU   A 1 450 ? -35.894 -41.422 -26.754 1.00 161.91 ? 470 GLU   A OE2 1 
ATOM   3388 N  N   . THR   A 1 451 ? -34.307 -37.603 -29.461 1.00 152.66 ? 471 THR   A N   1 
ATOM   3389 C  CA  . THR   A 1 451 ? -33.133 -36.787 -29.191 1.00 144.83 ? 471 THR   A CA  1 
ATOM   3390 C  C   . THR   A 1 451 ? -33.151 -35.546 -30.072 1.00 140.34 ? 471 THR   A C   1 
ATOM   3391 O  O   . THR   A 1 451 ? -33.496 -35.605 -31.256 1.00 140.27 ? 471 THR   A O   1 
ATOM   3392 C  CB  . THR   A 1 451 ? -31.852 -37.593 -29.422 1.00 143.21 ? 471 THR   A CB  1 
ATOM   3393 O  OG1 . THR   A 1 451 ? -31.628 -38.464 -28.308 1.00 134.50 ? 471 THR   A OG1 1 
ATOM   3394 C  CG2 . THR   A 1 451 ? -30.643 -36.679 -29.595 1.00 134.09 ? 471 THR   A CG2 1 
ATOM   3395 N  N   . GLN   A 1 452 ? -32.790 -34.417 -29.475 1.00 134.47 ? 472 GLN   A N   1 
ATOM   3396 C  CA  . GLN   A 1 452 ? -32.833 -33.119 -30.134 1.00 133.63 ? 472 GLN   A CA  1 
ATOM   3397 C  C   . GLN   A 1 452 ? -31.528 -32.897 -30.893 1.00 130.99 ? 472 GLN   A C   1 
ATOM   3398 O  O   . GLN   A 1 452 ? -30.463 -32.745 -30.284 1.00 127.48 ? 472 GLN   A O   1 
ATOM   3399 C  CB  . GLN   A 1 452 ? -33.079 -32.035 -29.090 1.00 126.99 ? 472 GLN   A CB  1 
ATOM   3400 C  CG  . GLN   A 1 452 ? -32.718 -30.631 -29.492 1.00 124.48 ? 472 GLN   A CG  1 
ATOM   3401 C  CD  . GLN   A 1 452 ? -33.019 -29.655 -28.378 1.00 126.07 ? 472 GLN   A CD  1 
ATOM   3402 O  OE1 . GLN   A 1 452 ? -32.116 -29.032 -27.814 1.00 120.99 ? 472 GLN   A OE1 1 
ATOM   3403 N  NE2 . GLN   A 1 452 ? -34.298 -29.522 -28.045 1.00 129.66 ? 472 GLN   A NE2 1 
ATOM   3404 N  N   . ILE   A 1 453 ? -31.610 -32.896 -32.225 1.00 133.51 ? 473 ILE   A N   1 
ATOM   3405 C  CA  . ILE   A 1 453 ? -30.469 -32.637 -33.089 1.00 129.77 ? 473 ILE   A CA  1 
ATOM   3406 C  C   . ILE   A 1 453 ? -30.876 -31.557 -34.083 1.00 130.05 ? 473 ILE   A C   1 
ATOM   3407 O  O   . ILE   A 1 453 ? -31.764 -31.782 -34.909 1.00 133.30 ? 473 ILE   A O   1 
ATOM   3408 C  CB  . ILE   A 1 453 ? -29.994 -33.895 -33.838 1.00 128.96 ? 473 ILE   A CB  1 
ATOM   3409 C  CG1 . ILE   A 1 453 ? -29.831 -35.067 -32.870 1.00 127.76 ? 473 ILE   A CG1 1 
ATOM   3410 C  CG2 . ILE   A 1 453 ? -28.680 -33.623 -34.556 1.00 126.90 ? 473 ILE   A CG2 1 
ATOM   3411 C  CD1 . ILE   A 1 453 ? -29.539 -36.385 -33.551 1.00 129.96 ? 473 ILE   A CD1 1 
ATOM   3412 N  N   . PRO   A 1 454 ? -30.249 -30.377 -34.064 1.00 131.31 ? 474 PRO   A N   1 
ATOM   3413 C  CA  . PRO   A 1 454 ? -29.122 -29.990 -33.213 1.00 129.29 ? 474 PRO   A CA  1 
ATOM   3414 C  C   . PRO   A 1 454 ? -29.613 -29.597 -31.826 1.00 130.20 ? 474 PRO   A C   1 
ATOM   3415 O  O   . PRO   A 1 454 ? -30.778 -29.243 -31.662 1.00 130.62 ? 474 PRO   A O   1 
ATOM   3416 C  CB  . PRO   A 1 454 ? -28.511 -28.819 -33.988 1.00 129.19 ? 474 PRO   A CB  1 
ATOM   3417 C  CG  . PRO   A 1 454 ? -29.719 -28.135 -34.576 1.00 131.80 ? 474 PRO   A CG  1 
ATOM   3418 C  CD  . PRO   A 1 454 ? -30.683 -29.259 -34.925 1.00 132.78 ? 474 PRO   A CD  1 
ATOM   3419 N  N   . LEU   A 1 455 ? -28.765 -29.677 -30.805 1.00 122.30 ? 475 LEU   A N   1 
ATOM   3420 C  CA  . LEU   A 1 455 ? -29.154 -29.216 -29.479 1.00 117.62 ? 475 LEU   A CA  1 
ATOM   3421 C  C   . LEU   A 1 455 ? -29.346 -27.706 -29.509 1.00 114.53 ? 475 LEU   A C   1 
ATOM   3422 O  O   . LEU   A 1 455 ? -28.415 -26.961 -29.834 1.00 115.52 ? 475 LEU   A O   1 
ATOM   3423 C  CB  . LEU   A 1 455 ? -28.101 -29.608 -28.444 1.00 112.95 ? 475 LEU   A CB  1 
ATOM   3424 C  CG  . LEU   A 1 455 ? -28.282 -29.086 -27.014 1.00 107.35 ? 475 LEU   A CG  1 
ATOM   3425 C  CD1 . LEU   A 1 455 ? -27.921 -30.162 -26.006 1.00 104.36 ? 475 LEU   A CD1 1 
ATOM   3426 C  CD2 . LEU   A 1 455 ? -27.440 -27.840 -26.770 1.00 103.98 ? 475 LEU   A CD2 1 
ATOM   3427 N  N   . LYS   A 1 456 ? -30.555 -27.255 -29.193 1.00 123.53 ? 476 LYS   A N   1 
ATOM   3428 C  CA  . LYS   A 1 456 ? -30.836 -25.837 -29.031 1.00 122.52 ? 476 LYS   A CA  1 
ATOM   3429 C  C   . LYS   A 1 456 ? -30.732 -25.485 -27.554 1.00 120.57 ? 476 LYS   A C   1 
ATOM   3430 O  O   . LYS   A 1 456 ? -31.356 -26.135 -26.708 1.00 124.74 ? 476 LYS   A O   1 
ATOM   3431 C  CB  . LYS   A 1 456 ? -32.216 -25.468 -29.584 1.00 125.26 ? 476 LYS   A CB  1 
ATOM   3432 C  CG  . LYS   A 1 456 ? -33.284 -26.520 -29.374 1.00 124.84 ? 476 LYS   A CG  1 
ATOM   3433 C  CD  . LYS   A 1 456 ? -34.503 -26.272 -30.246 1.00 128.06 ? 476 LYS   A CD  1 
ATOM   3434 C  CE  . LYS   A 1 456 ? -35.344 -27.533 -30.368 1.00 127.39 ? 476 LYS   A CE  1 
ATOM   3435 N  NZ  . LYS   A 1 456 ? -36.792 -27.242 -30.544 1.00 127.84 ? 476 LYS   A NZ  1 
ATOM   3436 N  N   . LEU   A 1 457 ? -29.928 -24.472 -27.253 1.00 111.54 ? 477 LEU   A N   1 
ATOM   3437 C  CA  . LEU   A 1 457 ? -29.676 -24.092 -25.873 1.00 111.32 ? 477 LEU   A CA  1 
ATOM   3438 C  C   . LEU   A 1 457 ? -30.894 -23.402 -25.273 1.00 120.93 ? 477 LEU   A C   1 
ATOM   3439 O  O   . LEU   A 1 457 ? -31.669 -22.740 -25.968 1.00 128.44 ? 477 LEU   A O   1 
ATOM   3440 C  CB  . LEU   A 1 457 ? -28.457 -23.173 -25.793 1.00 108.25 ? 477 LEU   A CB  1 
ATOM   3441 C  CG  . LEU   A 1 457 ? -27.096 -23.846 -25.978 1.00 102.78 ? 477 LEU   A CG  1 
ATOM   3442 C  CD1 . LEU   A 1 457 ? -25.997 -22.803 -26.077 1.00 96.70  ? 477 LEU   A CD1 1 
ATOM   3443 C  CD2 . LEU   A 1 457 ? -26.821 -24.800 -24.829 1.00 100.57 ? 477 LEU   A CD2 1 
ATOM   3444 N  N   . SER   A 1 458 ? -31.062 -23.578 -23.965 1.00 122.19 ? 478 SER   A N   1 
ATOM   3445 C  CA  . SER   A 1 458 ? -32.137 -22.909 -23.245 1.00 128.70 ? 478 SER   A CA  1 
ATOM   3446 C  C   . SER   A 1 458 ? -31.989 -21.400 -23.375 1.00 135.24 ? 478 SER   A C   1 
ATOM   3447 O  O   . SER   A 1 458 ? -30.958 -20.832 -23.002 1.00 127.83 ? 478 SER   A O   1 
ATOM   3448 C  CB  . SER   A 1 458 ? -32.123 -23.330 -21.776 1.00 123.03 ? 478 SER   A CB  1 
ATOM   3449 O  OG  . SER   A 1 458 ? -32.988 -22.525 -20.994 1.00 125.99 ? 478 SER   A OG  1 
ATOM   3450 N  N   . LEU   A 1 459 ? -33.034 -20.738 -23.877 1.00 155.05 ? 479 LEU   A N   1 
ATOM   3451 C  CA  . LEU   A 1 459 ? -32.976 -19.262 -24.071 1.00 144.54 ? 479 LEU   A CA  1 
ATOM   3452 C  C   . LEU   A 1 459 ? -32.970 -18.541 -22.718 1.00 141.65 ? 479 LEU   A C   1 
ATOM   3453 O  O   . LEU   A 1 459 ? -32.882 -17.298 -22.722 1.00 140.33 ? 479 LEU   A O   1 
ATOM   3454 C  CB  . LEU   A 1 459 ? -34.094 -18.842 -25.029 1.00 146.40 ? 479 LEU   A CB  1 
ATOM   3455 C  CG  . LEU   A 1 459 ? -33.965 -19.379 -26.453 1.00 149.19 ? 479 LEU   A CG  1 
ATOM   3456 C  CD1 . LEU   A 1 459 ? -35.194 -19.027 -27.276 1.00 146.85 ? 479 LEU   A CD1 1 
ATOM   3457 C  CD2 . LEU   A 1 459 ? -32.705 -18.852 -27.121 1.00 146.88 ? 479 LEU   A CD2 1 
ATOM   3458 N  N   . GLY   A 1 460 ? -33.051 -19.286 -21.611 1.00 133.05 ? 480 GLY   A N   1 
ATOM   3459 C  CA  . GLY   A 1 460 ? -33.074 -18.681 -20.297 1.00 127.65 ? 480 GLY   A CA  1 
ATOM   3460 C  C   . GLY   A 1 460 ? -31.649 -18.432 -19.847 1.00 126.21 ? 480 GLY   A C   1 
ATOM   3461 O  O   . GLY   A 1 460 ? -30.722 -18.452 -20.663 1.00 125.44 ? 480 GLY   A O   1 
ATOM   3462 N  N   . GLY   A 1 461 ? -31.455 -18.202 -18.549 1.00 126.94 ? 481 GLY   A N   1 
ATOM   3463 C  CA  . GLY   A 1 461 ? -30.284 -17.554 -17.984 1.00 126.08 ? 481 GLY   A CA  1 
ATOM   3464 C  C   . GLY   A 1 461 ? -29.188 -18.525 -17.599 1.00 126.58 ? 481 GLY   A C   1 
ATOM   3465 O  O   . GLY   A 1 461 ? -28.147 -18.124 -17.067 1.00 125.85 ? 481 GLY   A O   1 
ATOM   3466 N  N   . LEU   A 1 462 ? -29.421 -19.807 -17.863 1.00 130.25 ? 482 LEU   A N   1 
ATOM   3467 C  CA  . LEU   A 1 462 ? -28.471 -20.868 -17.570 1.00 125.35 ? 482 LEU   A CA  1 
ATOM   3468 C  C   . LEU   A 1 462 ? -28.060 -21.557 -18.863 1.00 119.87 ? 482 LEU   A C   1 
ATOM   3469 O  O   . LEU   A 1 462 ? -28.893 -21.794 -19.743 1.00 122.33 ? 482 LEU   A O   1 
ATOM   3470 C  CB  . LEU   A 1 462 ? -29.070 -21.903 -16.607 1.00 129.17 ? 482 LEU   A CB  1 
ATOM   3471 C  CG  . LEU   A 1 462 ? -28.557 -21.910 -15.166 1.00 135.01 ? 482 LEU   A CG  1 
ATOM   3472 C  CD1 . LEU   A 1 462 ? -27.056 -22.148 -15.137 1.00 132.20 ? 482 LEU   A CD1 1 
ATOM   3473 C  CD2 . LEU   A 1 462 ? -28.910 -20.613 -14.465 1.00 140.29 ? 482 LEU   A CD2 1 
ATOM   3474 N  N   . LEU   A 1 463 ? -26.770 -21.872 -18.976 1.00 111.10 ? 483 LEU   A N   1 
ATOM   3475 C  CA  . LEU   A 1 463 ? -26.252 -22.593 -20.135 1.00 103.48 ? 483 LEU   A CA  1 
ATOM   3476 C  C   . LEU   A 1 463 ? -26.671 -24.047 -19.986 1.00 104.96 ? 483 LEU   A C   1 
ATOM   3477 O  O   . LEU   A 1 463 ? -25.928 -24.901 -19.503 1.00 105.13 ? 483 LEU   A O   1 
ATOM   3478 C  CB  . LEU   A 1 463 ? -24.750 -22.456 -20.256 1.00 93.53  ? 483 LEU   A CB  1 
ATOM   3479 C  CG  . LEU   A 1 463 ? -24.277 -23.009 -21.602 1.00 90.96  ? 483 LEU   A CG  1 
ATOM   3480 C  CD1 . LEU   A 1 463 ? -24.543 -22.042 -22.758 1.00 91.09  ? 483 LEU   A CD1 1 
ATOM   3481 C  CD2 . LEU   A 1 463 ? -22.823 -23.392 -21.550 1.00 85.03  ? 483 LEU   A CD2 1 
ATOM   3482 N  N   . GLN   A 1 464 ? -27.896 -24.320 -20.409 1.00 111.10 ? 484 GLN   A N   1 
ATOM   3483 C  CA  . GLN   A 1 464 ? -28.506 -25.637 -20.328 1.00 107.65 ? 484 GLN   A CA  1 
ATOM   3484 C  C   . GLN   A 1 464 ? -29.224 -25.897 -21.645 1.00 109.57 ? 484 GLN   A C   1 
ATOM   3485 O  O   . GLN   A 1 464 ? -29.440 -24.958 -22.420 1.00 114.98 ? 484 GLN   A O   1 
ATOM   3486 C  CB  . GLN   A 1 464 ? -29.468 -25.710 -19.138 1.00 108.01 ? 484 GLN   A CB  1 
ATOM   3487 C  CG  . GLN   A 1 464 ? -28.831 -25.287 -17.823 1.00 113.45 ? 484 GLN   A CG  1 
ATOM   3488 C  CD  . GLN   A 1 464 ? -29.779 -25.378 -16.645 1.00 118.62 ? 484 GLN   A CD  1 
ATOM   3489 O  OE1 . GLN   A 1 464 ? -30.991 -25.508 -16.816 1.00 115.16 ? 484 GLN   A OE1 1 
ATOM   3490 N  NE2 . GLN   A 1 464 ? -29.228 -25.314 -15.436 1.00 123.14 ? 484 GLN   A NE2 1 
ATOM   3491 N  N   . PRO   A 1 465 ? -29.587 -27.136 -21.953 1.00 117.51 ? 485 PRO   A N   1 
ATOM   3492 C  CA  . PRO   A 1 465 ? -30.365 -27.392 -23.166 1.00 122.15 ? 485 PRO   A CA  1 
ATOM   3493 C  C   . PRO   A 1 465 ? -31.811 -26.957 -22.986 1.00 128.10 ? 485 PRO   A C   1 
ATOM   3494 O  O   . PRO   A 1 465 ? -32.338 -26.889 -21.874 1.00 125.42 ? 485 PRO   A O   1 
ATOM   3495 C  CB  . PRO   A 1 465 ? -30.273 -28.914 -23.345 1.00 119.44 ? 485 PRO   A CB  1 
ATOM   3496 C  CG  . PRO   A 1 465 ? -29.223 -29.375 -22.381 1.00 110.45 ? 485 PRO   A CG  1 
ATOM   3497 C  CD  . PRO   A 1 465 ? -29.227 -28.387 -21.268 1.00 111.56 ? 485 PRO   A CD  1 
ATOM   3498 N  N   . GLU   A 1 466 ? -32.450 -26.652 -24.116 1.00 133.96 ? 486 GLU   A N   1 
ATOM   3499 C  CA  . GLU   A 1 466 ? -33.878 -26.362 -24.086 1.00 138.00 ? 486 GLU   A CA  1 
ATOM   3500 C  C   . GLU   A 1 466 ? -34.660 -27.589 -23.635 1.00 141.57 ? 486 GLU   A C   1 
ATOM   3501 O  O   . GLU   A 1 466 ? -35.481 -27.514 -22.714 1.00 147.40 ? 486 GLU   A O   1 
ATOM   3502 C  CB  . GLU   A 1 466 ? -34.348 -25.887 -25.462 1.00 140.22 ? 486 GLU   A CB  1 
ATOM   3503 C  CG  . GLU   A 1 466 ? -35.590 -25.008 -25.419 1.00 144.09 ? 486 GLU   A CG  1 
ATOM   3504 C  CD  . GLU   A 1 466 ? -35.923 -24.395 -26.766 1.00 143.18 ? 486 GLU   A CD  1 
ATOM   3505 O  OE1 . GLU   A 1 466 ? -36.081 -25.154 -27.744 1.00 147.35 ? 486 GLU   A OE1 1 
ATOM   3506 O  OE2 . GLU   A 1 466 ? -36.019 -23.152 -26.846 1.00 152.55 ? 486 GLU   A OE2 1 
ATOM   3507 N  N   . LYS   A 1 467 ? -34.398 -28.740 -24.265 1.00 147.13 ? 487 LYS   A N   1 
ATOM   3508 C  CA  . LYS   A 1 467 ? -34.975 -30.022 -23.890 1.00 146.58 ? 487 LYS   A CA  1 
ATOM   3509 C  C   . LYS   A 1 467 ? -33.897 -30.909 -23.292 1.00 143.09 ? 487 LYS   A C   1 
ATOM   3510 O  O   . LYS   A 1 467 ? -32.791 -30.981 -23.847 1.00 141.16 ? 487 LYS   A O   1 
ATOM   3511 C  CB  . LYS   A 1 467 ? -35.605 -30.709 -25.107 1.00 147.46 ? 487 LYS   A CB  1 
ATOM   3512 C  CG  . LYS   A 1 467 ? -36.715 -31.703 -24.779 1.00 144.25 ? 487 LYS   A CG  1 
ATOM   3513 C  CD  . LYS   A 1 467 ? -37.803 -31.661 -25.847 1.00 152.22 ? 487 LYS   A CD  1 
ATOM   3514 C  CE  . LYS   A 1 467 ? -38.769 -32.837 -25.740 1.00 151.40 ? 487 LYS   A CE  1 
ATOM   3515 N  NZ  . LYS   A 1 467 ? -39.819 -32.648 -24.701 1.00 153.93 ? 487 LYS   A NZ  1 
ATOM   3516 N  N   . PRO   A 1 468 ? -34.164 -31.568 -22.164 1.00 136.43 ? 488 PRO   A N   1 
ATOM   3517 C  CA  . PRO   A 1 468 ? -33.160 -32.457 -21.568 1.00 129.95 ? 488 PRO   A CA  1 
ATOM   3518 C  C   . PRO   A 1 468 ? -32.652 -33.496 -22.561 1.00 125.37 ? 488 PRO   A C   1 
ATOM   3519 O  O   . PRO   A 1 468 ? -33.366 -33.925 -23.470 1.00 128.00 ? 488 PRO   A O   1 
ATOM   3520 C  CB  . PRO   A 1 468 ? -33.916 -33.108 -20.406 1.00 125.53 ? 488 PRO   A CB  1 
ATOM   3521 C  CG  . PRO   A 1 468 ? -34.913 -32.067 -20.002 1.00 133.38 ? 488 PRO   A CG  1 
ATOM   3522 C  CD  . PRO   A 1 468 ? -35.321 -31.362 -21.276 1.00 137.66 ? 488 PRO   A CD  1 
ATOM   3523 N  N   . VAL   A 1 469 ? -31.398 -33.895 -22.372 1.00 121.86 ? 489 VAL   A N   1 
ATOM   3524 C  CA  . VAL   A 1 469 ? -30.684 -34.743 -23.320 1.00 117.09 ? 489 VAL   A CA  1 
ATOM   3525 C  C   . VAL   A 1 469 ? -30.996 -36.204 -23.032 1.00 120.09 ? 489 VAL   A C   1 
ATOM   3526 O  O   . VAL   A 1 469 ? -30.820 -36.677 -21.904 1.00 120.46 ? 489 VAL   A O   1 
ATOM   3527 C  CB  . VAL   A 1 469 ? -29.171 -34.475 -23.253 1.00 113.27 ? 489 VAL   A CB  1 
ATOM   3528 C  CG1 . VAL   A 1 469 ? -28.395 -35.627 -23.870 1.00 108.16 ? 489 VAL   A CG1 1 
ATOM   3529 C  CG2 . VAL   A 1 469 ? -28.839 -33.169 -23.956 1.00 109.59 ? 489 VAL   A CG2 1 
ATOM   3530 N  N   . VAL   A 1 470 ? -31.452 -36.922 -24.060 1.00 121.52 ? 490 VAL   A N   1 
ATOM   3531 C  CA  . VAL   A 1 470 ? -31.796 -38.334 -23.962 1.00 123.14 ? 490 VAL   A CA  1 
ATOM   3532 C  C   . VAL   A 1 470 ? -31.033 -39.099 -25.036 1.00 125.52 ? 490 VAL   A C   1 
ATOM   3533 O  O   . VAL   A 1 470 ? -30.920 -38.636 -26.177 1.00 126.59 ? 490 VAL   A O   1 
ATOM   3534 C  CB  . VAL   A 1 470 ? -33.319 -38.558 -24.106 1.00 131.01 ? 490 VAL   A CB  1 
ATOM   3535 C  CG1 . VAL   A 1 470 ? -34.050 -37.984 -22.910 1.00 125.75 ? 490 VAL   A CG1 1 
ATOM   3536 C  CG2 . VAL   A 1 470 ? -33.834 -37.914 -25.385 1.00 131.78 ? 490 VAL   A CG2 1 
ATOM   3537 N  N   . LEU   A 1 471 ? -30.507 -40.269 -24.673 1.00 124.21 ? 491 LEU   A N   1 
ATOM   3538 C  CA  . LEU   A 1 471 ? -29.710 -41.071 -25.591 1.00 127.96 ? 491 LEU   A CA  1 
ATOM   3539 C  C   . LEU   A 1 471 ? -29.998 -42.552 -25.388 1.00 133.60 ? 491 LEU   A C   1 
ATOM   3540 O  O   . LEU   A 1 471 ? -30.450 -42.984 -24.325 1.00 135.40 ? 491 LEU   A O   1 
ATOM   3541 C  CB  . LEU   A 1 471 ? -28.203 -40.834 -25.409 1.00 117.01 ? 491 LEU   A CB  1 
ATOM   3542 C  CG  . LEU   A 1 471 ? -27.587 -39.441 -25.545 1.00 114.75 ? 491 LEU   A CG  1 
ATOM   3543 C  CD1 . LEU   A 1 471 ? -26.090 -39.530 -25.302 1.00 108.33 ? 491 LEU   A CD1 1 
ATOM   3544 C  CD2 . LEU   A 1 471 ? -27.866 -38.839 -26.908 1.00 116.55 ? 491 LEU   A CD2 1 
ATOM   3545 N  N   . LYS   A 1 472 ? -29.712 -43.328 -26.431 1.00 132.10 ? 492 LYS   A N   1 
ATOM   3546 C  CA  . LYS   A 1 472 ? -29.709 -44.779 -26.337 1.00 128.98 ? 492 LYS   A CA  1 
ATOM   3547 C  C   . LYS   A 1 472 ? -28.367 -45.250 -25.785 1.00 127.59 ? 492 LYS   A C   1 
ATOM   3548 O  O   . LYS   A 1 472 ? -27.324 -44.629 -26.015 1.00 119.22 ? 492 LYS   A O   1 
ATOM   3549 C  CB  . LYS   A 1 472 ? -29.978 -45.399 -27.710 1.00 128.08 ? 492 LYS   A CB  1 
ATOM   3550 C  CG  . LYS   A 1 472 ? -30.403 -46.856 -27.704 1.00 134.31 ? 492 LYS   A CG  1 
ATOM   3551 C  CD  . LYS   A 1 472 ? -31.428 -47.102 -28.805 1.00 134.33 ? 492 LYS   A CD  1 
ATOM   3552 C  CE  . LYS   A 1 472 ? -31.522 -48.571 -29.183 1.00 137.89 ? 492 LYS   A CE  1 
ATOM   3553 N  NZ  . LYS   A 1 472 ? -31.850 -49.439 -28.020 1.00 142.46 ? 492 LYS   A NZ  1 
ATOM   3554 N  N   . VAL   A 1 473 ? -28.402 -46.344 -25.026 1.00 126.26 ? 493 VAL   A N   1 
ATOM   3555 C  CA  . VAL   A 1 473 ? -27.220 -46.846 -24.328 1.00 125.61 ? 493 VAL   A CA  1 
ATOM   3556 C  C   . VAL   A 1 473 ? -27.154 -48.354 -24.518 1.00 132.48 ? 493 VAL   A C   1 
ATOM   3557 O  O   . VAL   A 1 473 ? -28.116 -49.064 -24.205 1.00 137.72 ? 493 VAL   A O   1 
ATOM   3558 C  CB  . VAL   A 1 473 ? -27.236 -46.494 -22.830 1.00 124.29 ? 493 VAL   A CB  1 
ATOM   3559 C  CG1 . VAL   A 1 473 ? -26.005 -47.043 -22.149 1.00 119.47 ? 493 VAL   A CG1 1 
ATOM   3560 C  CG2 . VAL   A 1 473 ? -27.318 -44.991 -22.633 1.00 119.66 ? 493 VAL   A CG2 1 
ATOM   3561 N  N   . GLU   A 1 474 ? -26.024 -48.845 -25.025 1.00 128.37 ? 494 GLU   A N   1 
ATOM   3562 C  CA  . GLU   A 1 474 ? -25.846 -50.258 -25.328 1.00 129.77 ? 494 GLU   A CA  1 
ATOM   3563 C  C   . GLU   A 1 474 ? -24.550 -50.756 -24.701 1.00 126.18 ? 494 GLU   A C   1 
ATOM   3564 O  O   . GLU   A 1 474 ? -23.617 -49.983 -24.469 1.00 126.59 ? 494 GLU   A O   1 
ATOM   3565 C  CB  . GLU   A 1 474 ? -25.858 -50.496 -26.848 1.00 132.17 ? 494 GLU   A CB  1 
ATOM   3566 C  CG  . GLU   A 1 474 ? -27.067 -49.859 -27.533 1.00 135.99 ? 494 GLU   A CG  1 
ATOM   3567 C  CD  . GLU   A 1 474 ? -27.225 -50.260 -28.987 1.00 143.82 ? 494 GLU   A CD  1 
ATOM   3568 O  OE1 . GLU   A 1 474 ? -26.285 -50.854 -29.553 1.00 143.75 ? 494 GLU   A OE1 1 
ATOM   3569 O  OE2 . GLU   A 1 474 ? -28.299 -49.978 -29.562 1.00 144.48 ? 494 GLU   A OE2 1 
ATOM   3570 N  N   . SER   A 1 475 ? -24.503 -52.058 -24.427 1.00 124.93 ? 495 SER   A N   1 
ATOM   3571 C  CA  . SER   A 1 475 ? -23.460 -52.656 -23.598 1.00 126.73 ? 495 SER   A CA  1 
ATOM   3572 C  C   . SER   A 1 475 ? -22.376 -53.278 -24.474 1.00 127.19 ? 495 SER   A C   1 
ATOM   3573 O  O   . SER   A 1 475 ? -22.651 -54.202 -25.249 1.00 125.78 ? 495 SER   A O   1 
ATOM   3574 C  CB  . SER   A 1 475 ? -24.065 -53.704 -22.663 1.00 121.96 ? 495 SER   A CB  1 
ATOM   3575 O  OG  . SER   A 1 475 ? -23.098 -54.220 -21.766 1.00 127.52 ? 495 SER   A OG  1 
ATOM   3576 N  N   . ARG   A 1 476 ? -21.147 -52.781 -24.335 1.00 127.26 ? 496 ARG   A N   1 
ATOM   3577 C  CA  . ARG   A 1 476 ? -20.001 -53.303 -25.081 1.00 121.33 ? 496 ARG   A CA  1 
ATOM   3578 C  C   . ARG   A 1 476 ? -19.753 -54.776 -24.767 1.00 119.09 ? 496 ARG   A C   1 
ATOM   3579 O  O   . ARG   A 1 476 ? -18.889 -55.413 -25.373 1.00 119.53 ? 496 ARG   A O   1 
ATOM   3580 C  CB  . ARG   A 1 476 ? -18.736 -52.493 -24.777 1.00 116.72 ? 496 ARG   A CB  1 
ATOM   3581 C  CG  . ARG   A 1 476 ? -18.802 -51.030 -25.185 1.00 116.36 ? 496 ARG   A CG  1 
ATOM   3582 C  CD  . ARG   A 1 476 ? -17.464 -50.330 -24.966 1.00 110.08 ? 496 ARG   A CD  1 
ATOM   3583 N  NE  . ARG   A 1 476 ? -16.420 -50.831 -25.853 1.00 110.76 ? 496 ARG   A NE  1 
ATOM   3584 C  CZ  . ARG   A 1 476 ? -15.167 -50.395 -25.854 1.00 106.12 ? 496 ARG   A CZ  1 
ATOM   3585 N  NH1 . ARG   A 1 476 ? -14.763 -49.451 -25.020 1.00 102.28 ? 496 ARG   A NH1 1 
ATOM   3586 N  NH2 . ARG   A 1 476 ? -14.298 -50.919 -26.715 1.00 102.53 ? 496 ARG   A NH2 1 
HETATM 3587 C  CHA . HEM   B 2 .   ? -15.242 -19.952 -10.232 1.00 81.81  ? 601 HEM   A CHA 1 
HETATM 3588 C  CHB . HEM   B 2 .   ? -15.941 -22.619 -14.225 1.00 83.45  ? 601 HEM   A CHB 1 
HETATM 3589 C  CHC . HEM   B 2 .   ? -16.422 -26.611 -11.519 1.00 85.21  ? 601 HEM   A CHC 1 
HETATM 3590 C  CHD . HEM   B 2 .   ? -15.407 -24.006 -7.563  1.00 81.50  ? 601 HEM   A CHD 1 
HETATM 3591 C  C1A . HEM   B 2 .   ? -15.389 -20.320 -11.551 1.00 81.32  ? 601 HEM   A C1A 1 
HETATM 3592 C  C2A . HEM   B 2 .   ? -15.304 -19.442 -12.700 1.00 82.11  ? 601 HEM   A C2A 1 
HETATM 3593 C  C3A . HEM   B 2 .   ? -15.500 -20.182 -13.793 1.00 80.02  ? 601 HEM   A C3A 1 
HETATM 3594 C  C4A . HEM   B 2 .   ? -15.710 -21.555 -13.383 1.00 77.16  ? 601 HEM   A C4A 1 
HETATM 3595 C  CMA . HEM   B 2 .   ? -15.495 -19.674 -15.250 1.00 78.17  ? 601 HEM   A CMA 1 
HETATM 3596 C  CAA . HEM   B 2 .   ? -15.044 -17.918 -12.667 1.00 75.65  ? 601 HEM   A CAA 1 
HETATM 3597 C  CBA . HEM   B 2 .   ? -13.590 -17.636 -13.031 1.00 78.18  ? 601 HEM   A CBA 1 
HETATM 3598 C  CGA . HEM   B 2 .   ? -13.335 -16.151 -13.124 1.00 77.05  ? 601 HEM   A CGA 1 
HETATM 3599 O  O1A . HEM   B 2 .   ? -12.250 -15.766 -13.626 1.00 69.86  ? 601 HEM   A O1A 1 
HETATM 3600 O  O2A . HEM   B 2 .   ? -14.203 -15.344 -12.703 1.00 79.01  ? 601 HEM   A O2A 1 
HETATM 3601 C  C1B . HEM   B 2 .   ? -16.121 -23.931 -13.847 1.00 81.41  ? 601 HEM   A C1B 1 
HETATM 3602 C  C2B . HEM   B 2 .   ? -16.332 -25.050 -14.744 1.00 81.76  ? 601 HEM   A C2B 1 
HETATM 3603 C  C3B . HEM   B 2 .   ? -16.463 -26.160 -13.994 1.00 83.41  ? 601 HEM   A C3B 1 
HETATM 3604 C  C4B . HEM   B 2 .   ? -16.344 -25.766 -12.605 1.00 81.10  ? 601 HEM   A C4B 1 
HETATM 3605 C  CMB . HEM   B 2 .   ? -16.374 -24.908 -16.284 1.00 77.24  ? 601 HEM   A CMB 1 
HETATM 3606 C  CAB . HEM   B 2 .   ? -16.705 -27.632 -14.421 1.00 85.26  ? 601 HEM   A CAB 1 
HETATM 3607 C  CBB . HEM   B 2 .   ? -16.886 -28.047 -15.680 1.00 83.91  ? 601 HEM   A CBB 1 
HETATM 3608 C  C1C . HEM   B 2 .   ? -16.118 -26.276 -10.218 1.00 84.07  ? 601 HEM   A C1C 1 
HETATM 3609 C  C2C . HEM   B 2 .   ? -15.933 -27.195 -9.114  1.00 86.69  ? 601 HEM   A C2C 1 
HETATM 3610 C  C3C . HEM   B 2 .   ? -15.648 -26.490 -8.017  1.00 88.07  ? 601 HEM   A C3C 1 
HETATM 3611 C  C4C . HEM   B 2 .   ? -15.647 -25.083 -8.386  1.00 84.05  ? 601 HEM   A C4C 1 
HETATM 3612 C  CMC . HEM   B 2 .   ? -16.038 -28.733 -9.185  1.00 92.15  ? 601 HEM   A CMC 1 
HETATM 3613 C  CAC . HEM   B 2 .   ? -15.386 -27.130 -6.631  1.00 88.45  ? 601 HEM   A CAC 1 
HETATM 3614 C  CBC . HEM   B 2 .   ? -15.055 -26.423 -5.546  1.00 94.33  ? 601 HEM   A CBC 1 
HETATM 3615 C  C1D . HEM   B 2 .   ? -15.342 -22.683 -7.935  1.00 81.65  ? 601 HEM   A C1D 1 
HETATM 3616 C  C2D . HEM   B 2 .   ? -15.258 -21.557 -7.032  1.00 84.47  ? 601 HEM   A C2D 1 
HETATM 3617 C  C3D . HEM   B 2 .   ? -15.221 -20.442 -7.763  1.00 84.37  ? 601 HEM   A C3D 1 
HETATM 3618 C  C4D . HEM   B 2 .   ? -15.264 -20.816 -9.159  1.00 80.78  ? 601 HEM   A C4D 1 
HETATM 3619 C  CMD . HEM   B 2 .   ? -15.236 -21.648 -5.492  1.00 84.96  ? 601 HEM   A CMD 1 
HETATM 3620 C  CAD . HEM   B 2 .   ? -15.110 -19.001 -7.231  1.00 84.11  ? 601 HEM   A CAD 1 
HETATM 3621 C  CBD . HEM   B 2 .   ? -13.649 -18.828 -6.826  1.00 84.22  ? 601 HEM   A CBD 1 
HETATM 3622 C  CGD . HEM   B 2 .   ? -13.293 -17.386 -6.599  1.00 85.43  ? 601 HEM   A CGD 1 
HETATM 3623 O  O1D . HEM   B 2 .   ? -12.237 -17.148 -5.957  1.00 82.68  ? 601 HEM   A O1D 1 
HETATM 3624 O  O2D . HEM   B 2 .   ? -14.054 -16.490 -7.051  1.00 84.60  ? 601 HEM   A O2D 1 
HETATM 3625 N  NA  . HEM   B 2 .   ? -15.632 -21.603 -12.006 1.00 77.11  ? 601 HEM   A NA  1 
HETATM 3626 N  NB  . HEM   B 2 .   ? -16.135 -24.402 -12.552 1.00 80.31  ? 601 HEM   A NB  1 
HETATM 3627 N  NC  . HEM   B 2 .   ? -15.937 -24.995 -9.735  1.00 85.23  ? 601 HEM   A NC  1 
HETATM 3628 N  ND  . HEM   B 2 .   ? -15.341 -22.194 -9.226  1.00 81.71  ? 601 HEM   A ND  1 
HETATM 3629 FE FE  . HEM   B 2 .   ? -15.688 -23.289 -10.878 1.00 70.07  ? 601 HEM   A FE  1 
HETATM 3630 C  C11 . A1A4T C 3 .   ? -20.408 -17.030 -10.828 1.00 121.46 ? 602 A1A4T A C11 1 
HETATM 3631 C  C15 . A1A4T C 3 .   ? -24.456 -14.836 -10.769 1.00 149.46 ? 602 A1A4T A C15 1 
HETATM 3632 C  C16 . A1A4T C 3 .   ? -25.420 -13.843 -11.012 1.00 145.34 ? 602 A1A4T A C16 1 
HETATM 3633 C  C17 . A1A4T C 3 .   ? -24.777 -16.170 -11.095 1.00 150.77 ? 602 A1A4T A C17 1 
HETATM 3634 C  C18 . A1A4T C 3 .   ? -26.036 -16.481 -11.654 1.00 155.13 ? 602 A1A4T A C18 1 
HETATM 3635 C  C19 . A1A4T C 3 .   ? -26.985 -15.472 -11.893 1.00 150.67 ? 602 A1A4T A C19 1 
HETATM 3636 C  C20 . A1A4T C 3 .   ? -26.673 -14.147 -11.566 1.00 145.73 ? 602 A1A4T A C20 1 
HETATM 3637 C  C23 . A1A4T C 3 .   ? -19.782 -22.689 -9.381  1.00 94.35  ? 602 A1A4T A C23 1 
HETATM 3638 C  C25 . A1A4T C 3 .   ? -18.398 -22.888 -9.485  1.00 88.19  ? 602 A1A4T A C25 1 
HETATM 3639 C  C26 . A1A4T C 3 .   ? -20.532 -22.467 -10.544 1.00 98.54  ? 602 A1A4T A C26 1 
HETATM 3640 C  C13 . A1A4T C 3 .   ? -24.254 -18.347 -6.340  1.00 130.86 ? 602 A1A4T A C13 1 
HETATM 3641 C  C14 . A1A4T C 3 .   ? -23.119 -14.339 -10.145 1.00 143.43 ? 602 A1A4T A C14 1 
HETATM 3642 C  C22 . A1A4T C 3 .   ? -20.160 -18.318 -11.636 1.00 116.57 ? 602 A1A4T A C22 1 
HETATM 3643 C  C01 . A1A4T C 3 .   ? -20.479 -22.720 -8.006  1.00 103.90 ? 602 A1A4T A C01 1 
HETATM 3644 C  C02 . A1A4T C 3 .   ? -20.177 -21.487 -7.128  1.00 105.81 ? 602 A1A4T A C02 1 
HETATM 3645 C  C03 . A1A4T C 3 .   ? -19.984 -20.183 -7.923  1.00 106.50 ? 602 A1A4T A C03 1 
HETATM 3646 C  C05 . A1A4T C 3 .   ? -21.916 -18.676 -7.215  1.00 120.26 ? 602 A1A4T A C05 1 
HETATM 3647 C  C06 . A1A4T C 3 .   ? -23.298 -18.059 -7.510  1.00 131.08 ? 602 A1A4T A C06 1 
HETATM 3648 C  C08 . A1A4T C 3 .   ? -21.718 -15.603 -8.377  1.00 129.15 ? 602 A1A4T A C08 1 
HETATM 3649 C  C09 . A1A4T C 3 .   ? -21.874 -15.232 -9.876  1.00 134.67 ? 602 A1A4T A C09 1 
HETATM 3650 C  C27 . A1A4T C 3 .   ? -19.862 -22.445 -11.775 1.00 92.48  ? 602 A1A4T A C27 1 
HETATM 3651 C  C28 . A1A4T C 3 .   ? -18.477 -22.648 -11.800 1.00 89.18  ? 602 A1A4T A C28 1 
HETATM 3652 C  C29 . A1A4T C 3 .   ? -21.394 -19.230 -11.521 1.00 117.48 ? 602 A1A4T A C29 1 
HETATM 3653 C  C30 . A1A4T C 3 .   ? -18.911 -19.049 -11.104 1.00 100.41 ? 602 A1A4T A C30 1 
HETATM 3654 C  C31 . A1A4T C 3 .   ? -19.914 -17.944 -13.103 1.00 110.69 ? 602 A1A4T A C31 1 
HETATM 3655 C  C32 . A1A4T C 3 .   ? -24.587 -19.822 -6.072  1.00 130.43 ? 602 A1A4T A C32 1 
HETATM 3656 C  C33 . A1A4T C 3 .   ? -23.717 -20.606 -5.308  1.00 124.07 ? 602 A1A4T A C33 1 
HETATM 3657 C  C34 . A1A4T C 3 .   ? -25.778 -20.354 -6.574  1.00 138.21 ? 602 A1A4T A C34 1 
HETATM 3658 C  C35 . A1A4T C 3 .   ? -26.095 -21.690 -6.322  1.00 137.14 ? 602 A1A4T A C35 1 
HETATM 3659 C  C36 . A1A4T C 3 .   ? -25.223 -22.473 -5.560  1.00 129.76 ? 602 A1A4T A C36 1 
HETATM 3660 C  C37 . A1A4T C 3 .   ? -24.031 -21.943 -5.056  1.00 125.29 ? 602 A1A4T A C37 1 
HETATM 3661 C  C38 . A1A4T C 3 .   ? -28.371 -15.799 -12.498 1.00 149.12 ? 602 A1A4T A C38 1 
HETATM 3662 C  C39 . A1A4T C 3 .   ? -29.291 -14.763 -12.714 1.00 143.60 ? 602 A1A4T A C39 1 
HETATM 3663 C  C40 . A1A4T C 3 .   ? -30.554 -15.036 -13.258 1.00 141.13 ? 602 A1A4T A C40 1 
HETATM 3664 C  C41 . A1A4T C 3 .   ? -30.902 -16.352 -13.588 1.00 141.66 ? 602 A1A4T A C41 1 
HETATM 3665 C  C42 . A1A4T C 3 .   ? -29.988 -17.392 -13.373 1.00 144.85 ? 602 A1A4T A C42 1 
HETATM 3666 C  C43 . A1A4T C 3 .   ? -28.725 -17.117 -12.829 1.00 146.24 ? 602 A1A4T A C43 1 
HETATM 3667 N  N04 . A1A4T C 3 .   ? -21.296 -19.581 -8.197  1.00 114.67 ? 602 A1A4T A N04 1 
HETATM 3668 N  N10 . A1A4T C 3 .   ? -21.761 -16.455 -10.689 1.00 127.69 ? 602 A1A4T A N10 1 
HETATM 3669 N  N24 . A1A4T C 3 .   ? -17.783 -22.862 -10.675 1.00 88.46  ? 602 A1A4T A N24 1 
HETATM 3670 O  O12 . A1A4T C 3 .   ? -21.350 -18.431 -6.183  1.00 115.06 ? 602 A1A4T A O12 1 
HETATM 3671 O  O21 . A1A4T C 3 .   ? -19.471 -16.486 -10.311 1.00 112.28 ? 602 A1A4T A O21 1 
HETATM 3672 S  S07 . A1A4T C 3 .   ? -23.251 -16.241 -7.646  1.00 136.37 ? 602 A1A4T A S07 1 
HETATM 3673 O  O   . HOH   D 4 .   ? -23.189 -11.747 -15.971 1.00 95.74  ? 701 HOH   A O   1 
HETATM 3674 O  O   . HOH   D 4 .   ? -22.599 -35.776 -36.960 1.00 104.88 ? 702 HOH   A O   1 
HETATM 3675 O  O   . HOH   D 4 .   ? -19.924 -53.729 -21.616 1.00 120.18 ? 703 HOH   A O   1 
HETATM 3676 O  O   . HOH   D 4 .   ? -9.961  -20.963 -18.233 1.00 80.01  ? 704 HOH   A O   1 
HETATM 3677 O  O   . HOH   D 4 .   ? -31.023 -16.651 5.543   1.00 130.65 ? 705 HOH   A O   1 
HETATM 3678 O  O   . HOH   D 4 .   ? -35.730 -50.259 -16.221 1.00 155.79 ? 706 HOH   A O   1 
HETATM 3679 O  O   . HOH   D 4 .   ? -2.379  -9.410  -9.679  1.00 109.71 ? 707 HOH   A O   1 
HETATM 3680 O  O   . HOH   D 4 .   ? -36.488 -47.610 -26.809 1.00 167.80 ? 708 HOH   A O   1 
HETATM 3681 O  O   . HOH   D 4 .   ? -33.126 5.656   -15.709 1.00 94.79  ? 709 HOH   A O   1 
HETATM 3682 O  O   . HOH   D 4 .   ? -9.966  -23.362 -34.091 1.00 89.99  ? 710 HOH   A O   1 
HETATM 3683 O  O   . HOH   D 4 .   ? -27.477 -53.157 -24.672 1.00 137.72 ? 711 HOH   A O   1 
HETATM 3684 O  O   . HOH   D 4 .   ? -21.278 -57.398 -24.366 1.00 125.11 ? 712 HOH   A O   1 
HETATM 3685 O  O   . HOH   D 4 .   ? -28.346 -17.657 -22.918 1.00 99.25  ? 713 HOH   A O   1 
HETATM 3686 O  O   . HOH   D 4 .   ? -5.867  -25.483 -22.279 1.00 88.65  ? 714 HOH   A O   1 
HETATM 3687 O  O   . HOH   D 4 .   ? -8.661  -25.537 -19.793 1.00 78.43  ? 715 HOH   A O   1 
HETATM 3688 O  O   . HOH   D 4 .   ? -6.747  -27.827 -18.346 1.00 76.49  ? 716 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   ? 1.7969 1.4532 1.6829 0.2403  0.0161  -0.0018 28  HIS   A N   
2    C  CA  . HIS   A 8   ? 1.9860 1.5881 1.8667 0.2106  0.0280  0.0065  28  HIS   A CA  
3    C  C   . HIS   A 8   ? 2.0103 1.6408 1.9081 0.1749  0.0333  0.0133  28  HIS   A C   
4    O  O   . HIS   A 8   ? 1.9874 1.6794 1.9023 0.1697  0.0278  0.0059  28  HIS   A O   
5    C  CB  . HIS   A 8   ? 2.0392 1.6221 1.9295 0.2022  0.0279  -0.0159 28  HIS   A CB  
6    C  CG  . HIS   A 8   ? 2.1393 1.6718 2.0330 0.1705  0.0350  -0.0140 28  HIS   A CG  
7    N  ND1 . HIS   A 8   ? 2.1634 1.6254 2.0416 0.1702  0.0445  0.0034  28  HIS   A ND1 
8    C  CD2 . HIS   A 8   ? 2.1197 1.6622 2.0336 0.1385  0.0330  -0.0283 28  HIS   A CD2 
9    C  CE1 . HIS   A 8   ? 2.1447 1.5794 2.0419 0.1366  0.0482  -0.0024 28  HIS   A CE1 
10   N  NE2 . HIS   A 8   ? 2.0689 1.5527 1.9867 0.1184  0.0388  -0.0225 28  HIS   A NE2 
11   N  N   . SER   A 9   ? 1.7725 1.3568 1.6690 0.1511  0.0451  0.0271  29  SER   A N   
12   C  CA  . SER   A 9   ? 1.6986 1.3022 1.6144 0.1183  0.0525  0.0354  29  SER   A CA  
13   C  C   . SER   A 9   ? 1.4553 1.0813 1.3547 0.1293  0.0564  0.0554  29  SER   A C   
14   O  O   . SER   A 9   ? 1.4145 1.0525 1.3251 0.1068  0.0658  0.0660  29  SER   A O   
15   C  CB  . SER   A 9   ? 1.7062 1.3620 1.6512 0.0960  0.0435  0.0132  29  SER   A CB  
16   O  OG  . SER   A 9   ? 1.6004 1.3176 1.5488 0.1053  0.0372  0.0093  29  SER   A OG  
17   N  N   . HIS   A 10  ? 1.5292 1.1606 1.4017 0.1658  0.0481  0.0591  30  HIS   A N   
18   C  CA  . HIS   A 10  ? 1.4502 1.0982 1.2987 0.1822  0.0473  0.0750  30  HIS   A CA  
19   C  C   . HIS   A 10  ? 1.4047 0.9869 1.2147 0.1888  0.0663  0.1057  30  HIS   A C   
20   O  O   . HIS   A 10  ? 1.4028 0.9900 1.1848 0.2008  0.0695  0.1214  30  HIS   A O   
21   C  CB  . HIS   A 10  ? 1.3986 1.0786 1.2355 0.2213  0.0268  0.0642  30  HIS   A CB  
22   C  CG  . HIS   A 10  ? 1.3316 1.0870 1.2081 0.2137  0.0135  0.0385  30  HIS   A CG  
23   N  ND1 . HIS   A 10  ? 1.2814 1.0835 1.1645 0.2412  -0.0047 0.0255  30  HIS   A ND1 
24   C  CD2 . HIS   A 10  ? 1.3216 1.1113 1.2337 0.1821  0.0170  0.0236  30  HIS   A CD2 
25   C  CE1 . HIS   A 10  ? 1.2747 1.1357 1.1995 0.2241  -0.0080 0.0047  30  HIS   A CE1 
26   N  NE2 . HIS   A 10  ? 1.2670 1.1189 1.2045 0.1897  0.0055  0.0045  30  HIS   A NE2 
27   N  N   . GLY   A 11  ? 1.4505 0.9681 1.2566 0.1817  0.0806  0.1142  31  GLY   A N   
28   C  CA  . GLY   A 11  ? 1.5218 0.9711 1.2999 0.1797  0.1067  0.1444  31  GLY   A CA  
29   C  C   . GLY   A 11  ? 1.5156 0.9644 1.3304 0.1359  0.1278  0.1510  31  GLY   A C   
30   O  O   . GLY   A 11  ? 1.6189 1.0099 1.4223 0.1278  0.1555  0.1755  31  GLY   A O   
31   N  N   . LEU   A 12  ? 1.4651 0.9761 1.3250 0.1085  0.1168  0.1303  32  LEU   A N   
32   C  CA  . LEU   A 12  ? 1.4046 0.9231 1.3081 0.0681  0.1316  0.1316  32  LEU   A CA  
33   C  C   . LEU   A 12  ? 1.4557 0.9623 1.3418 0.0666  0.1572  0.1598  32  LEU   A C   
34   O  O   . LEU   A 12  ? 1.5296 0.9843 1.4218 0.0524  0.1856  0.1792  32  LEU   A O   
35   C  CB  . LEU   A 12  ? 1.3357 0.9255 1.2781 0.0483  0.1121  0.1059  32  LEU   A CB  
36   C  CG  . LEU   A 12  ? 1.3567 0.9549 1.3520 0.0081  0.1183  0.0983  32  LEU   A CG  
37   C  CD1 . LEU   A 12  ? 1.4990 1.0718 1.5189 -0.0050 0.1070  0.0769  32  LEU   A CD1 
38   C  CD2 . LEU   A 12  ? 1.2653 0.9315 1.2834 -0.0052 0.1072  0.0865  32  LEU   A CD2 
39   N  N   . PHE   A 13  ? 1.4117 0.9640 1.2766 0.0812  0.1493  0.1615  33  PHE   A N   
40   C  CA  . PHE   A 13  ? 1.4502 0.9937 1.2935 0.0819  0.1735  0.1861  33  PHE   A CA  
41   C  C   . PHE   A 13  ? 1.5518 1.0215 1.3338 0.1103  0.1960  0.2168  33  PHE   A C   
42   O  O   . PHE   A 13  ? 1.5724 1.0125 1.3384 0.1057  0.2279  0.2420  33  PHE   A O   
43   C  CB  . PHE   A 13  ? 1.3507 0.9553 1.1796 0.0948  0.1562  0.1776  33  PHE   A CB  
44   C  CG  . PHE   A 13  ? 1.2717 0.9423 1.1547 0.0676  0.1396  0.1521  33  PHE   A CG  
45   C  CD1 . PHE   A 13  ? 1.2485 0.9297 1.1805 0.0319  0.1534  0.1511  33  PHE   A CD1 
46   C  CD2 . PHE   A 13  ? 1.1843 0.9049 1.0704 0.0789  0.1111  0.1292  33  PHE   A CD2 
47   C  CE1 . PHE   A 13  ? 1.1928 0.9291 1.1668 0.0113  0.1368  0.1289  33  PHE   A CE1 
48   C  CE2 . PHE   A 13  ? 1.1442 0.9171 1.0727 0.0557  0.0994  0.1086  33  PHE   A CE2 
49   C  CZ  . PHE   A 13  ? 1.1165 0.8953 1.0843 0.0235  0.1111  0.1091  33  PHE   A CZ  
50   N  N   . LYS   A 14  ? 1.5744 1.0113 1.3195 0.1415  0.1820  0.2161  34  LYS   A N   
51   C  CA  . LYS   A 14  ? 1.6405 0.9970 1.3226 0.1707  0.2038  0.2467  34  LYS   A CA  
52   C  C   . LYS   A 14  ? 1.7407 1.0292 1.4471 0.1441  0.2377  0.2624  34  LYS   A C   
53   O  O   . LYS   A 14  ? 1.8441 1.0612 1.5052 0.1572  0.2705  0.2947  34  LYS   A O   
54   C  CB  . LYS   A 14  ? 1.7296 1.0722 1.3674 0.2153  0.1762  0.2400  34  LYS   A CB  
55   C  CG  . LYS   A 14  ? 1.7972 1.2033 1.4132 0.2448  0.1428  0.2244  34  LYS   A CG  
56   C  CD  . LYS   A 14  ? 1.9083 1.2809 1.4580 0.3000  0.1251  0.2316  34  LYS   A CD  
57   C  CE  . LYS   A 14  ? 1.8877 1.2445 1.4533 0.3117  0.1095  0.2168  34  LYS   A CE  
58   N  NZ  . LYS   A 14  ? 1.8553 1.1960 1.3651 0.3688  0.0850  0.2182  34  LYS   A NZ  
59   N  N   . LYS   A 15  ? 1.6784 0.9846 1.4539 0.1078  0.2310  0.2396  35  LYS   A N   
60   C  CA  . LYS   A 15  ? 1.7398 0.9896 1.5545 0.0763  0.2593  0.2476  35  LYS   A CA  
61   C  C   . LYS   A 15  ? 1.7288 0.9925 1.5916 0.0388  0.2896  0.2578  35  LYS   A C   
62   O  O   . LYS   A 15  ? 1.8097 1.0146 1.6905 0.0200  0.3265  0.2772  35  LYS   A O   
63   C  CB  . LYS   A 15  ? 1.7598 1.0233 1.6268 0.0559  0.2341  0.2141  35  LYS   A CB  
64   C  CG  . LYS   A 15  ? 1.7899 0.9948 1.7034 0.0233  0.2561  0.2149  35  LYS   A CG  
65   C  CD  . LYS   A 15  ? 1.9064 1.1458 1.8806 -0.0038 0.2271  0.1757  35  LYS   A CD  
66   C  CE  . LYS   A 15  ? 1.8456 1.1331 1.8921 -0.0465 0.2307  0.1642  35  LYS   A CE  
67   N  NZ  . LYS   A 15  ? 1.7298 1.0812 1.8107 -0.0586 0.1923  0.1265  35  LYS   A NZ  
68   N  N   . LEU   A 16  ? 1.6763 1.0155 1.5633 0.0278  0.2765  0.2451  36  LEU   A N   
69   C  CA  . LEU   A 16  ? 1.6058 0.9694 1.5447 -0.0058 0.3014  0.2508  36  LEU   A CA  
70   C  C   . LEU   A 16  ? 1.6031 0.9460 1.4926 0.0111  0.3364  0.2843  36  LEU   A C   
71   O  O   . LEU   A 16  ? 1.6228 0.9770 1.5535 -0.0145 0.3658  0.2936  36  LEU   A O   
72   C  CB  . LEU   A 16  ? 1.5567 1.0079 1.5427 -0.0237 0.2703  0.2207  36  LEU   A CB  
73   C  CG  . LEU   A 16  ? 1.5349 1.0097 1.6016 -0.0615 0.2552  0.1924  36  LEU   A CG  
74   C  CD1 . LEU   A 16  ? 1.4837 1.0325 1.5661 -0.0633 0.2164  0.1627  36  LEU   A CD1 
75   C  CD2 . LEU   A 16  ? 1.6059 1.0791 1.7377 -0.0967 0.2868  0.2011  36  LEU   A CD2 
76   N  N   . GLY   A 17  ? 1.6651 0.9785 1.4673 0.0555  0.3334  0.3012  37  GLY   A N   
77   C  CA  . GLY   A 17  ? 1.6049 0.8994 1.3476 0.0771  0.3620  0.3301  37  GLY   A CA  
78   C  C   . GLY   A 17  ? 1.6228 0.9933 1.3681 0.0790  0.3437  0.3162  37  GLY   A C   
79   O  O   . GLY   A 17  ? 1.6019 0.9683 1.3249 0.0821  0.3729  0.3355  37  GLY   A O   
80   N  N   . ILE   A 18  ? 1.5959 1.0322 1.3665 0.0775  0.2988  0.2837  38  ILE   A N   
81   C  CA  . ILE   A 18  ? 1.4920 0.9998 1.2699 0.0774  0.2790  0.2674  38  ILE   A CA  
82   C  C   . ILE   A 18  ? 1.4611 0.9803 1.1712 0.1208  0.2478  0.2612  38  ILE   A C   
83   O  O   . ILE   A 18  ? 1.4584 0.9796 1.1640 0.1351  0.2193  0.2464  38  ILE   A O   
84   C  CB  . ILE   A 18  ? 1.4039 0.9767 1.2611 0.0435  0.2532  0.2352  38  ILE   A CB  
85   C  CG1 . ILE   A 18  ? 1.3916 0.9641 1.3207 0.0023  0.2798  0.2379  38  ILE   A CG1 
86   C  CG2 . ILE   A 18  ? 1.3673 1.0074 1.2222 0.0497  0.2283  0.2174  38  ILE   A CG2 
87   C  CD1 . ILE   A 18  ? 1.2837 0.9030 1.2842 -0.0275 0.2526  0.2068  38  ILE   A CD1 
88   N  N   . PRO   A 19  ? 1.4503 0.9786 1.1108 0.1431  0.2508  0.2696  39  PRO   A N   
89   C  CA  . PRO   A 19  ? 1.4042 0.9421 1.0024 0.1863  0.2180  0.2612  39  PRO   A CA  
90   C  C   . PRO   A 19  ? 1.4102 1.0264 1.0527 0.1787  0.1760  0.2248  39  PRO   A C   
91   O  O   . PRO   A 19  ? 1.3719 1.0337 1.0807 0.1432  0.1737  0.2086  39  PRO   A O   
92   C  CB  . PRO   A 19  ? 1.4639 0.9857 0.9998 0.2077  0.2371  0.2796  39  PRO   A CB  
93   C  CG  . PRO   A 19  ? 1.4318 0.9808 1.0260 0.1674  0.2649  0.2813  39  PRO   A CG  
94   C  CD  . PRO   A 19  ? 1.4278 0.9602 1.0896 0.1307  0.2832  0.2845  39  PRO   A CD  
95   N  N   . GLY   A 20  ? 1.4017 1.0315 1.0061 0.2146  0.1430  0.2119  40  GLY   A N   
96   C  CA  . GLY   A 20  ? 1.3650 1.0655 1.0086 0.2112  0.1061  0.1784  40  GLY   A CA  
97   C  C   . GLY   A 20  ? 1.4154 1.1210 1.0253 0.2526  0.0719  0.1655  40  GLY   A C   
98   O  O   . GLY   A 20  ? 1.4977 1.1491 1.0501 0.2862  0.0739  0.1828  40  GLY   A O   
99   N  N   . PRO   A 21  ? 1.4013 1.1720 1.0488 0.2518  0.0404  0.1346  41  PRO   A N   
100  C  CA  . PRO   A 21  ? 1.3481 1.1343 0.9806 0.2895  0.0055  0.1174  41  PRO   A CA  
101  C  C   . PRO   A 21  ? 1.3894 1.1597 1.0439 0.2925  0.0024  0.1148  41  PRO   A C   
102  O  O   . PRO   A 21  ? 1.4000 1.1808 1.1057 0.2590  0.0141  0.1094  41  PRO   A O   
103  C  CB  . PRO   A 21  ? 1.2921 1.1556 0.9753 0.2777  -0.0196 0.0846  41  PRO   A CB  
104  C  CG  . PRO   A 21  ? 1.2172 1.1022 0.9541 0.2300  0.0017  0.0832  41  PRO   A CG  
105  C  CD  . PRO   A 21  ? 1.2263 1.0582 0.9336 0.2174  0.0364  0.1140  41  PRO   A CD  
106  N  N   . THR   A 22  ? 1.4907 1.2331 1.1024 0.3357  -0.0148 0.1178  42  THR   A N   
107  C  CA  . THR   A 22  ? 1.5255 1.2492 1.1531 0.3446  -0.0187 0.1147  42  THR   A CA  
108  C  C   . THR   A 22  ? 1.4209 1.2171 1.1201 0.3336  -0.0411 0.0799  42  THR   A C   
109  O  O   . THR   A 22  ? 1.4012 1.2502 1.1153 0.3509  -0.0692 0.0574  42  THR   A O   
110  C  CB  . THR   A 22  ? 1.5677 1.2429 1.1288 0.3986  -0.0332 0.1266  42  THR   A CB  
111  O  OG1 . THR   A 22  ? 1.6050 1.3002 1.1259 0.4313  -0.0584 0.1199  42  THR   A OG1 
112  C  CG2 . THR   A 22  ? 1.6390 1.2217 1.1418 0.4024  0.0013  0.1649  42  THR   A CG2 
113  N  N   . PRO   A 23  ? 1.2869 1.0864 1.0317 0.3056  -0.0286 0.0736  43  PRO   A N   
114  C  CA  . PRO   A 23  ? 1.2232 1.0872 1.0320 0.2940  -0.0427 0.0429  43  PRO   A CA  
115  C  C   . PRO   A 23  ? 1.2793 1.1520 1.0954 0.3305  -0.0636 0.0281  43  PRO   A C   
116  O  O   . PRO   A 23  ? 1.3338 1.1522 1.1098 0.3587  -0.0635 0.0425  43  PRO   A O   
117  C  CB  . PRO   A 23  ? 1.2010 1.0523 1.0407 0.2540  -0.0195 0.0447  43  PRO   A CB  
118  C  CG  . PRO   A 23  ? 1.2429 1.0168 1.0409 0.2583  -0.0012 0.0712  43  PRO   A CG  
119  C  CD  . PRO   A 23  ? 1.2806 1.0246 1.0218 0.2804  0.0008  0.0932  43  PRO   A CD  
120  N  N   . LEU   A 24  ? 1.1648 1.1064 1.0361 0.3298  -0.0800 -0.0009 44  LEU   A N   
121  C  CA  . LEU   A 24  ? 1.1400 1.1030 1.0387 0.3582  -0.0960 -0.0198 44  LEU   A CA  
122  C  C   . LEU   A 24  ? 1.1153 1.0696 1.0444 0.3366  -0.0761 -0.0250 44  LEU   A C   
123  O  O   . LEU   A 24  ? 1.0678 1.0239 1.0129 0.2972  -0.0567 -0.0232 44  LEU   A O   
124  C  CB  . LEU   A 24  ? 1.1292 1.1731 1.0830 0.3656  -0.1194 -0.0506 44  LEU   A CB  
125  C  CG  . LEU   A 24  ? 1.0930 1.1547 1.0229 0.3902  -0.1468 -0.0545 44  LEU   A CG  
126  C  CD1 . LEU   A 24  ? 1.0011 1.1472 1.0035 0.3865  -0.1667 -0.0894 44  LEU   A CD1 
127  C  CD2 . LEU   A 24  ? 1.1361 1.1567 1.0102 0.4432  -0.1686 -0.0448 44  LEU   A CD2 
128  N  N   . PRO   A 25  ? 1.1263 1.0682 1.0601 0.3640  -0.0816 -0.0322 45  PRO   A N   
129  C  CA  . PRO   A 25  ? 1.1090 1.0452 1.0701 0.3468  -0.0639 -0.0415 45  PRO   A CA  
130  C  C   . PRO   A 25  ? 1.0880 1.0908 1.1082 0.3184  -0.0567 -0.0638 45  PRO   A C   
131  O  O   . PRO   A 25  ? 1.0579 1.1224 1.1167 0.3241  -0.0699 -0.0807 45  PRO   A O   
132  C  CB  . PRO   A 25  ? 1.1060 1.0331 1.0684 0.3900  -0.0763 -0.0505 45  PRO   A CB  
133  C  CG  . PRO   A 25  ? 1.1711 1.0590 1.0791 0.4259  -0.0937 -0.0321 45  PRO   A CG  
134  C  CD  . PRO   A 25  ? 1.1531 1.0749 1.0575 0.4149  -0.1035 -0.0299 45  PRO   A CD  
135  N  N   . PHE   A 26  ? 1.0514 1.0375 1.0762 0.2873  -0.0354 -0.0636 46  PHE   A N   
136  C  CA  . PHE   A 26  ? 1.0311 1.0647 1.0996 0.2614  -0.0227 -0.0812 46  PHE   A CA  
137  C  C   . PHE   A 26  ? 0.9767 1.0487 1.0608 0.2356  -0.0231 -0.0806 46  PHE   A C   
138  O  O   . PHE   A 26  ? 1.0536 1.1305 1.1451 0.2043  -0.0079 -0.0812 46  PHE   A O   
139  C  CB  . PHE   A 26  ? 1.0102 1.0929 1.1267 0.2836  -0.0250 -0.1053 46  PHE   A CB  
140  C  CG  . PHE   A 26  ? 1.1544 1.2030 1.2611 0.3051  -0.0188 -0.1098 46  PHE   A CG  
141  C  CD1 . PHE   A 26  ? 1.2585 1.2418 1.3235 0.2933  -0.0073 -0.0982 46  PHE   A CD1 
142  C  CD2 . PHE   A 26  ? 1.2103 1.2931 1.3534 0.3376  -0.0252 -0.1280 46  PHE   A CD2 
143  C  CE1 . PHE   A 26  ? 1.2653 1.2129 1.3190 0.3137  -0.0022 -0.1044 46  PHE   A CE1 
144  C  CE2 . PHE   A 26  ? 1.2371 1.2866 1.3697 0.3595  -0.0184 -0.1328 46  PHE   A CE2 
145  C  CZ  . PHE   A 26  ? 1.2667 1.2460 1.3514 0.3476  -0.0068 -0.1210 46  PHE   A CZ  
146  N  N   . LEU   A 27  ? 0.9883 1.0848 1.0739 0.2507  -0.0417 -0.0804 47  LEU   A N   
147  C  CA  . LEU   A 27  ? 0.9928 1.1292 1.0981 0.2290  -0.0434 -0.0845 47  LEU   A CA  
148  C  C   . LEU   A 27  ? 1.0487 1.1480 1.1127 0.2076  -0.0366 -0.0622 47  LEU   A C   
149  O  O   . LEU   A 27  ? 1.0107 1.1310 1.0886 0.1801  -0.0289 -0.0635 47  LEU   A O   
150  C  CB  . LEU   A 27  ? 0.9176 1.0977 1.0437 0.2546  -0.0692 -0.0985 47  LEU   A CB  
151  C  CG  . LEU   A 27  ? 0.9284 1.1627 1.1156 0.2730  -0.0771 -0.1257 47  LEU   A CG  
152  C  CD1 . LEU   A 27  ? 0.8885 1.1628 1.0942 0.3006  -0.1096 -0.1410 47  LEU   A CD1 
153  C  CD2 . LEU   A 27  ? 0.9232 1.1988 1.1647 0.2415  -0.0546 -0.1406 47  LEU   A CD2 
154  N  N   . GLY   A 28  ? 1.0890 1.1325 1.1048 0.2199  -0.0371 -0.0414 48  GLY   A N   
155  C  CA  . GLY   A 28  ? 1.0171 1.0305 1.0000 0.2023  -0.0288 -0.0205 48  GLY   A CA  
156  C  C   . GLY   A 28  ? 0.9886 1.0239 0.9583 0.2168  -0.0442 -0.0202 48  GLY   A C   
157  O  O   . GLY   A 28  ? 1.0418 1.0813 0.9980 0.2517  -0.0640 -0.0248 48  GLY   A O   
158  N  N   . ASN   A 29  ? 0.9999 1.0492 0.9719 0.1927  -0.0376 -0.0167 49  ASN   A N   
159  C  CA  . ASN   A 29  ? 1.0188 1.0874 0.9757 0.2047  -0.0518 -0.0188 49  ASN   A CA  
160  C  C   . ASN   A 29  ? 1.0053 1.1359 1.0118 0.1904  -0.0603 -0.0435 49  ASN   A C   
161  O  O   . ASN   A 29  ? 1.0253 1.1732 1.0234 0.1960  -0.0725 -0.0489 49  ASN   A O   
162  C  CB  . ASN   A 29  ? 1.0148 1.0464 0.9310 0.1924  -0.0362 0.0051  49  ASN   A CB  
163  C  CG  . ASN   A 29  ? 1.0658 1.0330 0.9292 0.2107  -0.0267 0.0309  49  ASN   A CG  
164  O  OD1 . ASN   A 29  ? 1.0202 0.9508 0.8803 0.1908  -0.0050 0.0472  49  ASN   A OD1 
165  N  ND2 . ASN   A 29  ? 1.1127 1.0638 0.9348 0.2499  -0.0435 0.0341  49  ASN   A ND2 
166  N  N   . ILE   A 30  ? 1.0131 1.1735 1.0687 0.1732  -0.0525 -0.0589 50  ILE   A N   
167  C  CA  . ILE   A 30  ? 0.9798 1.1911 1.0837 0.1538  -0.0522 -0.0788 50  ILE   A CA  
168  C  C   . ILE   A 30  ? 0.9441 1.1985 1.0729 0.1747  -0.0781 -0.1011 50  ILE   A C   
169  O  O   . ILE   A 30  ? 0.9897 1.2790 1.1503 0.1592  -0.0805 -0.1160 50  ILE   A O   
170  C  CB  . ILE   A 30  ? 0.9740 1.2024 1.1194 0.1366  -0.0352 -0.0894 50  ILE   A CB  
171  C  CG1 . ILE   A 30  ? 0.9301 1.1716 1.0976 0.1621  -0.0431 -0.1022 50  ILE   A CG1 
172  C  CG2 . ILE   A 30  ? 0.9987 1.1862 1.1189 0.1155  -0.0147 -0.0716 50  ILE   A CG2 
173  C  CD1 . ILE   A 30  ? 0.9614 1.2230 1.1698 0.1487  -0.0236 -0.1146 50  ILE   A CD1 
174  N  N   . LEU   A 31  ? 1.0622 1.3140 1.1783 0.2106  -0.0995 -0.1054 51  LEU   A N   
175  C  CA  . LEU   A 31  ? 0.9883 1.2787 1.1223 0.2344  -0.1309 -0.1281 51  LEU   A CA  
176  C  C   . LEU   A 31  ? 1.0674 1.3442 1.1579 0.2359  -0.1410 -0.1221 51  LEU   A C   
177  O  O   . LEU   A 31  ? 1.1355 1.4499 1.2494 0.2439  -0.1648 -0.1458 51  LEU   A O   
178  C  CB  . LEU   A 31  ? 0.8903 1.1734 1.0080 0.2785  -0.1550 -0.1316 51  LEU   A CB  
179  C  CG  . LEU   A 31  ? 0.9225 1.2302 1.0923 0.2852  -0.1509 -0.1451 51  LEU   A CG  
180  C  CD1 . LEU   A 31  ? 0.8640 1.1856 1.0354 0.3328  -0.1849 -0.1592 51  LEU   A CD1 
181  C  CD2 . LEU   A 31  ? 0.7704 1.1366 1.0223 0.2554  -0.1381 -0.1690 51  LEU   A CD2 
182  N  N   . SER   A 32  ? 1.0527 1.2770 1.0835 0.2286  -0.1229 -0.0928 52  SER   A N   
183  C  CA  . SER   A 32  ? 1.1575 1.3661 1.1452 0.2290  -0.1258 -0.0852 52  SER   A CA  
184  C  C   . SER   A 32  ? 1.1936 1.4286 1.2170 0.1924  -0.1125 -0.0936 52  SER   A C   
185  O  O   . SER   A 32  ? 1.2677 1.4936 1.2610 0.1913  -0.1141 -0.0905 52  SER   A O   
186  C  CB  . SER   A 32  ? 1.1651 1.3087 1.0826 0.2343  -0.1061 -0.0500 52  SER   A CB  
187  O  OG  . SER   A 32  ? 1.1311 1.2412 1.0092 0.2696  -0.1160 -0.0395 52  SER   A OG  
188  N  N   . TYR   A 33  ? 1.1417 1.4044 1.2231 0.1647  -0.0980 -0.1033 53  TYR   A N   
189  C  CA  . TYR   A 33  ? 1.1342 1.4225 1.2526 0.1334  -0.0870 -0.1139 53  TYR   A CA  
190  C  C   . TYR   A 33  ? 1.2129 1.5509 1.3805 0.1371  -0.1092 -0.1468 53  TYR   A C   
191  O  O   . TYR   A 33  ? 1.1992 1.5604 1.4086 0.1105  -0.0986 -0.1587 53  TYR   A O   
192  C  CB  . TYR   A 33  ? 1.0348 1.3264 1.1878 0.1052  -0.0608 -0.1099 53  TYR   A CB  
193  C  CG  . TYR   A 33  ? 1.0576 1.3051 1.1732 0.0926  -0.0395 -0.0825 53  TYR   A CG  
194  C  CD1 . TYR   A 33  ? 1.0800 1.2962 1.1506 0.0919  -0.0351 -0.0635 53  TYR   A CD1 
195  C  CD2 . TYR   A 33  ? 1.0236 1.2613 1.1518 0.0816  -0.0237 -0.0777 53  TYR   A CD2 
196  C  CE1 . TYR   A 33  ? 1.0886 1.2696 1.1377 0.0785  -0.0162 -0.0414 53  TYR   A CE1 
197  C  CE2 . TYR   A 33  ? 1.0739 1.2734 1.1741 0.0698  -0.0086 -0.0571 53  TYR   A CE2 
198  C  CZ  . TYR   A 33  ? 1.1147 1.2883 1.1805 0.0671  -0.0054 -0.0396 53  TYR   A CZ  
199  O  OH  . TYR   A 33  ? 1.0648 1.2053 1.1148 0.0536  0.0089  -0.0221 53  TYR   A OH  
200  N  N   . HIS   A 34  ? 1.4137 1.7673 1.5793 0.1700  -0.1405 -0.1629 54  HIS   A N   
201  C  CA  . HIS   A 34  ? 1.4105 1.8172 1.6360 0.1732  -0.1652 -0.1994 54  HIS   A CA  
202  C  C   . HIS   A 34  ? 1.3823 1.7903 1.5938 0.1664  -0.1759 -0.2101 54  HIS   A C   
203  O  O   . HIS   A 34  ? 1.3587 1.8092 1.6292 0.1580  -0.1908 -0.2416 54  HIS   A O   
204  C  CB  . HIS   A 34  ? 1.4674 1.8929 1.6968 0.2141  -0.2010 -0.2166 54  HIS   A CB  
205  C  CG  . HIS   A 34  ? 1.5628 1.9488 1.7066 0.2515  -0.2244 -0.2046 54  HIS   A CG  
206  N  ND1 . HIS   A 34  ? 1.5612 1.8863 1.6256 0.2545  -0.2037 -0.1678 54  HIS   A ND1 
207  C  CD2 . HIS   A 34  ? 1.5693 1.9658 1.6927 0.2896  -0.2661 -0.2246 54  HIS   A CD2 
208  C  CE1 . HIS   A 34  ? 1.5974 1.8935 1.5923 0.2924  -0.2269 -0.1629 54  HIS   A CE1 
209  N  NE2 . HIS   A 34  ? 1.6049 1.9421 1.6290 0.3161  -0.2670 -0.1971 54  HIS   A NE2 
210  N  N   . LYS   A 35  ? 1.3492 1.7118 1.4881 0.1692  -0.1671 -0.1857 55  LYS   A N   
211  C  CA  . LYS   A 35  ? 1.3354 1.6935 1.4571 0.1602  -0.1700 -0.1927 55  LYS   A CA  
212  C  C   . LYS   A 35  ? 1.2932 1.6293 1.4094 0.1261  -0.1334 -0.1707 55  LYS   A C   
213  O  O   . LYS   A 35  ? 1.3340 1.6547 1.4216 0.1210  -0.1300 -0.1682 55  LYS   A O   
214  C  CB  . LYS   A 35  ? 1.4129 1.7380 1.4529 0.1962  -0.1907 -0.1861 55  LYS   A CB  
215  C  CG  . LYS   A 35  ? 1.5044 1.8576 1.5514 0.2288  -0.2368 -0.2202 55  LYS   A CG  
216  C  CD  . LYS   A 35  ? 1.5309 1.8708 1.5428 0.2685  -0.2558 -0.2128 55  LYS   A CD  
217  C  CE  . LYS   A 35  ? 1.5074 1.8805 1.5320 0.3040  -0.3072 -0.2504 55  LYS   A CE  
218  N  NZ  . LYS   A 35  ? 1.5826 1.9279 1.5449 0.3526  -0.3290 -0.2393 55  LYS   A NZ  
219  N  N   . GLY   A 36  ? 1.2681 1.6016 1.4091 0.1054  -0.1077 -0.1560 56  GLY   A N   
220  C  CA  . GLY   A 36  ? 1.2344 1.5529 1.3787 0.0744  -0.0777 -0.1400 56  GLY   A CA  
221  C  C   . GLY   A 36  ? 1.2817 1.5571 1.3728 0.0754  -0.0594 -0.1069 56  GLY   A C   
222  O  O   . GLY   A 36  ? 1.2955 1.5454 1.3373 0.0990  -0.0663 -0.0938 56  GLY   A O   
223  N  N   . PHE   A 37  ? 1.1466 1.4125 1.2496 0.0494  -0.0351 -0.0938 57  PHE   A N   
224  C  CA  . PHE   A 37  ? 1.0993 1.3298 1.1671 0.0450  -0.0175 -0.0662 57  PHE   A CA  
225  C  C   . PHE   A 37  ? 1.1328 1.3415 1.1551 0.0560  -0.0168 -0.0546 57  PHE   A C   
226  O  O   . PHE   A 37  ? 1.1377 1.3164 1.1216 0.0684  -0.0103 -0.0346 57  PHE   A O   
227  C  CB  . PHE   A 37  ? 1.1199 1.3486 1.2098 0.0171  0.0024  -0.0599 57  PHE   A CB  
228  C  CG  . PHE   A 37  ? 1.0988 1.3363 1.2183 0.0081  0.0085  -0.0648 57  PHE   A CG  
229  C  CD1 . PHE   A 37  ? 1.2408 1.5086 1.3995 0.0077  0.0032  -0.0859 57  PHE   A CD1 
230  C  CD2 . PHE   A 37  ? 1.0917 1.3071 1.2022 -0.0001 0.0205  -0.0499 57  PHE   A CD2 
231  C  CE1 . PHE   A 37  ? 1.2362 1.5100 1.4192 0.0009  0.0139  -0.0895 57  PHE   A CE1 
232  C  CE2 . PHE   A 37  ? 1.1594 1.3783 1.2887 -0.0056 0.0269  -0.0552 57  PHE   A CE2 
233  C  CZ  . PHE   A 37  ? 1.2354 1.4826 1.3986 -0.0044 0.0257  -0.0738 57  PHE   A CZ  
234  N  N   . CYS   A 38  ? 1.0804 1.3009 1.1060 0.0517  -0.0208 -0.0670 58  CYS   A N   
235  C  CA  . CYS   A 38  ? 1.1124 1.3112 1.0954 0.0598  -0.0144 -0.0559 58  CYS   A CA  
236  C  C   . CYS   A 38  ? 1.0983 1.2797 1.0293 0.0930  -0.0288 -0.0539 58  CYS   A C   
237  O  O   . CYS   A 38  ? 1.0650 1.2135 0.9504 0.1040  -0.0140 -0.0311 58  CYS   A O   
238  C  CB  . CYS   A 38  ? 1.0633 1.2769 1.0624 0.0485  -0.0164 -0.0726 58  CYS   A CB  
239  S  SG  . CYS   A 38  ? 1.0424 1.2644 1.0874 0.0142  0.0035  -0.0698 58  CYS   A SG  
240  N  N   . MET   A 39  ? 1.1390 1.3410 1.0763 0.1107  -0.0570 -0.0778 59  MET   A N   
241  C  CA  . MET   A 39  ? 1.1711 1.3539 1.0515 0.1478  -0.0754 -0.0774 59  MET   A CA  
242  C  C   . MET   A 39  ? 1.1574 1.3105 1.0087 0.1621  -0.0666 -0.0529 59  MET   A C   
243  O  O   . MET   A 39  ? 1.1867 1.3036 0.9733 0.1902  -0.0662 -0.0376 59  MET   A O   
244  C  CB  . MET   A 39  ? 1.2475 1.4642 1.1505 0.1646  -0.1128 -0.1123 59  MET   A CB  
245  C  CG  . MET   A 39  ? 1.3094 1.5374 1.2075 0.1674  -0.1290 -0.1367 59  MET   A CG  
246  S  SD  . MET   A 39  ? 1.6827 1.9210 1.5507 0.2115  -0.1783 -0.1676 59  MET   A SD  
247  C  CE  . MET   A 39  ? 1.4787 1.6567 1.2401 0.2511  -0.1697 -0.1323 59  MET   A CE  
248  N  N   . PHE   A 40  ? 1.1720 1.3350 1.0661 0.1444  -0.0581 -0.0488 60  PHE   A N   
249  C  CA  . PHE   A 40  ? 1.1560 1.2870 1.0260 0.1556  -0.0486 -0.0267 60  PHE   A CA  
250  C  C   . PHE   A 40  ? 1.1754 1.2650 1.0121 0.1468  -0.0173 0.0043  60  PHE   A C   
251  O  O   . PHE   A 40  ? 1.2492 1.2975 1.0356 0.1675  -0.0089 0.0252  60  PHE   A O   
252  C  CB  . PHE   A 40  ? 1.0818 1.2328 1.0058 0.1383  -0.0469 -0.0330 60  PHE   A CB  
253  C  CG  . PHE   A 40  ? 1.0654 1.1806 0.9711 0.1436  -0.0342 -0.0113 60  PHE   A CG  
254  C  CD1 . PHE   A 40  ? 1.0559 1.1464 0.9218 0.1772  -0.0464 -0.0052 60  PHE   A CD1 
255  C  CD2 . PHE   A 40  ? 1.0710 1.1751 0.9992 0.1163  -0.0120 0.0012  60  PHE   A CD2 
256  C  CE1 . PHE   A 40  ? 1.1157 1.1678 0.9654 0.1814  -0.0332 0.0146  60  PHE   A CE1 
257  C  CE2 . PHE   A 40  ? 1.1001 1.1692 1.0154 0.1195  -0.0015 0.0180  60  PHE   A CE2 
258  C  CZ  . PHE   A 40  ? 1.0386 1.0802 0.9153 0.1511  -0.0105 0.0253  60  PHE   A CZ  
259  N  N   . ASP   A 41  ? 1.1100 1.2092 0.9759 0.1169  0.0011  0.0078  61  ASP   A N   
260  C  CA  . ASP   A 41  ? 1.1088 1.1769 0.9574 0.1066  0.0307  0.0340  61  ASP   A CA  
261  C  C   . ASP   A 41  ? 1.1562 1.1993 0.9468 0.1282  0.0387  0.0443  61  ASP   A C   
262  O  O   . ASP   A 41  ? 1.1888 1.1929 0.9452 0.1351  0.0628  0.0699  61  ASP   A O   
263  C  CB  . ASP   A 41  ? 1.1310 1.2197 1.0273 0.0733  0.0437  0.0318  61  ASP   A CB  
264  C  CG  . ASP   A 41  ? 1.0704 1.1751 1.0124 0.0542  0.0394  0.0242  61  ASP   A CG  
265  O  OD1 . ASP   A 41  ? 1.0843 1.1779 1.0229 0.0636  0.0336  0.0261  61  ASP   A OD1 
266  O  OD2 . ASP   A 41  ? 1.0638 1.1886 1.0407 0.0322  0.0426  0.0168  61  ASP   A OD2 
267  N  N   . MET   A 42  ? 1.1991 1.2614 0.9776 0.1393  0.0206  0.0243  62  MET   A N   
268  C  CA  A MET   A 42  ? 1.2056 1.2420 0.9207 0.1638  0.0263  0.0310  62  MET   A CA  
269  C  CA  B MET   A 42  ? 1.1440 1.1796 0.8591 0.1634  0.0272  0.0318  62  MET   A CA  
270  C  C   . MET   A 42  ? 1.3396 1.3358 0.9872 0.2006  0.0219  0.0448  62  MET   A C   
271  O  O   . MET   A 42  ? 1.3846 1.3376 0.9758 0.2159  0.0471  0.0693  62  MET   A O   
272  C  CB  A MET   A 42  ? 1.2070 1.2714 0.9237 0.1700  0.0010  0.0009  62  MET   A CB  
273  C  CB  B MET   A 42  ? 1.2234 1.2859 0.9394 0.1687  0.0042  0.0030  62  MET   A CB  
274  C  CG  A MET   A 42  ? 1.2257 1.3168 0.9925 0.1387  0.0106  -0.0086 62  MET   A CG  
275  C  CG  B MET   A 42  ? 1.2239 1.3101 0.9876 0.1372  0.0172  -0.0034 62  MET   A CG  
276  S  SD  A MET   A 42  ? 1.2400 1.3061 0.9712 0.1395  0.0429  0.0093  62  MET   A SD  
277  S  SD  B MET   A 42  ? 1.2229 1.3223 0.9713 0.1461  0.0001  -0.0311 62  MET   A SD  
278  C  CE  A MET   A 42  ? 1.2465 1.2987 0.9065 0.1780  0.0196  -0.0101 62  MET   A CE  
279  C  CE  B MET   A 42  ? 1.3172 1.3686 0.9760 0.1777  0.0212  -0.0097 62  MET   A CE  
280  N  N   . GLU   A 43  ? 1.3998 1.4080 1.0518 0.2171  -0.0085 0.0296  63  GLU   A N   
281  C  CA  . GLU   A 43  ? 1.4409 1.4085 1.0263 0.2561  -0.0161 0.0424  63  GLU   A CA  
282  C  C   . GLU   A 43  ? 1.4555 1.3781 1.0279 0.2496  0.0186  0.0775  63  GLU   A C   
283  O  O   . GLU   A 43  ? 1.5422 1.4115 1.0447 0.2739  0.0381  0.1028  63  GLU   A O   
284  C  CB  . GLU   A 43  ? 1.4538 1.4498 1.0598 0.2740  -0.0568 0.0171  63  GLU   A CB  
285  C  CG  . GLU   A 43  ? 1.5403 1.5780 1.1592 0.2852  -0.0948 -0.0203 63  GLU   A CG  
286  C  CD  . GLU   A 43  ? 1.6851 1.6925 1.2200 0.3215  -0.1050 -0.0212 63  GLU   A CD  
287  O  OE1 . GLU   A 43  ? 1.7689 1.7217 1.2248 0.3522  -0.0928 0.0050  63  GLU   A OE1 
288  O  OE2 . GLU   A 43  ? 1.6708 1.7051 1.2156 0.3201  -0.1241 -0.0482 63  GLU   A OE2 
289  N  N   . CYS   A 44  ? 1.2862 1.2264 0.9242 0.2170  0.0279  0.0788  64  CYS   A N   
290  C  CA  . CYS   A 44  ? 1.2562 1.1553 0.8921 0.2079  0.0573  0.1071  64  CYS   A CA  
291  C  C   . CYS   A 44  ? 1.2842 1.1498 0.8979 0.1982  0.0980  0.1339  64  CYS   A C   
292  O  O   . CYS   A 44  ? 1.3038 1.1171 0.8818 0.2074  0.1248  0.1617  64  CYS   A O   
293  C  CB  . CYS   A 44  ? 1.1948 1.1220 0.9058 0.1737  0.0568  0.0984  64  CYS   A CB  
294  S  SG  . CYS   A 44  ? 0.9849 0.9209 0.7109 0.1895  0.0279  0.0836  64  CYS   A SG  
295  N  N   . HIS   A 45  ? 1.2708 1.1646 0.9084 0.1798  0.1057  0.1262  65  HIS   A N   
296  C  CA  . HIS   A 45  ? 1.2975 1.1653 0.9208 0.1719  0.1460  0.1497  65  HIS   A CA  
297  C  C   . HIS   A 45  ? 1.4058 1.2245 0.9364 0.2112  0.1587  0.1671  65  HIS   A C   
298  O  O   . HIS   A 45  ? 1.4153 1.1870 0.9167 0.2143  0.1983  0.1973  65  HIS   A O   
299  C  CB  . HIS   A 45  ? 1.2457 1.1555 0.9121 0.1486  0.1481  0.1353  65  HIS   A CB  
300  C  CG  . HIS   A 45  ? 1.2907 1.1845 0.9632 0.1358  0.1901  0.1567  65  HIS   A CG  
301  N  ND1 . HIS   A 45  ? 1.3051 1.1566 0.9688 0.1334  0.2265  0.1858  65  HIS   A ND1 
302  C  CD2 . HIS   A 45  ? 1.2163 1.1316 0.9082 0.1245  0.2031  0.1524  65  HIS   A CD2 
303  C  CE1 . HIS   A 45  ? 1.3072 1.1588 0.9895 0.1204  0.2610  0.1981  65  HIS   A CE1 
304  N  NE2 . HIS   A 45  ? 1.2567 1.1471 0.9547 0.1162  0.2467  0.1782  65  HIS   A NE2 
305  N  N   . LYS   A 46  ? 1.3855 1.2120 0.8683 0.2424  0.1259  0.1478  66  LYS   A N   
306  C  CA  . LYS   A 46  ? 1.4637 1.2405 0.8464 0.2855  0.1330  0.1617  66  LYS   A CA  
307  C  C   . LYS   A 46  ? 1.5748 1.2935 0.9033 0.3113  0.1430  0.1874  66  LYS   A C   
308  O  O   . LYS   A 46  ? 1.6793 1.3384 0.9390 0.3314  0.1789  0.2178  66  LYS   A O   
309  C  CB  . LYS   A 46  ? 1.4980 1.2998 0.8476 0.3137  0.0871  0.1290  66  LYS   A CB  
310  C  CG  . LYS   A 46  ? 1.7097 1.4604 0.9482 0.3687  0.0757  0.1360  66  LYS   A CG  
311  C  CD  . LYS   A 46  ? 1.7651 1.4598 0.9271 0.3851  0.1217  0.1661  66  LYS   A CD  
312  C  CE  . LYS   A 46  ? 1.8851 1.5069 0.9396 0.4336  0.1291  0.1917  66  LYS   A CE  
313  N  NZ  . LYS   A 46  ? 1.9823 1.5413 0.9812 0.4385  0.1920  0.2329  66  LYS   A NZ  
314  N  N   . LYS   A 47  ? 1.5139 1.2454 0.8715 0.3117  0.1151  0.1769  67  LYS   A N   
315  C  CA  . LYS   A 47  ? 1.5293 1.2039 0.8292 0.3427  0.1179  0.1980  67  LYS   A CA  
316  C  C   . LYS   A 47  ? 1.5350 1.1718 0.8636 0.3167  0.1605  0.2283  67  LYS   A C   
317  O  O   . LYS   A 47  ? 1.6532 1.2218 0.9180 0.3410  0.1839  0.2577  67  LYS   A O   
318  C  CB  . LYS   A 47  ? 1.5370 1.2417 0.8525 0.3609  0.0666  0.1710  67  LYS   A CB  
319  C  CG  . LYS   A 47  ? 1.5950 1.2448 0.8543 0.3972  0.0618  0.1887  67  LYS   A CG  
320  C  CD  . LYS   A 47  ? 1.7776 1.3500 0.9198 0.4415  0.0829  0.2188  67  LYS   A CD  
321  C  CE  . LYS   A 47  ? 1.8365 1.4191 0.9139 0.4786  0.0523  0.1993  67  LYS   A CE  
322  N  NZ  . LYS   A 47  ? 1.8713 1.3805 0.8434 0.5073  0.0908  0.2323  67  LYS   A NZ  
323  N  N   . TYR   A 48  ? 1.5254 1.2004 0.9459 0.2692  0.1716  0.2217  68  TYR   A N   
324  C  CA  . TYR   A 48  ? 1.4998 1.1439 0.9577 0.2435  0.2035  0.2432  68  TYR   A CA  
325  C  C   . TYR   A 48  ? 1.5109 1.1452 1.0010 0.2125  0.2516  0.2628  68  TYR   A C   
326  O  O   . TYR   A 48  ? 1.4887 1.0768 0.9858 0.2010  0.2875  0.2880  68  TYR   A O   
327  C  CB  . TYR   A 48  ? 1.4424 1.1306 0.9808 0.2158  0.1773  0.2200  68  TYR   A CB  
328  C  CG  . TYR   A 48  ? 1.4625 1.1568 0.9781 0.2461  0.1364  0.2033  68  TYR   A CG  
329  C  CD1 . TYR   A 48  ? 1.4862 1.1206 0.9371 0.2816  0.1384  0.2221  68  TYR   A CD1 
330  C  CD2 . TYR   A 48  ? 1.3410 1.0994 0.9008 0.2407  0.0974  0.1692  68  TYR   A CD2 
331  C  CE1 . TYR   A 48  ? 1.4569 1.1001 0.8911 0.3124  0.0993  0.2056  68  TYR   A CE1 
332  C  CE2 . TYR   A 48  ? 1.3479 1.1172 0.8969 0.2684  0.0615  0.1524  68  TYR   A CE2 
333  C  CZ  . TYR   A 48  ? 1.4283 1.1422 0.9158 0.3050  0.0608  0.1697  68  TYR   A CZ  
334  O  OH  . TYR   A 48  ? 1.3107 1.0389 0.7920 0.3353  0.0233  0.1515  68  TYR   A OH  
335  N  N   . GLY   A 49  ? 1.4717 1.1475 0.9858 0.1986  0.2542  0.2513  69  GLY   A N   
336  C  CA  . GLY   A 49  ? 1.4561 1.1232 0.9968 0.1756  0.3011  0.2701  69  GLY   A CA  
337  C  C   . GLY   A 49  ? 1.4124 1.1354 1.0549 0.1304  0.3006  0.2541  69  GLY   A C   
338  O  O   . GLY   A 49  ? 1.3209 1.0982 0.9979 0.1210  0.2661  0.2261  69  GLY   A O   
339  N  N   . LYS   A 50  ? 1.4436 1.1516 1.1354 0.1031  0.3398  0.2718  70  LYS   A N   
340  C  CA  . LYS   A 50  ? 1.3655 1.1231 1.1517 0.0637  0.3423  0.2585  70  LYS   A CA  
341  C  C   . LYS   A 50  ? 1.2691 1.0549 1.1173 0.0399  0.3095  0.2375  70  LYS   A C   
342  O  O   . LYS   A 50  ? 1.1829 1.0184 1.0934 0.0161  0.2936  0.2178  70  LYS   A O   
343  C  CB  . LYS   A 50  ? 1.3645 1.0979 1.1879 0.0441  0.3956  0.2827  70  LYS   A CB  
344  C  CG  . LYS   A 50  ? 1.4355 1.0946 1.2115 0.0577  0.4308  0.3139  70  LYS   A CG  
345  C  CD  . LYS   A 50  ? 1.6119 1.2415 1.3993 0.0493  0.4930  0.3420  70  LYS   A CD  
346  C  CE  . LYS   A 50  ? 1.6522 1.2869 1.5435 0.0065  0.5161  0.3441  70  LYS   A CE  
347  N  NZ  . LYS   A 50  ? 1.6417 1.2461 1.5522 -0.0029 0.5822  0.3725  70  LYS   A NZ  
348  N  N   . VAL   A 51  ? 1.3950 1.1469 1.2225 0.0485  0.2997  0.2415  71  VAL   A N   
349  C  CA  . VAL   A 51  ? 1.3366 1.1059 1.2150 0.0290  0.2726  0.2229  71  VAL   A CA  
350  C  C   . VAL   A 51  ? 1.3633 1.1065 1.1883 0.0570  0.2490  0.2209  71  VAL   A C   
351  O  O   . VAL   A 51  ? 1.4394 1.1282 1.2051 0.0816  0.2663  0.2429  71  VAL   A O   
352  C  CB  . VAL   A 51  ? 1.2948 1.0428 1.2350 -0.0019 0.2979  0.2320  71  VAL   A CB  
353  C  CG1 . VAL   A 51  ? 1.2657 1.0151 1.2368 -0.0135 0.2698  0.2144  71  VAL   A CG1 
354  C  CG2 . VAL   A 51  ? 1.2756 1.0632 1.2869 -0.0312 0.3120  0.2264  71  VAL   A CG2 
355  N  N   . TRP   A 52  ? 1.2889 1.0690 1.1338 0.0552  0.2111  0.1951  72  TRP   A N   
356  C  CA  . TRP   A 52  ? 1.3039 1.0667 1.1118 0.0807  0.1876  0.1898  72  TRP   A CA  
357  C  C   . TRP   A 52  ? 1.1842 0.9813 1.0415 0.0641  0.1598  0.1642  72  TRP   A C   
358  O  O   . TRP   A 52  ? 1.1115 0.9454 1.0215 0.0366  0.1555  0.1503  72  TRP   A O   
359  C  CB  . TRP   A 52  ? 1.3023 1.0751 1.0504 0.1164  0.1681  0.1848  72  TRP   A CB  
360  C  CG  . TRP   A 52  ? 1.2321 1.0679 1.0077 0.1095  0.1412  0.1576  72  TRP   A CG  
361  C  CD1 . TRP   A 52  ? 1.1767 1.0493 0.9728 0.1124  0.1088  0.1326  72  TRP   A CD1 
362  C  CD2 . TRP   A 52  ? 1.2372 1.1034 1.0242 0.0986  0.1477  0.1532  72  TRP   A CD2 
363  N  NE1 . TRP   A 52  ? 1.1450 1.0663 0.9648 0.1023  0.0959  0.1138  72  TRP   A NE1 
364  C  CE2 . TRP   A 52  ? 1.1830 1.1003 0.9958 0.0945  0.1177  0.1256  72  TRP   A CE2 
365  C  CE3 . TRP   A 52  ? 1.2292 1.0832 1.0087 0.0924  0.1783  0.1700  72  TRP   A CE3 
366  C  CZ2 . TRP   A 52  ? 1.1938 1.1459 1.0218 0.0847  0.1156  0.1146  72  TRP   A CZ2 
367  C  CZ3 . TRP   A 52  ? 1.2178 1.1101 1.0128 0.0843  0.1750  0.1579  72  TRP   A CZ3 
368  C  CH2 . TRP   A 52  ? 1.2056 1.1444 1.0230 0.0806  0.1430  0.1306  72  TRP   A CH2 
369  N  N   . GLY   A 53  ? 1.1952 0.9780 1.0313 0.0841  0.1414  0.1582  73  GLY   A N   
370  C  CA  . GLY   A 53  ? 1.1653 0.9728 1.0404 0.0727  0.1195  0.1356  73  GLY   A CA  
371  C  C   . GLY   A 53  ? 1.1262 0.9497 0.9783 0.1016  0.0922  0.1209  73  GLY   A C   
372  O  O   . GLY   A 53  ? 1.2194 1.0185 1.0220 0.1340  0.0884  0.1306  73  GLY   A O   
373  N  N   . PHE   A 54  ? 1.1120 0.9768 1.0013 0.0910  0.0735  0.0969  74  PHE   A N   
374  C  CA  . PHE   A 54  ? 1.0991 0.9885 0.9849 0.1138  0.0495  0.0789  74  PHE   A CA  
375  C  C   . PHE   A 54  ? 1.0269 0.9333 0.9523 0.0979  0.0429  0.0605  74  PHE   A C   
376  O  O   . PHE   A 54  ? 0.9888 0.8840 0.9371 0.0723  0.0529  0.0613  74  PHE   A O   
377  C  CB  . PHE   A 54  ? 1.0587 0.9950 0.9435 0.1227  0.0345  0.0658  74  PHE   A CB  
378  C  CG  . PHE   A 54  ? 1.0579 1.0319 0.9785 0.0933  0.0384  0.0563  74  PHE   A CG  
379  C  CD1 . PHE   A 54  ? 0.9919 0.9590 0.9062 0.0800  0.0545  0.0697  74  PHE   A CD1 
380  C  CD2 . PHE   A 54  ? 0.9865 1.0003 0.9454 0.0809  0.0281  0.0348  74  PHE   A CD2 
381  C  CE1 . PHE   A 54  ? 0.9762 0.9757 0.9218 0.0563  0.0568  0.0611  74  PHE   A CE1 
382  C  CE2 . PHE   A 54  ? 1.0270 1.0684 1.0120 0.0568  0.0323  0.0280  74  PHE   A CE2 
383  C  CZ  . PHE   A 54  ? 0.9496 0.9842 0.9281 0.0452  0.0448  0.0407  74  PHE   A CZ  
384  N  N   . TYR   A 55  ? 1.0534 0.9873 0.9874 0.1146  0.0257  0.0423  75  TYR   A N   
385  C  CA  . TYR   A 55  ? 1.0370 0.9818 0.9996 0.1060  0.0224  0.0255  75  TYR   A CA  
386  C  C   . TYR   A 55  ? 0.9627 0.9643 0.9548 0.1051  0.0121  0.0037  75  TYR   A C   
387  O  O   . TYR   A 55  ? 0.9383 0.9656 0.9308 0.1268  -0.0011 -0.0046 75  TYR   A O   
388  C  CB  . TYR   A 55  ? 1.0596 0.9703 1.0064 0.1298  0.0185  0.0262  75  TYR   A CB  
389  C  CG  . TYR   A 55  ? 1.1230 0.9703 1.0391 0.1330  0.0312  0.0491  75  TYR   A CG  
390  C  CD1 . TYR   A 55  ? 1.1405 0.9610 1.0158 0.1569  0.0327  0.0676  75  TYR   A CD1 
391  C  CD2 . TYR   A 55  ? 1.1338 0.9447 1.0605 0.1129  0.0421  0.0515  75  TYR   A CD2 
392  C  CE1 . TYR   A 55  ? 1.1903 0.9470 1.0360 0.1596  0.0501  0.0912  75  TYR   A CE1 
393  C  CE2 . TYR   A 55  ? 1.1415 0.8925 1.0477 0.1128  0.0569  0.0719  75  TYR   A CE2 
394  C  CZ  . TYR   A 55  ? 1.2298 0.9526 1.0955 0.1356  0.0635  0.0934  75  TYR   A CZ  
395  O  OH  . TYR   A 55  ? 1.3406 0.9978 1.1840 0.1353  0.0840  0.1164  75  TYR   A OH  
396  N  N   . ASP   A 56  ? 1.0066 1.0259 1.0236 0.0809  0.0181  -0.0059 76  ASP   A N   
397  C  CA  . ASP   A 56  ? 0.9523 1.0159 0.9986 0.0782  0.0154  -0.0257 76  ASP   A CA  
398  C  C   . ASP   A 56  ? 0.9804 1.0342 1.0328 0.0867  0.0174  -0.0363 76  ASP   A C   
399  O  O   . ASP   A 56  ? 1.0203 1.0601 1.0731 0.0720  0.0251  -0.0399 76  ASP   A O   
400  C  CB  . ASP   A 56  ? 0.8766 0.9572 0.9367 0.0513  0.0233  -0.0280 76  ASP   A CB  
401  C  CG  . ASP   A 56  ? 0.9277 1.0210 0.9840 0.0448  0.0222  -0.0200 76  ASP   A CG  
402  O  OD1 . ASP   A 56  ? 1.0110 1.1114 1.0573 0.0626  0.0134  -0.0184 76  ASP   A OD1 
403  O  OD2 . ASP   A 56  ? 0.9324 1.0276 0.9933 0.0244  0.0288  -0.0165 76  ASP   A OD2 
404  N  N   . GLY   A 57  ? 0.9625 1.0226 1.0174 0.1135  0.0089  -0.0427 77  GLY   A N   
405  C  CA  . GLY   A 57  ? 1.0378 1.0815 1.0938 0.1266  0.0114  -0.0510 77  GLY   A CA  
406  C  C   . GLY   A 57  ? 1.1042 1.0883 1.1277 0.1305  0.0126  -0.0365 77  GLY   A C   
407  O  O   . GLY   A 57  ? 1.1241 1.0840 1.1248 0.1457  0.0071  -0.0222 77  GLY   A O   
408  N  N   . GLN   A 58  ? 1.0991 1.0552 1.1180 0.1177  0.0201  -0.0403 78  GLN   A N   
409  C  CA  . GLN   A 58  ? 1.0883 0.9863 1.0847 0.1140  0.0222  -0.0291 78  GLN   A CA  
410  C  C   . GLN   A 58  ? 1.0795 0.9651 1.0769 0.0838  0.0269  -0.0196 78  GLN   A C   
411  O  O   . GLN   A 58  ? 1.1317 0.9732 1.1223 0.0737  0.0296  -0.0144 78  GLN   A O   
412  C  CB  . GLN   A 58  ? 1.1537 1.0244 1.1452 0.1206  0.0240  -0.0429 78  GLN   A CB  
413  C  CG  . GLN   A 58  ? 1.2020 1.0937 1.2017 0.1496  0.0223  -0.0564 78  GLN   A CG  
414  C  CD  . GLN   A 58  ? 1.2523 1.1179 1.2369 0.1799  0.0152  -0.0475 78  GLN   A CD  
415  O  OE1 . GLN   A 58  ? 1.3479 1.1835 1.3124 0.1805  0.0133  -0.0285 78  GLN   A OE1 
416  N  NE2 . GLN   A 58  ? 1.2812 1.1559 1.2736 0.2072  0.0129  -0.0607 78  GLN   A NE2 
417  N  N   . GLN   A 59  ? 1.0083 0.9323 1.0186 0.0695  0.0276  -0.0188 79  GLN   A N   
418  C  CA  . GLN   A 59  ? 1.0035 0.9235 1.0209 0.0425  0.0310  -0.0129 79  GLN   A CA  
419  C  C   . GLN   A 59  ? 1.0018 0.9103 1.0131 0.0398  0.0364  0.0075  79  GLN   A C   
420  O  O   . GLN   A 59  ? 0.9477 0.8822 0.9546 0.0492  0.0353  0.0125  79  GLN   A O   
421  C  CB  . GLN   A 59  ? 0.9550 0.9174 0.9864 0.0300  0.0310  -0.0224 79  GLN   A CB  
422  C  CG  . GLN   A 59  ? 0.9630 0.9272 1.0033 0.0062  0.0322  -0.0164 79  GLN   A CG  
423  C  CD  . GLN   A 59  ? 1.0709 1.0048 1.1129 -0.0072 0.0281  -0.0228 79  GLN   A CD  
424  O  OE1 . GLN   A 59  ? 1.0563 0.9674 1.1080 -0.0191 0.0290  -0.0145 79  GLN   A OE1 
425  N  NE2 . GLN   A 59  ? 1.0725 1.0055 1.1059 -0.0048 0.0240  -0.0390 79  GLN   A NE2 
426  N  N   . PRO   A 60  ? 1.0294 0.8988 1.0413 0.0274  0.0433  0.0186  80  PRO   A N   
427  C  CA  . PRO   A 60  ? 1.0353 0.8922 1.0414 0.0239  0.0551  0.0398  80  PRO   A CA  
428  C  C   . PRO   A 60  ? 1.0529 0.9440 1.0790 0.0037  0.0577  0.0403  80  PRO   A C   
429  O  O   . PRO   A 60  ? 1.0514 0.9526 1.1011 -0.0161 0.0534  0.0296  80  PRO   A O   
430  C  CB  . PRO   A 60  ? 1.0653 0.8688 1.0761 0.0136  0.0652  0.0489  80  PRO   A CB  
431  C  CG  . PRO   A 60  ? 1.0522 0.8379 1.0646 0.0169  0.0545  0.0309  80  PRO   A CG  
432  C  CD  . PRO   A 60  ? 1.0279 0.8596 1.0467 0.0169  0.0422  0.0113  80  PRO   A CD  
433  N  N   . VAL   A 61  ? 1.0250 0.9320 1.0384 0.0115  0.0631  0.0516  81  VAL   A N   
434  C  CA  . VAL   A 61  ? 0.9926 0.9282 1.0216 -0.0042 0.0679  0.0540  81  VAL   A CA  
435  C  C   . VAL   A 61  ? 1.0322 0.9454 1.0472 -0.0018 0.0864  0.0764  81  VAL   A C   
436  O  O   . VAL   A 61  ? 1.0658 0.9621 1.0445 0.0214  0.0894  0.0873  81  VAL   A O   
437  C  CB  . VAL   A 61  ? 0.9808 0.9606 1.0069 0.0032  0.0576  0.0424  81  VAL   A CB  
438  C  CG1 . VAL   A 61  ? 0.9517 0.9545 0.9898 -0.0105 0.0635  0.0459  81  VAL   A CG1 
439  C  CG2 . VAL   A 61  ? 0.9574 0.9560 0.9970 0.0002  0.0464  0.0226  81  VAL   A CG2 
440  N  N   . LEU   A 62  ? 1.0258 0.9381 1.0685 -0.0236 0.0992  0.0829  82  LEU   A N   
441  C  CA  . LEU   A 62  ? 1.0833 0.9728 1.1185 -0.0241 0.1240  0.1053  82  LEU   A CA  
442  C  C   . LEU   A 62  ? 1.0301 0.9548 1.0720 -0.0289 0.1288  0.1061  82  LEU   A C   
443  O  O   . LEU   A 62  ? 0.9949 0.9464 1.0761 -0.0487 0.1250  0.0965  82  LEU   A O   
444  C  CB  . LEU   A 62  ? 1.0392 0.8990 1.1111 -0.0461 0.1397  0.1121  82  LEU   A CB  
445  C  CG  . LEU   A 62  ? 1.0521 0.8872 1.1246 -0.0499 0.1729  0.1367  82  LEU   A CG  
446  C  CD1 . LEU   A 62  ? 1.0555 0.8367 1.0766 -0.0272 0.1894  0.1580  82  LEU   A CD1 
447  C  CD2 . LEU   A 62  ? 1.0956 0.9267 1.2322 -0.0807 0.1855  0.1354  82  LEU   A CD2 
448  N  N   . ALA   A 63  ? 1.0361 0.9581 1.0369 -0.0083 0.1355  0.1166  83  ALA   A N   
449  C  CA  . ALA   A 63  ? 1.0794 1.0286 1.0797 -0.0095 0.1415  0.1174  83  ALA   A CA  
450  C  C   . ALA   A 63  ? 1.1080 1.0364 1.1169 -0.0177 0.1739  0.1382  83  ALA   A C   
451  O  O   . ALA   A 63  ? 1.1233 1.0089 1.1028 -0.0066 0.1947  0.1582  83  ALA   A O   
452  C  CB  . ALA   A 63  ? 1.0162 0.9726 0.9674 0.0179  0.1307  0.1145  83  ALA   A CB  
453  N  N   . ILE   A 64  ? 1.0142 0.9714 1.0642 -0.0361 0.1802  0.1341  84  ILE   A N   
454  C  CA  . ILE   A 64  ? 1.0826 1.0295 1.1544 -0.0460 0.2132  0.1513  84  ILE   A CA  
455  C  C   . ILE   A 64  ? 1.0949 1.0697 1.1583 -0.0398 0.2188  0.1501  84  ILE   A C   
456  O  O   . ILE   A 64  ? 1.1088 1.1198 1.1866 -0.0438 0.1964  0.1318  84  ILE   A O   
457  C  CB  . ILE   A 64  ? 1.1099 1.0657 1.2551 -0.0757 0.2162  0.1456  84  ILE   A CB  
458  C  CG1 . ILE   A 64  ? 1.0034 1.0040 1.1845 -0.0876 0.1870  0.1218  84  ILE   A CG1 
459  C  CG2 . ILE   A 64  ? 1.0812 1.0017 1.2320 -0.0813 0.2132  0.1467  84  ILE   A CG2 
460  C  CD1 . ILE   A 64  ? 0.9989 1.0159 1.2526 -0.1127 0.1873  0.1140  84  ILE   A CD1 
461  N  N   . THR   A 65  ? 1.1346 1.0879 1.1709 -0.0287 0.2506  0.1699  85  THR   A N   
462  C  CA  . THR   A 65  ? 1.1102 1.0838 1.1330 -0.0200 0.2596  0.1693  85  THR   A CA  
463  C  C   . THR   A 65  ? 1.1308 1.1061 1.1944 -0.0326 0.2976  0.1835  85  THR   A C   
464  O  O   . THR   A 65  ? 1.1487 1.1422 1.2079 -0.0262 0.3078  0.1825  85  THR   A O   
465  C  CB  . THR   A 65  ? 1.1375 1.0859 1.0763 0.0131  0.2609  0.1763  85  THR   A CB  
466  O  OG1 . THR   A 65  ? 1.1869 1.0839 1.0866 0.0259  0.2906  0.2018  85  THR   A OG1 
467  C  CG2 . THR   A 65  ? 1.0800 1.0388 0.9918 0.0254  0.2209  0.1573  85  THR   A CG2 
468  N  N   . ASP   A 66  ? 1.1521 1.1095 1.2593 -0.0505 0.3198  0.1954  86  ASP   A N   
469  C  CA  . ASP   A 66  ? 1.1132 1.0764 1.2733 -0.0650 0.3586  0.2075  86  ASP   A CA  
470  C  C   . ASP   A 66  ? 1.1380 1.1563 1.3750 -0.0851 0.3402  0.1866  86  ASP   A C   
471  O  O   . ASP   A 66  ? 1.1250 1.1601 1.4097 -0.1033 0.3126  0.1703  86  ASP   A O   
472  C  CB  . ASP   A 66  ? 1.1377 1.0646 1.3301 -0.0809 0.3873  0.2241  86  ASP   A CB  
473  C  CG  . ASP   A 66  ? 1.1708 1.1074 1.4333 -0.0995 0.4305  0.2353  86  ASP   A CG  
474  O  OD1 . ASP   A 66  ? 1.1738 1.1543 1.5230 -0.1233 0.4175  0.2176  86  ASP   A OD1 
475  O  OD2 . ASP   A 66  ? 1.2270 1.1269 1.4578 -0.0889 0.4779  0.2615  86  ASP   A OD2 
476  N  N   . PRO   A 67  ? 1.1720 1.2164 1.4192 -0.0798 0.3536  0.1860  87  PRO   A N   
477  C  CA  . PRO   A 67  ? 1.0983 1.1934 1.4102 -0.0932 0.3314  0.1654  87  PRO   A CA  
478  C  C   . PRO   A 67  ? 1.0822 1.1981 1.4915 -0.1206 0.3352  0.1597  87  PRO   A C   
479  O  O   . PRO   A 67  ? 1.0550 1.2072 1.5118 -0.1306 0.3031  0.1388  87  PRO   A O   
480  C  CB  . PRO   A 67  ? 1.0721 1.1810 1.3686 -0.0779 0.3540  0.1703  87  PRO   A CB  
481  C  CG  . PRO   A 67  ? 1.1308 1.1976 1.3804 -0.0644 0.3997  0.1964  87  PRO   A CG  
482  C  CD  . PRO   A 67  ? 1.1563 1.1814 1.3486 -0.0574 0.3883  0.2033  87  PRO   A CD  
483  N  N   . ASP   A 68  ? 1.0788 1.1713 1.5198 -0.1324 0.3724  0.1766  88  ASP   A N   
484  C  CA  . ASP   A 68  ? 1.0869 1.1978 1.6269 -0.1610 0.3709  0.1668  88  ASP   A CA  
485  C  C   . ASP   A 68  ? 1.0417 1.1437 1.5819 -0.1707 0.3286  0.1497  88  ASP   A C   
486  O  O   . ASP   A 68  ? 1.0434 1.1777 1.6445 -0.1852 0.2964  0.1267  88  ASP   A O   
487  C  CB  . ASP   A 68  ? 1.0846 1.1661 1.6588 -0.1731 0.4252  0.1897  88  ASP   A CB  
488  C  CG  . ASP   A 68  ? 1.1371 1.2546 1.7905 -0.1824 0.4598  0.1924  88  ASP   A CG  
489  O  OD1 . ASP   A 68  ? 1.1277 1.2980 1.8326 -0.1853 0.4332  0.1713  88  ASP   A OD1 
490  O  OD2 . ASP   A 68  ? 1.2748 1.3664 1.9391 -0.1857 0.5153  0.2162  88  ASP   A OD2 
491  N  N   . MET   A 69  ? 1.1106 1.1676 1.5798 -0.1599 0.3273  0.1601  89  MET   A N   
492  C  CA  . MET   A 69  ? 1.1360 1.1799 1.5971 -0.1655 0.2910  0.1450  89  MET   A CA  
493  C  C   . MET   A 69  ? 1.0627 1.1362 1.4997 -0.1565 0.2451  0.1229  89  MET   A C   
494  O  O   . MET   A 69  ? 0.9950 1.0702 1.4460 -0.1646 0.2129  0.1048  89  MET   A O   
495  C  CB  . MET   A 69  ? 1.1813 1.1702 1.5701 -0.1514 0.3035  0.1629  89  MET   A CB  
496  C  CG  . MET   A 69  ? 1.2118 1.1761 1.6110 -0.1621 0.2820  0.1524  89  MET   A CG  
497  S  SD  . MET   A 69  ? 1.3507 1.2474 1.6684 -0.1425 0.2982  0.1746  89  MET   A SD  
498  C  CE  . MET   A 69  ? 1.2653 1.1548 1.5074 -0.1130 0.3253  0.1978  89  MET   A CE  
499  N  N   . ILE   A 70  ? 1.0835 1.1756 1.4818 -0.1395 0.2434  0.1241  90  ILE   A N   
500  C  CA  . ILE   A 70  ? 1.0519 1.1700 1.4330 -0.1329 0.2056  0.1046  90  ILE   A CA  
501  C  C   . ILE   A 70  ? 1.0718 1.2277 1.5230 -0.1465 0.1869  0.0869  90  ILE   A C   
502  O  O   . ILE   A 70  ? 1.0723 1.2396 1.5210 -0.1465 0.1520  0.0688  90  ILE   A O   
503  C  CB  . ILE   A 70  ? 1.0073 1.1306 1.3311 -0.1121 0.2106  0.1098  90  ILE   A CB  
504  C  CG1 . ILE   A 70  ? 0.9890 1.0763 1.2413 -0.0951 0.2197  0.1227  90  ILE   A CG1 
505  C  CG2 . ILE   A 70  ? 0.9206 1.0687 1.2335 -0.1075 0.1772  0.0910  90  ILE   A CG2 
506  C  CD1 . ILE   A 70  ? 0.9867 1.0763 1.1828 -0.0739 0.2227  0.1249  90  ILE   A CD1 
507  N  N   . LYS   A 71  ? 0.9890 1.1643 1.5031 -0.1563 0.2100  0.0915  91  LYS   A N   
508  C  CA  . LYS   A 71  ? 0.9578 1.1722 1.5459 -0.1671 0.1888  0.0724  91  LYS   A CA  
509  C  C   . LYS   A 71  ? 0.9569 1.1657 1.5904 -0.1849 0.1655  0.0565  91  LYS   A C   
510  O  O   . LYS   A 71  ? 0.9421 1.1735 1.6049 -0.1872 0.1287  0.0343  91  LYS   A O   
511  C  CB  . LYS   A 71  ? 0.9370 1.1781 1.5897 -0.1723 0.2212  0.0800  91  LYS   A CB  
512  C  CG  . LYS   A 71  ? 0.9010 1.1883 1.6402 -0.1812 0.1974  0.0584  91  LYS   A CG  
513  C  CD  . LYS   A 71  ? 0.8175 1.1378 1.6123 -0.1795 0.2287  0.0650  91  LYS   A CD  
514  C  CE  . LYS   A 71  ? 0.9386 1.2541 1.7977 -0.1978 0.2745  0.0787  91  LYS   A CE  
515  N  NZ  . LYS   A 71  ? 0.9397 1.3035 1.9197 -0.2139 0.2693  0.0609  91  LYS   A NZ  
516  N  N   . THR   A 72  ? 0.9520 1.1266 1.5879 -0.1957 0.1855  0.0669  92  THR   A N   
517  C  CA  . THR   A 72  ? 0.9523 1.1156 1.6283 -0.2126 0.1633  0.0500  92  THR   A CA  
518  C  C   . THR   A 72  ? 1.0019 1.1534 1.6204 -0.2019 0.1219  0.0341  92  THR   A C   
519  O  O   . THR   A 72  ? 1.0065 1.1658 1.6552 -0.2089 0.0876  0.0104  92  THR   A O   
520  C  CB  . THR   A 72  ? 1.0157 1.1360 1.6970 -0.2244 0.1969  0.0671  92  THR   A CB  
521  O  OG1 . THR   A 72  ? 1.0135 1.1360 1.7231 -0.2282 0.2453  0.0891  92  THR   A OG1 
522  C  CG2 . THR   A 72  ? 1.0369 1.1516 1.7883 -0.2475 0.1796  0.0471  92  THR   A CG2 
523  N  N   . VAL   A 73  ? 1.0291 1.1625 1.5656 -0.1837 0.1247  0.0453  93  VAL   A N   
524  C  CA  . VAL   A 73  ? 0.9864 1.1082 1.4692 -0.1732 0.0928  0.0323  93  VAL   A CA  
525  C  C   . VAL   A 73  ? 0.9686 1.1207 1.4443 -0.1640 0.0656  0.0178  93  VAL   A C   
526  O  O   . VAL   A 73  ? 0.9614 1.1162 1.4419 -0.1643 0.0333  -0.0021 93  VAL   A O   
527  C  CB  . VAL   A 73  ? 1.0057 1.1003 1.4140 -0.1575 0.1064  0.0479  93  VAL   A CB  
528  C  CG1 . VAL   A 73  ? 0.9392 1.0245 1.3008 -0.1476 0.0782  0.0342  93  VAL   A CG1 
529  C  CG2 . VAL   A 73  ? 1.0197 1.0779 1.4275 -0.1624 0.1335  0.0643  93  VAL   A CG2 
530  N  N   . LEU   A 74  ? 0.9664 1.1371 1.4256 -0.1538 0.0785  0.0278  94  LEU   A N   
531  C  CA  . LEU   A 74  ? 0.9400 1.1301 1.3794 -0.1423 0.0563  0.0174  94  LEU   A CA  
532  C  C   . LEU   A 74  ? 0.9057 1.1250 1.4059 -0.1470 0.0364  0.0021  94  LEU   A C   
533  O  O   . LEU   A 74  ? 0.9317 1.1579 1.4144 -0.1370 0.0087  -0.0107 94  LEU   A O   
534  C  CB  . LEU   A 74  ? 0.8544 1.0520 1.2597 -0.1300 0.0756  0.0306  94  LEU   A CB  
535  C  CG  . LEU   A 74  ? 0.9164 1.0924 1.2572 -0.1198 0.0870  0.0407  94  LEU   A CG  
536  C  CD1 . LEU   A 74  ? 0.8448 1.0326 1.1587 -0.1077 0.0953  0.0451  94  LEU   A CD1 
537  C  CD2 . LEU   A 74  ? 0.8316 0.9911 1.1353 -0.1165 0.0654  0.0304  94  LEU   A CD2 
538  N  N   . VAL   A 75  ? 0.9624 1.1982 1.5348 -0.1608 0.0502  0.0030  95  VAL   A N   
539  C  CA  . VAL   A 75  ? 0.9203 1.1929 1.5608 -0.1631 0.0329  -0.0119 95  VAL   A CA  
540  C  C   . VAL   A 75  ? 0.9279 1.2063 1.6415 -0.1813 0.0172  -0.0295 95  VAL   A C   
541  O  O   . VAL   A 75  ? 0.9250 1.2108 1.6510 -0.1782 -0.0234 -0.0528 95  VAL   A O   
542  C  CB  . VAL   A 75  ? 0.9065 1.2060 1.5835 -0.1616 0.0647  0.0015  95  VAL   A CB  
543  C  CG1 . VAL   A 75  ? 0.8106 1.1525 1.5748 -0.1653 0.0486  -0.0152 95  VAL   A CG1 
544  C  CG2 . VAL   A 75  ? 0.8683 1.1641 1.4775 -0.1422 0.0712  0.0119  95  VAL   A CG2 
545  N  N   . LYS   A 76  ? 0.8548 1.1266 1.6154 -0.1995 0.0491  -0.0191 96  LYS   A N   
546  C  CA  . LYS   A 76  ? 0.9021 1.1830 1.7507 -0.2209 0.0397  -0.0364 96  LYS   A CA  
547  C  C   . LYS   A 76  ? 0.9428 1.1956 1.7678 -0.2236 0.0033  -0.0565 96  LYS   A C   
548  O  O   . LYS   A 76  ? 0.9410 1.2105 1.7946 -0.2218 -0.0395 -0.0841 96  LYS   A O   
549  C  CB  . LYS   A 76  ? 0.8696 1.1375 1.7626 -0.2400 0.0893  -0.0166 96  LYS   A CB  
550  C  CG  . LYS   A 76  ? 0.9230 1.2224 1.8614 -0.2400 0.1272  -0.0013 96  LYS   A CG  
551  C  CD  . LYS   A 76  ? 1.0445 1.3207 2.0124 -0.2566 0.1817  0.0218  96  LYS   A CD  
552  C  CE  . LYS   A 76  ? 1.0864 1.3909 2.0909 -0.2536 0.2239  0.0381  96  LYS   A CE  
553  N  NZ  . LYS   A 76  ? 1.1711 1.4377 2.1570 -0.2588 0.2835  0.0694  96  LYS   A NZ  
554  N  N   . GLU   A 77  ? 1.0180 1.2266 1.7883 -0.2254 0.0188  -0.0439 97  GLU   A N   
555  C  CA  . GLU   A 77  ? 1.0007 1.1775 1.7458 -0.2272 -0.0104 -0.0619 97  GLU   A CA  
556  C  C   . GLU   A 77  ? 0.9742 1.1362 1.6255 -0.2041 -0.0347 -0.0654 97  GLU   A C   
557  O  O   . GLU   A 77  ? 1.0201 1.1460 1.6229 -0.2007 -0.0415 -0.0684 97  GLU   A O   
558  C  CB  . GLU   A 77  ? 1.0115 1.1458 1.7534 -0.2405 0.0196  -0.0476 97  GLU   A CB  
559  C  CG  . GLU   A 77  ? 1.0199 1.1608 1.8508 -0.2644 0.0540  -0.0390 97  GLU   A CG  
560  C  CD  . GLU   A 77  ? 1.0328 1.1989 1.9649 -0.2843 0.0269  -0.0700 97  GLU   A CD  
561  O  OE1 . GLU   A 77  ? 0.9236 1.0836 1.8462 -0.2809 -0.0188 -0.0984 97  GLU   A OE1 
562  O  OE2 . GLU   A 77  ? 0.9925 1.1845 2.0149 -0.3025 0.0513  -0.0673 97  GLU   A OE2 
563  N  N   . CYS   A 78  ? 0.9789 1.1660 1.6053 -0.1879 -0.0452 -0.0649 98  CYS   A N   
564  C  CA  . CYS   A 78  ? 1.0107 1.1826 1.5530 -0.1673 -0.0641 -0.0676 98  CYS   A CA  
565  C  C   . CYS   A 78  ? 1.0461 1.2029 1.5758 -0.1625 -0.1058 -0.0950 98  CYS   A C   
566  O  O   . CYS   A 78  ? 1.0538 1.1786 1.5200 -0.1534 -0.1122 -0.0975 98  CYS   A O   
567  C  CB  . CYS   A 78  ? 0.9518 1.1498 1.4769 -0.1523 -0.0651 -0.0616 98  CYS   A CB  
568  S  SG  . CYS   A 78  ? 1.1088 1.2886 1.5445 -0.1282 -0.0910 -0.0688 98  CYS   A SG  
569  N  N   . TYR   A 79  ? 1.2519 1.4318 1.8421 -0.1665 -0.1354 -0.1174 99  TYR   A N   
570  C  CA  . TYR   A 79  ? 1.2453 1.4104 1.8201 -0.1583 -0.1804 -0.1469 99  TYR   A CA  
571  C  C   . TYR   A 79  ? 1.2112 1.3464 1.8050 -0.1739 -0.1851 -0.1603 99  TYR   A C   
572  O  O   . TYR   A 79  ? 1.2314 1.3403 1.7852 -0.1637 -0.2168 -0.1820 99  TYR   A O   
573  C  CB  . TYR   A 79  ? 1.2827 1.4846 1.9190 -0.1548 -0.2161 -0.1698 99  TYR   A CB  
574  C  CG  . TYR   A 79  ? 1.3354 1.5525 1.9284 -0.1303 -0.2264 -0.1640 99  TYR   A CG  
575  C  CD1 . TYR   A 79  ? 1.4623 1.6528 1.9707 -0.1050 -0.2546 -0.1732 99  TYR   A CD1 
576  C  CD2 . TYR   A 79  ? 1.3122 1.5653 1.9449 -0.1310 -0.2054 -0.1486 99  TYR   A CD2 
577  C  CE1 . TYR   A 79  ? 1.4896 1.6865 1.9550 -0.0822 -0.2610 -0.1658 99  TYR   A CE1 
578  C  CE2 . TYR   A 79  ? 1.4145 1.6764 2.0064 -0.1079 -0.2144 -0.1433 99  TYR   A CE2 
579  C  CZ  . TYR   A 79  ? 1.4676 1.6999 1.9759 -0.0840 -0.2420 -0.1513 99  TYR   A CZ  
580  O  OH  . TYR   A 79  ? 1.3860 1.6194 1.8499 -0.0604 -0.2483 -0.1442 99  TYR   A OH  
581  N  N   . SER   A 80  ? 1.0691 1.2026 1.7175 -0.1966 -0.1527 -0.1477 100 SER   A N   
582  C  CA  . SER   A 80  ? 1.0399 1.1426 1.7172 -0.2134 -0.1561 -0.1611 100 SER   A CA  
583  C  C   . SER   A 80  ? 1.0895 1.1482 1.7055 -0.2117 -0.1270 -0.1411 100 SER   A C   
584  O  O   . SER   A 80  ? 1.1425 1.1648 1.7468 -0.2150 -0.1392 -0.1558 100 SER   A O   
585  C  CB  . SER   A 80  ? 1.0731 1.1974 1.8628 -0.2417 -0.1401 -0.1633 100 SER   A CB  
586  O  OG  . SER   A 80  ? 1.0524 1.2020 1.8639 -0.2457 -0.0987 -0.1341 100 SER   A OG  
587  N  N   . VAL   A 81  ? 1.1129 1.1732 1.6898 -0.2048 -0.0911 -0.1101 101 VAL   A N   
588  C  CA  . VAL   A 81  ? 1.0860 1.1079 1.6119 -0.2012 -0.0649 -0.0917 101 VAL   A CA  
589  C  C   . VAL   A 81  ? 1.0623 1.0868 1.5096 -0.1794 -0.0550 -0.0751 101 VAL   A C   
590  O  O   . VAL   A 81  ? 1.0393 1.0358 1.4292 -0.1676 -0.0530 -0.0728 101 VAL   A O   
591  C  CB  . VAL   A 81  ? 1.0802 1.0924 1.6504 -0.2185 -0.0243 -0.0692 101 VAL   A CB  
592  C  CG1 . VAL   A 81  ? 1.0874 1.0571 1.5989 -0.2097 -0.0014 -0.0506 101 VAL   A CG1 
593  C  CG2 . VAL   A 81  ? 1.1045 1.1125 1.7628 -0.2439 -0.0297 -0.0862 101 VAL   A CG2 
594  N  N   . PHE   A 82  ? 1.0914 1.1499 1.5398 -0.1739 -0.0481 -0.0646 102 PHE   A N   
595  C  CA  . PHE   A 82  ? 1.0281 1.0894 1.4132 -0.1571 -0.0341 -0.0483 102 PHE   A CA  
596  C  C   . PHE   A 82  ? 1.0740 1.1533 1.4288 -0.1430 -0.0557 -0.0579 102 PHE   A C   
597  O  O   . PHE   A 82  ? 1.0925 1.1965 1.4481 -0.1386 -0.0465 -0.0476 102 PHE   A O   
598  C  CB  . PHE   A 82  ? 1.0012 1.0766 1.4002 -0.1603 0.0000  -0.0236 102 PHE   A CB  
599  C  CG  . PHE   A 82  ? 1.0232 1.0741 1.4430 -0.1711 0.0263  -0.0097 102 PHE   A CG  
600  C  CD1 . PHE   A 82  ? 1.0386 1.0573 1.4101 -0.1619 0.0378  0.0005  102 PHE   A CD1 
601  C  CD2 . PHE   A 82  ? 1.0606 1.1194 1.5494 -0.1892 0.0413  -0.0062 102 PHE   A CD2 
602  C  CE1 . PHE   A 82  ? 1.0461 1.0348 1.4287 -0.1686 0.0627  0.0154  102 PHE   A CE1 
603  C  CE2 . PHE   A 82  ? 1.0564 1.0851 1.5600 -0.1988 0.0706  0.0094  102 PHE   A CE2 
604  C  CZ  . PHE   A 82  ? 1.0424 1.0332 1.4883 -0.1874 0.0809  0.0211  102 PHE   A CZ  
605  N  N   . THR   A 83  ? 1.0825 1.1443 1.4040 -0.1338 -0.0824 -0.0767 103 THR   A N   
606  C  CA  . THR   A 83  ? 1.0980 1.1686 1.3878 -0.1189 -0.1041 -0.0863 103 THR   A CA  
607  C  C   . THR   A 83  ? 1.0283 1.0875 1.2478 -0.1031 -0.0918 -0.0766 103 THR   A C   
608  O  O   . THR   A 83  ? 1.0000 1.0683 1.1948 -0.0921 -0.0957 -0.0745 103 THR   A O   
609  C  CB  . THR   A 83  ? 1.1228 1.1779 1.4111 -0.1145 -0.1417 -0.1138 103 THR   A CB  
610  O  OG1 . THR   A 83  ? 1.1212 1.1887 1.4872 -0.1326 -0.1529 -0.1258 103 THR   A OG1 
611  C  CG2 . THR   A 83  ? 1.1155 1.1770 1.3714 -0.0961 -0.1665 -0.1232 103 THR   A CG2 
612  N  N   . ASN   A 84  ? 1.0642 1.1037 1.2548 -0.1014 -0.0758 -0.0707 104 ASN   A N   
613  C  CA  . ASN   A 84  ? 1.1049 1.1334 1.2368 -0.0871 -0.0663 -0.0670 104 ASN   A CA  
614  C  C   . ASN   A 84  ? 1.0404 1.0785 1.1697 -0.0883 -0.0381 -0.0492 104 ASN   A C   
615  O  O   . ASN   A 84  ? 1.0440 1.0872 1.2038 -0.0972 -0.0263 -0.0396 104 ASN   A O   
616  C  CB  . ASN   A 84  ? 1.0772 1.0734 1.1722 -0.0783 -0.0768 -0.0817 104 ASN   A CB  
617  C  CG  . ASN   A 84  ? 1.1611 1.1437 1.2687 -0.0795 -0.1085 -0.1032 104 ASN   A CG  
618  O  OD1 . ASN   A 84  ? 1.1490 1.1423 1.2632 -0.0762 -0.1286 -0.1109 104 ASN   A OD1 
619  N  ND2 . ASN   A 84  ? 1.2152 1.1732 1.3275 -0.0830 -0.1151 -0.1146 104 ASN   A ND2 
620  N  N   . ARG   A 85  ? 1.0551 1.0941 1.1470 -0.0783 -0.0274 -0.0456 105 ARG   A N   
621  C  CA  . ARG   A 85  ? 1.0363 1.0842 1.1226 -0.0762 -0.0062 -0.0349 105 ARG   A CA  
622  C  C   . ARG   A 85  ? 1.0295 1.0587 1.0920 -0.0679 -0.0026 -0.0412 105 ARG   A C   
623  O  O   . ARG   A 85  ? 1.1229 1.1302 1.1644 -0.0627 -0.0136 -0.0533 105 ARG   A O   
624  C  CB  . ARG   A 85  ? 0.9661 1.0298 1.0383 -0.0726 0.0044  -0.0295 105 ARG   A CB  
625  C  CG  . ARG   A 85  ? 0.9437 1.0232 1.0355 -0.0775 0.0005  -0.0244 105 ARG   A CG  
626  C  CD  . ARG   A 85  ? 0.9465 1.0380 1.0270 -0.0748 0.0137  -0.0185 105 ARG   A CD  
627  N  NE  . ARG   A 85  ? 0.9499 1.0562 1.0508 -0.0778 0.0119  -0.0131 105 ARG   A NE  
628  C  CZ  . ARG   A 85  ? 0.9572 1.0603 1.0507 -0.0734 0.0019  -0.0155 105 ARG   A CZ  
629  N  NH1 . ARG   A 85  ? 0.9663 1.0484 1.0254 -0.0649 -0.0069 -0.0220 105 ARG   A NH1 
630  N  NH2 . ARG   A 85  ? 0.9198 1.0390 1.0373 -0.0747 0.0012  -0.0109 105 ARG   A NH2 
631  N  N   . ARG   A 86  ? 1.0325 1.0701 1.0973 -0.0644 0.0117  -0.0342 106 ARG   A N   
632  C  CA  . ARG   A 86  ? 1.1184 1.1405 1.1694 -0.0550 0.0149  -0.0398 106 ARG   A CA  
633  C  C   . ARG   A 86  ? 1.1582 1.1745 1.1793 -0.0456 0.0194  -0.0496 106 ARG   A C   
634  O  O   . ARG   A 86  ? 1.1331 1.1627 1.1466 -0.0458 0.0276  -0.0476 106 ARG   A O   
635  C  CB  . ARG   A 86  ? 1.0265 1.0615 1.0870 -0.0494 0.0258  -0.0313 106 ARG   A CB  
636  C  CG  . ARG   A 86  ? 1.0460 1.1020 1.1011 -0.0411 0.0364  -0.0345 106 ARG   A CG  
637  C  CD  . ARG   A 86  ? 0.9964 1.0601 1.0588 -0.0299 0.0395  -0.0319 106 ARG   A CD  
638  N  NE  . ARG   A 86  ? 1.0028 1.0779 1.0745 -0.0315 0.0396  -0.0207 106 ARG   A NE  
639  C  CZ  . ARG   A 86  ? 1.0135 1.0903 1.0839 -0.0192 0.0391  -0.0161 106 ARG   A CZ  
640  N  NH1 . ARG   A 86  ? 0.9761 1.0458 1.0420 -0.0046 0.0372  -0.0214 106 ARG   A NH1 
641  N  NH2 . ARG   A 86  ? 0.9699 1.0538 1.0398 -0.0186 0.0403  -0.0062 106 ARG   A NH2 
642  N  N   . PRO   A 87  ? 1.1468 1.1392 1.1488 -0.0369 0.0166  -0.0598 107 PRO   A N   
643  C  CA  . PRO   A 87  ? 1.1951 1.1769 1.1632 -0.0261 0.0250  -0.0685 107 PRO   A CA  
644  C  C   . PRO   A 87  ? 1.2689 1.2759 1.2441 -0.0227 0.0470  -0.0644 107 PRO   A C   
645  O  O   . PRO   A 87  ? 1.2737 1.3026 1.2761 -0.0225 0.0524  -0.0603 107 PRO   A O   
646  C  CB  . PRO   A 87  ? 1.3017 1.2555 1.2543 -0.0159 0.0205  -0.0797 107 PRO   A CB  
647  C  CG  . PRO   A 87  ? 1.2202 1.1607 1.1934 -0.0255 0.0021  -0.0798 107 PRO   A CG  
648  C  CD  . PRO   A 87  ? 1.2013 1.1694 1.2091 -0.0367 0.0063  -0.0643 107 PRO   A CD  
649  N  N   . PHE   A 88  ? 1.3696 1.3712 1.3196 -0.0190 0.0597  -0.0664 108 PHE   A N   
650  C  CA  . PHE   A 88  ? 1.4524 1.4776 1.4163 -0.0206 0.0826  -0.0628 108 PHE   A CA  
651  C  C   . PHE   A 88  ? 1.6023 1.6068 1.5307 -0.0105 0.1029  -0.0678 108 PHE   A C   
652  O  O   . PHE   A 88  ? 1.6259 1.6047 1.5143 -0.0077 0.1023  -0.0660 108 PHE   A O   
653  C  CB  . PHE   A 88  ? 1.4573 1.4964 1.4324 -0.0322 0.0808  -0.0538 108 PHE   A CB  
654  C  CG  . PHE   A 88  ? 1.5305 1.5875 1.5195 -0.0363 0.1040  -0.0517 108 PHE   A CG  
655  C  CD1 . PHE   A 88  ? 1.5571 1.6443 1.5845 -0.0371 0.1142  -0.0562 108 PHE   A CD1 
656  C  CD2 . PHE   A 88  ? 1.5586 1.6012 1.5247 -0.0390 0.1141  -0.0463 108 PHE   A CD2 
657  C  CE1 . PHE   A 88  ? 1.5921 1.6974 1.6421 -0.0435 0.1346  -0.0575 108 PHE   A CE1 
658  C  CE2 . PHE   A 88  ? 1.6142 1.6690 1.5971 -0.0452 0.1379  -0.0445 108 PHE   A CE2 
659  C  CZ  . PHE   A 88  ? 1.5975 1.6852 1.6264 -0.0492 0.1483  -0.0512 108 PHE   A CZ  
660  N  N   . GLY   A 89  ? 1.7211 1.7350 1.6618 -0.0025 0.1211  -0.0741 109 GLY   A N   
661  C  CA  . GLY   A 89  ? 1.6647 1.6576 1.5722 0.0089  0.1460  -0.0786 109 GLY   A CA  
662  C  C   . GLY   A 89  ? 1.5415 1.5639 1.4884 0.0117  0.1737  -0.0833 109 GLY   A C   
663  O  O   . GLY   A 89  ? 1.5000 1.5581 1.4975 0.0084  0.1670  -0.0861 109 GLY   A O   
664  N  N   . PRO   A 90  ? 1.5475 1.5550 1.4720 0.0195  0.2060  -0.0850 110 PRO   A N   
665  C  CA  . PRO   A 90  ? 1.5829 1.5416 1.4355 0.0297  0.2169  -0.0820 110 PRO   A CA  
666  C  C   . PRO   A 90  ? 1.6907 1.6362 1.5218 0.0203  0.2236  -0.0695 110 PRO   A C   
667  O  O   . PRO   A 90  ? 1.6731 1.6447 1.5456 0.0067  0.2419  -0.0640 110 PRO   A O   
668  C  CB  . PRO   A 90  ? 1.5473 1.5019 1.3958 0.0423  0.2568  -0.0875 110 PRO   A CB  
669  C  CG  . PRO   A 90  ? 1.5208 1.5307 1.4527 0.0308  0.2738  -0.0904 110 PRO   A CG  
670  C  CD  . PRO   A 90  ? 1.5304 1.5725 1.5058 0.0180  0.2378  -0.0896 110 PRO   A CD  
671  N  N   . VAL   A 91  ? 1.6735 1.5774 1.4405 0.0287  0.2071  -0.0663 111 VAL   A N   
672  C  CA  . VAL   A 91  ? 1.6239 1.5122 1.3668 0.0236  0.2077  -0.0542 111 VAL   A CA  
673  C  C   . VAL   A 91  ? 1.6696 1.5027 1.3290 0.0421  0.2266  -0.0488 111 VAL   A C   
674  O  O   . VAL   A 91  ? 1.7447 1.5596 1.3807 0.0405  0.2385  -0.0362 111 VAL   A O   
675  C  CB  . VAL   A 91  ? 1.5955 1.4900 1.3454 0.0170  0.1642  -0.0539 111 VAL   A CB  
676  C  CG1 . VAL   A 91  ? 1.5619 1.5055 1.3859 -0.0019 0.1558  -0.0525 111 VAL   A CG1 
677  C  CG2 . VAL   A 91  ? 1.5645 1.4395 1.2875 0.0281  0.1323  -0.0662 111 VAL   A CG2 
678  N  N   . GLY   A 92  ? 1.7246 1.5256 1.3325 0.0619  0.2297  -0.0576 112 GLY   A N   
679  C  CA  . GLY   A 92  ? 1.7343 1.4768 1.2511 0.0839  0.2486  -0.0522 112 GLY   A CA  
680  C  C   . GLY   A 92  ? 1.7854 1.4962 1.2476 0.0931  0.2124  -0.0494 112 GLY   A C   
681  O  O   . GLY   A 92  ? 1.7500 1.4703 1.2233 0.0917  0.1658  -0.0605 112 GLY   A O   
682  N  N   . PHE   A 93  ? 1.7125 1.3847 1.1179 0.1033  0.2349  -0.0344 113 PHE   A N   
683  C  CA  . PHE   A 93  ? 1.7173 1.3555 1.0638 0.1177  0.2015  -0.0314 113 PHE   A CA  
684  C  C   . PHE   A 93  ? 1.6424 1.3211 1.0527 0.0975  0.1711  -0.0283 113 PHE   A C   
685  O  O   . PHE   A 93  ? 1.6666 1.3282 1.0446 0.1086  0.1359  -0.0293 113 PHE   A O   
686  C  CB  . PHE   A 93  ? 1.8025 1.3827 1.0661 0.1367  0.2381  -0.0132 113 PHE   A CB  
687  C  CG  . PHE   A 93  ? 1.7481 1.3434 1.0564 0.1163  0.2762  0.0058  113 PHE   A CG  
688  C  CD1 . PHE   A 93  ? 1.7455 1.3637 1.1060 0.0993  0.3263  0.0102  113 PHE   A CD1 
689  C  CD2 . PHE   A 93  ? 1.7482 1.3356 1.0509 0.1145  0.2609  0.0171  113 PHE   A CD2 
690  C  CE1 . PHE   A 93  ? 1.7962 1.4282 1.2038 0.0788  0.3592  0.0240  113 PHE   A CE1 
691  C  CE2 . PHE   A 93  ? 1.7878 1.3850 1.1315 0.0954  0.2952  0.0326  113 PHE   A CE2 
692  C  CZ  . PHE   A 93  ? 1.8780 1.4969 1.2748 0.0766  0.3438  0.0353  113 PHE   A CZ  
693  N  N   . MET   A 94  ? 1.6028 1.3340 1.1010 0.0706  0.1831  -0.0257 114 MET   A N   
694  C  CA  . MET   A 94  ? 1.5660 1.3364 1.1247 0.0525  0.1557  -0.0242 114 MET   A CA  
695  C  C   . MET   A 94  ? 1.5501 1.3464 1.1424 0.0483  0.1110  -0.0395 114 MET   A C   
696  O  O   . MET   A 94  ? 1.4122 1.2453 1.0624 0.0320  0.0922  -0.0389 114 MET   A O   
697  C  CB  . MET   A 94  ? 1.5521 1.3646 1.1852 0.0282  0.1840  -0.0177 114 MET   A CB  
698  C  CG  . MET   A 94  ? 1.5412 1.3308 1.1569 0.0263  0.2256  -0.0023 114 MET   A CG  
699  S  SD  . MET   A 94  ? 1.6179 1.3892 1.2140 0.0277  0.2102  0.0107  114 MET   A SD  
700  C  CE  . MET   A 94  ? 1.3958 1.2328 1.0926 -0.0005 0.1957  0.0060  114 MET   A CE  
701  N  N   . LYS   A 95  ? 1.5296 1.3039 1.0860 0.0627  0.0963  -0.0533 115 LYS   A N   
702  C  CA  . LYS   A 95  ? 1.4790 1.2659 1.0590 0.0602  0.0523  -0.0689 115 LYS   A CA  
703  C  C   . LYS   A 95  ? 1.4595 1.2430 1.0322 0.0642  0.0159  -0.0701 115 LYS   A C   
704  O  O   . LYS   A 95  ? 1.4150 1.2246 1.0368 0.0531  -0.0160 -0.0790 115 LYS   A O   
705  C  CB  . LYS   A 95  ? 1.5311 1.2841 1.0617 0.0784  0.0433  -0.0854 115 LYS   A CB  
706  C  CG  . LYS   A 95  ? 1.6253 1.3215 1.0573 0.1069  0.0522  -0.0847 115 LYS   A CG  
707  C  CD  . LYS   A 95  ? 1.6491 1.3090 1.0274 0.1271  0.0379  -0.1046 115 LYS   A CD  
708  C  CE  . LYS   A 95  ? 1.7757 1.4053 1.1046 0.1457  -0.0122 -0.1207 115 LYS   A CE  
709  N  NZ  . LYS   A 95  ? 1.9036 1.4876 1.1444 0.1716  -0.0062 -0.1106 115 LYS   A NZ  
710  N  N   . SER   A 96  ? 1.5634 1.3140 1.0770 0.0808  0.0215  -0.0609 116 SER   A N   
711  C  CA  . SER   A 96  ? 1.5263 1.2702 1.0256 0.0910  -0.0147 -0.0631 116 SER   A CA  
712  C  C   . SER   A 96  ? 1.4844 1.2578 1.0313 0.0763  -0.0077 -0.0481 116 SER   A C   
713  O  O   . SER   A 96  ? 1.5077 1.2793 1.0491 0.0854  -0.0355 -0.0488 116 SER   A O   
714  C  CB  . SER   A 96  ? 1.7162 1.3994 1.1118 0.1242  -0.0171 -0.0621 116 SER   A CB  
715  O  OG  . SER   A 96  ? 1.7535 1.4061 1.0987 0.1413  -0.0299 -0.0796 116 SER   A OG  
716  N  N   . ALA   A 97  ? 1.4464 1.2465 1.0395 0.0558  0.0268  -0.0365 117 ALA   A N   
717  C  CA  . ALA   A 97  ? 1.3957 1.2241 1.0362 0.0414  0.0315  -0.0254 117 ALA   A CA  
718  C  C   . ALA   A 97  ? 1.3048 1.1725 1.0063 0.0305  -0.0038 -0.0343 117 ALA   A C   
719  O  O   . ALA   A 97  ? 1.3092 1.1956 1.0436 0.0219  -0.0174 -0.0456 117 ALA   A O   
720  C  CB  . ALA   A 97  ? 1.3717 1.2236 1.0543 0.0217  0.0702  -0.0169 117 ALA   A CB  
721  N  N   . ILE   A 98  ? 1.2726 1.1505 0.9901 0.0314  -0.0160 -0.0287 118 ILE   A N   
722  C  CA  . ILE   A 98  ? 1.2448 1.1576 1.0188 0.0240  -0.0481 -0.0374 118 ILE   A CA  
723  C  C   . ILE   A 98  ? 1.2183 1.1718 1.0607 -0.0003 -0.0372 -0.0369 118 ILE   A C   
724  O  O   . ILE   A 98  ? 1.1783 1.1533 1.0634 -0.0085 -0.0577 -0.0464 118 ILE   A O   
725  C  CB  . ILE   A 98  ? 1.2515 1.1685 1.0309 0.0318  -0.0586 -0.0306 118 ILE   A CB  
726  C  CG1 . ILE   A 98  ? 1.1927 1.1490 1.0377 0.0245  -0.0890 -0.0406 118 ILE   A CG1 
727  C  CG2 . ILE   A 98  ? 1.1794 1.1025 0.9714 0.0212  -0.0247 -0.0147 118 ILE   A CG2 
728  C  CD1 . ILE   A 98  ? 1.1735 1.1388 1.0310 0.0342  -0.1008 -0.0360 118 ILE   A CD1 
729  N  N   . SER   A 99  ? 1.1644 1.1268 1.0180 -0.0113 -0.0053 -0.0267 119 SER   A N   
730  C  CA  . SER   A 99  ? 1.1383 1.1350 1.0465 -0.0294 0.0036  -0.0261 119 SER   A CA  
731  C  C   . SER   A 99  ? 1.1616 1.1560 1.0707 -0.0319 0.0046  -0.0341 119 SER   A C   
732  O  O   . SER   A 99  ? 1.1124 1.1300 1.0623 -0.0432 0.0057  -0.0344 119 SER   A O   
733  C  CB  . SER   A 99  ? 1.1750 1.1825 1.0953 -0.0378 0.0320  -0.0167 119 SER   A CB  
734  O  OG  . SER   A 99  ? 1.2331 1.2156 1.1157 -0.0326 0.0551  -0.0143 119 SER   A OG  
735  N  N   . ILE   A 100 ? 1.2165 1.1798 1.0772 -0.0192 0.0054  -0.0399 120 ILE   A N   
736  C  CA  . ILE   A 100 ? 1.1684 1.1251 1.0250 -0.0186 0.0080  -0.0485 120 ILE   A CA  
737  C  C   . ILE   A 100 ? 1.1957 1.1331 1.0355 -0.0102 -0.0227 -0.0632 120 ILE   A C   
738  O  O   . ILE   A 100 ? 1.2023 1.1371 1.0524 -0.0127 -0.0267 -0.0718 120 ILE   A O   
739  C  CB  . ILE   A 100 ? 1.2584 1.1951 1.0765 -0.0106 0.0382  -0.0458 120 ILE   A CB  
740  C  CG1 . ILE   A 100 ? 1.3031 1.2648 1.1541 -0.0225 0.0659  -0.0359 120 ILE   A CG1 
741  C  CG2 . ILE   A 100 ? 1.2818 1.2094 1.0917 -0.0058 0.0417  -0.0559 120 ILE   A CG2 
742  C  CD1 . ILE   A 100 ? 1.4272 1.3680 1.2453 -0.0170 0.0983  -0.0300 120 ILE   A CD1 
743  N  N   . ALA   A 101 ? 1.2701 1.1947 1.0891 -0.0002 -0.0471 -0.0678 121 ALA   A N   
744  C  CA  . ALA   A 101 ? 1.2724 1.1800 1.0787 0.0085  -0.0817 -0.0862 121 ALA   A CA  
745  C  C   . ALA   A 101 ? 1.2424 1.1774 1.1185 -0.0097 -0.0985 -0.0936 121 ALA   A C   
746  O  O   . ALA   A 101 ? 1.2234 1.1892 1.1511 -0.0261 -0.0848 -0.0824 121 ALA   A O   
747  C  CB  . ALA   A 101 ? 1.3225 1.2150 1.0958 0.0256  -0.1072 -0.0905 121 ALA   A CB  
748  N  N   . GLU   A 102 ? 1.2835 1.2032 1.1587 -0.0059 -0.1279 -0.1134 122 GLU   A N   
749  C  CA  . GLU   A 102 ? 1.2676 1.2045 1.2080 -0.0241 -0.1411 -0.1219 122 GLU   A CA  
750  C  C   . GLU   A 102 ? 1.3281 1.2608 1.2843 -0.0205 -0.1835 -0.1448 122 GLU   A C   
751  O  O   . GLU   A 102 ? 1.3795 1.2833 1.2798 0.0000  -0.2064 -0.1600 122 GLU   A O   
752  C  CB  . GLU   A 102 ? 1.2510 1.1705 1.1868 -0.0279 -0.1288 -0.1259 122 GLU   A CB  
753  C  CG  . GLU   A 102 ? 1.2475 1.1779 1.1835 -0.0322 -0.0917 -0.1071 122 GLU   A CG  
754  C  CD  . GLU   A 102 ? 1.2346 1.1431 1.1536 -0.0280 -0.0821 -0.1133 122 GLU   A CD  
755  O  OE1 . GLU   A 102 ? 1.3408 1.2200 1.2366 -0.0201 -0.1019 -0.1320 122 GLU   A OE1 
756  O  OE2 . GLU   A 102 ? 1.2913 1.2115 1.2201 -0.0309 -0.0565 -0.1011 122 GLU   A OE2 
757  N  N   . ASP   A 103 ? 1.2385 1.1998 1.2724 -0.0398 -0.1932 -0.1480 123 ASP   A N   
758  C  CA  . ASP   A 103 ? 1.2791 1.2425 1.3544 -0.0438 -0.2323 -0.1737 123 ASP   A CA  
759  C  C   . ASP   A 103 ? 1.3025 1.2664 1.3514 -0.0231 -0.2659 -0.1862 123 ASP   A C   
760  O  O   . ASP   A 103 ? 1.3205 1.3087 1.3813 -0.0205 -0.2591 -0.1722 123 ASP   A O   
761  C  CB  . ASP   A 103 ? 1.3281 1.2568 1.3849 -0.0438 -0.2421 -0.1922 123 ASP   A CB  
762  C  CG  . ASP   A 103 ? 1.2590 1.1905 1.3616 -0.0657 -0.2151 -0.1814 123 ASP   A CG  
763  O  OD1 . ASP   A 103 ? 1.2745 1.2300 1.4541 -0.0868 -0.2142 -0.1799 123 ASP   A OD1 
764  O  OD2 . ASP   A 103 ? 1.3181 1.2270 1.3794 -0.0603 -0.1930 -0.1737 123 ASP   A OD2 
765  N  N   . GLU   A 104 ? 1.3197 1.2552 1.3296 -0.0057 -0.3034 -0.2128 124 GLU   A N   
766  C  CA  . GLU   A 104 ? 1.3926 1.3291 1.3814 0.0168  -0.3422 -0.2273 124 GLU   A CA  
767  C  C   . GLU   A 104 ? 1.4274 1.3390 1.3242 0.0431  -0.3265 -0.2089 124 GLU   A C   
768  O  O   . GLU   A 104 ? 1.4532 1.3733 1.3403 0.0593  -0.3438 -0.2074 124 GLU   A O   
769  C  CB  . GLU   A 104 ? 1.4721 1.3825 1.4427 0.0299  -0.3909 -0.2643 124 GLU   A CB  
770  C  CG  . GLU   A 104 ? 1.4538 1.3862 1.5229 0.0023  -0.4089 -0.2860 124 GLU   A CG  
771  C  CD  . GLU   A 104 ? 1.3623 1.3496 1.5345 -0.0144 -0.4198 -0.2871 124 GLU   A CD  
772  O  OE1 . GLU   A 104 ? 1.3653 1.3668 1.5330 0.0054  -0.4524 -0.2976 124 GLU   A OE1 
773  O  OE2 . GLU   A 104 ? 1.3038 1.3184 1.5592 -0.0451 -0.3939 -0.2768 124 GLU   A OE2 
774  N  N   . GLU   A 105 ? 1.4536 1.3335 1.2854 0.0483  -0.2926 -0.1949 125 GLU   A N   
775  C  CA  . GLU   A 105 ? 1.5009 1.3530 1.2485 0.0708  -0.2707 -0.1763 125 GLU   A CA  
776  C  C   . GLU   A 105 ? 1.4340 1.3173 1.2155 0.0602  -0.2434 -0.1504 125 GLU   A C   
777  O  O   . GLU   A 105 ? 1.4954 1.3651 1.2318 0.0794  -0.2431 -0.1404 125 GLU   A O   
778  C  CB  . GLU   A 105 ? 1.5525 1.3700 1.2397 0.0750  -0.2363 -0.1687 125 GLU   A CB  
779  C  CG  . GLU   A 105 ? 1.7678 1.5382 1.3847 0.0978  -0.2606 -0.1927 125 GLU   A CG  
780  C  CD  . GLU   A 105 ? 1.7035 1.4830 1.3755 0.0855  -0.2977 -0.2218 125 GLU   A CD  
781  O  OE1 . GLU   A 105 ? 1.6264 1.4452 1.3900 0.0561  -0.2924 -0.2188 125 GLU   A OE1 
782  O  OE2 . GLU   A 105 ? 1.7944 1.5384 1.4162 0.1059  -0.3312 -0.2481 125 GLU   A OE2 
783  N  N   . TRP   A 106 ? 1.4004 1.3210 1.2565 0.0319  -0.2205 -0.1395 126 TRP   A N   
784  C  CA  . TRP   A 106 ? 1.2814 1.2338 1.1762 0.0220  -0.1999 -0.1194 126 TRP   A CA  
785  C  C   . TRP   A 106 ? 1.2556 1.2316 1.1885 0.0286  -0.2329 -0.1283 126 TRP   A C   
786  O  O   . TRP   A 106 ? 1.2612 1.2380 1.1755 0.0409  -0.2289 -0.1165 126 TRP   A O   
787  C  CB  . TRP   A 106 ? 1.1826 1.1666 1.1444 -0.0062 -0.1732 -0.1088 126 TRP   A CB  
788  C  CG  . TRP   A 106 ? 1.1536 1.1725 1.1629 -0.0161 -0.1586 -0.0934 126 TRP   A CG  
789  C  CD1 . TRP   A 106 ? 1.0858 1.1043 1.0716 -0.0130 -0.1318 -0.0748 126 TRP   A CD1 
790  C  CD2 . TRP   A 106 ? 1.1216 1.1786 1.2105 -0.0304 -0.1680 -0.0963 126 TRP   A CD2 
791  N  NE1 . TRP   A 106 ? 1.0612 1.1135 1.1013 -0.0225 -0.1261 -0.0667 126 TRP   A NE1 
792  C  CE2 . TRP   A 106 ? 1.0803 1.1574 1.1838 -0.0327 -0.1461 -0.0786 126 TRP   A CE2 
793  C  CE3 . TRP   A 106 ? 1.0695 1.1447 1.2220 -0.0420 -0.1906 -0.1128 126 TRP   A CE3 
794  C  CZ2 . TRP   A 106 ? 1.0439 1.1583 1.2178 -0.0439 -0.1445 -0.0759 126 TRP   A CZ2 
795  C  CZ3 . TRP   A 106 ? 1.0700 1.1843 1.2993 -0.0555 -0.1869 -0.1093 126 TRP   A CZ3 
796  C  CH2 . TRP   A 106 ? 1.0348 1.1682 1.2715 -0.0551 -0.1633 -0.0905 126 TRP   A CH2 
797  N  N   . LYS   A 107 ? 1.2405 1.2359 1.2316 0.0206  -0.2655 -0.1502 127 LYS   A N   
798  C  CA  . LYS   A 107 ? 1.2387 1.2667 1.2867 0.0243  -0.2975 -0.1620 127 LYS   A CA  
799  C  C   . LYS   A 107 ? 1.2502 1.2542 1.2309 0.0590  -0.3255 -0.1670 127 LYS   A C   
800  O  O   . LYS   A 107 ? 1.2541 1.2797 1.2579 0.0679  -0.3334 -0.1620 127 LYS   A O   
801  C  CB  . LYS   A 107 ? 1.1951 1.2411 1.3126 0.0107  -0.3300 -0.1897 127 LYS   A CB  
802  C  CG  . LYS   A 107 ? 1.2118 1.3086 1.4292 0.0004  -0.3483 -0.1991 127 LYS   A CG  
803  C  CD  . LYS   A 107 ? 1.2681 1.3875 1.5759 -0.0306 -0.3460 -0.2108 127 LYS   A CD  
804  C  CE  . LYS   A 107 ? 1.3455 1.4332 1.6316 -0.0292 -0.3749 -0.2376 127 LYS   A CE  
805  N  NZ  . LYS   A 107 ? 1.3143 1.4121 1.6783 -0.0615 -0.3622 -0.2435 127 LYS   A NZ  
806  N  N   . ARG   A 108 ? 1.3714 1.3269 1.2638 0.0816  -0.3396 -0.1764 128 ARG   A N   
807  C  CA  . ARG   A 108 ? 1.4397 1.3608 1.2499 0.1193  -0.3630 -0.1782 128 ARG   A CA  
808  C  C   . ARG   A 108 ? 1.4289 1.3314 1.1883 0.1270  -0.3220 -0.1463 128 ARG   A C   
809  O  O   . ARG   A 108 ? 1.4531 1.3498 1.1895 0.1492  -0.3347 -0.1407 128 ARG   A O   
810  C  CB  . ARG   A 108 ? 1.6044 1.4724 1.3249 0.1425  -0.3833 -0.1952 128 ARG   A CB  
811  C  CG  . ARG   A 108 ? 1.7579 1.5692 1.3584 0.1816  -0.3819 -0.1844 128 ARG   A CG  
812  C  CD  . ARG   A 108 ? 1.8995 1.6549 1.4064 0.2011  -0.3867 -0.1966 128 ARG   A CD  
813  N  NE  . ARG   A 108 ? 2.1119 1.8058 1.4966 0.2360  -0.3695 -0.1793 128 ARG   A NE  
814  C  CZ  . ARG   A 108 ? 2.0894 1.7515 1.4196 0.2330  -0.3139 -0.1539 128 ARG   A CZ  
815  N  NH1 . ARG   A 108 ? 1.9255 1.6128 1.3091 0.1994  -0.2742 -0.1444 128 ARG   A NH1 
816  N  NH2 . ARG   A 108 ? 2.2732 1.8759 1.4936 0.2656  -0.2973 -0.1379 128 ARG   A NH2 
817  N  N   . LEU   A 109 ? 1.4342 1.3270 1.1788 0.1095  -0.2737 -0.1267 129 LEU   A N   
818  C  CA  . LEU   A 109 ? 1.4048 1.2814 1.1120 0.1123  -0.2329 -0.0989 129 LEU   A CA  
819  C  C   . LEU   A 109 ? 1.3340 1.2549 1.1149 0.0974  -0.2239 -0.0880 129 LEU   A C   
820  O  O   . LEU   A 109 ? 1.3617 1.2695 1.1150 0.1113  -0.2145 -0.0736 129 LEU   A O   
821  C  CB  . LEU   A 109 ? 1.3982 1.2604 1.0846 0.0961  -0.1871 -0.0856 129 LEU   A CB  
822  C  CG  . LEU   A 109 ? 1.4978 1.3098 1.1000 0.1135  -0.1834 -0.0916 129 LEU   A CG  
823  C  CD1 . LEU   A 109 ? 1.4237 1.2374 1.0333 0.0935  -0.1397 -0.0815 129 LEU   A CD1 
824  C  CD2 . LEU   A 109 ? 1.6134 1.3711 1.1168 0.1465  -0.1791 -0.0811 129 LEU   A CD2 
825  N  N   . ARG   A 110 ? 1.2628 1.2317 1.1339 0.0703  -0.2237 -0.0937 130 ARG   A N   
826  C  CA  . ARG   A 110 ? 1.1973 1.2086 1.1387 0.0587  -0.2165 -0.0857 130 ARG   A CA  
827  C  C   . ARG   A 110 ? 1.2596 1.2795 1.2097 0.0822  -0.2539 -0.0956 130 ARG   A C   
828  O  O   . ARG   A 110 ? 1.2312 1.2538 1.1790 0.0916  -0.2444 -0.0827 130 ARG   A O   
829  C  CB  . ARG   A 110 ? 1.1145 1.1696 1.1453 0.0292  -0.2116 -0.0916 130 ARG   A CB  
830  C  CG  . ARG   A 110 ? 1.0635 1.1603 1.1636 0.0169  -0.1966 -0.0817 130 ARG   A CG  
831  C  CD  . ARG   A 110 ? 1.0944 1.1889 1.1832 0.0033  -0.1520 -0.0602 130 ARG   A CD  
832  N  NE  . ARG   A 110 ? 1.0655 1.1920 1.2046 -0.0028 -0.1376 -0.0510 130 ARG   A NE  
833  C  CZ  . ARG   A 110 ? 0.9925 1.1266 1.1398 -0.0160 -0.1038 -0.0366 130 ARG   A CZ  
834  N  NH1 . ARG   A 110 ? 1.0149 1.1322 1.1318 -0.0257 -0.0820 -0.0300 130 ARG   A NH1 
835  N  NH2 . ARG   A 110 ? 0.9128 1.0724 1.0998 -0.0176 -0.0929 -0.0303 130 ARG   A NH2 
836  N  N   . SER   A 111 ? 1.2402 1.2639 1.2012 0.0933  -0.2987 -0.1205 131 SER   A N   
837  C  CA  . SER   A 111 ? 1.2052 1.2402 1.1778 0.1192  -0.3414 -0.1342 131 SER   A CA  
838  C  C   . SER   A 111 ? 1.2958 1.2794 1.1665 0.1550  -0.3428 -0.1215 131 SER   A C   
839  O  O   . SER   A 111 ? 1.2831 1.2746 1.1607 0.1731  -0.3529 -0.1166 131 SER   A O   
840  C  CB  . SER   A 111 ? 1.2017 1.2457 1.1993 0.1253  -0.3925 -0.1675 131 SER   A CB  
841  O  OG  . SER   A 111 ? 1.2915 1.3557 1.3153 0.1501  -0.4388 -0.1849 131 SER   A OG  
842  N  N   . LEU   A 112 ? 1.4008 1.3286 1.1753 0.1662  -0.3291 -0.1146 132 LEU   A N   
843  C  CA  . LEU   A 112 ? 1.4834 1.3521 1.1512 0.2027  -0.3292 -0.1023 132 LEU   A CA  
844  C  C   . LEU   A 112 ? 1.4879 1.3405 1.1356 0.1967  -0.2796 -0.0715 132 LEU   A C   
845  O  O   . LEU   A 112 ? 1.5753 1.3896 1.1609 0.2253  -0.2798 -0.0591 132 LEU   A O   
846  C  CB  . LEU   A 112 ? 1.6071 1.4199 1.1791 0.2183  -0.3302 -0.1073 132 LEU   A CB  
847  C  CG  . LEU   A 112 ? 1.8760 1.6126 1.3186 0.2520  -0.3131 -0.0898 132 LEU   A CG  
848  C  CD1 . LEU   A 112 ? 2.1077 1.8011 1.4708 0.2752  -0.3384 -0.1081 132 LEU   A CD1 
849  C  CD2 . LEU   A 112 ? 1.8656 1.5835 1.2901 0.2307  -0.2475 -0.0612 132 LEU   A CD2 
850  N  N   . LEU   A 113 ? 1.4500 1.3273 1.1461 0.1616  -0.2381 -0.0599 133 LEU   A N   
851  C  CA  . LEU   A 113 ? 1.4337 1.3017 1.1242 0.1520  -0.1935 -0.0355 133 LEU   A CA  
852  C  C   . LEU   A 113 ? 1.3714 1.2884 1.1445 0.1403  -0.1935 -0.0336 133 LEU   A C   
853  O  O   . LEU   A 113 ? 1.3977 1.3038 1.1635 0.1382  -0.1643 -0.0164 133 LEU   A O   
854  C  CB  . LEU   A 113 ? 1.4446 1.3100 1.1366 0.1237  -0.1495 -0.0259 133 LEU   A CB  
855  C  CG  . LEU   A 113 ? 1.5012 1.3078 1.1031 0.1340  -0.1216 -0.0148 133 LEU   A CG  
856  C  CD1 . LEU   A 113 ? 1.4687 1.2901 1.0963 0.1055  -0.0897 -0.0137 133 LEU   A CD1 
857  C  CD2 . LEU   A 113 ? 1.5696 1.3352 1.1227 0.1458  -0.0921 0.0069  133 LEU   A CD2 
858  N  N   . SER   A 114 ? 1.3210 1.2899 1.1738 0.1324  -0.2234 -0.0515 134 SER   A N   
859  C  CA  . SER   A 114 ? 1.2885 1.3056 1.2226 0.1219  -0.2195 -0.0498 134 SER   A CA  
860  C  C   . SER   A 114 ? 1.3318 1.3338 1.2430 0.1498  -0.2269 -0.0419 134 SER   A C   
861  O  O   . SER   A 114 ? 1.3213 1.3337 1.2569 0.1411  -0.1989 -0.0288 134 SER   A O   
862  C  CB  . SER   A 114 ? 1.2434 1.3151 1.2672 0.1109  -0.2500 -0.0716 134 SER   A CB  
863  O  OG  . SER   A 114 ? 1.2118 1.3299 1.3172 0.0868  -0.2265 -0.0663 134 SER   A OG  
864  N  N   . PRO   A 115 ? 1.3869 1.3623 1.2495 0.1853  -0.2640 -0.0495 135 PRO   A N   
865  C  CA  . PRO   A 115 ? 1.4247 1.3871 1.2708 0.2143  -0.2725 -0.0418 135 PRO   A CA  
866  C  C   . PRO   A 115 ? 1.5098 1.4191 1.2886 0.2174  -0.2295 -0.0155 135 PRO   A C   
867  O  O   . PRO   A 115 ? 1.5437 1.4338 1.3028 0.2414  -0.2318 -0.0068 135 PRO   A O   
868  C  CB  . PRO   A 115 ? 1.3700 1.3050 1.1604 0.2549  -0.3238 -0.0562 135 PRO   A CB  
869  C  CG  . PRO   A 115 ? 1.3892 1.3392 1.1936 0.2427  -0.3470 -0.0771 135 PRO   A CG  
870  C  CD  . PRO   A 115 ? 1.3740 1.3223 1.1829 0.2051  -0.3001 -0.0652 135 PRO   A CD  
871  N  N   . THR   A 116 ? 1.5496 1.4352 1.2978 0.1940  -0.1905 -0.0040 136 THR   A N   
872  C  CA  . THR   A 116 ? 1.5917 1.4285 1.2862 0.1923  -0.1474 0.0184  136 THR   A CA  
873  C  C   . THR   A 116 ? 1.6526 1.5199 1.4092 0.1713  -0.1203 0.0248  136 THR   A C   
874  O  O   . THR   A 116 ? 1.7114 1.5416 1.4356 0.1783  -0.0960 0.0397  136 THR   A O   
875  C  CB  . THR   A 116 ? 1.6316 1.4394 1.2831 0.1742  -0.1166 0.0248  136 THR   A CB  
876  O  OG1 . THR   A 116 ? 1.6479 1.4433 1.2609 0.1885  -0.1454 0.0125  136 THR   A OG1 
877  C  CG2 . THR   A 116 ? 1.7753 1.5168 1.3516 0.1826  -0.0790 0.0462  136 THR   A CG2 
878  N  N   . PHE   A 117 ? 1.6319 1.5617 1.4739 0.1471  -0.1231 0.0138  137 PHE   A N   
879  C  CA  . PHE   A 117 ? 1.6440 1.6023 1.5396 0.1271  -0.0960 0.0185  137 PHE   A CA  
880  C  C   . PHE   A 117 ? 1.6445 1.6464 1.6045 0.1377  -0.1153 0.0108  137 PHE   A C   
881  O  O   . PHE   A 117 ? 1.6472 1.6866 1.6655 0.1194  -0.0979 0.0099  137 PHE   A O   
882  C  CB  . PHE   A 117 ? 1.5584 1.5490 1.4953 0.0927  -0.0763 0.0150  137 PHE   A CB  
883  C  CG  . PHE   A 117 ? 1.5132 1.4699 1.3998 0.0816  -0.0564 0.0204  137 PHE   A CG  
884  C  CD1 . PHE   A 117 ? 1.4788 1.4294 1.3430 0.0840  -0.0738 0.0129  137 PHE   A CD1 
885  C  CD2 . PHE   A 117 ? 1.4250 1.3572 1.2911 0.0687  -0.0203 0.0309  137 PHE   A CD2 
886  C  CE1 . PHE   A 117 ? 1.4501 1.3708 1.2701 0.0755  -0.0527 0.0176  137 PHE   A CE1 
887  C  CE2 . PHE   A 117 ? 1.4848 1.3910 1.3146 0.0582  0.0001  0.0347  137 PHE   A CE2 
888  C  CZ  . PHE   A 117 ? 1.4685 1.3692 1.2743 0.0623  -0.0147 0.0290  137 PHE   A CZ  
889  N  N   . THR   A 118 ? 1.6969 1.6951 1.6476 0.1686  -0.1509 0.0044  138 THR   A N   
890  C  CA  . THR   A 118 ? 1.7505 1.7917 1.7673 0.1812  -0.1676 -0.0035 138 THR   A CA  
891  C  C   . THR   A 118 ? 1.8335 1.8536 1.8385 0.1883  -0.1405 0.0096  138 THR   A C   
892  O  O   . THR   A 118 ? 1.8424 1.8039 1.7766 0.1939  -0.1199 0.0239  138 THR   A O   
893  C  CB  . THR   A 118 ? 1.7302 1.7721 1.7395 0.2169  -0.2165 -0.0158 138 THR   A CB  
894  O  OG1 . THR   A 118 ? 1.7553 1.8294 1.8191 0.2353  -0.2279 -0.0203 138 THR   A OG1 
895  C  CG2 . THR   A 118 ? 1.6931 1.6604 1.5931 0.2458  -0.2230 -0.0046 138 THR   A CG2 
896  N  N   . SER   A 119 ? 2.0746 2.1413 2.1516 0.1876  -0.1382 0.0040  139 SER   A N   
897  C  CA  . SER   A 119 ? 2.0935 2.1411 2.1621 0.1986  -0.1167 0.0132  139 SER   A CA  
898  C  C   . SER   A 119 ? 2.0978 2.0932 2.1031 0.2374  -0.1345 0.0200  139 SER   A C   
899  O  O   . SER   A 119 ? 2.1236 2.0713 2.0848 0.2449  -0.1111 0.0326  139 SER   A O   
900  C  CB  . SER   A 119 ? 2.0441 2.1524 2.2008 0.1972  -0.1142 0.0044  139 SER   A CB  
901  O  OG  . SER   A 119 ? 2.0465 2.1941 2.2526 0.2188  -0.1526 -0.0093 139 SER   A OG  
902  N  N   . GLY   A 120 ? 1.8855 1.8854 1.8832 0.2636  -0.1768 0.0111  140 GLY   A N   
903  C  CA  . GLY   A 120 ? 1.8630 1.8062 1.7876 0.3054  -0.1965 0.0187  140 GLY   A CA  
904  C  C   . GLY   A 120 ? 1.8801 1.7418 1.7010 0.3044  -0.1713 0.0377  140 GLY   A C   
905  O  O   . GLY   A 120 ? 1.9209 1.7242 1.6860 0.3221  -0.1536 0.0531  140 GLY   A O   
906  N  N   . LYS   A 121 ? 1.8363 1.6916 1.6326 0.2835  -0.1668 0.0368  141 LYS   A N   
907  C  CA  . LYS   A 121 ? 1.8700 1.6540 1.5787 0.2777  -0.1354 0.0545  141 LYS   A CA  
908  C  C   . LYS   A 121 ? 1.8780 1.6521 1.6015 0.2469  -0.0866 0.0647  141 LYS   A C   
909  O  O   . LYS   A 121 ? 1.8936 1.6033 1.5579 0.2523  -0.0583 0.0810  141 LYS   A O   
910  C  CB  . LYS   A 121 ? 1.7831 1.5699 1.4714 0.2626  -0.1413 0.0488  141 LYS   A CB  
911  C  CG  . LYS   A 121 ? 1.7778 1.5191 1.3846 0.2989  -0.1731 0.0485  141 LYS   A CG  
912  C  CD  . LYS   A 121 ? 1.7465 1.5221 1.3847 0.3322  -0.2283 0.0313  141 LYS   A CD  
913  C  CE  . LYS   A 121 ? 1.7189 1.4623 1.2857 0.3639  -0.2680 0.0233  141 LYS   A CE  
914  N  NZ  . LYS   A 121 ? 1.6510 1.4120 1.2250 0.3362  -0.2660 0.0129  141 LYS   A NZ  
915  N  N   . LEU   A 122 ? 1.8045 1.6396 1.6062 0.2150  -0.0762 0.0545  142 LEU   A N   
916  C  CA  . LEU   A 122 ? 1.7617 1.5933 1.5812 0.1872  -0.0360 0.0594  142 LEU   A CA  
917  C  C   . LEU   A 122 ? 1.7413 1.5403 1.5488 0.2047  -0.0235 0.0667  142 LEU   A C   
918  O  O   . LEU   A 122 ? 1.7584 1.5186 1.5438 0.1906  0.0101  0.0744  142 LEU   A O   
919  C  CB  . LEU   A 122 ? 1.7012 1.6039 1.6020 0.1594  -0.0338 0.0466  142 LEU   A CB  
920  C  CG  . LEU   A 122 ? 1.6086 1.5241 1.5423 0.1371  -0.0028 0.0456  142 LEU   A CG  
921  C  CD1 . LEU   A 122 ? 1.5535 1.4327 1.4527 0.1137  0.0279  0.0515  142 LEU   A CD1 
922  C  CD2 . LEU   A 122 ? 1.5211 1.5045 1.5269 0.1196  -0.0068 0.0345  142 LEU   A CD2 
923  N  N   . LYS   A 123 ? 1.7656 1.5797 1.5912 0.2355  -0.0506 0.0626  143 LYS   A N   
924  C  CA  . LYS   A 123 ? 1.7802 1.5584 1.5899 0.2570  -0.0404 0.0696  143 LYS   A CA  
925  C  C   . LYS   A 123 ? 1.8920 1.5806 1.6079 0.2778  -0.0295 0.0878  143 LYS   A C   
926  O  O   . LYS   A 123 ? 1.9064 1.5461 1.5975 0.2809  -0.0035 0.0971  143 LYS   A O   
927  C  CB  . LYS   A 123 ? 1.7136 1.5341 1.5705 0.2878  -0.0735 0.0597  143 LYS   A CB  
928  C  CG  . LYS   A 123 ? 1.7136 1.4971 1.5539 0.3162  -0.0668 0.0661  143 LYS   A CG  
929  C  CD  . LYS   A 123 ? 1.6294 1.4780 1.5499 0.3315  -0.0845 0.0521  143 LYS   A CD  
930  C  CE  . LYS   A 123 ? 1.6092 1.5095 1.5679 0.3507  -0.1302 0.0397  143 LYS   A CE  
931  N  NZ  . LYS   A 123 ? 1.5154 1.4795 1.5596 0.3676  -0.1451 0.0260  143 LYS   A NZ  
932  N  N   . GLU   A 124 ? 1.8612 1.5227 1.5210 0.2926  -0.0469 0.0932  144 GLU   A N   
933  C  CA  . GLU   A 124 ? 1.9603 1.5300 1.5221 0.3129  -0.0307 0.1134  144 GLU   A CA  
934  C  C   . GLU   A 124 ? 1.9517 1.4821 1.4903 0.2774  0.0184  0.1237  144 GLU   A C   
935  O  O   . GLU   A 124 ? 1.9919 1.4433 1.4653 0.2866  0.0465  0.1417  144 GLU   A O   
936  C  CB  . GLU   A 124 ? 2.0808 1.6311 1.5823 0.3425  -0.0642 0.1149  144 GLU   A CB  
937  C  CG  . GLU   A 124 ? 2.0809 1.6814 1.6192 0.3751  -0.1191 0.0988  144 GLU   A CG  
938  C  CD  . GLU   A 124 ? 2.1548 1.7154 1.6136 0.4169  -0.1561 0.1010  144 GLU   A CD  
939  O  OE1 . GLU   A 124 ? 2.2383 1.7352 1.6115 0.4183  -0.1369 0.1153  144 GLU   A OE1 
940  O  OE2 . GLU   A 124 ? 2.1690 1.7620 1.6513 0.4501  -0.2046 0.0871  144 GLU   A OE2 
941  N  N   . MET   A 125 ? 2.0217 1.6046 1.6150 0.2377  0.0300  0.1125  145 MET   A N   
942  C  CA  . MET   A 125 ? 1.9736 1.5312 1.5619 0.2027  0.0739  0.1178  145 MET   A CA  
943  C  C   . MET   A 125 ? 1.9599 1.5037 1.5766 0.1882  0.1013  0.1168  145 MET   A C   
944  O  O   . MET   A 125 ? 1.9818 1.4950 1.5934 0.1622  0.1378  0.1204  145 MET   A O   
945  C  CB  . MET   A 125 ? 1.9048 1.5251 1.5443 0.1690  0.0733  0.1043  145 MET   A CB  
946  C  CG  . MET   A 125 ? 1.8726 1.5226 1.5045 0.1805  0.0396  0.0984  145 MET   A CG  
947  S  SD  . MET   A 125 ? 1.8424 1.4956 1.4629 0.1518  0.0591  0.0975  145 MET   A SD  
948  C  CE  . MET   A 125 ? 2.0663 1.6197 1.5845 0.1695  0.0907  0.1205  145 MET   A CE  
949  N  N   . VAL   A 126 ? 1.9817 1.5480 1.6310 0.2048  0.0845  0.1101  146 VAL   A N   
950  C  CA  . VAL   A 126 ? 1.9718 1.5314 1.6525 0.1908  0.1074  0.1046  146 VAL   A CA  
951  C  C   . VAL   A 126 ? 2.0074 1.4792 1.6352 0.1903  0.1427  0.1190  146 VAL   A C   
952  O  O   . VAL   A 126 ? 2.0176 1.4813 1.6686 0.1580  0.1724  0.1130  146 VAL   A O   
953  C  CB  . VAL   A 126 ? 1.9625 1.5555 1.6793 0.2156  0.0840  0.0963  146 VAL   A CB  
954  C  CG1 . VAL   A 126 ? 1.9808 1.5356 1.6995 0.2152  0.1077  0.0951  146 VAL   A CG1 
955  C  CG2 . VAL   A 126 ? 1.9290 1.6112 1.7189 0.2003  0.0666  0.0793  146 VAL   A CG2 
956  N  N   . PRO   A 127 ? 2.0522 1.4548 1.6110 0.2247  0.1418  0.1373  147 PRO   A N   
957  C  CA  . PRO   A 127 ? 2.0745 1.3872 1.5852 0.2218  0.1816  0.1526  147 PRO   A CA  
958  C  C   . PRO   A 127 ? 2.1261 1.4137 1.6247 0.1878  0.2183  0.1583  147 PRO   A C   
959  O  O   . PRO   A 127 ? 2.1740 1.4186 1.6791 0.1645  0.2559  0.1596  147 PRO   A O   
960  C  CB  . PRO   A 127 ? 2.0787 1.3246 1.5078 0.2711  0.1684  0.1733  147 PRO   A CB  
961  C  CG  . PRO   A 127 ? 2.0448 1.3555 1.5025 0.3001  0.1182  0.1619  147 PRO   A CG  
962  C  CD  . PRO   A 127 ? 2.0389 1.4379 1.5601 0.2695  0.1044  0.1441  147 PRO   A CD  
963  N  N   . ILE   A 128 ? 2.1291 1.4433 1.6152 0.1838  0.2088  0.1599  148 ILE   A N   
964  C  CA  . ILE   A 128 ? 2.1429 1.4341 1.6178 0.1546  0.2456  0.1657  148 ILE   A CA  
965  C  C   . ILE   A 128 ? 2.1771 1.5251 1.7355 0.1093  0.2591  0.1444  148 ILE   A C   
966  O  O   . ILE   A 128 ? 2.1993 1.5165 1.7705 0.0814  0.2979  0.1447  148 ILE   A O   
967  C  CB  . ILE   A 128 ? 2.0523 1.3547 1.4867 0.1666  0.2302  0.1717  148 ILE   A CB  
968  C  CG1 . ILE   A 128 ? 2.0673 1.3026 1.4070 0.2150  0.2169  0.1923  148 ILE   A CG1 
969  C  CG2 . ILE   A 128 ? 2.0855 1.3733 1.5181 0.1356  0.2702  0.1755  148 ILE   A CG2 
970  C  CD1 . ILE   A 128 ? 2.0963 1.3752 1.4425 0.2494  0.1610  0.1831  148 ILE   A CD1 
971  N  N   . ILE   A 129 ? 2.2546 1.6851 1.8715 0.1024  0.2274  0.1251  149 ILE   A N   
972  C  CA  . ILE   A 129 ? 2.1553 1.6387 1.8444 0.0660  0.2346  0.1041  149 ILE   A CA  
973  C  C   . ILE   A 129 ? 2.1479 1.6032 1.8587 0.0572  0.2519  0.0963  149 ILE   A C   
974  O  O   . ILE   A 129 ? 2.1236 1.5974 1.8819 0.0259  0.2670  0.0798  149 ILE   A O   
975  C  CB  . ILE   A 129 ? 2.0932 1.6616 1.8290 0.0665  0.1983  0.0888  149 ILE   A CB  
976  C  CG1 . ILE   A 129 ? 2.1035 1.6947 1.8192 0.0736  0.1810  0.0943  149 ILE   A CG1 
977  C  CG2 . ILE   A 129 ? 2.0119 1.6310 1.8114 0.0342  0.2035  0.0682  149 ILE   A CG2 
978  C  CD1 . ILE   A 129 ? 2.0799 1.7492 1.8434 0.0715  0.1490  0.0805  149 ILE   A CD1 
979  N  N   . ALA   A 130 ? 2.0584 1.4667 1.7342 0.0860  0.2486  0.1063  150 ALA   A N   
980  C  CA  . ALA   A 130 ? 2.0848 1.4567 1.7745 0.0812  0.2652  0.0991  150 ALA   A CA  
981  C  C   . ALA   A 130 ? 2.1277 1.4168 1.7898 0.0667  0.3084  0.1106  150 ALA   A C   
982  O  O   . ALA   A 130 ? 2.1258 1.3820 1.8069 0.0553  0.3259  0.1012  150 ALA   A O   
983  C  CB  . ALA   A 130 ? 2.1046 1.4605 1.7712 0.1204  0.2440  0.1045  150 ALA   A CB  
984  N  N   . GLN   A 131 ? 2.1472 1.3991 1.7650 0.0672  0.3280  0.1300  151 GLN   A N   
985  C  CA  . GLN   A 131 ? 2.1716 1.3437 1.7669 0.0510  0.3764  0.1428  151 GLN   A CA  
986  C  C   . GLN   A 131 ? 2.1617 1.3660 1.8274 0.0032  0.4000  0.1227  151 GLN   A C   
987  O  O   . GLN   A 131 ? 2.1884 1.3489 1.8781 -0.0195 0.4323  0.1171  151 GLN   A O   
988  C  CB  . GLN   A 131 ? 2.2155 1.3308 1.7302 0.0725  0.3927  0.1724  151 GLN   A CB  
989  C  CG  . GLN   A 131 ? 2.2459 1.2788 1.7376 0.0536  0.4507  0.1886  151 GLN   A CG  
990  C  CD  . GLN   A 131 ? 2.2833 1.2615 1.6893 0.0758  0.4699  0.2179  151 GLN   A CD  
991  O  OE1 . GLN   A 131 ? 2.3473 1.2662 1.7343 0.0595  0.5211  0.2328  151 GLN   A OE1 
992  N  NE2 . GLN   A 131 ? 2.2295 1.2267 1.5838 0.1137  0.4295  0.2254  151 GLN   A NE2 
993  N  N   . TYR   A 132 ? 2.0716 1.3516 1.7741 -0.0117 0.3831  0.1104  152 TYR   A N   
994  C  CA  . TYR   A 132 ? 2.0485 1.3682 1.8207 -0.0530 0.3993  0.0895  152 TYR   A CA  
995  C  C   . TYR   A 132 ? 1.9996 1.3799 1.8384 -0.0682 0.3738  0.0580  152 TYR   A C   
996  O  O   . TYR   A 132 ? 1.9680 1.3830 1.8681 -0.1001 0.3811  0.0361  152 TYR   A O   
997  C  CB  . TYR   A 132 ? 2.0029 1.3676 1.7762 -0.0588 0.3958  0.0927  152 TYR   A CB  
998  C  CG  . TYR   A 132 ? 2.0567 1.3617 1.7505 -0.0362 0.4153  0.1232  152 TYR   A CG  
999  C  CD1 . TYR   A 132 ? 2.0944 1.3348 1.7694 -0.0497 0.4665  0.1381  152 TYR   A CD1 
1000 C  CD2 . TYR   A 132 ? 2.0505 1.3610 1.6870 -0.0001 0.3831  0.1363  152 TYR   A CD2 
1001 C  CE1 . TYR   A 132 ? 2.1389 1.3175 1.7293 -0.0251 0.4865  0.1674  152 TYR   A CE1 
1002 C  CE2 . TYR   A 132 ? 2.1089 1.3612 1.6640 0.0248  0.3969  0.1621  152 TYR   A CE2 
1003 C  CZ  . TYR   A 132 ? 2.1684 1.3524 1.6949 0.0137  0.4493  0.1788  152 TYR   A CZ  
1004 O  OH  . TYR   A 132 ? 2.1834 1.3034 1.6175 0.0424  0.4649  0.2058  152 TYR   A OH  
1005 N  N   . GLY   A 133 ? 2.0997 1.4939 1.9271 -0.0439 0.3438  0.0546  153 GLY   A N   
1006 C  CA  . GLY   A 133 ? 2.0133 1.4397 1.8893 -0.0544 0.3287  0.0271  153 GLY   A CA  
1007 C  C   . GLY   A 133 ? 2.0458 1.4077 1.9306 -0.0665 0.3549  0.0195  153 GLY   A C   
1008 O  O   . GLY   A 133 ? 1.9908 1.3724 1.9248 -0.0865 0.3508  -0.0088 153 GLY   A O   
1009 N  N   . ASP   A 134 ? 2.0450 1.3252 1.8795 -0.0535 0.3816  0.0439  154 ASP   A N   
1010 C  CA  . ASP   A 134 ? 2.0877 1.2950 1.9292 -0.0674 0.4130  0.0396  154 ASP   A CA  
1011 C  C   . ASP   A 134 ? 2.1299 1.3211 2.0130 -0.1075 0.4509  0.0338  154 ASP   A C   
1012 O  O   . ASP   A 134 ? 2.1467 1.3106 2.0742 -0.1333 0.4693  0.0140  154 ASP   A O   
1013 C  CB  . ASP   A 134 ? 2.1373 1.2569 1.9036 -0.0343 0.4282  0.0703  154 ASP   A CB  
1014 C  CG  . ASP   A 134 ? 2.1441 1.2821 1.8782 0.0069  0.3907  0.0741  154 ASP   A CG  
1015 O  OD1 . ASP   A 134 ? 2.0499 1.2604 1.8235 0.0063  0.3594  0.0517  154 ASP   A OD1 
1016 O  OD2 . ASP   A 134 ? 2.2391 1.3187 1.9082 0.0414  0.3934  0.0998  154 ASP   A OD2 
1017 N  N   . VAL   A 135 ? 2.2292 1.4368 2.1023 -0.1131 0.4634  0.0492  155 VAL   A N   
1018 C  CA  . VAL   A 135 ? 2.2666 1.4746 2.1920 -0.1518 0.4988  0.0408  155 VAL   A CA  
1019 C  C   . VAL   A 135 ? 2.1989 1.4929 2.2097 -0.1794 0.4738  0.0019  155 VAL   A C   
1020 O  O   . VAL   A 135 ? 2.2015 1.4993 2.2795 -0.2148 0.4955  -0.0188 155 VAL   A O   
1021 C  CB  . VAL   A 135 ? 2.3033 1.5037 2.1882 -0.1457 0.5201  0.0682  155 VAL   A CB  
1022 C  CG1 . VAL   A 135 ? 2.3010 1.4881 2.2382 -0.1840 0.5676  0.0637  155 VAL   A CG1 
1023 C  CG2 . VAL   A 135 ? 2.2972 1.4173 2.0821 -0.1080 0.5326  0.1061  155 VAL   A CG2 
1024 N  N   . LEU   A 136 ? 2.0615 1.4241 2.0721 -0.1628 0.4282  -0.0091 156 LEU   A N   
1025 C  CA  . LEU   A 136 ? 1.9458 1.3859 2.0243 -0.1824 0.4014  -0.0442 156 LEU   A CA  
1026 C  C   . LEU   A 136 ? 1.9847 1.4106 2.1065 -0.1979 0.3975  -0.0755 156 LEU   A C   
1027 O  O   . LEU   A 136 ? 2.0229 1.4795 2.2136 -0.2272 0.3973  -0.1058 156 LEU   A O   
1028 C  CB  . LEU   A 136 ? 1.7872 1.2919 1.8453 -0.1579 0.3585  -0.0441 156 LEU   A CB  
1029 C  CG  . LEU   A 136 ? 1.6597 1.2425 1.7703 -0.1696 0.3277  -0.0753 156 LEU   A CG  
1030 C  CD1 . LEU   A 136 ? 1.6458 1.2613 1.8108 -0.1985 0.3404  -0.0875 156 LEU   A CD1 
1031 C  CD2 . LEU   A 136 ? 1.5658 1.1995 1.6476 -0.1441 0.2945  -0.0670 156 LEU   A CD2 
1032 N  N   . VAL   A 137 ? 2.0767 1.4560 2.1604 -0.1772 0.3930  -0.0709 157 VAL   A N   
1033 C  CA  . VAL   A 137 ? 2.0751 1.4315 2.1939 -0.1902 0.3905  -0.1016 157 VAL   A CA  
1034 C  C   . VAL   A 137 ? 2.2275 1.5236 2.3840 -0.2226 0.4332  -0.1060 157 VAL   A C   
1035 O  O   . VAL   A 137 ? 2.2570 1.5519 2.4722 -0.2474 0.4317  -0.1410 157 VAL   A O   
1036 C  CB  . VAL   A 137 ? 2.0444 1.3629 2.1112 -0.1572 0.3776  -0.0947 157 VAL   A CB  
1037 C  CG1 . VAL   A 137 ? 1.9558 1.3271 1.9838 -0.1242 0.3455  -0.0809 157 VAL   A CG1 
1038 C  CG2 . VAL   A 137 ? 2.1021 1.3252 2.1221 -0.1469 0.4128  -0.0656 157 VAL   A CG2 
1039 N  N   . ARG   A 138 ? 2.3468 1.5905 2.4708 -0.2228 0.4724  -0.0719 158 ARG   A N   
1040 C  CA  . ARG   A 138 ? 2.3653 1.5444 2.5234 -0.2538 0.5213  -0.0715 158 ARG   A CA  
1041 C  C   . ARG   A 138 ? 2.3907 1.6246 2.6425 -0.2947 0.5292  -0.1001 158 ARG   A C   
1042 O  O   . ARG   A 138 ? 2.3829 1.5875 2.6988 -0.3278 0.5543  -0.1217 158 ARG   A O   
1043 C  CB  . ARG   A 138 ? 2.4447 1.5509 2.5328 -0.2390 0.5635  -0.0245 158 ARG   A CB  
1044 C  CG  . ARG   A 138 ? 2.5327 1.5399 2.5570 -0.2164 0.5817  -0.0030 158 ARG   A CG  
1045 C  CD  . ARG   A 138 ? 2.5976 1.5493 2.6782 -0.2490 0.6105  -0.0255 158 ARG   A CD  
1046 N  NE  . ARG   A 138 ? 2.7330 1.5774 2.7500 -0.2298 0.6401  0.0013  158 ARG   A NE  
1047 C  CZ  . ARG   A 138 ? 2.7627 1.5703 2.8112 -0.2454 0.6575  -0.0122 158 ARG   A CZ  
1048 N  NH1 . ARG   A 138 ? 2.7113 1.5645 2.8558 -0.2834 0.6524  -0.0531 158 ARG   A NH1 
1049 N  NH2 . ARG   A 138 ? 2.8037 1.5270 2.7854 -0.2207 0.6784  0.0153  158 ARG   A NH2 
1050 N  N   . ASN   A 139 ? 2.3381 1.6515 2.6038 -0.2930 0.5077  -0.1024 159 ASN   A N   
1051 C  CA  . ASN   A 139 ? 2.3880 1.7598 2.7434 -0.3272 0.5120  -0.1295 159 ASN   A CA  
1052 C  C   . ASN   A 139 ? 2.3924 1.8362 2.8071 -0.3350 0.4634  -0.1761 159 ASN   A C   
1053 O  O   . ASN   A 139 ? 2.3995 1.8678 2.9026 -0.3675 0.4664  -0.2109 159 ASN   A O   
1054 C  CB  . ASN   A 139 ? 2.2941 1.7088 2.6324 -0.3202 0.5175  -0.1072 159 ASN   A CB  
1055 C  CG  . ASN   A 139 ? 2.3383 1.7115 2.6943 -0.3418 0.5770  -0.0876 159 ASN   A CG  
1056 O  OD1 . ASN   A 139 ? 2.3612 1.7073 2.7705 -0.3661 0.6050  -0.1009 159 ASN   A OD1 
1057 N  ND2 . ASN   A 139 ? 2.2741 1.6514 2.5801 -0.3258 0.5906  -0.0567 159 ASN   A ND2 
1058 N  N   . LEU   A 140 ? 2.1701 1.6483 2.5388 -0.3049 0.4189  -0.1781 160 LEU   A N   
1059 C  CA  . LEU   A 140 ? 2.0445 1.5792 2.4517 -0.3059 0.3732  -0.2204 160 LEU   A CA  
1060 C  C   . LEU   A 140 ? 2.0327 1.5320 2.4887 -0.3267 0.3741  -0.2569 160 LEU   A C   
1061 O  O   . LEU   A 140 ? 1.9929 1.5393 2.5067 -0.3394 0.3441  -0.2993 160 LEU   A O   
1062 C  CB  . LEU   A 140 ? 1.9387 1.4954 2.2779 -0.2680 0.3362  -0.2110 160 LEU   A CB  
1063 C  CG  . LEU   A 140 ? 1.7824 1.4204 2.1204 -0.2558 0.3028  -0.2140 160 LEU   A CG  
1064 C  CD1 . LEU   A 140 ? 1.5832 1.2342 1.8631 -0.2219 0.2719  -0.2088 160 LEU   A CD1 
1065 C  CD2 . LEU   A 140 ? 1.6466 1.3414 2.0607 -0.2777 0.2813  -0.2560 160 LEU   A CD2 
1066 N  N   . ARG   A 141 ? 2.0936 1.5086 2.5273 -0.3297 0.4075  -0.2423 161 ARG   A N   
1067 C  CA  . ARG   A 141 ? 2.1015 1.4722 2.5798 -0.3502 0.4117  -0.2761 161 ARG   A CA  
1068 C  C   . ARG   A 141 ? 2.0996 1.4737 2.6809 -0.3966 0.4386  -0.3017 161 ARG   A C   
1069 O  O   . ARG   A 141 ? 2.0789 1.4871 2.7258 -0.4120 0.4113  -0.3470 161 ARG   A O   
1070 C  CB  . ARG   A 141 ? 2.1182 1.3944 2.5327 -0.3343 0.4392  -0.2484 161 ARG   A CB  
1071 C  CG  . ARG   A 141 ? 2.0717 1.3264 2.4491 -0.3103 0.4087  -0.2666 161 ARG   A CG  
1072 C  CD  . ARG   A 141 ? 2.1230 1.2756 2.4657 -0.3071 0.4457  -0.2460 161 ARG   A CD  
1073 N  NE  . ARG   A 141 ? 2.0736 1.1993 2.3349 -0.2644 0.4291  -0.2284 161 ARG   A NE  
1074 C  CZ  . ARG   A 141 ? 2.0354 1.1634 2.2262 -0.2311 0.4295  -0.1870 161 ARG   A CZ  
1075 N  NH1 . ARG   A 141 ? 2.0463 1.1969 2.2280 -0.2339 0.4451  -0.1576 161 ARG   A NH1 
1076 N  NH2 . ARG   A 141 ? 1.9090 1.0172 2.0393 -0.1932 0.4127  -0.1770 161 ARG   A NH2 
1077 N  N   . ARG   A 142 ? 2.1422 1.4973 2.7247 -0.4058 0.4840  -0.2674 162 ARG   A N   
1078 C  CA  . ARG   A 142 ? 2.1502 1.5358 2.8133 -0.4317 0.5039  -0.2797 162 ARG   A CA  
1079 C  C   . ARG   A 142 ? 2.0777 1.5586 2.8254 -0.4456 0.4630  -0.3250 162 ARG   A C   
1080 O  O   . ARG   A 142 ? 2.0348 1.5409 2.8617 -0.4664 0.4655  -0.3510 162 ARG   A O   
1081 C  CB  . ARG   A 142 ? 2.1840 1.5545 2.8227 -0.4304 0.5515  -0.2361 162 ARG   A CB  
1082 C  CG  . ARG   A 142 ? 2.2806 1.5546 2.8241 -0.4101 0.5879  -0.1898 162 ARG   A CG  
1083 C  CD  . ARG   A 142 ? 2.3376 1.5653 2.8816 -0.4178 0.6426  -0.1641 162 ARG   A CD  
1084 N  NE  . ARG   A 142 ? 2.4038 1.5410 2.8454 -0.3919 0.6727  -0.1184 162 ARG   A NE  
1085 C  CZ  . ARG   A 142 ? 2.4296 1.5477 2.7941 -0.3686 0.6886  -0.0783 162 ARG   A CZ  
1086 N  NH1 . ARG   A 142 ? 2.3778 1.5595 2.7516 -0.3679 0.6763  -0.0772 162 ARG   A NH1 
1087 N  NH2 . ARG   A 142 ? 2.4948 1.5273 2.7686 -0.3433 0.7160  -0.0391 162 ARG   A NH2 
1088 N  N   . GLU   A 143 ? 2.0256 1.5578 2.7570 -0.4327 0.4240  -0.3361 163 GLU   A N   
1089 C  CA  . GLU   A 143 ? 1.9705 1.5870 2.7650 -0.4374 0.3747  -0.3820 163 GLU   A CA  
1090 C  C   . GLU   A 143 ? 1.9711 1.5814 2.7584 -0.4290 0.3298  -0.4221 163 GLU   A C   
1091 O  O   . GLU   A 143 ? 1.9985 1.6617 2.8443 -0.4346 0.2918  -0.4653 163 GLU   A O   
1092 C  CB  . GLU   A 143 ? 1.9008 1.5747 2.6759 -0.4254 0.3566  -0.3724 163 GLU   A CB  
1093 C  CG  . GLU   A 143 ? 1.8345 1.6013 2.6816 -0.4304 0.3214  -0.4061 163 GLU   A CG  
1094 C  CD  . GLU   A 143 ? 1.8538 1.6581 2.7065 -0.4302 0.3432  -0.3782 163 GLU   A CD  
1095 O  OE1 . GLU   A 143 ? 1.8360 1.6042 2.6207 -0.4198 0.3719  -0.3349 163 GLU   A OE1 
1096 O  OE2 . GLU   A 143 ? 1.7866 1.6550 2.7077 -0.4367 0.3303  -0.3993 163 GLU   A OE2 
1097 N  N   . ALA   A 144 ? 2.0489 1.5968 2.7591 -0.4101 0.3314  -0.4078 164 ALA   A N   
1098 C  CA  . ALA   A 144 ? 2.0112 1.5524 2.6974 -0.3928 0.2894  -0.4414 164 ALA   A CA  
1099 C  C   . ALA   A 144 ? 2.0305 1.5209 2.7563 -0.4114 0.2980  -0.4674 164 ALA   A C   
1100 O  O   . ALA   A 144 ? 2.0424 1.5577 2.7978 -0.4109 0.2571  -0.5129 164 ALA   A O   
1101 C  CB  . ALA   A 144 ? 1.9094 1.4220 2.4850 -0.3510 0.2835  -0.4059 164 ALA   A CB  
1102 N  N   . GLU   A 145 ? 2.1184 1.5412 2.8323 -0.4204 0.3466  -0.4343 165 GLU   A N   
1103 C  CA  . GLU   A 145 ? 2.1244 1.5078 2.8770 -0.4366 0.3562  -0.4525 165 GLU   A CA  
1104 C  C   . GLU   A 145 ? 2.0155 1.4618 2.8703 -0.4632 0.3465  -0.4840 165 GLU   A C   
1105 O  O   . GLU   A 145 ? 2.1124 1.5427 3.0133 -0.4777 0.3408  -0.5125 165 GLU   A O   
1106 C  CB  . GLU   A 145 ? 2.1907 1.4897 2.9067 -0.4392 0.4138  -0.4068 165 GLU   A CB  
1107 C  CG  . GLU   A 145 ? 2.2787 1.4996 2.8991 -0.4107 0.4209  -0.3825 165 GLU   A CG  
1108 C  CD  . GLU   A 145 ? 2.3200 1.4693 2.8875 -0.4044 0.4756  -0.3271 165 GLU   A CD  
1109 O  OE1 . GLU   A 145 ? 2.4411 1.6088 3.0306 -0.4176 0.5072  -0.3028 165 GLU   A OE1 
1110 O  OE2 . GLU   A 145 ? 2.3116 1.3853 2.8108 -0.3827 0.4862  -0.3080 165 GLU   A OE2 
1111 N  N   . THR   A 146 ? 2.0276 1.5441 2.9195 -0.4684 0.3446  -0.4799 166 THR   A N   
1112 C  CA  . THR   A 146 ? 1.9712 1.5567 2.9617 -0.4884 0.3329  -0.5100 166 THR   A CA  
1113 C  C   . THR   A 146 ? 1.9669 1.6340 2.9679 -0.4739 0.2762  -0.5406 166 THR   A C   
1114 O  O   . THR   A 146 ? 1.9491 1.6677 2.9585 -0.4706 0.2780  -0.5264 166 THR   A O   
1115 C  CB  . THR   A 146 ? 1.9725 1.5650 2.9953 -0.5033 0.3854  -0.4762 166 THR   A CB  
1116 O  OG1 . THR   A 146 ? 1.9614 1.5759 2.9342 -0.4878 0.3912  -0.4443 166 THR   A OG1 
1117 C  CG2 . THR   A 146 ? 2.0005 1.5052 2.9981 -0.5126 0.4425  -0.4428 166 THR   A CG2 
1118 N  N   . GLY   A 147 ? 1.9613 1.6370 2.9576 -0.4632 0.2257  -0.5827 167 GLY   A N   
1119 C  CA  . GLY   A 147 ? 2.0125 1.7492 2.9924 -0.4411 0.1682  -0.6115 167 GLY   A CA  
1120 C  C   . GLY   A 147 ? 1.9339 1.7557 2.9621 -0.4409 0.1522  -0.6164 167 GLY   A C   
1121 O  O   . GLY   A 147 ? 1.9025 1.7814 2.9813 -0.4377 0.1093  -0.6563 167 GLY   A O   
1122 N  N   . LYS   A 148 ? 1.8880 1.7171 2.8971 -0.4414 0.1854  -0.5758 168 LYS   A N   
1123 C  CA  . LYS   A 148 ? 1.8510 1.7562 2.8921 -0.4368 0.1715  -0.5756 168 LYS   A CA  
1124 C  C   . LYS   A 148 ? 1.8738 1.7913 2.8395 -0.4132 0.1528  -0.5600 168 LYS   A C   
1125 O  O   . LYS   A 148 ? 1.8585 1.7216 2.7569 -0.4086 0.1796  -0.5276 168 LYS   A O   
1126 C  CB  . LYS   A 148 ? 1.8758 1.7852 2.9570 -0.4549 0.2252  -0.5423 168 LYS   A CB  
1127 C  CG  . LYS   A 148 ? 1.8673 1.7699 3.0298 -0.4794 0.2528  -0.5538 168 LYS   A CG  
1128 C  CD  . LYS   A 148 ? 1.8963 1.8384 3.1073 -0.4880 0.2853  -0.5354 168 LYS   A CD  
1129 C  CE  . LYS   A 148 ? 1.8833 1.7808 3.1343 -0.5116 0.3441  -0.5189 168 LYS   A CE  
1130 N  NZ  . LYS   A 148 ? 1.8226 1.7537 3.1253 -0.5199 0.3797  -0.5050 168 LYS   A NZ  
1131 N  N   . PRO   A 149 ? 1.8519 1.8383 2.8272 -0.3972 0.1094  -0.5804 169 PRO   A N   
1132 C  CA  . PRO   A 149 ? 1.8239 1.8253 2.7281 -0.3743 0.0952  -0.5614 169 PRO   A CA  
1133 C  C   . PRO   A 149 ? 1.8546 1.8445 2.7317 -0.3773 0.1441  -0.5056 169 PRO   A C   
1134 O  O   . PRO   A 149 ? 1.8857 1.8763 2.8252 -0.4034 0.1828  -0.4966 169 PRO   A O   
1135 C  CB  . PRO   A 149 ? 1.7665 1.8464 2.7023 -0.3592 0.0437  -0.5941 169 PRO   A CB  
1136 C  CG  . PRO   A 149 ? 1.7533 1.8439 2.7433 -0.3625 0.0152  -0.6367 169 PRO   A CG  
1137 C  CD  . PRO   A 149 ? 1.7715 1.8188 2.8104 -0.3929 0.0643  -0.6245 169 PRO   A CD  
1138 N  N   . VAL   A 150 ? 1.7341 1.7132 2.5114 -0.3459 0.1420  -0.4661 170 VAL   A N   
1139 C  CA  . VAL   A 150 ? 1.6920 1.6462 2.4238 -0.3432 0.1844  -0.4128 170 VAL   A CA  
1140 C  C   . VAL   A 150 ? 1.6251 1.6319 2.3231 -0.3205 0.1668  -0.3933 170 VAL   A C   
1141 O  O   . VAL   A 150 ? 1.5868 1.6162 2.2341 -0.2924 0.1290  -0.3973 170 VAL   A O   
1142 C  CB  . VAL   A 150 ? 1.6773 1.5637 2.3235 -0.3270 0.2013  -0.3814 170 VAL   A CB  
1143 C  CG1 . VAL   A 150 ? 1.6657 1.5219 2.2703 -0.3251 0.2440  -0.3305 170 VAL   A CG1 
1144 C  CG2 . VAL   A 150 ? 1.7369 1.5681 2.4107 -0.3454 0.2128  -0.4045 170 VAL   A CG2 
1145 N  N   . THR   A 151 ? 1.5944 1.6158 2.3173 -0.3319 0.1971  -0.3713 171 THR   A N   
1146 C  CA  . THR   A 151 ? 1.5240 1.5833 2.2084 -0.3110 0.1877  -0.3470 171 THR   A CA  
1147 C  C   . THR   A 151 ? 1.4838 1.4993 2.0754 -0.2919 0.2062  -0.3003 171 THR   A C   
1148 O  O   . THR   A 151 ? 1.4659 1.4354 2.0441 -0.3020 0.2475  -0.2736 171 THR   A O   
1149 C  CB  . THR   A 151 ? 1.5153 1.6084 2.2652 -0.3292 0.2120  -0.3458 171 THR   A CB  
1150 O  OG1 . THR   A 151 ? 1.5593 1.6024 2.3209 -0.3511 0.2668  -0.3236 171 THR   A OG1 
1151 C  CG2 . THR   A 151 ? 1.4996 1.6476 2.3497 -0.3448 0.1873  -0.3950 171 THR   A CG2 
1152 N  N   . LEU   A 152 ? 1.3305 1.3595 1.8585 -0.2630 0.1759  -0.2910 172 LEU   A N   
1153 C  CA  . LEU   A 152 ? 1.3483 1.3412 1.7969 -0.2439 0.1878  -0.2521 172 LEU   A CA  
1154 C  C   . LEU   A 152 ? 1.3517 1.3486 1.7815 -0.2418 0.2099  -0.2193 172 LEU   A C   
1155 O  O   . LEU   A 152 ? 1.3272 1.2793 1.7176 -0.2396 0.2376  -0.1896 172 LEU   A O   
1156 C  CB  . LEU   A 152 ? 1.3398 1.3491 1.7355 -0.2155 0.1529  -0.2527 172 LEU   A CB  
1157 C  CG  . LEU   A 152 ? 1.2747 1.2718 1.6698 -0.2109 0.1312  -0.2828 172 LEU   A CG  
1158 C  CD1 . LEU   A 152 ? 1.2141 1.2236 1.5485 -0.1804 0.1053  -0.2766 172 LEU   A CD1 
1159 C  CD2 . LEU   A 152 ? 1.2685 1.2049 1.6584 -0.2211 0.1568  -0.2786 172 LEU   A CD2 
1160 N  N   . LYS   A 153 ? 1.3021 1.3498 1.7561 -0.2400 0.1968  -0.2251 173 LYS   A N   
1161 C  CA  . LYS   A 153 ? 1.2733 1.3251 1.7022 -0.2341 0.2134  -0.1959 173 LYS   A CA  
1162 C  C   . LYS   A 153 ? 1.2928 1.3059 1.7340 -0.2520 0.2594  -0.1798 173 LYS   A C   
1163 O  O   . LYS   A 153 ? 1.3131 1.3038 1.7073 -0.2427 0.2778  -0.1494 173 LYS   A O   
1164 C  CB  . LYS   A 153 ? 1.2735 1.3840 1.7349 -0.2305 0.1934  -0.2089 173 LYS   A CB  
1165 C  CG  . LYS   A 153 ? 1.2965 1.4307 1.8357 -0.2528 0.2129  -0.2267 173 LYS   A CG  
1166 C  CD  . LYS   A 153 ? 1.2977 1.4799 1.8507 -0.2433 0.2012  -0.2269 173 LYS   A CD  
1167 C  CE  . LYS   A 153 ? 1.2902 1.4936 1.9189 -0.2640 0.2292  -0.2389 173 LYS   A CE  
1168 N  NZ  . LYS   A 153 ? 1.3057 1.5266 1.9193 -0.2536 0.2390  -0.2209 173 LYS   A NZ  
1169 N  N   . ASP   A 154 ? 1.3328 1.3339 1.8345 -0.2767 0.2792  -0.2000 174 ASP   A N   
1170 C  CA  . ASP   A 154 ? 1.3299 1.2841 1.8403 -0.2942 0.3296  -0.1829 174 ASP   A CA  
1171 C  C   . ASP   A 154 ? 1.3495 1.2327 1.7948 -0.2858 0.3465  -0.1583 174 ASP   A C   
1172 O  O   . ASP   A 154 ? 1.3448 1.1883 1.7321 -0.2748 0.3707  -0.1249 174 ASP   A O   
1173 C  CB  . ASP   A 154 ? 1.3772 1.3435 1.9848 -0.3260 0.3474  -0.2143 174 ASP   A CB  
1174 C  CG  . ASP   A 154 ? 1.3934 1.4309 2.0718 -0.3329 0.3340  -0.2381 174 ASP   A CG  
1175 O  OD1 . ASP   A 154 ? 1.3603 1.4135 2.0209 -0.3242 0.3458  -0.2190 174 ASP   A OD1 
1176 O  OD2 . ASP   A 154 ? 1.4905 1.5676 2.2412 -0.3448 0.3092  -0.2775 174 ASP   A OD2 
1177 N  N   . VAL   A 155 ? 1.3908 1.2559 1.8421 -0.2880 0.3318  -0.1757 175 VAL   A N   
1178 C  CA  . VAL   A 155 ? 1.3803 1.1770 1.7742 -0.2784 0.3468  -0.1548 175 VAL   A CA  
1179 C  C   . VAL   A 155 ? 1.4406 1.2328 1.7524 -0.2459 0.3285  -0.1263 175 VAL   A C   
1180 O  O   . VAL   A 155 ? 1.4728 1.2097 1.7274 -0.2328 0.3463  -0.0990 175 VAL   A O   
1181 C  CB  . VAL   A 155 ? 1.3816 1.1635 1.8011 -0.2857 0.3315  -0.1836 175 VAL   A CB  
1182 C  CG1 . VAL   A 155 ? 1.4395 1.2372 1.9532 -0.3191 0.3422  -0.2186 175 VAL   A CG1 
1183 C  CG2 . VAL   A 155 ? 1.3747 1.1977 1.7721 -0.2639 0.2829  -0.1989 175 VAL   A CG2 
1184 N  N   . PHE   A 156 ? 1.3636 1.2120 1.6696 -0.2318 0.2930  -0.1326 176 PHE   A N   
1185 C  CA  . PHE   A 156 ? 1.3580 1.2078 1.5987 -0.2044 0.2772  -0.1073 176 PHE   A CA  
1186 C  C   . PHE   A 156 ? 1.4168 1.2642 1.6324 -0.2001 0.2941  -0.0828 176 PHE   A C   
1187 O  O   . PHE   A 156 ? 1.4644 1.2788 1.6212 -0.1819 0.2990  -0.0564 176 PHE   A O   
1188 C  CB  . PHE   A 156 ? 1.2465 1.1505 1.4892 -0.1913 0.2373  -0.1217 176 PHE   A CB  
1189 C  CG  . PHE   A 156 ? 1.1851 1.0789 1.4136 -0.1806 0.2192  -0.1333 176 PHE   A CG  
1190 C  CD1 . PHE   A 156 ? 1.2101 1.0561 1.3967 -0.1678 0.2288  -0.1162 176 PHE   A CD1 
1191 C  CD2 . PHE   A 156 ? 1.2108 1.1408 1.4641 -0.1802 0.1923  -0.1617 176 PHE   A CD2 
1192 C  CE1 . PHE   A 156 ? 1.1793 1.0157 1.3533 -0.1561 0.2143  -0.1275 176 PHE   A CE1 
1193 C  CE2 . PHE   A 156 ? 1.1876 1.1049 1.4217 -0.1679 0.1778  -0.1730 176 PHE   A CE2 
1194 C  CZ  . PHE   A 156 ? 1.1031 0.9746 1.2998 -0.1565 0.1901  -0.1559 176 PHE   A CZ  
1195 N  N   . GLY   A 157 ? 1.3486 1.2310 1.6076 -0.2144 0.3012  -0.0929 177 GLY   A N   
1196 C  CA  . GLY   A 157 ? 1.4027 1.2789 1.6369 -0.2101 0.3207  -0.0718 177 GLY   A CA  
1197 C  C   . GLY   A 157 ? 1.4535 1.2605 1.6490 -0.2105 0.3611  -0.0476 177 GLY   A C   
1198 O  O   . GLY   A 157 ? 1.4980 1.2786 1.6318 -0.1921 0.3671  -0.0224 177 GLY   A O   
1199 N  N   . ALA   A 158 ? 1.5150 1.2881 1.7435 -0.2302 0.3888  -0.0557 178 ALA   A N   
1200 C  CA  . ALA   A 158 ? 1.5764 1.2726 1.7614 -0.2288 0.4300  -0.0306 178 ALA   A CA  
1201 C  C   . ALA   A 158 ? 1.5947 1.2493 1.7011 -0.1999 0.4138  -0.0091 178 ALA   A C   
1202 O  O   . ALA   A 158 ? 1.6327 1.2392 1.6714 -0.1814 0.4305  0.0191  178 ALA   A O   
1203 C  CB  . ALA   A 158 ? 1.5888 1.2559 1.8311 -0.2570 0.4604  -0.0461 178 ALA   A CB  
1204 N  N   . TYR   A 159 ? 1.6182 1.2906 1.7317 -0.1932 0.3809  -0.0231 179 TYR   A N   
1205 C  CA  . TYR   A 159 ? 1.6172 1.2624 1.6664 -0.1639 0.3620  -0.0055 179 TYR   A CA  
1206 C  C   . TYR   A 159 ? 1.6483 1.3198 1.6550 -0.1414 0.3398  0.0098  179 TYR   A C   
1207 O  O   . TYR   A 159 ? 1.6846 1.3178 1.6283 -0.1172 0.3390  0.0326  179 TYR   A O   
1208 C  CB  . TYR   A 159 ? 1.5316 1.1997 1.6014 -0.1603 0.3319  -0.0254 179 TYR   A CB  
1209 C  CG  . TYR   A 159 ? 1.5623 1.2237 1.5788 -0.1288 0.3076  -0.0101 179 TYR   A CG  
1210 C  CD1 . TYR   A 159 ? 1.6593 1.2564 1.6263 -0.1110 0.3201  0.0093  179 TYR   A CD1 
1211 C  CD2 . TYR   A 159 ? 1.5174 1.2359 1.5359 -0.1162 0.2732  -0.0149 179 TYR   A CD2 
1212 C  CE1 . TYR   A 159 ? 1.6636 1.2598 1.5905 -0.0808 0.2961  0.0209  179 TYR   A CE1 
1213 C  CE2 . TYR   A 159 ? 1.3538 1.0708 1.3355 -0.0892 0.2529  -0.0027 179 TYR   A CE2 
1214 C  CZ  . TYR   A 159 ? 1.5678 1.2267 1.5067 -0.0713 0.2630  0.0140  179 TYR   A CZ  
1215 O  OH  . TYR   A 159 ? 1.5413 1.2035 1.4517 -0.0429 0.2410  0.0238  179 TYR   A OH  
1216 N  N   . SER   A 160 ? 1.5928 1.3282 1.6335 -0.1479 0.3198  -0.0039 180 SER   A N   
1217 C  CA  . SER   A 160 ? 1.6267 1.3879 1.6342 -0.1292 0.2977  0.0074  180 SER   A CA  
1218 C  C   . SER   A 160 ? 1.6712 1.3955 1.6333 -0.1219 0.3218  0.0281  180 SER   A C   
1219 O  O   . SER   A 160 ? 1.6900 1.4040 1.5997 -0.0987 0.3063  0.0432  180 SER   A O   
1220 C  CB  . SER   A 160 ? 1.5324 1.3625 1.5856 -0.1382 0.2751  -0.0113 180 SER   A CB  
1221 O  OG  . SER   A 160 ? 1.4876 1.3400 1.5117 -0.1208 0.2521  -0.0018 180 SER   A OG  
1222 N  N   . MET   A 161 ? 1.6878 1.3911 1.6692 -0.1405 0.3598  0.0282  181 MET   A N   
1223 C  CA  . MET   A 161 ? 1.7338 1.3920 1.6612 -0.1305 0.3885  0.0501  181 MET   A CA  
1224 C  C   . MET   A 161 ? 1.7973 1.3781 1.6549 -0.1111 0.4041  0.0736  181 MET   A C   
1225 O  O   . MET   A 161 ? 1.8423 1.3891 1.6277 -0.0855 0.4023  0.0933  181 MET   A O   
1226 C  CB  . MET   A 161 ? 1.7492 1.4079 1.7207 -0.1555 0.4304  0.0444  181 MET   A CB  
1227 C  CG  . MET   A 161 ? 1.7878 1.4155 1.7046 -0.1429 0.4565  0.0640  181 MET   A CG  
1228 S  SD  . MET   A 161 ? 1.8368 1.4908 1.6962 -0.1117 0.4077  0.0694  181 MET   A SD  
1229 C  CE  . MET   A 161 ? 1.9816 1.5796 1.7600 -0.0926 0.4409  0.0923  181 MET   A CE  
1230 N  N   . ASP   A 162 ? 1.8033 1.3533 1.6785 -0.1204 0.4170  0.0707  182 ASP   A N   
1231 C  CA  . ASP   A 162 ? 1.8869 1.3593 1.6948 -0.0993 0.4307  0.0933  182 ASP   A CA  
1232 C  C   . ASP   A 162 ? 1.9270 1.4009 1.6760 -0.0633 0.3898  0.1038  182 ASP   A C   
1233 O  O   . ASP   A 162 ? 1.9843 1.3986 1.6561 -0.0359 0.3963  0.1268  182 ASP   A O   
1234 C  CB  . ASP   A 162 ? 1.8956 1.3442 1.7392 -0.1139 0.4409  0.0833  182 ASP   A CB  
1235 C  CG  . ASP   A 162 ? 1.9427 1.3495 1.8187 -0.1425 0.4939  0.0834  182 ASP   A CG  
1236 O  OD1 . ASP   A 162 ? 1.9309 1.3599 1.8385 -0.1607 0.5167  0.0795  182 ASP   A OD1 
1237 O  OD2 . ASP   A 162 ? 2.0099 1.3604 1.8826 -0.1467 0.5144  0.0870  182 ASP   A OD2 
1238 N  N   . VAL   A 163 ? 1.8825 1.4232 1.6677 -0.0617 0.3476  0.0869  183 VAL   A N   
1239 C  CA  . VAL   A 163 ? 1.9104 1.4599 1.6561 -0.0304 0.3089  0.0936  183 VAL   A CA  
1240 C  C   . VAL   A 163 ? 1.9132 1.4777 1.6229 -0.0154 0.2933  0.1004  183 VAL   A C   
1241 O  O   . VAL   A 163 ? 1.9171 1.4683 1.5786 0.0142  0.2678  0.1098  183 VAL   A O   
1242 C  CB  . VAL   A 163 ? 1.7728 1.3824 1.5714 -0.0342 0.2757  0.0743  183 VAL   A CB  
1243 C  CG1 . VAL   A 163 ? 1.7273 1.4065 1.5816 -0.0553 0.2640  0.0559  183 VAL   A CG1 
1244 C  CG2 . VAL   A 163 ? 1.7793 1.3974 1.5488 -0.0030 0.2402  0.0805  183 VAL   A CG2 
1245 N  N   . ILE   A 164 ? 1.9322 1.5220 1.6639 -0.0334 0.3070  0.0944  184 ILE   A N   
1246 C  CA  . ILE   A 164 ? 1.9993 1.5958 1.6917 -0.0182 0.2942  0.0997  184 ILE   A CA  
1247 C  C   . ILE   A 164 ? 2.1211 1.6407 1.7281 0.0037  0.3191  0.1225  184 ILE   A C   
1248 O  O   . ILE   A 164 ? 2.2189 1.7166 1.7636 0.0348  0.2945  0.1315  184 ILE   A O   
1249 C  CB  . ILE   A 164 ? 1.9190 1.5634 1.6593 -0.0414 0.3026  0.0862  184 ILE   A CB  
1250 C  CG1 . ILE   A 164 ? 1.8147 1.5311 1.6237 -0.0556 0.2727  0.0658  184 ILE   A CG1 
1251 C  CG2 . ILE   A 164 ? 1.9329 1.5708 1.6245 -0.0250 0.2964  0.0924  184 ILE   A CG2 
1252 C  CD1 . ILE   A 164 ? 1.6833 1.4340 1.5484 -0.0815 0.2901  0.0519  184 ILE   A CD1 
1253 N  N   . THR   A 165 ? 2.0633 1.5416 1.6675 -0.0120 0.3688  0.1309  185 THR   A N   
1254 C  CA  . THR   A 165 ? 2.1814 1.5779 1.6995 0.0080  0.4027  0.1553  185 THR   A CA  
1255 C  C   . THR   A 165 ? 2.2797 1.6229 1.7238 0.0445  0.3818  0.1712  185 THR   A C   
1256 O  O   . THR   A 165 ? 2.4942 1.7961 1.8535 0.0777  0.3722  0.1849  185 THR   A O   
1257 C  CB  . THR   A 165 ? 2.2172 1.5729 1.7584 -0.0177 0.4626  0.1623  185 THR   A CB  
1258 O  OG1 . THR   A 165 ? 2.1871 1.5131 1.7413 -0.0215 0.4674  0.1648  185 THR   A OG1 
1259 C  CG2 . THR   A 165 ? 2.0791 1.5005 1.7159 -0.0555 0.4755  0.1404  185 THR   A CG2 
1260 N  N   . SER   A 166 ? 2.3571 1.7023 1.8325 0.0411  0.3716  0.1673  186 SER   A N   
1261 C  CA  . SER   A 166 ? 2.3886 1.6891 1.8039 0.0770  0.3493  0.1802  186 SER   A CA  
1262 C  C   . SER   A 166 ? 2.4230 1.7685 1.8258 0.1034  0.2915  0.1714  186 SER   A C   
1263 O  O   . SER   A 166 ? 2.4855 1.7889 1.8095 0.1412  0.2733  0.1839  186 SER   A O   
1264 C  CB  . SER   A 166 ? 2.3245 1.6235 1.7859 0.0656  0.3519  0.1745  186 SER   A CB  
1265 O  OG  . SER   A 166 ? 2.2525 1.6333 1.8063 0.0370  0.3335  0.1490  186 SER   A OG  
1266 N  N   . THR   A 167 ? 2.2759 1.7055 1.7559 0.0848  0.2618  0.1492  187 THR   A N   
1267 C  CA  . THR   A 167 ? 2.3180 1.7933 1.8017 0.1058  0.2091  0.1393  187 THR   A CA  
1268 C  C   . THR   A 167 ? 2.4678 1.9422 1.9050 0.1213  0.1934  0.1396  187 THR   A C   
1269 O  O   . THR   A 167 ? 2.4306 1.9222 1.8515 0.1464  0.1498  0.1339  187 THR   A O   
1270 C  CB  . THR   A 167 ? 2.1725 1.7318 1.7484 0.0812  0.1879  0.1178  187 THR   A CB  
1271 O  OG1 . THR   A 167 ? 2.1214 1.7092 1.7426 0.0472  0.2128  0.1091  187 THR   A OG1 
1272 C  CG2 . THR   A 167 ? 2.0320 1.5950 1.6421 0.0801  0.1860  0.1147  187 THR   A CG2 
1273 N  N   . SER   A 168 ? 2.9290 2.3849 2.3477 0.1075  0.2269  0.1441  188 SER   A N   
1274 C  CA  . SER   A 168 ? 3.0125 2.4715 2.3914 0.1204  0.2123  0.1409  188 SER   A CA  
1275 C  C   . SER   A 168 ? 3.0749 2.4518 2.3533 0.1432  0.2432  0.1609  188 SER   A C   
1276 O  O   . SER   A 168 ? 3.1428 2.5101 2.3684 0.1639  0.2250  0.1584  188 SER   A O   
1277 C  CB  . SER   A 168 ? 2.9283 2.4493 2.3756 0.0875  0.2189  0.1248  188 SER   A CB  
1278 O  OG  . SER   A 168 ? 2.9044 2.4233 2.3927 0.0571  0.2648  0.1269  188 SER   A OG  
1279 N  N   . PHE   A 169 ? 2.9305 2.3052 2.2420 0.1306  0.2713  0.1667  189 PHE   A N   
1280 C  CA  . PHE   A 169 ? 3.0956 2.3894 2.3080 0.1526  0.3040  0.1880  189 PHE   A CA  
1281 C  C   . PHE   A 169 ? 3.3951 2.6063 2.5507 0.1689  0.3349  0.2127  189 PHE   A C   
1282 O  O   . PHE   A 169 ? 3.6109 2.7444 2.6715 0.1928  0.3629  0.2342  189 PHE   A O   
1283 C  CB  . PHE   A 169 ? 3.0289 2.3251 2.2588 0.1242  0.3517  0.1863  189 PHE   A CB  
1284 C  CG  . PHE   A 169 ? 2.9495 2.3194 2.2310 0.1090  0.3268  0.1635  189 PHE   A CG  
1285 C  CD1 . PHE   A 169 ? 2.8706 2.2330 2.0923 0.1331  0.3057  0.1610  189 PHE   A CD1 
1286 C  CD2 . PHE   A 169 ? 2.8041 2.2467 2.1895 0.0728  0.3236  0.1440  189 PHE   A CD2 
1287 C  CE1 . PHE   A 169 ? 2.6939 2.1189 1.9629 0.1193  0.2843  0.1401  189 PHE   A CE1 
1288 C  CE2 . PHE   A 169 ? 2.6421 2.1463 2.0707 0.0612  0.3020  0.1251  189 PHE   A CE2 
1289 C  CZ  . PHE   A 169 ? 2.5109 2.0058 1.8833 0.0834  0.2835  0.1234  189 PHE   A CZ  
1290 N  N   . GLY   A 170 ? 2.9206 2.1406 2.1260 0.1585  0.3329  0.2110  190 GLY   A N   
1291 C  CA  . GLY   A 170 ? 2.8028 1.9412 1.9623 0.1689  0.3687  0.2337  190 GLY   A CA  
1292 C  C   . GLY   A 170 ? 2.7697 1.8638 1.9361 0.1388  0.4379  0.2443  190 GLY   A C   
1293 O  O   . GLY   A 170 ? 2.7801 1.7867 1.8840 0.1522  0.4763  0.2688  190 GLY   A O   
1294 N  N   . VAL   A 171 ? 2.5196 1.6705 1.7622 0.0993  0.4555  0.2265  191 VAL   A N   
1295 C  CA  . VAL   A 171 ? 2.5230 1.6466 1.7958 0.0656  0.5199  0.2308  191 VAL   A CA  
1296 C  C   . VAL   A 171 ? 2.4151 1.5585 1.7722 0.0356  0.5265  0.2180  191 VAL   A C   
1297 O  O   . VAL   A 171 ? 2.3438 1.5676 1.7843 0.0149  0.4944  0.1921  191 VAL   A O   
1298 C  CB  . VAL   A 171 ? 2.4696 1.6492 1.7892 0.0404  0.5319  0.2150  191 VAL   A CB  
1299 C  CG1 . VAL   A 171 ? 2.3555 1.5171 1.7230 0.0036  0.5972  0.2158  191 VAL   A CG1 
1300 C  CG2 . VAL   A 171 ? 2.6032 1.7592 1.8335 0.0727  0.5235  0.2257  191 VAL   A CG2 
1301 N  N   . ASN   A 172 ? 2.3200 1.3857 1.6505 0.0352  0.5674  0.2359  192 ASN   A N   
1302 C  CA  . ASN   A 172 ? 2.3480 1.4190 1.7455 0.0124  0.5715  0.2239  192 ASN   A CA  
1303 C  C   . ASN   A 172 ? 2.3846 1.4517 1.8520 -0.0336 0.6273  0.2149  192 ASN   A C   
1304 O  O   . ASN   A 172 ? 2.5076 1.4968 1.9401 -0.0371 0.6827  0.2349  192 ASN   A O   
1305 C  CB  . ASN   A 172 ? 2.3862 1.3739 1.7129 0.0445  0.5739  0.2471  192 ASN   A CB  
1306 C  CG  . ASN   A 172 ? 2.4444 1.4498 1.7214 0.0889  0.5123  0.2501  192 ASN   A CG  
1307 O  OD1 . ASN   A 172 ? 2.4272 1.5155 1.7613 0.0849  0.4643  0.2272  192 ASN   A OD1 
1308 N  ND2 . ASN   A 172 ? 2.5389 1.4648 1.7093 0.1325  0.5142  0.2782  192 ASN   A ND2 
1309 N  N   . ILE   A 173 ? 2.3398 1.4928 1.9094 -0.0678 0.6110  0.1830  193 ILE   A N   
1310 C  CA  . ILE   A 173 ? 2.3343 1.5032 1.9876 -0.1124 0.6539  0.1666  193 ILE   A CA  
1311 C  C   . ILE   A 173 ? 2.2631 1.4856 2.0093 -0.1391 0.6298  0.1349  193 ILE   A C   
1312 O  O   . ILE   A 173 ? 2.2287 1.5127 1.9941 -0.1298 0.5765  0.1189  193 ILE   A O   
1313 C  CB  . ILE   A 173 ? 2.3212 1.5489 2.0073 -0.1263 0.6592  0.1557  193 ILE   A CB  
1314 C  CG1 . ILE   A 173 ? 2.3452 1.5197 1.9321 -0.0968 0.6807  0.1850  193 ILE   A CG1 
1315 C  CG2 . ILE   A 173 ? 2.3918 1.6459 2.1745 -0.1689 0.6980  0.1346  193 ILE   A CG2 
1316 C  CD1 . ILE   A 173 ? 2.3508 1.5823 1.9640 -0.1057 0.6824  0.1737  193 ILE   A CD1 
1317 N  N   . ASP   A 174 ? 2.4704 1.6692 2.2756 -0.1729 0.6708  0.1245  194 ASP   A N   
1318 C  CA  . ASP   A 174 ? 2.4232 1.6760 2.3255 -0.2035 0.6526  0.0885  194 ASP   A CA  
1319 C  C   . ASP   A 174 ? 2.3961 1.7220 2.3805 -0.2340 0.6590  0.0642  194 ASP   A C   
1320 O  O   . ASP   A 174 ? 2.4581 1.7868 2.4993 -0.2575 0.6897  0.0505  194 ASP   A O   
1321 C  CB  . ASP   A 174 ? 2.5826 1.7706 2.5056 -0.2209 0.6878  0.0865  194 ASP   A CB  
1322 C  CG  . ASP   A 174 ? 2.5579 1.7874 2.5597 -0.2437 0.6610  0.0505  194 ASP   A CG  
1323 O  OD1 . ASP   A 174 ? 2.4038 1.7172 2.4416 -0.2429 0.6131  0.0272  194 ASP   A OD1 
1324 O  OD2 . ASP   A 174 ? 2.6162 1.8014 2.6387 -0.2557 0.6802  0.0428  194 ASP   A OD2 
1325 N  N   . SER   A 175 ? 2.2716 1.6722 2.2617 -0.2226 0.6140  0.0537  195 SER   A N   
1326 C  CA  . SER   A 175 ? 2.2223 1.6859 2.2674 -0.2404 0.6191  0.0382  195 SER   A CA  
1327 C  C   . SER   A 175 ? 2.2420 1.7510 2.3997 -0.2805 0.6287  0.0027  195 SER   A C   
1328 O  O   . SER   A 175 ? 2.2703 1.8121 2.4765 -0.2937 0.6458  -0.0089 195 SER   A O   
1329 C  CB  . SER   A 175 ? 2.0638 1.5961 2.0961 -0.2201 0.5646  0.0317  195 SER   A CB  
1330 O  OG  . SER   A 175 ? 2.1238 1.6199 2.0606 -0.1845 0.5537  0.0604  195 SER   A OG  
1331 N  N   . LEU   A 176 ? 2.1799 1.7020 2.3775 -0.2904 0.6037  -0.0201 196 LEU   A N   
1332 C  CA  . LEU   A 176 ? 2.2233 1.7886 2.5264 -0.3254 0.6062  -0.0582 196 LEU   A CA  
1333 C  C   . LEU   A 176 ? 2.4457 1.9656 2.7686 -0.3360 0.6476  -0.0577 196 LEU   A C   
1334 O  O   . LEU   A 176 ? 2.2863 1.8448 2.6788 -0.3529 0.6590  -0.0782 196 LEU   A O   
1335 C  CB  . LEU   A 176 ? 2.1954 1.7841 2.5229 -0.3267 0.5631  -0.0841 196 LEU   A CB  
1336 C  CG  . LEU   A 176 ? 1.9748 1.6324 2.4072 -0.3555 0.5443  -0.1300 196 LEU   A CG  
1337 C  CD1 . LEU   A 176 ? 1.9512 1.6783 2.4279 -0.3606 0.5399  -0.1398 196 LEU   A CD1 
1338 C  CD2 . LEU   A 176 ? 1.6942 1.3890 2.1282 -0.3438 0.4892  -0.1534 196 LEU   A CD2 
1339 N  N   . ASN   A 177 ? 2.7533 2.1904 3.0164 -0.3249 0.6712  -0.0342 197 ASN   A N   
1340 C  CA  . ASN   A 177 ? 2.7153 2.1014 2.9879 -0.3327 0.7151  -0.0295 197 ASN   A CA  
1341 C  C   . ASN   A 177 ? 2.6287 1.9817 2.8486 -0.3173 0.7525  -0.0001 197 ASN   A C   
1342 O  O   . ASN   A 177 ? 2.7276 2.0478 2.9651 -0.3258 0.7931  0.0018  197 ASN   A O   
1343 C  CB  . ASN   A 177 ? 2.8034 2.1112 3.0302 -0.3245 0.7254  -0.0162 197 ASN   A CB  
1344 C  CG  . ASN   A 177 ? 2.8057 2.1334 3.0535 -0.3294 0.6849  -0.0375 197 ASN   A CG  
1345 O  OD1 . ASN   A 177 ? 3.0216 2.3882 3.2563 -0.3212 0.6505  -0.0390 197 ASN   A OD1 
1346 N  ND2 . ASN   A 177 ? 2.6109 1.9112 2.8921 -0.3429 0.6896  -0.0554 197 ASN   A ND2 
1347 N  N   . ASN   A 178 ? 2.5975 1.9569 2.7529 -0.2944 0.7404  0.0216  198 ASN   A N   
1348 C  CA  . ASN   A 178 ? 2.6353 1.9709 2.7394 -0.2778 0.7700  0.0453  198 ASN   A CA  
1349 C  C   . ASN   A 178 ? 2.5518 1.9671 2.6936 -0.2819 0.7494  0.0313  198 ASN   A C   
1350 O  O   . ASN   A 178 ? 2.5253 1.9418 2.6018 -0.2594 0.7359  0.0500  198 ASN   A O   
1351 C  CB  . ASN   A 178 ? 2.7525 2.0146 2.7311 -0.2404 0.7739  0.0854  198 ASN   A CB  
1352 C  CG  . ASN   A 178 ? 2.9929 2.1786 2.9267 -0.2304 0.7843  0.1002  198 ASN   A CG  
1353 O  OD1 . ASN   A 178 ? 2.9314 2.1169 2.9269 -0.2529 0.7894  0.0803  198 ASN   A OD1 
1354 N  ND2 . ASN   A 178 ? 3.3917 2.5115 3.2151 -0.1938 0.7846  0.1342  198 ASN   A ND2 
1355 N  N   . PRO   A 179 ? 2.7532 2.2357 2.9988 -0.3085 0.7450  -0.0023 199 PRO   A N   
1356 C  CA  . PRO   A 179 ? 2.5874 2.1457 2.8691 -0.3097 0.7239  -0.0161 199 PRO   A CA  
1357 C  C   . PRO   A 179 ? 2.6755 2.2131 2.9115 -0.2940 0.7548  0.0049  199 PRO   A C   
1358 O  O   . PRO   A 179 ? 2.6150 2.1910 2.8341 -0.2825 0.7367  0.0071  199 PRO   A O   
1359 C  CB  . PRO   A 179 ? 2.3057 1.9295 2.7071 -0.3389 0.7145  -0.0569 199 PRO   A CB  
1360 C  CG  . PRO   A 179 ? 2.4006 1.9710 2.8220 -0.3520 0.7527  -0.0574 199 PRO   A CG  
1361 C  CD  . PRO   A 179 ? 2.6046 2.0949 2.9373 -0.3359 0.7604  -0.0290 199 PRO   A CD  
1362 N  N   . GLN   A 180 ? 3.0765 2.5513 3.2895 -0.2921 0.8018  0.0202  200 GLN   A N   
1363 C  CA  . GLN   A 180 ? 3.0471 2.4957 3.2156 -0.2767 0.8357  0.0392  200 GLN   A CA  
1364 C  C   . GLN   A 180 ? 3.0285 2.4550 3.0909 -0.2441 0.8191  0.0658  200 GLN   A C   
1365 O  O   . GLN   A 180 ? 3.0007 2.4593 3.0553 -0.2353 0.8154  0.0657  200 GLN   A O   
1366 C  CB  . GLN   A 180 ? 3.0963 2.4648 3.2371 -0.2753 0.8893  0.0563  200 GLN   A CB  
1367 C  CG  . GLN   A 180 ? 3.1141 2.4669 3.3129 -0.2984 0.8981  0.0411  200 GLN   A CG  
1368 C  CD  . GLN   A 180 ? 3.1101 2.4180 3.2472 -0.2860 0.8766  0.0549  200 GLN   A CD  
1369 O  OE1 . GLN   A 180 ? 3.2402 2.5214 3.2857 -0.2581 0.8588  0.0789  200 GLN   A OE1 
1370 N  NE2 . GLN   A 180 ? 3.1199 2.4198 3.3084 -0.3058 0.8771  0.0386  200 GLN   A NE2 
1371 N  N   . ASP   A 181 ? 2.7379 2.1084 2.7176 -0.2245 0.8086  0.0879  201 ASP   A N   
1372 C  CA  . ASP   A 181 ? 2.6294 1.9830 2.5115 -0.1928 0.7852  0.1098  201 ASP   A CA  
1373 C  C   . ASP   A 181 ? 2.5032 1.9380 2.4302 -0.2014 0.7386  0.0902  201 ASP   A C   
1374 O  O   . ASP   A 181 ? 2.4683 1.9237 2.4280 -0.2130 0.7122  0.0789  201 ASP   A O   
1375 C  CB  . ASP   A 181 ? 2.5882 1.8630 2.3760 -0.1680 0.7827  0.1367  201 ASP   A CB  
1376 C  CG  . ASP   A 181 ? 2.5259 1.7628 2.1965 -0.1282 0.7691  0.1630  201 ASP   A CG  
1377 O  OD1 . ASP   A 181 ? 2.4913 1.7775 2.1597 -0.1230 0.7454  0.1567  201 ASP   A OD1 
1378 O  OD2 . ASP   A 181 ? 2.5077 1.6651 2.0874 -0.1003 0.7803  0.1884  201 ASP   A OD2 
1379 N  N   . PRO   A 182 ? 2.3955 1.7758 2.2576 -0.1691 0.7828  0.1346  202 PRO   A N   
1380 C  CA  . PRO   A 182 ? 2.2380 1.6980 2.1397 -0.1743 0.7483  0.1165  202 PRO   A CA  
1381 C  C   . PRO   A 182 ? 2.1436 1.6244 2.0256 -0.1705 0.7028  0.1150  202 PRO   A C   
1382 O  O   . PRO   A 182 ? 2.1118 1.6030 2.0376 -0.1866 0.6862  0.1047  202 PRO   A O   
1383 C  CB  . PRO   A 182 ? 2.2321 1.6702 2.0554 -0.1463 0.7601  0.1314  202 PRO   A CB  
1384 C  CG  . PRO   A 182 ? 2.2968 1.6387 2.0058 -0.1169 0.7793  0.1615  202 PRO   A CG  
1385 C  CD  . PRO   A 182 ? 2.4127 1.7200 2.1617 -0.1348 0.8070  0.1624  202 PRO   A CD  
1386 N  N   . PHE   A 183 ? 2.0591 1.5558 1.8824 -0.1448 0.6687  0.1184  203 PHE   A N   
1387 C  CA  . PHE   A 183 ? 2.0684 1.5952 1.8686 -0.1274 0.6011  0.1110  203 PHE   A CA  
1388 C  C   . PHE   A 183 ? 1.9841 1.5993 1.8834 -0.1487 0.5603  0.0801  203 PHE   A C   
1389 O  O   . PHE   A 183 ? 1.9456 1.6016 1.8361 -0.1355 0.5098  0.0715  203 PHE   A O   
1390 C  CB  . PHE   A 183 ? 2.0864 1.5525 1.8267 -0.1122 0.5925  0.1280  203 PHE   A CB  
1391 C  CG  . PHE   A 183 ? 2.1524 1.5475 1.7692 -0.0734 0.5938  0.1547  203 PHE   A CG  
1392 C  CD1 . PHE   A 183 ? 2.1328 1.5438 1.6998 -0.0453 0.5376  0.1530  203 PHE   A CD1 
1393 C  CD2 . PHE   A 183 ? 2.2149 1.5263 1.7653 -0.0640 0.6511  0.1806  203 PHE   A CD2 
1394 C  CE1 . PHE   A 183 ? 2.2522 1.6007 1.7072 -0.0073 0.5321  0.1734  203 PHE   A CE1 
1395 C  CE2 . PHE   A 183 ? 2.2436 1.4861 1.6706 -0.0234 0.6484  0.2043  203 PHE   A CE2 
1396 C  CZ  . PHE   A 183 ? 2.2976 1.5605 1.6777 0.0056  0.5858  0.1990  203 PHE   A CZ  
1397 N  N   . VAL   A 184 ? 2.0114 1.6560 2.0046 -0.1805 0.5808  0.0624  204 VAL   A N   
1398 C  CA  . VAL   A 184 ? 1.8758 1.6021 1.9551 -0.1962 0.5405  0.0320  204 VAL   A CA  
1399 C  C   . VAL   A 184 ? 1.8267 1.6080 1.9345 -0.1943 0.5328  0.0202  204 VAL   A C   
1400 O  O   . VAL   A 184 ? 1.7689 1.5963 1.8780 -0.1838 0.4859  0.0097  204 VAL   A O   
1401 C  CB  . VAL   A 184 ? 1.8102 1.5513 1.9813 -0.2285 0.5583  0.0123  204 VAL   A CB  
1402 C  CG1 . VAL   A 184 ? 1.7348 1.5607 2.0036 -0.2457 0.5360  -0.0205 204 VAL   A CG1 
1403 C  CG2 . VAL   A 184 ? 1.7483 1.4676 1.9047 -0.2268 0.5329  0.0115  204 VAL   A CG2 
1404 N  N   . GLU   A 185 ? 1.8023 1.5762 1.9326 -0.2036 0.5816  0.0227  205 GLU   A N   
1405 C  CA  . GLU   A 185 ? 1.7158 1.5296 1.8662 -0.1991 0.5869  0.0148  205 GLU   A CA  
1406 C  C   . GLU   A 185 ? 1.6525 1.5364 1.8341 -0.1930 0.5298  -0.0058 205 GLU   A C   
1407 O  O   . GLU   A 185 ? 1.6615 1.6052 1.9323 -0.2102 0.5154  -0.0312 205 GLU   A O   
1408 C  CB  . GLU   A 185 ? 1.7757 1.5323 1.8229 -0.1722 0.6093  0.0406  205 GLU   A CB  
1409 C  CG  . GLU   A 185 ? 1.8331 1.5286 1.8594 -0.1774 0.6813  0.0596  205 GLU   A CG  
1410 C  CD  . GLU   A 185 ? 1.9033 1.5540 1.9358 -0.1895 0.6958  0.0668  205 GLU   A CD  
1411 O  OE1 . GLU   A 185 ? 1.9333 1.5648 1.9295 -0.1843 0.6684  0.0733  205 GLU   A OE1 
1412 O  OE2 . GLU   A 185 ? 1.8726 1.5090 1.9486 -0.2020 0.7295  0.0639  205 GLU   A OE2 
1413 N  N   . ASN   A 186 ? 1.6988 1.5726 1.8062 -0.1676 0.4976  0.0046  206 ASN   A N   
1414 C  CA  . ASN   A 186 ? 1.6830 1.6103 1.8046 -0.1590 0.4455  -0.0096 206 ASN   A CA  
1415 C  C   . ASN   A 186 ? 1.5727 1.5638 1.7768 -0.1694 0.4447  -0.0326 206 ASN   A C   
1416 O  O   . ASN   A 186 ? 1.4481 1.4835 1.6707 -0.1630 0.4043  -0.0453 206 ASN   A O   
1417 C  CB  . ASN   A 186 ? 1.6361 1.5780 1.7675 -0.1619 0.4045  -0.0157 206 ASN   A CB  
1418 C  CG  . ASN   A 186 ? 1.6079 1.5881 1.8273 -0.1856 0.4043  -0.0377 206 ASN   A CG  
1419 O  OD1 . ASN   A 186 ? 1.5601 1.5971 1.8347 -0.1896 0.3785  -0.0584 206 ASN   A OD1 
1420 N  ND2 . ASN   A 186 ? 1.5950 1.5410 1.8255 -0.2000 0.4317  -0.0341 206 ASN   A ND2 
1421 N  N   . ASP   A 197 ? 1.5926 1.9947 2.0262 -0.0331 0.0906  -0.1673 217 ASP   A N   
1422 C  CA  . ASP   A 197 ? 1.5798 2.0224 2.0855 -0.0347 0.1047  -0.1885 217 ASP   A CA  
1423 C  C   . ASP   A 197 ? 1.5649 2.0124 2.0695 -0.0132 0.1044  -0.1890 217 ASP   A C   
1424 O  O   . ASP   A 197 ? 1.4560 1.8688 1.9008 -0.0012 0.0966  -0.1718 217 ASP   A O   
1425 C  CB  . ASP   A 197 ? 1.5976 2.0308 2.1239 -0.0593 0.1459  -0.1861 217 ASP   A CB  
1426 C  CG  . ASP   A 197 ? 1.5923 1.9800 2.0603 -0.0599 0.1729  -0.1638 217 ASP   A CG  
1427 O  OD1 . ASP   A 197 ? 1.5275 1.8980 1.9545 -0.0428 0.1621  -0.1548 217 ASP   A OD1 
1428 O  OD2 . ASP   A 197 ? 1.6953 2.0609 2.1560 -0.0764 0.2047  -0.1558 217 ASP   A OD2 
1429 N  N   . PRO   A 198 ? 1.5698 2.0599 2.1439 -0.0082 0.1131  -0.2097 218 PRO   A N   
1430 C  CA  . PRO   A 198 ? 1.5383 2.0329 2.1132 0.0147  0.1142  -0.2114 218 PRO   A CA  
1431 C  C   . PRO   A 198 ? 1.5498 1.9953 2.0626 0.0152  0.1391  -0.1902 218 PRO   A C   
1432 O  O   . PRO   A 198 ? 1.5538 1.9848 2.0388 0.0365  0.1297  -0.1861 218 PRO   A O   
1433 C  CB  . PRO   A 198 ? 1.4454 1.9948 2.1155 0.0120  0.1322  -0.2369 218 PRO   A CB  
1434 C  CG  . PRO   A 198 ? 1.4732 2.0575 2.1963 -0.0015 0.1148  -0.2555 218 PRO   A CG  
1435 C  CD  . PRO   A 198 ? 1.5310 2.0717 2.1933 -0.0203 0.1161  -0.2361 218 PRO   A CD  
1436 N  N   . PHE   A 199 ? 1.4193 1.8354 1.9065 -0.0054 0.1690  -0.1777 219 PHE   A N   
1437 C  CA  . PHE   A 199 ? 1.3320 1.7027 1.7610 -0.0021 0.1916  -0.1621 219 PHE   A CA  
1438 C  C   . PHE   A 199 ? 1.3719 1.7008 1.7289 0.0071  0.1655  -0.1457 219 PHE   A C   
1439 O  O   . PHE   A 199 ? 1.3428 1.6533 1.6729 0.0244  0.1605  -0.1436 219 PHE   A O   
1440 C  CB  . PHE   A 199 ? 1.3044 1.6501 1.7171 -0.0227 0.2277  -0.1525 219 PHE   A CB  
1441 C  CG  . PHE   A 199 ? 1.2637 1.5635 1.6160 -0.0158 0.2521  -0.1402 219 PHE   A CG  
1442 C  CD1 . PHE   A 199 ? 1.2209 1.5282 1.5931 -0.0055 0.2824  -0.1480 219 PHE   A CD1 
1443 C  CD2 . PHE   A 199 ? 1.3019 1.5518 1.5783 -0.0176 0.2438  -0.1228 219 PHE   A CD2 
1444 C  CE1 . PHE   A 199 ? 1.2161 1.4770 1.5245 0.0040  0.3039  -0.1383 219 PHE   A CE1 
1445 C  CE2 . PHE   A 199 ? 1.2876 1.4938 1.5047 -0.0085 0.2613  -0.1149 219 PHE   A CE2 
1446 C  CZ  . PHE   A 199 ? 1.2488 1.4581 1.4775 0.0029  0.2914  -0.1225 219 PHE   A CZ  
1447 N  N   . PHE   A 200 ? 1.3186 1.6316 1.6475 -0.0048 0.1501  -0.1349 220 PHE   A N   
1448 C  CA  . PHE   A 200 ? 1.3234 1.5961 1.5906 -0.0005 0.1317  -0.1188 220 PHE   A CA  
1449 C  C   . PHE   A 200 ? 1.2379 1.5142 1.5017 0.0191  0.1042  -0.1200 220 PHE   A C   
1450 O  O   . PHE   A 200 ? 1.2182 1.4592 1.4388 0.0260  0.0953  -0.1093 220 PHE   A O   
1451 C  CB  . PHE   A 200 ? 1.4010 1.6611 1.6474 -0.0167 0.1242  -0.1080 220 PHE   A CB  
1452 C  CG  . PHE   A 200 ? 1.4455 1.6908 1.6828 -0.0331 0.1500  -0.1032 220 PHE   A CG  
1453 C  CD1 . PHE   A 200 ? 1.4494 1.7204 1.7327 -0.0453 0.1678  -0.1128 220 PHE   A CD1 
1454 C  CD2 . PHE   A 200 ? 1.4766 1.6800 1.6596 -0.0355 0.1556  -0.0900 220 PHE   A CD2 
1455 C  CE1 . PHE   A 200 ? 1.4463 1.6963 1.7169 -0.0592 0.1949  -0.1060 220 PHE   A CE1 
1456 C  CE2 . PHE   A 200 ? 1.4672 1.6513 1.6333 -0.0462 0.1786  -0.0841 220 PHE   A CE2 
1457 C  CZ  . PHE   A 200 ? 1.4556 1.6604 1.6631 -0.0579 0.2003  -0.0904 220 PHE   A CZ  
1458 N  N   . LEU   A 201 ? 1.2431 1.5587 1.5510 0.0293  0.0896  -0.1335 221 LEU   A N   
1459 C  CA  . LEU   A 201 ? 1.2484 1.5622 1.5463 0.0530  0.0644  -0.1335 221 LEU   A CA  
1460 C  C   . LEU   A 201 ? 1.2342 1.5416 1.5342 0.0711  0.0723  -0.1385 221 LEU   A C   
1461 O  O   . LEU   A 201 ? 1.2547 1.5326 1.5205 0.0873  0.0594  -0.1305 221 LEU   A O   
1462 C  CB  . LEU   A 201 ? 1.2445 1.6006 1.5832 0.0635  0.0420  -0.1486 221 LEU   A CB  
1463 C  CG  . LEU   A 201 ? 1.2011 1.5507 1.5161 0.0580  0.0234  -0.1413 221 LEU   A CG  
1464 C  CD1 . LEU   A 201 ? 1.0459 1.3457 1.2966 0.0599  0.0189  -0.1176 221 LEU   A CD1 
1465 C  CD2 . LEU   A 201 ? 1.3139 1.6754 1.6487 0.0315  0.0371  -0.1447 221 LEU   A CD2 
1466 N  N   . SER   A 202 ? 1.2444 1.5764 1.5846 0.0689  0.0962  -0.1516 222 SER   A N   
1467 C  CA  . SER   A 202 ? 1.2537 1.5731 1.5883 0.0850  0.1100  -0.1555 222 SER   A CA  
1468 C  C   . SER   A 202 ? 1.2742 1.5360 1.5419 0.0798  0.1183  -0.1403 222 SER   A C   
1469 O  O   . SER   A 202 ? 1.3054 1.5412 1.5492 0.0962  0.1187  -0.1407 222 SER   A O   
1470 C  CB  . SER   A 202 ? 1.2507 1.6059 1.6408 0.0813  0.1414  -0.1710 222 SER   A CB  
1471 O  OG  . SER   A 202 ? 1.2226 1.6347 1.6847 0.0795  0.1332  -0.1879 222 SER   A OG  
1472 N  N   . ILE   A 203 ? 1.2630 1.5041 1.5012 0.0583  0.1226  -0.1287 223 ILE   A N   
1473 C  CA  . ILE   A 203 ? 1.2608 1.4510 1.4400 0.0531  0.1261  -0.1176 223 ILE   A CA  
1474 C  C   . ILE   A 203 ? 1.2869 1.4471 1.4339 0.0571  0.0996  -0.1069 223 ILE   A C   
1475 O  O   . ILE   A 203 ? 1.3020 1.4218 1.4115 0.0610  0.0968  -0.1037 223 ILE   A O   
1476 C  CB  . ILE   A 203 ? 1.2649 1.4469 1.4288 0.0317  0.1405  -0.1106 223 ILE   A CB  
1477 C  CG1 . ILE   A 203 ? 1.2336 1.4337 1.4231 0.0284  0.1744  -0.1188 223 ILE   A CG1 
1478 C  CG2 . ILE   A 203 ? 1.2960 1.4293 1.4011 0.0276  0.1357  -0.1010 223 ILE   A CG2 
1479 C  CD1 . ILE   A 203 ? 1.2579 1.4455 1.4374 0.0455  0.1937  -0.1266 223 ILE   A CD1 
1480 N  N   . THR   A 204 ? 1.3146 1.4912 1.4754 0.0566  0.0811  -0.1020 224 THR   A N   
1481 C  CA  . THR   A 204 ? 1.2897 1.4356 1.4216 0.0611  0.0621  -0.0897 224 THR   A CA  
1482 C  C   . THR   A 204 ? 1.3204 1.4532 1.4491 0.0857  0.0539  -0.0928 224 THR   A C   
1483 O  O   . THR   A 204 ? 1.3158 1.4066 1.4137 0.0892  0.0473  -0.0842 224 THR   A O   
1484 C  CB  . THR   A 204 ? 1.2204 1.3828 1.3592 0.0559  0.0488  -0.0822 224 THR   A CB  
1485 O  OG1 . THR   A 204 ? 1.2264 1.4349 1.4059 0.0622  0.0468  -0.0952 224 THR   A OG1 
1486 C  CG2 . THR   A 204 ? 1.2062 1.3604 1.3317 0.0326  0.0534  -0.0733 224 THR   A CG2 
1487 N  N   . VAL   A 205 ? 1.2703 1.4381 1.4340 0.1033  0.0539  -0.1059 225 VAL   A N   
1488 C  CA  . VAL   A 205 ? 1.2834 1.4386 1.4444 0.1306  0.0463  -0.1100 225 VAL   A CA  
1489 C  C   . VAL   A 205 ? 1.3382 1.4724 1.4892 0.1355  0.0636  -0.1180 225 VAL   A C   
1490 O  O   . VAL   A 205 ? 1.3593 1.4596 1.4890 0.1530  0.0587  -0.1175 225 VAL   A O   
1491 C  CB  . VAL   A 205 ? 1.3107 1.5146 1.5164 0.1514  0.0347  -0.1230 225 VAL   A CB  
1492 C  CG1 . VAL   A 205 ? 1.3028 1.5039 1.5176 0.1817  0.0325  -0.1325 225 VAL   A CG1 
1493 C  CG2 . VAL   A 205 ? 1.2691 1.4722 1.4610 0.1581  0.0113  -0.1133 225 VAL   A CG2 
1494 N  N   . PHE   A 206 ? 1.3884 1.5352 1.5476 0.1212  0.0851  -0.1246 226 PHE   A N   
1495 C  CA  . PHE   A 206 ? 1.3913 1.5114 1.5280 0.1259  0.1039  -0.1315 226 PHE   A CA  
1496 C  C   . PHE   A 206 ? 1.3810 1.4659 1.4743 0.1050  0.1091  -0.1240 226 PHE   A C   
1497 O  O   . PHE   A 206 ? 1.3787 1.4673 1.4663 0.0975  0.1307  -0.1279 226 PHE   A O   
1498 C  CB  . PHE   A 206 ? 1.4004 1.5600 1.5779 0.1328  0.1297  -0.1461 226 PHE   A CB  
1499 C  CG  . PHE   A 206 ? 1.4401 1.6488 1.6760 0.1515  0.1222  -0.1573 226 PHE   A CG  
1500 C  CD1 . PHE   A 206 ? 1.4332 1.6314 1.6647 0.1752  0.0988  -0.1568 226 PHE   A CD1 
1501 C  CD2 . PHE   A 206 ? 1.4427 1.7068 1.7399 0.1464  0.1386  -0.1694 226 PHE   A CD2 
1502 C  CE1 . PHE   A 206 ? 1.3819 1.6258 1.6650 0.1966  0.0875  -0.1688 226 PHE   A CE1 
1503 C  CE2 . PHE   A 206 ? 1.3920 1.7063 1.7504 0.1646  0.1273  -0.1838 226 PHE   A CE2 
1504 C  CZ  . PHE   A 206 ? 1.3600 1.6649 1.7094 0.1915  0.0997  -0.1839 226 PHE   A CZ  
1505 N  N   . PRO   A 207 ? 1.4336 1.4827 1.4961 0.0964  0.0905  -0.1135 227 PRO   A N   
1506 C  CA  . PRO   A 207 ? 1.3964 1.4133 1.4212 0.0802  0.0909  -0.1104 227 PRO   A CA  
1507 C  C   . PRO   A 207 ? 1.4293 1.4097 1.4182 0.0913  0.0997  -0.1217 227 PRO   A C   
1508 O  O   . PRO   A 207 ? 1.4114 1.3691 1.3660 0.0831  0.1026  -0.1233 227 PRO   A O   
1509 C  CB  . PRO   A 207 ? 1.3657 1.3582 1.3805 0.0703  0.0690  -0.0990 227 PRO   A CB  
1510 C  CG  . PRO   A 207 ? 1.3982 1.3843 1.4230 0.0881  0.0610  -0.0977 227 PRO   A CG  
1511 C  CD  . PRO   A 207 ? 1.4308 1.4626 1.4901 0.1031  0.0699  -0.1046 227 PRO   A CD  
1512 N  N   . PHE   A 208 ? 1.3080 1.2801 1.3000 0.1127  0.1030  -0.1305 228 PHE   A N   
1513 C  CA  . PHE   A 208 ? 1.3416 1.2786 1.2978 0.1272  0.1137  -0.1435 228 PHE   A CA  
1514 C  C   . PHE   A 208 ? 1.3007 1.2559 1.2539 0.1313  0.1446  -0.1500 228 PHE   A C   
1515 O  O   . PHE   A 208 ? 1.3559 1.2776 1.2672 0.1432  0.1568  -0.1599 228 PHE   A O   
1516 C  CB  . PHE   A 208 ? 1.3556 1.2798 1.3196 0.1513  0.1103  -0.1509 228 PHE   A CB  
1517 C  CG  . PHE   A 208 ? 1.3756 1.3479 1.3918 0.1630  0.1119  -0.1489 228 PHE   A CG  
1518 C  CD1 . PHE   A 208 ? 1.3584 1.3742 1.4099 0.1737  0.1350  -0.1582 228 PHE   A CD1 
1519 C  CD2 . PHE   A 208 ? 1.4119 1.3847 1.4421 0.1647  0.0905  -0.1386 228 PHE   A CD2 
1520 C  CE1 . PHE   A 208 ? 1.3789 1.4427 1.4845 0.1857  0.1313  -0.1606 228 PHE   A CE1 
1521 C  CE2 . PHE   A 208 ? 1.4449 1.4599 1.5171 0.1797  0.0868  -0.1389 228 PHE   A CE2 
1522 C  CZ  . PHE   A 208 ? 1.4580 1.5210 1.5710 0.1902  0.1045  -0.1516 228 PHE   A CZ  
1523 N  N   . LEU   A 209 ? 1.3623 1.3657 1.3568 0.1220  0.1590  -0.1452 229 LEU   A N   
1524 C  CA  . LEU   A 209 ? 1.3122 1.3326 1.3118 0.1239  0.1944  -0.1496 229 LEU   A CA  
1525 C  C   . LEU   A 209 ? 1.3465 1.3508 1.3105 0.1068  0.2033  -0.1411 229 LEU   A C   
1526 O  O   . LEU   A 209 ? 1.3622 1.3653 1.3143 0.1094  0.2364  -0.1424 229 LEU   A O   
1527 C  CB  . LEU   A 209 ? 1.2924 1.3752 1.3664 0.1237  0.2079  -0.1526 229 LEU   A CB  
1528 C  CG  . LEU   A 209 ? 1.3118 1.4171 1.4255 0.1473  0.2051  -0.1640 229 LEU   A CG  
1529 C  CD1 . LEU   A 209 ? 1.3149 1.4869 1.5083 0.1469  0.2183  -0.1713 229 LEU   A CD1 
1530 C  CD2 . LEU   A 209 ? 1.2665 1.3388 1.3462 0.1693  0.2244  -0.1744 229 LEU   A CD2 
1531 N  N   . ILE   A 210 ? 1.3311 1.3218 1.2782 0.0909  0.1768  -0.1319 230 ILE   A N   
1532 C  CA  . ILE   A 210 ? 1.3498 1.3227 1.2603 0.0783  0.1815  -0.1242 230 ILE   A CA  
1533 C  C   . ILE   A 210 ? 1.3702 1.2950 1.2121 0.0927  0.1952  -0.1306 230 ILE   A C   
1534 O  O   . ILE   A 210 ? 1.4094 1.3269 1.2272 0.0922  0.2221  -0.1258 230 ILE   A O   
1535 C  CB  . ILE   A 210 ? 1.3448 1.3114 1.2520 0.0621  0.1486  -0.1157 230 ILE   A CB  
1536 C  CG1 . ILE   A 210 ? 1.3146 1.3270 1.2768 0.0473  0.1452  -0.1070 230 ILE   A CG1 
1537 C  CG2 . ILE   A 210 ? 1.3853 1.3202 1.2409 0.0570  0.1451  -0.1120 230 ILE   A CG2 
1538 C  CD1 . ILE   A 210 ? 1.3161 1.3507 1.3180 0.0534  0.1321  -0.1091 230 ILE   A CD1 
1539 N  N   . PRO   A 211 ? 1.4351 1.3217 1.2396 0.1070  0.1791  -0.1415 231 PRO   A N   
1540 C  CA  . PRO   A 211 ? 1.4728 1.3116 1.2056 0.1250  0.1928  -0.1503 231 PRO   A CA  
1541 C  C   . PRO   A 211 ? 1.5035 1.3513 1.2374 0.1400  0.2392  -0.1529 231 PRO   A C   
1542 O  O   . PRO   A 211 ? 1.6031 1.4141 1.2739 0.1530  0.2615  -0.1543 231 PRO   A O   
1543 C  CB  . PRO   A 211 ? 1.4624 1.2646 1.1710 0.1363  0.1642  -0.1648 231 PRO   A CB  
1544 C  CG  . PRO   A 211 ? 1.4343 1.2553 1.1889 0.1181  0.1319  -0.1588 231 PRO   A CG  
1545 C  CD  . PRO   A 211 ? 1.4290 1.3062 1.2475 0.1074  0.1471  -0.1465 231 PRO   A CD  
1546 N  N   . ILE   A 212 ? 1.3689 1.2638 1.1722 0.1403  0.2550  -0.1541 232 ILE   A N   
1547 C  CA  . ILE   A 212 ? 1.3769 1.2900 1.1984 0.1516  0.3025  -0.1571 232 ILE   A CA  
1548 C  C   . ILE   A 212 ? 1.3755 1.2943 1.1919 0.1381  0.3336  -0.1443 232 ILE   A C   
1549 O  O   . ILE   A 212 ? 1.4789 1.3678 1.2475 0.1497  0.3710  -0.1428 232 ILE   A O   
1550 C  CB  . ILE   A 212 ? 1.3286 1.2998 1.2384 0.1536  0.3067  -0.1630 232 ILE   A CB  
1551 C  CG1 . ILE   A 212 ? 1.3114 1.2684 1.2193 0.1698  0.2772  -0.1734 232 ILE   A CG1 
1552 C  CG2 . ILE   A 212 ? 1.3533 1.3510 1.2971 0.1631  0.3580  -0.1680 232 ILE   A CG2 
1553 C  CD1 . ILE   A 212 ? 1.3725 1.2788 1.2176 0.1942  0.2885  -0.1853 232 ILE   A CD1 
1554 N  N   . LEU   A 213 ? 1.3979 1.3507 1.2598 0.1146  0.3204  -0.1344 233 LEU   A N   
1555 C  CA  . LEU   A 213 ? 1.4416 1.3969 1.3022 0.1003  0.3490  -0.1219 233 LEU   A CA  
1556 C  C   . LEU   A 213 ? 1.5402 1.4342 1.3058 0.1059  0.3459  -0.1137 233 LEU   A C   
1557 O  O   . LEU   A 213 ? 1.6148 1.4834 1.3423 0.1102  0.3848  -0.1055 233 LEU   A O   
1558 C  CB  . LEU   A 213 ? 1.3685 1.3685 1.2932 0.0756  0.3304  -0.1153 233 LEU   A CB  
1559 C  CG  . LEU   A 213 ? 1.2707 1.3347 1.2901 0.0685  0.3246  -0.1233 233 LEU   A CG  
1560 C  CD1 . LEU   A 213 ? 1.2744 1.3643 1.3369 0.0820  0.3599  -0.1351 233 LEU   A CD1 
1561 C  CD2 . LEU   A 213 ? 1.2939 1.3654 1.3227 0.0708  0.2771  -0.1266 233 LEU   A CD2 
1562 N  N   . GLU   A 214 ? 1.4797 1.3482 1.2071 0.1069  0.3002  -0.1161 234 GLU   A N   
1563 C  CA  . GLU   A 214 ? 1.5270 1.3442 1.1727 0.1121  0.2878  -0.1104 234 GLU   A CA  
1564 C  C   . GLU   A 214 ? 1.5676 1.3315 1.1300 0.1380  0.3176  -0.1139 234 GLU   A C   
1565 O  O   . GLU   A 214 ? 1.6425 1.3695 1.1430 0.1441  0.3351  -0.1033 234 GLU   A O   
1566 C  CB  . GLU   A 214 ? 1.5522 1.3557 1.1834 0.1099  0.2332  -0.1177 234 GLU   A CB  
1567 C  CG  . GLU   A 214 ? 1.5484 1.3927 1.2426 0.0857  0.2058  -0.1102 234 GLU   A CG  
1568 C  CD  . GLU   A 214 ? 1.5864 1.4252 1.2634 0.0748  0.2025  -0.0970 234 GLU   A CD  
1569 O  OE1 . GLU   A 214 ? 1.5590 1.3771 1.1984 0.0809  0.2343  -0.0887 234 GLU   A OE1 
1570 O  OE2 . GLU   A 214 ? 1.5897 1.4428 1.2905 0.0612  0.1700  -0.0941 234 GLU   A OE2 
1571 N  N   . VAL   A 215 ? 1.6214 1.3768 1.1762 0.1559  0.3253  -0.1281 235 VAL   A N   
1572 C  CA  . VAL   A 215 ? 1.6617 1.3606 1.1279 0.1845  0.3503  -0.1342 235 VAL   A CA  
1573 C  C   . VAL   A 215 ? 1.7028 1.4109 1.1811 0.1874  0.4163  -0.1235 235 VAL   A C   
1574 O  O   . VAL   A 215 ? 1.8071 1.4707 1.2152 0.2113  0.4528  -0.1243 235 VAL   A O   
1575 C  CB  . VAL   A 215 ? 1.6282 1.3104 1.0799 0.2039  0.3340  -0.1550 235 VAL   A CB  
1576 C  CG1 . VAL   A 215 ? 1.6326 1.3582 1.1560 0.2068  0.3681  -0.1595 235 VAL   A CG1 
1577 C  CG2 . VAL   A 215 ? 1.7205 1.3302 1.0579 0.2346  0.3383  -0.1648 235 VAL   A CG2 
1578 N  N   . LEU   A 216 ? 1.5972 1.3627 1.1666 0.1628  0.4327  -0.1143 236 LEU   A N   
1579 C  CA  . LEU   A 216 ? 1.6480 1.4302 1.2500 0.1577  0.4947  -0.1042 236 LEU   A CA  
1580 C  C   . LEU   A 216 ? 1.7297 1.5027 1.3229 0.1398  0.5075  -0.0847 236 LEU   A C   
1581 O  O   . LEU   A 216 ? 1.7347 1.5211 1.3637 0.1301  0.5593  -0.0751 236 LEU   A O   
1582 C  CB  . LEU   A 216 ? 1.5183 1.3750 1.2403 0.1445  0.5060  -0.1129 236 LEU   A CB  
1583 C  CG  . LEU   A 216 ? 1.5093 1.3827 1.2596 0.1642  0.5310  -0.1282 236 LEU   A CG  
1584 C  CD1 . LEU   A 216 ? 1.5295 1.3658 1.2189 0.1874  0.4943  -0.1419 236 LEU   A CD1 
1585 C  CD2 . LEU   A 216 ? 1.3900 1.3437 1.2663 0.1493  0.5286  -0.1370 236 LEU   A CD2 
1586 N  N   . ASN   A 217 ? 1.7405 1.4907 1.2911 0.1352  0.4626  -0.0794 237 ASN   A N   
1587 C  CA  . ASN   A 217 ? 1.8147 1.5531 1.3531 0.1206  0.4670  -0.0615 237 ASN   A CA  
1588 C  C   . ASN   A 217 ? 1.7967 1.5980 1.4443 0.0897  0.4778  -0.0573 237 ASN   A C   
1589 O  O   . ASN   A 217 ? 1.8176 1.6105 1.4673 0.0765  0.4989  -0.0425 237 ASN   A O   
1590 C  CB  . ASN   A 217 ? 1.8289 1.5038 1.2788 0.1377  0.5168  -0.0460 237 ASN   A CB  
1591 C  CG  . ASN   A 217 ? 1.9834 1.6229 1.3825 0.1339  0.5041  -0.0289 237 ASN   A CG  
1592 O  OD1 . ASN   A 217 ? 2.0219 1.6873 1.4551 0.1181  0.4583  -0.0298 237 ASN   A OD1 
1593 N  ND2 . ASN   A 217 ? 2.0591 1.6362 1.3728 0.1509  0.5462  -0.0126 237 ASN   A ND2 
1594 N  N   . ILE   A 218 ? 1.7658 1.6273 1.5022 0.0796  0.4625  -0.0710 238 ILE   A N   
1595 C  CA  . ILE   A 218 ? 1.6733 1.5929 1.5050 0.0526  0.4544  -0.0708 238 ILE   A CA  
1596 C  C   . ILE   A 218 ? 1.7051 1.6206 1.5210 0.0425  0.4041  -0.0656 238 ILE   A C   
1597 O  O   . ILE   A 218 ? 1.6763 1.5734 1.4512 0.0529  0.3632  -0.0702 238 ILE   A O   
1598 C  CB  . ILE   A 218 ? 1.5447 1.5263 1.4666 0.0500  0.4462  -0.0878 238 ILE   A CB  
1599 C  CG1 . ILE   A 218 ? 1.4744 1.4800 1.4484 0.0511  0.5025  -0.0929 238 ILE   A CG1 
1600 C  CG2 . ILE   A 218 ? 1.5007 1.5343 1.4985 0.0284  0.4133  -0.0908 238 ILE   A CG2 
1601 C  CD1 . ILE   A 218 ? 1.4906 1.4590 1.4065 0.0775  0.5319  -0.0961 238 ILE   A CD1 
1602 N  N   . CYS   A 219 ? 1.7201 1.6517 1.5713 0.0221  0.4085  -0.0567 239 CYS   A N   
1603 C  CA  . CYS   A 219 ? 1.7480 1.6753 1.5857 0.0132  0.3675  -0.0505 239 CYS   A CA  
1604 C  C   . CYS   A 219 ? 1.7173 1.6960 1.6406 -0.0108 0.3631  -0.0524 239 CYS   A C   
1605 O  O   . CYS   A 219 ? 1.7713 1.7657 1.7396 -0.0230 0.4005  -0.0515 239 CYS   A O   
1606 C  CB  . CYS   A 219 ? 1.8110 1.6790 1.5654 0.0210  0.3774  -0.0347 239 CYS   A CB  
1607 S  SG  . CYS   A 219 ? 1.8801 1.7449 1.6246 0.0112  0.3333  -0.0267 239 CYS   A SG  
1608 N  N   . VAL   A 220 ? 1.6926 1.6956 1.6386 -0.0172 0.3186  -0.0559 240 VAL   A N   
1609 C  CA  . VAL   A 220 ? 1.6507 1.6982 1.6677 -0.0366 0.3098  -0.0591 240 VAL   A CA  
1610 C  C   . VAL   A 220 ? 1.6729 1.7018 1.6830 -0.0496 0.3299  -0.0479 240 VAL   A C   
1611 O  O   . VAL   A 220 ? 1.6335 1.6942 1.7034 -0.0667 0.3325  -0.0523 240 VAL   A O   
1612 C  CB  . VAL   A 220 ? 1.6108 1.6774 1.6380 -0.0379 0.2618  -0.0619 240 VAL   A CB  
1613 C  CG1 . VAL   A 220 ? 1.5950 1.6821 1.6412 -0.0268 0.2454  -0.0730 240 VAL   A CG1 
1614 C  CG2 . VAL   A 220 ? 1.6544 1.6815 1.6173 -0.0325 0.2391  -0.0516 240 VAL   A CG2 
1615 N  N   . PHE   A 221 ? 1.7079 1.6823 1.6428 -0.0401 0.3424  -0.0342 241 PHE   A N   
1616 C  CA  . PHE   A 221 ? 1.7763 1.7222 1.6949 -0.0486 0.3668  -0.0211 241 PHE   A CA  
1617 C  C   . PHE   A 221 ? 1.8201 1.7398 1.7265 -0.0465 0.4234  -0.0153 241 PHE   A C   
1618 O  O   . PHE   A 221 ? 1.8948 1.7726 1.7309 -0.0263 0.4374  -0.0096 241 PHE   A O   
1619 C  CB  . PHE   A 221 ? 1.8189 1.7184 1.6589 -0.0359 0.3429  -0.0086 241 PHE   A CB  
1620 C  CG  . PHE   A 221 ? 1.7746 1.6991 1.6287 -0.0377 0.2915  -0.0139 241 PHE   A CG  
1621 C  CD1 . PHE   A 221 ? 1.7364 1.6840 1.6312 -0.0528 0.2779  -0.0130 241 PHE   A CD1 
1622 C  CD2 . PHE   A 221 ? 1.7754 1.6979 1.6032 -0.0246 0.2596  -0.0202 241 PHE   A CD2 
1623 C  CE1 . PHE   A 221 ? 1.6861 1.6550 1.5933 -0.0537 0.2366  -0.0163 241 PHE   A CE1 
1624 C  CE2 . PHE   A 221 ? 1.7072 1.6511 1.5531 -0.0281 0.2183  -0.0238 241 PHE   A CE2 
1625 C  CZ  . PHE   A 221 ? 1.6595 1.6270 1.5444 -0.0421 0.2085  -0.0209 241 PHE   A CZ  
1626 N  N   . PRO   A 222 ? 1.9418 1.8844 1.9164 -0.0664 0.4583  -0.0181 242 PRO   A N   
1627 C  CA  . PRO   A 222 ? 2.0305 1.9487 2.0032 -0.0672 0.5200  -0.0116 242 PRO   A CA  
1628 C  C   . PRO   A 222 ? 2.2809 2.1201 2.1428 -0.0473 0.5448  0.0099  242 PRO   A C   
1629 O  O   . PRO   A 222 ? 2.2991 2.0984 2.1116 -0.0456 0.5365  0.0241  242 PRO   A O   
1630 C  CB  . PRO   A 222 ? 1.9666 1.9079 2.0196 -0.0954 0.5439  -0.0145 242 PRO   A CB  
1631 C  CG  . PRO   A 222 ? 1.8132 1.7987 1.9126 -0.1066 0.4899  -0.0265 242 PRO   A CG  
1632 C  CD  . PRO   A 222 ? 1.8164 1.8144 1.8822 -0.0886 0.4417  -0.0314 242 PRO   A CD  
1633 N  N   . ARG   A 223 ? 2.3672 2.1813 2.1856 -0.0290 0.5751  0.0117  243 ARG   A N   
1634 C  CA  . ARG   A 223 ? 2.4585 2.1938 2.1562 -0.0026 0.5925  0.0297  243 ARG   A CA  
1635 C  C   . ARG   A 223 ? 2.6444 2.3255 2.3102 -0.0073 0.6461  0.0516  243 ARG   A C   
1636 O  O   . ARG   A 223 ? 2.7216 2.3298 2.2770 0.0171  0.6573  0.0693  243 ARG   A O   
1637 C  CB  . ARG   A 223 ? 2.4649 2.1860 2.1240 0.0194  0.6151  0.0244  243 ARG   A CB  
1638 C  CG  . ARG   A 223 ? 2.5177 2.2347 2.2092 0.0133  0.6899  0.0292  243 ARG   A CG  
1639 C  CD  . ARG   A 223 ? 2.5653 2.2295 2.1633 0.0452  0.7202  0.0341  243 ARG   A CD  
1640 N  NE  . ARG   A 223 ? 2.5924 2.1748 2.0556 0.0719  0.7093  0.0514  243 ARG   A NE  
1641 C  CZ  . ARG   A 223 ? 2.6143 2.1432 1.9737 0.1058  0.7084  0.0530  243 ARG   A CZ  
1642 N  NH1 . ARG   A 223 ? 2.5197 2.0650 1.8907 0.1170  0.7201  0.0395  243 ARG   A NH1 
1643 N  NH2 . ARG   A 223 ? 2.6853 2.1432 1.9282 0.1306  0.6902  0.0668  243 ARG   A NH2 
1644 N  N   . GLU   A 224 ? 2.8758 2.5872 2.6332 -0.0368 0.6789  0.0502  244 GLU   A N   
1645 C  CA  . GLU   A 224 ? 2.9377 2.5941 2.6714 -0.0432 0.7279  0.0710  244 GLU   A CA  
1646 C  C   . GLU   A 224 ? 2.9061 2.5348 2.6084 -0.0472 0.7022  0.0824  244 GLU   A C   
1647 O  O   . GLU   A 224 ? 2.9088 2.4650 2.5310 -0.0337 0.7214  0.1045  244 GLU   A O   
1648 C  CB  . GLU   A 224 ? 2.9253 2.6253 2.7793 -0.0719 0.7576  0.0603  244 GLU   A CB  
1649 C  CG  . GLU   A 224 ? 2.8721 2.6522 2.8443 -0.1015 0.7308  0.0377  244 GLU   A CG  
1650 C  CD  . GLU   A 224 ? 2.9907 2.7992 3.0697 -0.1291 0.7549  0.0276  244 GLU   A CD  
1651 O  OE1 . GLU   A 224 ? 3.0014 2.7715 3.0694 -0.1265 0.7972  0.0382  244 GLU   A OE1 
1652 O  OE2 . GLU   A 224 ? 2.9698 2.8369 3.1420 -0.1523 0.7309  0.0080  244 GLU   A OE2 
1653 N  N   . VAL   A 225 ? 2.6230 2.3096 2.3907 -0.0624 0.6482  0.0660  245 VAL   A N   
1654 C  CA  . VAL   A 225 ? 2.5581 2.2242 2.2973 -0.0621 0.6131  0.0740  245 VAL   A CA  
1655 C  C   . VAL   A 225 ? 2.6312 2.2423 2.2500 -0.0274 0.5832  0.0868  245 VAL   A C   
1656 O  O   . VAL   A 225 ? 2.6700 2.2151 2.2121 -0.0131 0.5953  0.1070  245 VAL   A O   
1657 C  CB  . VAL   A 225 ? 2.3838 2.1236 2.2093 -0.0806 0.5605  0.0528  245 VAL   A CB  
1658 C  CG1 . VAL   A 225 ? 2.2776 1.9977 2.0776 -0.0798 0.5284  0.0604  245 VAL   A CG1 
1659 C  CG2 . VAL   A 225 ? 2.2376 2.0326 2.1806 -0.1115 0.5847  0.0360  245 VAL   A CG2 
1660 N  N   . THR   A 226 ? 2.5314 2.1666 2.1319 -0.0120 0.5442  0.0741  246 THR   A N   
1661 C  CA  . THR   A 226 ? 2.5496 2.1446 2.0520 0.0187  0.5035  0.0791  246 THR   A CA  
1662 C  C   . THR   A 226 ? 2.6484 2.1595 2.0361 0.0478  0.5408  0.0984  246 THR   A C   
1663 O  O   . THR   A 226 ? 2.6107 2.0692 1.9090 0.0731  0.5182  0.1094  246 THR   A O   
1664 C  CB  . THR   A 226 ? 2.4283 2.0658 1.9447 0.0257  0.4589  0.0591  246 THR   A CB  
1665 O  OG1 . THR   A 226 ? 2.4644 2.0807 1.9410 0.0415  0.4882  0.0572  246 THR   A OG1 
1666 C  CG2 . THR   A 226 ? 2.2835 2.0008 1.9150 -0.0024 0.4409  0.0416  246 THR   A CG2 
1667 N  N   . ASN   A 227 ? 2.9456 2.4421 2.3320 0.0472  0.5981  0.1023  247 ASN   A N   
1668 C  CA  . ASN   A 227 ? 3.0714 2.4812 2.3420 0.0762  0.6418  0.1233  247 ASN   A CA  
1669 C  C   . ASN   A 227 ? 3.1042 2.4585 2.3469 0.0733  0.6743  0.1475  247 ASN   A C   
1670 O  O   . ASN   A 227 ? 3.1907 2.4708 2.3317 0.1039  0.6767  0.1642  247 ASN   A O   
1671 C  CB  . ASN   A 227 ? 3.0679 2.4820 2.3592 0.0752  0.6932  0.1203  247 ASN   A CB  
1672 C  CG  . ASN   A 227 ? 3.1478 2.4887 2.3232 0.1136  0.7026  0.1310  247 ASN   A CG  
1673 O  OD1 . ASN   A 227 ? 3.1572 2.4779 2.2506 0.1424  0.6666  0.1232  247 ASN   A OD1 
1674 N  ND2 . ASN   A 227 ? 3.2175 2.5164 2.3859 0.1149  0.7500  0.1470  247 ASN   A ND2 
1675 N  N   . PHE   A 228 ? 2.8870 2.2798 2.2291 0.0381  0.6877  0.1458  248 PHE   A N   
1676 C  CA  . PHE   A 228 ? 2.8682 2.2137 2.1987 0.0339  0.7042  0.1641  248 PHE   A CA  
1677 C  C   . PHE   A 228 ? 2.8970 2.2109 2.1523 0.0543  0.6588  0.1728  248 PHE   A C   
1678 O  O   . PHE   A 228 ? 2.9893 2.2292 2.1575 0.0789  0.6652  0.1930  248 PHE   A O   
1679 C  CB  . PHE   A 228 ? 2.7321 2.1306 2.1948 -0.0093 0.7248  0.1542  248 PHE   A CB  
1680 C  CG  . PHE   A 228 ? 2.6296 2.0073 2.0998 -0.0200 0.7170  0.1634  248 PHE   A CG  
1681 C  CD1 . PHE   A 228 ? 2.6817 1.9811 2.0888 -0.0052 0.7398  0.1849  248 PHE   A CD1 
1682 C  CD2 . PHE   A 228 ? 2.4773 1.9165 2.0257 -0.0436 0.6818  0.1474  248 PHE   A CD2 
1683 C  CE1 . PHE   A 228 ? 2.5824 1.8611 1.9975 -0.0139 0.7333  0.1925  248 PHE   A CE1 
1684 C  CE2 . PHE   A 228 ? 2.4249 1.8462 1.9839 -0.0523 0.6719  0.1534  248 PHE   A CE2 
1685 C  CZ  . PHE   A 228 ? 2.4498 1.7865 1.9375 -0.0387 0.7046  0.1784  248 PHE   A CZ  
1686 N  N   . LEU   A 229 ? 2.7329 2.1139 2.0423 0.0472  0.5933  0.1515  249 LEU   A N   
1687 C  CA  . LEU   A 229 ? 2.7087 2.0763 1.9717 0.0667  0.5363  0.1531  249 LEU   A CA  
1688 C  C   . LEU   A 229 ? 2.8104 2.1229 1.9499 0.1106  0.5122  0.1587  249 LEU   A C   
1689 O  O   . LEU   A 229 ? 2.8350 2.0938 1.8953 0.1374  0.4936  0.1720  249 LEU   A O   
1690 C  CB  . LEU   A 229 ? 2.5278 1.9804 1.8803 0.0483  0.4778  0.1292  249 LEU   A CB  
1691 C  CG  . LEU   A 229 ? 2.4315 1.9307 1.8859 0.0142  0.4791  0.1229  249 LEU   A CG  
1692 C  CD1 . LEU   A 229 ? 2.4466 1.8866 1.8770 0.0116  0.5183  0.1436  249 LEU   A CD1 
1693 C  CD2 . LEU   A 229 ? 2.4032 1.9641 1.9568 -0.0162 0.5005  0.1065  249 LEU   A CD2 
1694 N  N   . ARG   A 230 ? 2.9053 2.2303 2.0270 0.1203  0.5091  0.1467  250 ARG   A N   
1695 C  CA  . ARG   A 230 ? 2.9086 2.1833 1.9141 0.1626  0.4814  0.1465  250 ARG   A CA  
1696 C  C   . ARG   A 230 ? 3.0871 2.2606 1.9693 0.1945  0.5209  0.1745  250 ARG   A C   
1697 O  O   . ARG   A 230 ? 3.0469 2.1746 1.8439 0.2273  0.4842  0.1807  250 ARG   A O   
1698 C  CB  . ARG   A 230 ? 2.8175 2.1148 1.8255 0.1657  0.4850  0.1297  250 ARG   A CB  
1699 C  CG  . ARG   A 230 ? 2.9226 2.1418 1.8082 0.2016  0.5208  0.1407  250 ARG   A CG  
1700 C  CD  . ARG   A 230 ? 2.7911 2.0345 1.6756 0.2091  0.5095  0.1192  250 ARG   A CD  
1701 N  NE  . ARG   A 230 ? 2.7828 2.0919 1.7804 0.1745  0.5418  0.1093  250 ARG   A NE  
1702 C  CZ  . ARG   A 230 ? 2.6021 1.9868 1.6897 0.1548  0.5026  0.0857  250 ARG   A CZ  
1703 N  NH1 . ARG   A 230 ? 2.3789 1.7855 1.4650 0.1618  0.4335  0.0698  250 ARG   A NH1 
1704 N  NH2 . ARG   A 230 ? 2.5667 2.0053 1.7494 0.1284  0.5342  0.0777  250 ARG   A NH2 
1705 N  N   . LYS   A 231 ? 3.5488 2.6940 2.4401 0.1839  0.5889  0.1892  251 LYS   A N   
1706 C  CA  . LYS   A 231 ? 3.6466 2.7099 2.4616 0.2098  0.6141  0.2105  251 LYS   A CA  
1707 C  C   . LYS   A 231 ? 3.6877 2.7256 2.5091 0.2039  0.6157  0.2266  251 LYS   A C   
1708 O  O   . LYS   A 231 ? 3.7532 2.7187 2.4892 0.2357  0.6152  0.2426  251 LYS   A O   
1709 C  CB  . LYS   A 231 ? 3.6687 2.7192 2.5165 0.1976  0.6782  0.2166  251 LYS   A CB  
1710 C  CG  . LYS   A 231 ? 3.5992 2.7002 2.5767 0.1495  0.7189  0.2150  251 LYS   A CG  
1711 C  CD  . LYS   A 231 ? 3.6451 2.7368 2.6579 0.1395  0.7783  0.2182  251 LYS   A CD  
1712 C  CE  . LYS   A 231 ? 3.6005 2.7363 2.7419 0.0941  0.8143  0.2146  251 LYS   A CE  
1713 N  NZ  . LYS   A 231 ? 3.6306 2.7266 2.7655 0.0893  0.8191  0.2291  251 LYS   A NZ  
1714 N  N   . SER   A 232 ? 3.2121 2.3064 2.1326 0.1655  0.6174  0.2216  252 SER   A N   
1715 C  CA  . SER   A 232 ? 3.0984 2.1702 2.0239 0.1612  0.6125  0.2345  252 SER   A CA  
1716 C  C   . SER   A 232 ? 3.0368 2.0863 1.8780 0.1969  0.5511  0.2362  252 SER   A C   
1717 O  O   . SER   A 232 ? 3.0943 2.0834 1.8708 0.2232  0.5440  0.2517  252 SER   A O   
1718 C  CB  . SER   A 232 ? 2.9247 2.0649 1.9760 0.1132  0.6226  0.2251  252 SER   A CB  
1719 O  OG  . SER   A 232 ? 2.8841 2.0443 2.0207 0.0816  0.6749  0.2213  252 SER   A OG  
1720 N  N   . VAL   A 233 ? 3.1668 2.2842 2.0456 0.1966  0.4897  0.2100  253 VAL   A N   
1721 C  CA  . VAL   A 233 ? 3.0926 2.2108 1.9282 0.2270  0.4183  0.2015  253 VAL   A CA  
1722 C  C   . VAL   A 233 ? 3.2737 2.3031 1.9576 0.2802  0.4128  0.2145  253 VAL   A C   
1723 O  O   . VAL   A 233 ? 3.3095 2.2943 1.9256 0.3126  0.3832  0.2239  253 VAL   A O   
1724 C  CB  . VAL   A 233 ? 2.8641 2.0724 1.7790 0.2126  0.3597  0.1698  253 VAL   A CB  
1725 C  CG1 . VAL   A 233 ? 2.7976 2.0032 1.6648 0.2462  0.2892  0.1589  253 VAL   A CG1 
1726 C  CG2 . VAL   A 233 ? 2.6985 1.9860 1.7483 0.1679  0.3568  0.1590  253 VAL   A CG2 
1727 N  N   . LYS   A 234 ? 3.1477 2.1498 1.7762 0.2925  0.4399  0.2139  254 LYS   A N   
1728 C  CA  . LYS   A 234 ? 3.1936 2.1257 1.7121 0.3402  0.4267  0.2176  254 LYS   A CA  
1729 C  C   . LYS   A 234 ? 3.3334 2.1923 1.8091 0.3552  0.4644  0.2428  254 LYS   A C   
1730 O  O   . LYS   A 234 ? 3.4474 2.2442 1.8262 0.4001  0.4427  0.2473  254 LYS   A O   
1731 C  CB  . LYS   A 234 ? 3.2224 2.1487 1.7205 0.3452  0.4503  0.2088  254 LYS   A CB  
1732 C  CG  . LYS   A 234 ? 3.1690 2.1633 1.7125 0.3286  0.4240  0.1830  254 LYS   A CG  
1733 C  CD  . LYS   A 234 ? 3.0179 2.0186 1.5063 0.3599  0.3454  0.1604  254 LYS   A CD  
1734 C  CE  . LYS   A 234 ? 2.8140 1.8997 1.4119 0.3314  0.2931  0.1418  254 LYS   A CE  
1735 N  NZ  . LYS   A 234 ? 2.7090 1.8406 1.3273 0.3372  0.2286  0.1090  254 LYS   A NZ  
1736 N  N   . ARG   A 235 ? 3.3123 2.1761 1.8594 0.3194  0.5194  0.2569  255 ARG   A N   
1737 C  CA  . ARG   A 235 ? 3.3866 2.1797 1.8966 0.3322  0.5536  0.2792  255 ARG   A CA  
1738 C  C   . ARG   A 235 ? 3.4266 2.2106 1.9215 0.3458  0.5124  0.2844  255 ARG   A C   
1739 O  O   . ARG   A 235 ? 3.4631 2.1786 1.8802 0.3817  0.5087  0.2973  255 ARG   A O   
1740 C  CB  . ARG   A 235 ? 3.3739 2.1743 1.9710 0.2889  0.6254  0.2887  255 ARG   A CB  
1741 C  CG  . ARG   A 235 ? 3.3153 2.1414 1.9939 0.2555  0.6328  0.2930  255 ARG   A CG  
1742 C  CD  . ARG   A 235 ? 3.2968 2.0864 2.0155 0.2336  0.6996  0.3066  255 ARG   A CD  
1743 N  NE  . ARG   A 235 ? 3.2646 2.0928 2.0652 0.1986  0.7463  0.2983  255 ARG   A NE  
1744 C  CZ  . ARG   A 235 ? 3.1491 2.0462 2.0739 0.1505  0.7615  0.2857  255 ARG   A CZ  
1745 N  NH1 . ARG   A 235 ? 3.0456 1.9791 2.0262 0.1295  0.7367  0.2804  255 ARG   A NH1 
1746 N  NH2 . ARG   A 235 ? 3.1436 2.0738 2.1390 0.1244  0.8012  0.2769  255 ARG   A NH2 
1747 N  N   . MET   A 236 ? 3.3200 2.1712 1.8863 0.3203  0.4808  0.2742  256 MET   A N   
1748 C  CA  . MET   A 236 ? 3.3451 2.1928 1.9040 0.3334  0.4399  0.2787  256 MET   A CA  
1749 C  C   . MET   A 236 ? 3.3895 2.2291 1.8694 0.3815  0.3663  0.2671  256 MET   A C   
1750 O  O   . MET   A 236 ? 3.4836 2.2873 1.9172 0.4135  0.3366  0.2736  256 MET   A O   
1751 C  CB  . MET   A 236 ? 3.1569 2.0855 1.8333 0.2889  0.4293  0.2678  256 MET   A CB  
1752 C  CG  . MET   A 236 ? 3.1217 2.0742 1.8899 0.2384  0.4941  0.2711  256 MET   A CG  
1753 S  SD  . MET   A 236 ? 3.0868 2.1719 2.0236 0.1878  0.4585  0.2366  256 MET   A SD  
1754 C  CE  . MET   A 236 ? 3.0034 2.1025 2.0206 0.1399  0.5365  0.2394  256 MET   A CE  
1755 N  N   . LYS   A 237 ? 3.3840 2.2595 1.8544 0.3871  0.3341  0.2468  257 LYS   A N   
1756 C  CA  . LYS   A 237 ? 3.4011 2.2705 1.8034 0.4322  0.2621  0.2297  257 LYS   A CA  
1757 C  C   . LYS   A 237 ? 3.6074 2.3927 1.9080 0.4793  0.2658  0.2397  257 LYS   A C   
1758 O  O   . LYS   A 237 ? 3.6512 2.4165 1.9073 0.5167  0.2160  0.2359  257 LYS   A O   
1759 C  CB  . LYS   A 237 ? 3.2737 2.1840 1.6799 0.4287  0.2381  0.2052  257 LYS   A CB  
1760 C  CG  . LYS   A 237 ? 3.0213 2.0403 1.5679 0.3835  0.2100  0.1796  257 LYS   A CG  
1761 C  CD  . LYS   A 237 ? 2.8776 1.9316 1.4309 0.3813  0.1873  0.1538  257 LYS   A CD  
1762 C  CE  . LYS   A 237 ? 2.8832 1.9156 1.3553 0.4281  0.1178  0.1345  257 LYS   A CE  
1763 N  NZ  . LYS   A 237 ? 2.7561 1.8350 1.2596 0.4196  0.0866  0.1039  257 LYS   A NZ  
1764 N  N   . GLU   A 238 ? 3.7907 2.5264 2.0559 0.4793  0.3252  0.2519  258 GLU   A N   
1765 C  CA  . GLU   A 238 ? 3.9227 2.5726 2.0822 0.5261  0.3336  0.2616  258 GLU   A CA  
1766 C  C   . GLU   A 238 ? 3.9917 2.5815 2.1341 0.5295  0.3782  0.2876  258 GLU   A C   
1767 O  O   . GLU   A 238 ? 4.1521 2.6646 2.2015 0.5710  0.3864  0.2973  258 GLU   A O   
1768 C  CB  . GLU   A 238 ? 4.0474 2.6670 2.1680 0.5301  0.3745  0.2618  258 GLU   A CB  
1769 C  CG  . GLU   A 238 ? 4.2220 2.7993 2.2396 0.5836  0.3300  0.2475  258 GLU   A CG  
1770 C  CD  . GLU   A 238 ? 4.3302 2.8821 2.3128 0.5872  0.3678  0.2465  258 GLU   A CD  
1771 O  OE1 . GLU   A 238 ? 4.3450 2.9236 2.3937 0.5461  0.4240  0.2540  258 GLU   A OE1 
1772 O  OE2 . GLU   A 238 ? 4.4358 2.9420 2.3274 0.6321  0.3403  0.2369  258 GLU   A OE2 
1773 N  N   . SER   A 239 ? 3.7271 2.3471 1.9546 0.4881  0.4076  0.2981  259 SER   A N   
1774 C  CA  . SER   A 239 ? 3.7099 2.2760 1.9246 0.4930  0.4385  0.3190  259 SER   A CA  
1775 C  C   . SER   A 239 ? 3.6709 2.2443 1.8721 0.5190  0.3765  0.3149  259 SER   A C   
1776 O  O   . SER   A 239 ? 3.6478 2.1572 1.7811 0.5553  0.3743  0.3258  259 SER   A O   
1777 C  CB  . SER   A 239 ? 3.6223 2.2134 1.9381 0.4369  0.4994  0.3296  259 SER   A CB  
1778 O  OG  . SER   A 239 ? 3.4656 2.1273 1.8663 0.4073  0.4685  0.3210  259 SER   A OG  
1779 N  N   . ARG   A 240 ? 3.5446 2.1956 1.8110 0.5024  0.3263  0.2989  260 ARG   A N   
1780 C  CA  . ARG   A 240 ? 3.5095 2.1762 1.7732 0.5285  0.2626  0.2924  260 ARG   A CA  
1781 C  C   . ARG   A 240 ? 3.5843 2.2376 1.7700 0.5822  0.1970  0.2741  260 ARG   A C   
1782 O  O   . ARG   A 240 ? 3.6175 2.2740 1.7908 0.6131  0.1441  0.2673  260 ARG   A O   
1783 C  CB  . ARG   A 240 ? 3.3407 2.0942 1.7024 0.4946  0.2309  0.2811  260 ARG   A CB  
1784 C  CG  . ARG   A 240 ? 3.3272 2.1413 1.7006 0.4971  0.1777  0.2550  260 ARG   A CG  
1785 C  CD  . ARG   A 240 ? 3.1609 2.0611 1.6239 0.4896  0.1110  0.2320  260 ARG   A CD  
1786 N  NE  . ARG   A 240 ? 3.0506 2.0121 1.6422 0.4375  0.1372  0.2306  260 ARG   A NE  
1787 C  CZ  . ARG   A 240 ? 2.9671 1.9496 1.6110 0.4368  0.1189  0.2308  260 ARG   A CZ  
1788 N  NH1 . ARG   A 240 ? 2.9979 1.9548 1.5897 0.4838  0.0711  0.2309  260 ARG   A NH1 
1789 N  NH2 . ARG   A 240 ? 2.8757 1.9061 1.6261 0.3899  0.1476  0.2293  260 ARG   A NH2 
1790 N  N   . LEU   A 241 ? 3.6928 2.3345 1.8324 0.5937  0.1975  0.2634  261 LEU   A N   
1791 C  CA  . LEU   A 241 ? 3.7191 2.3354 1.7768 0.6461  0.1423  0.2449  261 LEU   A CA  
1792 C  C   . LEU   A 241 ? 3.7664 2.2869 1.7255 0.6737  0.1945  0.2627  261 LEU   A C   
1793 O  O   . LEU   A 241 ? 3.8599 2.3621 1.7902 0.6707  0.2245  0.2618  261 LEU   A O   
1794 C  CB  . LEU   A 241 ? 3.7166 2.3908 1.7960 0.6406  0.0983  0.2161  261 LEU   A CB  
1795 C  CG  . LEU   A 241 ? 3.6524 2.4229 1.8306 0.6112  0.0494  0.1964  261 LEU   A CG  
1796 C  CD1 . LEU   A 241 ? 3.5284 2.3408 1.7149 0.6082  0.0137  0.1676  261 LEU   A CD1 
1797 C  CD2 . LEU   A 241 ? 3.6377 2.4339 1.8364 0.6359  -0.0161 0.1854  261 LEU   A CD2 
1798 N  N   . GLU   A 242 ? 3.7824 2.2398 1.6883 0.7023  0.2061  0.2790  262 GLU   A N   
1799 C  CA  . GLU   A 242 ? 3.7164 2.1830 1.6381 0.7179  0.1673  0.2792  262 GLU   A CA  
1800 C  C   . GLU   A 242 ? 3.6565 2.0938 1.6101 0.6911  0.2286  0.3074  262 GLU   A C   
1801 O  O   . GLU   A 242 ? 3.7354 2.1223 1.6717 0.6744  0.3015  0.3274  262 GLU   A O   
1802 C  CB  . GLU   A 242 ? 3.7744 2.1838 1.5933 0.7829  0.1235  0.2706  262 GLU   A CB  
1803 C  CG  . GLU   A 242 ? 3.7532 2.1659 1.5776 0.8083  0.0804  0.2689  262 GLU   A CG  
1804 C  CD  . GLU   A 242 ? 3.8466 2.1999 1.5655 0.8739  0.0401  0.2589  262 GLU   A CD  
1805 O  OE1 . GLU   A 242 ? 3.8919 2.1862 1.5230 0.8999  0.0574  0.2591  262 GLU   A OE1 
1806 O  OE2 . GLU   A 242 ? 3.7910 2.1566 1.5152 0.9009  -0.0090 0.2502  262 GLU   A OE2 
1807 N  N   . ASP   A 243 ? 3.6233 2.0936 1.6289 0.6868  0.1989  0.3071  263 ASP   A N   
1808 C  CA  . ASP   A 243 ? 3.5489 1.9887 1.5832 0.6657  0.2494  0.3307  263 ASP   A CA  
1809 C  C   . ASP   A 243 ? 3.4977 1.9359 1.5286 0.6962  0.2030  0.3291  263 ASP   A C   
1810 O  O   . ASP   A 243 ? 3.5264 1.9541 1.4992 0.7454  0.1464  0.3151  263 ASP   A O   
1811 C  CB  . ASP   A 243 ? 3.4689 1.9684 1.6151 0.6023  0.2841  0.3346  263 ASP   A CB  
1812 C  CG  . ASP   A 243 ? 3.4159 2.0061 1.6418 0.5890  0.2223  0.3159  263 ASP   A CG  
1813 O  OD1 . ASP   A 243 ? 3.4463 2.0667 1.6503 0.6215  0.1537  0.2950  263 ASP   A OD1 
1814 O  OD2 . ASP   A 243 ? 3.2739 1.9052 1.5874 0.5460  0.2422  0.3207  263 ASP   A OD2 
1815 N  N   . VAL   A 249 ? 2.7419 1.9336 1.7403 0.3830  0.0460  0.1949  269 VAL   A N   
1816 C  CA  . VAL   A 249 ? 2.6919 1.9609 1.8065 0.3535  0.0370  0.1793  269 VAL   A CA  
1817 C  C   . VAL   A 249 ? 2.6096 1.9410 1.8062 0.3002  0.0611  0.1667  269 VAL   A C   
1818 O  O   . VAL   A 249 ? 2.5250 1.9184 1.8144 0.2711  0.0611  0.1543  269 VAL   A O   
1819 C  CB  . VAL   A 249 ? 2.6671 1.8904 1.7787 0.3567  0.0659  0.1955  269 VAL   A CB  
1820 C  CG1 . VAL   A 249 ? 2.6616 1.8400 1.7670 0.3215  0.1328  0.2113  269 VAL   A CG1 
1821 C  CG2 . VAL   A 249 ? 2.4898 1.7866 1.7025 0.3450  0.0420  0.1779  269 VAL   A CG2 
1822 N  N   . ASP   A 250 ? 2.6522 1.9658 1.8108 0.2907  0.0809  0.1696  270 ASP   A N   
1823 C  CA  . ASP   A 250 ? 2.5842 1.9478 1.8102 0.2445  0.1063  0.1596  270 ASP   A CA  
1824 C  C   . ASP   A 250 ? 2.4729 1.8927 1.7218 0.2423  0.0691  0.1393  270 ASP   A C   
1825 O  O   . ASP   A 250 ? 2.4119 1.8237 1.6154 0.2760  0.0271  0.1330  270 ASP   A O   
1826 C  CB  . ASP   A 250 ? 2.6593 1.9617 1.8384 0.2300  0.1669  0.1780  270 ASP   A CB  
1827 C  CG  . ASP   A 250 ? 2.6961 1.9167 1.7531 0.2684  0.1739  0.1953  270 ASP   A CG  
1828 O  OD1 . ASP   A 250 ? 2.6867 1.9195 1.7091 0.2913  0.1346  0.1844  270 ASP   A OD1 
1829 O  OD2 . ASP   A 250 ? 2.7925 1.9331 1.7861 0.2760  0.2201  0.2194  270 ASP   A OD2 
1830 N  N   . PHE   A 251 ? 2.4426 1.9178 1.7635 0.2027  0.0839  0.1276  271 PHE   A N   
1831 C  CA  . PHE   A 251 ? 2.3617 1.8892 1.7120 0.1955  0.0540  0.1085  271 PHE   A CA  
1832 C  C   . PHE   A 251 ? 2.4073 1.8858 1.6651 0.2235  0.0462  0.1112  271 PHE   A C   
1833 O  O   . PHE   A 251 ? 2.3357 1.8395 1.5922 0.2375  0.0022  0.0942  271 PHE   A O   
1834 C  CB  . PHE   A 251 ? 2.2659 1.8420 1.6886 0.1523  0.0807  0.1005  271 PHE   A CB  
1835 C  CG  . PHE   A 251 ? 2.1317 1.7697 1.6484 0.1271  0.0752  0.0909  271 PHE   A CG  
1836 C  CD1 . PHE   A 251 ? 1.9773 1.6702 1.5456 0.1304  0.0335  0.0761  271 PHE   A CD1 
1837 C  CD2 . PHE   A 251 ? 2.1447 1.7857 1.6992 0.1000  0.1126  0.0952  271 PHE   A CD2 
1838 C  CE1 . PHE   A 251 ? 1.8133 1.5583 1.4602 0.1098  0.0327  0.0687  271 PHE   A CE1 
1839 C  CE2 . PHE   A 251 ? 1.9510 1.6442 1.5816 0.0806  0.1066  0.0853  271 PHE   A CE2 
1840 C  CZ  . PHE   A 251 ? 1.7476 1.4911 1.4205 0.0864  0.0684  0.0734  271 PHE   A CZ  
1841 N  N   . LEU   A 252 ? 2.6421 2.0479 1.8217 0.2321  0.0900  0.1315  272 LEU   A N   
1842 C  CA  . LEU   A 252 ? 2.6044 1.9557 1.6845 0.2611  0.0890  0.1356  272 LEU   A CA  
1843 C  C   . LEU   A 252 ? 2.6681 1.9807 1.6705 0.3113  0.0420  0.1355  272 LEU   A C   
1844 O  O   . LEU   A 252 ? 2.6401 1.9501 1.5993 0.3346  0.0049  0.1214  272 LEU   A O   
1845 C  CB  . LEU   A 252 ? 2.6212 1.9020 1.6393 0.2574  0.1551  0.1598  272 LEU   A CB  
1846 C  CG  . LEU   A 252 ? 2.6277 1.8267 1.5173 0.2949  0.1681  0.1728  272 LEU   A CG  
1847 C  CD1 . LEU   A 252 ? 2.5773 1.8037 1.4545 0.3020  0.1361  0.1514  272 LEU   A CD1 
1848 C  CD2 . LEU   A 252 ? 2.8000 1.9421 1.6566 0.2804  0.2443  0.1965  272 LEU   A CD2 
1849 N  N   . GLN   A 253 ? 2.7496 2.0301 1.7322 0.3303  0.0407  0.1493  273 GLN   A N   
1850 C  CA  . GLN   A 253 ? 2.7985 2.0496 1.7168 0.3807  -0.0102 0.1468  273 GLN   A CA  
1851 C  C   . GLN   A 253 ? 2.7670 2.0980 1.7556 0.3822  -0.0763 0.1151  273 GLN   A C   
1852 O  O   . GLN   A 253 ? 2.8212 2.1378 1.7558 0.4207  -0.1254 0.1027  273 GLN   A O   
1853 C  CB  . GLN   A 253 ? 2.8024 2.0219 1.7139 0.3960  -0.0030 0.1636  273 GLN   A CB  
1854 C  CG  . GLN   A 253 ? 2.8422 2.0348 1.6934 0.4516  -0.0588 0.1603  273 GLN   A CG  
1855 C  CD  . GLN   A 253 ? 2.8780 2.0514 1.7400 0.4653  -0.0556 0.1736  273 GLN   A CD  
1856 O  OE1 . GLN   A 253 ? 2.9184 2.0273 1.7398 0.4612  -0.0033 0.1997  273 GLN   A OE1 
1857 N  NE2 . GLN   A 253 ? 2.7999 2.0298 1.7220 0.4807  -0.1099 0.1548  273 GLN   A NE2 
1858 N  N   . LEU   A 254 ? 2.5785 1.9923 1.6877 0.3409  -0.0779 0.1009  274 LEU   A N   
1859 C  CA  . LEU   A 254 ? 2.4970 1.9872 1.6844 0.3381  -0.1337 0.0724  274 LEU   A CA  
1860 C  C   . LEU   A 254 ? 2.5078 2.0152 1.6900 0.3307  -0.1503 0.0540  274 LEU   A C   
1861 O  O   . LEU   A 254 ? 2.4686 2.0072 1.6690 0.3461  -0.2048 0.0302  274 LEU   A O   
1862 C  CB  . LEU   A 254 ? 2.3047 1.8693 1.6141 0.2993  -0.1247 0.0664  274 LEU   A CB  
1863 C  CG  . LEU   A 254 ? 2.2486 1.7941 1.5665 0.3007  -0.0993 0.0840  274 LEU   A CG  
1864 C  CD1 . LEU   A 254 ? 1.9990 1.6200 1.4323 0.2702  -0.1000 0.0738  274 LEU   A CD1 
1865 C  CD2 . LEU   A 254 ? 2.2929 1.7905 1.5435 0.3508  -0.1285 0.0908  274 LEU   A CD2 
1866 N  N   . MET   A 255 ? 2.4543 1.9422 1.6156 0.3078  -0.1049 0.0630  275 MET   A N   
1867 C  CA  . MET   A 255 ? 2.4452 1.9345 1.5826 0.3071  -0.1166 0.0476  275 MET   A CA  
1868 C  C   . MET   A 255 ? 2.5105 1.9197 1.5148 0.3535  -0.1272 0.0522  275 MET   A C   
1869 O  O   . MET   A 255 ? 2.5518 1.9601 1.5274 0.3651  -0.1561 0.0330  275 MET   A O   
1870 C  CB  . MET   A 255 ? 2.3615 1.8624 1.5289 0.2682  -0.0644 0.0541  275 MET   A CB  
1871 C  CG  . MET   A 255 ? 2.2638 1.8316 1.5458 0.2248  -0.0463 0.0528  275 MET   A CG  
1872 S  SD  . MET   A 255 ? 2.0522 1.6246 1.3552 0.1880  0.0123  0.0598  275 MET   A SD  
1873 C  CE  . MET   A 255 ? 1.8186 1.4441 1.2253 0.1504  0.0349  0.0643  275 MET   A CE  
1874 N  N   . ILE   A 256 ? 2.6730 2.0104 1.5910 0.3813  -0.1033 0.0773  276 ILE   A N   
1875 C  CA  . ILE   A 256 ? 2.7861 2.0391 1.5646 0.4307  -0.1121 0.0841  276 ILE   A CA  
1876 C  C   . ILE   A 256 ? 2.8484 2.1063 1.6031 0.4739  -0.1879 0.0635  276 ILE   A C   
1877 O  O   . ILE   A 256 ? 2.8775 2.0960 1.5439 0.5108  -0.2207 0.0513  276 ILE   A O   
1878 C  CB  . ILE   A 256 ? 2.8260 1.9923 1.5159 0.4456  -0.0538 0.1209  276 ILE   A CB  
1879 C  CG1 . ILE   A 256 ? 2.8733 1.9579 1.4368 0.4699  -0.0211 0.1335  276 ILE   A CG1 
1880 C  CG2 . ILE   A 256 ? 2.8642 1.9921 1.5066 0.4866  -0.0816 0.1313  276 ILE   A CG2 
1881 C  CD1 . ILE   A 256 ? 2.7864 1.8991 1.3924 0.4304  0.0200  0.1289  276 ILE   A CD1 
1882 N  N   . ASP   A 257 ? 2.7846 2.0928 1.6198 0.4709  -0.2182 0.0569  277 ASP   A N   
1883 C  CA  . ASP   A 257 ? 2.8063 2.1328 1.6413 0.5092  -0.2925 0.0337  277 ASP   A CA  
1884 C  C   . ASP   A 257 ? 2.7522 2.1596 1.6814 0.4893  -0.3417 -0.0042 277 ASP   A C   
1885 O  O   . ASP   A 257 ? 2.7667 2.1868 1.6900 0.5214  -0.4076 -0.0302 277 ASP   A O   
1886 C  CB  . ASP   A 257 ? 2.8480 2.1967 1.7358 0.5160  -0.3024 0.0416  277 ASP   A CB  
1887 C  CG  . ASP   A 257 ? 2.8857 2.1508 1.6859 0.5342  -0.2527 0.0790  277 ASP   A CG  
1888 O  OD1 . ASP   A 257 ? 2.8956 2.0729 1.5667 0.5639  -0.2316 0.0964  277 ASP   A OD1 
1889 O  OD2 . ASP   A 257 ? 2.8242 2.1080 1.6833 0.5190  -0.2325 0.0911  277 ASP   A OD2 
1890 N  N   . SER   A 258 ? 2.6780 2.1381 1.6944 0.4378  -0.3119 -0.0085 278 SER   A N   
1891 C  CA  . SER   A 258 ? 2.6355 2.1662 1.7418 0.4163  -0.3526 -0.0421 278 SER   A CA  
1892 C  C   . SER   A 258 ? 2.7063 2.1993 1.7329 0.4372  -0.3766 -0.0603 278 SER   A C   
1893 O  O   . SER   A 258 ? 2.7017 2.2232 1.7541 0.4501  -0.4374 -0.0933 278 SER   A O   
1894 C  CB  . SER   A 258 ? 2.4604 2.0514 1.6751 0.3588  -0.3119 -0.0387 278 SER   A CB  
1895 O  OG  . SER   A 258 ? 2.4704 2.0218 1.6351 0.3422  -0.2543 -0.0192 278 SER   A OG  
1896 N  N   . GLN   A 259 ? 2.7673 2.1963 1.6998 0.4406  -0.3290 -0.0410 279 GLN   A N   
1897 C  CA  . GLN   A 259 ? 2.8040 2.1882 1.6473 0.4639  -0.3454 -0.0563 279 GLN   A CA  
1898 C  C   . GLN   A 259 ? 2.9374 2.2561 1.6590 0.5268  -0.3908 -0.0615 279 GLN   A C   
1899 O  O   . GLN   A 259 ? 3.0054 2.2891 1.6504 0.5556  -0.4234 -0.0821 279 GLN   A O   
1900 C  CB  . GLN   A 259 ? 2.8090 2.1457 1.5916 0.4495  -0.2747 -0.0326 279 GLN   A CB  
1901 C  CG  . GLN   A 259 ? 2.7990 2.0780 1.5188 0.4570  -0.2152 0.0070  279 GLN   A CG  
1902 C  CD  . GLN   A 259 ? 2.7763 2.0138 1.4480 0.4416  -0.1447 0.0272  279 GLN   A CD  
1903 O  OE1 . GLN   A 259 ? 2.7189 1.9314 1.3845 0.4277  -0.0855 0.0568  279 GLN   A OE1 
1904 N  NE2 . GLN   A 259 ? 2.7232 1.9537 1.3649 0.4438  -0.1504 0.0096  279 GLN   A NE2 
1905 N  N   . LYS   A 268 ? 2.5590 2.1165 1.6744 0.3806  -0.5540 -0.2656 288 LYS   A N   
1906 C  CA  . LYS   A 268 ? 2.4328 2.0668 1.6874 0.3414  -0.5457 -0.2575 288 LYS   A CA  
1907 C  C   . LYS   A 268 ? 2.4999 2.1287 1.7371 0.3414  -0.4973 -0.2162 288 LYS   A C   
1908 O  O   . LYS   A 268 ? 2.4131 2.0867 1.7358 0.3034  -0.4576 -0.1969 288 LYS   A O   
1909 C  CB  . LYS   A 268 ? 2.3805 2.0615 1.7142 0.3486  -0.6166 -0.2917 288 LYS   A CB  
1910 C  CG  . LYS   A 268 ? 2.2801 2.0344 1.7436 0.3187  -0.6087 -0.2813 288 LYS   A CG  
1911 C  CD  . LYS   A 268 ? 2.1077 1.9130 1.6849 0.2643  -0.5738 -0.2776 288 LYS   A CD  
1912 C  CE  . LYS   A 268 ? 1.9791 1.8594 1.6924 0.2395  -0.5835 -0.2805 288 LYS   A CE  
1913 N  NZ  . LYS   A 268 ? 2.0209 1.9286 1.7818 0.2585  -0.6557 -0.3198 288 LYS   A NZ  
1914 N  N   . ALA   A 269 ? 2.9277 2.4972 2.0497 0.3856  -0.5007 -0.2032 289 ALA   A N   
1915 C  CA  . ALA   A 269 ? 2.9302 2.4819 2.0238 0.3879  -0.4524 -0.1640 289 ALA   A CA  
1916 C  C   . ALA   A 269 ? 2.9528 2.4751 2.0096 0.3668  -0.3786 -0.1355 289 ALA   A C   
1917 O  O   . ALA   A 269 ? 2.9329 2.4428 1.9720 0.3573  -0.3660 -0.1451 289 ALA   A O   
1918 C  CB  . ALA   A 269 ? 3.0206 2.5091 1.9958 0.4438  -0.4762 -0.1572 289 ALA   A CB  
1919 N  N   . LEU   A 270 ? 2.7071 2.2188 1.7562 0.3601  -0.3299 -0.1017 290 LEU   A N   
1920 C  CA  . LEU   A 270 ? 2.5690 2.0669 1.6105 0.3342  -0.2597 -0.0764 290 LEU   A CA  
1921 C  C   . LEU   A 270 ? 2.5920 2.0118 1.5040 0.3627  -0.2340 -0.0692 290 LEU   A C   
1922 O  O   . LEU   A 270 ? 2.7155 2.0727 1.5171 0.4081  -0.2528 -0.0677 290 LEU   A O   
1923 C  CB  . LEU   A 270 ? 2.5203 2.0203 1.5822 0.3224  -0.2171 -0.0451 290 LEU   A CB  
1924 C  CG  . LEU   A 270 ? 2.4331 1.9954 1.6092 0.2726  -0.1814 -0.0366 290 LEU   A CG  
1925 C  CD1 . LEU   A 270 ? 2.4385 1.9805 1.6045 0.2639  -0.1275 -0.0053 290 LEU   A CD1 
1926 C  CD2 . LEU   A 270 ? 2.2957 1.8766 1.5014 0.2464  -0.1618 -0.0460 290 LEU   A CD2 
1927 N  N   . SER   A 271 ? 2.6488 2.0714 1.5731 0.3382  -0.1903 -0.0650 291 SER   A N   
1928 C  CA  . SER   A 271 ? 2.6606 2.0137 1.4746 0.3591  -0.1486 -0.0529 291 SER   A CA  
1929 C  C   . SER   A 271 ? 2.6646 1.9938 1.4640 0.3478  -0.0781 -0.0162 291 SER   A C   
1930 O  O   . SER   A 271 ? 2.6142 1.9875 1.4992 0.3179  -0.0613 -0.0037 291 SER   A O   
1931 C  CB  . SER   A 271 ? 2.5845 1.9537 1.4225 0.3412  -0.1395 -0.0705 291 SER   A CB  
1932 O  OG  . SER   A 271 ? 2.5975 1.9234 1.3752 0.3434  -0.0752 -0.0509 291 SER   A OG  
1933 N  N   . ASP   A 272 ? 2.6632 1.9195 1.3525 0.3722  -0.0349 0.0003  292 ASP   A N   
1934 C  CA  . ASP   A 272 ? 2.6356 1.8592 1.3043 0.3643  0.0338  0.0351  292 ASP   A CA  
1935 C  C   . ASP   A 272 ? 2.4740 1.7495 1.2438 0.3161  0.0846  0.0412  292 ASP   A C   
1936 O  O   . ASP   A 272 ? 2.4287 1.7239 1.2563 0.2909  0.1176  0.0594  292 ASP   A O   
1937 C  CB  . ASP   A 272 ? 2.7671 1.8927 1.2861 0.4060  0.0693  0.0522  292 ASP   A CB  
1938 C  CG  . ASP   A 272 ? 2.7929 1.9021 1.2743 0.4094  0.0920  0.0410  292 ASP   A CG  
1939 O  OD1 . ASP   A 272 ? 2.7281 1.8979 1.2914 0.3846  0.0692  0.0165  292 ASP   A OD1 
1940 O  OD2 . ASP   A 272 ? 2.8714 1.9050 1.2431 0.4376  0.1352  0.0575  292 ASP   A OD2 
1941 N  N   . LEU   A 273 ? 2.4375 1.7344 1.2291 0.3047  0.0895  0.0247  293 LEU   A N   
1942 C  CA  . LEU   A 273 ? 2.3605 1.7117 1.2522 0.2624  0.1300  0.0271  293 LEU   A CA  
1943 C  C   . LEU   A 273 ? 2.2737 1.7060 1.2899 0.2283  0.0962  0.0156  293 LEU   A C   
1944 O  O   . LEU   A 273 ? 2.1553 1.6289 1.2534 0.1955  0.1273  0.0250  293 LEU   A O   
1945 C  CB  . LEU   A 273 ? 2.3969 1.7451 1.2728 0.2645  0.1428  0.0123  293 LEU   A CB  
1946 C  CG  . LEU   A 273 ? 2.2568 1.6400 1.2031 0.2332  0.1971  0.0172  293 LEU   A CG  
1947 C  CD1 . LEU   A 273 ? 2.1164 1.5835 1.1923 0.1953  0.1744  0.0037  293 LEU   A CD1 
1948 C  CD2 . LEU   A 273 ? 2.2008 1.5594 1.1408 0.2246  0.2631  0.0456  293 LEU   A CD2 
1949 N  N   . GLU   A 274 ? 2.3642 1.8193 1.3967 0.2363  0.0333  -0.0058 294 GLU   A N   
1950 C  CA  . GLU   A 274 ? 2.2814 1.8067 1.4242 0.2080  0.0029  -0.0144 294 GLU   A CA  
1951 C  C   . GLU   A 274 ? 2.2102 1.7437 1.3826 0.1974  0.0226  0.0066  294 GLU   A C   
1952 O  O   . GLU   A 274 ? 2.1348 1.7198 1.3976 0.1649  0.0368  0.0101  294 GLU   A O   
1953 C  CB  . GLU   A 274 ? 2.3301 1.8671 1.4748 0.2241  -0.0652 -0.0386 294 GLU   A CB  
1954 C  CG  . GLU   A 274 ? 2.3382 1.9121 1.5369 0.2090  -0.0933 -0.0645 294 GLU   A CG  
1955 C  CD  . GLU   A 274 ? 2.4611 1.9879 1.5787 0.2312  -0.0915 -0.0771 294 GLU   A CD  
1956 O  OE1 . GLU   A 274 ? 2.5444 2.0137 1.5690 0.2540  -0.0566 -0.0622 294 GLU   A OE1 
1957 O  OE2 . GLU   A 274 ? 2.4772 2.0214 1.6230 0.2262  -0.1232 -0.1019 294 GLU   A OE2 
1958 N  N   . LEU   A 275 ? 2.2442 1.7223 1.3350 0.2273  0.0235  0.0205  295 LEU   A N   
1959 C  CA  . LEU   A 275 ? 2.1775 1.6531 1.2868 0.2212  0.0419  0.0405  295 LEU   A CA  
1960 C  C   . LEU   A 275 ? 2.0527 1.5282 1.1922 0.1938  0.1068  0.0589  295 LEU   A C   
1961 O  O   . LEU   A 275 ? 1.9417 1.4443 1.1434 0.1720  0.1203  0.0675  295 LEU   A O   
1962 C  CB  . LEU   A 275 ? 2.2760 1.6811 1.2778 0.2643  0.0303  0.0522  295 LEU   A CB  
1963 C  CG  . LEU   A 275 ? 2.2503 1.6225 1.2331 0.2696  0.0567  0.0773  295 LEU   A CG  
1964 C  CD1 . LEU   A 275 ? 2.4228 1.7716 1.3570 0.3076  0.0060  0.0745  295 LEU   A CD1 
1965 C  CD2 . LEU   A 275 ? 2.3171 1.6150 1.2131 0.2808  0.1177  0.1015  295 LEU   A CD2 
1966 N  N   . VAL   A 276 ? 2.1447 1.5917 1.2450 0.1946  0.1470  0.0631  296 VAL   A N   
1967 C  CA  . VAL   A 276 ? 2.0576 1.5143 1.2031 0.1660  0.2069  0.0759  296 VAL   A CA  
1968 C  C   . VAL   A 276 ? 1.9364 1.4743 1.2005 0.1286  0.1989  0.0613  296 VAL   A C   
1969 O  O   . VAL   A 276 ? 1.8361 1.4005 1.1653 0.1015  0.2293  0.0679  296 VAL   A O   
1970 C  CB  . VAL   A 276 ? 2.1356 1.5444 1.2134 0.1785  0.2529  0.0826  296 VAL   A CB  
1971 C  CG1 . VAL   A 276 ? 2.1615 1.5881 1.3011 0.1472  0.3144  0.0923  296 VAL   A CG1 
1972 C  CG2 . VAL   A 276 ? 2.3302 1.6500 1.2787 0.2189  0.2641  0.0999  296 VAL   A CG2 
1973 N  N   . ALA   A 277 ? 1.8460 1.4213 1.1384 0.1275  0.1572  0.0407  297 ALA   A N   
1974 C  CA  . ALA   A 277 ? 1.6944 1.3390 1.0884 0.0959  0.1510  0.0286  297 ALA   A CA  
1975 C  C   . ALA   A 277 ? 1.5947 1.2815 1.0565 0.0797  0.1282  0.0287  297 ALA   A C   
1976 O  O   . ALA   A 277 ? 1.5125 1.2454 1.0510 0.0530  0.1399  0.0269  297 ALA   A O   
1977 C  CB  . ALA   A 277 ? 1.6936 1.3565 1.0929 0.1003  0.1178  0.0082  297 ALA   A CB  
1978 N  N   . GLN   A 278 ? 1.7348 1.4071 1.1690 0.0977  0.0948  0.0296  298 GLN   A N   
1979 C  CA  . GLN   A 278 ? 1.6226 1.3333 1.1194 0.0848  0.0766  0.0301  298 GLN   A CA  
1980 C  C   . GLN   A 278 ? 1.6020 1.2990 1.1072 0.0745  0.1148  0.0469  298 GLN   A C   
1981 O  O   . GLN   A 278 ? 1.5387 1.2755 1.1120 0.0536  0.1162  0.0460  298 GLN   A O   
1982 C  CB  . GLN   A 278 ? 1.6269 1.3290 1.0982 0.1089  0.0300  0.0245  298 GLN   A CB  
1983 C  CG  . GLN   A 278 ? 1.6739 1.3737 1.1201 0.1246  -0.0087 0.0060  298 GLN   A CG  
1984 C  CD  . GLN   A 278 ? 1.6058 1.3522 1.1174 0.1005  -0.0140 -0.0086 298 GLN   A CD  
1985 O  OE1 . GLN   A 278 ? 1.5279 1.3234 1.1186 0.0758  -0.0125 -0.0096 298 GLN   A OE1 
1986 N  NE2 . GLN   A 278 ? 1.6354 1.3618 1.1084 0.1100  -0.0192 -0.0196 298 GLN   A NE2 
1987 N  N   . SER   A 279 ? 1.6881 1.3248 1.1220 0.0896  0.1471  0.0622  299 SER   A N   
1988 C  CA  . SER   A 279 ? 1.6363 1.2521 1.0779 0.0784  0.1876  0.0780  299 SER   A CA  
1989 C  C   . SER   A 279 ? 1.6131 1.2745 1.1369 0.0435  0.2160  0.0724  299 SER   A C   
1990 O  O   . SER   A 279 ? 1.5976 1.2755 1.1702 0.0259  0.2274  0.0747  299 SER   A O   
1991 C  CB  . SER   A 279 ? 1.8262 1.3647 1.1753 0.0994  0.2250  0.0963  299 SER   A CB  
1992 O  OG  . SER   A 279 ? 1.9380 1.4329 1.2002 0.1369  0.1939  0.0982  299 SER   A OG  
1993 N  N   . ILE   A 280 ? 1.6159 1.2980 1.1558 0.0354  0.2249  0.0631  300 ILE   A N   
1994 C  CA  . ILE   A 280 ? 1.5098 1.2348 1.1256 0.0065  0.2501  0.0561  300 ILE   A CA  
1995 C  C   . ILE   A 280 ? 1.3925 1.1794 1.0842 -0.0104 0.2184  0.0434  300 ILE   A C   
1996 O  O   . ILE   A 280 ? 1.3782 1.1945 1.1299 -0.0315 0.2320  0.0398  300 ILE   A O   
1997 C  CB  . ILE   A 280 ? 1.4944 1.2223 1.1028 0.0073  0.2677  0.0496  300 ILE   A CB  
1998 C  CG1 . ILE   A 280 ? 1.5773 1.2379 1.1025 0.0265  0.3046  0.0641  300 ILE   A CG1 
1999 C  CG2 . ILE   A 280 ? 1.4998 1.2754 1.1907 -0.0194 0.2906  0.0404  300 ILE   A CG2 
2000 C  CD1 . ILE   A 280 ? 1.6559 1.3136 1.1653 0.0315  0.3254  0.0582  300 ILE   A CD1 
2001 N  N   . ILE   A 281 ? 1.5063 1.3121 1.1964 -0.0009 0.1764  0.0357  301 ILE   A N   
2002 C  CA  . ILE   A 281 ? 1.4624 1.3200 1.2172 -0.0145 0.1502  0.0268  301 ILE   A CA  
2003 C  C   . ILE   A 281 ? 1.4808 1.3367 1.2505 -0.0178 0.1509  0.0334  301 ILE   A C   
2004 O  O   . ILE   A 281 ? 1.5363 1.4245 1.3601 -0.0352 0.1558  0.0289  301 ILE   A O   
2005 C  CB  . ILE   A 281 ? 1.3712 1.2435 1.1226 -0.0041 0.1092  0.0182  301 ILE   A CB  
2006 C  CG1 . ILE   A 281 ? 1.3772 1.2546 1.1238 -0.0038 0.1084  0.0090  301 ILE   A CG1 
2007 C  CG2 . ILE   A 281 ? 1.3563 1.2742 1.1686 -0.0159 0.0875  0.0131  301 ILE   A CG2 
2008 C  CD1 . ILE   A 281 ? 1.3984 1.3166 1.2044 -0.0235 0.1205  0.0026  301 ILE   A CD1 
2009 N  N   . PHE   A 282 ? 1.3480 1.1635 1.0660 0.0016  0.1445  0.0431  302 PHE   A N   
2010 C  CA  . PHE   A 282 ? 1.4265 1.2357 1.1543 0.0023  0.1441  0.0494  302 PHE   A CA  
2011 C  C   . PHE   A 282 ? 1.4662 1.2642 1.2145 -0.0154 0.1830  0.0539  302 PHE   A C   
2012 O  O   . PHE   A 282 ? 1.4532 1.2738 1.2465 -0.0281 0.1828  0.0498  302 PHE   A O   
2013 C  CB  . PHE   A 282 ? 1.4999 1.2608 1.1606 0.0310  0.1314  0.0597  302 PHE   A CB  
2014 C  CG  . PHE   A 282 ? 1.4550 1.2354 1.1140 0.0477  0.0855  0.0512  302 PHE   A CG  
2015 C  CD1 . PHE   A 282 ? 1.4354 1.2537 1.1247 0.0405  0.0643  0.0377  302 PHE   A CD1 
2016 C  CD2 . PHE   A 282 ? 1.5648 1.3247 1.1957 0.0711  0.0634  0.0558  302 PHE   A CD2 
2017 C  CE1 . PHE   A 282 ? 1.4029 1.2393 1.0998 0.0531  0.0232  0.0278  302 PHE   A CE1 
2018 C  CE2 . PHE   A 282 ? 1.5885 1.3711 1.2287 0.0859  0.0199  0.0449  302 PHE   A CE2 
2019 C  CZ  . PHE   A 282 ? 1.5574 1.3789 1.2335 0.0752  0.0004  0.0303  302 PHE   A CZ  
2020 N  N   . ILE   A 283 ? 1.5214 1.2834 1.2384 -0.0165 0.2179  0.0610  303 ILE   A N   
2021 C  CA  . ILE   A 283 ? 1.4805 1.2297 1.2238 -0.0355 0.2580  0.0639  303 ILE   A CA  
2022 C  C   . ILE   A 283 ? 1.4292 1.2380 1.2551 -0.0609 0.2550  0.0468  303 ILE   A C   
2023 O  O   . ILE   A 283 ? 1.4805 1.2974 1.3445 -0.0745 0.2617  0.0423  303 ILE   A O   
2024 C  CB  . ILE   A 283 ? 1.5022 1.2093 1.2071 -0.0339 0.2997  0.0734  303 ILE   A CB  
2025 C  CG1 . ILE   A 283 ? 1.6634 1.2969 1.2776 -0.0072 0.3105  0.0934  303 ILE   A CG1 
2026 C  CG2 . ILE   A 283 ? 1.5409 1.2532 1.3007 -0.0606 0.3407  0.0699  303 ILE   A CG2 
2027 C  CD1 . ILE   A 283 ? 1.7928 1.3802 1.3564 -0.0008 0.3527  0.1044  303 ILE   A CD1 
2028 N  N   . PHE   A 284 ? 1.4540 1.3024 1.3048 -0.0653 0.2432  0.0361  304 PHE   A N   
2029 C  CA  . PHE   A 284 ? 1.3815 1.2834 1.3031 -0.0846 0.2379  0.0201  304 PHE   A CA  
2030 C  C   . PHE   A 284 ? 1.4505 1.3797 1.3967 -0.0851 0.2083  0.0149  304 PHE   A C   
2031 O  O   . PHE   A 284 ? 1.4669 1.4121 1.4528 -0.0979 0.2122  0.0067  304 PHE   A O   
2032 C  CB  . PHE   A 284 ? 1.3450 1.2784 1.2815 -0.0848 0.2294  0.0114  304 PHE   A CB  
2033 C  CG  . PHE   A 284 ? 1.3767 1.3627 1.3776 -0.0988 0.2185  -0.0045 304 PHE   A CG  
2034 C  CD1 . PHE   A 284 ? 1.3638 1.3680 1.4115 -0.1138 0.2410  -0.0152 304 PHE   A CD1 
2035 C  CD2 . PHE   A 284 ? 1.3790 1.3951 1.3941 -0.0956 0.1863  -0.0090 304 PHE   A CD2 
2036 C  CE1 . PHE   A 284 ? 1.3710 1.4223 1.4734 -0.1223 0.2262  -0.0316 304 PHE   A CE1 
2037 C  CE2 . PHE   A 284 ? 1.3957 1.4532 1.4585 -0.1040 0.1762  -0.0221 304 PHE   A CE2 
2038 C  CZ  . PHE   A 284 ? 1.4091 1.4842 1.5131 -0.1158 0.1935  -0.0341 304 PHE   A CZ  
2039 N  N   . ALA   A 285 ? 1.3417 1.2774 1.2673 -0.0711 0.1789  0.0180  305 ALA   A N   
2040 C  CA  . ALA   A 285 ? 1.2606 1.2231 1.2102 -0.0700 0.1544  0.0144  305 ALA   A CA  
2041 C  C   . ALA   A 285 ? 1.2869 1.2332 1.2416 -0.0724 0.1638  0.0164  305 ALA   A C   
2042 O  O   . ALA   A 285 ? 1.3226 1.2934 1.3150 -0.0826 0.1623  0.0068  305 ALA   A O   
2043 C  CB  . ALA   A 285 ? 1.2444 1.2050 1.1691 -0.0534 0.1272  0.0192  305 ALA   A CB  
2044 N  N   . GLY   A 286 ? 1.3260 1.2263 1.2382 -0.0609 0.1736  0.0283  306 GLY   A N   
2045 C  CA  . GLY   A 286 ? 1.3645 1.2407 1.2773 -0.0619 0.1851  0.0310  306 GLY   A CA  
2046 C  C   . GLY   A 286 ? 1.4337 1.3077 1.3804 -0.0832 0.2124  0.0225  306 GLY   A C   
2047 O  O   . GLY   A 286 ? 1.4357 1.2946 1.3931 -0.0872 0.2196  0.0201  306 GLY   A O   
2048 N  N   . TYR   A 287 ? 1.4247 1.3135 1.3924 -0.0964 0.2272  0.0162  307 TYR   A N   
2049 C  CA  . TYR   A 287 ? 1.3963 1.2882 1.4079 -0.1179 0.2523  0.0046  307 TYR   A CA  
2050 C  C   . TYR   A 287 ? 1.3428 1.2893 1.4105 -0.1292 0.2332  -0.0163 307 TYR   A C   
2051 O  O   . TYR   A 287 ? 1.3464 1.2984 1.4372 -0.1348 0.2273  -0.0268 307 TYR   A O   
2052 C  CB  . TYR   A 287 ? 1.4229 1.3014 1.4334 -0.1255 0.2831  0.0079  307 TYR   A CB  
2053 C  CG  . TYR   A 287 ? 1.4070 1.3023 1.4813 -0.1498 0.3060  -0.0086 307 TYR   A CG  
2054 C  CD1 . TYR   A 287 ? 1.4497 1.3123 1.5385 -0.1622 0.3296  -0.0096 307 TYR   A CD1 
2055 C  CD2 . TYR   A 287 ? 1.3467 1.2907 1.4706 -0.1598 0.3022  -0.0249 307 TYR   A CD2 
2056 C  CE1 . TYR   A 287 ? 1.3881 1.2686 1.5449 -0.1864 0.3483  -0.0285 307 TYR   A CE1 
2057 C  CE2 . TYR   A 287 ? 1.3490 1.3140 1.5398 -0.1811 0.3190  -0.0436 307 TYR   A CE2 
2058 C  CZ  . TYR   A 287 ? 1.3719 1.3064 1.5819 -0.1956 0.3417  -0.0464 307 TYR   A CZ  
2059 O  OH  . TYR   A 287 ? 1.3537 1.3115 1.6395 -0.2188 0.3566  -0.0686 307 TYR   A OH  
2060 N  N   . GLU   A 288 ? 1.3098 1.2929 1.3950 -0.1303 0.2234  -0.0228 308 GLU   A N   
2061 C  CA  . GLU   A 288 ? 1.2600 1.2907 1.3930 -0.1379 0.2063  -0.0423 308 GLU   A CA  
2062 C  C   . GLU   A 288 ? 1.2601 1.3052 1.3864 -0.1284 0.1795  -0.0440 308 GLU   A C   
2063 O  O   . GLU   A 288 ? 1.2645 1.3234 1.4164 -0.1335 0.1723  -0.0587 308 GLU   A O   
2064 C  CB  . GLU   A 288 ? 1.2697 1.3305 1.4140 -0.1359 0.2003  -0.0459 308 GLU   A CB  
2065 C  CG  . GLU   A 288 ? 1.3013 1.4046 1.5007 -0.1451 0.1931  -0.0679 308 GLU   A CG  
2066 C  CD  . GLU   A 288 ? 1.3268 1.4548 1.5342 -0.1394 0.1644  -0.0779 308 GLU   A CD  
2067 O  OE1 . GLU   A 288 ? 1.2794 1.4057 1.4549 -0.1269 0.1482  -0.0666 308 GLU   A OE1 
2068 O  OE2 . GLU   A 288 ? 1.3513 1.4996 1.5974 -0.1468 0.1586  -0.0982 308 GLU   A OE2 
2069 N  N   . THR   A 289 ? 1.2725 1.3140 1.3657 -0.1141 0.1652  -0.0303 309 THR   A N   
2070 C  CA  . THR   A 289 ? 1.2156 1.2747 1.3080 -0.1053 0.1441  -0.0309 309 THR   A CA  
2071 C  C   . THR   A 289 ? 1.2267 1.2675 1.3178 -0.1045 0.1478  -0.0336 309 THR   A C   
2072 O  O   . THR   A 289 ? 1.1995 1.2576 1.3049 -0.1037 0.1380  -0.0444 309 THR   A O   
2073 C  CB  . THR   A 289 ? 1.1546 1.2122 1.2214 -0.0923 0.1310  -0.0170 309 THR   A CB  
2074 O  OG1 . THR   A 289 ? 1.1355 1.1595 1.1736 -0.0837 0.1353  -0.0058 309 THR   A OG1 
2075 C  CG2 . THR   A 289 ? 1.1467 1.2096 1.2072 -0.0926 0.1304  -0.0144 309 THR   A CG2 
2076 N  N   . THR   A 290 ? 1.2994 1.3007 1.3681 -0.1025 0.1624  -0.0237 310 THR   A N   
2077 C  CA  . THR   A 290 ? 1.2624 1.2402 1.3270 -0.0998 0.1666  -0.0254 310 THR   A CA  
2078 C  C   . THR   A 290 ? 1.1976 1.1789 1.2961 -0.1155 0.1747  -0.0452 310 THR   A C   
2079 O  O   . THR   A 290 ? 1.1398 1.1277 1.2470 -0.1129 0.1654  -0.0566 310 THR   A O   
2080 C  CB  . THR   A 290 ? 1.2590 1.1870 1.2877 -0.0923 0.1818  -0.0093 310 THR   A CB  
2081 O  OG1 . THR   A 290 ? 1.3003 1.2266 1.2984 -0.0773 0.1704  0.0051  310 THR   A OG1 
2082 C  CG2 . THR   A 290 ? 1.2988 1.2023 1.3186 -0.0836 0.1817  -0.0089 310 THR   A CG2 
2083 N  N   . SER   A 291 ? 1.2303 1.2078 1.3505 -0.1314 0.1920  -0.0514 311 SER   A N   
2084 C  CA  . SER   A 291 ? 1.2079 1.1889 1.3701 -0.1483 0.1991  -0.0736 311 SER   A CA  
2085 C  C   . SER   A 291 ? 1.1461 1.1752 1.3380 -0.1487 0.1747  -0.0947 311 SER   A C   
2086 O  O   . SER   A 291 ? 1.1662 1.1999 1.3795 -0.1531 0.1665  -0.1154 311 SER   A O   
2087 C  CB  . SER   A 291 ? 1.2812 1.2482 1.4676 -0.1660 0.2277  -0.0746 311 SER   A CB  
2088 O  OG  . SER   A 291 ? 1.3133 1.3139 1.5135 -0.1673 0.2248  -0.0754 311 SER   A OG  
2089 N  N   . SER   A 292 ? 1.1034 1.1645 1.2928 -0.1421 0.1619  -0.0906 312 SER   A N   
2090 C  CA  . SER   A 292 ? 1.0978 1.1990 1.3072 -0.1385 0.1389  -0.1084 312 SER   A CA  
2091 C  C   . SER   A 292 ? 1.0619 1.1643 1.2469 -0.1237 0.1217  -0.1097 312 SER   A C   
2092 O  O   . SER   A 292 ? 1.0567 1.1742 1.2534 -0.1212 0.1067  -0.1302 312 SER   A O   
2093 C  CB  . SER   A 292 ? 1.1185 1.2458 1.3258 -0.1330 0.1316  -0.1010 312 SER   A CB  
2094 O  OG  . SER   A 292 ? 1.1486 1.3109 1.3780 -0.1293 0.1120  -0.1193 312 SER   A OG  
2095 N  N   . VAL   A 293 ? 1.0671 1.1540 1.2186 -0.1123 0.1237  -0.0894 313 VAL   A N   
2096 C  CA  . VAL   A 293 ? 1.0541 1.1427 1.1857 -0.0977 0.1131  -0.0890 313 VAL   A CA  
2097 C  C   . VAL   A 293 ? 1.0568 1.1207 1.1892 -0.0992 0.1177  -0.1017 313 VAL   A C   
2098 O  O   . VAL   A 293 ? 1.0689 1.1385 1.1956 -0.0908 0.1070  -0.1159 313 VAL   A O   
2099 C  CB  . VAL   A 293 ? 1.0628 1.1476 1.1708 -0.0860 0.1139  -0.0658 313 VAL   A CB  
2100 C  CG1 . VAL   A 293 ? 1.0295 1.1150 1.1232 -0.0715 0.1096  -0.0650 313 VAL   A CG1 
2101 C  CG2 . VAL   A 293 ? 0.9044 1.0125 1.0129 -0.0846 0.1068  -0.0569 313 VAL   A CG2 
2102 N  N   . LEU   A 294 ? 1.1518 1.1829 1.2865 -0.1080 0.1348  -0.0968 314 LEU   A N   
2103 C  CA  . LEU   A 294 ? 1.1560 1.1568 1.2926 -0.1105 0.1412  -0.1091 314 LEU   A CA  
2104 C  C   . LEU   A 294 ? 1.1425 1.1555 1.3115 -0.1220 0.1324  -0.1400 314 LEU   A C   
2105 O  O   . LEU   A 294 ? 1.1289 1.1255 1.2969 -0.1197 0.1284  -0.1569 314 LEU   A O   
2106 C  CB  . LEU   A 294 ? 1.0808 1.0383 1.2125 -0.1184 0.1642  -0.0964 314 LEU   A CB  
2107 C  CG  . LEU   A 294 ? 1.0729 1.0053 1.1671 -0.1011 0.1687  -0.0719 314 LEU   A CG  
2108 C  CD1 . LEU   A 294 ? 1.1396 1.0277 1.2198 -0.1063 0.1911  -0.0567 314 LEU   A CD1 
2109 C  CD2 . LEU   A 294 ? 1.0697 0.9872 1.1513 -0.0873 0.1640  -0.0774 314 LEU   A CD2 
2110 N  N   . SER   A 295 ? 1.0156 1.0576 1.2150 -0.1331 0.1276  -0.1499 315 SER   A N   
2111 C  CA  . SER   A 295 ? 1.0143 1.0753 1.2509 -0.1419 0.1134  -0.1827 315 SER   A CA  
2112 C  C   . SER   A 295 ? 1.0112 1.0972 1.2262 -0.1224 0.0858  -0.1950 315 SER   A C   
2113 O  O   . SER   A 295 ? 0.9992 1.0831 1.2194 -0.1197 0.0708  -0.2218 315 SER   A O   
2114 C  CB  . SER   A 295 ? 1.0951 1.1816 1.3773 -0.1583 0.1180  -0.1900 315 SER   A CB  
2115 O  OG  . SER   A 295 ? 1.1756 1.2352 1.4681 -0.1734 0.1488  -0.1741 315 SER   A OG  
2116 N  N   . PHE   A 296 ? 1.0082 1.1139 1.1962 -0.1080 0.0794  -0.1763 316 PHE   A N   
2117 C  CA  . PHE   A 296 ? 1.0401 1.1606 1.1969 -0.0867 0.0596  -0.1817 316 PHE   A CA  
2118 C  C   . PHE   A 296 ? 1.0392 1.1345 1.1637 -0.0737 0.0614  -0.1837 316 PHE   A C   
2119 O  O   . PHE   A 296 ? 0.9701 1.0665 1.0765 -0.0603 0.0450  -0.2038 316 PHE   A O   
2120 C  CB  . PHE   A 296 ? 1.0905 1.2269 1.2245 -0.0758 0.0605  -0.1560 316 PHE   A CB  
2121 C  CG  . PHE   A 296 ? 1.0340 1.1973 1.1913 -0.0813 0.0532  -0.1580 316 PHE   A CG  
2122 C  CD1 . PHE   A 296 ? 1.0353 1.2202 1.2129 -0.0793 0.0328  -0.1843 316 PHE   A CD1 
2123 C  CD2 . PHE   A 296 ? 1.0182 1.1851 1.1771 -0.0861 0.0646  -0.1355 316 PHE   A CD2 
2124 C  CE1 . PHE   A 296 ? 1.0678 1.2791 1.2697 -0.0817 0.0260  -0.1867 316 PHE   A CE1 
2125 C  CE2 . PHE   A 296 ? 1.0425 1.2320 1.2214 -0.0892 0.0592  -0.1378 316 PHE   A CE2 
2126 C  CZ  . PHE   A 296 ? 1.0603 1.2729 1.2621 -0.0867 0.0409  -0.1627 316 PHE   A CZ  
2127 N  N   . ILE   A 297 ? 1.0214 1.0924 1.1356 -0.0747 0.0802  -0.1639 317 ILE   A N   
2128 C  CA  . ILE   A 297 ? 1.0517 1.0994 1.1377 -0.0602 0.0845  -0.1641 317 ILE   A CA  
2129 C  C   . ILE   A 297 ? 1.0563 1.0838 1.1514 -0.0646 0.0774  -0.1953 317 ILE   A C   
2130 O  O   . ILE   A 297 ? 1.0662 1.0872 1.1342 -0.0480 0.0675  -0.2103 317 ILE   A O   
2131 C  CB  . ILE   A 297 ? 1.0579 1.0842 1.1382 -0.0599 0.1034  -0.1391 317 ILE   A CB  
2132 C  CG1 . ILE   A 297 ? 1.0109 1.0584 1.0815 -0.0519 0.1060  -0.1126 317 ILE   A CG1 
2133 C  CG2 . ILE   A 297 ? 1.0944 1.0928 1.1546 -0.0463 0.1091  -0.1438 317 ILE   A CG2 
2134 C  CD1 . ILE   A 297 ? 1.0256 1.0568 1.0903 -0.0462 0.1181  -0.0914 317 ILE   A CD1 
2135 N  N   . MET   A 298 ? 1.0201 1.0345 1.1530 -0.0869 0.0840  -0.2061 318 MET   A N   
2136 C  CA  . MET   A 298 ? 1.0508 1.0421 1.2006 -0.0947 0.0788  -0.2372 318 MET   A CA  
2137 C  C   . MET   A 298 ? 1.0638 1.0809 1.2281 -0.0931 0.0504  -0.2719 318 MET   A C   
2138 O  O   . MET   A 298 ? 1.0486 1.0490 1.2159 -0.0921 0.0382  -0.3023 318 MET   A O   
2139 C  CB  . MET   A 298 ? 1.0799 1.0452 1.2693 -0.1206 0.0995  -0.2367 318 MET   A CB  
2140 C  CG  . MET   A 298 ? 1.1444 1.0694 1.3093 -0.1165 0.1239  -0.2089 318 MET   A CG  
2141 S  SD  . MET   A 298 ? 1.2703 1.1514 1.4079 -0.1019 0.1242  -0.2226 318 MET   A SD  
2142 C  CE  . MET   A 298 ? 1.2204 1.0825 1.3179 -0.0817 0.1413  -0.1829 318 MET   A CE  
2143 N  N   . TYR   A 299 ? 1.0660 1.1217 1.2382 -0.0908 0.0374  -0.2697 319 TYR   A N   
2144 C  CA  . TYR   A 299 ? 1.0727 1.1522 1.2413 -0.0783 0.0055  -0.2994 319 TYR   A CA  
2145 C  C   . TYR   A 299 ? 1.1242 1.1908 1.2274 -0.0480 -0.0040 -0.2995 319 TYR   A C   
2146 O  O   . TYR   A 299 ? 1.1676 1.2236 1.2564 -0.0372 -0.0243 -0.3310 319 TYR   A O   
2147 C  CB  . TYR   A 299 ? 1.1078 1.2274 1.2908 -0.0772 -0.0049 -0.2924 319 TYR   A CB  
2148 C  CG  . TYR   A 299 ? 1.1556 1.2969 1.3154 -0.0543 -0.0389 -0.3148 319 TYR   A CG  
2149 C  CD1 . TYR   A 299 ? 1.1588 1.3202 1.3609 -0.0594 -0.0671 -0.3551 319 TYR   A CD1 
2150 C  CD2 . TYR   A 299 ? 1.1882 1.3286 1.2843 -0.0262 -0.0427 -0.2960 319 TYR   A CD2 
2151 C  CE1 . TYR   A 299 ? 1.2084 1.3875 1.3829 -0.0336 -0.1026 -0.3766 319 TYR   A CE1 
2152 C  CE2 . TYR   A 299 ? 1.2254 1.3779 1.2891 -0.0012 -0.0724 -0.3140 319 TYR   A CE2 
2153 C  CZ  . TYR   A 299 ? 1.2631 1.4345 1.3626 -0.0031 -0.1045 -0.3545 319 TYR   A CZ  
2154 O  OH  . TYR   A 299 ? 1.4083 1.5893 1.4686 0.0266  -0.1380 -0.3729 319 TYR   A OH  
2155 N  N   . GLU   A 300 ? 1.1434 1.2095 1.2073 -0.0336 0.0116  -0.2652 320 GLU   A N   
2156 C  CA  . GLU   A 300 ? 1.1664 1.2212 1.1694 -0.0044 0.0099  -0.2609 320 GLU   A CA  
2157 C  C   . GLU   A 300 ? 1.1984 1.2178 1.1843 0.0016  0.0163  -0.2746 320 GLU   A C   
2158 O  O   . GLU   A 300 ? 1.2297 1.2360 1.1732 0.0237  0.0035  -0.2940 320 GLU   A O   
2159 C  CB  . GLU   A 300 ? 1.0498 1.1124 1.0305 0.0043  0.0307  -0.2211 320 GLU   A CB  
2160 C  CG  . GLU   A 300 ? 1.0923 1.1843 1.0790 0.0035  0.0242  -0.2074 320 GLU   A CG  
2161 C  CD  . GLU   A 300 ? 1.1111 1.2118 1.0635 0.0249  0.0000  -0.2245 320 GLU   A CD  
2162 O  OE1 . GLU   A 300 ? 1.1457 1.2282 1.0543 0.0460  -0.0075 -0.2397 320 GLU   A OE1 
2163 O  OE2 . GLU   A 300 ? 1.1390 1.2626 1.1044 0.0232  -0.0123 -0.2232 320 GLU   A OE2 
2164 N  N   . LEU   A 301 ? 1.1642 1.1635 1.1773 -0.0153 0.0361  -0.2649 321 LEU   A N   
2165 C  CA  . LEU   A 301 ? 1.1962 1.1576 1.1945 -0.0091 0.0429  -0.2778 321 LEU   A CA  
2166 C  C   . LEU   A 301 ? 1.2960 1.2436 1.3089 -0.0153 0.0203  -0.3222 321 LEU   A C   
2167 O  O   . LEU   A 301 ? 1.3304 1.2494 1.3128 0.0000  0.0158  -0.3419 321 LEU   A O   
2168 C  CB  . LEU   A 301 ? 1.1761 1.1148 1.1984 -0.0241 0.0678  -0.2568 321 LEU   A CB  
2169 C  CG  . LEU   A 301 ? 1.1971 1.1424 1.2015 -0.0123 0.0874  -0.2185 321 LEU   A CG  
2170 C  CD1 . LEU   A 301 ? 1.2576 1.1717 1.2748 -0.0193 0.1067  -0.2037 321 LEU   A CD1 
2171 C  CD2 . LEU   A 301 ? 1.1718 1.1190 1.1305 0.0171  0.0894  -0.2153 321 LEU   A CD2 
2172 N  N   . ALA   A 302 ? 1.2736 1.2420 1.3359 -0.0368 0.0054  -0.3406 322 ALA   A N   
2173 C  CA  . ALA   A 302 ? 1.2923 1.2530 1.3817 -0.0452 -0.0191 -0.3869 322 ALA   A CA  
2174 C  C   . ALA   A 302 ? 1.2881 1.2641 1.3371 -0.0184 -0.0539 -0.4140 322 ALA   A C   
2175 O  O   . ALA   A 302 ? 1.3996 1.3566 1.4406 -0.0115 -0.0757 -0.4529 322 ALA   A O   
2176 C  CB  . ALA   A 302 ? 1.2719 1.2524 1.4393 -0.0788 -0.0200 -0.3984 322 ALA   A CB  
2177 N  N   . THR   A 303 ? 1.4676 1.4732 1.4871 -0.0015 -0.0603 -0.3951 323 THR   A N   
2178 C  CA  . THR   A 303 ? 1.4971 1.5103 1.4636 0.0298  -0.0910 -0.4154 323 THR   A CA  
2179 C  C   . THR   A 303 ? 1.5528 1.5383 1.4360 0.0631  -0.0781 -0.3999 323 THR   A C   
2180 O  O   . THR   A 303 ? 1.6898 1.6720 1.5134 0.0940  -0.0989 -0.4135 323 THR   A O   
2181 C  CB  . THR   A 303 ? 1.4512 1.5041 1.4227 0.0345  -0.1037 -0.4030 323 THR   A CB  
2182 O  OG1 . THR   A 303 ? 1.6015 1.6543 1.5096 0.0699  -0.1327 -0.4198 323 THR   A OG1 
2183 C  CG2 . THR   A 303 ? 1.3992 1.4593 1.3583 0.0330  -0.0708 -0.3527 323 THR   A CG2 
2184 N  N   . HIS   A 304 ? 1.4061 1.3712 1.2831 0.0597  -0.0438 -0.3719 324 HIS   A N   
2185 C  CA  . HIS   A 304 ? 1.4503 1.3904 1.2601 0.0894  -0.0258 -0.3580 324 HIS   A CA  
2186 C  C   . HIS   A 304 ? 1.4382 1.3447 1.2620 0.0812  -0.0074 -0.3619 324 HIS   A C   
2187 O  O   . HIS   A 304 ? 1.4373 1.3404 1.2711 0.0767  0.0226  -0.3296 324 HIS   A O   
2188 C  CB  . HIS   A 304 ? 1.3880 1.3459 1.1781 0.0983  0.0005  -0.3123 324 HIS   A CB  
2189 C  CG  . HIS   A 304 ? 1.3659 1.3477 1.1323 0.1105  -0.0149 -0.3065 324 HIS   A CG  
2190 N  ND1 . HIS   A 304 ? 1.3431 1.3565 1.1564 0.0901  -0.0250 -0.3001 324 HIS   A ND1 
2191 C  CD2 . HIS   A 304 ? 1.3891 1.3636 1.0855 0.1435  -0.0202 -0.3051 324 HIS   A CD2 
2192 C  CE1 . HIS   A 304 ? 1.3607 1.3858 1.1364 0.1099  -0.0379 -0.2957 324 HIS   A CE1 
2193 N  NE2 . HIS   A 304 ? 1.4029 1.4031 1.1053 0.1426  -0.0349 -0.2977 324 HIS   A NE2 
2194 N  N   . PRO   A 305 ? 1.4118 1.2914 1.2368 0.0806  -0.0265 -0.4027 325 PRO   A N   
2195 C  CA  . PRO   A 305 ? 1.4271 1.2696 1.2721 0.0696  -0.0096 -0.4081 325 PRO   A CA  
2196 C  C   . PRO   A 305 ? 1.4447 1.2640 1.2413 0.0953  0.0184  -0.3859 325 PRO   A C   
2197 O  O   . PRO   A 305 ? 1.4112 1.2072 1.2283 0.0871  0.0399  -0.3742 325 PRO   A O   
2198 C  CB  . PRO   A 305 ? 1.4695 1.2880 1.3179 0.0683  -0.0408 -0.4616 325 PRO   A CB  
2199 C  CG  . PRO   A 305 ? 1.4578 1.3121 1.3137 0.0688  -0.0763 -0.4832 325 PRO   A CG  
2200 C  CD  . PRO   A 305 ? 1.4445 1.3238 1.2516 0.0919  -0.0665 -0.4476 325 PRO   A CD  
2201 N  N   . ASP   A 306 ? 1.4341 1.2576 1.1667 0.1280  0.0203  -0.3796 326 ASP   A N   
2202 C  CA  . ASP   A 306 ? 1.4503 1.2579 1.1434 0.1532  0.0513  -0.3573 326 ASP   A CA  
2203 C  C   . ASP   A 306 ? 1.4114 1.2410 1.1445 0.1401  0.0806  -0.3134 326 ASP   A C   
2204 O  O   . ASP   A 306 ? 1.4014 1.2143 1.1405 0.1460  0.1033  -0.3006 326 ASP   A O   
2205 C  CB  . ASP   A 306 ? 1.4991 1.3092 1.1183 0.1886  0.0526  -0.3546 326 ASP   A CB  
2206 C  CG  . ASP   A 306 ? 1.5497 1.3956 1.1691 0.1845  0.0405  -0.3406 326 ASP   A CG  
2207 O  OD1 . ASP   A 306 ? 1.5794 1.4394 1.2320 0.1650  0.0102  -0.3611 326 ASP   A OD1 
2208 O  OD2 . ASP   A 306 ? 1.6331 1.4929 1.2244 0.2000  0.0628  -0.3089 326 ASP   A OD2 
2209 N  N   . VAL   A 307 ? 1.4213 1.2879 1.1816 0.1243  0.0783  -0.2917 327 VAL   A N   
2210 C  CA  . VAL   A 307 ? 1.3119 1.2001 1.1100 0.1118  0.1007  -0.2535 327 VAL   A CA  
2211 C  C   . VAL   A 307 ? 1.2753 1.1471 1.1215 0.0878  0.1035  -0.2537 327 VAL   A C   
2212 O  O   . VAL   A 307 ? 1.2327 1.1040 1.0971 0.0875  0.1230  -0.2288 327 VAL   A O   
2213 C  CB  . VAL   A 307 ? 1.2859 1.2126 1.0975 0.1013  0.0949  -0.2346 327 VAL   A CB  
2214 C  CG1 . VAL   A 307 ? 1.2372 1.1859 1.0826 0.0918  0.1159  -0.1975 327 VAL   A CG1 
2215 C  CG2 . VAL   A 307 ? 1.3127 1.2455 1.0685 0.1269  0.0917  -0.2359 327 VAL   A CG2 
2216 N  N   . GLN   A 308 ? 1.2823 1.1389 1.1503 0.0685  0.0846  -0.2820 328 GLN   A N   
2217 C  CA  . GLN   A 308 ? 1.2487 1.0813 1.1582 0.0455  0.0918  -0.2813 328 GLN   A CA  
2218 C  C   . GLN   A 308 ? 1.2690 1.0580 1.1612 0.0602  0.1055  -0.2869 328 GLN   A C   
2219 O  O   . GLN   A 308 ? 1.3097 1.0829 1.2178 0.0573  0.1233  -0.2653 328 GLN   A O   
2220 C  CB  . GLN   A 308 ? 1.2486 1.0769 1.1932 0.0196  0.0717  -0.3119 328 GLN   A CB  
2221 C  CG  . GLN   A 308 ? 1.2314 1.0352 1.2221 -0.0081 0.0849  -0.3066 328 GLN   A CG  
2222 C  CD  . GLN   A 308 ? 1.2657 1.0686 1.3017 -0.0356 0.0691  -0.3385 328 GLN   A CD  
2223 O  OE1 . GLN   A 308 ? 1.3205 1.0886 1.3890 -0.0561 0.0796  -0.3471 328 GLN   A OE1 
2224 N  NE2 . GLN   A 308 ? 1.2525 1.0930 1.2935 -0.0357 0.0445  -0.3564 328 GLN   A NE2 
2225 N  N   . GLN   A 309 ? 1.3162 1.0827 1.1718 0.0791  0.0962  -0.3165 329 GLN   A N   
2226 C  CA  . GLN   A 309 ? 1.3095 1.0331 1.1441 0.0972  0.1099  -0.3229 329 GLN   A CA  
2227 C  C   . GLN   A 309 ? 1.3346 1.0722 1.1548 0.1205  0.1349  -0.2888 329 GLN   A C   
2228 O  O   . GLN   A 309 ? 1.3644 1.0768 1.1926 0.1273  0.1508  -0.2778 329 GLN   A O   
2229 C  CB  . GLN   A 309 ? 1.3430 1.0409 1.1336 0.1166  0.0940  -0.3627 329 GLN   A CB  
2230 C  CG  . GLN   A 309 ? 1.3623 1.0109 1.1297 0.1361  0.1074  -0.3741 329 GLN   A CG  
2231 C  CD  . GLN   A 309 ? 1.4285 1.0499 1.1441 0.1588  0.0909  -0.4149 329 GLN   A CD  
2232 O  OE1 . GLN   A 309 ? 1.4615 1.0981 1.1609 0.1582  0.0649  -0.4384 329 GLN   A OE1 
2233 N  NE2 . GLN   A 309 ? 1.4721 1.0515 1.1582 0.1820  0.1042  -0.4248 329 GLN   A NE2 
2234 N  N   . LYS   A 310 ? 1.3291 1.1064 1.1315 0.1334  0.1389  -0.2717 330 LYS   A N   
2235 C  CA  . LYS   A 310 ? 1.3193 1.1158 1.1207 0.1528  0.1637  -0.2409 330 LYS   A CA  
2236 C  C   . LYS   A 310 ? 1.2811 1.0926 1.1299 0.1361  0.1708  -0.2118 330 LYS   A C   
2237 O  O   . LYS   A 310 ? 1.2821 1.0890 1.1417 0.1499  0.1865  -0.1959 330 LYS   A O   
2238 C  CB  . LYS   A 310 ? 1.2511 1.0833 1.0270 0.1668  0.1696  -0.2285 330 LYS   A CB  
2239 C  CG  . LYS   A 310 ? 1.2418 1.0954 1.0233 0.1869  0.1986  -0.2005 330 LYS   A CG  
2240 C  CD  . LYS   A 310 ? 1.3608 1.2389 1.1110 0.2025  0.2110  -0.1897 330 LYS   A CD  
2241 C  CE  . LYS   A 310 ? 1.3223 1.2199 1.0858 0.2225  0.2444  -0.1658 330 LYS   A CE  
2242 N  NZ  . LYS   A 310 ? 1.3019 1.2204 1.0393 0.2354  0.2637  -0.1507 330 LYS   A NZ  
2243 N  N   . LEU   A 311 ? 1.2492 1.0779 1.1250 0.1090  0.1584  -0.2058 331 LEU   A N   
2244 C  CA  . LEU   A 311 ? 1.2202 1.0558 1.1318 0.0947  0.1634  -0.1807 331 LEU   A CA  
2245 C  C   . LEU   A 311 ? 1.2300 1.0172 1.1484 0.0920  0.1680  -0.1858 331 LEU   A C   
2246 O  O   . LEU   A 311 ? 1.2148 0.9957 1.1436 0.1009  0.1779  -0.1650 331 LEU   A O   
2247 C  CB  . LEU   A 311 ? 1.2326 1.0922 1.1661 0.0678  0.1510  -0.1760 331 LEU   A CB  
2248 C  CG  . LEU   A 311 ? 1.1938 1.0637 1.1562 0.0541  0.1549  -0.1496 331 LEU   A CG  
2249 C  CD1 . LEU   A 311 ? 1.1240 1.0384 1.0981 0.0441  0.1486  -0.1359 331 LEU   A CD1 
2250 C  CD2 . LEU   A 311 ? 1.2250 1.0595 1.2018 0.0326  0.1535  -0.1574 331 LEU   A CD2 
2251 N  N   . GLN   A 312 ? 1.2856 1.0359 1.1984 0.0810  0.1602  -0.2143 332 GLN   A N   
2252 C  CA  . GLN   A 312 ? 1.3200 1.0158 1.2379 0.0774  0.1677  -0.2195 332 GLN   A CA  
2253 C  C   . GLN   A 312 ? 1.2822 0.9539 1.1778 0.1090  0.1801  -0.2174 332 GLN   A C   
2254 O  O   . GLN   A 312 ? 1.2990 0.9370 1.1987 0.1153  0.1903  -0.2045 332 GLN   A O   
2255 C  CB  . GLN   A 312 ? 1.3386 1.0016 1.2624 0.0573  0.1567  -0.2546 332 GLN   A CB  
2256 C  CG  . GLN   A 312 ? 1.2800 0.9589 1.2391 0.0235  0.1491  -0.2561 332 GLN   A CG  
2257 C  CD  . GLN   A 312 ? 1.3673 1.0206 1.3449 0.0029  0.1369  -0.2949 332 GLN   A CD  
2258 O  OE1 . GLN   A 312 ? 1.3885 1.0326 1.3457 0.0148  0.1233  -0.3259 332 GLN   A OE1 
2259 N  NE2 . GLN   A 312 ? 1.4022 1.0433 1.4196 -0.0278 0.1424  -0.2948 332 GLN   A NE2 
2260 N  N   . GLU   A 313 ? 1.2713 0.9573 1.1402 0.1316  0.1806  -0.2298 333 GLU   A N   
2261 C  CA  . GLU   A 313 ? 1.2598 0.9307 1.1109 0.1644  0.1957  -0.2267 333 GLU   A CA  
2262 C  C   . GLU   A 313 ? 1.2536 0.9547 1.1284 0.1763  0.2070  -0.1922 333 GLU   A C   
2263 O  O   . GLU   A 313 ? 1.3080 0.9850 1.1855 0.1953  0.2164  -0.1844 333 GLU   A O   
2264 C  CB  . GLU   A 313 ? 1.3260 1.0113 1.1413 0.1870  0.1984  -0.2429 333 GLU   A CB  
2265 C  CG  . GLU   A 313 ? 1.4202 1.0649 1.2028 0.1874  0.1855  -0.2829 333 GLU   A CG  
2266 C  CD  . GLU   A 313 ? 1.4486 1.1107 1.1863 0.2088  0.1845  -0.2969 333 GLU   A CD  
2267 O  OE1 . GLU   A 313 ? 1.4669 1.1620 1.1967 0.2291  0.2031  -0.2749 333 GLU   A OE1 
2268 O  OE2 . GLU   A 313 ? 1.5595 1.2011 1.2698 0.2060  0.1652  -0.3304 333 GLU   A OE2 
2269 N  N   . GLU   A 314 ? 1.2549 1.0084 1.1485 0.1667  0.2042  -0.1729 334 GLU   A N   
2270 C  CA  . GLU   A 314 ? 1.2442 1.0305 1.1666 0.1763  0.2105  -0.1439 334 GLU   A CA  
2271 C  C   . GLU   A 314 ? 1.3109 1.0690 1.2470 0.1675  0.2052  -0.1304 334 GLU   A C   
2272 O  O   . GLU   A 314 ? 1.3117 1.0682 1.2595 0.1874  0.2091  -0.1155 334 GLU   A O   
2273 C  CB  . GLU   A 314 ? 1.2412 1.0843 1.1809 0.1648  0.2076  -0.1291 334 GLU   A CB  
2274 C  CG  . GLU   A 314 ? 1.2618 1.1391 1.2384 0.1680  0.2077  -0.1026 334 GLU   A CG  
2275 C  CD  . GLU   A 314 ? 1.1884 1.1171 1.1843 0.1551  0.2055  -0.0897 334 GLU   A CD  
2276 O  OE1 . GLU   A 314 ? 1.2383 1.1957 1.2350 0.1663  0.2186  -0.0885 334 GLU   A OE1 
2277 O  OE2 . GLU   A 314 ? 1.1761 1.1131 1.1845 0.1346  0.1930  -0.0801 334 GLU   A OE2 
2278 N  N   . ILE   A 315 ? 1.3168 1.0516 1.2511 0.1397  0.1970  -0.1356 335 ILE   A N   
2279 C  CA  . ILE   A 315 ? 1.2951 0.9963 1.2343 0.1315  0.1966  -0.1205 335 ILE   A CA  
2280 C  C   . ILE   A 315 ? 1.3651 1.0093 1.2884 0.1525  0.2053  -0.1233 335 ILE   A C   
2281 O  O   . ILE   A 315 ? 1.4291 1.0579 1.3522 0.1683  0.2065  -0.1036 335 ILE   A O   
2282 C  CB  . ILE   A 315 ? 1.2872 0.9698 1.2297 0.0973  0.1928  -0.1285 335 ILE   A CB  
2283 C  CG1 . ILE   A 315 ? 1.2398 0.9777 1.1976 0.0793  0.1833  -0.1253 335 ILE   A CG1 
2284 C  CG2 . ILE   A 315 ? 1.3750 1.0163 1.3150 0.0911  0.1986  -0.1102 335 ILE   A CG2 
2285 C  CD1 . ILE   A 315 ? 1.2481 0.9748 1.2172 0.0475  0.1806  -0.1314 335 ILE   A CD1 
2286 N  N   . ASP   A 316 ? 1.3939 1.0030 1.3007 0.1551  0.2095  -0.1491 336 ASP   A N   
2287 C  CA  . ASP   A 316 ? 1.4455 0.9927 1.3352 0.1742  0.2185  -0.1547 336 ASP   A CA  
2288 C  C   . ASP   A 316 ? 1.4719 1.0348 1.3598 0.2135  0.2244  -0.1477 336 ASP   A C   
2289 O  O   . ASP   A 316 ? 1.4219 0.9368 1.2975 0.2351  0.2310  -0.1464 336 ASP   A O   
2290 C  CB  . ASP   A 316 ? 1.3995 0.9030 1.2748 0.1627  0.2191  -0.1887 336 ASP   A CB  
2291 C  CG  . ASP   A 316 ? 1.4619 0.9534 1.3513 0.1230  0.2137  -0.1990 336 ASP   A CG  
2292 O  OD1 . ASP   A 316 ? 1.4742 0.9809 1.3786 0.1063  0.2138  -0.1770 336 ASP   A OD1 
2293 O  OD2 . ASP   A 316 ? 1.4913 0.9593 1.3789 0.1095  0.2089  -0.2307 336 ASP   A OD2 
2294 N  N   . ALA   A 317 ? 1.3755 1.0030 1.2779 0.2236  0.2241  -0.1431 337 ALA   A N   
2295 C  CA  . ALA   A 317 ? 1.3271 0.9792 1.2416 0.2592  0.2322  -0.1341 337 ALA   A CA  
2296 C  C   . ALA   A 317 ? 1.3697 1.0484 1.3121 0.2676  0.2245  -0.1067 337 ALA   A C   
2297 O  O   . ALA   A 317 ? 1.3809 1.0631 1.3361 0.2991  0.2272  -0.0992 337 ALA   A O   
2298 C  CB  . ALA   A 317 ? 1.3016 1.0077 1.2219 0.2669  0.2406  -0.1407 337 ALA   A CB  
2299 N  N   . VAL   A 318 ? 1.3070 1.0048 1.2589 0.2421  0.2133  -0.0935 338 VAL   A N   
2300 C  CA  . VAL   A 318 ? 1.3836 1.1013 1.3549 0.2498  0.2017  -0.0702 338 VAL   A CA  
2301 C  C   . VAL   A 318 ? 1.4157 1.0666 1.3588 0.2498  0.1980  -0.0606 338 VAL   A C   
2302 O  O   . VAL   A 318 ? 1.4361 1.0766 1.3793 0.2749  0.1904  -0.0457 338 VAL   A O   
2303 C  CB  . VAL   A 318 ? 1.3893 1.1627 1.3826 0.2253  0.1925  -0.0609 338 VAL   A CB  
2304 C  CG1 . VAL   A 318 ? 1.3704 1.1693 1.3855 0.2367  0.1772  -0.0408 338 VAL   A CG1 
2305 C  CG2 . VAL   A 318 ? 1.3436 1.1715 1.3566 0.2235  0.2009  -0.0692 338 VAL   A CG2 
2306 N  N   . LEU   A 319 ? 1.4336 1.0373 1.3531 0.2230  0.2040  -0.0693 339 LEU   A N   
2307 C  CA  . LEU   A 319 ? 1.5199 1.0538 1.4114 0.2177  0.2077  -0.0590 339 LEU   A CA  
2308 C  C   . LEU   A 319 ? 1.5846 1.0519 1.4561 0.2129  0.2218  -0.0787 339 LEU   A C   
2309 O  O   . LEU   A 319 ? 1.6144 1.0598 1.4847 0.1808  0.2276  -0.0920 339 LEU   A O   
2310 C  CB  . LEU   A 319 ? 1.5509 1.0914 1.4422 0.1851  0.2050  -0.0494 339 LEU   A CB  
2311 C  CG  . LEU   A 319 ? 1.5172 1.1088 1.4213 0.1911  0.1896  -0.0294 339 LEU   A CG  
2312 C  CD1 . LEU   A 319 ? 1.4677 1.0891 1.3817 0.1567  0.1873  -0.0288 339 LEU   A CD1 
2313 C  CD2 . LEU   A 319 ? 1.5713 1.1172 1.4464 0.2140  0.1855  -0.0077 339 LEU   A CD2 
2314 N  N   . PRO   A 320 ? 1.7269 1.1612 1.5865 0.2445  0.2269  -0.0830 340 PRO   A N   
2315 C  CA  . PRO   A 320 ? 1.7919 1.1586 1.6323 0.2417  0.2395  -0.1043 340 PRO   A CA  
2316 C  C   . PRO   A 320 ? 1.9830 1.2651 1.7980 0.2325  0.2506  -0.0931 340 PRO   A C   
2317 O  O   . PRO   A 320 ? 2.0357 1.3032 1.8371 0.2403  0.2492  -0.0660 340 PRO   A O   
2318 C  CB  . PRO   A 320 ? 1.7377 1.1030 1.5746 0.2838  0.2416  -0.1097 340 PRO   A CB  
2319 C  CG  . PRO   A 320 ? 1.6748 1.0762 1.5234 0.3111  0.2313  -0.0832 340 PRO   A CG  
2320 C  CD  . PRO   A 320 ? 1.6733 1.1353 1.5425 0.2853  0.2203  -0.0713 340 PRO   A CD  
2321 N  N   . ASN   A 321 ? 2.3014 1.5238 2.1085 0.2165  0.2626  -0.1152 341 ASN   A N   
2322 C  CA  . ASN   A 321 ? 2.3375 1.4743 2.1268 0.1993  0.2796  -0.1084 341 ASN   A CA  
2323 C  C   . ASN   A 321 ? 2.2840 1.4348 2.0825 0.1664  0.2829  -0.0920 341 ASN   A C   
2324 O  O   . ASN   A 321 ? 2.3294 1.4202 2.1052 0.1631  0.2982  -0.0701 341 ASN   A O   
2325 C  CB  . ASN   A 321 ? 2.3909 1.4604 2.1442 0.2369  0.2876  -0.0858 341 ASN   A CB  
2326 C  CG  . ASN   A 321 ? 2.4605 1.5030 2.2045 0.2690  0.2885  -0.1039 341 ASN   A CG  
2327 O  OD1 . ASN   A 321 ? 2.4804 1.5112 2.2335 0.2554  0.2918  -0.1357 341 ASN   A OD1 
2328 N  ND2 . ASN   A 321 ? 2.5793 1.6118 2.3048 0.3139  0.2842  -0.0854 341 ASN   A ND2 
2329 N  N   . LYS   A 322 ? 1.9995 1.2259 1.8274 0.1438  0.2705  -0.1020 342 LYS   A N   
2330 C  CA  . LYS   A 322 ? 1.9078 1.1611 1.7474 0.1162  0.2714  -0.0874 342 LYS   A CA  
2331 C  C   . LYS   A 322 ? 1.8757 1.1233 1.6880 0.1387  0.2701  -0.0511 342 LYS   A C   
2332 O  O   . LYS   A 322 ? 1.8545 1.0671 1.6516 0.1248  0.2832  -0.0325 342 LYS   A O   
2333 C  CB  . LYS   A 322 ? 1.8851 1.0871 1.7373 0.0773  0.2908  -0.0980 342 LYS   A CB  
2334 C  CG  . LYS   A 322 ? 1.8370 1.0602 1.7246 0.0504  0.2842  -0.1379 342 LYS   A CG  
2335 C  CD  . LYS   A 322 ? 1.8459 1.0292 1.7611 0.0088  0.3023  -0.1495 342 LYS   A CD  
2336 C  CE  . LYS   A 322 ? 1.7976 0.9929 1.7487 -0.0137 0.2913  -0.1946 342 LYS   A CE  
2337 N  NZ  . LYS   A 322 ? 1.7527 0.9142 1.7447 -0.0561 0.3085  -0.2094 342 LYS   A NZ  
2338 N  N   . ALA   A 323 ? 1.7721 1.0547 1.5788 0.1753  0.2541  -0.0423 343 ALA   A N   
2339 C  CA  . ALA   A 323 ? 1.7420 1.0272 1.5261 0.2012  0.2449  -0.0127 343 ALA   A CA  
2340 C  C   . ALA   A 323 ? 1.6791 1.0108 1.4730 0.1781  0.2383  -0.0018 343 ALA   A C   
2341 O  O   . ALA   A 323 ? 1.6650 1.0544 1.4922 0.1520  0.2333  -0.0170 343 ALA   A O   
2342 C  CB  . ALA   A 323 ? 1.6718 1.0060 1.4677 0.2402  0.2257  -0.0119 343 ALA   A CB  
2343 N  N   . PRO   A 324 ? 1.7339 1.0379 1.4944 0.1896  0.2378  0.0242  344 PRO   A N   
2344 C  CA  . PRO   A 324 ? 1.6652 1.0055 1.4294 0.1692  0.2333  0.0340  344 PRO   A CA  
2345 C  C   . PRO   A 324 ? 1.6294 1.0571 1.4217 0.1810  0.2052  0.0330  344 PRO   A C   
2346 O  O   . PRO   A 324 ? 1.6630 1.1069 1.4543 0.2160  0.1878  0.0385  344 PRO   A O   
2347 C  CB  . PRO   A 324 ? 1.7189 0.9883 1.4258 0.1857  0.2429  0.0622  344 PRO   A CB  
2348 C  CG  . PRO   A 324 ? 1.7582 0.9784 1.4349 0.2273  0.2390  0.0699  344 PRO   A CG  
2349 C  CD  . PRO   A 324 ? 1.7541 0.9988 1.4685 0.2297  0.2363  0.0455  344 PRO   A CD  
2350 N  N   . PRO   A 325 ? 1.7210 1.2064 1.5429 0.1528  0.2007  0.0253  345 PRO   A N   
2351 C  CA  . PRO   A 325 ? 1.6704 1.2354 1.5222 0.1609  0.1770  0.0245  345 PRO   A CA  
2352 C  C   . PRO   A 325 ? 1.7549 1.3183 1.5824 0.1856  0.1594  0.0447  345 PRO   A C   
2353 O  O   . PRO   A 325 ? 1.7746 1.2927 1.5620 0.1828  0.1662  0.0597  345 PRO   A O   
2354 C  CB  . PRO   A 325 ? 1.5680 1.1759 1.4454 0.1241  0.1798  0.0147  345 PRO   A CB  
2355 C  CG  . PRO   A 325 ? 1.5596 1.1203 1.4317 0.0979  0.2024  0.0043  345 PRO   A CG  
2356 C  CD  . PRO   A 325 ? 1.7042 1.1831 1.5359 0.1131  0.2173  0.0175  345 PRO   A CD  
2357 N  N   . THR   A 326 ? 1.8710 1.4825 1.7229 0.2114  0.1371  0.0439  346 THR   A N   
2358 C  CA  . THR   A 326 ? 1.9087 1.5345 1.7493 0.2351  0.1121  0.0567  346 THR   A CA  
2359 C  C   . THR   A 326 ? 1.8513 1.5616 1.7428 0.2228  0.0945  0.0488  346 THR   A C   
2360 O  O   . THR   A 326 ? 1.7844 1.5382 1.7152 0.2015  0.1033  0.0360  346 THR   A O   
2361 C  CB  . THR   A 326 ? 1.9169 1.5255 1.7488 0.2798  0.0970  0.0615  346 THR   A CB  
2362 O  OG1 . THR   A 326 ? 1.9608 1.5614 1.7635 0.3048  0.0717  0.0745  346 THR   A OG1 
2363 C  CG2 . THR   A 326 ? 1.8763 1.5556 1.7719 0.2907  0.0869  0.0470  346 THR   A CG2 
2364 N  N   . TYR   A 327 ? 1.8375 1.5666 1.7245 0.2377  0.0692  0.0561  347 TYR   A N   
2365 C  CA  . TYR   A 327 ? 1.7137 1.5177 1.6502 0.2251  0.0523  0.0486  347 TYR   A CA  
2366 C  C   . TYR   A 327 ? 1.6575 1.5223 1.6588 0.2303  0.0511  0.0363  347 TYR   A C   
2367 O  O   . TYR   A 327 ? 1.5948 1.5105 1.6369 0.2072  0.0567  0.0285  347 TYR   A O   
2368 C  CB  . TYR   A 327 ? 1.7047 1.5157 1.6279 0.2462  0.0205  0.0547  347 TYR   A CB  
2369 C  CG  . TYR   A 327 ? 1.5897 1.4712 1.5638 0.2307  0.0029  0.0459  347 TYR   A CG  
2370 C  CD1 . TYR   A 327 ? 1.5432 1.4894 1.5854 0.2417  -0.0142 0.0355  347 TYR   A CD1 
2371 C  CD2 . TYR   A 327 ? 1.5952 1.4771 1.5529 0.2048  0.0056  0.0478  347 TYR   A CD2 
2372 C  CE1 . TYR   A 327 ? 1.4928 1.4987 1.5851 0.2254  -0.0274 0.0277  347 TYR   A CE1 
2373 C  CE2 . TYR   A 327 ? 1.5782 1.5183 1.5809 0.1908  -0.0097 0.0398  347 TYR   A CE2 
2374 C  CZ  . TYR   A 327 ? 1.5346 1.5348 1.6044 0.2002  -0.0259 0.0299  347 TYR   A CZ  
2375 O  OH  . TYR   A 327 ? 1.5421 1.5961 1.6603 0.1842  -0.0384 0.0220  347 TYR   A OH  
2376 N  N   . ASP   A 328 ? 1.6002 1.4580 1.6098 0.2621  0.0461  0.0352  348 ASP   A N   
2377 C  CA  . ASP   A 328 ? 1.5513 1.4684 1.6253 0.2704  0.0477  0.0242  348 ASP   A CA  
2378 C  C   . ASP   A 328 ? 1.4777 1.3881 1.5546 0.2548  0.0784  0.0160  348 ASP   A C   
2379 O  O   . ASP   A 328 ? 1.3664 1.3290 1.4911 0.2499  0.0875  0.0075  348 ASP   A O   
2380 C  CB  . ASP   A 328 ? 1.6619 1.5795 1.7496 0.3133  0.0294  0.0243  348 ASP   A CB  
2381 C  CG  . ASP   A 328 ? 1.6614 1.6098 1.7677 0.3308  -0.0077 0.0255  348 ASP   A CG  
2382 O  OD1 . ASP   A 328 ? 1.6210 1.6354 1.7853 0.3159  -0.0174 0.0180  348 ASP   A OD1 
2383 O  OD2 . ASP   A 328 ? 1.7376 1.6410 1.7980 0.3601  -0.0277 0.0334  348 ASP   A OD2 
2384 N  N   . THR   A 329 ? 1.6158 1.4613 1.6421 0.2473  0.0951  0.0174  349 THR   A N   
2385 C  CA  . THR   A 329 ? 1.5481 1.3857 1.5751 0.2330  0.1195  0.0054  349 THR   A CA  
2386 C  C   . THR   A 329 ? 1.4719 1.3385 1.5082 0.1971  0.1275  -0.0005 349 THR   A C   
2387 O  O   . THR   A 329 ? 1.4359 1.3247 1.4880 0.1899  0.1410  -0.0119 349 THR   A O   
2388 C  CB  . THR   A 329 ? 1.5923 1.3503 1.5698 0.2349  0.1336  0.0053  349 THR   A CB  
2389 O  OG1 . THR   A 329 ? 1.6669 1.3820 1.6058 0.2207  0.1321  0.0169  349 THR   A OG1 
2390 C  CG2 . THR   A 329 ? 1.5983 1.3260 1.5674 0.2740  0.1305  0.0079  349 THR   A CG2 
2391 N  N   . VAL   A 330 ? 1.4137 1.2784 1.4368 0.1774  0.1196  0.0069  350 VAL   A N   
2392 C  CA  . VAL   A 330 ? 1.3874 1.2760 1.4178 0.1455  0.1263  0.0010  350 VAL   A CA  
2393 C  C   . VAL   A 330 ? 1.3400 1.2969 1.4158 0.1427  0.1210  -0.0007 350 VAL   A C   
2394 O  O   . VAL   A 330 ? 1.3315 1.3110 1.4173 0.1277  0.1321  -0.0085 350 VAL   A O   
2395 C  CB  . VAL   A 330 ? 1.3818 1.2445 1.3845 0.1265  0.1230  0.0090  350 VAL   A CB  
2396 C  CG1 . VAL   A 330 ? 1.4457 1.3140 1.4438 0.1418  0.1027  0.0218  350 VAL   A CG1 
2397 C  CG2 . VAL   A 330 ? 1.2845 1.1787 1.3007 0.0970  0.1267  0.0025  350 VAL   A CG2 
2398 N  N   . LEU   A 331 ? 1.3470 1.3357 1.4512 0.1577  0.1041  0.0060  351 LEU   A N   
2399 C  CA  . LEU   A 331 ? 1.2975 1.3494 1.4549 0.1556  0.1032  0.0038  351 LEU   A CA  
2400 C  C   . LEU   A 331 ? 1.2988 1.3688 1.4805 0.1702  0.1214  -0.0031 351 LEU   A C   
2401 O  O   . LEU   A 331 ? 1.2679 1.3832 1.4876 0.1649  0.1318  -0.0047 351 LEU   A O   
2402 C  CB  . LEU   A 331 ? 1.2483 1.3310 1.4392 0.1687  0.0782  0.0083  351 LEU   A CB  
2403 C  CG  . LEU   A 331 ? 1.2521 1.3401 1.4355 0.1526  0.0599  0.0127  351 LEU   A CG  
2404 C  CD1 . LEU   A 331 ? 1.3242 1.3526 1.4452 0.1547  0.0531  0.0195  351 LEU   A CD1 
2405 C  CD2 . LEU   A 331 ? 1.2724 1.4070 1.5075 0.1641  0.0356  0.0108  351 LEU   A CD2 
2406 N  N   . GLN   A 332 ? 1.3003 1.3316 1.4583 0.1892  0.1281  -0.0068 352 GLN   A N   
2407 C  CA  . GLN   A 332 ? 1.2662 1.3067 1.4396 0.2070  0.1467  -0.0145 352 GLN   A CA  
2408 C  C   . GLN   A 332 ? 1.2881 1.3161 1.4351 0.1922  0.1678  -0.0242 352 GLN   A C   
2409 O  O   . GLN   A 332 ? 1.2590 1.2944 1.4121 0.2069  0.1860  -0.0315 352 GLN   A O   
2410 C  CB  . GLN   A 332 ? 1.3368 1.3337 1.4900 0.2352  0.1439  -0.0156 352 GLN   A CB  
2411 C  CG  . GLN   A 332 ? 1.4112 1.4319 1.5996 0.2649  0.1547  -0.0210 352 GLN   A CG  
2412 C  CD  . GLN   A 332 ? 1.4846 1.4488 1.6398 0.2908  0.1569  -0.0244 352 GLN   A CD  
2413 O  OE1 . GLN   A 332 ? 1.4681 1.3964 1.5920 0.2903  0.1750  -0.0343 352 GLN   A OE1 
2414 N  NE2 . GLN   A 332 ? 1.4298 1.3825 1.5891 0.3153  0.1370  -0.0171 352 GLN   A NE2 
2415 N  N   . MET   A 333 ? 1.2312 1.2416 1.3491 0.1659  0.1651  -0.0257 353 MET   A N   
2416 C  CA  . MET   A 333 ? 1.2511 1.2421 1.3380 0.1539  0.1778  -0.0385 353 MET   A CA  
2417 C  C   . MET   A 333 ? 1.2371 1.2678 1.3350 0.1374  0.1820  -0.0370 353 MET   A C   
2418 O  O   . MET   A 333 ? 1.1871 1.2274 1.2871 0.1172  0.1710  -0.0312 353 MET   A O   
2419 C  CB  . MET   A 333 ? 1.2390 1.1792 1.2900 0.1377  0.1717  -0.0442 353 MET   A CB  
2420 C  CG  . MET   A 333 ? 1.2848 1.1760 1.3195 0.1535  0.1702  -0.0426 353 MET   A CG  
2421 S  SD  . MET   A 333 ? 1.3099 1.1376 1.3086 0.1310  0.1719  -0.0500 353 MET   A SD  
2422 C  CE  . MET   A 333 ? 1.2014 1.0340 1.1917 0.1188  0.1794  -0.0745 353 MET   A CE  
2423 N  N   . GLU   A 334 ? 1.1157 1.1637 1.2147 0.1477  0.2000  -0.0418 354 GLU   A N   
2424 C  CA  . GLU   A 334 ? 1.0875 1.1715 1.1974 0.1386  0.2094  -0.0363 354 GLU   A CA  
2425 C  C   . GLU   A 334 ? 1.0834 1.1497 1.1506 0.1250  0.2085  -0.0464 354 GLU   A C   
2426 O  O   . GLU   A 334 ? 0.9793 1.0635 1.0494 0.1086  0.2033  -0.0403 354 GLU   A O   
2427 C  CB  . GLU   A 334 ? 1.0901 1.2001 1.2219 0.1593  0.2342  -0.0337 354 GLU   A CB  
2428 C  CG  . GLU   A 334 ? 1.2256 1.3056 1.3261 0.1820  0.2489  -0.0472 354 GLU   A CG  
2429 C  CD  . GLU   A 334 ? 1.3029 1.3653 1.4172 0.1991  0.2420  -0.0498 354 GLU   A CD  
2430 O  OE1 . GLU   A 334 ? 1.2847 1.3576 1.4288 0.1948  0.2243  -0.0406 354 GLU   A OE1 
2431 O  OE2 . GLU   A 334 ? 1.3513 1.3859 1.4420 0.2190  0.2532  -0.0614 354 GLU   A OE2 
2432 N  N   . TYR   A 335 ? 1.1516 1.1829 1.1800 0.1332  0.2116  -0.0637 355 TYR   A N   
2433 C  CA  . TYR   A 335 ? 1.0819 1.0974 1.0730 0.1218  0.2042  -0.0777 355 TYR   A CA  
2434 C  C   . TYR   A 335 ? 1.0527 1.0614 1.0505 0.0965  0.1843  -0.0783 355 TYR   A C   
2435 O  O   . TYR   A 335 ? 1.0724 1.0855 1.0569 0.0833  0.1754  -0.0845 355 TYR   A O   
2436 C  CB  . TYR   A 335 ? 1.1255 1.1029 1.0778 0.1356  0.2069  -0.1005 355 TYR   A CB  
2437 C  CG  . TYR   A 335 ? 1.1542 1.1224 1.0647 0.1350  0.2012  -0.1178 355 TYR   A CG  
2438 C  CD1 . TYR   A 335 ? 1.1240 1.1101 1.0125 0.1481  0.2149  -0.1115 355 TYR   A CD1 
2439 C  CD2 . TYR   A 335 ? 1.1563 1.0956 1.0490 0.1233  0.1824  -0.1413 355 TYR   A CD2 
2440 C  CE1 . TYR   A 335 ? 1.1848 1.1584 1.0262 0.1530  0.2067  -0.1275 355 TYR   A CE1 
2441 C  CE2 . TYR   A 335 ? 1.1794 1.1126 1.0354 0.1259  0.1715  -0.1607 355 TYR   A CE2 
2442 C  CZ  . TYR   A 335 ? 1.2135 1.1627 1.0394 0.1428  0.1821  -0.1535 355 TYR   A CZ  
2443 O  OH  . TYR   A 335 ? 1.1684 1.1079 0.9489 0.1506  0.1687  -0.1724 355 TYR   A OH  
2444 N  N   . LEU   A 336 ? 1.0546 1.0515 1.0712 0.0918  0.1781  -0.0713 356 LEU   A N   
2445 C  CA  . LEU   A 336 ? 1.1436 1.1349 1.1672 0.0696  0.1647  -0.0676 356 LEU   A CA  
2446 C  C   . LEU   A 336 ? 1.0030 1.0329 1.0459 0.0590  0.1601  -0.0532 356 LEU   A C   
2447 O  O   . LEU   A 336 ? 0.9825 1.0154 1.0231 0.0410  0.1513  -0.0551 356 LEU   A O   
2448 C  CB  . LEU   A 336 ? 1.1166 1.0808 1.1461 0.0727  0.1624  -0.0601 356 LEU   A CB  
2449 C  CG  . LEU   A 336 ? 1.0482 0.9983 1.0788 0.0537  0.1540  -0.0533 356 LEU   A CG  
2450 C  CD1 . LEU   A 336 ? 1.0776 1.0077 1.0976 0.0333  0.1530  -0.0698 356 LEU   A CD1 
2451 C  CD2 . LEU   A 336 ? 1.1135 1.0294 1.1383 0.0647  0.1544  -0.0435 356 LEU   A CD2 
2452 N  N   . ASP   A 337 ? 1.0006 1.0606 1.0670 0.0699  0.1667  -0.0400 357 ASP   A N   
2453 C  CA  . ASP   A 337 ? 0.9664 1.0603 1.0544 0.0595  0.1635  -0.0277 357 ASP   A CA  
2454 C  C   . ASP   A 337 ? 0.9618 1.0659 1.0315 0.0561  0.1702  -0.0311 357 ASP   A C   
2455 O  O   . ASP   A 337 ? 0.9277 1.0425 0.9980 0.0419  0.1626  -0.0275 357 ASP   A O   
2456 C  CB  . ASP   A 337 ? 0.9478 1.0717 1.0759 0.0707  0.1687  -0.0154 357 ASP   A CB  
2457 C  CG  . ASP   A 337 ? 0.9349 1.0884 1.0922 0.0574  0.1608  -0.0044 357 ASP   A CG  
2458 O  OD1 . ASP   A 337 ? 0.8904 1.0351 1.0421 0.0447  0.1446  -0.0030 357 ASP   A OD1 
2459 O  OD2 . ASP   A 337 ? 0.9380 1.1212 1.1245 0.0597  0.1728  0.0027  357 ASP   A OD2 
2460 N  N   . MET   A 338 ? 0.9865 1.0838 1.0345 0.0720  0.1845  -0.0382 358 MET   A N   
2461 C  CA  . MET   A 338 ? 0.9138 1.0130 0.9315 0.0746  0.1904  -0.0415 358 MET   A CA  
2462 C  C   . MET   A 338 ? 1.0131 1.0962 1.0055 0.0622  0.1712  -0.0568 358 MET   A C   
2463 O  O   . MET   A 338 ? 0.9450 1.0379 0.9270 0.0564  0.1659  -0.0546 358 MET   A O   
2464 C  CB  . MET   A 338 ? 0.9647 1.0519 0.9537 0.0979  0.2093  -0.0483 358 MET   A CB  
2465 C  CG  . MET   A 338 ? 0.9818 1.0890 1.0031 0.1116  0.2324  -0.0347 358 MET   A CG  
2466 S  SD  . MET   A 338 ? 0.9188 1.0049 0.9058 0.1415  0.2555  -0.0460 358 MET   A SD  
2467 C  CE  . MET   A 338 ? 1.0652 1.1268 0.9802 0.1481  0.2533  -0.0585 358 MET   A CE  
2468 N  N   . VAL   A 339 ? 0.9976 1.0556 0.9837 0.0585  0.1614  -0.0730 359 VAL   A N   
2469 C  CA  . VAL   A 339 ? 0.9399 0.9867 0.9160 0.0443  0.1439  -0.0902 359 VAL   A CA  
2470 C  C   . VAL   A 339 ? 0.9316 0.9945 0.9336 0.0243  0.1350  -0.0794 359 VAL   A C   
2471 O  O   . VAL   A 339 ? 0.9969 1.0697 0.9948 0.0160  0.1244  -0.0850 359 VAL   A O   
2472 C  CB  . VAL   A 339 ? 1.0691 1.0828 1.0416 0.0420  0.1395  -0.1096 359 VAL   A CB  
2473 C  CG1 . VAL   A 339 ? 0.9985 1.0058 0.9812 0.0212  0.1239  -0.1256 359 VAL   A CG1 
2474 C  CG2 . VAL   A 339 ? 1.0411 1.0364 0.9798 0.0623  0.1438  -0.1269 359 VAL   A CG2 
2475 N  N   . VAL   A 340 ? 0.9509 1.0157 0.9770 0.0189  0.1381  -0.0647 360 VAL   A N   
2476 C  CA  . VAL   A 340 ? 0.9607 1.0375 1.0053 0.0029  0.1307  -0.0544 360 VAL   A CA  
2477 C  C   . VAL   A 340 ? 0.8873 0.9918 0.9352 0.0025  0.1303  -0.0441 360 VAL   A C   
2478 O  O   . VAL   A 340 ? 0.8551 0.9669 0.9022 -0.0080 0.1217  -0.0468 360 VAL   A O   
2479 C  CB  . VAL   A 340 ? 0.9921 1.0629 1.0530 0.0036  0.1320  -0.0410 360 VAL   A CB  
2480 C  CG1 . VAL   A 340 ? 0.9418 1.0304 1.0177 -0.0066 0.1250  -0.0282 360 VAL   A CG1 
2481 C  CG2 . VAL   A 340 ? 0.9273 0.9624 0.9806 -0.0013 0.1323  -0.0486 360 VAL   A CG2 
2482 N  N   . ASN   A 341 ? 0.9475 1.0666 1.0019 0.0142  0.1417  -0.0322 361 ASN   A N   
2483 C  CA  . ASN   A 341 ? 0.9002 1.0403 0.9607 0.0128  0.1460  -0.0200 361 ASN   A CA  
2484 C  C   . ASN   A 341 ? 0.9085 1.0444 0.9369 0.0158  0.1430  -0.0279 361 ASN   A C   
2485 O  O   . ASN   A 341 ? 0.8482 0.9931 0.8777 0.0086  0.1373  -0.0225 361 ASN   A O   
2486 C  CB  . ASN   A 341 ? 0.8633 1.0174 0.9402 0.0249  0.1645  -0.0080 361 ASN   A CB  
2487 C  CG  . ASN   A 341 ? 0.8673 1.0350 0.9854 0.0226  0.1619  0.0002  361 ASN   A CG  
2488 O  OD1 . ASN   A 341 ? 0.9506 1.1105 1.0742 0.0149  0.1468  -0.0021 361 ASN   A OD1 
2489 N  ND2 . ASN   A 341 ? 0.9455 1.1328 1.0927 0.0309  0.1771  0.0092  361 ASN   A ND2 
2490 N  N   . GLU   A 342 ? 0.9399 1.0605 0.9371 0.0288  0.1450  -0.0418 362 GLU   A N   
2491 C  CA  . GLU   A 342 ? 0.9013 1.0166 0.8614 0.0377  0.1390  -0.0505 362 GLU   A CA  
2492 C  C   . GLU   A 342 ? 0.9305 1.0480 0.8956 0.0244  0.1167  -0.0643 362 GLU   A C   
2493 O  O   . GLU   A 342 ? 0.9819 1.1055 0.9329 0.0271  0.1089  -0.0635 362 GLU   A O   
2494 C  CB  . GLU   A 342 ? 1.0151 1.1107 0.9364 0.0573  0.1430  -0.0659 362 GLU   A CB  
2495 C  CG  . GLU   A 342 ? 1.0178 1.1031 0.8941 0.0697  0.1282  -0.0823 362 GLU   A CG  
2496 C  CD  . GLU   A 342 ? 1.0255 1.1104 0.8672 0.0857  0.1406  -0.0656 362 GLU   A CD  
2497 O  OE1 . GLU   A 342 ? 0.9652 1.0631 0.8306 0.0785  0.1568  -0.0416 362 GLU   A OE1 
2498 O  OE2 . GLU   A 342 ? 1.0247 1.0929 0.8131 0.1065  0.1340  -0.0771 362 GLU   A OE2 
2499 N  N   . THR   A 343 ? 0.8627 0.9741 0.8491 0.0110  0.1082  -0.0766 363 THR   A N   
2500 C  CA  . THR   A 343 ? 0.9393 1.0565 0.9417 -0.0039 0.0921  -0.0886 363 THR   A CA  
2501 C  C   . THR   A 343 ? 0.9343 1.0687 0.9531 -0.0128 0.0918  -0.0717 363 THR   A C   
2502 O  O   . THR   A 343 ? 0.8622 1.0066 0.8797 -0.0143 0.0803  -0.0774 363 THR   A O   
2503 C  CB  . THR   A 343 ? 0.9750 1.0785 1.0011 -0.0187 0.0916  -0.0991 363 THR   A CB  
2504 O  OG1 . THR   A 343 ? 1.0023 1.0859 1.0139 -0.0107 0.0914  -0.1167 363 THR   A OG1 
2505 C  CG2 . THR   A 343 ? 0.9510 1.0628 1.0002 -0.0348 0.0800  -0.1122 363 THR   A CG2 
2506 N  N   . LEU   A 344 ? 0.9388 1.0765 0.9734 -0.0170 0.1026  -0.0525 364 LEU   A N   
2507 C  CA  . LEU   A 344 ? 0.8800 1.0307 0.9294 -0.0249 0.1014  -0.0383 364 LEU   A CA  
2508 C  C   . LEU   A 344 ? 0.8261 0.9840 0.8587 -0.0152 0.1036  -0.0299 364 LEU   A C   
2509 O  O   . LEU   A 344 ? 0.7988 0.9637 0.8374 -0.0206 0.0985  -0.0242 364 LEU   A O   
2510 C  CB  . LEU   A 344 ? 0.8159 0.9682 0.8858 -0.0287 0.1085  -0.0235 364 LEU   A CB  
2511 C  CG  . LEU   A 344 ? 0.8501 0.9895 0.9297 -0.0375 0.1055  -0.0274 364 LEU   A CG  
2512 C  CD1 . LEU   A 344 ? 0.8304 0.9701 0.9239 -0.0349 0.1078  -0.0146 364 LEU   A CD1 
2513 C  CD2 . LEU   A 344 ? 0.8754 1.0156 0.9603 -0.0502 0.0985  -0.0315 364 LEU   A CD2 
2514 N  N   . ARG   A 345 ? 0.9169 1.0685 0.9243 0.0006  0.1133  -0.0282 365 ARG   A N   
2515 C  CA  . ARG   A 345 ? 0.9393 1.0889 0.9200 0.0127  0.1180  -0.0193 365 ARG   A CA  
2516 C  C   . ARG   A 345 ? 0.9382 1.0860 0.8966 0.0184  0.0983  -0.0349 365 ARG   A C   
2517 O  O   . ARG   A 345 ? 0.9566 1.1066 0.9090 0.0201  0.0936  -0.0280 365 ARG   A O   
2518 C  CB  . ARG   A 345 ? 0.9106 1.0492 0.8623 0.0312  0.1370  -0.0133 365 ARG   A CB  
2519 C  CG  . ARG   A 345 ? 0.9709 1.1003 0.8921 0.0443  0.1499  0.0024  365 ARG   A CG  
2520 C  CD  . ARG   A 345 ? 0.9940 1.1067 0.8746 0.0662  0.1713  0.0069  365 ARG   A CD  
2521 N  NE  . ARG   A 345 ? 1.0576 1.1577 0.8993 0.0809  0.1561  -0.0165 365 ARG   A NE  
2522 C  CZ  . ARG   A 345 ? 1.1233 1.2108 0.9190 0.0966  0.1377  -0.0293 365 ARG   A CZ  
2523 N  NH1 . ARG   A 345 ? 1.2124 1.2959 0.9904 0.1017  0.1335  -0.0189 365 ARG   A NH1 
2524 N  NH2 . ARG   A 345 ? 1.1796 1.2573 0.9471 0.1086  0.1211  -0.0546 365 ARG   A NH2 
2525 N  N   . LEU   A 346 ? 0.9226 1.0665 0.8720 0.0218  0.0850  -0.0578 366 LEU   A N   
2526 C  CA  . LEU   A 346 ? 0.9311 1.0783 0.8670 0.0285  0.0622  -0.0774 366 LEU   A CA  
2527 C  C   . LEU   A 346 ? 0.9739 1.1381 0.9503 0.0101  0.0506  -0.0832 366 LEU   A C   
2528 O  O   . LEU   A 346 ? 1.0044 1.1775 0.9777 0.0160  0.0344  -0.0918 366 LEU   A O   
2529 C  CB  . LEU   A 346 ? 1.0430 1.1816 0.9636 0.0366  0.0498  -0.1041 366 LEU   A CB  
2530 C  CG  . LEU   A 346 ? 1.0931 1.2122 0.9557 0.0640  0.0531  -0.1063 366 LEU   A CG  
2531 C  CD1 . LEU   A 346 ? 1.1445 1.2537 0.9969 0.0696  0.0378  -0.1371 366 LEU   A CD1 
2532 C  CD2 . LEU   A 346 ? 1.1169 1.2320 0.9379 0.0849  0.0430  -0.1024 366 LEU   A CD2 
2533 N  N   . PHE   A 347 ? 0.9360 1.1034 0.9475 -0.0095 0.0591  -0.0784 367 PHE   A N   
2534 C  CA  . PHE   A 347 ? 0.9125 1.0918 0.9585 -0.0262 0.0535  -0.0830 367 PHE   A CA  
2535 C  C   . PHE   A 347 ? 0.8733 1.0508 0.9350 -0.0379 0.0668  -0.0625 367 PHE   A C   
2536 O  O   . PHE   A 347 ? 0.8629 1.0346 0.9425 -0.0502 0.0728  -0.0628 367 PHE   A O   
2537 C  CB  . PHE   A 347 ? 0.9201 1.0994 0.9911 -0.0379 0.0482  -0.1056 367 PHE   A CB  
2538 C  CG  . PHE   A 347 ? 0.9569 1.1375 1.0165 -0.0268 0.0311  -0.1311 367 PHE   A CG  
2539 C  CD1 . PHE   A 347 ? 0.9814 1.1777 1.0384 -0.0164 0.0111  -0.1448 367 PHE   A CD1 
2540 C  CD2 . PHE   A 347 ? 1.0180 1.1824 1.0683 -0.0247 0.0327  -0.1433 367 PHE   A CD2 
2541 C  CE1 . PHE   A 347 ? 1.0145 1.2121 1.0591 -0.0033 -0.0100 -0.1716 367 PHE   A CE1 
2542 C  CE2 . PHE   A 347 ? 1.0006 1.1641 1.0383 -0.0134 0.0137  -0.1703 367 PHE   A CE2 
2543 C  CZ  . PHE   A 347 ? 1.0007 1.1815 1.0352 -0.0024 -0.0091 -0.1854 367 PHE   A CZ  
2544 N  N   . PRO   A 348 ? 0.8562 1.0356 0.9100 -0.0334 0.0707  -0.0451 368 PRO   A N   
2545 C  CA  . PRO   A 348 ? 0.8741 1.0532 0.9453 -0.0441 0.0775  -0.0304 368 PRO   A CA  
2546 C  C   . PRO   A 348 ? 0.9087 1.0931 0.9961 -0.0541 0.0716  -0.0359 368 PRO   A C   
2547 O  O   . PRO   A 348 ? 0.9390 1.1293 1.0246 -0.0506 0.0659  -0.0349 368 PRO   A O   
2548 C  CB  . PRO   A 348 ? 0.8390 1.0172 0.9005 -0.0367 0.0835  -0.0138 368 PRO   A CB  
2549 C  CG  . PRO   A 348 ? 0.8761 1.0531 0.9117 -0.0226 0.0773  -0.0190 368 PRO   A CG  
2550 C  CD  . PRO   A 348 ? 0.8368 1.0142 0.8629 -0.0173 0.0696  -0.0384 368 PRO   A CD  
2551 N  N   . ILE   A 349 ? 0.8800 1.0590 0.9807 -0.0649 0.0755  -0.0407 369 ILE   A N   
2552 C  CA  . ILE   A 349 ? 0.9130 1.0958 1.0291 -0.0738 0.0752  -0.0485 369 ILE   A CA  
2553 C  C   . ILE   A 349 ? 0.9023 1.0868 1.0179 -0.0741 0.0739  -0.0390 369 ILE   A C   
2554 O  O   . ILE   A 349 ? 0.9230 1.1121 1.0499 -0.0786 0.0750  -0.0455 369 ILE   A O   
2555 C  CB  . ILE   A 349 ? 0.9537 1.1211 1.0768 -0.0842 0.0861  -0.0504 369 ILE   A CB  
2556 C  CG1 . ILE   A 349 ? 0.8983 1.0497 1.0072 -0.0817 0.0903  -0.0348 369 ILE   A CG1 
2557 C  CG2 . ILE   A 349 ? 0.9358 1.1009 1.0680 -0.0870 0.0870  -0.0661 369 ILE   A CG2 
2558 C  CD1 . ILE   A 349 ? 0.9661 1.0993 1.0692 -0.0870 0.0981  -0.0289 369 ILE   A CD1 
2559 N  N   . ALA   A 350 ? 0.9169 1.0975 1.0230 -0.0698 0.0728  -0.0252 370 ALA   A N   
2560 C  CA  . ALA   A 350 ? 0.9038 1.0827 1.0100 -0.0702 0.0700  -0.0186 370 ALA   A CA  
2561 C  C   . ALA   A 350 ? 0.9184 1.1035 1.0198 -0.0617 0.0644  -0.0184 370 ALA   A C   
2562 O  O   . ALA   A 350 ? 0.9443 1.1283 1.0474 -0.0611 0.0614  -0.0185 370 ALA   A O   
2563 C  CB  . ALA   A 350 ? 0.8261 0.9970 0.9323 -0.0716 0.0701  -0.0064 370 ALA   A CB  
2564 N  N   . MET   A 351 ? 0.9002 1.0878 0.9903 -0.0525 0.0635  -0.0178 371 MET   A N   
2565 C  CA  . MET   A 351 ? 0.9014 1.0892 0.9763 -0.0391 0.0577  -0.0171 371 MET   A CA  
2566 C  C   . MET   A 351 ? 0.8946 1.0689 0.9628 -0.0369 0.0627  -0.0007 371 MET   A C   
2567 O  O   . MET   A 351 ? 0.8362 1.0004 0.8847 -0.0263 0.0677  0.0092  371 MET   A O   
2568 C  CB  . MET   A 351 ? 0.8297 1.0303 0.9144 -0.0357 0.0470  -0.0325 371 MET   A CB  
2569 C  CG  . MET   A 351 ? 0.9583 1.1733 1.0578 -0.0389 0.0422  -0.0517 371 MET   A CG  
2570 S  SD  . MET   A 351 ? 1.0080 1.2457 1.1366 -0.0373 0.0315  -0.0723 371 MET   A SD  
2571 C  CE  . MET   A 351 ? 1.0737 1.3059 1.2197 -0.0528 0.0466  -0.0656 371 MET   A CE  
2572 N  N   . ARG   A 352 ? 0.8948 1.0652 0.9771 -0.0464 0.0625  0.0019  372 ARG   A N   
2573 C  CA  . ARG   A 352 ? 0.8399 0.9957 0.9231 -0.0477 0.0662  0.0144  372 ARG   A CA  
2574 C  C   . ARG   A 352 ? 0.8311 0.9847 0.9335 -0.0609 0.0662  0.0159  372 ARG   A C   
2575 O  O   . ARG   A 352 ? 0.8763 1.0344 0.9826 -0.0661 0.0619  0.0075  372 ARG   A O   
2576 C  CB  . ARG   A 352 ? 0.8929 1.0412 0.9697 -0.0408 0.0600  0.0122  372 ARG   A CB  
2577 C  CG  . ARG   A 352 ? 0.9221 1.0744 0.9810 -0.0239 0.0534  0.0070  372 ARG   A CG  
2578 C  CD  . ARG   A 352 ? 0.9785 1.1295 1.0408 -0.0182 0.0458  0.0004  372 ARG   A CD  
2579 N  NE  . ARG   A 352 ? 0.9923 1.1400 1.0352 0.0026  0.0376  -0.0005 372 ARG   A NE  
2580 C  CZ  . ARG   A 352 ? 1.0096 1.1506 1.0506 0.0131  0.0315  -0.0026 372 ARG   A CZ  
2581 N  NH1 . ARG   A 352 ? 1.0622 1.1981 1.1182 0.0039  0.0342  -0.0045 372 ARG   A NH1 
2582 N  NH2 . ARG   A 352 ? 1.0976 1.2344 1.1172 0.0361  0.0216  -0.0032 372 ARG   A NH2 
2583 N  N   . LEU   A 353 ? 0.8347 0.9798 0.9491 -0.0654 0.0712  0.0261  373 LEU   A N   
2584 C  CA  . LEU   A 353 ? 0.8597 1.0014 0.9949 -0.0758 0.0652  0.0244  373 LEU   A CA  
2585 C  C   . LEU   A 353 ? 0.8041 0.9284 0.9415 -0.0772 0.0628  0.0264  373 LEU   A C   
2586 O  O   . LEU   A 353 ? 0.8628 0.9756 0.9919 -0.0717 0.0715  0.0354  373 LEU   A O   
2587 C  CB  . LEU   A 353 ? 0.8289 0.9786 0.9903 -0.0817 0.0710  0.0306  373 LEU   A CB  
2588 C  CG  . LEU   A 353 ? 0.8770 1.0395 1.0352 -0.0770 0.0793  0.0327  373 LEU   A CG  
2589 C  CD1 . LEU   A 353 ? 0.7769 0.9482 0.9673 -0.0813 0.0886  0.0398  373 LEU   A CD1 
2590 C  CD2 . LEU   A 353 ? 0.8596 1.0274 1.0084 -0.0763 0.0701  0.0227  373 LEU   A CD2 
2591 N  N   . GLU   A 354 ? 0.8709 0.9884 1.0143 -0.0825 0.0511  0.0177  374 GLU   A N   
2592 C  CA  . GLU   A 354 ? 0.8540 0.9513 0.9972 -0.0832 0.0473  0.0163  374 GLU   A CA  
2593 C  C   . GLU   A 354 ? 0.8572 0.9473 1.0205 -0.0926 0.0343  0.0079  374 GLU   A C   
2594 O  O   . GLU   A 354 ? 0.8673 0.9660 1.0309 -0.0936 0.0237  0.0000  374 GLU   A O   
2595 C  CB  . GLU   A 354 ? 0.9305 1.0225 1.0485 -0.0735 0.0436  0.0087  374 GLU   A CB  
2596 C  CG  . GLU   A 354 ? 0.9085 1.0080 1.0114 -0.0619 0.0505  0.0129  374 GLU   A CG  
2597 C  CD  . GLU   A 354 ? 0.9681 1.0672 1.0583 -0.0521 0.0464  0.0034  374 GLU   A CD  
2598 O  OE1 . GLU   A 354 ? 0.9807 1.0719 1.0690 -0.0542 0.0418  -0.0052 374 GLU   A OE1 
2599 O  OE2 . GLU   A 354 ? 1.0071 1.1140 1.0890 -0.0403 0.0473  0.0035  374 GLU   A OE2 
2600 N  N   . ARG   A 355 ? 0.9509 1.0221 1.1296 -0.0981 0.0340  0.0088  375 ARG   A N   
2601 C  CA  . ARG   A 355 ? 0.9538 1.0145 1.1532 -0.1066 0.0177  -0.0037 375 ARG   A CA  
2602 C  C   . ARG   A 355 ? 1.0042 1.0347 1.1960 -0.1058 0.0168  -0.0067 375 ARG   A C   
2603 O  O   . ARG   A 355 ? 0.9624 0.9794 1.1527 -0.1041 0.0325  0.0061  375 ARG   A O   
2604 C  CB  . ARG   A 355 ? 0.9252 0.9971 1.1753 -0.1202 0.0188  -0.0018 375 ARG   A CB  
2605 C  CG  . ARG   A 355 ? 0.9385 1.0395 1.2012 -0.1196 0.0201  0.0010  375 ARG   A CG  
2606 C  CD  . ARG   A 355 ? 0.9239 1.0321 1.1755 -0.1145 -0.0035 -0.0139 375 ARG   A CD  
2607 N  NE  . ARG   A 355 ? 0.8002 0.9326 1.0628 -0.1118 -0.0016 -0.0102 375 ARG   A NE  
2608 C  CZ  . ARG   A 355 ? 0.7746 0.9129 1.0059 -0.1031 0.0074  -0.0040 375 ARG   A CZ  
2609 N  NH1 . ARG   A 355 ? 0.8546 0.9812 1.0466 -0.0970 0.0141  -0.0022 375 ARG   A NH1 
2610 N  NH2 . ARG   A 355 ? 0.8607 1.0175 1.1049 -0.1006 0.0098  -0.0009 375 ARG   A NH2 
2611 N  N   . VAL   A 356 ? 1.0332 1.0490 1.2151 -0.1045 -0.0014 -0.0234 376 VAL   A N   
2612 C  CA  . VAL   A 356 ? 1.0390 1.0225 1.2165 -0.1039 -0.0040 -0.0290 376 VAL   A CA  
2613 C  C   . VAL   A 356 ? 1.0563 1.0281 1.2816 -0.1210 -0.0081 -0.0326 376 VAL   A C   
2614 O  O   . VAL   A 356 ? 1.0404 1.0293 1.2990 -0.1308 -0.0213 -0.0418 376 VAL   A O   
2615 C  CB  . VAL   A 356 ? 1.1020 1.0707 1.2441 -0.0932 -0.0198 -0.0469 376 VAL   A CB  
2616 C  CG1 . VAL   A 356 ? 1.0431 1.0287 1.1500 -0.0801 -0.0126 -0.0441 376 VAL   A CG1 
2617 C  CG2 . VAL   A 356 ? 1.1504 1.1155 1.3030 -0.0986 -0.0447 -0.0659 376 VAL   A CG2 
2618 N  N   . CYS   A 357 ? 1.1424 1.0849 1.3751 -0.1243 0.0039  -0.0256 377 CYS   A N   
2619 C  CA  . CYS   A 357 ? 1.0657 0.9904 1.3484 -0.1428 0.0039  -0.0297 377 CYS   A CA  
2620 C  C   . CYS   A 357 ? 1.1070 1.0030 1.3834 -0.1427 -0.0195 -0.0536 377 CYS   A C   
2621 O  O   . CYS   A 357 ? 1.1714 1.0365 1.4138 -0.1316 -0.0163 -0.0537 377 CYS   A O   
2622 C  CB  . CYS   A 357 ? 1.0849 0.9851 1.3744 -0.1457 0.0337  -0.0068 377 CYS   A CB  
2623 S  SG  . CYS   A 357 ? 1.2634 1.1393 1.6238 -0.1724 0.0434  -0.0083 377 CYS   A SG  
2624 N  N   . LYS   A 358 ? 1.1466 1.0524 1.4533 -0.1523 -0.0451 -0.0756 378 LYS   A N   
2625 C  CA  . LYS   A 358 ? 1.1678 1.0468 1.4602 -0.1488 -0.0727 -0.1027 378 LYS   A CA  
2626 C  C   . LYS   A 358 ? 1.1908 1.0402 1.5349 -0.1678 -0.0776 -0.1150 378 LYS   A C   
2627 O  O   . LYS   A 358 ? 1.2270 1.0509 1.5635 -0.1661 -0.1032 -0.1411 378 LYS   A O   
2628 C  CB  . LYS   A 358 ? 1.1942 1.0956 1.4772 -0.1425 -0.1036 -0.1232 378 LYS   A CB  
2629 C  CG  . LYS   A 358 ? 1.1754 1.1112 1.5226 -0.1578 -0.1143 -0.1279 378 LYS   A CG  
2630 C  CD  . LYS   A 358 ? 1.1434 1.0980 1.4669 -0.1444 -0.1453 -0.1451 378 LYS   A CD  
2631 C  CE  . LYS   A 358 ? 1.1676 1.1635 1.5523 -0.1545 -0.1529 -0.1459 378 LYS   A CE  
2632 N  NZ  . LYS   A 358 ? 1.2101 1.2102 1.6434 -0.1615 -0.1918 -0.1776 378 LYS   A NZ  
2633 N  N   . LYS   A 359 ? 1.1695 1.0184 1.5646 -0.1856 -0.0521 -0.0973 379 LYS   A N   
2634 C  CA  . LYS   A 359 ? 1.2358 1.0533 1.6877 -0.2070 -0.0495 -0.1060 379 LYS   A CA  
2635 C  C   . LYS   A 359 ? 1.2605 1.0581 1.7252 -0.2143 -0.0062 -0.0737 379 LYS   A C   
2636 O  O   . LYS   A 359 ? 1.2862 1.1073 1.7364 -0.2077 0.0171  -0.0485 379 LYS   A O   
2637 C  CB  . LYS   A 359 ? 1.2063 1.0528 1.7397 -0.2290 -0.0693 -0.1270 379 LYS   A CB  
2638 C  CG  . LYS   A 359 ? 1.2426 1.1072 1.7669 -0.2205 -0.1164 -0.1609 379 LYS   A CG  
2639 C  CD  . LYS   A 359 ? 1.2187 1.1196 1.8327 -0.2405 -0.1354 -0.1796 379 LYS   A CD  
2640 C  CE  . LYS   A 359 ? 1.1732 1.0599 1.8738 -0.2709 -0.1107 -0.1753 379 LYS   A CE  
2641 N  NZ  . LYS   A 359 ? 1.1612 1.0620 1.9512 -0.2916 -0.1437 -0.2117 379 LYS   A NZ  
2642 N  N   . ASP   A 360 ? 1.2460 0.9958 1.7346 -0.2266 0.0048  -0.0747 380 ASP   A N   
2643 C  CA  . ASP   A 360 ? 1.2975 1.0241 1.8115 -0.2381 0.0479  -0.0447 380 ASP   A CA  
2644 C  C   . ASP   A 360 ? 1.2622 1.0316 1.8489 -0.2590 0.0612  -0.0394 380 ASP   A C   
2645 O  O   . ASP   A 360 ? 1.2531 1.0525 1.9018 -0.2753 0.0352  -0.0662 380 ASP   A O   
2646 C  CB  . ASP   A 360 ? 1.3779 1.0431 1.9184 -0.2525 0.0567  -0.0502 380 ASP   A CB  
2647 C  CG  . ASP   A 360 ? 1.4418 1.0589 1.9082 -0.2284 0.0524  -0.0491 380 ASP   A CG  
2648 O  OD1 . ASP   A 360 ? 1.4035 1.0168 1.8072 -0.2043 0.0697  -0.0240 380 ASP   A OD1 
2649 O  OD2 . ASP   A 360 ? 1.5458 1.1295 2.0184 -0.2325 0.0302  -0.0755 380 ASP   A OD2 
2650 N  N   . VAL   A 361 ? 1.2807 1.0538 1.8583 -0.2559 0.1006  -0.0059 381 VAL   A N   
2651 C  CA  . VAL   A 361 ? 1.2663 1.0829 1.9054 -0.2712 0.1178  0.0016  381 VAL   A CA  
2652 C  C   . VAL   A 361 ? 1.3416 1.1335 1.9665 -0.2692 0.1708  0.0406  381 VAL   A C   
2653 O  O   . VAL   A 361 ? 1.3977 1.1529 1.9471 -0.2476 0.1859  0.0620  381 VAL   A O   
2654 C  CB  . VAL   A 361 ? 1.2351 1.1105 1.8533 -0.2568 0.0927  -0.0071 381 VAL   A CB  
2655 C  CG1 . VAL   A 361 ? 1.2115 1.0859 1.7422 -0.2289 0.1052  0.0164  381 VAL   A CG1 
2656 C  CG2 . VAL   A 361 ? 1.2155 1.1388 1.9103 -0.2732 0.1021  -0.0078 381 VAL   A CG2 
2657 N  N   . GLU   A 362 ? 1.2700 1.0814 1.9675 -0.2899 0.1992  0.0491  382 GLU   A N   
2658 C  CA  . GLU   A 362 ? 1.3128 1.1045 1.9977 -0.2872 0.2537  0.0867  382 GLU   A CA  
2659 C  C   . GLU   A 362 ? 1.2875 1.1395 2.0100 -0.2898 0.2628  0.0894  382 GLU   A C   
2660 O  O   . GLU   A 362 ? 1.3025 1.1818 2.1212 -0.3152 0.2729  0.0799  382 GLU   A O   
2661 C  CB  . GLU   A 362 ? 1.4079 1.1494 2.1494 -0.3121 0.2929  0.0984  382 GLU   A CB  
2662 C  CG  . GLU   A 362 ? 1.5458 1.2120 2.2243 -0.3006 0.3022  0.1116  382 GLU   A CG  
2663 C  CD  . GLU   A 362 ? 1.6258 1.2505 2.3753 -0.3302 0.3059  0.0968  382 GLU   A CD  
2664 O  OE1 . GLU   A 362 ? 1.6586 1.3168 2.5126 -0.3612 0.3005  0.0748  382 GLU   A OE1 
2665 O  OE2 . GLU   A 362 ? 1.6708 1.2296 2.3743 -0.3218 0.3126  0.1054  382 GLU   A OE2 
2666 N  N   . ILE   A 363 ? 1.3878 1.2616 2.0397 -0.2636 0.2586  0.1004  383 ILE   A N   
2667 C  CA  . ILE   A 363 ? 1.3638 1.2889 2.0384 -0.2613 0.2688  0.1047  383 ILE   A CA  
2668 C  C   . ILE   A 363 ? 1.4339 1.3324 2.0690 -0.2498 0.3226  0.1417  383 ILE   A C   
2669 O  O   . ILE   A 363 ? 1.4582 1.3135 2.0067 -0.2276 0.3333  0.1614  383 ILE   A O   
2670 C  CB  . ILE   A 363 ? 1.3034 1.2687 1.9291 -0.2408 0.2284  0.0898  383 ILE   A CB  
2671 C  CG1 . ILE   A 363 ? 1.2589 1.1986 1.7798 -0.2116 0.2309  0.1069  383 ILE   A CG1 
2672 C  CG2 . ILE   A 363 ? 1.2416 1.2210 1.8877 -0.2471 0.1779  0.0559  383 ILE   A CG2 
2673 C  CD1 . ILE   A 363 ? 1.2459 1.2203 1.7244 -0.1946 0.1945  0.0917  383 ILE   A CD1 
2674 N  N   . ASN   A 364 ? 1.4774 1.4004 2.1758 -0.2631 0.3564  0.1503  384 ASN   A N   
2675 C  CA  . ASN   A 364 ? 1.5141 1.4152 2.1766 -0.2510 0.4110  0.1847  384 ASN   A CA  
2676 C  C   . ASN   A 364 ? 1.5276 1.3517 2.1246 -0.2410 0.4436  0.2130  384 ASN   A C   
2677 O  O   . ASN   A 364 ? 1.5754 1.3693 2.0775 -0.2118 0.4600  0.2364  384 ASN   A O   
2678 C  CB  . ASN   A 364 ? 1.5009 1.4310 2.0939 -0.2225 0.4005  0.1885  384 ASN   A CB  
2679 C  CG  . ASN   A 364 ? 1.4235 1.4234 2.0787 -0.2299 0.3748  0.1647  384 ASN   A CG  
2680 O  OD1 . ASN   A 364 ? 1.3641 1.3922 2.0137 -0.2267 0.3253  0.1399  384 ASN   A OD1 
2681 N  ND2 . ASN   A 364 ? 1.4099 1.4358 2.1235 -0.2383 0.4101  0.1727  384 ASN   A ND2 
2682 N  N   . GLY   A 365 ? 1.4327 1.2223 2.0805 -0.2643 0.4505  0.2092  385 GLY   A N   
2683 C  CA  . GLY   A 365 ? 1.4777 1.1877 2.0733 -0.2572 0.4866  0.2376  385 GLY   A CA  
2684 C  C   . GLY   A 365 ? 1.5443 1.2165 2.0406 -0.2292 0.4557  0.2383  385 GLY   A C   
2685 O  O   . GLY   A 365 ? 1.5987 1.2036 2.0300 -0.2128 0.4844  0.2657  385 GLY   A O   
2686 N  N   . MET   A 366 ? 1.4555 1.1674 1.9384 -0.2218 0.3994  0.2095  386 MET   A N   
2687 C  CA  . MET   A 366 ? 1.4584 1.1434 1.8556 -0.1948 0.3697  0.2073  386 MET   A CA  
2688 C  C   . MET   A 366 ? 1.4380 1.1373 1.8696 -0.2076 0.3224  0.1730  386 MET   A C   
2689 O  O   . MET   A 366 ? 1.3898 1.1449 1.8692 -0.2199 0.2911  0.1464  386 MET   A O   
2690 C  CB  . MET   A 366 ? 1.4885 1.2053 1.8117 -0.1638 0.3521  0.2094  386 MET   A CB  
2691 C  CG  . MET   A 366 ? 1.5116 1.2207 1.7689 -0.1396 0.3133  0.1980  386 MET   A CG  
2692 S  SD  . MET   A 366 ? 1.3831 1.1163 1.5535 -0.1024 0.3020  0.2049  386 MET   A SD  
2693 C  CE  . MET   A 366 ? 1.5392 1.2171 1.6573 -0.0850 0.3572  0.2456  386 MET   A CE  
2694 N  N   . PHE   A 367 ? 1.4621 1.1077 1.8624 -0.2013 0.3171  0.1740  387 PHE   A N   
2695 C  CA  . PHE   A 367 ? 1.4125 1.0613 1.8328 -0.2091 0.2747  0.1421  387 PHE   A CA  
2696 C  C   . PHE   A 367 ? 1.4168 1.0914 1.7695 -0.1809 0.2368  0.1299  387 PHE   A C   
2697 O  O   . PHE   A 367 ? 1.4779 1.1265 1.7558 -0.1521 0.2420  0.1466  387 PHE   A O   
2698 C  CB  . PHE   A 367 ? 1.4736 1.0497 1.8916 -0.2141 0.2883  0.1479  387 PHE   A CB  
2699 C  CG  . PHE   A 367 ? 1.4980 1.0661 1.9124 -0.2130 0.2460  0.1174  387 PHE   A CG  
2700 C  CD1 . PHE   A 367 ? 1.4798 1.0669 1.9696 -0.2409 0.2205  0.0844  387 PHE   A CD1 
2701 C  CD2 . PHE   A 367 ? 1.4967 1.0376 1.8324 -0.1820 0.2314  0.1202  387 PHE   A CD2 
2702 C  CE1 . PHE   A 367 ? 1.4528 1.0274 1.9306 -0.2369 0.1826  0.0557  387 PHE   A CE1 
2703 C  CE2 . PHE   A 367 ? 1.4453 0.9770 1.7755 -0.1790 0.1965  0.0924  387 PHE   A CE2 
2704 C  CZ  . PHE   A 367 ? 1.4640 1.0101 1.8610 -0.2061 0.1729  0.0606  387 PHE   A CZ  
2705 N  N   . ILE   A 368 ? 1.4180 1.1424 1.7975 -0.1880 0.1995  0.1006  388 ILE   A N   
2706 C  CA  . ILE   A 368 ? 1.3570 1.1058 1.6831 -0.1656 0.1659  0.0863  388 ILE   A CA  
2707 C  C   . ILE   A 368 ? 1.3965 1.1330 1.7353 -0.1717 0.1340  0.0575  388 ILE   A C   
2708 O  O   . ILE   A 368 ? 1.4022 1.1553 1.8001 -0.1938 0.1175  0.0356  388 ILE   A O   
2709 C  CB  . ILE   A 368 ? 1.3116 1.1228 1.6435 -0.1639 0.1523  0.0788  388 ILE   A CB  
2710 C  CG1 . ILE   A 368 ? 1.3446 1.1625 1.6474 -0.1514 0.1818  0.1058  388 ILE   A CG1 
2711 C  CG2 . ILE   A 368 ? 1.2792 1.1124 1.5678 -0.1462 0.1193  0.0610  388 ILE   A CG2 
2712 C  CD1 . ILE   A 368 ? 1.3215 1.1769 1.6768 -0.1676 0.1952  0.1079  388 ILE   A CD1 
2713 N  N   . PRO   A 369 ? 1.3704 1.0781 1.6559 -0.1509 0.1235  0.0551  389 PRO   A N   
2714 C  CA  . PRO   A 369 ? 1.3443 1.0335 1.6358 -0.1542 0.0962  0.0277  389 PRO   A CA  
2715 C  C   . PRO   A 369 ? 1.3197 1.0537 1.5993 -0.1479 0.0629  0.0030  389 PRO   A C   
2716 O  O   . PRO   A 369 ? 1.2505 1.0230 1.5031 -0.1350 0.0610  0.0089  389 PRO   A O   
2717 C  CB  . PRO   A 369 ? 1.3599 1.0009 1.5948 -0.1298 0.1031  0.0381  389 PRO   A CB  
2718 C  CG  . PRO   A 369 ? 1.3738 1.0067 1.5740 -0.1138 0.1327  0.0717  389 PRO   A CG  
2719 C  CD  . PRO   A 369 ? 1.3556 1.0428 1.5741 -0.1216 0.1365  0.0766  389 PRO   A CD  
2720 N  N   . LYS   A 370 ? 1.3223 1.0461 1.6204 -0.1566 0.0371  -0.0252 390 LYS   A N   
2721 C  CA  . LYS   A 370 ? 1.2684 1.0202 1.5422 -0.1465 0.0068  -0.0487 390 LYS   A CA  
2722 C  C   . LYS   A 370 ? 1.2161 0.9700 1.4254 -0.1183 0.0091  -0.0420 390 LYS   A C   
2723 O  O   . LYS   A 370 ? 1.3155 1.0325 1.4972 -0.1047 0.0166  -0.0374 390 LYS   A O   
2724 C  CB  . LYS   A 370 ? 1.2643 0.9892 1.5532 -0.1543 -0.0200 -0.0800 390 LYS   A CB  
2725 C  CG  . LYS   A 370 ? 1.2687 1.0042 1.5113 -0.1364 -0.0470 -0.1024 390 LYS   A CG  
2726 C  CD  . LYS   A 370 ? 1.2537 0.9547 1.5011 -0.1402 -0.0741 -0.1346 390 LYS   A CD  
2727 C  CE  . LYS   A 370 ? 1.2852 1.0104 1.5134 -0.1331 -0.1057 -0.1592 390 LYS   A CE  
2728 N  NZ  . LYS   A 370 ? 1.3472 1.0336 1.5444 -0.1229 -0.1313 -0.1901 390 LYS   A NZ  
2729 N  N   . GLY   A 371 ? 1.1983 0.9954 1.3879 -0.1095 0.0034  -0.0420 391 GLY   A N   
2730 C  CA  . GLY   A 371 ? 1.1882 0.9960 1.3290 -0.0858 0.0044  -0.0403 391 GLY   A CA  
2731 C  C   . GLY   A 371 ? 1.2063 1.0436 1.3349 -0.0768 0.0209  -0.0190 391 GLY   A C   
2732 O  O   . GLY   A 371 ? 1.1508 1.0105 1.2516 -0.0612 0.0191  -0.0212 391 GLY   A O   
2733 N  N   . VAL   A 372 ? 1.1027 0.9394 1.2520 -0.0858 0.0378  0.0002  392 VAL   A N   
2734 C  CA  . VAL   A 372 ? 1.0760 0.9337 1.2066 -0.0742 0.0524  0.0193  392 VAL   A CA  
2735 C  C   . VAL   A 372 ? 1.0581 0.9625 1.1975 -0.0798 0.0469  0.0155  392 VAL   A C   
2736 O  O   . VAL   A 372 ? 1.0765 0.9942 1.2485 -0.0969 0.0410  0.0089  392 VAL   A O   
2737 C  CB  . VAL   A 372 ? 1.1049 0.9373 1.2446 -0.0786 0.0761  0.0426  392 VAL   A CB  
2738 C  CG1 . VAL   A 372 ? 1.0967 0.9433 1.2038 -0.0605 0.0883  0.0604  392 VAL   A CG1 
2739 C  CG2 . VAL   A 372 ? 1.1660 0.9441 1.2987 -0.0750 0.0826  0.0464  392 VAL   A CG2 
2740 N  N   . VAL   A 373 ? 0.9846 0.9136 1.0977 -0.0646 0.0478  0.0183  393 VAL   A N   
2741 C  CA  . VAL   A 373 ? 0.9985 0.9665 1.1164 -0.0683 0.0459  0.0169  393 VAL   A CA  
2742 C  C   . VAL   A 373 ? 1.0271 1.0014 1.1528 -0.0711 0.0624  0.0352  393 VAL   A C   
2743 O  O   . VAL   A 373 ? 1.0338 1.0032 1.1344 -0.0562 0.0717  0.0470  393 VAL   A O   
2744 C  CB  . VAL   A 373 ? 0.9019 0.8921 0.9951 -0.0533 0.0412  0.0097  393 VAL   A CB  
2745 C  CG1 . VAL   A 373 ? 0.8943 0.9185 0.9923 -0.0575 0.0424  0.0104  393 VAL   A CG1 
2746 C  CG2 . VAL   A 373 ? 0.9453 0.9290 1.0295 -0.0504 0.0302  -0.0076 393 VAL   A CG2 
2747 N  N   . VAL   A 374 ? 0.9518 0.9363 1.1110 -0.0878 0.0658  0.0367  394 VAL   A N   
2748 C  CA  . VAL   A 374 ? 0.9418 0.9349 1.1092 -0.0899 0.0847  0.0532  394 VAL   A CA  
2749 C  C   . VAL   A 374 ? 0.9591 0.9858 1.1117 -0.0826 0.0810  0.0505  394 VAL   A C   
2750 O  O   . VAL   A 374 ? 0.9359 0.9843 1.0994 -0.0883 0.0676  0.0378  394 VAL   A O   
2751 C  CB  . VAL   A 374 ? 0.9556 0.9505 1.1745 -0.1105 0.0916  0.0544  394 VAL   A CB  
2752 C  CG1 . VAL   A 374 ? 0.9274 0.9295 1.1536 -0.1108 0.1170  0.0728  394 VAL   A CG1 
2753 C  CG2 . VAL   A 374 ? 0.8999 0.8589 1.1390 -0.1203 0.0944  0.0538  394 VAL   A CG2 
2754 N  N   . MET   A 375 ? 0.9308 0.9578 1.0552 -0.0686 0.0922  0.0619  395 MET   A N   
2755 C  CA  . MET   A 375 ? 0.8840 0.9384 0.9917 -0.0601 0.0874  0.0569  395 MET   A CA  
2756 C  C   . MET   A 375 ? 0.8599 0.9180 0.9628 -0.0570 0.1049  0.0701  395 MET   A C   
2757 O  O   . MET   A 375 ? 0.8556 0.8897 0.9392 -0.0482 0.1211  0.0857  395 MET   A O   
2758 C  CB  . MET   A 375 ? 0.9028 0.9568 0.9784 -0.0419 0.0781  0.0511  395 MET   A CB  
2759 C  CG  . MET   A 375 ? 0.8896 0.9713 0.9546 -0.0347 0.0719  0.0424  395 MET   A CG  
2760 S  SD  . MET   A 375 ? 0.9096 0.9874 0.9430 -0.0176 0.0817  0.0537  395 MET   A SD  
2761 C  CE  . MET   A 375 ? 1.0341 1.1119 1.0389 0.0066  0.0658  0.0447  395 MET   A CE  
2762 N  N   . ILE   A 376 ? 0.8498 0.9335 0.9655 -0.0621 0.1034  0.0647  396 ILE   A N   
2763 C  CA  . ILE   A 376 ? 0.8799 0.9695 0.9885 -0.0569 0.1196  0.0743  396 ILE   A CA  
2764 C  C   . ILE   A 376 ? 0.9107 1.0116 0.9852 -0.0418 0.1107  0.0661  396 ILE   A C   
2765 O  O   . ILE   A 376 ? 0.8362 0.9566 0.9187 -0.0460 0.0966  0.0518  396 ILE   A O   
2766 C  CB  . ILE   A 376 ? 0.8884 0.9984 1.0375 -0.0708 0.1236  0.0723  396 ILE   A CB  
2767 C  CG1 . ILE   A 376 ? 0.8653 0.9680 1.0585 -0.0865 0.1309  0.0771  396 ILE   A CG1 
2768 C  CG2 . ILE   A 376 ? 0.8409 0.9578 0.9792 -0.0626 0.1411  0.0801  396 ILE   A CG2 
2769 C  CD1 . ILE   A 376 ? 0.8001 0.9061 1.0160 -0.0974 0.1079  0.0622  396 ILE   A CD1 
2770 N  N   . PRO   A 377 ? 0.9683 1.0552 1.0039 -0.0235 0.1180  0.0738  397 PRO   A N   
2771 C  CA  . PRO   A 377 ? 0.9578 1.0567 0.9651 -0.0086 0.1045  0.0614  397 PRO   A CA  
2772 C  C   . PRO   A 377 ? 0.9293 1.0429 0.9366 -0.0089 0.1097  0.0572  397 PRO   A C   
2773 O  O   . PRO   A 377 ? 0.9027 1.0047 0.8801 0.0048  0.1224  0.0654  397 PRO   A O   
2774 C  CB  . PRO   A 377 ? 0.9759 1.0490 0.9364 0.0149  0.1076  0.0711  397 PRO   A CB  
2775 C  CG  . PRO   A 377 ? 0.9533 0.9993 0.9122 0.0118  0.1348  0.0939  397 PRO   A CG  
2776 C  CD  . PRO   A 377 ? 0.9426 0.9974 0.9556 -0.0141 0.1376  0.0935  397 PRO   A CD  
2777 N  N   . SER   A 378 ? 0.9214 1.0563 0.9567 -0.0221 0.1008  0.0447  398 SER   A N   
2778 C  CA  . SER   A 378 ? 0.8964 1.0420 0.9367 -0.0237 0.1071  0.0417  398 SER   A CA  
2779 C  C   . SER   A 378 ? 0.9614 1.1068 0.9674 -0.0073 0.1015  0.0316  398 SER   A C   
2780 O  O   . SER   A 378 ? 1.0062 1.1454 0.9933 0.0021  0.1141  0.0364  398 SER   A O   
2781 C  CB  . SER   A 378 ? 0.8440 1.0052 0.9154 -0.0388 0.0981  0.0316  398 SER   A CB  
2782 O  OG  . SER   A 378 ? 0.7748 0.9364 0.8762 -0.0508 0.1020  0.0393  398 SER   A OG  
2783 N  N   . TYR   A 379 ? 0.9170 1.0702 0.9172 -0.0032 0.0824  0.0157  399 TYR   A N   
2784 C  CA  . TYR   A 379 ? 0.9958 1.1511 0.9692 0.0121  0.0716  0.0009  399 TYR   A CA  
2785 C  C   . TYR   A 379 ? 1.0334 1.1670 0.9581 0.0353  0.0787  0.0117  399 TYR   A C   
2786 O  O   . TYR   A 379 ? 1.0434 1.1707 0.9389 0.0484  0.0808  0.0067  399 TYR   A O   
2787 C  CB  . TYR   A 379 ? 0.9754 1.1457 0.9601 0.0132  0.0496  -0.0187 399 TYR   A CB  
2788 C  CG  . TYR   A 379 ? 0.9915 1.1673 0.9560 0.0292  0.0325  -0.0391 399 TYR   A CG  
2789 C  CD1 . TYR   A 379 ? 1.0736 1.2380 0.9960 0.0550  0.0216  -0.0396 399 TYR   A CD1 
2790 C  CD2 . TYR   A 379 ? 1.0096 1.1988 0.9953 0.0197  0.0258  -0.0590 399 TYR   A CD2 
2791 C  CE1 . TYR   A 379 ? 1.0403 1.2098 0.9427 0.0721  0.0005  -0.0621 399 TYR   A CE1 
2792 C  CE2 . TYR   A 379 ? 1.0413 1.2356 1.0134 0.0333  0.0070  -0.0819 399 TYR   A CE2 
2793 C  CZ  . TYR   A 379 ? 1.0465 1.2327 0.9771 0.0600  -0.0077 -0.0847 399 TYR   A CZ  
2794 O  OH  . TYR   A 379 ? 1.0644 1.2561 0.9800 0.0760  -0.0316 -0.1111 399 TYR   A OH  
2795 N  N   . ALA   A 380 ? 1.0556 1.1726 0.9659 0.0422  0.0839  0.0269  400 ALA   A N   
2796 C  CA  . ALA   A 380 ? 1.1125 1.2005 0.9677 0.0670  0.0937  0.0405  400 ALA   A CA  
2797 C  C   . ALA   A 380 ? 1.1063 1.1796 0.9524 0.0660  0.1248  0.0588  400 ALA   A C   
2798 O  O   . ALA   A 380 ? 1.1883 1.2449 0.9868 0.0867  0.1330  0.0609  400 ALA   A O   
2799 C  CB  . ALA   A 380 ? 1.1635 1.2317 1.0070 0.0739  0.0943  0.0542  400 ALA   A CB  
2800 N  N   . LEU   A 381 ? 1.1074 1.1877 0.9999 0.0434  0.1421  0.0704  401 LEU   A N   
2801 C  CA  . LEU   A 381 ? 1.0438 1.1160 0.9418 0.0409  0.1736  0.0869  401 LEU   A CA  
2802 C  C   . LEU   A 381 ? 1.0814 1.1654 0.9722 0.0463  0.1749  0.0754  401 LEU   A C   
2803 O  O   . LEU   A 381 ? 1.1150 1.1849 0.9813 0.0584  0.1998  0.0862  401 LEU   A O   
2804 C  CB  . LEU   A 381 ? 0.9602 1.0454 0.9214 0.0148  0.1840  0.0949  401 LEU   A CB  
2805 C  CG  . LEU   A 381 ? 0.9340 1.0009 0.9043 0.0084  0.1890  0.1079  401 LEU   A CG  
2806 C  CD1 . LEU   A 381 ? 0.9376 1.0207 0.9743 -0.0178 0.1917  0.1087  401 LEU   A CD1 
2807 C  CD2 . LEU   A 381 ? 1.0693 1.0994 0.9990 0.0243  0.2188  0.1308  401 LEU   A CD2 
2808 N  N   . HIS   A 382 ? 1.0219 1.1284 0.9330 0.0380  0.1509  0.0539  402 HIS   A N   
2809 C  CA  . HIS   A 382 ? 1.0343 1.1471 0.9369 0.0436  0.1501  0.0408  402 HIS   A CA  
2810 C  C   . HIS   A 382 ? 1.1057 1.1986 0.9437 0.0713  0.1459  0.0334  402 HIS   A C   
2811 O  O   . HIS   A 382 ? 1.1739 1.2624 0.9927 0.0812  0.1534  0.0269  402 HIS   A O   
2812 C  CB  . HIS   A 382 ? 0.9958 1.1297 0.9315 0.0285  0.1269  0.0201  402 HIS   A CB  
2813 C  CG  . HIS   A 382 ? 0.9662 1.1155 0.9544 0.0066  0.1305  0.0254  402 HIS   A CG  
2814 N  ND1 . HIS   A 382 ? 0.9560 1.1173 0.9698 -0.0057 0.1175  0.0119  402 HIS   A ND1 
2815 C  CD2 . HIS   A 382 ? 0.9819 1.1341 1.0003 -0.0038 0.1443  0.0415  402 HIS   A CD2 
2816 C  CE1 . HIS   A 382 ? 0.9698 1.1395 1.0198 -0.0195 0.1212  0.0199  402 HIS   A CE1 
2817 N  NE2 . HIS   A 382 ? 0.9387 1.1057 0.9960 -0.0193 0.1354  0.0360  402 HIS   A NE2 
2818 N  N   . ARG   A 383 ? 1.1322 1.2114 0.9334 0.0865  0.1325  0.0330  403 ARG   A N   
2819 C  CA  . ARG   A 383 ? 1.1996 1.2587 0.9338 0.1171  0.1211  0.0230  403 ARG   A CA  
2820 C  C   . ARG   A 383 ? 1.3136 1.3364 0.9904 0.1401  0.1413  0.0474  403 ARG   A C   
2821 O  O   . ARG   A 383 ? 1.4081 1.4118 1.0290 0.1668  0.1239  0.0423  403 ARG   A O   
2822 C  CB  . ARG   A 383 ? 1.1789 1.2538 0.9166 0.1207  0.0813  -0.0040 403 ARG   A CB  
2823 C  CG  . ARG   A 383 ? 1.1537 1.2568 0.9404 0.1004  0.0651  -0.0286 403 ARG   A CG  
2824 C  CD  . ARG   A 383 ? 1.1619 1.2863 0.9746 0.0961  0.0330  -0.0513 403 ARG   A CD  
2825 N  NE  . ARG   A 383 ? 1.1013 1.2475 0.9610 0.0757  0.0226  -0.0736 403 ARG   A NE  
2826 C  CZ  . ARG   A 383 ? 1.1646 1.3161 1.0205 0.0822  0.0015  -0.1023 403 ARG   A CZ  
2827 N  NH1 . ARG   A 383 ? 1.2804 1.4194 1.0848 0.1109  -0.0164 -0.1151 403 ARG   A NH1 
2828 N  NH2 . ARG   A 383 ? 1.1072 1.2735 1.0103 0.0604  -0.0021 -0.1193 403 ARG   A NH2 
2829 N  N   . ASP   A 384 ? 1.4373 1.4489 1.1286 0.1308  0.1788  0.0740  404 ASP   A N   
2830 C  CA  . ASP   A 384 ? 1.5663 1.5375 1.2064 0.1499  0.2069  0.1011  404 ASP   A CA  
2831 C  C   . ASP   A 384 ? 1.6863 1.6312 1.2668 0.1744  0.2334  0.1082  404 ASP   A C   
2832 O  O   . ASP   A 384 ? 1.6347 1.5936 1.2477 0.1627  0.2559  0.1100  404 ASP   A O   
2833 C  CB  . ASP   A 384 ? 1.5324 1.5039 1.2267 0.1249  0.2362  0.1250  404 ASP   A CB  
2834 C  CG  . ASP   A 384 ? 1.6174 1.5428 1.2652 0.1409  0.2633  0.1533  404 ASP   A CG  
2835 O  OD1 . ASP   A 384 ? 1.6817 1.5700 1.2524 0.1717  0.2799  0.1637  404 ASP   A OD1 
2836 O  OD2 . ASP   A 384 ? 1.5666 1.4883 1.2511 0.1238  0.2686  0.1652  404 ASP   A OD2 
2837 N  N   . PRO   A 385 ? 1.9031 1.8088 1.3940 0.2112  0.2312  0.1116  405 PRO   A N   
2838 C  CA  . PRO   A 385 ? 1.9610 1.8354 1.3836 0.2386  0.2589  0.1186  405 PRO   A CA  
2839 C  C   . PRO   A 385 ? 1.9570 1.8097 1.3867 0.2331  0.3185  0.1533  405 PRO   A C   
2840 O  O   . PRO   A 385 ? 2.0298 1.8568 1.4083 0.2544  0.3505  0.1623  405 PRO   A O   
2841 C  CB  . PRO   A 385 ? 1.9802 1.8140 1.3012 0.2813  0.2377  0.1151  405 PRO   A CB  
2842 C  CG  . PRO   A 385 ? 1.9615 1.8251 1.3146 0.2737  0.1848  0.0898  405 PRO   A CG  
2843 C  CD  . PRO   A 385 ? 1.8927 1.7872 1.3400 0.2325  0.1930  0.0999  405 PRO   A CD  
2844 N  N   . LYS   A 386 ? 1.7625 1.6248 1.2576 0.2047  0.3354  0.1716  406 LYS   A N   
2845 C  CA  . LYS   A 386 ? 1.7208 1.5709 1.2452 0.1930  0.3920  0.2009  406 LYS   A CA  
2846 C  C   . LYS   A 386 ? 1.6715 1.5670 1.2772 0.1678  0.4031  0.1913  406 LYS   A C   
2847 O  O   . LYS   A 386 ? 1.7473 1.6351 1.3522 0.1733  0.4465  0.2046  406 LYS   A O   
2848 C  CB  . LYS   A 386 ? 1.7231 1.5626 1.2879 0.1727  0.4047  0.2217  406 LYS   A CB  
2849 C  CG  . LYS   A 386 ? 1.6769 1.5430 1.3430 0.1358  0.4377  0.2337  406 LYS   A CG  
2850 C  CD  . LYS   A 386 ? 1.7294 1.5704 1.3881 0.1420  0.5014  0.2604  406 LYS   A CD  
2851 C  CE  . LYS   A 386 ? 1.6988 1.5802 1.4753 0.1042  0.5256  0.2638  406 LYS   A CE  
2852 N  NZ  . LYS   A 386 ? 1.8363 1.7198 1.6270 0.1090  0.5774  0.2760  406 LYS   A NZ  
2853 N  N   . TYR   A 387 ? 1.5939 1.5350 1.2676 0.1426  0.3659  0.1688  407 TYR   A N   
2854 C  CA  . TYR   A 387 ? 1.4814 1.4640 1.2319 0.1206  0.3712  0.1596  407 TYR   A CA  
2855 C  C   . TYR   A 387 ? 1.4544 1.4503 1.1831 0.1329  0.3492  0.1342  407 TYR   A C   
2856 O  O   . TYR   A 387 ? 1.4354 1.4586 1.2150 0.1218  0.3574  0.1278  407 TYR   A O   
2857 C  CB  . TYR   A 387 ? 1.4475 1.4663 1.2834 0.0867  0.3470  0.1522  407 TYR   A CB  
2858 C  CG  . TYR   A 387 ? 1.5320 1.5402 1.4037 0.0702  0.3682  0.1737  407 TYR   A CG  
2859 C  CD1 . TYR   A 387 ? 1.5286 1.5455 1.4596 0.0552  0.4081  0.1897  407 TYR   A CD1 
2860 C  CD2 . TYR   A 387 ? 1.4999 1.4899 1.3515 0.0694  0.3483  0.1762  407 TYR   A CD2 
2861 C  CE1 . TYR   A 387 ? 1.5512 1.5566 1.5214 0.0376  0.4275  0.2070  407 TYR   A CE1 
2862 C  CE2 . TYR   A 387 ? 1.4538 1.4291 1.3377 0.0541  0.3677  0.1946  407 TYR   A CE2 
2863 C  CZ  . TYR   A 387 ? 1.5319 1.5139 1.4755 0.0371  0.4072  0.2096  407 TYR   A CZ  
2864 O  OH  . TYR   A 387 ? 1.5619 1.5276 1.5438 0.0195  0.4267  0.2257  407 TYR   A OH  
2865 N  N   . TRP   A 388 ? 1.5024 1.4790 1.1595 0.1561  0.3205  0.1182  408 TRP   A N   
2866 C  CA  . TRP   A 388 ? 1.4785 1.4649 1.1179 0.1657  0.2960  0.0905  408 TRP   A CA  
2867 C  C   . TRP   A 388 ? 1.5817 1.5286 1.1189 0.2046  0.2929  0.0840  408 TRP   A C   
2868 O  O   . TRP   A 388 ? 1.6429 1.5638 1.1252 0.2221  0.2817  0.0892  408 TRP   A O   
2869 C  CB  . TRP   A 388 ? 1.3913 1.4062 1.0697 0.1471  0.2485  0.0653  408 TRP   A CB  
2870 C  CG  . TRP   A 388 ? 1.3060 1.3520 1.0682 0.1136  0.2455  0.0714  408 TRP   A CG  
2871 C  CD1 . TRP   A 388 ? 1.2552 1.3040 1.0392 0.1003  0.2364  0.0801  408 TRP   A CD1 
2872 C  CD2 . TRP   A 388 ? 1.2191 1.2946 1.0493 0.0925  0.2494  0.0676  408 TRP   A CD2 
2873 N  NE1 . TRP   A 388 ? 1.2075 1.2853 1.0665 0.0720  0.2338  0.0809  408 TRP   A NE1 
2874 C  CE2 . TRP   A 388 ? 1.1870 1.2818 1.0746 0.0675  0.2406  0.0736  408 TRP   A CE2 
2875 C  CE3 . TRP   A 388 ? 1.1980 1.2833 1.0429 0.0949  0.2582  0.0591  408 TRP   A CE3 
2876 C  CZ2 . TRP   A 388 ? 1.1377 1.2605 1.0926 0.0466  0.2382  0.0709  408 TRP   A CZ2 
2877 C  CZ3 . TRP   A 388 ? 1.1225 1.2364 1.0375 0.0740  0.2566  0.0579  408 TRP   A CZ3 
2878 C  CH2 . TRP   A 388 ? 1.1145 1.2467 1.0819 0.0509  0.2456  0.0636  408 TRP   A CH2 
2879 N  N   . THR   A 389 ? 1.5101 1.4505 1.0190 0.2205  0.3010  0.0715  409 THR   A N   
2880 C  CA  . THR   A 389 ? 1.5785 1.4812 0.9870 0.2595  0.2923  0.0587  409 THR   A CA  
2881 C  C   . THR   A 389 ? 1.5973 1.5144 1.0043 0.2594  0.2367  0.0200  409 THR   A C   
2882 O  O   . THR   A 389 ? 1.5488 1.4969 1.0197 0.2357  0.2218  0.0023  409 THR   A O   
2883 C  CB  . THR   A 389 ? 1.6335 1.5190 1.0104 0.2783  0.3309  0.0628  409 THR   A CB  
2884 O  OG1 . THR   A 389 ? 1.6375 1.5561 1.0790 0.2589  0.3215  0.0434  409 THR   A OG1 
2885 C  CG2 . THR   A 389 ? 1.5747 1.4497 0.9654 0.2759  0.3909  0.1007  409 THR   A CG2 
2886 N  N   . GLU   A 390 ? 1.7007 1.5941 1.0366 0.2865  0.2067  0.0068  410 GLU   A N   
2887 C  CA  . GLU   A 390 ? 1.7095 1.6191 1.0514 0.2861  0.1519  -0.0321 410 GLU   A CA  
2888 C  C   . GLU   A 390 ? 1.6345 1.5899 1.0779 0.2444  0.1325  -0.0394 410 GLU   A C   
2889 O  O   . GLU   A 390 ? 1.6029 1.5800 1.0931 0.2263  0.1172  -0.0624 410 GLU   A O   
2890 C  CB  . GLU   A 390 ? 1.7568 1.6568 1.0687 0.3008  0.1412  -0.0617 410 GLU   A CB  
2891 C  CG  . GLU   A 390 ? 1.8280 1.6788 1.0291 0.3463  0.1578  -0.0589 410 GLU   A CG  
2892 C  CD  . GLU   A 390 ? 1.9461 1.7861 1.1188 0.3606  0.1439  -0.0924 410 GLU   A CD  
2893 O  OE1 . GLU   A 390 ? 1.9496 1.8159 1.1763 0.3403  0.1074  -0.1249 410 GLU   A OE1 
2894 O  OE2 . GLU   A 390 ? 2.0770 1.8795 1.1733 0.3922  0.1719  -0.0862 410 GLU   A OE2 
2895 N  N   . PRO   A 391 ? 1.5933 1.5597 1.0688 0.2296  0.1347  -0.0200 411 PRO   A N   
2896 C  CA  . PRO   A 391 ? 1.5146 1.5201 1.0825 0.1908  0.1257  -0.0218 411 PRO   A CA  
2897 C  C   . PRO   A 391 ? 1.4906 1.5207 1.0923 0.1794  0.0830  -0.0568 411 PRO   A C   
2898 O  O   . PRO   A 391 ? 1.4139 1.4711 1.0855 0.1491  0.0799  -0.0614 411 PRO   A O   
2899 C  CB  . PRO   A 391 ? 1.4822 1.4849 1.0578 0.1860  0.1336  0.0031  411 PRO   A CB  
2900 C  CG  . PRO   A 391 ? 1.5796 1.5470 1.0681 0.2237  0.1255  0.0052  411 PRO   A CG  
2901 C  CD  . PRO   A 391 ? 1.6254 1.5646 1.0479 0.2506  0.1416  0.0018  411 PRO   A CD  
2902 N  N   . GLU   A 392 ? 1.5181 1.5385 1.0734 0.2035  0.0505  -0.0823 412 GLU   A N   
2903 C  CA  . GLU   A 392 ? 1.4960 1.5416 1.0909 0.1924  0.0103  -0.1186 412 GLU   A CA  
2904 C  C   . GLU   A 392 ? 1.4697 1.5151 1.0762 0.1864  0.0053  -0.1443 412 GLU   A C   
2905 O  O   . GLU   A 392 ? 1.4983 1.5572 1.1283 0.1817  -0.0280 -0.1789 412 GLU   A O   
2906 C  CB  . GLU   A 392 ? 1.5543 1.5936 1.1024 0.2218  -0.0273 -0.1387 412 GLU   A CB  
2907 C  CG  . GLU   A 392 ? 1.6023 1.6381 1.1366 0.2308  -0.0257 -0.1153 412 GLU   A CG  
2908 C  CD  . GLU   A 392 ? 1.6419 1.7142 1.2594 0.1985  -0.0327 -0.1147 412 GLU   A CD  
2909 O  OE1 . GLU   A 392 ? 1.5696 1.6716 1.2407 0.1826  -0.0591 -0.1447 412 GLU   A OE1 
2910 O  OE2 . GLU   A 392 ? 1.6047 1.6739 1.2344 0.1890  -0.0101 -0.0848 412 GLU   A OE2 
2911 N  N   . LYS   A 393 ? 1.4454 1.4760 1.0409 0.1863  0.0378  -0.1294 413 LYS   A N   
2912 C  CA  . LYS   A 393 ? 1.4150 1.4366 1.0083 0.1873  0.0353  -0.1527 413 LYS   A CA  
2913 C  C   . LYS   A 393 ? 1.3792 1.4146 1.0363 0.1579  0.0590  -0.1407 413 LYS   A C   
2914 O  O   . LYS   A 393 ? 1.3883 1.4294 1.0642 0.1492  0.0888  -0.1095 413 LYS   A O   
2915 C  CB  . LYS   A 393 ? 1.5120 1.4970 1.0198 0.2236  0.0508  -0.1506 413 LYS   A CB  
2916 C  CG  . LYS   A 393 ? 1.5537 1.5223 1.0314 0.2385  0.0262  -0.1899 413 LYS   A CG  
2917 C  CD  . LYS   A 393 ? 1.5789 1.5669 1.0893 0.2290  -0.0225 -0.2269 413 LYS   A CD  
2918 C  CE  . LYS   A 393 ? 1.5213 1.5201 1.0962 0.2010  -0.0311 -0.2524 413 LYS   A CE  
2919 N  NZ  . LYS   A 393 ? 1.4122 1.4391 1.0484 0.1799  -0.0676 -0.2810 413 LYS   A NZ  
2920 N  N   . PHE   A 394 ? 1.2917 1.3303 0.9822 0.1437  0.0445  -0.1668 414 PHE   A N   
2921 C  CA  . PHE   A 394 ? 1.2379 1.2828 0.9812 0.1201  0.0627  -0.1590 414 PHE   A CA  
2922 C  C   . PHE   A 394 ? 1.2023 1.2249 0.9115 0.1384  0.0877  -0.1539 414 PHE   A C   
2923 O  O   . PHE   A 394 ? 1.2289 1.2319 0.9168 0.1484  0.0790  -0.1792 414 PHE   A O   
2924 C  CB  . PHE   A 394 ? 1.2116 1.2623 1.0013 0.0985  0.0401  -0.1877 414 PHE   A CB  
2925 C  CG  . PHE   A 394 ? 1.1745 1.2248 1.0113 0.0767  0.0577  -0.1786 414 PHE   A CG  
2926 C  CD1 . PHE   A 394 ? 1.0720 1.1409 0.9533 0.0556  0.0682  -0.1556 414 PHE   A CD1 
2927 C  CD2 . PHE   A 394 ? 1.1600 1.1876 0.9920 0.0800  0.0620  -0.1940 414 PHE   A CD2 
2928 C  CE1 . PHE   A 394 ? 1.0675 1.1318 0.9834 0.0403  0.0818  -0.1471 414 PHE   A CE1 
2929 C  CE2 . PHE   A 394 ? 1.1796 1.2020 1.0494 0.0638  0.0772  -0.1845 414 PHE   A CE2 
2930 C  CZ  . PHE   A 394 ? 1.1239 1.1646 1.0338 0.0449  0.0865  -0.1606 414 PHE   A CZ  
2931 N  N   . LEU   A 395 ? 1.1724 1.1983 0.8800 0.1426  0.1200  -0.1221 415 LEU   A N   
2932 C  CA  . LEU   A 395 ? 1.1944 1.2037 0.8733 0.1622  0.1501  -0.1132 415 LEU   A CA  
2933 C  C   . LEU   A 395 ? 1.1659 1.1938 0.9046 0.1450  0.1744  -0.0914 415 LEU   A C   
2934 O  O   . LEU   A 395 ? 1.1145 1.1551 0.8674 0.1443  0.1991  -0.0642 415 LEU   A O   
2935 C  CB  . LEU   A 395 ? 1.1844 1.1779 0.8000 0.1895  0.1700  -0.0963 415 LEU   A CB  
2936 C  CG  . LEU   A 395 ? 1.2832 1.2527 0.8253 0.2151  0.1441  -0.1183 415 LEU   A CG  
2937 C  CD1 . LEU   A 395 ? 1.4322 1.3828 0.9110 0.2408  0.1665  -0.0941 415 LEU   A CD1 
2938 C  CD2 . LEU   A 395 ? 1.2702 1.2143 0.7723 0.2340  0.1344  -0.1490 415 LEU   A CD2 
2939 N  N   . PRO   A 396 ? 1.1614 1.1897 0.9367 0.1321  0.1674  -0.1035 416 PRO   A N   
2940 C  CA  . PRO   A 396 ? 1.1042 1.1501 0.9352 0.1187  0.1841  -0.0846 416 PRO   A CA  
2941 C  C   . PRO   A 396 ? 1.1757 1.2271 1.0067 0.1349  0.2188  -0.0648 416 PRO   A C   
2942 O  O   . PRO   A 396 ? 1.1378 1.2127 1.0197 0.1241  0.2311  -0.0459 416 PRO   A O   
2943 C  CB  . PRO   A 396 ? 1.0783 1.1091 0.9257 0.1122  0.1724  -0.1042 416 PRO   A CB  
2944 C  CG  . PRO   A 396 ? 1.1174 1.1344 0.9437 0.1073  0.1443  -0.1314 416 PRO   A CG  
2945 C  CD  . PRO   A 396 ? 1.1522 1.1629 0.9218 0.1289  0.1425  -0.1356 416 PRO   A CD  
2946 N  N   . GLU   A 397 ? 1.1784 1.2093 0.9554 0.1613  0.2352  -0.0696 417 GLU   A N   
2947 C  CA  . GLU   A 397 ? 1.1664 1.2031 0.9462 0.1770  0.2744  -0.0500 417 GLU   A CA  
2948 C  C   . GLU   A 397 ? 1.1780 1.2360 0.9819 0.1681  0.2933  -0.0219 417 GLU   A C   
2949 O  O   . GLU   A 397 ? 1.1842 1.2558 1.0150 0.1736  0.3275  -0.0038 417 GLU   A O   
2950 C  CB  . GLU   A 397 ? 1.2405 1.2448 0.9449 0.2096  0.2902  -0.0605 417 GLU   A CB  
2951 C  CG  . GLU   A 397 ? 1.2988 1.2785 0.9809 0.2200  0.2744  -0.0901 417 GLU   A CG  
2952 C  CD  . GLU   A 397 ? 1.2910 1.2810 1.0238 0.2190  0.2899  -0.0872 417 GLU   A CD  
2953 O  OE1 . GLU   A 397 ? 1.3027 1.3166 1.0733 0.2211  0.3206  -0.0643 417 GLU   A OE1 
2954 O  OE2 . GLU   A 397 ? 1.3119 1.2855 1.0492 0.2165  0.2713  -0.1084 417 GLU   A OE2 
2955 N  N   . ARG   A 398 ? 1.2133 1.2744 1.0126 0.1544  0.2730  -0.0189 418 ARG   A N   
2956 C  CA  . ARG   A 398 ? 1.1354 1.2156 0.9683 0.1412  0.2876  0.0064  418 ARG   A CA  
2957 C  C   . ARG   A 398 ? 1.1682 1.2807 1.0819 0.1240  0.2974  0.0177  418 ARG   A C   
2958 O  O   . ARG   A 398 ? 1.2053 1.3337 1.1532 0.1204  0.3245  0.0378  418 ARG   A O   
2959 C  CB  . ARG   A 398 ? 1.1337 1.2160 0.9640 0.1255  0.2574  0.0037  418 ARG   A CB  
2960 C  CG  . ARG   A 398 ? 1.1774 1.2332 0.9349 0.1433  0.2436  -0.0062 418 ARG   A CG  
2961 C  CD  . ARG   A 398 ? 1.0864 1.1513 0.8566 0.1271  0.2162  -0.0070 418 ARG   A CD  
2962 N  NE  . ARG   A 398 ? 1.1581 1.2050 0.8723 0.1421  0.1888  -0.0269 418 ARG   A NE  
2963 C  CZ  . ARG   A 398 ? 1.3099 1.3330 0.9589 0.1664  0.1936  -0.0209 418 ARG   A CZ  
2964 N  NH1 . ARG   A 398 ? 1.3699 1.3798 0.9981 0.1774  0.2302  0.0065  418 ARG   A NH1 
2965 N  NH2 . ARG   A 398 ? 1.4069 1.4179 1.0111 0.1811  0.1611  -0.0434 418 ARG   A NH2 
2966 N  N   . PHE   A 399 ? 1.1753 1.2963 1.1209 0.1140  0.2754  0.0043  419 PHE   A N   
2967 C  CA  . PHE   A 399 ? 1.1087 1.2584 1.1256 0.1000  0.2749  0.0121  419 PHE   A CA  
2968 C  C   . PHE   A 399 ? 1.1405 1.2953 1.1789 0.1147  0.2902  0.0083  419 PHE   A C   
2969 O  O   . PHE   A 399 ? 1.1321 1.3068 1.2236 0.1077  0.2815  0.0093  419 PHE   A O   
2970 C  CB  . PHE   A 399 ? 0.9309 1.0830 0.9658 0.0806  0.2405  0.0034  419 PHE   A CB  
2971 C  CG  . PHE   A 399 ? 0.9882 1.1418 1.0158 0.0655  0.2264  0.0081  419 PHE   A CG  
2972 C  CD1 . PHE   A 399 ? 1.0030 1.1371 0.9825 0.0677  0.2111  -0.0040 419 PHE   A CD1 
2973 C  CD2 . PHE   A 399 ? 0.9612 1.1364 1.0330 0.0505  0.2270  0.0224  419 PHE   A CD2 
2974 C  CE1 . PHE   A 399 ? 0.9496 1.0864 0.9247 0.0567  0.1981  -0.0001 419 PHE   A CE1 
2975 C  CE2 . PHE   A 399 ? 0.8842 1.0580 0.9479 0.0385  0.2150  0.0263  419 PHE   A CE2 
2976 C  CZ  . PHE   A 399 ? 0.8902 1.0451 0.9053 0.0423  0.2014  0.0159  419 PHE   A CZ  
2977 N  N   . SER   A 400 ? 1.1941 1.3298 1.1895 0.1376  0.3116  0.0033  420 SER   A N   
2978 C  CA  . SER   A 400 ? 1.2411 1.3829 1.2591 0.1543  0.3308  0.0007  420 SER   A CA  
2979 C  C   . SER   A 400 ? 1.2936 1.4743 1.3828 0.1506  0.3565  0.0193  420 SER   A C   
2980 O  O   . SER   A 400 ? 1.2751 1.4686 1.3800 0.1398  0.3701  0.0348  420 SER   A O   
2981 C  CB  . SER   A 400 ? 1.2272 1.3385 1.1793 0.1817  0.3521  -0.0082 420 SER   A CB  
2982 O  OG  . SER   A 400 ? 1.2982 1.4083 1.2273 0.1913  0.3858  0.0080  420 SER   A OG  
2983 N  N   . LYS   A 401 ? 1.2660 1.4653 1.4027 0.1600  0.3624  0.0162  421 LYS   A N   
2984 C  CA  . LYS   A 401 ? 1.2698 1.5136 1.4909 0.1552  0.3796  0.0287  421 LYS   A CA  
2985 C  C   . LYS   A 401 ? 1.2637 1.5165 1.4911 0.1609  0.4263  0.0444  421 LYS   A C   
2986 O  O   . LYS   A 401 ? 1.2930 1.5815 1.5924 0.1480  0.4407  0.0565  421 LYS   A O   
2987 C  CB  . LYS   A 401 ? 1.3347 1.5948 1.5995 0.1711  0.3778  0.0202  421 LYS   A CB  
2988 C  CG  . LYS   A 401 ? 1.3252 1.6251 1.6727 0.1591  0.3551  0.0221  421 LYS   A CG  
2989 C  CD  . LYS   A 401 ? 1.3459 1.6382 1.6989 0.1732  0.3297  0.0098  421 LYS   A CD  
2990 C  CE  . LYS   A 401 ? 1.3925 1.6815 1.7441 0.2023  0.3563  0.0038  421 LYS   A CE  
2991 N  NZ  . LYS   A 401 ? 1.4346 1.7092 1.7868 0.2181  0.3319  -0.0073 421 LYS   A NZ  
2992 N  N   . LYS   A 402 ? 1.2848 1.5031 1.4373 0.1802  0.4506  0.0440  422 LYS   A N   
2993 C  CA  . LYS   A 402 ? 1.2875 1.5036 1.4303 0.1886  0.4998  0.0616  422 LYS   A CA  
2994 C  C   . LYS   A 402 ? 1.2683 1.4668 1.3752 0.1743  0.4995  0.0751  422 LYS   A C   
2995 O  O   . LYS   A 402 ? 1.2688 1.4648 1.3765 0.1767  0.5416  0.0942  422 LYS   A O   
2996 C  CB  . LYS   A 402 ? 1.3026 1.4836 1.3698 0.2214  0.5277  0.0553  422 LYS   A CB  
2997 C  CG  . LYS   A 402 ? 1.3009 1.4317 1.2610 0.2309  0.5050  0.0437  422 LYS   A CG  
2998 C  CD  . LYS   A 402 ? 1.3553 1.4498 1.2404 0.2651  0.5237  0.0307  422 LYS   A CD  
2999 C  CE  . LYS   A 402 ? 1.4625 1.5594 1.3492 0.2854  0.5858  0.0484  422 LYS   A CE  
3000 N  NZ  . LYS   A 402 ? 1.5282 1.6154 1.3931 0.2796  0.6134  0.0729  422 LYS   A NZ  
3001 N  N   . ASN   A 403 ? 1.3503 1.5348 1.4265 0.1604  0.4558  0.0665  423 ASN   A N   
3002 C  CA  . ASN   A 403 ? 1.3183 1.4837 1.3555 0.1503  0.4513  0.0772  423 ASN   A CA  
3003 C  C   . ASN   A 403 ? 1.3292 1.5178 1.4213 0.1205  0.4208  0.0798  423 ASN   A C   
3004 O  O   . ASN   A 403 ? 1.3975 1.5748 1.4729 0.1108  0.4225  0.0916  423 ASN   A O   
3005 C  CB  . ASN   A 403 ? 1.3047 1.4278 1.2434 0.1653  0.4280  0.0628  423 ASN   A CB  
3006 C  CG  . ASN   A 403 ? 1.3656 1.4554 1.2296 0.1980  0.4593  0.0617  423 ASN   A CG  
3007 O  OD1 . ASN   A 403 ? 1.4184 1.5147 1.3009 0.2096  0.5046  0.0750  423 ASN   A OD1 
3008 N  ND2 . ASN   A 403 ? 1.3686 1.4229 1.1492 0.2139  0.4355  0.0443  423 ASN   A ND2 
3009 N  N   . LYS   A 404 ? 1.2784 1.4950 1.4299 0.1082  0.3933  0.0693  424 LYS   A N   
3010 C  CA  . LYS   A 404 ? 1.3210 1.5560 1.5171 0.0829  0.3634  0.0700  424 LYS   A CA  
3011 C  C   . LYS   A 404 ? 1.3817 1.6437 1.6478 0.0673  0.3850  0.0858  424 LYS   A C   
3012 O  O   . LYS   A 404 ? 1.3005 1.5660 1.5842 0.0478  0.3669  0.0892  424 LYS   A O   
3013 C  CB  . LYS   A 404 ? 1.2957 1.5470 1.5268 0.0788  0.3300  0.0554  424 LYS   A CB  
3014 C  CG  . LYS   A 404 ? 1.2173 1.4886 1.4897 0.0942  0.3450  0.0513  424 LYS   A CG  
3015 C  CD  . LYS   A 404 ? 1.3020 1.5803 1.5969 0.0936  0.3100  0.0385  424 LYS   A CD  
3016 C  CE  . LYS   A 404 ? 1.3231 1.6360 1.6912 0.0774  0.2913  0.0412  424 LYS   A CE  
3017 N  NZ  . LYS   A 404 ? 1.3114 1.6223 1.6856 0.0793  0.2551  0.0306  424 LYS   A NZ  
3018 N  N   . ASP   A 405 ? 1.5280 1.8087 1.8377 0.0751  0.4245  0.0943  425 ASP   A N   
3019 C  CA  . ASP   A 405 ? 1.4850 1.7911 1.8696 0.0584  0.4503  0.1084  425 ASP   A CA  
3020 C  C   . ASP   A 405 ? 1.5155 1.7896 1.8561 0.0522  0.4719  0.1261  425 ASP   A C   
3021 O  O   . ASP   A 405 ? 1.4445 1.7316 1.8425 0.0328  0.4858  0.1370  425 ASP   A O   
3022 C  CB  . ASP   A 405 ? 1.4614 1.7936 1.9019 0.0700  0.4943  0.1133  425 ASP   A CB  
3023 C  CG  . ASP   A 405 ? 1.5094 1.8078 1.8707 0.0981  0.5302  0.1185  425 ASP   A CG  
3024 O  OD1 . ASP   A 405 ? 1.5649 1.8237 1.8541 0.1038  0.5513  0.1318  425 ASP   A OD1 
3025 O  OD2 . ASP   A 405 ? 1.5442 1.8528 1.9113 0.1170  0.5363  0.1086  425 ASP   A OD2 
3026 N  N   . ASN   A 406 ? 1.4495 1.6804 1.6899 0.0698  0.4741  0.1282  426 ASN   A N   
3027 C  CA  . ASN   A 406 ? 1.4563 1.6494 1.6380 0.0708  0.4901  0.1446  426 ASN   A CA  
3028 C  C   . ASN   A 406 ? 1.4319 1.6186 1.6039 0.0534  0.4475  0.1396  426 ASN   A C   
3029 O  O   . ASN   A 406 ? 1.4683 1.6352 1.6284 0.0457  0.4587  0.1545  426 ASN   A O   
3030 C  CB  . ASN   A 406 ? 1.5377 1.6888 1.6142 0.1023  0.5052  0.1449  426 ASN   A CB  
3031 C  CG  . ASN   A 406 ? 1.7694 1.8753 1.7591 0.1112  0.5012  0.1542  426 ASN   A CG  
3032 O  OD1 . ASN   A 406 ? 1.9126 2.0096 1.9159 0.0976  0.5104  0.1702  426 ASN   A OD1 
3033 N  ND2 . ASN   A 406 ? 1.8206 1.8954 1.7191 0.1366  0.4868  0.1428  426 ASN   A ND2 
3034 N  N   . ILE   A 407 ? 1.4185 1.6204 1.5990 0.0470  0.4020  0.1199  427 ILE   A N   
3035 C  CA  . ILE   A 407 ? 1.2665 1.4608 1.4311 0.0337  0.3633  0.1135  427 ILE   A CA  
3036 C  C   . ILE   A 407 ? 1.1722 1.3884 1.4114 0.0085  0.3585  0.1190  427 ILE   A C   
3037 O  O   . ILE   A 407 ? 1.1331 1.3837 1.4462 -0.0021 0.3526  0.1127  427 ILE   A O   
3038 C  CB  . ILE   A 407 ? 1.1869 1.3871 1.3375 0.0351  0.3230  0.0920  427 ILE   A CB  
3039 C  CG1 . ILE   A 407 ? 1.2057 1.3772 1.2757 0.0575  0.3212  0.0832  427 ILE   A CG1 
3040 C  CG2 . ILE   A 407 ? 1.1000 1.3028 1.2595 0.0173  0.2869  0.0856  427 ILE   A CG2 
3041 C  CD1 . ILE   A 407 ? 1.1696 1.3470 1.2394 0.0646  0.3046  0.0649  427 ILE   A CD1 
3042 N  N   . ASP   A 408 ? 1.0641 1.2589 1.2830 0.0007  0.3585  0.1289  428 ASP   A N   
3043 C  CA  . ASP   A 408 ? 0.9829 1.1918 1.2657 -0.0234 0.3503  0.1313  428 ASP   A CA  
3044 C  C   . ASP   A 408 ? 1.0029 1.2267 1.2979 -0.0336 0.3022  0.1128  428 ASP   A C   
3045 O  O   . ASP   A 408 ? 0.9175 1.1238 1.1553 -0.0270 0.2789  0.1055  428 ASP   A O   
3046 C  CB  . ASP   A 408 ? 0.9542 1.1282 1.2038 -0.0258 0.3666  0.1481  428 ASP   A CB  
3047 C  CG  . ASP   A 408 ? 0.9751 1.1587 1.2957 -0.0511 0.3666  0.1517  428 ASP   A CG  
3048 O  OD1 . ASP   A 408 ? 0.9179 1.1194 1.2702 -0.0647 0.3293  0.1363  428 ASP   A OD1 
3049 O  OD2 . ASP   A 408 ? 1.0432 1.2134 1.3865 -0.0569 0.4057  0.1695  428 ASP   A OD2 
3050 N  N   . PRO   A 409 ? 1.0296 1.2843 1.3974 -0.0485 0.2866  0.1041  429 PRO   A N   
3051 C  CA  . PRO   A 409 ? 0.9239 1.1870 1.2933 -0.0543 0.2434  0.0876  429 PRO   A CA  
3052 C  C   . PRO   A 409 ? 0.9107 1.1547 1.2575 -0.0645 0.2242  0.0869  429 PRO   A C   
3053 O  O   . PRO   A 409 ? 0.9235 1.1699 1.2644 -0.0682 0.1921  0.0745  429 PRO   A O   
3054 C  CB  . PRO   A 409 ? 0.8025 1.1018 1.2549 -0.0634 0.2340  0.0793  429 PRO   A CB  
3055 C  CG  . PRO   A 409 ? 0.8573 1.1652 1.3637 -0.0733 0.2682  0.0912  429 PRO   A CG  
3056 C  CD  . PRO   A 409 ? 0.8965 1.1796 1.3497 -0.0595 0.3074  0.1077  429 PRO   A CD  
3057 N  N   . TYR   A 410 ? 0.8871 1.1090 1.2180 -0.0673 0.2449  0.1006  430 TYR   A N   
3058 C  CA  . TYR   A 410 ? 0.9273 1.1285 1.2359 -0.0744 0.2288  0.1005  430 TYR   A CA  
3059 C  C   . TYR   A 410 ? 0.9277 1.0983 1.1594 -0.0588 0.2332  0.1071  430 TYR   A C   
3060 O  O   . TYR   A 410 ? 0.9436 1.0967 1.1521 -0.0607 0.2196  0.1067  430 TYR   A O   
3061 C  CB  . TYR   A 410 ? 0.9012 1.0985 1.2610 -0.0912 0.2439  0.1089  430 TYR   A CB  
3062 C  CG  . TYR   A 410 ? 0.9215 1.1529 1.3630 -0.1062 0.2310  0.0967  430 TYR   A CG  
3063 C  CD1 . TYR   A 410 ? 0.9573 1.1963 1.4151 -0.1149 0.1934  0.0802  430 TYR   A CD1 
3064 C  CD2 . TYR   A 410 ? 0.9370 1.1935 1.4382 -0.1091 0.2552  0.1002  430 TYR   A CD2 
3065 C  CE1 . TYR   A 410 ? 0.9390 1.2081 1.4667 -0.1246 0.1760  0.0664  430 TYR   A CE1 
3066 C  CE2 . TYR   A 410 ? 0.8765 1.1685 1.4577 -0.1205 0.2386  0.0859  430 TYR   A CE2 
3067 C  CZ  . TYR   A 410 ? 0.9007 1.1982 1.4929 -0.1274 0.1967  0.0684  430 TYR   A CZ  
3068 O  OH  . TYR   A 410 ? 0.8365 1.1683 1.5040 -0.1350 0.1753  0.0518  430 TYR   A OH  
3069 N  N   . ILE   A 411 ? 0.9748 1.1385 1.1666 -0.0414 0.2499  0.1115  431 ILE   A N   
3070 C  CA  . ILE   A 411 ? 1.0138 1.1545 1.1322 -0.0235 0.2423  0.1098  431 ILE   A CA  
3071 C  C   . ILE   A 411 ? 0.9839 1.1383 1.0883 -0.0202 0.2130  0.0899  431 ILE   A C   
3072 O  O   . ILE   A 411 ? 0.9827 1.1282 1.0512 -0.0148 0.1927  0.0810  431 ILE   A O   
3073 C  CB  . ILE   A 411 ? 1.0834 1.2026 1.1560 -0.0033 0.2744  0.1233  431 ILE   A CB  
3074 C  CG1 . ILE   A 411 ? 1.1277 1.2311 1.2213 -0.0086 0.3121  0.1458  431 ILE   A CG1 
3075 C  CG2 . ILE   A 411 ? 1.0775 1.1707 1.0722 0.0180  0.2616  0.1198  431 ILE   A CG2 
3076 C  CD1 . ILE   A 411 ? 1.1640 1.2421 1.2465 -0.0142 0.3083  0.1548  431 ILE   A CD1 
3077 N  N   . TYR   A 412 ? 0.9633 1.1388 1.0994 -0.0234 0.2115  0.0825  432 TYR   A N   
3078 C  CA  . TYR   A 412 ? 0.9483 1.1315 1.0737 -0.0209 0.1892  0.0656  432 TYR   A CA  
3079 C  C   . TYR   A 412 ? 0.9194 1.1189 1.0877 -0.0363 0.1687  0.0585  432 TYR   A C   
3080 O  O   . TYR   A 412 ? 0.9091 1.1257 1.1186 -0.0397 0.1707  0.0581  432 TYR   A O   
3081 C  CB  . TYR   A 412 ? 0.9194 1.1063 1.0385 -0.0084 0.2034  0.0630  432 TYR   A CB  
3082 C  CG  . TYR   A 412 ? 0.9246 1.1126 1.0320 -0.0060 0.1835  0.0462  432 TYR   A CG  
3083 C  CD1 . TYR   A 412 ? 0.8598 1.0343 0.9260 -0.0014 0.1678  0.0341  432 TYR   A CD1 
3084 C  CD2 . TYR   A 412 ? 0.8519 1.0534 0.9922 -0.0078 0.1805  0.0417  432 TYR   A CD2 
3085 C  CE1 . TYR   A 412 ? 0.8662 1.0388 0.9275 -0.0020 0.1532  0.0186  432 TYR   A CE1 
3086 C  CE2 . TYR   A 412 ? 0.8172 1.0121 0.9438 -0.0055 0.1657  0.0283  432 TYR   A CE2 
3087 C  CZ  . TYR   A 412 ? 0.7869 0.9665 0.8755 -0.0043 0.1539  0.0171  432 TYR   A CZ  
3088 O  OH  . TYR   A 412 ? 0.7909 0.9612 0.8715 -0.0048 0.1425  0.0035  432 TYR   A OH  
3089 N  N   . THR   A 413 ? 0.9705 1.1640 1.1274 -0.0429 0.1485  0.0521  433 THR   A N   
3090 C  CA  . THR   A 413 ? 0.9746 1.1761 1.1591 -0.0545 0.1292  0.0458  433 THR   A CA  
3091 C  C   . THR   A 413 ? 0.9663 1.1608 1.1243 -0.0543 0.1120  0.0340  433 THR   A C   
3092 O  O   . THR   A 413 ? 0.9280 1.1165 1.0783 -0.0596 0.1012  0.0308  433 THR   A O   
3093 C  CB  . THR   A 413 ? 0.9394 1.1377 1.1429 -0.0647 0.1267  0.0510  433 THR   A CB  
3094 O  OG1 . THR   A 413 ? 0.9034 1.0855 1.0716 -0.0614 0.1252  0.0522  433 THR   A OG1 
3095 C  CG2 . THR   A 413 ? 0.8702 1.0746 1.1099 -0.0684 0.1478  0.0628  433 THR   A CG2 
3096 N  N   . PRO   A 414 ? 0.9436 1.1370 1.0900 -0.0486 0.1114  0.0269  434 PRO   A N   
3097 C  CA  . PRO   A 414 ? 0.9353 1.1202 1.0644 -0.0512 0.0994  0.0160  434 PRO   A CA  
3098 C  C   . PRO   A 414 ? 0.8779 1.0602 1.0185 -0.0578 0.0877  0.0148  434 PRO   A C   
3099 O  O   . PRO   A 414 ? 0.8520 1.0242 0.9782 -0.0613 0.0821  0.0084  434 PRO   A O   
3100 C  CB  . PRO   A 414 ? 0.8543 1.0345 0.9716 -0.0437 0.1048  0.0096  434 PRO   A CB  
3101 C  CG  . PRO   A 414 ? 0.8807 1.0699 1.0176 -0.0375 0.1152  0.0175  434 PRO   A CG  
3102 C  CD  . PRO   A 414 ? 0.8394 1.0373 0.9907 -0.0396 0.1237  0.0283  434 PRO   A CD  
3103 N  N   . PHE   A 415 ? 0.8988 1.0893 1.0651 -0.0583 0.0840  0.0198  435 PHE   A N   
3104 C  CA  . PHE   A 415 ? 0.9027 1.0882 1.0735 -0.0601 0.0688  0.0172  435 PHE   A CA  
3105 C  C   . PHE   A 415 ? 0.8547 1.0472 1.0482 -0.0665 0.0604  0.0187  435 PHE   A C   
3106 O  O   . PHE   A 415 ? 0.8053 0.9970 1.0086 -0.0656 0.0445  0.0149  435 PHE   A O   
3107 C  CB  . PHE   A 415 ? 0.8198 1.0072 1.0011 -0.0514 0.0643  0.0168  435 PHE   A CB  
3108 C  CG  . PHE   A 415 ? 0.9172 1.0897 1.0742 -0.0454 0.0716  0.0144  435 PHE   A CG  
3109 C  CD1 . PHE   A 415 ? 0.8918 1.0407 1.0206 -0.0454 0.0679  0.0116  435 PHE   A CD1 
3110 C  CD2 . PHE   A 415 ? 0.8613 1.0398 1.0228 -0.0396 0.0845  0.0147  435 PHE   A CD2 
3111 C  CE1 . PHE   A 415 ? 0.9457 1.0772 1.0570 -0.0423 0.0767  0.0089  435 PHE   A CE1 
3112 C  CE2 . PHE   A 415 ? 0.8209 0.9824 0.9614 -0.0347 0.0900  0.0100  435 PHE   A CE2 
3113 C  CZ  . PHE   A 415 ? 0.9459 1.0838 1.0642 -0.0373 0.0860  0.0069  435 PHE   A CZ  
3114 N  N   . GLY   A 416 ? 0.8722 1.0680 1.0716 -0.0714 0.0698  0.0234  436 GLY   A N   
3115 C  CA  . GLY   A 416 ? 0.7862 0.9853 1.0123 -0.0788 0.0651  0.0249  436 GLY   A CA  
3116 C  C   . GLY   A 416 ? 0.7899 1.0081 1.0634 -0.0801 0.0672  0.0267  436 GLY   A C   
3117 O  O   . GLY   A 416 ? 0.7498 0.9791 1.0331 -0.0739 0.0785  0.0300  436 GLY   A O   
3118 N  N   . SER   A 417 ? 0.7537 0.9765 1.0609 -0.0881 0.0558  0.0226  437 SER   A N   
3119 C  CA  . SER   A 417 ? 0.7359 0.9822 1.1023 -0.0913 0.0544  0.0204  437 SER   A CA  
3120 C  C   . SER   A 417 ? 0.7895 1.0361 1.1837 -0.0990 0.0300  0.0085  437 SER   A C   
3121 O  O   . SER   A 417 ? 0.8224 1.0481 1.1872 -0.1020 0.0202  0.0048  437 SER   A O   
3122 C  CB  . SER   A 417 ? 0.7651 1.0202 1.1614 -0.0968 0.0850  0.0326  437 SER   A CB  
3123 O  OG  . SER   A 417 ? 0.8473 1.1306 1.3021 -0.0967 0.0901  0.0310  437 SER   A OG  
3124 N  N   . GLY   A 418 ? 0.7785 1.0498 1.2316 -0.1008 0.0190  0.0003  438 GLY   A N   
3125 C  CA  . GLY   A 418 ? 0.8014 1.0759 1.2889 -0.1077 -0.0080 -0.0153 438 GLY   A CA  
3126 C  C   . GLY   A 418 ? 0.8277 1.0889 1.2740 -0.0941 -0.0423 -0.0285 438 GLY   A C   
3127 O  O   . GLY   A 418 ? 0.7733 1.0222 1.1676 -0.0805 -0.0422 -0.0238 438 GLY   A O   
3128 N  N   . PRO   A 419 ? 0.8524 1.1116 1.3188 -0.0971 -0.0713 -0.0456 439 PRO   A N   
3129 C  CA  . PRO   A 419 ? 0.8892 1.1326 1.3120 -0.0800 -0.1060 -0.0593 439 PRO   A CA  
3130 C  C   . PRO   A 419 ? 0.8669 1.0739 1.2030 -0.0708 -0.0991 -0.0513 439 PRO   A C   
3131 O  O   . PRO   A 419 ? 0.9071 1.0961 1.1958 -0.0533 -0.1184 -0.0567 439 PRO   A O   
3132 C  CB  . PRO   A 419 ? 0.8941 1.1371 1.3518 -0.0876 -0.1350 -0.0802 439 PRO   A CB  
3133 C  CG  . PRO   A 419 ? 0.8644 1.1360 1.4092 -0.1085 -0.1181 -0.0793 439 PRO   A CG  
3134 C  CD  . PRO   A 419 ? 0.8496 1.1183 1.3801 -0.1155 -0.0736 -0.0544 439 PRO   A CD  
3135 N  N   . ARG   A 420 ? 0.8154 1.0101 1.1296 -0.0805 -0.0717 -0.0388 440 ARG   A N   
3136 C  CA  . ARG   A 420 ? 0.9141 1.0799 1.1593 -0.0737 -0.0635 -0.0334 440 ARG   A CA  
3137 C  C   . ARG   A 420 ? 0.8838 1.0523 1.1101 -0.0729 -0.0359 -0.0184 440 ARG   A C   
3138 O  O   . ARG   A 420 ? 0.8317 0.9850 1.0221 -0.0740 -0.0214 -0.0131 440 ARG   A O   
3139 C  CB  . ARG   A 420 ? 0.8974 1.0452 1.1302 -0.0823 -0.0608 -0.0364 440 ARG   A CB  
3140 C  CG  . ARG   A 420 ? 0.9877 1.1060 1.1550 -0.0723 -0.0614 -0.0381 440 ARG   A CG  
3141 C  CD  . ARG   A 420 ? 0.9832 1.0808 1.1378 -0.0730 -0.0762 -0.0507 440 ARG   A CD  
3142 N  NE  . ARG   A 420 ? 1.0375 1.1067 1.1276 -0.0595 -0.0767 -0.0533 440 ARG   A NE  
3143 C  CZ  . ARG   A 420 ? 1.0396 1.0843 1.1004 -0.0555 -0.0837 -0.0632 440 ARG   A CZ  
3144 N  NH1 . ARG   A 420 ? 1.0524 1.0949 1.1420 -0.0644 -0.0936 -0.0726 440 ARG   A NH1 
3145 N  NH2 . ARG   A 420 ? 1.0999 1.1188 1.1009 -0.0419 -0.0779 -0.0634 440 ARG   A NH2 
3146 N  N   . ASN   A 421 ? 0.8532 1.0414 1.1053 -0.0698 -0.0299 -0.0136 441 ASN   A N   
3147 C  CA  . ASN   A 421 ? 0.8018 0.9902 1.0351 -0.0674 -0.0070 -0.0027 441 ASN   A CA  
3148 C  C   . ASN   A 421 ? 0.9004 1.0645 1.0802 -0.0565 -0.0096 -0.0028 441 ASN   A C   
3149 O  O   . ASN   A 421 ? 0.9555 1.1001 1.1061 -0.0498 -0.0255 -0.0089 441 ASN   A O   
3150 C  CB  . ASN   A 421 ? 0.7969 1.0103 1.0713 -0.0650 0.0007  0.0010  441 ASN   A CB  
3151 C  CG  . ASN   A 421 ? 0.8079 1.0271 1.0917 -0.0512 -0.0203 -0.0058 441 ASN   A CG  
3152 O  OD1 . ASN   A 421 ? 0.8505 1.0560 1.1147 -0.0438 -0.0445 -0.0145 441 ASN   A OD1 
3153 N  ND2 . ASN   A 421 ? 0.7140 0.9516 1.0245 -0.0449 -0.0116 -0.0024 441 ASN   A ND2 
3154 N  N   . CYS   A 422 ? 0.8379 0.9992 1.0025 -0.0544 0.0079  0.0036  442 CYS   A N   
3155 C  CA  . CYS   A 422 ? 0.8833 1.0188 1.0035 -0.0462 0.0107  0.0048  442 CYS   A CA  
3156 C  C   . CYS   A 422 ? 0.8744 1.0017 0.9875 -0.0307 -0.0067 0.0031  442 CYS   A C   
3157 O  O   . CYS   A 422 ? 0.8866 1.0300 1.0267 -0.0247 -0.0082 0.0043  442 CYS   A O   
3158 C  CB  . CYS   A 422 ? 0.9518 1.0865 1.0655 -0.0489 0.0318  0.0091  442 CYS   A CB  
3159 S  SG  . CYS   A 422 ? 0.8532 0.9521 0.9210 -0.0423 0.0409  0.0109  442 CYS   A SG  
3160 N  N   . ILE   A 423 ? 0.9447 1.0456 1.0186 -0.0212 -0.0200 0.0002  443 ILE   A N   
3161 C  CA  . ILE   A 423 ? 1.0529 1.1404 1.1095 -0.0013 -0.0403 -0.0016 443 ILE   A CA  
3162 C  C   . ILE   A 423 ? 1.1414 1.2060 1.1689 0.0086  -0.0255 0.0075  443 ILE   A C   
3163 O  O   . ILE   A 423 ? 1.2528 1.3093 1.2726 0.0273  -0.0400 0.0079  443 ILE   A O   
3164 C  CB  . ILE   A 423 ? 1.1302 1.1892 1.1414 0.0097  -0.0592 -0.0075 443 ILE   A CB  
3165 C  CG1 . ILE   A 423 ? 1.1475 1.1990 1.1475 0.0337  -0.0906 -0.0134 443 ILE   A CG1 
3166 C  CG2 . ILE   A 423 ? 1.1836 1.2025 1.1341 0.0111  -0.0368 0.0005  443 ILE   A CG2 
3167 C  CD1 . ILE   A 423 ? 1.1778 1.2012 1.1304 0.0482  -0.1150 -0.0226 443 ILE   A CD1 
3168 N  N   . GLY   A 424 ? 1.1128 1.1664 1.1273 -0.0029 0.0019  0.0132  444 GLY   A N   
3169 C  CA  . GLY   A 424 ? 1.1238 1.1524 1.1152 0.0034  0.0180  0.0202  444 GLY   A CA  
3170 C  C   . GLY   A 424 ? 1.1124 1.1642 1.1404 -0.0040 0.0308  0.0199  444 GLY   A C   
3171 O  O   . GLY   A 424 ? 1.1751 1.2078 1.1893 -0.0067 0.0494  0.0224  444 GLY   A O   
3172 N  N   . MET   A 425 ? 0.9784 1.0686 1.0526 -0.0072 0.0226  0.0161  445 MET   A N   
3173 C  CA  . MET   A 425 ? 0.9883 1.0984 1.0909 -0.0114 0.0368  0.0161  445 MET   A CA  
3174 C  C   . MET   A 425 ? 1.0593 1.1553 1.1552 0.0041  0.0389  0.0183  445 MET   A C   
3175 O  O   . MET   A 425 ? 1.0511 1.1362 1.1394 0.0019  0.0558  0.0181  445 MET   A O   
3176 C  CB  . MET   A 425 ? 0.9310 1.0805 1.0825 -0.0163 0.0322  0.0140  445 MET   A CB  
3177 C  CG  . MET   A 425 ? 0.8651 1.0328 1.0414 -0.0153 0.0484  0.0151  445 MET   A CG  
3178 S  SD  . MET   A 425 ? 0.7732 0.9813 1.0053 -0.0223 0.0527  0.0162  445 MET   A SD  
3179 C  CE  . MET   A 425 ? 0.9786 1.2058 1.2515 -0.0117 0.0276  0.0114  445 MET   A CE  
3180 N  N   . ARG   A 426 ? 1.1277 1.2226 1.2261 0.0217  0.0196  0.0187  446 ARG   A N   
3181 C  CA  . ARG   A 426 ? 1.1716 1.2519 1.2634 0.0407  0.0194  0.0210  446 ARG   A CA  
3182 C  C   . ARG   A 426 ? 1.1576 1.1861 1.1956 0.0438  0.0334  0.0269  446 ARG   A C   
3183 O  O   . ARG   A 426 ? 1.1404 1.1532 1.1737 0.0480  0.0475  0.0278  446 ARG   A O   
3184 C  CB  . ARG   A 426 ? 1.2356 1.3255 1.3402 0.0620  -0.0091 0.0186  446 ARG   A CB  
3185 C  CG  . ARG   A 426 ? 1.3120 1.4544 1.4816 0.0568  -0.0223 0.0108  446 ARG   A CG  
3186 C  CD  . ARG   A 426 ? 1.4334 1.5882 1.6225 0.0792  -0.0549 0.0041  446 ARG   A CD  
3187 N  NE  . ARG   A 426 ? 1.5279 1.7297 1.7886 0.0838  -0.0562 -0.0016 446 ARG   A NE  
3188 C  CZ  . ARG   A 426 ? 1.6215 1.8254 1.8929 0.0978  -0.0448 0.0010  446 ARG   A CZ  
3189 N  NH1 . ARG   A 426 ? 1.6613 1.8207 1.8771 0.1073  -0.0322 0.0087  446 ARG   A NH1 
3190 N  NH2 . ARG   A 426 ? 1.6201 1.8705 1.9623 0.1020  -0.0437 -0.0048 446 ARG   A NH2 
3191 N  N   . PHE   A 427 ? 1.2507 1.2495 1.2479 0.0419  0.0322  0.0307  447 PHE   A N   
3192 C  CA  . PHE   A 427 ? 1.2450 1.1915 1.1939 0.0426  0.0514  0.0378  447 PHE   A CA  
3193 C  C   . PHE   A 427 ? 1.2549 1.2026 1.2169 0.0200  0.0769  0.0337  447 PHE   A C   
3194 O  O   . PHE   A 427 ? 1.2277 1.1418 1.1733 0.0195  0.0945  0.0356  447 PHE   A O   
3195 C  CB  . PHE   A 427 ? 1.2646 1.1802 1.1670 0.0461  0.0485  0.0432  447 PHE   A CB  
3196 C  CG  . PHE   A 427 ? 1.2938 1.1573 1.1527 0.0410  0.0767  0.0514  447 PHE   A CG  
3197 C  CD1 . PHE   A 427 ? 1.3488 1.1593 1.1622 0.0605  0.0834  0.0623  447 PHE   A CD1 
3198 C  CD2 . PHE   A 427 ? 1.2592 1.1258 1.1257 0.0174  0.0980  0.0484  447 PHE   A CD2 
3199 C  CE1 . PHE   A 427 ? 1.4440 1.2028 1.2210 0.0537  0.1147  0.0711  447 PHE   A CE1 
3200 C  CE2 . PHE   A 427 ? 1.3437 1.1656 1.1813 0.0102  0.1273  0.0549  447 PHE   A CE2 
3201 C  CZ  . PHE   A 427 ? 1.4510 1.2173 1.2441 0.0271  0.1377  0.0669  447 PHE   A CZ  
3202 N  N   . ALA   A 428 ? 1.1976 1.1816 1.1892 0.0022  0.0778  0.0268  448 ALA   A N   
3203 C  CA  . ALA   A 428 ? 1.1425 1.1311 1.1472 -0.0162 0.0960  0.0197  448 ALA   A CA  
3204 C  C   . ALA   A 428 ? 1.1158 1.1132 1.1394 -0.0127 0.1006  0.0141  448 ALA   A C   
3205 O  O   . ALA   A 428 ? 1.1598 1.1364 1.1785 -0.0192 0.1150  0.0086  448 ALA   A O   
3206 C  CB  . ALA   A 428 ? 1.0927 1.1155 1.1189 -0.0307 0.0928  0.0142  448 ALA   A CB  
3207 N  N   . LEU   A 429 ? 1.1055 1.1331 1.1532 -0.0026 0.0896  0.0143  449 LEU   A N   
3208 C  CA  . LEU   A 429 ? 1.1028 1.1386 1.1654 0.0034  0.0966  0.0091  449 LEU   A CA  
3209 C  C   . LEU   A 429 ? 1.1474 1.1450 1.1897 0.0174  0.1018  0.0110  449 LEU   A C   
3210 O  O   . LEU   A 429 ? 1.1693 1.1574 1.2125 0.0191  0.1122  0.0040  449 LEU   A O   
3211 C  CB  . LEU   A 429 ? 0.9954 1.0713 1.0920 0.0119  0.0887  0.0104  449 LEU   A CB  
3212 C  CG  . LEU   A 429 ? 0.9887 1.0983 1.1065 -0.0010 0.0898  0.0089  449 LEU   A CG  
3213 C  CD1 . LEU   A 429 ? 0.9085 1.0528 1.0650 0.0065  0.0861  0.0121  449 LEU   A CD1 
3214 C  CD2 . LEU   A 429 ? 0.9442 1.0526 1.0534 -0.0083 0.1033  0.0012  449 LEU   A CD2 
3215 N  N   . MET   A 430 ? 1.1810 1.1518 1.1998 0.0297  0.0942  0.0202  450 MET   A N   
3216 C  CA  . MET   A 430 ? 1.2100 1.1374 1.2036 0.0462  0.0995  0.0244  450 MET   A CA  
3217 C  C   . MET   A 430 ? 1.2372 1.1157 1.2009 0.0333  0.1196  0.0251  450 MET   A C   
3218 O  O   . MET   A 430 ? 1.2765 1.1210 1.2302 0.0372  0.1321  0.0228  450 MET   A O   
3219 C  CB  . MET   A 430 ? 1.2741 1.1905 1.2504 0.0701  0.0806  0.0341  450 MET   A CB  
3220 C  CG  . MET   A 430 ? 1.3541 1.2973 1.3602 0.0921  0.0672  0.0319  450 MET   A CG  
3221 S  SD  . MET   A 430 ? 1.4943 1.3824 1.4676 0.1181  0.0734  0.0373  450 MET   A SD  
3222 C  CE  . MET   A 430 ? 1.4650 1.2954 1.3742 0.1284  0.0679  0.0515  450 MET   A CE  
3223 N  N   . ASN   A 431 ? 1.2302 1.1039 1.1831 0.0176  0.1248  0.0274  451 ASN   A N   
3224 C  CA  . ASN   A 431 ? 1.2756 1.1062 1.2097 0.0029  0.1480  0.0278  451 ASN   A CA  
3225 C  C   . ASN   A 431 ? 1.2406 1.0810 1.2042 -0.0158 0.1595  0.0111  451 ASN   A C   
3226 O  O   . ASN   A 431 ? 1.2870 1.0871 1.2439 -0.0213 0.1767  0.0077  451 ASN   A O   
3227 C  CB  . ASN   A 431 ? 1.2717 1.1023 1.1937 -0.0085 0.1524  0.0327  451 ASN   A CB  
3228 C  CG  . ASN   A 431 ? 1.3928 1.1834 1.3047 -0.0257 0.1812  0.0331  451 ASN   A CG  
3229 O  OD1 . ASN   A 431 ? 1.4117 1.2171 1.3373 -0.0435 0.1900  0.0286  451 ASN   A OD1 
3230 N  ND2 . ASN   A 431 ? 1.4444 1.1836 1.3362 -0.0206 0.1977  0.0381  451 ASN   A ND2 
3231 N  N   . MET   A 432 ? 1.1942 1.0842 1.1884 -0.0246 0.1496  -0.0001 452 MET   A N   
3232 C  CA  . MET   A 432 ? 1.1735 1.0732 1.1899 -0.0380 0.1550  -0.0185 452 MET   A CA  
3233 C  C   . MET   A 432 ? 1.1653 1.0488 1.1786 -0.0246 0.1562  -0.0245 452 MET   A C   
3234 O  O   . MET   A 432 ? 1.2077 1.0635 1.2231 -0.0326 0.1667  -0.0369 452 MET   A O   
3235 C  CB  . MET   A 432 ? 1.1693 1.1204 1.2080 -0.0442 0.1430  -0.0268 452 MET   A CB  
3236 C  CG  . MET   A 432 ? 1.0379 1.0067 1.0804 -0.0547 0.1403  -0.0216 452 MET   A CG  
3237 S  SD  . MET   A 432 ? 1.0263 1.0438 1.0923 -0.0629 0.1296  -0.0337 452 MET   A SD  
3238 C  CE  . MET   A 432 ? 1.1175 1.1572 1.1841 -0.0449 0.1210  -0.0301 452 MET   A CE  
3239 N  N   . LYS   A 433 ? 1.2066 1.1077 1.2191 -0.0043 0.1459  -0.0174 453 LYS   A N   
3240 C  CA  . LYS   A 433 ? 1.1700 1.0589 1.1808 0.0115  0.1484  -0.0232 453 LYS   A CA  
3241 C  C   . LYS   A 433 ? 1.2424 1.0723 1.2296 0.0186  0.1593  -0.0187 453 LYS   A C   
3242 O  O   . LYS   A 433 ? 1.2960 1.0997 1.2809 0.0202  0.1675  -0.0305 453 LYS   A O   
3243 C  CB  . LYS   A 433 ? 1.1431 1.0660 1.1659 0.0320  0.1378  -0.0154 453 LYS   A CB  
3244 C  CG  . LYS   A 433 ? 1.0330 1.0063 1.0782 0.0263  0.1333  -0.0200 453 LYS   A CG  
3245 C  CD  . LYS   A 433 ? 1.0133 1.0200 1.0801 0.0440  0.1277  -0.0122 453 LYS   A CD  
3246 C  CE  . LYS   A 433 ? 0.9548 1.0049 1.0419 0.0366  0.1281  -0.0132 453 LYS   A CE  
3247 N  NZ  . LYS   A 433 ? 0.9744 1.0573 1.0916 0.0517  0.1294  -0.0075 453 LYS   A NZ  
3248 N  N   . LEU   A 434 ? 1.2774 1.0808 1.2425 0.0242  0.1601  -0.0019 454 LEU   A N   
3249 C  CA  . LEU   A 434 ? 1.3250 1.0628 1.2601 0.0305  0.1748  0.0054  454 LEU   A CA  
3250 C  C   . LEU   A 434 ? 1.3246 1.0324 1.2672 0.0045  0.1948  -0.0074 454 LEU   A C   
3251 O  O   . LEU   A 434 ? 1.3227 0.9822 1.2559 0.0062  0.2082  -0.0116 454 LEU   A O   
3252 C  CB  . LEU   A 434 ? 1.3728 1.0840 1.2734 0.0416  0.1733  0.0262  454 LEU   A CB  
3253 C  CG  . LEU   A 434 ? 1.3871 1.0936 1.2686 0.0759  0.1558  0.0384  454 LEU   A CG  
3254 C  CD1 . LEU   A 434 ? 1.5647 1.2316 1.3991 0.0892  0.1542  0.0572  454 LEU   A CD1 
3255 C  CD2 . LEU   A 434 ? 1.3802 1.0526 1.2552 0.0936  0.1618  0.0356  454 LEU   A CD2 
3256 N  N   . ALA   A 435 ? 1.3705 1.1071 1.3347 -0.0196 0.1964  -0.0152 455 ALA   A N   
3257 C  CA  . ALA   A 435 ? 1.3177 1.0366 1.3031 -0.0457 0.2124  -0.0318 455 ALA   A CA  
3258 C  C   . ALA   A 435 ? 1.4330 1.1637 1.4393 -0.0479 0.2053  -0.0566 455 ALA   A C   
3259 O  O   . ALA   A 435 ? 1.4227 1.1127 1.4339 -0.0561 0.2176  -0.0692 455 ALA   A O   
3260 C  CB  . ALA   A 435 ? 1.2704 1.0244 1.2785 -0.0671 0.2127  -0.0357 455 ALA   A CB  
3261 N  N   . LEU   A 436 ? 1.2746 1.0567 1.2904 -0.0395 0.1867  -0.0639 456 LEU   A N   
3262 C  CA  . LEU   A 436 ? 1.2310 1.0251 1.2577 -0.0385 0.1792  -0.0881 456 LEU   A CA  
3263 C  C   . LEU   A 436 ? 1.2637 1.0138 1.2736 -0.0225 0.1859  -0.0919 456 LEU   A C   
3264 O  O   . LEU   A 436 ? 1.2962 1.0227 1.3130 -0.0300 0.1886  -0.1146 456 LEU   A O   
3265 C  CB  . LEU   A 436 ? 1.2131 1.0616 1.2416 -0.0266 0.1634  -0.0881 456 LEU   A CB  
3266 C  CG  . LEU   A 436 ? 1.1878 1.0795 1.2308 -0.0393 0.1551  -0.0851 456 LEU   A CG  
3267 C  CD1 . LEU   A 436 ? 1.0765 1.0079 1.1158 -0.0236 0.1460  -0.0726 456 LEU   A CD1 
3268 C  CD2 . LEU   A 436 ? 1.1704 1.0780 1.2311 -0.0545 0.1478  -0.1102 456 LEU   A CD2 
3269 N  N   . ILE   A 437 ? 1.3502 1.0885 1.3397 0.0009  0.1868  -0.0719 457 ILE   A N   
3270 C  CA  . ILE   A 437 ? 1.3412 1.0381 1.3140 0.0207  0.1929  -0.0741 457 ILE   A CA  
3271 C  C   . ILE   A 437 ? 1.3748 1.0060 1.3418 0.0069  0.2101  -0.0799 457 ILE   A C   
3272 O  O   . ILE   A 437 ? 1.4518 1.0513 1.4180 0.0087  0.2144  -0.0984 457 ILE   A O   
3273 C  CB  . ILE   A 437 ? 1.2945 0.9920 1.2511 0.0493  0.1886  -0.0508 457 ILE   A CB  
3274 C  CG1 . ILE   A 437 ? 1.2287 0.9921 1.2020 0.0600  0.1745  -0.0472 457 ILE   A CG1 
3275 C  CG2 . ILE   A 437 ? 1.3936 1.0471 1.3337 0.0724  0.1949  -0.0529 457 ILE   A CG2 
3276 C  CD1 . ILE   A 437 ? 1.2608 1.0360 1.2314 0.0832  0.1657  -0.0268 457 ILE   A CD1 
3277 N  N   . ARG   A 438 ? 1.3977 1.0044 1.3603 -0.0072 0.2224  -0.0648 458 ARG   A N   
3278 C  CA  . ARG   A 438 ? 1.4528 0.9906 1.4101 -0.0206 0.2453  -0.0659 458 ARG   A CA  
3279 C  C   . ARG   A 438 ? 1.4117 0.9524 1.4082 -0.0523 0.2497  -0.0959 458 ARG   A C   
3280 O  O   . ARG   A 438 ? 1.4304 0.9201 1.4331 -0.0609 0.2627  -0.1101 458 ARG   A O   
3281 C  CB  . ARG   A 438 ? 1.4592 0.9668 1.3943 -0.0235 0.2614  -0.0385 458 ARG   A CB  
3282 C  CG  . ARG   A 438 ? 1.5656 1.0149 1.4528 0.0062  0.2688  -0.0141 458 ARG   A CG  
3283 C  CD  . ARG   A 438 ? 1.6837 1.0567 1.5631 0.0020  0.2914  -0.0203 458 ARG   A CD  
3284 N  NE  . ARG   A 438 ? 1.7150 1.0260 1.5444 0.0344  0.2979  0.0029  458 ARG   A NE  
3285 C  CZ  . ARG   A 438 ? 1.7156 1.0057 1.5332 0.0598  0.2907  -0.0021 458 ARG   A CZ  
3286 N  NH1 . ARG   A 438 ? 1.7157 1.0397 1.5635 0.0574  0.2785  -0.0290 458 ARG   A NH1 
3287 N  NH2 . ARG   A 438 ? 1.7385 0.9694 1.5091 0.0912  0.2961  0.0201  458 ARG   A NH2 
3288 N  N   . VAL   A 439 ? 1.4794 1.0784 1.5050 -0.0688 0.2372  -0.1075 459 VAL   A N   
3289 C  CA  . VAL   A 439 ? 1.3994 1.0065 1.4678 -0.0974 0.2369  -0.1384 459 VAL   A CA  
3290 C  C   . VAL   A 439 ? 1.4663 1.0799 1.5387 -0.0897 0.2193  -0.1691 459 VAL   A C   
3291 O  O   . VAL   A 439 ? 1.5478 1.1391 1.6477 -0.1077 0.2209  -0.1977 459 VAL   A O   
3292 C  CB  . VAL   A 439 ? 1.3516 1.0177 1.4484 -0.1139 0.2278  -0.1412 459 VAL   A CB  
3293 C  CG1 . VAL   A 439 ? 1.3236 1.0478 1.4064 -0.0947 0.2031  -0.1382 459 VAL   A CG1 
3294 C  CG2 . VAL   A 439 ? 1.2841 0.9625 1.4320 -0.1414 0.2243  -0.1754 459 VAL   A CG2 
3295 N  N   . LEU   A 440 ? 1.3984 1.0404 1.4446 -0.0626 0.2035  -0.1652 460 LEU   A N   
3296 C  CA  . LEU   A 440 ? 1.3717 1.0176 1.4119 -0.0510 0.1890  -0.1932 460 LEU   A CA  
3297 C  C   . LEU   A 440 ? 1.4295 1.0198 1.4447 -0.0320 0.1988  -0.1941 460 LEU   A C   
3298 O  O   . LEU   A 440 ? 1.4585 1.0381 1.4671 -0.0239 0.1901  -0.2212 460 LEU   A O   
3299 C  CB  . LEU   A 440 ? 1.3113 1.0154 1.3366 -0.0319 0.1716  -0.1900 460 LEU   A CB  
3300 C  CG  . LEU   A 440 ? 1.2907 1.0445 1.3385 -0.0483 0.1561  -0.2027 460 LEU   A CG  
3301 C  CD1 . LEU   A 440 ? 1.2476 1.0404 1.2738 -0.0280 0.1396  -0.2107 460 LEU   A CD1 
3302 C  CD2 . LEU   A 440 ? 1.3303 1.0688 1.4127 -0.0742 0.1519  -0.2348 460 LEU   A CD2 
3303 N  N   . GLN   A 441 ? 1.4410 0.9929 1.4383 -0.0220 0.2156  -0.1662 461 GLN   A N   
3304 C  CA  . GLN   A 441 ? 1.4639 0.9524 1.4400 -0.0060 0.2270  -0.1680 461 GLN   A CA  
3305 C  C   . GLN   A 441 ? 1.5724 1.0054 1.5692 -0.0316 0.2387  -0.1919 461 GLN   A C   
3306 O  O   . GLN   A 441 ? 1.6214 1.0048 1.6055 -0.0211 0.2432  -0.2063 461 GLN   A O   
3307 C  CB  . GLN   A 441 ? 1.5112 0.9682 1.4600 0.0131  0.2401  -0.1318 461 GLN   A CB  
3308 C  CG  . GLN   A 441 ? 1.5038 0.9912 1.4321 0.0493  0.2292  -0.1171 461 GLN   A CG  
3309 C  CD  . GLN   A 441 ? 1.5867 1.0463 1.4899 0.0705  0.2357  -0.0845 461 GLN   A CD  
3310 O  OE1 . GLN   A 441 ? 1.5907 1.0391 1.4885 0.0585  0.2426  -0.0657 461 GLN   A OE1 
3311 N  NE2 . GLN   A 441 ? 1.6281 1.0754 1.5139 0.1047  0.2329  -0.0785 461 GLN   A NE2 
3312 N  N   . ASN   A 442 ? 1.5821 1.0228 1.6148 -0.0652 0.2446  -0.1981 462 ASN   A N   
3313 C  CA  . ASN   A 442 ? 1.6187 1.0071 1.6832 -0.0941 0.2604  -0.2188 462 ASN   A CA  
3314 C  C   . ASN   A 442 ? 1.5907 1.0154 1.7052 -0.1211 0.2429  -0.2598 462 ASN   A C   
3315 O  O   . ASN   A 442 ? 1.6814 1.0655 1.8274 -0.1419 0.2490  -0.2879 462 ASN   A O   
3316 C  CB  . ASN   A 442 ? 1.6334 0.9851 1.7040 -0.1123 0.2913  -0.1903 462 ASN   A CB  
3317 C  CG  . ASN   A 442 ? 1.7057 0.9931 1.7252 -0.0869 0.3111  -0.1565 462 ASN   A CG  
3318 O  OD1 . ASN   A 442 ? 1.7530 0.9684 1.7638 -0.0861 0.3279  -0.1611 462 ASN   A OD1 
3319 N  ND2 . ASN   A 442 ? 1.7157 1.0269 1.7011 -0.0647 0.3075  -0.1236 462 ASN   A ND2 
3320 N  N   . PHE   A 443 ? 1.5340 1.0315 1.6584 -0.1206 0.2203  -0.2653 463 PHE   A N   
3321 C  CA  . PHE   A 443 ? 1.5078 1.0432 1.6799 -0.1434 0.2003  -0.3033 463 PHE   A CA  
3322 C  C   . PHE   A 443 ? 1.4892 1.0794 1.6376 -0.1206 0.1675  -0.3187 463 PHE   A C   
3323 O  O   . PHE   A 443 ? 1.4392 1.0491 1.5442 -0.0930 0.1648  -0.2946 463 PHE   A O   
3324 C  CB  . PHE   A 443 ? 1.5501 1.1183 1.7672 -0.1712 0.2099  -0.2941 463 PHE   A CB  
3325 C  CG  . PHE   A 443 ? 1.6515 1.1650 1.8893 -0.1940 0.2481  -0.2760 463 PHE   A CG  
3326 C  CD1 . PHE   A 443 ? 1.6615 1.1428 1.8552 -0.1796 0.2723  -0.2323 463 PHE   A CD1 
3327 C  CD2 . PHE   A 443 ? 1.7026 1.1965 2.0044 -0.2290 0.2602  -0.3031 463 PHE   A CD2 
3328 C  CE1 . PHE   A 443 ? 1.7777 1.2014 1.9791 -0.1969 0.3100  -0.2132 463 PHE   A CE1 
3329 C  CE2 . PHE   A 443 ? 1.7785 1.2177 2.0978 -0.2503 0.3017  -0.2840 463 PHE   A CE2 
3330 C  CZ  . PHE   A 443 ? 1.8516 1.2526 2.1150 -0.2330 0.3277  -0.2374 463 PHE   A CZ  
3331 N  N   . SER   A 444 ? 1.5162 1.1296 1.6948 -0.1320 0.1427  -0.3600 464 SER   A N   
3332 C  CA  . SER   A 444 ? 1.4459 1.1125 1.6035 -0.1132 0.1111  -0.3757 464 SER   A CA  
3333 C  C   . SER   A 444 ? 1.4163 1.1278 1.6285 -0.1368 0.0921  -0.4007 464 SER   A C   
3334 O  O   . SER   A 444 ? 1.4786 1.1746 1.7491 -0.1663 0.0955  -0.4250 464 SER   A O   
3335 C  CB  . SER   A 444 ? 1.4755 1.1194 1.5963 -0.0901 0.0923  -0.4074 464 SER   A CB  
3336 O  OG  . SER   A 444 ? 1.5234 1.1773 1.6760 -0.1027 0.0637  -0.4560 464 SER   A OG  
3337 N  N   . PHE   A 445 ? 1.4360 1.2028 1.6326 -0.1234 0.0731  -0.3945 465 PHE   A N   
3338 C  CA  . PHE   A 445 ? 1.4086 1.2244 1.6545 -0.1414 0.0569  -0.4093 465 PHE   A CA  
3339 C  C   . PHE   A 445 ? 1.4620 1.3082 1.6930 -0.1237 0.0158  -0.4464 465 PHE   A C   
3340 O  O   . PHE   A 445 ? 1.4702 1.3250 1.6378 -0.0921 0.0051  -0.4372 465 PHE   A O   
3341 C  CB  . PHE   A 445 ? 1.3746 1.2265 1.6145 -0.1401 0.0696  -0.3690 465 PHE   A CB  
3342 C  CG  . PHE   A 445 ? 1.3585 1.1814 1.6099 -0.1559 0.1068  -0.3344 465 PHE   A CG  
3343 C  CD1 . PHE   A 445 ? 1.3808 1.1604 1.5890 -0.1414 0.1268  -0.3086 465 PHE   A CD1 
3344 C  CD2 . PHE   A 445 ? 1.2955 1.1333 1.5973 -0.1820 0.1217  -0.3277 465 PHE   A CD2 
3345 C  CE1 . PHE   A 445 ? 1.4101 1.1587 1.6196 -0.1510 0.1579  -0.2771 465 PHE   A CE1 
3346 C  CE2 . PHE   A 445 ? 1.3327 1.1376 1.6334 -0.1926 0.1570  -0.2950 465 PHE   A CE2 
3347 C  CZ  . PHE   A 445 ? 1.3582 1.1169 1.6096 -0.1762 0.1735  -0.2697 465 PHE   A CZ  
3348 N  N   . LYS   A 446 ? 1.5002 1.3621 1.7900 -0.1429 -0.0066 -0.4884 466 LYS   A N   
3349 C  CA  . LYS   A 446 ? 1.5594 1.4489 1.8409 -0.1265 -0.0512 -0.5300 466 LYS   A CA  
3350 C  C   . LYS   A 446 ? 1.5461 1.4924 1.8887 -0.1413 -0.0699 -0.5433 466 LYS   A C   
3351 O  O   . LYS   A 446 ? 1.5362 1.4906 1.9519 -0.1743 -0.0499 -0.5402 466 LYS   A O   
3352 C  CB  . LYS   A 446 ? 1.5409 1.3945 1.8413 -0.1326 -0.0700 -0.5801 466 LYS   A CB  
3353 C  CG  . LYS   A 446 ? 1.6160 1.4075 1.8664 -0.1210 -0.0482 -0.5696 466 LYS   A CG  
3354 C  CD  . LYS   A 446 ? 1.7388 1.4853 2.0395 -0.1455 -0.0483 -0.6088 466 LYS   A CD  
3355 C  CE  . LYS   A 446 ? 1.7834 1.5494 2.1141 -0.1456 -0.0972 -0.6711 466 LYS   A CE  
3356 N  NZ  . LYS   A 446 ? 1.8276 1.5457 2.2065 -0.1686 -0.0996 -0.7138 466 LYS   A NZ  
3357 N  N   . PRO   A 447 ? 1.5673 1.5515 1.8796 -0.1158 -0.1055 -0.5565 467 PRO   A N   
3358 C  CA  . PRO   A 447 ? 1.5753 1.6154 1.9453 -0.1257 -0.1253 -0.5692 467 PRO   A CA  
3359 C  C   . PRO   A 447 ? 1.6493 1.7023 2.1123 -0.1527 -0.1471 -0.6224 467 PRO   A C   
3360 O  O   . PRO   A 447 ? 1.6517 1.6717 2.1239 -0.1579 -0.1585 -0.6574 467 PRO   A O   
3361 C  CB  . PRO   A 447 ? 1.5348 1.5987 1.8344 -0.0849 -0.1611 -0.5734 467 PRO   A CB  
3362 C  CG  . PRO   A 447 ? 1.4694 1.4946 1.6752 -0.0581 -0.1428 -0.5429 467 PRO   A CG  
3363 C  CD  . PRO   A 447 ? 1.5145 1.4904 1.7317 -0.0737 -0.1232 -0.5523 467 PRO   A CD  
3364 N  N   . CYS   A 448 ? 1.5953 1.6978 2.1328 -0.1705 -0.1520 -0.6292 468 CYS   A N   
3365 C  CA  . CYS   A 448 ? 1.6895 1.8196 2.3316 -0.1965 -0.1745 -0.6810 468 CYS   A CA  
3366 C  C   . CYS   A 448 ? 1.7440 1.9302 2.3933 -0.1721 -0.2293 -0.7145 468 CYS   A C   
3367 O  O   . CYS   A 448 ? 1.6978 1.8995 2.2738 -0.1385 -0.2422 -0.6908 468 CYS   A O   
3368 C  CB  . CYS   A 448 ? 1.6221 1.7656 2.3582 -0.2383 -0.1321 -0.6650 468 CYS   A CB  
3369 S  SG  . CYS   A 448 ? 1.6467 1.7186 2.4000 -0.2726 -0.0740 -0.6437 468 CYS   A SG  
3370 N  N   . LYS   A 449 ? 1.9898 2.2039 2.7233 -0.1852 -0.2586 -0.7619 469 LYS   A N   
3371 C  CA  . LYS   A 449 ? 1.9638 2.2299 2.7001 -0.1554 -0.3082 -0.7835 469 LYS   A CA  
3372 C  C   . LYS   A 449 ? 1.9194 2.2378 2.6943 -0.1588 -0.2984 -0.7612 469 LYS   A C   
3373 O  O   . LYS   A 449 ? 1.9773 2.3276 2.7134 -0.1249 -0.3338 -0.7642 469 LYS   A O   
3374 C  CB  . LYS   A 449 ? 1.9174 2.1992 2.7270 -0.1620 -0.3340 -0.8233 469 LYS   A CB  
3375 C  CG  . LYS   A 449 ? 1.8890 2.2109 2.8234 -0.1960 -0.3107 -0.8251 469 LYS   A CG  
3376 C  CD  . LYS   A 449 ? 1.9745 2.3611 2.9457 -0.1735 -0.3485 -0.8419 469 LYS   A CD  
3377 C  CE  . LYS   A 449 ? 1.9137 2.3372 3.0126 -0.2020 -0.3345 -0.8588 469 LYS   A CE  
3378 N  NZ  . LYS   A 449 ? 2.0153 2.5014 3.1526 -0.1800 -0.3656 -0.8719 469 LYS   A NZ  
3379 N  N   . GLU   A 450 ? 1.7509 2.0735 2.5941 -0.1962 -0.2489 -0.7367 470 GLU   A N   
3380 C  CA  . GLU   A 450 ? 1.6576 2.0236 2.5304 -0.1996 -0.2333 -0.7118 470 GLU   A CA  
3381 C  C   . GLU   A 450 ? 1.6096 1.9520 2.3875 -0.1839 -0.2071 -0.6585 470 GLU   A C   
3382 O  O   . GLU   A 450 ? 1.4948 1.8640 2.2826 -0.1843 -0.1883 -0.6288 470 GLU   A O   
3383 C  CB  . GLU   A 450 ? 1.5636 1.9390 2.5365 -0.2393 -0.1852 -0.6992 470 GLU   A CB  
3384 C  CG  . GLU   A 450 ? 1.5426 1.8639 2.5090 -0.2708 -0.1279 -0.6685 470 GLU   A CG  
3385 C  CD  . GLU   A 450 ? 1.6529 1.9242 2.6228 -0.2841 -0.1235 -0.6872 470 GLU   A CD  
3386 O  OE1 . GLU   A 450 ? 1.7109 1.9915 2.6903 -0.2702 -0.1656 -0.7256 470 GLU   A OE1 
3387 O  OE2 . GLU   A 450 ? 1.6572 1.8769 2.6176 -0.3068 -0.0778 -0.6628 470 GLU   A OE2 
3388 N  N   . THR   A 451 ? 1.6091 1.8998 2.2915 -0.1665 -0.2015 -0.6396 471 THR   A N   
3389 C  CA  . THR   A 451 ? 1.5491 1.8185 2.1355 -0.1447 -0.1786 -0.5851 471 THR   A CA  
3390 C  C   . THR   A 451 ? 1.5026 1.7997 2.0300 -0.1042 -0.2165 -0.5848 471 THR   A C   
3391 O  O   . THR   A 451 ? 1.5055 1.8109 2.0132 -0.0800 -0.2632 -0.6228 471 THR   A O   
3392 C  CB  . THR   A 451 ? 1.5735 1.7831 2.0847 -0.1374 -0.1607 -0.5679 471 THR   A CB  
3393 O  OG1 . THR   A 451 ? 1.4612 1.6390 2.0100 -0.1710 -0.1148 -0.5494 471 THR   A OG1 
3394 C  CG2 . THR   A 451 ? 1.4969 1.6919 1.9059 -0.1058 -0.1517 -0.5235 471 THR   A CG2 
3395 N  N   . GLN   A 452 ? 1.4352 1.7426 1.9317 -0.0958 -0.1964 -0.5420 472 GLN   A N   
3396 C  CA  . GLN   A 452 ? 1.4346 1.7644 1.8782 -0.0596 -0.2246 -0.5347 472 GLN   A CA  
3397 C  C   . GLN   A 452 ? 1.4533 1.7419 1.7818 -0.0278 -0.2232 -0.5093 472 GLN   A C   
3398 O  O   . GLN   A 452 ? 1.4311 1.6930 1.7196 -0.0322 -0.1853 -0.4663 472 GLN   A O   
3399 C  CB  . GLN   A 452 ? 1.3327 1.6894 1.8028 -0.0679 -0.2009 -0.5022 472 GLN   A CB  
3400 C  CG  . GLN   A 452 ? 1.3229 1.6850 1.7216 -0.0332 -0.2128 -0.4764 472 GLN   A CG  
3401 C  CD  . GLN   A 452 ? 1.3240 1.7099 1.7564 -0.0445 -0.1887 -0.4485 472 GLN   A CD  
3402 O  OE1 . GLN   A 452 ? 1.2826 1.6475 1.6669 -0.0423 -0.1599 -0.4057 472 GLN   A OE1 
3403 N  NE2 . GLN   A 452 ? 1.3254 1.7564 1.8448 -0.0565 -0.2006 -0.4748 472 GLN   A NE2 
3404 N  N   . ILE   A 453 ? 1.5044 1.7875 1.7807 0.0052  -0.2642 -0.5374 473 ILE   A N   
3405 C  CA  . ILE   A 453 ? 1.5071 1.7516 1.6718 0.0396  -0.2627 -0.5163 473 ILE   A CA  
3406 C  C   . ILE   A 453 ? 1.5241 1.7828 1.6342 0.0811  -0.3014 -0.5244 473 ILE   A C   
3407 O  O   . ILE   A 453 ? 1.5560 1.8308 1.6780 0.0971  -0.3485 -0.5705 473 ILE   A O   
3408 C  CB  . ILE   A 453 ? 1.5206 1.7268 1.6527 0.0445  -0.2699 -0.5417 473 ILE   A CB  
3409 C  CG1 . ILE   A 453 ? 1.4887 1.6800 1.6854 0.0032  -0.2371 -0.5410 473 ILE   A CG1 
3410 C  CG2 . ILE   A 453 ? 1.5454 1.7106 1.5655 0.0774  -0.2552 -0.5122 473 ILE   A CG2 
3411 C  CD1 . ILE   A 453 ? 1.5351 1.6889 1.7137 0.0049  -0.2464 -0.5722 473 ILE   A CD1 
3412 N  N   . PRO   A 454 ? 1.5635 1.8141 1.6117 0.1013  -0.2846 -0.4822 474 PRO   A N   
3413 C  CA  . PRO   A 454 ? 1.5509 1.7828 1.5787 0.0877  -0.2345 -0.4299 474 PRO   A CA  
3414 C  C   . PRO   A 454 ? 1.5249 1.7883 1.6340 0.0547  -0.2136 -0.4143 474 PRO   A C   
3415 O  O   . PRO   A 454 ? 1.4985 1.7997 1.6649 0.0510  -0.2366 -0.4363 474 PRO   A O   
3416 C  CB  . PRO   A 454 ? 1.5876 1.8005 1.5206 0.1268  -0.2352 -0.4020 474 PRO   A CB  
3417 C  CG  . PRO   A 454 ? 1.6096 1.8502 1.5480 0.1505  -0.2809 -0.4294 474 PRO   A CG  
3418 C  CD  . PRO   A 454 ? 1.5972 1.8564 1.5916 0.1419  -0.3181 -0.4854 474 PRO   A CD  
3419 N  N   . LEU   A 455 ? 1.4271 1.6762 1.5436 0.0321  -0.1709 -0.3785 475 LEU   A N   
3420 C  CA  . LEU   A 455 ? 1.3394 1.6119 1.5176 0.0056  -0.1493 -0.3608 475 LEU   A CA  
3421 C  C   . LEU   A 455 ? 1.3027 1.5917 1.4574 0.0253  -0.1563 -0.3414 475 LEU   A C   
3422 O  O   . LEU   A 455 ? 1.3452 1.6120 1.4318 0.0449  -0.1453 -0.3112 475 LEU   A O   
3423 C  CB  . LEU   A 455 ? 1.2890 1.5367 1.4657 -0.0164 -0.1062 -0.3268 475 LEU   A CB  
3424 C  CG  . LEU   A 455 ? 1.1986 1.4604 1.4197 -0.0395 -0.0800 -0.3030 475 LEU   A CG  
3425 C  CD1 . LEU   A 455 ? 1.1573 1.3987 1.4090 -0.0680 -0.0494 -0.2951 475 LEU   A CD1 
3426 C  CD2 . LEU   A 455 ? 1.1742 1.4294 1.3472 -0.0259 -0.0661 -0.2643 475 LEU   A CD2 
3427 N  N   . LYS   A 456 ? 1.3844 1.7113 1.5979 0.0207  -0.1734 -0.3594 476 LYS   A N   
3428 C  CA  . LYS   A 456 ? 1.3705 1.7129 1.5718 0.0366  -0.1775 -0.3413 476 LYS   A CA  
3429 C  C   . LYS   A 456 ? 1.3297 1.6788 1.5726 0.0092  -0.1415 -0.3144 476 LYS   A C   
3430 O  O   . LYS   A 456 ? 1.3527 1.7195 1.6673 -0.0191 -0.1295 -0.3275 476 LYS   A O   
3431 C  CB  . LYS   A 456 ? 1.3799 1.7610 1.6186 0.0534  -0.2195 -0.3774 476 LYS   A CB  
3432 C  CG  . LYS   A 456 ? 1.3325 1.7464 1.6644 0.0295  -0.2333 -0.4203 476 LYS   A CG  
3433 C  CD  . LYS   A 456 ? 1.3513 1.8027 1.7119 0.0534  -0.2847 -0.4629 476 LYS   A CD  
3434 C  CE  . LYS   A 456 ? 1.3066 1.7827 1.7509 0.0315  -0.3031 -0.5116 476 LYS   A CE  
3435 N  NZ  . LYS   A 456 ? 1.2663 1.7992 1.7918 0.0382  -0.3411 -0.5523 476 LYS   A NZ  
3436 N  N   . LEU   A 457 ? 1.2370 1.5683 1.4329 0.0178  -0.1232 -0.2773 477 LEU   A N   
3437 C  CA  . LEU   A 457 ? 1.2257 1.5568 1.4472 -0.0043 -0.0912 -0.2512 477 LEU   A CA  
3438 C  C   . LEU   A 457 ? 1.3170 1.6833 1.5944 -0.0076 -0.0978 -0.2620 477 LEU   A C   
3439 O  O   . LEU   A 457 ? 1.4050 1.7920 1.6831 0.0150  -0.1269 -0.2780 477 LEU   A O   
3440 C  CB  . LEU   A 457 ? 1.2167 1.5196 1.3766 0.0064  -0.0735 -0.2128 477 LEU   A CB  
3441 C  CG  . LEU   A 457 ? 1.1715 1.4426 1.2909 0.0032  -0.0552 -0.1958 477 LEU   A CG  
3442 C  CD1 . LEU   A 457 ? 1.1189 1.3684 1.1867 0.0159  -0.0409 -0.1621 477 LEU   A CD1 
3443 C  CD2 . LEU   A 457 ? 1.1327 1.3987 1.2899 -0.0261 -0.0309 -0.1917 477 LEU   A CD2 
3444 N  N   . SER   A 458 ? 1.3165 1.6879 1.6385 -0.0337 -0.0699 -0.2532 478 SER   A N   
3445 C  CA  . SER   A 458 ? 1.3709 1.7734 1.7457 -0.0377 -0.0680 -0.2601 478 SER   A CA  
3446 C  C   . SER   A 458 ? 1.4685 1.8678 1.8021 -0.0136 -0.0759 -0.2408 478 SER   A C   
3447 O  O   . SER   A 458 ? 1.4005 1.7704 1.6861 -0.0125 -0.0584 -0.2097 478 SER   A O   
3448 C  CB  . SER   A 458 ? 1.2894 1.6855 1.6995 -0.0668 -0.0301 -0.2474 478 SER   A CB  
3449 O  OG  . SER   A 458 ? 1.3061 1.7261 1.7548 -0.0679 -0.0220 -0.2479 478 SER   A OG  
3450 N  N   . LEU   A 459 ? 1.7022 2.1314 2.0577 0.0064  -0.1034 -0.2607 479 LEU   A N   
3451 C  CA  . LEU   A 459 ? 1.5826 2.0070 1.9021 0.0318  -0.1125 -0.2449 479 LEU   A CA  
3452 C  C   . LEU   A 459 ? 1.5385 1.9638 1.8798 0.0192  -0.0851 -0.2270 479 LEU   A C   
3453 O  O   . LEU   A 459 ? 1.5261 1.9522 1.8537 0.0382  -0.0920 -0.2189 479 LEU   A O   
3454 C  CB  . LEU   A 459 ? 1.5885 2.0457 1.9285 0.0596  -0.1521 -0.2739 479 LEU   A CB  
3455 C  CG  . LEU   A 459 ? 1.6496 2.0918 1.9271 0.0926  -0.1865 -0.2818 479 LEU   A CG  
3456 C  CD1 . LEU   A 459 ? 1.6283 2.0583 1.8929 0.0821  -0.1894 -0.2942 479 LEU   A CD1 
3457 C  CD2 . LEU   A 459 ? 1.5979 2.0774 1.9055 0.1209  -0.2285 -0.3139 479 LEU   A CD2 
3458 N  N   . GLY   A 460 ? 1.4215 1.8423 1.7914 -0.0102 -0.0543 -0.2207 480 GLY   A N   
3459 C  CA  . GLY   A 460 ? 1.3493 1.7672 1.7337 -0.0206 -0.0279 -0.2058 480 GLY   A CA  
3460 C  C   . GLY   A 460 ? 1.3651 1.7424 1.6879 -0.0198 -0.0124 -0.1723 480 GLY   A C   
3461 O  O   . GLY   A 460 ? 1.3783 1.7367 1.6511 -0.0016 -0.0257 -0.1593 480 GLY   A O   
3462 N  N   . GLY   A 461 ? 1.3785 1.7402 1.7043 -0.0389 0.0162  -0.1588 481 GLY   A N   
3463 C  CA  . GLY   A 461 ? 1.3960 1.7226 1.6718 -0.0390 0.0278  -0.1314 481 GLY   A CA  
3464 C  C   . GLY   A 461 ? 1.4174 1.7193 1.6727 -0.0554 0.0430  -0.1189 481 GLY   A C   
3465 O  O   . GLY   A 461 ? 1.4284 1.7040 1.6492 -0.0570 0.0511  -0.0988 481 GLY   A O   
3466 N  N   . LEU   A 462 ? 1.4531 1.7632 1.7326 -0.0668 0.0453  -0.1323 482 LEU   A N   
3467 C  CA  . LEU   A 462 ? 1.4047 1.6908 1.6671 -0.0801 0.0587  -0.1227 482 LEU   A CA  
3468 C  C   . LEU   A 462 ? 1.3391 1.6255 1.5897 -0.0746 0.0427  -0.1307 482 LEU   A C   
3469 O  O   . LEU   A 462 ? 1.3549 1.6638 1.6294 -0.0688 0.0254  -0.1529 482 LEU   A O   
3470 C  CB  . LEU   A 462 ? 1.4419 1.7267 1.7391 -0.0995 0.0821  -0.1298 482 LEU   A CB  
3471 C  CG  . LEU   A 462 ? 1.5331 1.7890 1.8075 -0.1073 0.1069  -0.1105 482 LEU   A CG  
3472 C  CD1 . LEU   A 462 ? 1.5227 1.7496 1.7510 -0.1049 0.1050  -0.0917 482 LEU   A CD1 
3473 C  CD2 . LEU   A 462 ? 1.6008 1.8603 1.8691 -0.0989 0.1095  -0.1046 482 LEU   A CD2 
3474 N  N   . LEU   A 463 ? 1.2484 1.5103 1.4626 -0.0745 0.0474  -0.1144 483 LEU   A N   
3475 C  CA  . LEU   A 463 ? 1.1593 1.4162 1.3563 -0.0682 0.0370  -0.1204 483 LEU   A CA  
3476 C  C   . LEU   A 463 ? 1.1683 1.4245 1.3953 -0.0836 0.0440  -0.1371 483 LEU   A C   
3477 O  O   . LEU   A 463 ? 1.1810 1.4148 1.3986 -0.0930 0.0590  -0.1278 483 LEU   A O   
3478 C  CB  . LEU   A 463 ? 1.0542 1.2883 1.2111 -0.0632 0.0433  -0.0982 483 LEU   A CB  
3479 C  CG  . LEU   A 463 ? 1.0311 1.2604 1.1645 -0.0515 0.0337  -0.1045 483 LEU   A CG  
3480 C  CD1 . LEU   A 463 ? 1.0390 1.2747 1.1475 -0.0300 0.0166  -0.1067 483 LEU   A CD1 
3481 C  CD2 . LEU   A 463 ? 0.9707 1.1798 1.0805 -0.0518 0.0464  -0.0867 483 LEU   A CD2 
3482 N  N   . GLN   A 464 ? 1.2247 1.5051 1.4915 -0.0856 0.0324  -0.1631 484 GLN   A N   
3483 C  CA  . GLN   A 464 ? 1.1667 1.4489 1.4746 -0.1026 0.0386  -0.1838 484 GLN   A CA  
3484 C  C   . GLN   A 464 ? 1.1777 1.4822 1.5033 -0.0927 0.0092  -0.2146 484 GLN   A C   
3485 O  O   . GLN   A 464 ? 1.2468 1.5671 1.5546 -0.0719 -0.0137 -0.2183 484 GLN   A O   
3486 C  CB  . GLN   A 464 ? 1.1515 1.4438 1.5085 -0.1206 0.0599  -0.1872 484 GLN   A CB  
3487 C  CG  . GLN   A 464 ? 1.2375 1.5060 1.5670 -0.1247 0.0848  -0.1583 484 GLN   A CG  
3488 C  CD  . GLN   A 464 ? 1.2885 1.5611 1.6573 -0.1397 0.1105  -0.1603 484 GLN   A CD  
3489 O  OE1 . GLN   A 464 ? 1.2158 1.5178 1.6419 -0.1468 0.1095  -0.1832 484 GLN   A OE1 
3490 N  NE2 . GLN   A 464 ? 1.3657 1.6088 1.7043 -0.1432 0.1340  -0.1374 484 GLN   A NE2 
3491 N  N   . PRO   A 465 ? 1.2684 1.5714 1.6250 -0.1050 0.0075  -0.2376 485 PRO   A N   
3492 C  CA  . PRO   A 465 ? 1.3125 1.6386 1.6901 -0.0950 -0.0253 -0.2726 485 PRO   A CA  
3493 C  C   . PRO   A 465 ? 1.3512 1.7199 1.7962 -0.0990 -0.0362 -0.2960 485 PRO   A C   
3494 O  O   . PRO   A 465 ? 1.2995 1.6773 1.7887 -0.1172 -0.0113 -0.2903 485 PRO   A O   
3495 C  CB  . PRO   A 465 ? 1.2781 1.5851 1.6749 -0.1114 -0.0197 -0.2904 485 PRO   A CB  
3496 C  CG  . PRO   A 465 ? 1.1861 1.4552 1.5552 -0.1236 0.0146  -0.2592 485 PRO   A CG  
3497 C  CD  . PRO   A 465 ? 1.1986 1.4733 1.5666 -0.1263 0.0333  -0.2334 485 PRO   A CD  
3498 N  N   . GLU   A 466 ? 1.4149 1.8095 1.8654 -0.0789 -0.0744 -0.3231 486 GLU   A N   
3499 C  CA  . GLU   A 466 ? 1.4256 1.8671 1.9508 -0.0806 -0.0907 -0.3524 486 GLU   A CA  
3500 C  C   . GLU   A 466 ? 1.4380 1.8924 2.0485 -0.1124 -0.0770 -0.3792 486 GLU   A C   
3501 O  O   . GLU   A 466 ? 1.4818 1.9594 2.1595 -0.1308 -0.0554 -0.3824 486 GLU   A O   
3502 C  CB  . GLU   A 466 ? 1.4521 1.9153 1.9602 -0.0485 -0.1397 -0.3786 486 GLU   A CB  
3503 C  CG  . GLU   A 466 ? 1.4669 1.9781 2.0297 -0.0372 -0.1598 -0.3971 486 GLU   A CG  
3504 C  CD  . GLU   A 466 ? 1.4628 1.9875 1.9898 0.0022  -0.2101 -0.4173 486 GLU   A CD  
3505 O  OE1 . GLU   A 466 ? 1.5158 2.0419 2.0411 0.0100  -0.2408 -0.4485 486 GLU   A OE1 
3506 O  OE2 . GLU   A 466 ? 1.5905 2.1198 2.0859 0.0272  -0.2192 -0.4020 486 GLU   A OE2 
3507 N  N   . LYS   A 467 ? 1.5153 1.9514 2.1237 -0.1193 -0.0862 -0.3982 487 LYS   A N   
3508 C  CA  . LYS   A 467 ? 1.4830 1.9196 2.1666 -0.1515 -0.0700 -0.4220 487 LYS   A CA  
3509 C  C   . LYS   A 467 ? 1.4703 1.8527 2.1135 -0.1678 -0.0339 -0.3949 487 LYS   A C   
3510 O  O   . LYS   A 467 ? 1.4822 1.8328 2.0485 -0.1510 -0.0414 -0.3797 487 LYS   A O   
3511 C  CB  . LYS   A 467 ? 1.4759 1.9320 2.1947 -0.1463 -0.1128 -0.4712 487 LYS   A CB  
3512 C  CG  . LYS   A 467 ? 1.3898 1.8691 2.2218 -0.1796 -0.1046 -0.5078 487 LYS   A CG  
3513 C  CD  . LYS   A 467 ? 1.4544 1.9838 2.3453 -0.1670 -0.1581 -0.5611 487 LYS   A CD  
3514 C  CE  . LYS   A 467 ? 1.3995 1.9477 2.4053 -0.2017 -0.1548 -0.6042 487 LYS   A CE  
3515 N  NZ  . LYS   A 467 ? 1.3958 1.9699 2.4830 -0.2202 -0.1189 -0.5957 487 LYS   A NZ  
3516 N  N   . PRO   A 468 ? 1.3747 1.7437 2.0651 -0.1978 0.0069  -0.3868 488 PRO   A N   
3517 C  CA  . PRO   A 468 ? 1.3250 1.6385 1.9742 -0.2101 0.0399  -0.3611 488 PRO   A CA  
3518 C  C   . PRO   A 468 ? 1.2831 1.5706 1.9100 -0.2069 0.0207  -0.3806 488 PRO   A C   
3519 O  O   . PRO   A 468 ? 1.2946 1.6039 1.9648 -0.2079 -0.0095 -0.4217 488 PRO   A O   
3520 C  CB  . PRO   A 468 ? 1.2477 1.5550 1.9668 -0.2428 0.0822  -0.3610 488 PRO   A CB  
3521 C  CG  . PRO   A 468 ? 1.3146 1.6705 2.0826 -0.2417 0.0825  -0.3655 488 PRO   A CG  
3522 C  CD  . PRO   A 468 ? 1.3520 1.7531 2.1255 -0.2177 0.0293  -0.3943 488 PRO   A CD  
3523 N  N   . VAL   A 469 ? 1.2767 1.5175 1.8358 -0.2013 0.0372  -0.3525 489 VAL   A N   
3524 C  CA  . VAL   A 469 ? 1.2389 1.4506 1.7594 -0.1915 0.0210  -0.3650 489 VAL   A CA  
3525 C  C   . VAL   A 469 ? 1.2715 1.4522 1.8392 -0.2189 0.0408  -0.3825 489 VAL   A C   
3526 O  O   . VAL   A 469 ? 1.2842 1.4335 1.8593 -0.2371 0.0808  -0.3589 489 VAL   A O   
3527 C  CB  . VAL   A 469 ? 1.2305 1.4098 1.6635 -0.1715 0.0306  -0.3273 489 VAL   A CB  
3528 C  CG1 . VAL   A 469 ? 1.1897 1.3289 1.5908 -0.1672 0.0289  -0.3355 489 VAL   A CG1 
3529 C  CG2 . VAL   A 469 ? 1.1911 1.3962 1.5765 -0.1428 0.0053  -0.3184 489 VAL   A CG2 
3530 N  N   . VAL   A 470 ? 1.2788 1.4638 1.8747 -0.2203 0.0125  -0.4243 490 VAL   A N   
3531 C  CA  . VAL   A 470 ? 1.2930 1.4469 1.9387 -0.2467 0.0269  -0.4475 490 VAL   A CA  
3532 C  C   . VAL   A 470 ? 1.3515 1.4723 1.9454 -0.2299 0.0044  -0.4641 490 VAL   A C   
3533 O  O   . VAL   A 470 ? 1.3705 1.5114 1.9279 -0.2032 -0.0355 -0.4824 490 VAL   A O   
3534 C  CB  . VAL   A 470 ? 1.3430 1.5378 2.0969 -0.2704 0.0142  -0.4920 490 VAL   A CB  
3535 C  CG1 . VAL   A 470 ? 1.2496 1.4695 2.0587 -0.2897 0.0476  -0.4737 490 VAL   A CG1 
3536 C  CG2 . VAL   A 470 ? 1.3353 1.5787 2.0929 -0.2468 -0.0427 -0.5292 490 VAL   A CG2 
3537 N  N   . LEU   A 471 ? 1.3558 1.4219 1.9417 -0.2431 0.0313  -0.4571 491 LEU   A N   
3538 C  CA  . LEU   A 471 ? 1.4330 1.4613 1.9675 -0.2266 0.0156  -0.4707 491 LEU   A CA  
3539 C  C   . LEU   A 471 ? 1.5044 1.4866 2.0852 -0.2538 0.0341  -0.4918 491 LEU   A C   
3540 O  O   . LEU   A 471 ? 1.5159 1.4809 2.1477 -0.2830 0.0713  -0.4801 491 LEU   A O   
3541 C  CB  . LEU   A 471 ? 1.3350 1.3330 1.7778 -0.2015 0.0312  -0.4270 491 LEU   A CB  
3542 C  CG  . LEU   A 471 ? 1.3147 1.3444 1.7010 -0.1742 0.0211  -0.3984 491 LEU   A CG  
3543 C  CD1 . LEU   A 471 ? 1.2688 1.2635 1.5838 -0.1558 0.0408  -0.3611 491 LEU   A CD1 
3544 C  CD2 . LEU   A 471 ? 1.3337 1.3959 1.6988 -0.1500 -0.0228 -0.4271 491 LEU   A CD2 
3545 N  N   . LYS   A 472 ? 1.5014 1.4586 2.0593 -0.2425 0.0096  -0.5227 492 LYS   A N   
3546 C  CA  . LYS   A 472 ? 1.4720 1.3729 2.0556 -0.2627 0.0270  -0.5400 492 LYS   A CA  
3547 C  C   . LYS   A 472 ? 1.4980 1.3408 2.0091 -0.2498 0.0603  -0.4971 492 LYS   A C   
3548 O  O   . LYS   A 472 ? 1.4160 1.2630 1.8509 -0.2186 0.0548  -0.4701 492 LYS   A O   
3549 C  CB  . LYS   A 472 ? 1.4608 1.3578 2.0479 -0.2535 -0.0165 -0.5949 492 LYS   A CB  
3550 C  CG  . LYS   A 472 ? 1.5369 1.3857 2.1806 -0.2822 -0.0061 -0.6281 492 LYS   A CG  
3551 C  CD  . LYS   A 472 ? 1.5081 1.3865 2.2094 -0.2874 -0.0557 -0.6946 492 LYS   A CD  
3552 C  CE  . LYS   A 472 ? 1.5642 1.3882 2.2869 -0.3007 -0.0556 -0.7254 492 LYS   A CE  
3553 N  NZ  . LYS   A 472 ? 1.6152 1.4019 2.3957 -0.3371 -0.0031 -0.7012 492 LYS   A NZ  
3554 N  N   . VAL   A 473 ? 1.4904 1.2783 2.0287 -0.2736 0.0962  -0.4905 493 VAL   A N   
3555 C  CA  . VAL   A 473 ? 1.5221 1.2522 1.9983 -0.2618 0.1296  -0.4487 493 VAL   A CA  
3556 C  C   . VAL   A 473 ? 1.6277 1.2900 2.1158 -0.2735 0.1413  -0.4702 493 VAL   A C   
3557 O  O   . VAL   A 473 ? 1.6757 1.3193 2.2376 -0.3079 0.1568  -0.4919 493 VAL   A O   
3558 C  CB  . VAL   A 473 ? 1.5062 1.2282 1.9880 -0.2749 0.1716  -0.4032 493 VAL   A CB  
3559 C  CG1 . VAL   A 473 ? 1.4876 1.1492 1.9024 -0.2581 0.1998  -0.3633 493 VAL   A CG1 
3560 C  CG2 . VAL   A 473 ? 1.4298 1.2160 1.9009 -0.2636 0.1595  -0.3843 493 VAL   A CG2 
3561 N  N   . GLU   A 474 ? 1.6113 1.2358 2.0305 -0.2455 0.1359  -0.4645 494 GLU   A N   
3562 C  CA  . GLU   A 474 ? 1.6513 1.2078 2.0713 -0.2506 0.1435  -0.4863 494 GLU   A CA  
3563 C  C   . GLU   A 474 ? 1.6476 1.1468 1.9998 -0.2290 0.1731  -0.4438 494 GLU   A C   
3564 O  O   . GLU   A 474 ? 1.6643 1.1851 1.9604 -0.2019 0.1738  -0.4081 494 GLU   A O   
3565 C  CB  . GLU   A 474 ? 1.6835 1.2493 2.0890 -0.2336 0.0992  -0.5356 494 GLU   A CB  
3566 C  CG  . GLU   A 474 ? 1.6911 1.3207 2.1550 -0.2466 0.0614  -0.5780 494 GLU   A CG  
3567 C  CD  . GLU   A 474 ? 1.7946 1.4235 2.2464 -0.2312 0.0161  -0.6328 494 GLU   A CD  
3568 O  OE1 . GLU   A 474 ? 1.8301 1.4151 2.2164 -0.2054 0.0138  -0.6346 494 GLU   A OE1 
3569 O  OE2 . GLU   A 474 ? 1.7700 1.4423 2.2772 -0.2431 -0.0183 -0.6756 494 GLU   A OE2 
3570 N  N   . SER   A 475 ? 1.6536 1.0786 2.0146 -0.2408 0.1968  -0.4490 495 SER   A N   
3571 C  CA  . SER   A 475 ? 1.7153 1.0773 2.0226 -0.2242 0.2298  -0.4074 495 SER   A CA  
3572 C  C   . SER   A 475 ? 1.7517 1.0810 2.0001 -0.1901 0.2149  -0.4179 495 SER   A C   
3573 O  O   . SER   A 475 ? 1.7404 1.0339 2.0046 -0.1962 0.2041  -0.4580 495 SER   A O   
3574 C  CB  . SER   A 475 ? 1.6648 0.9565 2.0126 -0.2560 0.2710  -0.4013 495 SER   A CB  
3575 O  OG  . SER   A 475 ? 1.7757 1.0040 2.0654 -0.2367 0.3025  -0.3576 495 SER   A OG  
3576 N  N   . ARG   A 476 ? 1.7699 1.1114 1.9542 -0.1544 0.2151  -0.3833 496 ARG   A N   
3577 C  CA  . ARG   A 476 ? 1.7224 1.0370 1.8505 -0.1182 0.2062  -0.3878 496 ARG   A CA  
3578 C  C   . ARG   A 476 ? 1.7270 0.9503 1.8478 -0.1193 0.2304  -0.3894 496 ARG   A C   
3579 O  O   . ARG   A 476 ? 1.7574 0.9474 1.8367 -0.0908 0.2258  -0.3974 496 ARG   A O   
3580 C  CB  . ARG   A 476 ? 1.6712 1.0177 1.7461 -0.0832 0.2080  -0.3466 496 ARG   A CB  
3581 C  CG  . ARG   A 476 ? 1.6390 1.0694 1.7128 -0.0774 0.1855  -0.3434 496 ARG   A CG  
3582 C  CD  . ARG   A 476 ? 1.5658 1.0232 1.5937 -0.0436 0.1884  -0.3066 496 ARG   A CD  
3583 N  NE  . ARG   A 476 ? 1.5940 1.0340 1.5803 -0.0099 0.1835  -0.3158 496 ARG   A NE  
3584 C  CZ  . ARG   A 476 ? 1.5393 1.0008 1.4922 0.0218  0.1868  -0.2903 496 ARG   A CZ  
3585 N  NH1 . ARG   A 476 ? 1.4772 0.9772 1.4320 0.0243  0.1916  -0.2552 496 ARG   A NH1 
3586 N  NH2 . ARG   A 476 ? 1.5103 0.9549 1.4302 0.0519  0.1855  -0.3020 496 ARG   A NH2 
3587 C  CHA . HEM   B .   ? 0.9784 1.0850 1.0452 -0.0614 0.0300  0.0003  601 HEM   A CHA 
3588 C  CHB . HEM   B .   ? 0.9773 1.1169 1.0765 -0.0686 0.0705  0.0028  601 HEM   A CHB 
3589 C  CHC . HEM   B .   ? 1.0547 1.1015 1.0813 -0.0572 0.0934  0.0084  601 HEM   A CHC 
3590 C  CHD . HEM   B .   ? 1.0461 1.0554 0.9951 -0.0286 0.0485  0.0144  601 HEM   A CHD 
3591 C  C1A . HEM   B .   ? 0.9599 1.0835 1.0466 -0.0666 0.0421  0.0030  601 HEM   A C1A 
3592 C  C2A . HEM   B .   ? 0.9551 1.0979 1.0669 -0.0722 0.0450  0.0045  601 HEM   A C2A 
3593 C  C3A . HEM   B .   ? 0.9246 1.0757 1.0402 -0.0722 0.0561  0.0060  601 HEM   A C3A 
3594 C  C4A . HEM   B .   ? 0.8980 1.0364 0.9975 -0.0691 0.0607  0.0045  601 HEM   A C4A 
3595 C  CMA . HEM   B .   ? 0.8922 1.0575 1.0204 -0.0729 0.0637  0.0091  601 HEM   A CMA 
3596 C  CAA . HEM   B .   ? 0.8669 1.0136 0.9941 -0.0762 0.0374  0.0042  601 HEM   A CAA 
3597 C  CBA . HEM   B .   ? 0.8826 1.0433 1.0444 -0.0779 0.0323  0.0073  601 HEM   A CBA 
3598 C  CGA . HEM   B .   ? 0.8612 1.0224 1.0438 -0.0847 0.0289  0.0073  601 HEM   A CGA 
3599 O  O1A . HEM   B .   ? 0.7536 0.9276 0.9732 -0.0892 0.0310  0.0106  601 HEM   A O1A 
3600 O  O2A . HEM   B .   ? 0.8963 1.0442 1.0616 -0.0857 0.0261  0.0039  601 HEM   A O2A 
3601 C  C1B . HEM   B .   ? 0.9618 1.0840 1.0474 -0.0667 0.0767  0.0014  601 HEM   A C1B 
3602 C  C2B . HEM   B .   ? 0.9663 1.0866 1.0536 -0.0667 0.0857  -0.0031 601 HEM   A C2B 
3603 C  C3B . HEM   B .   ? 1.0006 1.0959 1.0726 -0.0655 0.0920  -0.0024 601 HEM   A C3B 
3604 C  C4B . HEM   B .   ? 0.9825 1.0623 1.0367 -0.0623 0.0872  0.0037  601 HEM   A C4B 
3605 C  CMB . HEM   B .   ? 0.8994 1.0380 0.9974 -0.0658 0.0877  -0.0077 601 HEM   A CMB 
3606 C  CAB . HEM   B .   ? 1.0312 1.1090 1.0995 -0.0660 0.1030  -0.0073 601 HEM   A CAB 
3607 C  CBB . HEM   B .   ? 1.0070 1.0950 1.0863 -0.0673 0.1053  -0.0164 601 HEM   A CBB 
3608 C  C1C . HEM   B .   ? 1.0558 1.0835 1.0551 -0.0483 0.0859  0.0142  601 HEM   A C1C 
3609 C  C2C . HEM   B .   ? 1.1158 1.1027 1.0755 -0.0364 0.0904  0.0219  601 HEM   A C2C 
3610 C  C3C . HEM   B .   ? 1.1456 1.1216 1.0792 -0.0264 0.0775  0.0242  601 HEM   A C3C 
3611 C  C4C . HEM   B .   ? 1.0740 1.0841 1.0355 -0.0342 0.0650  0.0173  601 HEM   A C4C 
3612 C  CMC . HEM   B .   ? 1.2001 1.1555 1.1455 -0.0338 0.1072  0.0263  601 HEM   A CMC 
3613 C  CAC . HEM   B .   ? 1.1852 1.1135 1.0620 -0.0072 0.0768  0.0330  601 HEM   A CAC 
3614 C  CBC . HEM   B .   ? 1.2748 1.1901 1.1192 0.0064  0.0597  0.0326  601 HEM   A CBC 
3615 C  C1D . HEM   B .   ? 1.0295 1.0662 1.0065 -0.0363 0.0375  0.0081  601 HEM   A C1D 
3616 C  C2D . HEM   B .   ? 1.0723 1.1025 1.0345 -0.0317 0.0218  0.0026  601 HEM   A C2D 
3617 C  C3D . HEM   B .   ? 1.0498 1.1072 1.0486 -0.0424 0.0167  -0.0021 601 HEM   A C3D 
3618 C  C4D . HEM   B .   ? 0.9850 1.0666 1.0179 -0.0520 0.0289  0.0012  601 HEM   A C4D 
3619 C  CMD . HEM   B .   ? 1.1101 1.1018 1.0160 -0.0147 0.0135  0.0024  601 HEM   A CMD 
3620 C  CAD . HEM   B .   ? 1.0456 1.1035 1.0466 -0.0429 0.0005  -0.0102 601 HEM   A CAD 
3621 C  CBD . HEM   B .   ? 1.0398 1.1039 1.0563 -0.0352 -0.0273 -0.0158 601 HEM   A CBD 
3622 C  CGD . HEM   B .   ? 1.0460 1.1166 1.0833 -0.0400 -0.0452 -0.0263 601 HEM   A CGD 
3623 O  O1D . HEM   B .   ? 1.0076 1.0793 1.0544 -0.0326 -0.0723 -0.0360 601 HEM   A O1D 
3624 O  O2D . HEM   B .   ? 1.0315 1.1054 1.0776 -0.0502 -0.0341 -0.0264 601 HEM   A O2D 
3625 N  NA  . HEM   B .   ? 0.9096 1.0299 0.9904 -0.0655 0.0535  0.0044  601 HEM   A NA  
3626 N  NB  . HEM   B .   ? 0.9630 1.0612 1.0272 -0.0633 0.0763  0.0042  601 HEM   A NB  
3627 N  NC  . HEM   B .   ? 1.0663 1.1059 1.0661 -0.0471 0.0718  0.0130  601 HEM   A NC  
3628 N  ND  . HEM   B .   ? 1.0053 1.0746 1.0246 -0.0482 0.0401  0.0058  601 HEM   A ND  
3629 FE FE  . HEM   B .   ? 0.8439 0.9298 0.8886 -0.0567 0.0594  0.0072  601 HEM   A FE  
3630 C  C11 . A1A4T C .   ? 1.4798 1.5999 1.5353 -0.0686 0.0694  -0.0171 602 A1A4T A C11 
3631 C  C15 . A1A4T C .   ? 1.8180 1.9639 1.8970 -0.0571 0.0885  -0.0415 602 A1A4T A C15 
3632 C  C16 . A1A4T C .   ? 1.7582 1.9145 1.8495 -0.0488 0.0873  -0.0489 602 A1A4T A C16 
3633 C  C17 . A1A4T C .   ? 1.8261 1.9836 1.9188 -0.0646 0.0985  -0.0425 602 A1A4T A C17 
3634 C  C18 . A1A4T C .   ? 1.8627 2.0451 1.9865 -0.0656 0.1054  -0.0531 602 A1A4T A C18 
3635 C  C19 . A1A4T C .   ? 1.7955 1.9935 1.9357 -0.0565 0.1016  -0.0619 602 A1A4T A C19 
3636 C  C20 . A1A4T C .   ? 1.7444 1.9274 1.8652 -0.0470 0.0933  -0.0586 602 A1A4T A C20 
3637 C  C23 . A1A4T C .   ? 1.1757 1.2340 1.1751 -0.0690 0.1080  0.0007  602 A1A4T A C23 
3638 C  C25 . A1A4T C .   ? 1.0992 1.1561 1.0955 -0.0612 0.0913  0.0053  602 A1A4T A C25 
3639 C  C26 . A1A4T C .   ? 1.2082 1.2936 1.2421 -0.0782 0.1112  -0.0071 602 A1A4T A C26 
3640 C  C13 . A1A4T C .   ? 1.6489 1.7049 1.6182 -0.0583 0.1482  -0.0248 602 A1A4T A C13 
3641 C  C14 . A1A4T C .   ? 1.7574 1.8796 1.8127 -0.0565 0.0767  -0.0351 602 A1A4T A C14 
3642 C  C22 . A1A4T C .   ? 1.4118 1.5402 1.4770 -0.0723 0.0750  -0.0137 602 A1A4T A C22 
3643 C  C01 . A1A4T C .   ? 1.3178 1.3476 1.2822 -0.0649 0.1231  0.0034  602 A1A4T A C01 
3644 C  C02 . A1A4T C .   ? 1.3518 1.3757 1.2929 -0.0550 0.1087  0.0014  602 A1A4T A C02 
3645 C  C03 . A1A4T C .   ? 1.3397 1.3940 1.3130 -0.0587 0.0914  -0.0058 602 A1A4T A C03 
3646 C  C05 . A1A4T C .   ? 1.5143 1.5713 1.4837 -0.0583 0.1085  -0.0167 602 A1A4T A C05 
3647 C  C06 . A1A4T C .   ? 1.6369 1.7128 1.6306 -0.0619 0.1220  -0.0247 602 A1A4T A C06 
3648 C  C08 . A1A4T C .   ? 1.6032 1.6908 1.6131 -0.0567 0.0754  -0.0287 602 A1A4T A C08 
3649 C  C09 . A1A4T C .   ? 1.6535 1.7656 1.6976 -0.0612 0.0719  -0.0280 602 A1A4T A C09 
3650 C  C27 . A1A4T C .   ? 1.1185 1.2228 1.1726 -0.0783 0.1001  -0.0080 602 A1A4T A C27 
3651 C  C28 . A1A4T C .   ? 1.0797 1.1800 1.1287 -0.0716 0.0891  -0.0015 602 A1A4T A C28 
3652 C  C29 . A1A4T C .   ? 1.4225 1.5520 1.4891 -0.0762 0.0911  -0.0189 602 A1A4T A C29 
3653 C  C30 . A1A4T C .   ? 1.2149 1.3309 1.2691 -0.0700 0.0691  -0.0079 602 A1A4T A C30 
3654 C  C31 . A1A4T C .   ? 1.3254 1.4705 1.4098 -0.0725 0.0710  -0.0122 602 A1A4T A C31 
3655 C  C32 . A1A4T C .   ? 1.6502 1.6914 1.6143 -0.0647 0.1733  -0.0179 602 A1A4T A C32 
3656 C  C33 . A1A4T C .   ? 1.5969 1.6021 1.5153 -0.0575 0.1732  -0.0071 602 A1A4T A C33 
3657 C  C34 . A1A4T C .   ? 1.7274 1.7895 1.7343 -0.0768 0.1953  -0.0237 602 A1A4T A C34 
3658 C  C35 . A1A4T C .   ? 1.7197 1.7644 1.7266 -0.0853 0.2209  -0.0180 602 A1A4T A C35 
3659 C  C36 . A1A4T C .   ? 1.6574 1.6598 1.6130 -0.0782 0.2243  -0.0042 602 A1A4T A C36 
3660 C  C37 . A1A4T C .   ? 1.6221 1.6060 1.5322 -0.0627 0.1987  0.0011  602 A1A4T A C37 
3661 C  C38 . A1A4T C .   ? 1.7504 1.9818 1.9336 -0.0558 0.1047  -0.0773 602 A1A4T A C38 
3662 C  C39 . A1A4T C .   ? 1.6692 1.9174 1.8697 -0.0427 0.0983  -0.0868 602 A1A4T A C39 
3663 C  C40 . A1A4T C .   ? 1.6103 1.8943 1.8576 -0.0402 0.0971  -0.1041 602 A1A4T A C40 
3664 C  C41 . A1A4T C .   ? 1.6008 1.9022 1.8796 -0.0536 0.1030  -0.1130 602 A1A4T A C41 
3665 C  C42 . A1A4T C .   ? 1.6556 1.9349 1.9133 -0.0676 0.1118  -0.1024 602 A1A4T A C42 
3666 C  C43 . A1A4T C .   ? 1.7007 1.9459 1.9098 -0.0673 0.1123  -0.0840 602 A1A4T A C43 
3667 N  N04 . A1A4T C .   ? 1.4324 1.5013 1.4231 -0.0646 0.1042  -0.0124 602 A1A4T A N04 
3668 N  N10 . A1A4T C .   ? 1.5564 1.6812 1.6139 -0.0669 0.0776  -0.0241 602 A1A4T A N10 
3669 N  N24 . A1A4T C .   ? 1.0853 1.1652 1.1105 -0.0637 0.0837  0.0040  602 A1A4T A N24 
3670 O  O12 . A1A4T C .   ? 1.4688 1.5014 1.4015 -0.0482 0.1003  -0.0155 602 A1A4T A O12 
3671 O  O21 . A1A4T C .   ? 1.3688 1.4792 1.4182 -0.0664 0.0573  -0.0159 602 A1A4T A O21 
3672 S  S07 . A1A4T C .   ? 1.6995 1.7833 1.6988 -0.0554 0.1033  -0.0320 602 A1A4T A S07 
3673 O  O   . HOH   D .   ? 1.1334 1.2809 1.2234 -0.0369 0.0464  -0.0135 701 HOH   A O   
3674 O  O   . HOH   D .   ? 1.4470 1.4122 1.1258 0.1656  -0.1370 -0.4338 702 HOH   A O   
3675 O  O   . HOH   D .   ? 1.7388 0.9637 1.8638 -0.1408 0.2902  -0.2895 703 HOH   A O   
3676 O  O   . HOH   D .   ? 0.8610 1.0833 1.0957 -0.0560 0.0997  0.0318  704 HOH   A O   
3677 O  O   . HOH   D .   ? 1.9120 1.6188 1.4335 0.0734  0.4482  -0.0083 705 HOH   A O   
3678 O  O   . HOH   D .   ? 1.7547 1.3990 2.7657 -0.5022 0.4845  -0.3804 706 HOH   A O   
3679 O  O   . HOH   D .   ? 1.0290 1.3283 1.8113 -0.1762 -0.1184 -0.1137 707 HOH   A O   
3680 O  O   . HOH   D .   ? 1.7568 1.7736 2.8452 -0.3930 -0.0063 -0.7197 708 HOH   A O   
3681 O  O   . HOH   D .   ? 1.2711 1.1079 1.2227 0.2691  -0.0100 -0.0345 709 HOH   A O   
3682 O  O   . HOH   D .   ? 1.2242 1.2547 0.9402 0.1576  0.3151  0.0619  710 HOH   A O   
3683 O  O   . HOH   D .   ? 1.7485 1.1724 2.3120 -0.3301 0.1959  -0.5394 711 HOH   A O   
3684 O  O   . HOH   D .   ? 1.8272 0.8953 2.0312 -0.1804 0.2709  -0.4350 712 HOH   A O   
3685 O  O   . HOH   D .   ? 1.1132 1.4052 1.2525 0.0192  -0.0351 -0.1257 713 HOH   A O   
3686 O  O   . HOH   D .   ? 0.9446 1.2033 1.2206 0.0071  0.1832  0.0366  714 HOH   A O   
3687 O  O   . HOH   D .   ? 0.8512 1.0671 1.0618 -0.0155 0.1244  0.0227  715 HOH   A O   
3688 O  O   . HOH   D .   ? 0.8150 1.0323 1.0589 0.0122  0.1066  0.0173  716 HOH   A O   
# 
